data_9GRT
# 
_entry.id   9GRT 
# 
_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   9GRT         pdb_00009grt 10.2210/pdb9grt/pdb 
WWPDB D_1292141084 ?            ?                   
# 
_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                        9GRT 
_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           Y 
# 
_pdbx_contact_author.id                 1 
_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 4-bromo-1H-pyrazole                                146.973   2   ? ? ? ? 
3 non-polymer syn 'SULFATE ION'                                      96.063    8   ? ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                               78.133    1   ? ? ? ? 
5 water       nat water                                              18.015    181 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 4-bromo-1H-pyrazole  BYZ 
3 'SULFATE ION'        SO4 
4 'DIMETHYL SULFOXIDE' DMS 
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 
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 
BYZ non-polymer         . 4-bromo-1H-pyrazole  ? 'C3 H3 Br N2'    146.973 
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 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   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 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 ?  ?   ?   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        BYZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BYZ 
_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 BYZ 1  101 101 BYZ C29 A . 
E 3 SO4 1  102 1   SO4 SO4 A . 
F 3 SO4 1  103 2   SO4 SO4 A . 
G 3 SO4 1  104 3   SO4 SO4 A . 
H 3 SO4 1  101 4   SO4 SO4 B . 
I 3 SO4 1  102 5   SO4 SO4 B . 
J 4 DMS 1  103 101 DMS DMS B . 
K 2 BYZ 1  101 101 BYZ C29 C . 
L 3 SO4 1  102 6   SO4 SO4 C . 
M 3 SO4 1  103 7   SO4 SO4 C . 
N 3 SO4 1  104 8   SO4 SO4 C . 
O 5 HOH 1  201 73  HOH HOH A . 
O 5 HOH 2  202 27  HOH HOH A . 
O 5 HOH 3  203 67  HOH HOH A . 
O 5 HOH 4  204 109 HOH HOH A . 
O 5 HOH 5  205 56  HOH HOH A . 
O 5 HOH 6  206 8   HOH HOH A . 
O 5 HOH 7  207 28  HOH HOH A . 
O 5 HOH 8  208 178 HOH HOH A . 
O 5 HOH 9  209 26  HOH HOH A . 
O 5 HOH 10 210 176 HOH HOH A . 
O 5 HOH 11 211 99  HOH HOH A . 
O 5 HOH 12 212 91  HOH HOH A . 
O 5 HOH 13 213 7   HOH HOH A . 
O 5 HOH 14 214 11  HOH HOH A . 
O 5 HOH 15 215 33  HOH HOH A . 
O 5 HOH 16 216 101 HOH HOH A . 
O 5 HOH 17 217 23  HOH HOH A . 
O 5 HOH 18 218 37  HOH HOH A . 
O 5 HOH 19 219 90  HOH HOH A . 
O 5 HOH 20 220 89  HOH HOH A . 
O 5 HOH 21 221 2   HOH HOH A . 
O 5 HOH 22 222 192 HOH HOH A . 
O 5 HOH 23 223 1   HOH HOH A . 
O 5 HOH 24 224 38  HOH HOH A . 
O 5 HOH 25 225 84  HOH HOH A . 
O 5 HOH 26 226 14  HOH HOH A . 
O 5 HOH 27 227 97  HOH HOH A . 
O 5 HOH 28 228 241 HOH HOH A . 
O 5 HOH 29 229 95  HOH HOH A . 
O 5 HOH 30 230 20  HOH HOH A . 
O 5 HOH 31 231 215 HOH HOH A . 
O 5 HOH 32 232 12  HOH HOH A . 
O 5 HOH 33 233 150 HOH HOH A . 
O 5 HOH 34 234 276 HOH HOH A . 
O 5 HOH 35 235 18  HOH HOH A . 
O 5 HOH 36 236 3   HOH HOH A . 
O 5 HOH 37 237 41  HOH HOH A . 
O 5 HOH 38 238 83  HOH HOH A . 
O 5 HOH 39 239 61  HOH HOH A . 
O 5 HOH 40 240 32  HOH HOH A . 
O 5 HOH 41 241 34  HOH HOH A . 
O 5 HOH 42 242 115 HOH HOH A . 
O 5 HOH 43 243 283 HOH HOH A . 
O 5 HOH 44 244 30  HOH HOH A . 
O 5 HOH 45 245 103 HOH HOH A . 
O 5 HOH 46 246 21  HOH HOH A . 
O 5 HOH 47 247 250 HOH HOH A . 
O 5 HOH 48 248 152 HOH HOH A . 
O 5 HOH 49 249 166 HOH HOH A . 
O 5 HOH 50 250 118 HOH HOH A . 
O 5 HOH 51 251 81  HOH HOH A . 
O 5 HOH 52 252 9   HOH HOH A . 
O 5 HOH 53 253 16  HOH HOH A . 
O 5 HOH 54 254 273 HOH HOH A . 
O 5 HOH 55 255 282 HOH HOH A . 
O 5 HOH 56 256 98  HOH HOH A . 
O 5 HOH 57 257 19  HOH HOH A . 
O 5 HOH 58 258 110 HOH HOH A . 
O 5 HOH 59 259 80  HOH HOH A . 
O 5 HOH 60 260 210 HOH HOH A . 
O 5 HOH 61 261 218 HOH HOH A . 
O 5 HOH 62 262 22  HOH HOH A . 
O 5 HOH 63 263 139 HOH HOH A . 
O 5 HOH 64 264 29  HOH HOH A . 
O 5 HOH 65 265 179 HOH HOH A . 
O 5 HOH 66 266 31  HOH HOH A . 
O 5 HOH 67 267 231 HOH HOH A . 
O 5 HOH 68 268 147 HOH HOH A . 
O 5 HOH 69 269 270 HOH HOH A . 
O 5 HOH 70 270 168 HOH HOH A . 
O 5 HOH 71 271 243 HOH HOH A . 
O 5 HOH 72 272 35  HOH HOH A . 
O 5 HOH 73 273 50  HOH HOH A . 
P 5 HOH 1  201 125 HOH HOH B . 
P 5 HOH 2  202 285 HOH HOH B . 
P 5 HOH 3  203 206 HOH HOH B . 
P 5 HOH 4  204 93  HOH HOH B . 
P 5 HOH 5  205 17  HOH HOH B . 
P 5 HOH 6  206 71  HOH HOH B . 
P 5 HOH 7  207 222 HOH HOH B . 
P 5 HOH 8  208 6   HOH HOH B . 
P 5 HOH 9  209 172 HOH HOH B . 
P 5 HOH 10 210 102 HOH HOH B . 
P 5 HOH 11 211 219 HOH HOH B . 
P 5 HOH 12 212 224 HOH HOH B . 
P 5 HOH 13 213 198 HOH HOH B . 
P 5 HOH 14 214 133 HOH HOH B . 
P 5 HOH 15 215 62  HOH HOH B . 
P 5 HOH 16 216 76  HOH HOH B . 
P 5 HOH 17 217 10  HOH HOH B . 
P 5 HOH 18 218 55  HOH HOH B . 
P 5 HOH 19 219 5   HOH HOH B . 
P 5 HOH 20 220 79  HOH HOH B . 
P 5 HOH 21 221 128 HOH HOH B . 
P 5 HOH 22 222 105 HOH HOH B . 
P 5 HOH 23 223 100 HOH HOH B . 
P 5 HOH 24 224 281 HOH HOH B . 
P 5 HOH 25 225 274 HOH HOH B . 
P 5 HOH 26 226 185 HOH HOH B . 
P 5 HOH 27 227 278 HOH HOH B . 
P 5 HOH 28 228 36  HOH HOH B . 
P 5 HOH 29 229 25  HOH HOH B . 
P 5 HOH 30 230 116 HOH HOH B . 
P 5 HOH 31 231 141 HOH HOH B . 
P 5 HOH 32 232 138 HOH HOH B . 
P 5 HOH 33 233 146 HOH HOH B . 
P 5 HOH 34 234 162 HOH HOH B . 
P 5 HOH 35 235 53  HOH HOH B . 
P 5 HOH 36 236 239 HOH HOH B . 
P 5 HOH 37 237 13  HOH HOH B . 
P 5 HOH 38 238 74  HOH HOH B . 
P 5 HOH 39 239 279 HOH HOH B . 
P 5 HOH 40 240 108 HOH HOH B . 
P 5 HOH 41 241 44  HOH HOH B . 
P 5 HOH 42 242 280 HOH HOH B . 
P 5 HOH 43 243 60  HOH HOH B . 
P 5 HOH 44 244 46  HOH HOH B . 
P 5 HOH 45 245 134 HOH HOH B . 
P 5 HOH 46 246 197 HOH HOH B . 
P 5 HOH 47 247 262 HOH HOH B . 
P 5 HOH 48 248 256 HOH HOH B . 
P 5 HOH 49 249 177 HOH HOH B . 
P 5 HOH 50 250 174 HOH HOH B . 
P 5 HOH 51 251 258 HOH HOH B . 
P 5 HOH 52 252 257 HOH HOH B . 
P 5 HOH 53 253 96  HOH HOH B . 
P 5 HOH 54 254 111 HOH HOH B . 
Q 5 HOH 1  201 214 HOH HOH C . 
Q 5 HOH 2  202 92  HOH HOH C . 
Q 5 HOH 3  203 131 HOH HOH C . 
Q 5 HOH 4  204 225 HOH HOH C . 
Q 5 HOH 5  205 68  HOH HOH C . 
Q 5 HOH 6  206 106 HOH HOH C . 
Q 5 HOH 7  207 159 HOH HOH C . 
Q 5 HOH 8  208 151 HOH HOH C . 
Q 5 HOH 9  209 237 HOH HOH C . 
Q 5 HOH 10 210 275 HOH HOH C . 
Q 5 HOH 11 211 220 HOH HOH C . 
Q 5 HOH 12 212 158 HOH HOH C . 
Q 5 HOH 13 213 127 HOH HOH C . 
Q 5 HOH 14 214 234 HOH HOH C . 
Q 5 HOH 15 215 135 HOH HOH C . 
Q 5 HOH 16 216 142 HOH HOH C . 
Q 5 HOH 17 217 64  HOH HOH C . 
Q 5 HOH 18 218 4   HOH HOH C . 
Q 5 HOH 19 219 94  HOH HOH C . 
Q 5 HOH 20 220 167 HOH HOH C . 
Q 5 HOH 21 221 186 HOH HOH C . 
Q 5 HOH 22 222 49  HOH HOH C . 
Q 5 HOH 23 223 119 HOH HOH C . 
Q 5 HOH 24 224 15  HOH HOH C . 
Q 5 HOH 25 225 45  HOH HOH C . 
Q 5 HOH 26 226 66  HOH HOH C . 
Q 5 HOH 27 227 228 HOH HOH C . 
Q 5 HOH 28 228 104 HOH HOH C . 
Q 5 HOH 29 229 175 HOH HOH C . 
Q 5 HOH 30 230 72  HOH HOH C . 
Q 5 HOH 31 231 211 HOH HOH C . 
Q 5 HOH 32 232 48  HOH HOH C . 
Q 5 HOH 33 233 163 HOH HOH C . 
Q 5 HOH 34 234 251 HOH HOH C . 
Q 5 HOH 35 235 57  HOH HOH C . 
Q 5 HOH 36 236 140 HOH HOH C . 
Q 5 HOH 37 237 51  HOH HOH C . 
Q 5 HOH 38 238 63  HOH HOH C . 
Q 5 HOH 39 239 39  HOH HOH C . 
Q 5 HOH 40 240 70  HOH HOH C . 
Q 5 HOH 41 241 117 HOH HOH C . 
Q 5 HOH 42 242 129 HOH HOH C . 
Q 5 HOH 43 243 261 HOH HOH C . 
Q 5 HOH 44 244 54  HOH HOH C . 
Q 5 HOH 45 245 149 HOH HOH C . 
Q 5 HOH 46 246 277 HOH HOH C . 
Q 5 HOH 47 247 52  HOH HOH C . 
Q 5 HOH 48 248 183 HOH HOH C . 
Q 5 HOH 49 249 284 HOH HOH C . 
Q 5 HOH 50 250 107 HOH HOH C . 
Q 5 HOH 51 251 207 HOH HOH C . 
Q 5 HOH 52 252 112 HOH HOH C . 
Q 5 HOH 53 253 205 HOH HOH C . 
Q 5 HOH 54 254 244 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 LYS 34 ? CG  ? B LYS 35 CG  
6  1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
7  1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
8  1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
9  1 Y 1 C ASP 26 ? CG  ? C ASP 27 CG  
10 1 Y 1 C ASP 26 ? OD1 ? C ASP 27 OD1 
11 1 Y 1 C ASP 26 ? OD2 ? C ASP 27 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 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                     9GRT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.144 
_cell.length_a_esd                 ? 
_cell.length_b                     41.633 
_cell.length_b_esd                 ? 
_cell.length_c                     157.277 
_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                         9GRT 
_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                   9GRT 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.30 
_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         2019-12-12 
_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                                       9GRT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.64 
_reflns.d_resolution_low                               78.64 
_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                                     34458 
_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                                11.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.74 
_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                                0.065 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       387976 
_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                              0.062 
_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                                    1.64 
_reflns_shell.d_res_low                                     1.72 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           50552 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4959 
_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                               10.2 
_reflns_shell.pdbx_chi_squared                              0.47 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               1.923 
_reflns_shell.pdbx_Rpim_I_all                               0.599 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.691 
_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                                  1.825 
_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                                 9GRT 
_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                            1.64 
_refine.ls_d_res_low                             40.25 
_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                     34364 
_refine.ls_number_reflns_R_free                  1655 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2316 
_refine.ls_R_factor_R_free                       0.2610 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2301 
_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                 31.15 
_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                            0.32 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.64 
_refine_hist.d_res_low                        40.25 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               2387 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2150 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 2290 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.807  ? 3102 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.010 ? 843  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 274  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 404  ? 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' 1.64 1.68  . . 123 2670 100.00 . . . . 0.5116 . . . . . . . . . . . 0.5375 
'X-RAY DIFFRACTION' 1.68 1.74  . . 141 2686 100.00 . . . . 0.4234 . . . . . . . . . . . 0.4989 
'X-RAY DIFFRACTION' 1.74 1.80  . . 145 2656 100.00 . . . . 0.3575 . . . . . . . . . . . 0.4095 
'X-RAY DIFFRACTION' 1.80 1.87  . . 116 2714 100.00 . . . . 0.2930 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 1.87 1.96  . . 164 2684 100.00 . . . . 0.2657 . . . . . . . . . . . 0.2705 
'X-RAY DIFFRACTION' 1.96 2.06  . . 151 2665 100.00 . . . . 0.2662 . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 2.06 2.19  . . 122 2720 100.00 . . . . 0.2704 . . . . . . . . . . . 0.3312 
'X-RAY DIFFRACTION' 2.19 2.36  . . 133 2717 100.00 . . . . 0.2576 . . . . . . . . . . . 0.3507 
'X-RAY DIFFRACTION' 2.36 2.60  . . 150 2704 100.00 . . . . 0.2554 . . . . . . . . . . . 0.3144 
'X-RAY DIFFRACTION' 2.60 2.97  . . 134 2774 100.00 . . . . 0.2508 . . . . . . . . . . . 0.2886 
'X-RAY DIFFRACTION' 2.97 3.74  . . 135 2785 100.00 . . . . 0.1996 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 3.74 40.25 . . 141 2934 100.00 . . . . 0.1902 . . . . . . . . . . . 0.1914 
# 
_struct.entry_id                     9GRT 
_struct.title                        'Crystal structure of HRP-2 PWWP domain in complex with compound 29' 
_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        9GRT 
_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 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 5 ? 
P N N 5 ? 
Q 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 9GRT A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 9GRT B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 9GRT 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 9GRT GLY A 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 1 
2 9GRT GLY B 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 2 
3 9GRT 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,G,O 
2 1 B,H,I,J,P   
3 1 C,K,L,M,N,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O 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 LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   9GRT 
_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 NZ B LYS 14  ? ? O B HOH 201 ? ? 2.00 
2 1 O4 C SO4 104 ? ? O C HOH 201 ? ? 2.11 
3 1 O  A HOH 236 ? ? O A HOH 264 ? ? 2.11 
4 1 O  C HOH 205 ? ? O C HOH 244 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     211 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     253 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.04 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -154.62 64.25 
2 1 HIS B 48 ? ? 57.93   20.00 
3 1 ASN B 87 ? ? -153.52 67.99 
# 
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 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 B VAL 33 ? B VAL 34 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ASP 27 ? C ASP 28 
12 1 Y 1 C ILE 28 ? C ILE 29 
13 1 Y 1 C ALA 29 ? C ALA 30 
14 1 Y 1 C ASP 30 ? C ASP 31 
15 1 Y 1 C GLY 31 ? C GLY 32 
16 1 Y 1 C ALA 32 ? C ALA 33 
17 1 Y 1 C VAL 33 ? C VAL 34 
18 1 Y 1 C LYS 34 ? C LYS 35 
19 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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BYZ BR4  BR N N 74  
BYZ C4   C  Y N 75  
BYZ C5   C  Y N 76  
BYZ N1   N  Y N 77  
BYZ N2   N  Y N 78  
BYZ C3   C  Y N 79  
BYZ H1   H  N N 80  
BYZ H2   H  N N 81  
BYZ H3   H  N N 82  
CYS N    N  N N 83  
CYS CA   C  N R 84  
CYS C    C  N N 85  
CYS O    O  N N 86  
CYS CB   C  N N 87  
CYS SG   S  N N 88  
CYS OXT  O  N N 89  
CYS H    H  N N 90  
CYS H2   H  N N 91  
CYS HA   H  N N 92  
CYS HB2  H  N N 93  
CYS HB3  H  N N 94  
CYS HG   H  N N 95  
CYS HXT  H  N N 96  
DMS S    S  N N 97  
DMS O    O  N N 98  
DMS C1   C  N N 99  
DMS C2   C  N N 100 
DMS H11  H  N N 101 
DMS H12  H  N N 102 
DMS H13  H  N N 103 
DMS H21  H  N N 104 
DMS H22  H  N N 105 
DMS H23  H  N N 106 
GLN N    N  N N 107 
GLN CA   C  N S 108 
GLN C    C  N N 109 
GLN O    O  N N 110 
GLN CB   C  N N 111 
GLN CG   C  N N 112 
GLN CD   C  N N 113 
GLN OE1  O  N N 114 
GLN NE2  N  N N 115 
GLN OXT  O  N N 116 
GLN H    H  N N 117 
GLN H2   H  N N 118 
GLN HA   H  N N 119 
GLN HB2  H  N N 120 
GLN HB3  H  N N 121 
GLN HG2  H  N N 122 
GLN HG3  H  N N 123 
GLN HE21 H  N N 124 
GLN HE22 H  N N 125 
GLN HXT  H  N N 126 
GLU N    N  N N 127 
GLU CA   C  N S 128 
GLU C    C  N N 129 
GLU O    O  N N 130 
GLU CB   C  N N 131 
GLU CG   C  N N 132 
GLU CD   C  N N 133 
GLU OE1  O  N N 134 
GLU OE2  O  N N 135 
GLU OXT  O  N N 136 
GLU H    H  N N 137 
GLU H2   H  N N 138 
GLU HA   H  N N 139 
GLU HB2  H  N N 140 
GLU HB3  H  N N 141 
GLU HG2  H  N N 142 
GLU HG3  H  N N 143 
GLU HE2  H  N N 144 
GLU HXT  H  N N 145 
GLY N    N  N N 146 
GLY CA   C  N N 147 
GLY C    C  N N 148 
GLY O    O  N N 149 
GLY OXT  O  N N 150 
GLY H    H  N N 151 
GLY H2   H  N N 152 
GLY HA2  H  N N 153 
GLY HA3  H  N N 154 
GLY HXT  H  N N 155 
HIS N    N  N N 156 
HIS CA   C  N S 157 
HIS C    C  N N 158 
HIS O    O  N N 159 
HIS CB   C  N N 160 
HIS CG   C  Y N 161 
HIS ND1  N  Y N 162 
HIS CD2  C  Y N 163 
HIS CE1  C  Y N 164 
HIS NE2  N  Y N 165 
HIS OXT  O  N N 166 
HIS H    H  N N 167 
HIS H2   H  N N 168 
HIS HA   H  N N 169 
HIS HB2  H  N N 170 
HIS HB3  H  N N 171 
HIS HD1  H  N N 172 
HIS HD2  H  N N 173 
HIS HE1  H  N N 174 
HIS HE2  H  N N 175 
HIS HXT  H  N N 176 
HOH O    O  N N 177 
HOH H1   H  N N 178 
HOH H2   H  N N 179 
ILE N    N  N N 180 
ILE CA   C  N S 181 
ILE C    C  N N 182 
ILE O    O  N N 183 
ILE CB   C  N S 184 
ILE CG1  C  N N 185 
ILE CG2  C  N N 186 
ILE CD1  C  N N 187 
ILE OXT  O  N N 188 
ILE H    H  N N 189 
ILE H2   H  N N 190 
ILE HA   H  N N 191 
ILE HB   H  N N 192 
ILE HG12 H  N N 193 
ILE HG13 H  N N 194 
ILE HG21 H  N N 195 
ILE HG22 H  N N 196 
ILE HG23 H  N N 197 
ILE HD11 H  N N 198 
ILE HD12 H  N N 199 
ILE HD13 H  N N 200 
ILE HXT  H  N N 201 
LEU N    N  N N 202 
LEU CA   C  N S 203 
LEU C    C  N N 204 
LEU O    O  N N 205 
LEU CB   C  N N 206 
LEU CG   C  N N 207 
LEU CD1  C  N N 208 
LEU CD2  C  N N 209 
LEU OXT  O  N N 210 
LEU H    H  N N 211 
LEU H2   H  N N 212 
LEU HA   H  N N 213 
LEU HB2  H  N N 214 
LEU HB3  H  N N 215 
LEU HG   H  N N 216 
LEU HD11 H  N N 217 
LEU HD12 H  N N 218 
LEU HD13 H  N N 219 
LEU HD21 H  N N 220 
LEU HD22 H  N N 221 
LEU HD23 H  N N 222 
LEU HXT  H  N N 223 
LYS N    N  N N 224 
LYS CA   C  N S 225 
LYS C    C  N N 226 
LYS O    O  N N 227 
LYS CB   C  N N 228 
LYS CG   C  N N 229 
LYS CD   C  N N 230 
LYS CE   C  N N 231 
LYS NZ   N  N N 232 
LYS OXT  O  N N 233 
LYS H    H  N N 234 
LYS H2   H  N N 235 
LYS HA   H  N N 236 
LYS HB2  H  N N 237 
LYS HB3  H  N N 238 
LYS HG2  H  N N 239 
LYS HG3  H  N N 240 
LYS HD2  H  N N 241 
LYS HD3  H  N N 242 
LYS HE2  H  N N 243 
LYS HE3  H  N N 244 
LYS HZ1  H  N N 245 
LYS HZ2  H  N N 246 
LYS HZ3  H  N N 247 
LYS HXT  H  N N 248 
MET N    N  N N 249 
MET CA   C  N S 250 
MET C    C  N N 251 
MET O    O  N N 252 
MET CB   C  N N 253 
MET CG   C  N N 254 
MET SD   S  N N 255 
MET CE   C  N N 256 
MET OXT  O  N N 257 
MET H    H  N N 258 
MET H2   H  N N 259 
MET HA   H  N N 260 
MET HB2  H  N N 261 
MET HB3  H  N N 262 
MET HG2  H  N N 263 
MET HG3  H  N N 264 
MET HE1  H  N N 265 
MET HE2  H  N N 266 
MET HE3  H  N N 267 
MET HXT  H  N N 268 
PHE N    N  N N 269 
PHE CA   C  N S 270 
PHE C    C  N N 271 
PHE O    O  N N 272 
PHE CB   C  N N 273 
PHE CG   C  Y N 274 
PHE CD1  C  Y N 275 
PHE CD2  C  Y N 276 
PHE CE1  C  Y N 277 
PHE CE2  C  Y N 278 
PHE CZ   C  Y N 279 
PHE OXT  O  N N 280 
PHE H    H  N N 281 
PHE H2   H  N N 282 
PHE HA   H  N N 283 
PHE HB2  H  N N 284 
PHE HB3  H  N N 285 
PHE HD1  H  N N 286 
PHE HD2  H  N N 287 
PHE HE1  H  N N 288 
PHE HE2  H  N N 289 
PHE HZ   H  N N 290 
PHE HXT  H  N N 291 
PRO N    N  N N 292 
PRO CA   C  N S 293 
PRO C    C  N N 294 
PRO O    O  N N 295 
PRO CB   C  N N 296 
PRO CG   C  N N 297 
PRO CD   C  N N 298 
PRO OXT  O  N N 299 
PRO H    H  N N 300 
PRO HA   H  N N 301 
PRO HB2  H  N N 302 
PRO HB3  H  N N 303 
PRO HG2  H  N N 304 
PRO HG3  H  N N 305 
PRO HD2  H  N N 306 
PRO HD3  H  N N 307 
PRO HXT  H  N N 308 
SER N    N  N N 309 
SER CA   C  N S 310 
SER C    C  N N 311 
SER O    O  N N 312 
SER CB   C  N N 313 
SER OG   O  N N 314 
SER OXT  O  N N 315 
SER H    H  N N 316 
SER H2   H  N N 317 
SER HA   H  N N 318 
SER HB2  H  N N 319 
SER HB3  H  N N 320 
SER HG   H  N N 321 
SER HXT  H  N N 322 
SO4 S    S  N N 323 
SO4 O1   O  N N 324 
SO4 O2   O  N N 325 
SO4 O3   O  N N 326 
SO4 O4   O  N N 327 
THR N    N  N N 328 
THR CA   C  N S 329 
THR C    C  N N 330 
THR O    O  N N 331 
THR CB   C  N R 332 
THR OG1  O  N N 333 
THR CG2  C  N N 334 
THR OXT  O  N N 335 
THR H    H  N N 336 
THR H2   H  N N 337 
THR HA   H  N N 338 
THR HB   H  N N 339 
THR HG1  H  N N 340 
THR HG21 H  N N 341 
THR HG22 H  N N 342 
THR HG23 H  N N 343 
THR HXT  H  N N 344 
TRP N    N  N N 345 
TRP CA   C  N S 346 
TRP C    C  N N 347 
TRP O    O  N N 348 
TRP CB   C  N N 349 
TRP CG   C  Y N 350 
TRP CD1  C  Y N 351 
TRP CD2  C  Y N 352 
TRP NE1  N  Y N 353 
TRP CE2  C  Y N 354 
TRP CE3  C  Y N 355 
TRP CZ2  C  Y N 356 
TRP CZ3  C  Y N 357 
TRP CH2  C  Y N 358 
TRP OXT  O  N N 359 
TRP H    H  N N 360 
TRP H2   H  N N 361 
TRP HA   H  N N 362 
TRP HB2  H  N N 363 
TRP HB3  H  N N 364 
TRP HD1  H  N N 365 
TRP HE1  H  N N 366 
TRP HE3  H  N N 367 
TRP HZ2  H  N N 368 
TRP HZ3  H  N N 369 
TRP HH2  H  N N 370 
TRP HXT  H  N N 371 
TYR N    N  N N 372 
TYR CA   C  N S 373 
TYR C    C  N N 374 
TYR O    O  N N 375 
TYR CB   C  N N 376 
TYR CG   C  Y N 377 
TYR CD1  C  Y N 378 
TYR CD2  C  Y N 379 
TYR CE1  C  Y N 380 
TYR CE2  C  Y N 381 
TYR CZ   C  Y N 382 
TYR OH   O  N N 383 
TYR OXT  O  N N 384 
TYR H    H  N N 385 
TYR H2   H  N N 386 
TYR HA   H  N N 387 
TYR HB2  H  N N 388 
TYR HB3  H  N N 389 
TYR HD1  H  N N 390 
TYR HD2  H  N N 391 
TYR HE1  H  N N 392 
TYR HE2  H  N N 393 
TYR HH   H  N N 394 
TYR HXT  H  N N 395 
VAL N    N  N N 396 
VAL CA   C  N S 397 
VAL C    C  N N 398 
VAL O    O  N N 399 
VAL CB   C  N N 400 
VAL CG1  C  N N 401 
VAL CG2  C  N N 402 
VAL OXT  O  N N 403 
VAL H    H  N N 404 
VAL H2   H  N N 405 
VAL HA   H  N N 406 
VAL HB   H  N N 407 
VAL HG11 H  N N 408 
VAL HG12 H  N N 409 
VAL HG13 H  N N 410 
VAL HG21 H  N N 411 
VAL HG22 H  N N 412 
VAL HG23 H  N N 413 
VAL HXT  H  N N 414 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BYZ N2  C3   doub Y N 70  
BYZ N2  N1   sing Y N 71  
BYZ C3  C4   sing Y N 72  
BYZ N1  C5   sing Y N 73  
BYZ C4  C5   doub Y N 74  
BYZ C4  BR4  sing N N 75  
BYZ C5  H1   sing N N 76  
BYZ N1  H2   sing N N 77  
BYZ C3  H3   sing N N 78  
CYS N   CA   sing N N 79  
CYS N   H    sing N N 80  
CYS N   H2   sing N N 81  
CYS CA  C    sing N N 82  
CYS CA  CB   sing N N 83  
CYS CA  HA   sing N N 84  
CYS C   O    doub N N 85  
CYS C   OXT  sing N N 86  
CYS CB  SG   sing N N 87  
CYS CB  HB2  sing N N 88  
CYS CB  HB3  sing N N 89  
CYS SG  HG   sing N N 90  
CYS OXT HXT  sing N N 91  
DMS S   O    doub N N 92  
DMS S   C1   sing N N 93  
DMS S   C2   sing N N 94  
DMS C1  H11  sing N N 95  
DMS C1  H12  sing N N 96  
DMS C1  H13  sing N N 97  
DMS C2  H21  sing N N 98  
DMS C2  H22  sing N N 99  
DMS C2  H23  sing N N 100 
GLN N   CA   sing N N 101 
GLN N   H    sing N N 102 
GLN N   H2   sing N N 103 
GLN CA  C    sing N N 104 
GLN CA  CB   sing N N 105 
GLN CA  HA   sing N N 106 
GLN C   O    doub N N 107 
GLN C   OXT  sing N N 108 
GLN CB  CG   sing N N 109 
GLN CB  HB2  sing N N 110 
GLN CB  HB3  sing N N 111 
GLN CG  CD   sing N N 112 
GLN CG  HG2  sing N N 113 
GLN CG  HG3  sing N N 114 
GLN CD  OE1  doub N N 115 
GLN CD  NE2  sing N N 116 
GLN NE2 HE21 sing N N 117 
GLN NE2 HE22 sing N N 118 
GLN OXT HXT  sing N N 119 
GLU N   CA   sing N N 120 
GLU N   H    sing N N 121 
GLU N   H2   sing N N 122 
GLU CA  C    sing N N 123 
GLU CA  CB   sing N N 124 
GLU CA  HA   sing N N 125 
GLU C   O    doub N N 126 
GLU C   OXT  sing N N 127 
GLU CB  CG   sing N N 128 
GLU CB  HB2  sing N N 129 
GLU CB  HB3  sing N N 130 
GLU CG  CD   sing N N 131 
GLU CG  HG2  sing N N 132 
GLU CG  HG3  sing N N 133 
GLU CD  OE1  doub N N 134 
GLU CD  OE2  sing N N 135 
GLU OE2 HE2  sing N N 136 
GLU OXT HXT  sing N N 137 
GLY N   CA   sing N N 138 
GLY N   H    sing N N 139 
GLY N   H2   sing N N 140 
GLY CA  C    sing N N 141 
GLY CA  HA2  sing N N 142 
GLY CA  HA3  sing N N 143 
GLY C   O    doub N N 144 
GLY C   OXT  sing N N 145 
GLY OXT HXT  sing N N 146 
HIS N   CA   sing N N 147 
HIS N   H    sing N N 148 
HIS N   H2   sing N N 149 
HIS CA  C    sing N N 150 
HIS CA  CB   sing N N 151 
HIS CA  HA   sing N N 152 
HIS C   O    doub N N 153 
HIS C   OXT  sing N N 154 
HIS CB  CG   sing N N 155 
HIS CB  HB2  sing N N 156 
HIS CB  HB3  sing N N 157 
HIS CG  ND1  sing Y N 158 
HIS CG  CD2  doub Y N 159 
HIS ND1 CE1  doub Y N 160 
HIS ND1 HD1  sing N N 161 
HIS CD2 NE2  sing Y N 162 
HIS CD2 HD2  sing N N 163 
HIS CE1 NE2  sing Y N 164 
HIS CE1 HE1  sing N N 165 
HIS NE2 HE2  sing N N 166 
HIS OXT HXT  sing N N 167 
HOH O   H1   sing N N 168 
HOH O   H2   sing N N 169 
ILE N   CA   sing N N 170 
ILE N   H    sing N N 171 
ILE N   H2   sing N N 172 
ILE CA  C    sing N N 173 
ILE CA  CB   sing N N 174 
ILE CA  HA   sing N N 175 
ILE C   O    doub N N 176 
ILE C   OXT  sing N N 177 
ILE CB  CG1  sing N N 178 
ILE CB  CG2  sing N N 179 
ILE CB  HB   sing N N 180 
ILE CG1 CD1  sing N N 181 
ILE CG1 HG12 sing N N 182 
ILE CG1 HG13 sing N N 183 
ILE CG2 HG21 sing N N 184 
ILE CG2 HG22 sing N N 185 
ILE CG2 HG23 sing N N 186 
ILE CD1 HD11 sing N N 187 
ILE CD1 HD12 sing N N 188 
ILE CD1 HD13 sing N N 189 
ILE OXT HXT  sing N N 190 
LEU N   CA   sing N N 191 
LEU N   H    sing N N 192 
LEU N   H2   sing N N 193 
LEU CA  C    sing N N 194 
LEU CA  CB   sing N N 195 
LEU CA  HA   sing N N 196 
LEU C   O    doub N N 197 
LEU C   OXT  sing N N 198 
LEU CB  CG   sing N N 199 
LEU CB  HB2  sing N N 200 
LEU CB  HB3  sing N N 201 
LEU CG  CD1  sing N N 202 
LEU CG  CD2  sing N N 203 
LEU CG  HG   sing N N 204 
LEU CD1 HD11 sing N N 205 
LEU CD1 HD12 sing N N 206 
LEU CD1 HD13 sing N N 207 
LEU CD2 HD21 sing N N 208 
LEU CD2 HD22 sing N N 209 
LEU CD2 HD23 sing N N 210 
LEU OXT HXT  sing N N 211 
LYS N   CA   sing N N 212 
LYS N   H    sing N N 213 
LYS N   H2   sing N N 214 
LYS CA  C    sing N N 215 
LYS CA  CB   sing N N 216 
LYS CA  HA   sing N N 217 
LYS C   O    doub N N 218 
LYS C   OXT  sing N N 219 
LYS CB  CG   sing N N 220 
LYS CB  HB2  sing N N 221 
LYS CB  HB3  sing N N 222 
LYS CG  CD   sing N N 223 
LYS CG  HG2  sing N N 224 
LYS CG  HG3  sing N N 225 
LYS CD  CE   sing N N 226 
LYS CD  HD2  sing N N 227 
LYS CD  HD3  sing N N 228 
LYS CE  NZ   sing N N 229 
LYS CE  HE2  sing N N 230 
LYS CE  HE3  sing N N 231 
LYS NZ  HZ1  sing N N 232 
LYS NZ  HZ2  sing N N 233 
LYS NZ  HZ3  sing N N 234 
LYS OXT HXT  sing N N 235 
MET N   CA   sing N N 236 
MET N   H    sing N N 237 
MET N   H2   sing N N 238 
MET CA  C    sing N N 239 
MET CA  CB   sing N N 240 
MET CA  HA   sing N N 241 
MET C   O    doub N N 242 
MET C   OXT  sing N N 243 
MET CB  CG   sing N N 244 
MET CB  HB2  sing N N 245 
MET CB  HB3  sing N N 246 
MET CG  SD   sing N N 247 
MET CG  HG2  sing N N 248 
MET CG  HG3  sing N N 249 
MET SD  CE   sing N N 250 
MET CE  HE1  sing N N 251 
MET CE  HE2  sing N N 252 
MET CE  HE3  sing N N 253 
MET OXT HXT  sing N N 254 
PHE N   CA   sing N N 255 
PHE N   H    sing N N 256 
PHE N   H2   sing N N 257 
PHE CA  C    sing N N 258 
PHE CA  CB   sing N N 259 
PHE CA  HA   sing N N 260 
PHE C   O    doub N N 261 
PHE C   OXT  sing N N 262 
PHE CB  CG   sing N N 263 
PHE CB  HB2  sing N N 264 
PHE CB  HB3  sing N N 265 
PHE CG  CD1  doub Y N 266 
PHE CG  CD2  sing Y N 267 
PHE CD1 CE1  sing Y N 268 
PHE CD1 HD1  sing N N 269 
PHE CD2 CE2  doub Y N 270 
PHE CD2 HD2  sing N N 271 
PHE CE1 CZ   doub Y N 272 
PHE CE1 HE1  sing N N 273 
PHE CE2 CZ   sing Y N 274 
PHE CE2 HE2  sing N N 275 
PHE CZ  HZ   sing N N 276 
PHE OXT HXT  sing N N 277 
PRO N   CA   sing N N 278 
PRO N   CD   sing N N 279 
PRO N   H    sing N N 280 
PRO CA  C    sing N N 281 
PRO CA  CB   sing N N 282 
PRO CA  HA   sing N N 283 
PRO C   O    doub N N 284 
PRO C   OXT  sing N N 285 
PRO CB  CG   sing N N 286 
PRO CB  HB2  sing N N 287 
PRO CB  HB3  sing N N 288 
PRO CG  CD   sing N N 289 
PRO CG  HG2  sing N N 290 
PRO CG  HG3  sing N N 291 
PRO CD  HD2  sing N N 292 
PRO CD  HD3  sing N N 293 
PRO OXT HXT  sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
SO4 S   O1   doub N N 308 
SO4 S   O2   doub N N 309 
SO4 S   O3   sing N N 310 
SO4 S   O4   sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TRP N   CA   sing N N 328 
TRP N   H    sing N N 329 
TRP N   H2   sing N N 330 
TRP CA  C    sing N N 331 
TRP CA  CB   sing N N 332 
TRP CA  HA   sing N N 333 
TRP C   O    doub N N 334 
TRP C   OXT  sing N N 335 
TRP CB  CG   sing N N 336 
TRP CB  HB2  sing N N 337 
TRP CB  HB3  sing N N 338 
TRP CG  CD1  doub Y N 339 
TRP CG  CD2  sing Y N 340 
TRP CD1 NE1  sing Y N 341 
TRP CD1 HD1  sing N N 342 
TRP CD2 CE2  doub Y N 343 
TRP CD2 CE3  sing Y N 344 
TRP NE1 CE2  sing Y N 345 
TRP NE1 HE1  sing N N 346 
TRP CE2 CZ2  sing Y N 347 
TRP CE3 CZ3  doub Y N 348 
TRP CE3 HE3  sing N N 349 
TRP CZ2 CH2  doub Y N 350 
TRP CZ2 HZ2  sing N N 351 
TRP CZ3 CH2  sing Y N 352 
TRP CZ3 HZ3  sing N N 353 
TRP CH2 HH2  sing N N 354 
TRP OXT HXT  sing N N 355 
TYR N   CA   sing N N 356 
TYR N   H    sing N N 357 
TYR N   H2   sing N N 358 
TYR CA  C    sing N N 359 
TYR CA  CB   sing N N 360 
TYR CA  HA   sing N N 361 
TYR C   O    doub N N 362 
TYR C   OXT  sing N N 363 
TYR CB  CG   sing N N 364 
TYR CB  HB2  sing N N 365 
TYR CB  HB3  sing N N 366 
TYR CG  CD1  doub Y N 367 
TYR CG  CD2  sing Y N 368 
TYR CD1 CE1  sing Y N 369 
TYR CD1 HD1  sing N N 370 
TYR CD2 CE2  doub Y N 371 
TYR CD2 HD2  sing N N 372 
TYR CE1 CZ   doub Y N 373 
TYR CE1 HE1  sing N N 374 
TYR CE2 CZ   sing Y N 375 
TYR CE2 HE2  sing N N 376 
TYR CZ  OH   sing N N 377 
TYR OH  HH   sing N N 378 
TYR OXT HXT  sing N N 379 
VAL N   CA   sing N N 380 
VAL N   H    sing N N 381 
VAL N   H2   sing N N 382 
VAL CA  C    sing N N 383 
VAL CA  CB   sing N N 384 
VAL CA  HA   sing N N 385 
VAL C   O    doub N N 386 
VAL C   OXT  sing N N 387 
VAL CB  CG1  sing N N 388 
VAL CB  CG2  sing N N 389 
VAL CB  HB   sing N N 390 
VAL CG1 HG11 sing N N 391 
VAL CG1 HG12 sing N N 392 
VAL CG1 HG13 sing N N 393 
VAL CG2 HG21 sing N N 394 
VAL CG2 HG22 sing N N 395 
VAL CG2 HG23 sing N N 396 
VAL OXT HXT  sing N N 397 
# 
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                    9GRT 
_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]   0.024305 
_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]   0.024019 
_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]   0.006358 
_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  ? 0.037   4.810   2.441   1.00 56.81  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 2  ? -0.959  4.052   1.695   1.00 45.20  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 2  ? -0.305  2.931   0.888   1.00 45.78  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 2  ? 0.853   3.041   0.487   1.00 47.15  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 2  ? -1.763  4.986   0.785   1.00 52.57  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 2  ? -2.988  5.587   1.472   1.00 63.71  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 2  ? -3.752  4.411   2.627   1.00 80.17  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 2  ? -5.346  5.141   2.900   1.00 52.81  ? 1   MET A CE  1 
ATOM   9    N  N   . PRO A 1 3  ? -1.041  1.841   0.675   1.00 44.02  ? 2   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 3  ? -0.473  0.695   -0.041  1.00 38.01  ? 2   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 3  ? -0.216  0.999   -1.506  1.00 39.38  ? 2   PRO A C   1 
ATOM   12   O  O   . PRO A 1 3  ? -0.916  1.792   -2.142  1.00 40.37  ? 2   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 3  ? -1.551  -0.387  0.116   1.00 33.72  ? 2   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 3  ? -2.256  -0.005  1.398   1.00 49.37  ? 2   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 3  ? -2.331  1.501   1.297   1.00 41.24  ? 2   PRO A CD  1 
ATOM   16   N  N   . HIS A 1 4  ? 0.814   0.353   -2.033  1.00 37.52  ? 3   HIS A N   1 
ATOM   17   C  CA  . HIS A 1 4  ? 1.118   0.379   -3.450  1.00 39.48  ? 3   HIS A CA  1 
ATOM   18   C  C   . HIS A 1 4  ? 0.678   -0.931  -4.088  1.00 35.98  ? 3   HIS A C   1 
ATOM   19   O  O   . HIS A 1 4  ? 0.325   -1.902  -3.410  1.00 38.69  ? 3   HIS A O   1 
ATOM   20   C  CB  . HIS A 1 4  ? 2.615   0.599   -3.680  1.00 45.63  ? 3   HIS A CB  1 
ATOM   21   C  CG  . HIS A 1 4  ? 3.215   1.635   -2.782  1.00 53.92  ? 3   HIS A CG  1 
ATOM   22   N  ND1 . HIS A 1 4  ? 4.083   1.320   -1.757  1.00 63.15  ? 3   HIS A ND1 1 
ATOM   23   C  CD2 . HIS A 1 4  ? 3.070   2.982   -2.753  1.00 57.47  ? 3   HIS A CD2 1 
ATOM   24   C  CE1 . HIS A 1 4  ? 4.448   2.431   -1.139  1.00 67.81  ? 3   HIS A CE1 1 
ATOM   25   N  NE2 . HIS A 1 4  ? 3.847   3.452   -1.723  1.00 62.81  ? 3   HIS A NE2 1 
ATOM   26   N  N   . ALA A 1 5  ? 0.707   -0.953  -5.416  1.00 32.36  ? 4   ALA A N   1 
ATOM   27   C  CA  . ALA A 1 5  ? 0.533   -2.216  -6.114  1.00 33.21  ? 4   ALA A CA  1 
ATOM   28   C  C   . ALA A 1 5  ? 1.650   -3.183  -5.714  1.00 34.35  ? 4   ALA A C   1 
ATOM   29   O  O   . ALA A 1 5  ? 2.727   -2.785  -5.258  1.00 33.24  ? 4   ALA A O   1 
ATOM   30   C  CB  . ALA A 1 5  ? 0.520   -1.994  -7.630  1.00 43.17  ? 4   ALA A CB  1 
ATOM   31   N  N   . PHE A 1 6  ? 1.379   -4.472  -5.873  1.00 31.86  ? 5   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 6  ? 2.414   -5.464  -5.639  1.00 30.98  ? 5   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 6  ? 3.524   -5.327  -6.673  1.00 32.82  ? 5   PHE A C   1 
ATOM   34   O  O   . PHE A 1 6  ? 3.295   -4.932  -7.822  1.00 35.96  ? 5   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 6  ? 1.829   -6.875  -5.690  1.00 28.96  ? 5   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 6  ? 1.098   -7.258  -4.436  1.00 34.59  ? 5   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 6  ? 1.805   -7.549  -3.279  1.00 30.21  ? 5   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 6  ? -0.289  -7.319  -4.411  1.00 32.55  ? 5   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 6  ? 1.148   -7.902  -2.118  1.00 29.49  ? 5   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 6  ? -0.957  -7.683  -3.235  1.00 30.35  ? 5   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 6  ? -0.232  -7.966  -2.098  1.00 24.77  ? 5   PHE A CZ  1 
ATOM   42   N  N   . LYS A 1 7  ? 4.736   -5.671  -6.257  1.00 28.01  ? 6   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7  ? 5.911   -5.631  -7.110  1.00 33.60  ? 6   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7  ? 6.763   -6.860  -6.833  1.00 29.30  ? 6   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7  ? 6.669   -7.460  -5.754  1.00 25.75  ? 6   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7  ? 6.725   -4.351  -6.873  1.00 29.42  ? 6   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7  ? 7.180   -4.200  -5.441  1.00 30.11  ? 6   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7  ? 8.021   -2.955  -5.245  1.00 38.49  ? 6   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7  ? 8.744   -3.049  -3.918  1.00 38.32  ? 6   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7  ? 7.753   -3.005  -2.823  1.00 40.64  ? 6   LYS A NZ  1 
ATOM   51   N  N   . PRO A 1 8  ? 7.603   -7.259  -7.790  1.00 28.27  ? 7   PRO A N   1 
ATOM   52   C  CA  . PRO A 1 8  ? 8.514   -8.389  -7.575  1.00 29.77  ? 7   PRO A CA  1 
ATOM   53   C  C   . PRO A 1 8  ? 9.363   -8.207  -6.327  1.00 29.06  ? 7   PRO A C   1 
ATOM   54   O  O   . PRO A 1 8  ? 9.871   -7.115  -6.047  1.00 27.89  ? 7   PRO A O   1 
ATOM   55   C  CB  . PRO A 1 8  ? 9.381   -8.382  -8.839  1.00 32.42  ? 7   PRO A CB  1 
ATOM   56   C  CG  . PRO A 1 8  ? 8.506   -7.764  -9.870  1.00 34.08  ? 7   PRO A CG  1 
ATOM   57   C  CD  . PRO A 1 8  ? 7.679   -6.745  -9.170  1.00 32.96  ? 7   PRO A CD  1 
ATOM   58   N  N   . GLY A 1 9  ? 9.509   -9.293  -5.573  1.00 25.87  ? 8   GLY A N   1 
ATOM   59   C  CA  . GLY A 1 9  ? 10.178  -9.288  -4.299  1.00 23.42  ? 8   GLY A CA  1 
ATOM   60   C  C   . GLY A 1 9  ? 9.263   -9.129  -3.096  1.00 25.26  ? 8   GLY A C   1 
ATOM   61   O  O   . GLY A 1 9  ? 9.683   -9.450  -1.977  1.00 27.04  ? 8   GLY A O   1 
ATOM   62   N  N   . ASP A 1 10 ? 8.031   -8.641  -3.282  1.00 21.29  ? 9   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 10 ? 7.110   -8.517  -2.148  1.00 22.33  ? 9   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 10 ? 6.825   -9.896  -1.536  1.00 25.10  ? 9   ASP A C   1 
ATOM   65   O  O   . ASP A 1 10 ? 6.618   -10.891 -2.248  1.00 24.08  ? 9   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 10 ? 5.777   -7.885  -2.567  1.00 20.29  ? 9   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 10 ? 5.879   -6.404  -2.829  1.00 27.58  ? 9   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 10 ? 6.894   -5.797  -2.444  1.00 29.31  ? 9   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 10 ? 4.907   -5.869  -3.398  1.00 26.12  ? 9   ASP A OD2 1 
ATOM   70   N  N   . LEU A 1 11 ? 6.801   -9.958  -0.205  1.00 18.82  ? 10  LEU A N   1 
ATOM   71   C  CA  . LEU A 1 11 ? 6.571   -11.229 0.482   1.00 18.78  ? 10  LEU A CA  1 
ATOM   72   C  C   . LEU A 1 11 ? 5.120   -11.302 0.940   1.00 21.80  ? 10  LEU A C   1 
ATOM   73   O  O   . LEU A 1 11 ? 4.566   -10.313 1.448   1.00 25.63  ? 10  LEU A O   1 
ATOM   74   C  CB  . LEU A 1 11 ? 7.511   -11.371 1.681   1.00 22.77  ? 10  LEU A CB  1 
ATOM   75   C  CG  . LEU A 1 11 ? 8.977   -11.191 1.292   1.00 24.38  ? 10  LEU A CG  1 
ATOM   76   C  CD1 . LEU A 1 11 ? 9.883   -11.366 2.495   1.00 26.41  ? 10  LEU A CD1 1 
ATOM   77   C  CD2 . LEU A 1 11 ? 9.360   -12.163 0.175   1.00 24.80  ? 10  LEU A CD2 1 
ATOM   78   N  N   . VAL A 1 12 ? 4.492   -12.459 0.739   1.00 19.86  ? 11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 12 ? 3.070   -12.612 0.970   1.00 19.73  ? 11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 12 ? 2.804   -13.973 1.604   1.00 21.10  ? 11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 12 ? 3.650   -14.875 1.620   1.00 22.16  ? 11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 12 ? 2.236   -12.495 -0.324  1.00 19.30  ? 11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 12 ? 2.409   -11.105 -0.966  1.00 21.29  ? 11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 12 ? 2.642   -13.600 -1.345  1.00 19.64  ? 11  VAL A CG2 1 
ATOM   85   N  N   . PHE A 1 13 ? 1.592   -14.112 2.118   1.00 21.68  ? 12  PHE A N   1 
ATOM   86   C  CA  . PHE A 1 13 ? 0.948   -15.415 2.171   1.00 22.98  ? 12  PHE A CA  1 
ATOM   87   C  C   . PHE A 1 13 ? -0.019  -15.472 1.003   1.00 22.86  ? 12  PHE A C   1 
ATOM   88   O  O   . PHE A 1 13 ? -0.806  -14.536 0.798   1.00 24.11  ? 12  PHE A O   1 
ATOM   89   C  CB  . PHE A 1 13 ? 0.205   -15.644 3.489   1.00 22.93  ? 12  PHE A CB  1 
ATOM   90   C  CG  . PHE A 1 13 ? 1.112   -15.771 4.657   1.00 23.48  ? 12  PHE A CG  1 
ATOM   91   C  CD1 . PHE A 1 13 ? 1.498   -14.623 5.352   1.00 26.27  ? 12  PHE A CD1 1 
ATOM   92   C  CD2 . PHE A 1 13 ? 1.614   -16.999 5.044   1.00 26.49  ? 12  PHE A CD2 1 
ATOM   93   C  CE1 . PHE A 1 13 ? 2.355   -14.717 6.420   1.00 29.17  ? 12  PHE A CE1 1 
ATOM   94   C  CE2 . PHE A 1 13 ? 2.471   -17.098 6.114   1.00 31.38  ? 12  PHE A CE2 1 
ATOM   95   C  CZ  . PHE A 1 13 ? 2.849   -15.952 6.801   1.00 30.18  ? 12  PHE A CZ  1 
ATOM   96   N  N   . ALA A 1 14 ? 0.051   -16.552 0.226   1.00 21.60  ? 13  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 14 ? -0.789  -16.687 -0.952  1.00 21.37  ? 13  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 14 ? -1.764  -17.831 -0.725  1.00 23.24  ? 13  ALA A C   1 
ATOM   99   O  O   . ALA A 1 14 ? -1.367  -18.895 -0.235  1.00 26.06  ? 13  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 14 ? 0.054   -16.957 -2.212  1.00 20.85  ? 13  ALA A CB  1 
ATOM   101  N  N   . LYS A 1 15 ? -3.025  -17.615 -1.078  1.00 26.87  ? 14  LYS A N   1 
ATOM   102  C  CA  . LYS A 1 15 ? -4.087  -18.576 -0.791  1.00 27.07  ? 14  LYS A CA  1 
ATOM   103  C  C   . LYS A 1 15 ? -4.528  -19.259 -2.079  1.00 34.27  ? 14  LYS A C   1 
ATOM   104  O  O   . LYS A 1 15 ? -4.952  -18.590 -3.033  1.00 35.51  ? 14  LYS A O   1 
ATOM   105  C  CB  . LYS A 1 15 ? -5.277  -17.885 -0.118  1.00 26.33  ? 14  LYS A CB  1 
ATOM   106  C  CG  . LYS A 1 15 ? -6.391  -18.821 0.315   1.00 35.88  ? 14  LYS A CG  1 
ATOM   107  C  CD  . LYS A 1 15 ? -5.964  -19.722 1.451   1.00 39.54  ? 14  LYS A CD  1 
ATOM   108  C  CE  . LYS A 1 15 ? -7.133  -20.569 1.938   1.00 40.29  ? 14  LYS A CE  1 
ATOM   109  N  NZ  . LYS A 1 15 ? -7.590  -21.544 0.909   1.00 35.92  ? 14  LYS A NZ  1 
ATOM   110  N  N   . MET A 1 16 ? -4.427  -20.586 -2.098  1.00 30.56  ? 15  MET A N   1 
ATOM   111  C  CA  . MET A 1 16 ? -4.977  -21.408 -3.160  1.00 34.45  ? 15  MET A CA  1 
ATOM   112  C  C   . MET A 1 16 ? -5.991  -22.373 -2.570  1.00 43.70  ? 15  MET A C   1 
ATOM   113  O  O   . MET A 1 16 ? -5.848  -22.822 -1.425  1.00 34.32  ? 15  MET A O   1 
ATOM   114  C  CB  . MET A 1 16 ? -3.893  -22.194 -3.873  1.00 35.89  ? 15  MET A CB  1 
ATOM   115  C  CG  . MET A 1 16 ? -2.713  -21.343 -4.271  1.00 42.38  ? 15  MET A CG  1 
ATOM   116  S  SD  . MET A 1 16 ? -2.175  -21.724 -5.930  1.00 40.28  ? 15  MET A SD  1 
ATOM   117  C  CE  . MET A 1 16 ? -3.674  -21.355 -6.828  1.00 48.27  ? 15  MET A CE  1 
ATOM   118  N  N   . LYS A 1 17 ? -7.024  -22.672 -3.361  1.00 44.98  ? 16  LYS A N   1 
ATOM   119  C  CA  . LYS A 1 17 ? -8.070  -23.585 -2.917  1.00 51.03  ? 16  LYS A CA  1 
ATOM   120  C  C   . LYS A 1 17 ? -7.455  -24.898 -2.458  1.00 40.92  ? 16  LYS A C   1 
ATOM   121  O  O   . LYS A 1 17 ? -6.522  -25.412 -3.077  1.00 36.38  ? 16  LYS A O   1 
ATOM   122  C  CB  . LYS A 1 17 ? -9.084  -23.839 -4.041  1.00 52.61  ? 16  LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 17 ? -10.531 -23.995 -3.534  1.00 61.39  ? 16  LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 17 ? -11.361 -24.949 -4.403  1.00 61.69  ? 16  LYS A CD  1 
ATOM   125  C  CE  . LYS A 1 17 ? -12.842 -24.917 -4.018  1.00 58.43  ? 16  LYS A CE  1 
ATOM   126  N  NZ  . LYS A 1 17 ? -13.690 -25.611 -5.033  1.00 54.99  ? 16  LYS A NZ  1 
ATOM   127  N  N   . GLY A 1 18 ? -7.964  -25.417 -1.342  1.00 38.35  ? 17  GLY A N   1 
ATOM   128  C  CA  . GLY A 1 18 ? -7.458  -26.622 -0.739  1.00 47.31  ? 17  GLY A CA  1 
ATOM   129  C  C   . GLY A 1 18 ? -6.178  -26.460 0.045   1.00 40.08  ? 17  GLY A C   1 
ATOM   130  O  O   . GLY A 1 18 ? -5.720  -27.432 0.654   1.00 40.44  ? 17  GLY A O   1 
ATOM   131  N  N   . TYR A 1 19 ? -5.593  -25.268 0.070   1.00 38.55  ? 18  TYR A N   1 
ATOM   132  C  CA  . TYR A 1 19 ? -4.335  -25.082 0.757   1.00 35.18  ? 18  TYR A CA  1 
ATOM   133  C  C   . TYR A 1 19 ? -4.460  -23.992 1.809   1.00 26.04  ? 18  TYR A C   1 
ATOM   134  O  O   . TYR A 1 19 ? -5.235  -23.050 1.634   1.00 33.78  ? 18  TYR A O   1 
ATOM   135  C  CB  . TYR A 1 19 ? -3.219  -24.695 -0.218  1.00 40.62  ? 18  TYR A CB  1 
ATOM   136  C  CG  . TYR A 1 19 ? -2.757  -25.797 -1.155  1.00 39.48  ? 18  TYR A CG  1 
ATOM   137  C  CD1 . TYR A 1 19 ? -1.906  -26.794 -0.708  1.00 46.22  ? 18  TYR A CD1 1 
ATOM   138  C  CD2 . TYR A 1 19 ? -3.133  -25.798 -2.492  1.00 42.75  ? 18  TYR A CD2 1 
ATOM   139  C  CE1 . TYR A 1 19 ? -1.460  -27.779 -1.557  1.00 55.81  ? 18  TYR A CE1 1 
ATOM   140  C  CE2 . TYR A 1 19 ? -2.692  -26.783 -3.354  1.00 46.93  ? 18  TYR A CE2 1 
ATOM   141  C  CZ  . TYR A 1 19 ? -1.854  -27.775 -2.880  1.00 61.60  ? 18  TYR A CZ  1 
ATOM   142  O  OH  . TYR A 1 19 ? -1.401  -28.767 -3.725  1.00 65.30  ? 18  TYR A OH  1 
ATOM   143  N  N   . PRO A 1 20 ? -3.712  -24.092 2.904   1.00 31.90  ? 19  PRO A N   1 
ATOM   144  C  CA  . PRO A 1 20 ? -3.647  -22.975 3.843   1.00 34.90  ? 19  PRO A CA  1 
ATOM   145  C  C   . PRO A 1 20 ? -2.903  -21.811 3.205   1.00 28.67  ? 19  PRO A C   1 
ATOM   146  O  O   . PRO A 1 20 ? -2.132  -21.984 2.261   1.00 28.92  ? 19  PRO A O   1 
ATOM   147  C  CB  . PRO A 1 20 ? -2.869  -23.544 5.029   1.00 32.92  ? 19  PRO A CB  1 
ATOM   148  C  CG  . PRO A 1 20 ? -1.991  -24.595 4.414   1.00 31.83  ? 19  PRO A CG  1 
ATOM   149  C  CD  . PRO A 1 20 ? -2.764  -25.167 3.247   1.00 36.50  ? 19  PRO A CD  1 
ATOM   150  N  N   . HIS A 1 21 ? -3.140  -20.621 3.745   1.00 31.47  ? 20  HIS A N   1 
ATOM   151  C  CA  . HIS A 1 21 ? -2.364  -19.449 3.349   1.00 29.11  ? 20  HIS A CA  1 
ATOM   152  C  C   . HIS A 1 21 ? -0.875  -19.764 3.453   1.00 29.25  ? 20  HIS A C   1 
ATOM   153  O  O   . HIS A 1 21 ? -0.388  -20.167 4.514   1.00 28.77  ? 20  HIS A O   1 
ATOM   154  C  CB  . HIS A 1 21 ? -2.728  -18.254 4.229   1.00 30.30  ? 20  HIS A CB  1 
ATOM   155  C  CG  . HIS A 1 21 ? -4.171  -17.841 4.138   1.00 36.59  ? 20  HIS A CG  1 
ATOM   156  N  ND1 . HIS A 1 21 ? -5.191  -18.537 4.758   1.00 36.79  ? 20  HIS A ND1 1 
ATOM   157  C  CD2 . HIS A 1 21 ? -4.761  -16.794 3.511   1.00 36.03  ? 20  HIS A CD2 1 
ATOM   158  C  CE1 . HIS A 1 21 ? -6.344  -17.940 4.509   1.00 33.65  ? 20  HIS A CE1 1 
ATOM   159  N  NE2 . HIS A 1 21 ? -6.111  -16.876 3.759   1.00 36.98  ? 20  HIS A NE2 1 
ATOM   160  N  N   . TRP A 1 22 ? -0.141  -19.568 2.344   1.00 25.40  ? 21  TRP A N   1 
ATOM   161  C  CA  . TRP A 1 22 ? 1.159   -20.216 2.193   1.00 22.86  ? 21  TRP A CA  1 
ATOM   162  C  C   . TRP A 1 22 ? 2.257   -19.180 1.989   1.00 24.79  ? 21  TRP A C   1 
ATOM   163  O  O   . TRP A 1 22 ? 2.078   -18.263 1.177   1.00 22.84  ? 21  TRP A O   1 
ATOM   164  C  CB  . TRP A 1 22 ? 1.140   -21.168 0.978   1.00 24.01  ? 21  TRP A CB  1 
ATOM   165  C  CG  . TRP A 1 22 ? 2.210   -22.203 0.986   1.00 24.89  ? 21  TRP A CG  1 
ATOM   166  C  CD1 . TRP A 1 22 ? 3.537   -22.028 0.715   1.00 21.73  ? 21  TRP A CD1 1 
ATOM   167  C  CD2 . TRP A 1 22 ? 2.052   -23.610 1.292   1.00 28.04  ? 21  TRP A CD2 1 
ATOM   168  N  NE1 . TRP A 1 22 ? 4.210   -23.235 0.823   1.00 29.46  ? 21  TRP A NE1 1 
ATOM   169  C  CE2 . TRP A 1 22 ? 3.322   -24.210 1.184   1.00 28.53  ? 21  TRP A CE2 1 
ATOM   170  C  CE3 . TRP A 1 22 ? 0.955   -24.411 1.642   1.00 32.83  ? 21  TRP A CE3 1 
ATOM   171  C  CZ2 . TRP A 1 22 ? 3.526   -25.583 1.395   1.00 27.57  ? 21  TRP A CZ2 1 
ATOM   172  C  CZ3 . TRP A 1 22 ? 1.164   -25.768 1.856   1.00 26.63  ? 21  TRP A CZ3 1 
ATOM   173  C  CH2 . TRP A 1 22 ? 2.436   -26.331 1.730   1.00 32.23  ? 21  TRP A CH2 1 
ATOM   174  N  N   . PRO A 1 23 ? 3.400   -19.308 2.677   1.00 23.03  ? 22  PRO A N   1 
ATOM   175  C  CA  . PRO A 1 23 ? 4.479   -18.326 2.502   1.00 22.23  ? 22  PRO A CA  1 
ATOM   176  C  C   . PRO A 1 23 ? 4.971   -18.320 1.062   1.00 22.61  ? 22  PRO A C   1 
ATOM   177  O  O   . PRO A 1 23 ? 5.301   -19.365 0.496   1.00 22.32  ? 22  PRO A O   1 
ATOM   178  C  CB  . PRO A 1 23 ? 5.568   -18.801 3.470   1.00 22.33  ? 22  PRO A CB  1 
ATOM   179  C  CG  . PRO A 1 23 ? 5.299   -20.287 3.624   1.00 22.07  ? 22  PRO A CG  1 
ATOM   180  C  CD  . PRO A 1 23 ? 3.809   -20.438 3.531   1.00 23.77  ? 22  PRO A CD  1 
ATOM   181  N  N   . ALA A 1 24 ? 5.022   -17.128 0.477   1.00 20.71  ? 23  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 24 ? 5.360   -16.998 -0.938  1.00 20.28  ? 23  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 24 ? 5.937   -15.609 -1.218  1.00 19.07  ? 23  ALA A C   1 
ATOM   184  O  O   . ALA A 1 24 ? 5.952   -14.733 -0.354  1.00 19.64  ? 23  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 24 ? 4.128   -17.261 -1.810  1.00 22.27  ? 23  ALA A CB  1 
ATOM   186  N  N   . ARG A 1 25 ? 6.424   -15.427 -2.451  1.00 21.13  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 25 ? 6.853   -14.107 -2.907  1.00 21.40  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 25 ? 6.320   -13.849 -4.308  1.00 22.08  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 25 ? 6.003   -14.777 -5.066  1.00 22.90  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 25 ? 8.377   -13.958 -2.912  1.00 20.52  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 25 ? 9.063   -14.909 -3.877  1.00 24.33  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 25 ? 10.570  -14.831 -3.768  1.00 24.92  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 25 ? 11.188  -15.580 -4.864  1.00 26.43  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 25 ? 12.429  -16.047 -4.852  1.00 29.50  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 25 ? 13.214  -15.893 -3.800  1.00 27.16  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 25 ? 12.902  -16.659 -5.934  1.00 32.33  ? 24  ARG A NH2 1 
ATOM   197  N  N   . ILE A 1 26 ? 6.236   -12.567 -4.641  1.00 21.10  ? 25  ILE A N   1 
ATOM   198  C  CA  . ILE A 1 26 ? 6.072   -12.136 -6.028  1.00 20.78  ? 25  ILE A CA  1 
ATOM   199  C  C   . ILE A 1 26 ? 7.398   -12.326 -6.740  1.00 22.63  ? 25  ILE A C   1 
ATOM   200  O  O   . ILE A 1 26 ? 8.403   -11.712 -6.376  1.00 25.68  ? 25  ILE A O   1 
ATOM   201  C  CB  . ILE A 1 26 ? 5.636   -10.668 -6.099  1.00 23.92  ? 25  ILE A CB  1 
ATOM   202  C  CG1 . ILE A 1 26 ? 4.511   -10.370 -5.105  1.00 30.70  ? 25  ILE A CG1 1 
ATOM   203  C  CG2 . ILE A 1 26 ? 5.348   -10.269 -7.558  1.00 25.95  ? 25  ILE A CG2 1 
ATOM   204  C  CD1 . ILE A 1 26 ? 3.141   -10.736 -5.540  1.00 31.22  ? 25  ILE A CD1 1 
ATOM   205  N  N   . ASP A 1 27 ? 7.415   -13.191 -7.745  1.00 24.93  ? 26  ASP A N   1 
ATOM   206  C  CA  . ASP A 1 27 ? 8.636   -13.389 -8.498  1.00 30.31  ? 26  ASP A CA  1 
ATOM   207  C  C   . ASP A 1 27 ? 8.814   -12.306 -9.561  1.00 29.77  ? 26  ASP A C   1 
ATOM   208  O  O   . ASP A 1 27 ? 7.873   -11.611 -9.961  1.00 28.30  ? 26  ASP A O   1 
ATOM   209  C  CB  . ASP A 1 27 ? 8.617   -14.756 -9.175  1.00 28.69  ? 26  ASP A CB  1 
ATOM   210  C  CG  . ASP A 1 27 ? 9.620   -15.722 -8.588  1.00 25.52  ? 26  ASP A CG  1 
ATOM   211  O  OD1 . ASP A 1 27 ? 10.337  -15.374 -7.616  1.00 32.76  ? 26  ASP A OD1 1 
ATOM   212  O  OD2 . ASP A 1 27 ? 9.684   -16.850 -9.108  1.00 30.92  ? 26  ASP A OD2 1 
ATOM   213  N  N   . ASP A 1 28 ? 10.055  -12.158 -10.005 1.00 34.61  ? 27  ASP A N   1 
ATOM   214  C  CA  . ASP A 1 28 ? 10.286  -11.473 -11.256 1.00 34.44  ? 27  ASP A CA  1 
ATOM   215  C  C   . ASP A 1 28 ? 9.978   -12.427 -12.401 1.00 29.69  ? 27  ASP A C   1 
ATOM   216  O  O   . ASP A 1 28 ? 9.780   -13.627 -12.212 1.00 35.79  ? 27  ASP A O   1 
ATOM   217  C  CB  . ASP A 1 28 ? 11.725  -10.980 -11.361 1.00 41.65  ? 27  ASP A CB  1 
ATOM   218  C  CG  . ASP A 1 28 ? 11.862  -9.512  -11.014 1.00 60.99  ? 27  ASP A CG  1 
ATOM   219  O  OD1 . ASP A 1 28 ? 12.509  -9.199  -9.986  1.00 64.94  ? 27  ASP A OD1 1 
ATOM   220  O  OD2 . ASP A 1 28 ? 11.304  -8.674  -11.761 1.00 55.79  ? 27  ASP A OD2 1 
ATOM   221  N  N   . ILE A 1 29 ? 9.934   -11.885 -13.604 1.00 35.24  ? 28  ILE A N   1 
ATOM   222  C  CA  . ILE A 1 29 ? 9.833   -12.701 -14.805 1.00 38.02  ? 28  ILE A CA  1 
ATOM   223  C  C   . ILE A 1 29 ? 11.172  -12.590 -15.508 1.00 36.35  ? 28  ILE A C   1 
ATOM   224  O  O   . ILE A 1 29 ? 11.601  -11.486 -15.852 1.00 37.47  ? 28  ILE A O   1 
ATOM   225  C  CB  . ILE A 1 29 ? 8.675   -12.249 -15.701 1.00 41.02  ? 28  ILE A CB  1 
ATOM   226  C  CG1 . ILE A 1 29 ? 7.369   -12.302 -14.911 1.00 37.21  ? 28  ILE A CG1 1 
ATOM   227  C  CG2 . ILE A 1 29 ? 8.595   -13.144 -16.937 1.00 42.15  ? 28  ILE A CG2 1 
ATOM   228  C  CD1 . ILE A 1 29 ? 6.368   -11.247 -15.314 1.00 40.40  ? 28  ILE A CD1 1 
ATOM   229  N  N   . ALA A 1 30 ? 11.861  -13.715 -15.656 1.00 43.19  ? 29  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 30 ? 13.147  -13.691 -16.336 1.00 45.11  ? 29  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 30 ? 12.961  -13.339 -17.811 1.00 40.06  ? 29  ALA A C   1 
ATOM   232  O  O   . ALA A 1 30 ? 11.894  -13.551 -18.396 1.00 35.27  ? 29  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 30 ? 13.858  -15.035 -16.201 1.00 36.56  ? 29  ALA A CB  1 
ATOM   234  N  N   . ASP A 1 31 ? 13.999  -12.738 -18.391 1.00 40.65  ? 30  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 31 ? 14.003  -12.490 -19.826 1.00 44.29  ? 30  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 31 ? 13.748  -13.793 -20.566 1.00 30.90  ? 30  ASP A C   1 
ATOM   237  O  O   . ASP A 1 31 ? 14.400  -14.804 -20.303 1.00 37.85  ? 30  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 31 ? 15.341  -11.884 -20.257 1.00 42.26  ? 30  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 31 ? 15.418  -10.394 -20.009 1.00 43.05  ? 30  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 31 ? 14.355  -9.737  -19.921 1.00 43.68  ? 30  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 31 ? 16.550  -9.872  -19.931 1.00 49.88  ? 30  ASP A OD2 1 
ATOM   242  N  N   . GLY A 1 32 ? 12.784  -13.775 -21.489 1.00 37.03  ? 31  GLY A N   1 
ATOM   243  C  CA  . GLY A 1 32 ? 12.470  -14.971 -22.245 1.00 33.54  ? 31  GLY A CA  1 
ATOM   244  C  C   . GLY A 1 32 ? 11.603  -15.988 -21.536 1.00 40.30  ? 31  GLY A C   1 
ATOM   245  O  O   . GLY A 1 32 ? 11.276  -17.022 -22.136 1.00 35.98  ? 31  GLY A O   1 
ATOM   246  N  N   . ALA A 1 33 ? 11.228  -15.744 -20.285 1.00 39.89  ? 32  ALA A N   1 
ATOM   247  C  CA  . ALA A 1 33 ? 10.377  -16.669 -19.551 1.00 38.18  ? 32  ALA A CA  1 
ATOM   248  C  C   . ALA A 1 33 ? 8.907   -16.367 -19.825 1.00 32.74  ? 32  ALA A C   1 
ATOM   249  O  O   . ALA A 1 33 ? 8.542   -15.281 -20.280 1.00 32.98  ? 32  ALA A O   1 
ATOM   250  C  CB  . ALA A 1 33 ? 10.659  -16.581 -18.046 1.00 40.00  ? 32  ALA A CB  1 
ATOM   251  N  N   . VAL A 1 34 ? 8.058   -17.355 -19.535 1.00 35.69  ? 33  VAL A N   1 
ATOM   252  C  CA  . VAL A 1 34 ? 6.624   -17.215 -19.771 1.00 33.51  ? 33  VAL A CA  1 
ATOM   253  C  C   . VAL A 1 34 ? 6.048   -16.143 -18.853 1.00 34.79  ? 33  VAL A C   1 
ATOM   254  O  O   . VAL A 1 34 ? 6.286   -16.146 -17.640 1.00 41.13  ? 33  VAL A O   1 
ATOM   255  C  CB  . VAL A 1 34 ? 5.911   -18.560 -19.561 1.00 35.26  ? 33  VAL A CB  1 
ATOM   256  C  CG1 . VAL A 1 34 ? 4.404   -18.365 -19.652 1.00 37.53  ? 33  VAL A CG1 1 
ATOM   257  C  CG2 . VAL A 1 34 ? 6.394   -19.593 -20.587 1.00 35.97  ? 33  VAL A CG2 1 
ATOM   258  N  N   . LYS A 1 35 ? 5.296   -15.240 -19.415 1.00 32.81  ? 34  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 35 ? 4.595   -14.173 -18.719 1.00 32.81  ? 34  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 35 ? 3.253   -14.669 -18.184 1.00 35.47  ? 34  LYS A C   1 
ATOM   261  O  O   . LYS A 1 35 ? 2.645   -15.578 -18.755 1.00 35.95  ? 34  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 35 ? 4.365   -12.994 -19.656 1.00 38.57  ? 34  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 35 ? 5.615   -12.186 -19.943 1.00 39.89  ? 34  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 35 ? 5.317   -11.047 -20.903 1.00 43.71  ? 34  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 35 ? 4.972   -11.586 -22.282 1.00 42.46  ? 34  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 35 ? 4.851   -10.491 -23.276 1.00 51.84  ? 34  LYS A NZ  1 
ATOM   267  N  N   . PRO A 1 36 ? 2.767   -14.082 -17.094 1.00 39.86  ? 35  PRO A N   1 
ATOM   268  C  CA  . PRO A 1 36 ? 1.468   -14.472 -16.565 1.00 37.28  ? 35  PRO A CA  1 
ATOM   269  C  C   . PRO A 1 36 ? 0.348   -13.826 -17.356 1.00 36.89  ? 35  PRO A C   1 
ATOM   270  O  O   . PRO A 1 36 ? 0.582   -12.888 -18.137 1.00 41.48  ? 35  PRO A O   1 
ATOM   271  C  CB  . PRO A 1 36 ? 1.500   -13.945 -15.116 1.00 39.03  ? 35  PRO A CB  1 
ATOM   272  C  CG  . PRO A 1 36 ? 2.768   -13.138 -14.978 1.00 42.28  ? 35  PRO A CG  1 
ATOM   273  C  CD  . PRO A 1 36 ? 3.331   -12.943 -16.353 1.00 40.77  ? 35  PRO A CD  1 
ATOM   274  N  N   . PRO A 1 37 ? -0.886  -14.288 -17.170 1.00 38.82  ? 36  PRO A N   1 
ATOM   275  C  CA  . PRO A 1 37 ? -2.048  -13.618 -17.771 1.00 42.49  ? 36  PRO A CA  1 
ATOM   276  C  C   . PRO A 1 37 ? -2.188  -12.190 -17.269 1.00 49.73  ? 36  PRO A C   1 
ATOM   277  O  O   . PRO A 1 37 ? -1.506  -11.789 -16.311 1.00 45.41  ? 36  PRO A O   1 
ATOM   278  C  CB  . PRO A 1 37 ? -3.226  -14.488 -17.303 1.00 43.51  ? 36  PRO A CB  1 
ATOM   279  C  CG  . PRO A 1 37 ? -2.623  -15.817 -16.992 1.00 49.46  ? 36  PRO A CG  1 
ATOM   280  C  CD  . PRO A 1 37 ? -1.266  -15.518 -16.454 1.00 41.25  ? 36  PRO A CD  1 
ATOM   281  N  N   . PRO A 1 38 ? -3.064  -11.388 -17.884 1.00 45.82  ? 37  PRO A N   1 
ATOM   282  C  CA  . PRO A 1 38 ? -3.250  -10.002 -17.427 1.00 49.40  ? 37  PRO A CA  1 
ATOM   283  C  C   . PRO A 1 38 ? -3.757  -9.926  -15.994 1.00 43.29  ? 37  PRO A C   1 
ATOM   284  O  O   . PRO A 1 38 ? -4.617  -10.701 -15.575 1.00 45.91  ? 37  PRO A O   1 
ATOM   285  C  CB  . PRO A 1 38 ? -4.285  -9.442  -18.408 1.00 47.74  ? 37  PRO A CB  1 
ATOM   286  C  CG  . PRO A 1 38 ? -4.139  -10.279 -19.624 1.00 48.53  ? 37  PRO A CG  1 
ATOM   287  C  CD  . PRO A 1 38 ? -3.805  -11.656 -19.130 1.00 49.99  ? 37  PRO A CD  1 
ATOM   288  N  N   . ASN A 1 39 ? -3.223  -8.958  -15.250 1.00 50.78  ? 38  ASN A N   1 
ATOM   289  C  CA  . ASN A 1 39 ? -3.588  -8.696  -13.859 1.00 52.05  ? 38  ASN A CA  1 
ATOM   290  C  C   . ASN A 1 39 ? -3.302  -9.885  -12.950 1.00 47.35  ? 38  ASN A C   1 
ATOM   291  O  O   . ASN A 1 39 ? -3.880  -9.995  -11.864 1.00 46.75  ? 38  ASN A O   1 
ATOM   292  C  CB  . ASN A 1 39 ? -5.058  -8.271  -13.733 1.00 58.48  ? 38  ASN A CB  1 
ATOM   293  C  CG  . ASN A 1 39 ? -5.336  -6.934  -14.399 1.00 58.65  ? 38  ASN A CG  1 
ATOM   294  O  OD1 . ASN A 1 39 ? -4.519  -6.006  -14.329 1.00 67.04  ? 38  ASN A OD1 1 
ATOM   295  N  ND2 . ASN A 1 39 ? -6.488  -6.828  -15.054 1.00 58.55  ? 38  ASN A ND2 1 
ATOM   296  N  N   . LYS A 1 40 ? -2.418  -10.783 -13.369 1.00 42.44  ? 39  LYS A N   1 
ATOM   297  C  CA  . LYS A 1 40 ? -1.915  -11.829 -12.494 1.00 36.24  ? 39  LYS A CA  1 
ATOM   298  C  C   . LYS A 1 40 ? -0.422  -11.630 -12.258 1.00 30.40  ? 39  LYS A C   1 
ATOM   299  O  O   . LYS A 1 40 ? 0.264   -10.920 -13.000 1.00 32.59  ? 39  LYS A O   1 
ATOM   300  C  CB  . LYS A 1 40 ? -2.193  -13.210 -13.066 1.00 36.77  ? 39  LYS A CB  1 
ATOM   301  C  CG  . LYS A 1 40 ? -3.668  -13.473 -13.317 1.00 43.89  ? 39  LYS A CG  1 
ATOM   302  C  CD  . LYS A 1 40 ? -4.454  -13.482 -12.021 1.00 41.74  ? 39  LYS A CD  1 
ATOM   303  C  CE  . LYS A 1 40 ? -5.911  -13.864 -12.248 1.00 48.89  ? 39  LYS A CE  1 
ATOM   304  N  NZ  . LYS A 1 40 ? -6.025  -15.298 -12.635 1.00 54.11  ? 39  LYS A NZ  1 
ATOM   305  N  N   . TYR A 1 41 ? 0.066   -12.237 -11.182 1.00 26.91  ? 40  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 41 ? 1.452   -12.178 -10.775 1.00 25.39  ? 40  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 41 ? 2.036   -13.579 -10.697 1.00 23.33  ? 40  TYR A C   1 
ATOM   308  O  O   . TYR A 1 41 ? 1.332   -14.524 -10.329 1.00 26.35  ? 40  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 41 ? 1.587   -11.524 -9.394  1.00 21.53  ? 40  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 41 ? 1.239   -10.056 -9.389  1.00 21.06  ? 40  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 41 ? 2.209   -9.095  -9.601  1.00 28.82  ? 40  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 41 ? -0.068  -9.645  -9.176  1.00 28.21  ? 40  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 41 ? 1.896   -7.755  -9.579  1.00 28.88  ? 40  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 41 ? -0.392  -8.296  -9.174  1.00 30.47  ? 40  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 41 ? 0.594   -7.366  -9.376  1.00 32.33  ? 40  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 41 ? 0.265   -6.026  -9.369  1.00 43.81  ? 40  TYR A OH  1 
ATOM   317  N  N   . PRO A 1 42 ? 3.322   -13.752 -11.011 1.00 23.56  ? 41  PRO A N   1 
ATOM   318  C  CA  . PRO A 1 42 ? 3.963   -15.057 -10.766 1.00 23.98  ? 41  PRO A CA  1 
ATOM   319  C  C   . PRO A 1 42 ? 4.265   -15.190 -9.281  1.00 24.74  ? 41  PRO A C   1 
ATOM   320  O  O   . PRO A 1 42 ? 4.980   -14.363 -8.710  1.00 25.51  ? 41  PRO A O   1 
ATOM   321  C  CB  . PRO A 1 42 ? 5.248   -14.989 -11.599 1.00 27.58  ? 41  PRO A CB  1 
ATOM   322  C  CG  . PRO A 1 42 ? 5.577   -13.506 -11.634 1.00 30.40  ? 41  PRO A CG  1 
ATOM   323  C  CD  . PRO A 1 42 ? 4.258   -12.753 -11.554 1.00 23.40  ? 41  PRO A CD  1 
ATOM   324  N  N   . ILE A 1 43 ? 3.676   -16.199 -8.645  1.00 19.39  ? 42  ILE A N   1 
ATOM   325  C  CA  . ILE A 1 43 ? 3.815   -16.380 -7.203  1.00 21.47  ? 42  ILE A CA  1 
ATOM   326  C  C   . ILE A 1 43 ? 4.692   -17.595 -6.974  1.00 24.62  ? 42  ILE A C   1 
ATOM   327  O  O   . ILE A 1 43 ? 4.339   -18.718 -7.367  1.00 28.14  ? 42  ILE A O   1 
ATOM   328  C  CB  . ILE A 1 43 ? 2.457   -16.546 -6.511  1.00 21.07  ? 42  ILE A CB  1 
ATOM   329  C  CG1 . ILE A 1 43 ? 1.557   -15.326 -6.769  1.00 25.30  ? 42  ILE A CG1 1 
ATOM   330  C  CG2 . ILE A 1 43 ? 2.664   -16.824 -4.998  1.00 22.24  ? 42  ILE A CG2 1 
ATOM   331  C  CD1 . ILE A 1 43 ? 2.182   -13.976 -6.421  1.00 22.90  ? 42  ILE A CD1 1 
ATOM   332  N  N   . PHE A 1 44 ? 5.833   -17.380 -6.339  1.00 20.80  ? 43  PHE A N   1 
ATOM   333  C  CA  . PHE A 1 44 ? 6.726   -18.468 -5.995  1.00 21.69  ? 43  PHE A CA  1 
ATOM   334  C  C   . PHE A 1 44 ? 6.423   -18.905 -4.565  1.00 22.20  ? 43  PHE A C   1 
ATOM   335  O  O   . PHE A 1 44 ? 6.471   -18.096 -3.630  1.00 22.22  ? 43  PHE A O   1 
ATOM   336  C  CB  . PHE A 1 44 ? 8.179   -18.033 -6.152  1.00 26.02  ? 43  PHE A CB  1 
ATOM   337  C  CG  . PHE A 1 44 ? 9.180   -19.078 -5.760  1.00 23.39  ? 43  PHE A CG  1 
ATOM   338  C  CD1 . PHE A 1 44 ? 9.540   -20.069 -6.650  1.00 28.43  ? 43  PHE A CD1 1 
ATOM   339  C  CD2 . PHE A 1 44 ? 9.766   -19.040 -4.508  1.00 25.95  ? 43  PHE A CD2 1 
ATOM   340  C  CE1 . PHE A 1 44 ? 10.471  -21.024 -6.291  1.00 30.65  ? 43  PHE A CE1 1 
ATOM   341  C  CE2 . PHE A 1 44 ? 10.691  -19.987 -4.150  1.00 27.60  ? 43  PHE A CE2 1 
ATOM   342  C  CZ  . PHE A 1 44 ? 11.049  -20.974 -5.049  1.00 28.11  ? 43  PHE A CZ  1 
ATOM   343  N  N   . PHE A 1 45 ? 6.085   -20.178 -4.403  1.00 22.35  ? 44  PHE A N   1 
ATOM   344  C  CA  . PHE A 1 45 ? 5.694   -20.700 -3.100  1.00 23.79  ? 44  PHE A CA  1 
ATOM   345  C  C   . PHE A 1 45 ? 6.925   -21.250 -2.396  1.00 24.81  ? 44  PHE A C   1 
ATOM   346  O  O   . PHE A 1 45 ? 7.612   -22.142 -2.921  1.00 24.69  ? 44  PHE A O   1 
ATOM   347  C  CB  . PHE A 1 45 ? 4.614   -21.768 -3.262  1.00 25.93  ? 44  PHE A CB  1 
ATOM   348  C  CG  . PHE A 1 45 ? 3.265   -21.203 -3.588  1.00 24.58  ? 44  PHE A CG  1 
ATOM   349  C  CD1 . PHE A 1 45 ? 2.889   -20.958 -4.900  1.00 29.12  ? 44  PHE A CD1 1 
ATOM   350  C  CD2 . PHE A 1 45 ? 2.385   -20.879 -2.579  1.00 27.07  ? 44  PHE A CD2 1 
ATOM   351  C  CE1 . PHE A 1 45 ? 1.652   -20.432 -5.199  1.00 27.80  ? 44  PHE A CE1 1 
ATOM   352  C  CE2 . PHE A 1 45 ? 1.134   -20.344 -2.863  1.00 28.89  ? 44  PHE A CE2 1 
ATOM   353  C  CZ  . PHE A 1 45 ? 0.766   -20.116 -4.159  1.00 26.18  ? 44  PHE A CZ  1 
ATOM   354  N  N   . PHE A 1 46 ? 7.216   -20.721 -1.212  1.00 22.70  ? 45  PHE A N   1 
ATOM   355  C  CA  . PHE A 1 46 ? 8.349   -21.234 -0.470  1.00 19.81  ? 45  PHE A CA  1 
ATOM   356  C  C   . PHE A 1 46 ? 8.078   -22.667 -0.027  1.00 22.64  ? 45  PHE A C   1 
ATOM   357  O  O   . PHE A 1 46 ? 6.929   -23.093 0.095   1.00 26.07  ? 45  PHE A O   1 
ATOM   358  C  CB  . PHE A 1 46 ? 8.641   -20.336 0.736   1.00 21.85  ? 45  PHE A CB  1 
ATOM   359  C  CG  . PHE A 1 46 ? 9.130   -18.958 0.349   1.00 21.44  ? 45  PHE A CG  1 
ATOM   360  C  CD1 . PHE A 1 46 ? 10.362  -18.812 -0.292  1.00 22.71  ? 45  PHE A CD1 1 
ATOM   361  C  CD2 . PHE A 1 46 ? 8.364   -17.828 0.599   1.00 22.10  ? 45  PHE A CD2 1 
ATOM   362  C  CE1 . PHE A 1 46 ? 10.823  -17.563 -0.650  1.00 24.88  ? 45  PHE A CE1 1 
ATOM   363  C  CE2 . PHE A 1 46 ? 8.820   -16.570 0.240   1.00 20.85  ? 45  PHE A CE2 1 
ATOM   364  C  CZ  . PHE A 1 46 ? 10.056  -16.443 -0.389  1.00 20.96  ? 45  PHE A CZ  1 
ATOM   365  N  N   . GLY A 1 47 ? 9.157   -23.421 0.145   1.00 25.72  ? 46  GLY A N   1 
ATOM   366  C  CA  . GLY A 1 47 ? 9.069   -24.816 0.563   1.00 25.50  ? 46  GLY A CA  1 
ATOM   367  C  C   . GLY A 1 47 ? 8.823   -25.756 -0.599  1.00 31.02  ? 46  GLY A C   1 
ATOM   368  O  O   . GLY A 1 47 ? 9.651   -26.619 -0.901  1.00 37.57  ? 46  GLY A O   1 
ATOM   369  N  N   . THR A 1 48 ? 7.678   -25.611 -1.263  1.00 27.23  ? 47  THR A N   1 
ATOM   370  C  CA  . THR A 1 48 ? 7.428   -26.439 -2.440  1.00 33.87  ? 47  THR A CA  1 
ATOM   371  C  C   . THR A 1 48 ? 8.160   -25.931 -3.685  1.00 34.32  ? 47  THR A C   1 
ATOM   372  O  O   . THR A 1 48 ? 8.437   -26.717 -4.603  1.00 31.09  ? 47  THR A O   1 
ATOM   373  C  CB  . THR A 1 48 ? 5.933   -26.507 -2.725  1.00 29.82  ? 47  THR A CB  1 
ATOM   374  O  OG1 . THR A 1 48 ? 5.498   -25.253 -3.272  1.00 33.80  ? 47  THR A OG1 1 
ATOM   375  C  CG2 . THR A 1 48 ? 5.152   -26.818 -1.479  1.00 36.69  ? 47  THR A CG2 1 
ATOM   376  N  N   . HIS A 1 49 ? 8.462   -24.629 -3.746  1.00 28.11  ? 48  HIS A N   1 
ATOM   377  C  CA  . HIS A 1 49 ? 9.147   -24.000 -4.870  1.00 29.85  ? 48  HIS A CA  1 
ATOM   378  C  C   . HIS A 1 49 ? 8.353   -24.098 -6.172  1.00 24.78  ? 48  HIS A C   1 
ATOM   379  O  O   . HIS A 1 49 ? 8.927   -23.999 -7.256  1.00 36.13  ? 48  HIS A O   1 
ATOM   380  C  CB  . HIS A 1 49 ? 10.563  -24.563 -5.033  1.00 27.19  ? 48  HIS A CB  1 
ATOM   381  C  CG  . HIS A 1 49 ? 11.278  -24.698 -3.729  1.00 35.49  ? 48  HIS A CG  1 
ATOM   382  N  ND1 . HIS A 1 49 ? 11.658  -25.917 -3.217  1.00 34.38  ? 48  HIS A ND1 1 
ATOM   383  C  CD2 . HIS A 1 49 ? 11.630  -23.771 -2.805  1.00 31.03  ? 48  HIS A CD2 1 
ATOM   384  C  CE1 . HIS A 1 49 ? 12.220  -25.734 -2.034  1.00 46.32  ? 48  HIS A CE1 1 
ATOM   385  N  NE2 . HIS A 1 49 ? 12.229  -24.439 -1.767  1.00 36.50  ? 48  HIS A NE2 1 
ATOM   386  N  N   . GLU A 1 50 ? 7.036   -24.255 -6.079  1.00 27.72  ? 49  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 50 ? 6.141   -24.187 -7.230  1.00 32.32  ? 49  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 50 ? 5.776   -22.738 -7.545  1.00 31.61  ? 49  GLU A C   1 
ATOM   389  O  O   . GLU A 1 50 ? 5.757   -21.879 -6.662  1.00 28.25  ? 49  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 50 ? 4.852   -24.973 -6.952  1.00 37.75  ? 49  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 50 ? 4.904   -26.476 -7.245  1.00 45.07  ? 49  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 50 ? 4.948   -26.784 -8.749  1.00 67.44  ? 49  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 50 ? 3.890   -26.688 -9.419  1.00 56.12  ? 49  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 50 ? 6.049   -27.109 -9.260  1.00 65.46  ? 49  GLU A OE2 1 
ATOM   395  N  N   . THR A 1 51 ? 5.501   -22.462 -8.820  1.00 28.88  ? 50  THR A N   1 
ATOM   396  C  CA  . THR A 1 51 ? 4.969   -21.166 -9.235  1.00 24.73  ? 50  THR A CA  1 
ATOM   397  C  C   . THR A 1 51 ? 3.526   -21.324 -9.698  1.00 30.01  ? 50  THR A C   1 
ATOM   398  O  O   . THR A 1 51 ? 3.194   -22.283 -10.406 1.00 33.69  ? 50  THR A O   1 
ATOM   399  C  CB  . THR A 1 51 ? 5.807   -20.525 -10.355 1.00 31.74  ? 50  THR A CB  1 
ATOM   400  O  OG1 . THR A 1 51 ? 7.112   -20.187 -9.866  1.00 30.90  ? 50  THR A OG1 1 
ATOM   401  C  CG2 . THR A 1 51 ? 5.137   -19.250 -10.896 1.00 30.27  ? 50  THR A CG2 1 
ATOM   402  N  N   . ALA A 1 52 ? 2.665   -20.389 -9.283  1.00 27.40  ? 51  ALA A N   1 
ATOM   403  C  CA  . ALA A 1 52 ? 1.321   -20.238 -9.830  1.00 27.40  ? 51  ALA A CA  1 
ATOM   404  C  C   . ALA A 1 52 ? 1.086   -18.777 -10.172 1.00 28.15  ? 51  ALA A C   1 
ATOM   405  O  O   . ALA A 1 52 ? 1.782   -17.891 -9.673  1.00 27.56  ? 51  ALA A O   1 
ATOM   406  C  CB  . ALA A 1 52 ? 0.238   -20.720 -8.853  1.00 26.83  ? 51  ALA A CB  1 
ATOM   407  N  N   . PHE A 1 53 ? 0.104   -18.525 -11.040 1.00 27.72  ? 52  PHE A N   1 
ATOM   408  C  CA  . PHE A 1 53 ? -0.297  -17.167 -11.409 1.00 28.64  ? 52  PHE A CA  1 
ATOM   409  C  C   . PHE A 1 53 ? -1.543  -16.772 -10.625 1.00 33.90  ? 52  PHE A C   1 
ATOM   410  O  O   . PHE A 1 53 ? -2.601  -17.390 -10.791 1.00 36.00  ? 52  PHE A O   1 
ATOM   411  C  CB  . PHE A 1 53 ? -0.555  -17.061 -12.917 1.00 32.56  ? 52  PHE A CB  1 
ATOM   412  C  CG  . PHE A 1 53 ? 0.663   -17.336 -13.762 1.00 35.68  ? 52  PHE A CG  1 
ATOM   413  C  CD1 . PHE A 1 53 ? 1.903   -16.823 -13.407 1.00 35.99  ? 52  PHE A CD1 1 
ATOM   414  C  CD2 . PHE A 1 53 ? 0.570   -18.112 -14.913 1.00 38.95  ? 52  PHE A CD2 1 
ATOM   415  C  CE1 . PHE A 1 53 ? 3.026   -17.073 -14.182 1.00 43.98  ? 52  PHE A CE1 1 
ATOM   416  C  CE2 . PHE A 1 53 ? 1.691   -18.366 -15.692 1.00 38.09  ? 52  PHE A CE2 1 
ATOM   417  C  CZ  . PHE A 1 53 ? 2.914   -17.858 -15.331 1.00 38.68  ? 52  PHE A CZ  1 
ATOM   418  N  N   . LEU A 1 54 ? -1.420  -15.742 -9.782  1.00 28.25  ? 53  LEU A N   1 
ATOM   419  C  CA  . LEU A 1 54 ? -2.484  -15.322 -8.883  1.00 28.10  ? 53  LEU A CA  1 
ATOM   420  C  C   . LEU A 1 54 ? -2.715  -13.828 -8.980  1.00 29.30  ? 53  LEU A C   1 
ATOM   421  O  O   . LEU A 1 54 ? -1.792  -13.055 -9.248  1.00 27.54  ? 53  LEU A O   1 
ATOM   422  C  CB  . LEU A 1 54 ? -2.154  -15.633 -7.426  1.00 23.66  ? 53  LEU A CB  1 
ATOM   423  C  CG  . LEU A 1 54 ? -1.910  -17.089 -7.068  1.00 26.77  ? 53  LEU A CG  1 
ATOM   424  C  CD1 . LEU A 1 54 ? -1.761  -17.161 -5.557  1.00 25.29  ? 53  LEU A CD1 1 
ATOM   425  C  CD2 . LEU A 1 54 ? -3.054  -17.947 -7.542  1.00 36.40  ? 53  LEU A CD2 1 
ATOM   426  N  N   . GLY A 1 55 ? -3.949  -13.422 -8.705  1.00 29.65  ? 54  GLY A N   1 
ATOM   427  C  CA  . GLY A 1 55 ? -4.264  -12.024 -8.587  1.00 28.94  ? 54  GLY A CA  1 
ATOM   428  C  C   . GLY A 1 55 ? -4.212  -11.586 -7.134  1.00 28.88  ? 54  GLY A C   1 
ATOM   429  O  O   . GLY A 1 55 ? -4.147  -12.425 -6.220  1.00 31.02  ? 54  GLY A O   1 
ATOM   430  N  N   . PRO A 1 56 ? -4.240  -10.268 -6.904  1.00 30.27  ? 55  PRO A N   1 
ATOM   431  C  CA  . PRO A 1 56 ? -4.148  -9.739  -5.528  1.00 27.74  ? 55  PRO A CA  1 
ATOM   432  C  C   . PRO A 1 56 ? -5.205  -10.251 -4.569  1.00 31.08  ? 55  PRO A C   1 
ATOM   433  O  O   . PRO A 1 56 ? -4.971  -10.211 -3.351  1.00 26.68  ? 55  PRO A O   1 
ATOM   434  C  CB  . PRO A 1 56 ? -4.289  -8.224  -5.729  1.00 29.46  ? 55  PRO A CB  1 
ATOM   435  C  CG  . PRO A 1 56 ? -3.759  -7.988  -7.079  1.00 33.33  ? 55  PRO A CG  1 
ATOM   436  C  CD  . PRO A 1 56 ? -4.156  -9.180  -7.898  1.00 27.76  ? 55  PRO A CD  1 
ATOM   437  N  N   . LYS A 1 57 ? -6.354  -10.729 -5.058  1.00 33.15  ? 56  LYS A N   1 
ATOM   438  C  CA  . LYS A 1 57 ? -7.372  -11.242 -4.144  1.00 30.05  ? 56  LYS A CA  1 
ATOM   439  C  C   . LYS A 1 57 ? -6.839  -12.388 -3.295  1.00 33.34  ? 56  LYS A C   1 
ATOM   440  O  O   . LYS A 1 57 ? -7.347  -12.622 -2.190  1.00 30.00  ? 56  LYS A O   1 
ATOM   441  C  CB  . LYS A 1 57 ? -8.616  -11.708 -4.916  1.00 38.05  ? 56  LYS A CB  1 
ATOM   442  C  CG  . LYS A 1 57 ? -8.422  -13.029 -5.688  1.00 33.66  ? 56  LYS A CG  1 
ATOM   443  C  CD  . LYS A 1 57 ? -9.684  -13.489 -6.444  1.00 43.29  ? 56  LYS A CD  1 
ATOM   444  C  CE  . LYS A 1 57 ? -9.487  -14.843 -7.156  1.00 52.38  ? 56  LYS A CE  1 
ATOM   445  N  NZ  . LYS A 1 57 ? -9.494  -16.056 -6.262  1.00 44.69  ? 56  LYS A NZ  1 
ATOM   446  N  N   . ASP A 1 58 ? -5.809  -13.088 -3.765  1.00 26.82  ? 57  ASP A N   1 
ATOM   447  C  CA  . ASP A 1 58 ? -5.272  -14.233 -3.051  1.00 25.97  ? 57  ASP A CA  1 
ATOM   448  C  C   . ASP A 1 58 ? -3.960  -13.935 -2.336  1.00 22.05  ? 57  ASP A C   1 
ATOM   449  O  O   . ASP A 1 58 ? -3.334  -14.863 -1.818  1.00 27.98  ? 57  ASP A O   1 
ATOM   450  C  CB  . ASP A 1 58 ? -5.114  -15.408 -4.013  1.00 31.63  ? 57  ASP A CB  1 
ATOM   451  C  CG  . ASP A 1 58 ? -6.440  -16.025 -4.350  1.00 36.87  ? 57  ASP A CG  1 
ATOM   452  O  OD1 . ASP A 1 58 ? -7.278  -16.123 -3.423  1.00 37.40  ? 57  ASP A OD1 1 
ATOM   453  O  OD2 . ASP A 1 58 ? -6.662  -16.374 -5.522  1.00 36.37  ? 57  ASP A OD2 1 
ATOM   454  N  N   . LEU A 1 59 ? -3.552  -12.671 -2.269  1.00 23.25  ? 58  LEU A N   1 
ATOM   455  C  CA  . LEU A 1 59 ? -2.227  -12.287 -1.788  1.00 22.76  ? 58  LEU A CA  1 
ATOM   456  C  C   . LEU A 1 59 ? -2.373  -11.469 -0.516  1.00 22.36  ? 58  LEU A C   1 
ATOM   457  O  O   . LEU A 1 59 ? -2.973  -10.392 -0.531  1.00 26.35  ? 58  LEU A O   1 
ATOM   458  C  CB  . LEU A 1 59 ? -1.468  -11.482 -2.852  1.00 24.21  ? 58  LEU A CB  1 
ATOM   459  C  CG  . LEU A 1 59 ? -1.320  -12.213 -4.189  1.00 26.03  ? 58  LEU A CG  1 
ATOM   460  C  CD1 . LEU A 1 59 ? -0.592  -11.304 -5.188  1.00 24.50  ? 58  LEU A CD1 1 
ATOM   461  C  CD2 . LEU A 1 59 ? -0.587  -13.519 -4.030  1.00 23.99  ? 58  LEU A CD2 1 
ATOM   462  N  N   . PHE A 1 60 ? -1.772  -11.951 0.560   1.00 20.61  ? 59  PHE A N   1 
ATOM   463  C  CA  . PHE A 1 60 ? -1.851  -11.296 1.861   1.00 23.74  ? 59  PHE A CA  1 
ATOM   464  C  C   . PHE A 1 60 ? -0.460  -10.843 2.280   1.00 22.26  ? 59  PHE A C   1 
ATOM   465  O  O   . PHE A 1 60 ? 0.484   -11.641 2.233   1.00 25.78  ? 59  PHE A O   1 
ATOM   466  C  CB  . PHE A 1 60 ? -2.424  -12.273 2.896   1.00 25.77  ? 59  PHE A CB  1 
ATOM   467  C  CG  . PHE A 1 60 ? -3.835  -12.698 2.618   1.00 24.22  ? 59  PHE A CG  1 
ATOM   468  C  CD1 . PHE A 1 60 ? -4.118  -13.596 1.598   1.00 24.13  ? 59  PHE A CD1 1 
ATOM   469  C  CD2 . PHE A 1 60 ? -4.882  -12.213 3.399   1.00 26.43  ? 59  PHE A CD2 1 
ATOM   470  C  CE1 . PHE A 1 60 ? -5.427  -14.002 1.356   1.00 32.10  ? 59  PHE A CE1 1 
ATOM   471  C  CE2 . PHE A 1 60 ? -6.172  -12.601 3.158   1.00 28.52  ? 59  PHE A CE2 1 
ATOM   472  C  CZ  . PHE A 1 60 ? -6.448  -13.511 2.142   1.00 25.93  ? 59  PHE A CZ  1 
ATOM   473  N  N   . PRO A 1 61 ? -0.280  -9.585  2.683   1.00 27.22  ? 60  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 61 ? 1.063   -9.107  3.040   1.00 24.83  ? 60  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 61 ? 1.679   -9.906  4.183   1.00 31.26  ? 60  PRO A C   1 
ATOM   476  O  O   . PRO A 1 61 ? 1.035   -10.165 5.204   1.00 28.64  ? 60  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 61 ? 0.813   -7.649  3.447   1.00 33.30  ? 60  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 61 ? -0.371  -7.254  2.605   1.00 41.15  ? 60  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 61 ? -1.251  -8.483  2.581   1.00 34.07  ? 60  PRO A CD  1 
ATOM   480  N  N   . TYR A 1 62 ? 2.950   -10.287 3.997   1.00 28.00  ? 61  TYR A N   1 
ATOM   481  C  CA  . TYR A 1 62 ? 3.625   -11.166 4.943   1.00 29.12  ? 61  TYR A CA  1 
ATOM   482  C  C   . TYR A 1 62 ? 3.719   -10.530 6.321   1.00 28.00  ? 61  TYR A C   1 
ATOM   483  O  O   . TYR A 1 62 ? 3.369   -11.156 7.321   1.00 29.77  ? 61  TYR A O   1 
ATOM   484  C  CB  . TYR A 1 62 ? 5.027   -11.524 4.445   1.00 30.79  ? 61  TYR A CB  1 
ATOM   485  C  CG  . TYR A 1 62 ? 5.822   -12.338 5.469   1.00 31.07  ? 61  TYR A CG  1 
ATOM   486  C  CD1 . TYR A 1 62 ? 5.464   -13.653 5.779   1.00 28.78  ? 61  TYR A CD1 1 
ATOM   487  C  CD2 . TYR A 1 62 ? 6.923   -11.789 6.113   1.00 37.98  ? 61  TYR A CD2 1 
ATOM   488  C  CE1 . TYR A 1 62 ? 6.175   -14.393 6.723   1.00 32.05  ? 61  TYR A CE1 1 
ATOM   489  C  CE2 . TYR A 1 62 ? 7.655   -12.539 7.047   1.00 33.43  ? 61  TYR A CE2 1 
ATOM   490  C  CZ  . TYR A 1 62 ? 7.272   -13.827 7.345   1.00 34.35  ? 61  TYR A CZ  1 
ATOM   491  O  OH  . TYR A 1 62 ? 7.988   -14.553 8.274   1.00 39.16  ? 61  TYR A OH  1 
ATOM   492  N  N   . ASP A 1 63 ? 4.212   -9.293  6.387   1.00 34.47  ? 62  ASP A N   1 
ATOM   493  C  CA  . ASP A 1 63 ? 4.444   -8.667  7.690   1.00 35.06  ? 62  ASP A CA  1 
ATOM   494  C  C   . ASP A 1 63 ? 3.140   -8.482  8.458   1.00 36.92  ? 62  ASP A C   1 
ATOM   495  O  O   . ASP A 1 63 ? 3.062   -8.803  9.650   1.00 42.35  ? 62  ASP A O   1 
ATOM   496  C  CB  . ASP A 1 63 ? 5.167   -7.337  7.520   1.00 35.73  ? 62  ASP A CB  1 
ATOM   497  C  CG  . ASP A 1 63 ? 4.421   -6.360  6.612   1.00 49.12  ? 62  ASP A CG  1 
ATOM   498  O  OD1 . ASP A 1 63 ? 3.288   -6.658  6.158   1.00 47.45  ? 62  ASP A OD1 1 
ATOM   499  O  OD2 . ASP A 1 63 ? 4.988   -5.280  6.343   1.00 57.27  ? 62  ASP A OD2 1 
ATOM   500  N  N   . LYS A 1 64 ? 2.098   -7.995  7.786   1.00 34.87  ? 63  LYS A N   1 
ATOM   501  C  CA  . LYS A 1 64 ? 0.824   -7.757  8.457   1.00 40.27  ? 63  LYS A CA  1 
ATOM   502  C  C   . LYS A 1 64 ? 0.182   -9.053  8.927   1.00 40.15  ? 63  LYS A C   1 
ATOM   503  O  O   . LYS A 1 64 ? -0.539  -9.060  9.933   1.00 35.05  ? 63  LYS A O   1 
ATOM   504  C  CB  . LYS A 1 64 ? -0.113  -6.994  7.511   1.00 41.50  ? 63  LYS A CB  1 
ATOM   505  C  CG  . LYS A 1 64 ? -1.615  -7.028  7.830   1.00 44.49  ? 63  LYS A CG  1 
ATOM   506  C  CD  . LYS A 1 64 ? -2.408  -6.244  6.758   1.00 43.78  ? 63  LYS A CD  1 
ATOM   507  C  CE  . LYS A 1 64 ? -3.897  -6.575  6.709   1.00 43.90  ? 63  LYS A CE  1 
ATOM   508  N  NZ  . LYS A 1 64 ? -4.704  -6.154  7.899   1.00 43.89  ? 63  LYS A NZ  1 
ATOM   509  N  N   . CYS A 1 65 ? 0.430   -10.164 8.232   1.00 27.93  ? 64  CYS A N   1 
ATOM   510  C  CA  . CYS A 1 65 ? -0.379  -11.353 8.445   1.00 25.24  ? 64  CYS A CA  1 
ATOM   511  C  C   . CYS A 1 65 ? 0.404   -12.547 9.002   1.00 32.47  ? 64  CYS A C   1 
ATOM   512  O  O   . CYS A 1 65 ? -0.192  -13.609 9.224   1.00 35.82  ? 64  CYS A O   1 
ATOM   513  C  CB  . CYS A 1 65 ? -1.099  -11.728 7.135   1.00 29.35  ? 64  CYS A CB  1 
ATOM   514  S  SG  . CYS A 1 65 ? -2.417  -10.559 6.653   1.00 38.53  ? 64  CYS A SG  1 
ATOM   515  N  N   . LYS A 1 66 ? 1.710   -12.400 9.268   1.00 32.14  ? 65  LYS A N   1 
ATOM   516  C  CA  . LYS A 1 66 ? 2.508   -13.535 9.735   1.00 35.49  ? 65  LYS A CA  1 
ATOM   517  C  C   . LYS A 1 66 ? 2.070   -14.040 11.109  1.00 36.43  ? 65  LYS A C   1 
ATOM   518  O  O   . LYS A 1 66 ? 2.212   -15.234 11.401  1.00 38.01  ? 65  LYS A O   1 
ATOM   519  C  CB  . LYS A 1 66 ? 3.999   -13.175 9.749   1.00 30.68  ? 65  LYS A CB  1 
ATOM   520  C  CG  . LYS A 1 66 ? 4.401   -12.027 10.653  1.00 40.57  ? 65  LYS A CG  1 
ATOM   521  C  CD  . LYS A 1 66 ? 5.886   -11.745 10.487  1.00 44.22  ? 65  LYS A CD  1 
ATOM   522  C  CE  . LYS A 1 66 ? 6.293   -10.412 11.114  1.00 46.18  ? 65  LYS A CE  1 
ATOM   523  N  NZ  . LYS A 1 66 ? 7.612   -9.973  10.562  1.00 48.01  ? 65  LYS A NZ  1 
ATOM   524  N  N   . ASP A 1 67 ? 1.524   -13.172 11.967  1.00 39.43  ? 66  ASP A N   1 
ATOM   525  C  CA  . ASP A 1 67 ? 1.025   -13.679 13.244  1.00 45.53  ? 66  ASP A CA  1 
ATOM   526  C  C   . ASP A 1 67 ? -0.142  -14.641 13.057  1.00 41.42  ? 66  ASP A C   1 
ATOM   527  O  O   . ASP A 1 67 ? -0.262  -15.618 13.802  1.00 46.34  ? 66  ASP A O   1 
ATOM   528  C  CB  . ASP A 1 67 ? 0.632   -12.516 14.156  1.00 48.01  ? 66  ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 67 ? 1.775   -12.077 15.049  1.00 54.04  ? 66  ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 67 ? 2.930   -12.069 14.562  1.00 56.18  ? 66  ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 67 ? 1.529   -11.746 16.229  1.00 67.70  ? 66  ASP A OD2 1 
ATOM   532  N  N   . LYS A 1 68 ? -0.982  -14.413 12.050  1.00 37.11  ? 67  LYS A N   1 
ATOM   533  C  CA  . LYS A 1 68 ? -2.114  -15.302 11.815  1.00 37.12  ? 67  LYS A CA  1 
ATOM   534  C  C   . LYS A 1 68 ? -1.708  -16.551 11.036  1.00 46.43  ? 67  LYS A C   1 
ATOM   535  O  O   . LYS A 1 68 ? -2.126  -17.667 11.370  1.00 35.72  ? 67  LYS A O   1 
ATOM   536  C  CB  . LYS A 1 68 ? -3.213  -14.542 11.068  1.00 43.71  ? 67  LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 68 ? -4.572  -15.217 11.055  1.00 44.28  ? 67  LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 68 ? -5.595  -14.336 10.338  1.00 51.32  ? 67  LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 68 ? -7.008  -14.895 10.513  1.00 63.09  ? 67  LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 68 ? -8.026  -14.143 9.722   1.00 59.06  ? 67  LYS A NZ  1 
ATOM   541  N  N   . TYR A 1 69 ? -0.895  -16.385 9.994   1.00 31.17  ? 68  TYR A N   1 
ATOM   542  C  CA  . TYR A 1 69 ? -0.656  -17.453 9.036   1.00 32.83  ? 68  TYR A CA  1 
ATOM   543  C  C   . TYR A 1 69 ? 0.710   -18.112 9.179   1.00 34.02  ? 68  TYR A C   1 
ATOM   544  O  O   . TYR A 1 69 ? 0.928   -19.176 8.589   1.00 36.37  ? 68  TYR A O   1 
ATOM   545  C  CB  . TYR A 1 69 ? -0.797  -16.900 7.603   1.00 29.95  ? 68  TYR A CB  1 
ATOM   546  C  CG  . TYR A 1 69 ? -2.179  -16.398 7.266   1.00 32.46  ? 68  TYR A CG  1 
ATOM   547  C  CD1 . TYR A 1 69 ? -3.313  -17.109 7.635   1.00 37.35  ? 68  TYR A CD1 1 
ATOM   548  C  CD2 . TYR A 1 69 ? -2.352  -15.207 6.565   1.00 32.62  ? 68  TYR A CD2 1 
ATOM   549  C  CE1 . TYR A 1 69 ? -4.584  -16.651 7.314   1.00 35.97  ? 68  TYR A CE1 1 
ATOM   550  C  CE2 . TYR A 1 69 ? -3.615  -14.728 6.259   1.00 34.11  ? 68  TYR A CE2 1 
ATOM   551  C  CZ  . TYR A 1 69 ? -4.724  -15.459 6.624   1.00 37.28  ? 68  TYR A CZ  1 
ATOM   552  O  OH  . TYR A 1 69 ? -5.973  -14.991 6.318   1.00 36.85  ? 68  TYR A OH  1 
ATOM   553  N  N   . GLY A 1 70 ? 1.627   -17.509 9.935   1.00 36.49  ? 69  GLY A N   1 
ATOM   554  C  CA  . GLY A 1 70 ? 3.003   -17.960 9.987   1.00 31.23  ? 69  GLY A CA  1 
ATOM   555  C  C   . GLY A 1 70 ? 3.272   -18.925 11.123  1.00 36.30  ? 69  GLY A C   1 
ATOM   556  O  O   . GLY A 1 70 ? 4.193   -18.732 11.924  1.00 42.45  ? 69  GLY A O   1 
ATOM   557  N  N   . LYS A 1 71 ? 2.447   -19.952 11.220  1.00 37.64  ? 70  LYS A N   1 
ATOM   558  C  CA  . LYS A 1 71 ? 2.612   -20.974 12.230  1.00 39.68  ? 70  LYS A CA  1 
ATOM   559  C  C   . LYS A 1 71 ? 2.839   -22.311 11.546  1.00 38.21  ? 70  LYS A C   1 
ATOM   560  O  O   . LYS A 1 71 ? 2.394   -22.512 10.410  1.00 40.31  ? 70  LYS A O   1 
ATOM   561  C  CB  . LYS A 1 71 ? 1.383   -21.056 13.143  1.00 38.66  ? 70  LYS A CB  1 
ATOM   562  C  CG  . LYS A 1 71 ? 0.819   -19.697 13.525  1.00 48.35  ? 70  LYS A CG  1 
ATOM   563  C  CD  . LYS A 1 71 ? 0.180   -19.718 14.908  1.00 59.61  ? 70  LYS A CD  1 
ATOM   564  C  CE  . LYS A 1 71 ? 1.052   -18.980 15.921  1.00 58.35  ? 70  LYS A CE  1 
ATOM   565  N  NZ  . LYS A 1 71 ? 1.212   -17.535 15.587  1.00 56.71  ? 70  LYS A NZ  1 
ATOM   566  N  N   . PRO A 1 72 ? 3.543   -23.239 12.196  1.00 36.54  ? 71  PRO A N   1 
ATOM   567  C  CA  . PRO A 1 72 ? 3.762   -24.557 11.590  1.00 34.95  ? 71  PRO A CA  1 
ATOM   568  C  C   . PRO A 1 72 ? 2.461   -25.214 11.137  1.00 35.34  ? 71  PRO A C   1 
ATOM   569  O  O   . PRO A 1 72 ? 1.400   -25.039 11.741  1.00 38.68  ? 71  PRO A O   1 
ATOM   570  C  CB  . PRO A 1 72 ? 4.433   -25.353 12.715  1.00 40.34  ? 71  PRO A CB  1 
ATOM   571  C  CG  . PRO A 1 72 ? 5.167   -24.319 13.493  1.00 41.14  ? 71  PRO A CG  1 
ATOM   572  C  CD  . PRO A 1 72 ? 4.305   -23.068 13.448  1.00 36.91  ? 71  PRO A CD  1 
ATOM   573  N  N   . ASN A 1 73 ? 2.561   -25.979 10.056  1.00 34.12  ? 72  ASN A N   1 
ATOM   574  C  CA  . ASN A 1 73 ? 1.423   -26.619 9.420   1.00 37.17  ? 72  ASN A CA  1 
ATOM   575  C  C   . ASN A 1 73 ? 1.873   -27.987 8.927   1.00 45.61  ? 72  ASN A C   1 
ATOM   576  O  O   . ASN A 1 73 ? 3.045   -28.183 8.591   1.00 44.05  ? 72  ASN A O   1 
ATOM   577  C  CB  . ASN A 1 73 ? 0.889   -25.738 8.266   1.00 39.08  ? 72  ASN A CB  1 
ATOM   578  C  CG  . ASN A 1 73 ? -0.300  -26.341 7.553   1.00 45.15  ? 72  ASN A CG  1 
ATOM   579  O  OD1 . ASN A 1 73 ? -0.165  -27.311 6.823   1.00 47.74  ? 72  ASN A OD1 1 
ATOM   580  N  ND2 . ASN A 1 73 ? -1.469  -25.731 7.723   1.00 50.32  ? 72  ASN A ND2 1 
ATOM   581  N  N   . LYS A 1 74 ? 0.937   -28.939 8.890   1.00 45.18  ? 73  LYS A N   1 
ATOM   582  C  CA  . LYS A 1 74 ? 1.305   -30.316 8.574   1.00 51.34  ? 73  LYS A CA  1 
ATOM   583  C  C   . LYS A 1 74 ? 1.597   -30.545 7.092   1.00 52.24  ? 73  LYS A C   1 
ATOM   584  O  O   . LYS A 1 74 ? 2.241   -31.546 6.753   1.00 47.87  ? 73  LYS A O   1 
ATOM   585  C  CB  . LYS A 1 74 ? 0.198   -31.274 9.034   1.00 46.74  ? 73  LYS A CB  1 
ATOM   586  N  N   . ARG A 1 75 ? 1.164   -29.647 6.208   1.00 41.18  ? 74  ARG A N   1 
ATOM   587  C  CA  . ARG A 1 75 ? 1.304   -29.891 4.778   1.00 37.17  ? 74  ARG A CA  1 
ATOM   588  C  C   . ARG A 1 75 ? 2.767   -29.932 4.361   1.00 44.21  ? 74  ARG A C   1 
ATOM   589  O  O   . ARG A 1 75 ? 3.618   -29.217 4.910   1.00 37.42  ? 74  ARG A O   1 
ATOM   590  C  CB  . ARG A 1 75 ? 0.571   -28.819 3.969   1.00 43.50  ? 74  ARG A CB  1 
ATOM   591  C  CG  . ARG A 1 75 ? -0.901  -28.751 4.260   1.00 48.23  ? 74  ARG A CG  1 
ATOM   592  C  CD  . ARG A 1 75 ? -1.622  -29.990 3.760   1.00 51.66  ? 74  ARG A CD  1 
ATOM   593  N  NE  . ARG A 1 75 ? -2.332  -29.724 2.516   1.00 55.03  ? 74  ARG A NE  1 
ATOM   594  C  CZ  . ARG A 1 75 ? -3.473  -29.052 2.440   1.00 46.20  ? 74  ARG A CZ  1 
ATOM   595  N  NH1 . ARG A 1 75 ? -4.044  -28.533 3.519   1.00 48.44  ? 74  ARG A NH1 1 
ATOM   596  N  NH2 . ARG A 1 75 ? -4.052  -28.895 1.254   1.00 55.58  ? 74  ARG A NH2 1 
ATOM   597  N  N   . LYS A 1 76 ? 3.048   -30.777 3.370   1.00 35.04  ? 75  LYS A N   1 
ATOM   598  C  CA  . LYS A 1 76 ? 4.417   -31.016 2.945   1.00 33.88  ? 75  LYS A CA  1 
ATOM   599  C  C   . LYS A 1 76 ? 5.019   -29.726 2.419   1.00 36.82  ? 75  LYS A C   1 
ATOM   600  O  O   . LYS A 1 76 ? 4.414   -29.036 1.596   1.00 32.94  ? 75  LYS A O   1 
ATOM   601  C  CB  . LYS A 1 76 ? 4.458   -32.110 1.871   1.00 43.66  ? 75  LYS A CB  1 
ATOM   602  C  CG  . LYS A 1 76 ? 5.827   -32.321 1.230   1.00 43.82  ? 75  LYS A CG  1 
ATOM   603  C  CD  . LYS A 1 76 ? 5.825   -33.500 0.226   1.00 50.73  ? 75  LYS A CD  1 
ATOM   604  C  CE  . LYS A 1 76 ? 5.922   -34.854 0.937   1.00 60.20  ? 75  LYS A CE  1 
ATOM   605  N  NZ  . LYS A 1 76 ? 6.059   -36.013 -0.005  1.00 61.89  ? 75  LYS A NZ  1 
ATOM   606  N  N   . GLY A 1 77 ? 6.205   -29.393 2.915   1.00 33.87  ? 76  GLY A N   1 
ATOM   607  C  CA  . GLY A 1 77 ? 6.906   -28.220 2.459   1.00 36.97  ? 76  GLY A CA  1 
ATOM   608  C  C   . GLY A 1 77 ? 6.525   -26.936 3.156   1.00 31.38  ? 76  GLY A C   1 
ATOM   609  O  O   . GLY A 1 77 ? 7.201   -25.925 2.943   1.00 31.73  ? 76  GLY A O   1 
ATOM   610  N  N   . PHE A 1 78 ? 5.483   -26.933 3.994   1.00 30.21  ? 77  PHE A N   1 
ATOM   611  C  CA  . PHE A 1 78 ? 5.063   -25.676 4.618   1.00 29.78  ? 77  PHE A CA  1 
ATOM   612  C  C   . PHE A 1 78 ? 6.121   -25.144 5.583   1.00 35.59  ? 77  PHE A C   1 
ATOM   613  O  O   . PHE A 1 78 ? 6.440   -23.947 5.579   1.00 26.15  ? 77  PHE A O   1 
ATOM   614  C  CB  . PHE A 1 78 ? 3.719   -25.854 5.340   1.00 31.59  ? 77  PHE A CB  1 
ATOM   615  C  CG  . PHE A 1 78 ? 3.047   -24.545 5.712   1.00 32.89  ? 77  PHE A CG  1 
ATOM   616  C  CD1 . PHE A 1 78 ? 3.374   -23.880 6.880   1.00 30.62  ? 77  PHE A CD1 1 
ATOM   617  C  CD2 . PHE A 1 78 ? 2.080   -23.982 4.871   1.00 27.24  ? 77  PHE A CD2 1 
ATOM   618  C  CE1 . PHE A 1 78 ? 2.763   -22.680 7.222   1.00 34.85  ? 77  PHE A CE1 1 
ATOM   619  C  CE2 . PHE A 1 78 ? 1.461   -22.787 5.205   1.00 29.90  ? 77  PHE A CE2 1 
ATOM   620  C  CZ  . PHE A 1 78 ? 1.803   -22.130 6.376   1.00 28.46  ? 77  PHE A CZ  1 
ATOM   621  N  N   . ASN A 1 79 ? 6.660   -26.008 6.443   1.00 30.14  ? 78  ASN A N   1 
ATOM   622  C  CA  . ASN A 1 79 ? 7.588   -25.519 7.454   1.00 26.26  ? 78  ASN A CA  1 
ATOM   623  C  C   . ASN A 1 79 ? 8.949   -25.183 6.857   1.00 27.98  ? 78  ASN A C   1 
ATOM   624  O  O   . ASN A 1 79 ? 9.629   -24.265 7.345   1.00 28.18  ? 78  ASN A O   1 
ATOM   625  C  CB  . ASN A 1 79 ? 7.717   -26.556 8.577   1.00 25.52  ? 78  ASN A CB  1 
ATOM   626  C  CG  . ASN A 1 79 ? 6.415   -26.779 9.305   1.00 33.70  ? 78  ASN A CG  1 
ATOM   627  O  OD1 . ASN A 1 79 ? 5.534   -25.930 9.299   1.00 29.04  ? 78  ASN A OD1 1 
ATOM   628  N  ND2 . ASN A 1 79 ? 6.277   -27.945 9.931   1.00 31.65  ? 78  ASN A ND2 1 
ATOM   629  N  N   . GLU A 1 80 ? 9.368   -25.901 5.814   1.00 27.36  ? 79  GLU A N   1 
ATOM   630  C  CA  . GLU A 1 80 ? 10.516  -25.436 5.049   1.00 26.15  ? 79  GLU A CA  1 
ATOM   631  C  C   . GLU A 1 80 ? 10.231  -24.057 4.472   1.00 25.03  ? 79  GLU A C   1 
ATOM   632  O  O   . GLU A 1 80 ? 11.066  -23.149 4.571   1.00 27.32  ? 79  GLU A O   1 
ATOM   633  C  CB  . GLU A 1 80 ? 10.874  -26.418 3.936   1.00 30.67  ? 79  GLU A CB  1 
ATOM   634  C  CG  . GLU A 1 80 ? 12.135  -26.006 3.187   1.00 27.53  ? 79  GLU A CG  1 
ATOM   635  C  CD  . GLU A 1 80 ? 12.547  -27.006 2.133   1.00 45.70  ? 79  GLU A CD  1 
ATOM   636  O  OE1 . GLU A 1 80 ? 11.770  -27.956 1.879   1.00 46.33  ? 79  GLU A OE1 1 
ATOM   637  O  OE2 . GLU A 1 80 ? 13.647  -26.842 1.561   1.00 46.42  ? 79  GLU A OE2 1 
ATOM   638  N  N   . GLY A 1 81 ? 9.030   -23.872 3.918   1.00 26.22  ? 80  GLY A N   1 
ATOM   639  C  CA  . GLY A 1 81 ? 8.668   -22.556 3.385   1.00 25.64  ? 80  GLY A CA  1 
ATOM   640  C  C   . GLY A 1 81 ? 8.634   -21.466 4.442   1.00 23.81  ? 80  GLY A C   1 
ATOM   641  O  O   . GLY A 1 81 ? 8.977   -20.309 4.169   1.00 25.43  ? 80  GLY A O   1 
ATOM   642  N  N   . LEU A 1 82 ? 8.211   -21.804 5.665   1.00 23.98  ? 81  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 82 ? 8.268   -20.814 6.730   1.00 23.72  ? 81  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 82 ? 9.707   -20.404 7.006   1.00 24.77  ? 81  LEU A C   1 
ATOM   645  O  O   . LEU A 1 82 ? 9.988   -19.224 7.231   1.00 25.83  ? 81  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 82 ? 7.607   -21.352 8.004   1.00 21.34  ? 81  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 82 ? 6.083   -21.448 8.024   1.00 25.11  ? 81  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 82 ? 5.679   -22.034 9.394   1.00 28.88  ? 81  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 82 ? 5.378   -20.089 7.821   1.00 26.98  ? 81  LEU A CD2 1 
ATOM   650  N  N   . TRP A 1 83 ? 10.639  -21.366 6.978   1.00 26.93  ? 82  TRP A N   1 
ATOM   651  C  CA  . TRP A 1 83 ? 12.042  -21.025 7.188   1.00 29.02  ? 82  TRP A CA  1 
ATOM   652  C  C   . TRP A 1 83 ? 12.560  -20.125 6.067   1.00 25.17  ? 82  TRP A C   1 
ATOM   653  O  O   . TRP A 1 83 ? 13.247  -19.133 6.327   1.00 28.06  ? 82  TRP A O   1 
ATOM   654  C  CB  . TRP A 1 83 ? 12.900  -22.292 7.294   1.00 31.22  ? 82  TRP A CB  1 
ATOM   655  C  CG  . TRP A 1 83 ? 14.362  -21.975 7.498   1.00 33.95  ? 82  TRP A CG  1 
ATOM   656  C  CD1 . TRP A 1 83 ? 15.019  -21.876 8.687   1.00 36.89  ? 82  TRP A CD1 1 
ATOM   657  C  CD2 . TRP A 1 83 ? 15.325  -21.653 6.481   1.00 31.47  ? 82  TRP A CD2 1 
ATOM   658  N  NE1 . TRP A 1 83 ? 16.332  -21.527 8.479   1.00 39.11  ? 82  TRP A NE1 1 
ATOM   659  C  CE2 . TRP A 1 83 ? 16.546  -21.393 7.132   1.00 40.21  ? 82  TRP A CE2 1 
ATOM   660  C  CE3 . TRP A 1 83 ? 15.276  -21.579 5.080   1.00 34.95  ? 82  TRP A CE3 1 
ATOM   661  C  CZ2 . TRP A 1 83 ? 17.705  -21.063 6.435   1.00 45.04  ? 82  TRP A CZ2 1 
ATOM   662  C  CZ3 . TRP A 1 83 ? 16.421  -21.253 4.392   1.00 35.57  ? 82  TRP A CZ3 1 
ATOM   663  C  CH2 . TRP A 1 83 ? 17.622  -20.996 5.068   1.00 40.74  ? 82  TRP A CH2 1 
ATOM   664  N  N   . GLU A 1 84 ? 12.242  -20.468 4.821   1.00 26.10  ? 83  GLU A N   1 
ATOM   665  C  CA  . GLU A 1 84 ? 12.707  -19.682 3.674   1.00 24.43  ? 83  GLU A CA  1 
ATOM   666  C  C   . GLU A 1 84 ? 12.206  -18.244 3.725   1.00 24.96  ? 83  GLU A C   1 
ATOM   667  O  O   . GLU A 1 84 ? 12.978  -17.303 3.493   1.00 27.47  ? 83  GLU A O   1 
ATOM   668  C  CB  . GLU A 1 84 ? 12.256  -20.352 2.377   1.00 27.48  ? 83  GLU A CB  1 
ATOM   669  C  CG  . GLU A 1 84 ? 12.944  -21.704 2.164   1.00 31.79  ? 83  GLU A CG  1 
ATOM   670  C  CD  . GLU A 1 84 ? 12.458  -22.447 0.943   1.00 30.75  ? 83  GLU A CD  1 
ATOM   671  O  OE1 . GLU A 1 84 ? 11.492  -22.010 0.300   1.00 29.99  ? 83  GLU A OE1 1 
ATOM   672  O  OE2 . GLU A 1 84 ? 13.056  -23.501 0.626   1.00 32.50  ? 83  GLU A OE2 1 
ATOM   673  N  N   . ILE A 1 85 ? 10.920  -18.039 4.006   1.00 21.15  ? 84  ILE A N   1 
ATOM   674  C  CA  . ILE A 1 85 ? 10.403  -16.672 3.918   1.00 22.94  ? 84  ILE A CA  1 
ATOM   675  C  C   . ILE A 1 85 ? 10.986  -15.796 5.025   1.00 27.62  ? 84  ILE A C   1 
ATOM   676  O  O   . ILE A 1 85 ? 11.130  -14.574 4.856   1.00 27.15  ? 84  ILE A O   1 
ATOM   677  C  CB  . ILE A 1 85 ? 8.862   -16.654 3.943   1.00 20.72  ? 84  ILE A CB  1 
ATOM   678  C  CG1 . ILE A 1 85 ? 8.371   -15.249 3.537   1.00 22.73  ? 84  ILE A CG1 1 
ATOM   679  C  CG2 . ILE A 1 85 ? 8.309   -17.048 5.347   1.00 20.81  ? 84  ILE A CG2 1 
ATOM   680  C  CD1 . ILE A 1 85 ? 6.964   -15.207 3.060   1.00 21.67  ? 84  ILE A CD1 1 
ATOM   681  N  N   . GLN A 1 86 ? 11.351  -16.393 6.161   1.00 25.65  ? 85  GLN A N   1 
ATOM   682  C  CA  . GLN A 1 86 ? 11.894  -15.615 7.267   1.00 29.43  ? 85  GLN A CA  1 
ATOM   683  C  C   . GLN A 1 86 ? 13.399  -15.394 7.153   1.00 25.94  ? 85  GLN A C   1 
ATOM   684  O  O   . GLN A 1 86 ? 13.902  -14.358 7.612   1.00 33.82  ? 85  GLN A O   1 
ATOM   685  C  CB  . GLN A 1 86 ? 11.568  -16.314 8.599   1.00 31.41  ? 85  GLN A CB  1 
ATOM   686  C  CG  . GLN A 1 86 ? 12.106  -15.589 9.821   1.00 34.40  ? 85  GLN A CG  1 
ATOM   687  C  CD  . GLN A 1 86 ? 11.423  -16.035 11.108  1.00 51.46  ? 85  GLN A CD  1 
ATOM   688  O  OE1 . GLN A 1 86 ? 10.965  -17.186 11.224  1.00 37.98  ? 85  GLN A OE1 1 
ATOM   689  N  NE2 . GLN A 1 86 ? 11.356  -15.134 12.082  1.00 44.93  ? 85  GLN A NE2 1 
ATOM   690  N  N   . ASN A 1 87 ? 14.119  -16.316 6.520   1.00 28.96  ? 86  ASN A N   1 
ATOM   691  C  CA  . ASN A 1 87 ? 15.571  -16.361 6.629   1.00 30.59  ? 86  ASN A CA  1 
ATOM   692  C  C   . ASN A 1 87 ? 16.320  -16.150 5.330   1.00 31.39  ? 86  ASN A C   1 
ATOM   693  O  O   . ASN A 1 87 ? 17.463  -15.680 5.384   1.00 32.58  ? 86  ASN A O   1 
ATOM   694  C  CB  . ASN A 1 87 ? 16.013  -17.695 7.228   1.00 32.19  ? 86  ASN A CB  1 
ATOM   695  C  CG  . ASN A 1 87 ? 15.503  -17.863 8.633   1.00 36.33  ? 86  ASN A CG  1 
ATOM   696  O  OD1 . ASN A 1 87 ? 15.758  -17.024 9.500   1.00 39.02  ? 86  ASN A OD1 1 
ATOM   697  N  ND2 . ASN A 1 87 ? 14.725  -18.904 8.853   1.00 38.57  ? 86  ASN A ND2 1 
ATOM   698  N  N   . ASN A 1 88 ? 15.744  -16.484 4.173   1.00 28.36  ? 87  ASN A N   1 
ATOM   699  C  CA  . ASN A 1 88 ? 16.339  -16.102 2.897   1.00 30.77  ? 87  ASN A CA  1 
ATOM   700  C  C   . ASN A 1 88 ? 15.260  -16.025 1.825   1.00 26.79  ? 87  ASN A C   1 
ATOM   701  O  O   . ASN A 1 88 ? 15.278  -16.768 0.837   1.00 28.29  ? 87  ASN A O   1 
ATOM   702  C  CB  . ASN A 1 88 ? 17.459  -17.063 2.501   1.00 32.04  ? 87  ASN A CB  1 
ATOM   703  C  CG  . ASN A 1 88 ? 18.551  -16.366 1.707   1.00 40.32  ? 87  ASN A CG  1 
ATOM   704  O  OD1 . ASN A 1 88 ? 18.292  -15.410 0.959   1.00 29.84  ? 87  ASN A OD1 1 
ATOM   705  N  ND2 . ASN A 1 88 ? 19.783  -16.824 1.880   1.00 35.56  ? 87  ASN A ND2 1 
ATOM   706  N  N   . PRO A 1 89 ? 14.311  -15.097 1.977   1.00 29.87  ? 88  PRO A N   1 
ATOM   707  C  CA  . PRO A 1 89 ? 13.161  -15.059 1.054   1.00 22.41  ? 88  PRO A CA  1 
ATOM   708  C  C   . PRO A 1 89 ? 13.514  -14.633 -0.366  1.00 28.24  ? 88  PRO A C   1 
ATOM   709  O  O   . PRO A 1 89 ? 12.724  -14.912 -1.274  1.00 25.73  ? 88  PRO A O   1 
ATOM   710  C  CB  . PRO A 1 89 ? 12.227  -14.036 1.715   1.00 26.89  ? 88  PRO A CB  1 
ATOM   711  C  CG  . PRO A 1 89 ? 13.162  -13.124 2.469   1.00 26.94  ? 88  PRO A CG  1 
ATOM   712  C  CD  . PRO A 1 89 ? 14.244  -14.040 3.000   1.00 27.07  ? 88  PRO A CD  1 
ATOM   713  N  N   . HIS A 1 90 ? 14.646  -13.954 -0.596  1.00 26.50  ? 89  HIS A N   1 
ATOM   714  C  CA  . HIS A 1 90 ? 14.995  -13.485 -1.934  1.00 23.24  ? 89  HIS A CA  1 
ATOM   715  C  C   . HIS A 1 90 ? 16.091  -14.307 -2.601  1.00 28.24  ? 89  HIS A C   1 
ATOM   716  O  O   . HIS A 1 90 ? 16.640  -13.874 -3.622  1.00 28.04  ? 89  HIS A O   1 
ATOM   717  C  CB  . HIS A 1 90 ? 15.410  -12.015 -1.876  1.00 23.42  ? 89  HIS A CB  1 
ATOM   718  C  CG  . HIS A 1 90 ? 14.393  -11.148 -1.221  1.00 27.67  ? 89  HIS A CG  1 
ATOM   719  N  ND1 . HIS A 1 90 ? 13.148  -10.928 -1.767  1.00 25.33  ? 89  HIS A ND1 1 
ATOM   720  C  CD2 . HIS A 1 90 ? 14.408  -10.489 -0.041  1.00 24.37  ? 89  HIS A CD2 1 
ATOM   721  C  CE1 . HIS A 1 90 ? 12.458  -10.131 -0.974  1.00 25.71  ? 89  HIS A CE1 1 
ATOM   722  N  NE2 . HIS A 1 90 ? 13.199  -9.853  0.083   1.00 26.73  ? 89  HIS A NE2 1 
ATOM   723  N  N   . ALA A 1 91 ? 16.396  -15.495 -2.090  1.00 28.32  ? 90  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 91 ? 17.465  -16.281 -2.678  1.00 29.74  ? 90  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 91 ? 17.000  -16.939 -3.980  1.00 30.41  ? 90  ALA A C   1 
ATOM   726  O  O   . ALA A 1 91 ? 15.814  -16.936 -4.321  1.00 32.58  ? 90  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 91 ? 17.949  -17.331 -1.679  1.00 30.58  ? 90  ALA A CB  1 
ATOM   728  N  N   . SER A 1 92 ? 17.957  -17.517 -4.714  1.00 38.21  ? 91  SER A N   1 
ATOM   729  C  CA  . SER A 1 92 ? 17.645  -18.349 -5.877  1.00 37.86  ? 91  SER A CA  1 
ATOM   730  C  C   . SER A 1 92 ? 17.268  -19.754 -5.431  1.00 38.46  ? 91  SER A C   1 
ATOM   731  O  O   . SER A 1 92 ? 18.023  -20.398 -4.698  1.00 46.25  ? 91  SER A O   1 
ATOM   732  C  CB  . SER A 1 92 ? 18.832  -18.465 -6.832  1.00 43.95  ? 91  SER A CB  1 
ATOM   733  O  OG  . SER A 1 92 ? 19.498  -17.233 -7.052  1.00 51.54  ? 91  SER A OG  1 
ATOM   734  N  N   . TYR A 1 93 ? 16.119  -20.240 -5.890  1.00 44.06  ? 92  TYR A N   1 
ATOM   735  C  CA  . TYR A 1 93 ? 15.654  -21.581 -5.538  1.00 45.75  ? 92  TYR A CA  1 
ATOM   736  C  C   . TYR A 1 93 ? 15.479  -22.457 -6.777  1.00 46.11  ? 92  TYR A C   1 
ATOM   737  O  O   . TYR A 1 93 ? 16.445  -22.777 -7.464  1.00 52.93  ? 92  TYR A O   1 
ATOM   738  C  CB  . TYR A 1 93 ? 14.335  -21.502 -4.760  1.00 44.68  ? 92  TYR A CB  1 
ATOM   739  C  CG  . TYR A 1 93 ? 14.477  -20.994 -3.341  1.00 39.72  ? 92  TYR A CG  1 
ATOM   740  C  CD1 . TYR A 1 93 ? 14.795  -21.852 -2.301  1.00 39.72  ? 92  TYR A CD1 1 
ATOM   741  C  CD2 . TYR A 1 93 ? 14.280  -19.645 -3.041  1.00 38.56  ? 92  TYR A CD2 1 
ATOM   742  C  CE1 . TYR A 1 93 ? 14.925  -21.379 -0.988  1.00 35.72  ? 92  TYR A CE1 1 
ATOM   743  C  CE2 . TYR A 1 93 ? 14.399  -19.165 -1.737  1.00 37.74  ? 92  TYR A CE2 1 
ATOM   744  C  CZ  . TYR A 1 93 ? 14.724  -20.031 -0.718  1.00 34.92  ? 92  TYR A CZ  1 
ATOM   745  O  OH  . TYR A 1 93 ? 14.866  -19.564 0.569   1.00 40.24  ? 92  TYR A OH  1 
ATOM   746  N  N   . MET B 1 2  ? 38.485  -11.055 -41.614 1.00 100.29 ? 1   MET B N   1 
ATOM   747  C  CA  . MET B 1 2  ? 38.060  -11.743 -42.826 1.00 87.34  ? 1   MET B CA  1 
ATOM   748  C  C   . MET B 1 2  ? 36.543  -11.773 -42.904 1.00 77.94  ? 1   MET B C   1 
ATOM   749  O  O   . MET B 1 2  ? 35.871  -11.941 -41.884 1.00 77.12  ? 1   MET B O   1 
ATOM   750  C  CB  . MET B 1 2  ? 38.618  -13.169 -42.867 1.00 85.50  ? 1   MET B CB  1 
ATOM   751  C  CG  . MET B 1 2  ? 40.088  -13.262 -42.501 1.00 94.11  ? 1   MET B CG  1 
ATOM   752  S  SD  . MET B 1 2  ? 41.061  -11.943 -43.259 1.00 107.56 ? 1   MET B SD  1 
ATOM   753  C  CE  . MET B 1 2  ? 41.988  -12.849 -44.487 1.00 88.35  ? 1   MET B CE  1 
ATOM   754  N  N   . PRO B 1 3  ? 35.999  -11.586 -44.106 1.00 72.04  ? 2   PRO B N   1 
ATOM   755  C  CA  . PRO B 1 3  ? 34.549  -11.743 -44.286 1.00 70.49  ? 2   PRO B CA  1 
ATOM   756  C  C   . PRO B 1 3  ? 34.129  -13.170 -43.976 1.00 70.17  ? 2   PRO B C   1 
ATOM   757  O  O   . PRO B 1 3  ? 34.578  -14.124 -44.617 1.00 73.98  ? 2   PRO B O   1 
ATOM   758  C  CB  . PRO B 1 3  ? 34.333  -11.388 -45.762 1.00 67.21  ? 2   PRO B CB  1 
ATOM   759  C  CG  . PRO B 1 3  ? 35.509  -10.547 -46.125 1.00 61.86  ? 2   PRO B CG  1 
ATOM   760  C  CD  . PRO B 1 3  ? 36.659  -11.089 -45.325 1.00 66.47  ? 2   PRO B CD  1 
ATOM   761  N  N   . HIS B 1 4  ? 33.279  -13.313 -42.964 1.00 67.74  ? 3   HIS B N   1 
ATOM   762  C  CA  . HIS B 1 4  ? 32.726  -14.607 -42.609 1.00 62.99  ? 3   HIS B CA  1 
ATOM   763  C  C   . HIS B 1 4  ? 31.372  -14.785 -43.297 1.00 66.01  ? 3   HIS B C   1 
ATOM   764  O  O   . HIS B 1 4  ? 30.892  -13.900 -44.011 1.00 61.91  ? 3   HIS B O   1 
ATOM   765  C  CB  . HIS B 1 4  ? 32.624  -14.733 -41.091 1.00 59.47  ? 3   HIS B CB  1 
ATOM   766  C  CG  . HIS B 1 4  ? 33.947  -14.648 -40.391 1.00 70.53  ? 3   HIS B CG  1 
ATOM   767  N  ND1 . HIS B 1 4  ? 34.207  -13.728 -39.396 1.00 77.40  ? 3   HIS B ND1 1 
ATOM   768  C  CD2 . HIS B 1 4  ? 35.084  -15.369 -40.543 1.00 68.78  ? 3   HIS B CD2 1 
ATOM   769  C  CE1 . HIS B 1 4  ? 35.447  -13.885 -38.966 1.00 70.93  ? 3   HIS B CE1 1 
ATOM   770  N  NE2 . HIS B 1 4  ? 35.999  -14.875 -39.645 1.00 76.82  ? 3   HIS B NE2 1 
ATOM   771  N  N   . ALA B 1 5  ? 30.752  -15.955 -43.099 1.00 54.76  ? 4   ALA B N   1 
ATOM   772  C  CA  . ALA B 1 5  ? 29.417  -16.185 -43.649 1.00 48.85  ? 4   ALA B CA  1 
ATOM   773  C  C   . ALA B 1 5  ? 28.420  -15.182 -43.091 1.00 47.00  ? 4   ALA B C   1 
ATOM   774  O  O   . ALA B 1 5  ? 27.583  -14.644 -43.827 1.00 46.21  ? 4   ALA B O   1 
ATOM   775  C  CB  . ALA B 1 5  ? 28.957  -17.610 -43.339 1.00 42.26  ? 4   ALA B CB  1 
ATOM   776  N  N   . PHE B 1 6  ? 28.485  -14.941 -41.789 1.00 46.25  ? 5   PHE B N   1 
ATOM   777  C  CA  . PHE B 1 6  ? 27.683  -13.929 -41.123 1.00 41.91  ? 5   PHE B CA  1 
ATOM   778  C  C   . PHE B 1 6  ? 28.533  -12.688 -40.909 1.00 47.39  ? 5   PHE B C   1 
ATOM   779  O  O   . PHE B 1 6  ? 29.693  -12.779 -40.496 1.00 54.70  ? 5   PHE B O   1 
ATOM   780  C  CB  . PHE B 1 6  ? 27.152  -14.443 -39.778 1.00 42.66  ? 5   PHE B CB  1 
ATOM   781  C  CG  . PHE B 1 6  ? 26.127  -15.537 -39.910 1.00 37.45  ? 5   PHE B CG  1 
ATOM   782  C  CD1 . PHE B 1 6  ? 24.780  -15.233 -40.056 1.00 38.78  ? 5   PHE B CD1 1 
ATOM   783  C  CD2 . PHE B 1 6  ? 26.514  -16.874 -39.902 1.00 38.16  ? 5   PHE B CD2 1 
ATOM   784  C  CE1 . PHE B 1 6  ? 23.834  -16.243 -40.187 1.00 50.22  ? 5   PHE B CE1 1 
ATOM   785  C  CE2 . PHE B 1 6  ? 25.581  -17.874 -40.030 1.00 36.68  ? 5   PHE B CE2 1 
ATOM   786  C  CZ  . PHE B 1 6  ? 24.243  -17.566 -40.171 1.00 36.16  ? 5   PHE B CZ  1 
ATOM   787  N  N   . LYS B 1 7  ? 27.952  -11.532 -41.195 1.00 39.44  ? 6   LYS B N   1 
ATOM   788  C  CA  . LYS B 1 7  ? 28.662  -10.282 -40.991 1.00 37.19  ? 6   LYS B CA  1 
ATOM   789  C  C   . LYS B 1 7  ? 27.893  -9.411  -40.005 1.00 37.46  ? 6   LYS B C   1 
ATOM   790  O  O   . LYS B 1 7  ? 26.673  -9.557  -39.870 1.00 34.42  ? 6   LYS B O   1 
ATOM   791  C  CB  . LYS B 1 7  ? 28.838  -9.530  -42.315 1.00 39.87  ? 6   LYS B CB  1 
ATOM   792  C  CG  . LYS B 1 7  ? 27.540  -9.324  -43.084 1.00 46.05  ? 6   LYS B CG  1 
ATOM   793  C  CD  . LYS B 1 7  ? 27.817  -8.872  -44.511 1.00 45.42  ? 6   LYS B CD  1 
ATOM   794  C  CE  . LYS B 1 7  ? 26.532  -8.520  -45.248 1.00 56.71  ? 6   LYS B CE  1 
ATOM   795  N  NZ  . LYS B 1 7  ? 25.534  -9.636  -45.268 1.00 47.79  ? 6   LYS B NZ  1 
ATOM   796  N  N   . PRO B 1 8  ? 28.576  -8.518  -39.287 1.00 40.84  ? 7   PRO B N   1 
ATOM   797  C  CA  . PRO B 1 8  ? 27.885  -7.693  -38.290 1.00 37.40  ? 7   PRO B CA  1 
ATOM   798  C  C   . PRO B 1 8  ? 26.732  -6.922  -38.909 1.00 38.64  ? 7   PRO B C   1 
ATOM   799  O  O   . PRO B 1 8  ? 26.850  -6.345  -39.993 1.00 44.22  ? 7   PRO B O   1 
ATOM   800  C  CB  . PRO B 1 8  ? 28.986  -6.758  -37.783 1.00 42.46  ? 7   PRO B CB  1 
ATOM   801  C  CG  . PRO B 1 8  ? 30.233  -7.538  -37.965 1.00 51.32  ? 7   PRO B CG  1 
ATOM   802  C  CD  . PRO B 1 8  ? 30.037  -8.326  -39.236 1.00 47.55  ? 7   PRO B CD  1 
ATOM   803  N  N   . GLY B 1 9  ? 25.599  -6.930  -38.214 1.00 32.41  ? 8   GLY B N   1 
ATOM   804  C  CA  . GLY B 1 9  ? 24.382  -6.349  -38.726 1.00 31.86  ? 8   GLY B CA  1 
ATOM   805  C  C   . GLY B 1 9  ? 23.463  -7.334  -39.409 1.00 30.79  ? 8   GLY B C   1 
ATOM   806  O  O   . GLY B 1 9  ? 22.317  -6.978  -39.710 1.00 32.74  ? 8   GLY B O   1 
ATOM   807  N  N   . ASP B 1 10 ? 23.920  -8.558  -39.673 1.00 29.76  ? 9   ASP B N   1 
ATOM   808  C  CA  . ASP B 1 10 ? 23.008  -9.561  -40.201 1.00 29.63  ? 9   ASP B CA  1 
ATOM   809  C  C   . ASP B 1 10 ? 21.904  -9.860  -39.192 1.00 24.62  ? 9   ASP B C   1 
ATOM   810  O  O   . ASP B 1 10 ? 22.144  -9.926  -37.985 1.00 25.75  ? 9   ASP B O   1 
ATOM   811  C  CB  . ASP B 1 10 ? 23.770  -10.846 -40.544 1.00 29.88  ? 9   ASP B CB  1 
ATOM   812  C  CG  . ASP B 1 10 ? 24.586  -10.726 -41.813 1.00 37.85  ? 9   ASP B CG  1 
ATOM   813  O  OD1 . ASP B 1 10 ? 24.376  -9.752  -42.574 1.00 46.05  ? 9   ASP B OD1 1 
ATOM   814  O  OD2 . ASP B 1 10 ? 25.439  -11.608 -42.047 1.00 36.62  ? 9   ASP B OD2 1 
ATOM   815  N  N   . LEU B 1 11 ? 20.682  -9.982  -39.701 1.00 26.58  ? 10  LEU B N   1 
ATOM   816  C  CA  . LEU B 1 11 ? 19.493  -10.183 -38.890 1.00 23.25  ? 10  LEU B CA  1 
ATOM   817  C  C   . LEU B 1 11 ? 19.146  -11.674 -38.918 1.00 23.73  ? 10  LEU B C   1 
ATOM   818  O  O   . LEU B 1 11 ? 19.124  -12.292 -39.992 1.00 24.09  ? 10  LEU B O   1 
ATOM   819  C  CB  . LEU B 1 11 ? 18.330  -9.343  -39.412 1.00 22.56  ? 10  LEU B CB  1 
ATOM   820  C  CG  . LEU B 1 11 ? 18.632  -7.830  -39.412 1.00 25.69  ? 10  LEU B CG  1 
ATOM   821  C  CD1 . LEU B 1 11 ? 17.363  -7.089  -39.788 1.00 25.41  ? 10  LEU B CD1 1 
ATOM   822  C  CD2 . LEU B 1 11 ? 19.185  -7.379  -38.038 1.00 25.34  ? 10  LEU B CD2 1 
ATOM   823  N  N   . VAL B 1 12 ? 18.877  -12.244 -37.743 1.00 21.18  ? 11  VAL B N   1 
ATOM   824  C  CA  . VAL B 1 12 ? 18.713  -13.698 -37.609 1.00 22.51  ? 11  VAL B CA  1 
ATOM   825  C  C   . VAL B 1 12 ? 17.626  -14.006 -36.587 1.00 25.31  ? 11  VAL B C   1 
ATOM   826  O  O   . VAL B 1 12 ? 17.162  -13.137 -35.847 1.00 23.49  ? 11  VAL B O   1 
ATOM   827  C  CB  . VAL B 1 12 ? 20.031  -14.396 -37.196 1.00 22.91  ? 11  VAL B CB  1 
ATOM   828  C  CG1 . VAL B 1 12 ? 21.135  -14.187 -38.247 1.00 25.60  ? 11  VAL B CG1 1 
ATOM   829  C  CG2 . VAL B 1 12 ? 20.504  -13.972 -35.761 1.00 24.65  ? 11  VAL B CG2 1 
ATOM   830  N  N   . PHE B 1 13 ? 17.213  -15.277 -36.568 1.00 23.03  ? 12  PHE B N   1 
ATOM   831  C  CA  . PHE B 1 13 ? 16.647  -15.882 -35.371 1.00 24.66  ? 12  PHE B CA  1 
ATOM   832  C  C   . PHE B 1 13 ? 17.742  -16.738 -34.763 1.00 23.05  ? 12  PHE B C   1 
ATOM   833  O  O   . PHE B 1 13 ? 18.378  -17.528 -35.475 1.00 23.08  ? 12  PHE B O   1 
ATOM   834  C  CB  . PHE B 1 13 ? 15.414  -16.740 -35.669 1.00 23.51  ? 12  PHE B CB  1 
ATOM   835  C  CG  . PHE B 1 13 ? 14.212  -15.951 -36.076 1.00 24.52  ? 12  PHE B CG  1 
ATOM   836  C  CD1 . PHE B 1 13 ? 13.383  -15.370 -35.123 1.00 25.83  ? 12  PHE B CD1 1 
ATOM   837  C  CD2 . PHE B 1 13 ? 13.912  -15.774 -37.411 1.00 26.99  ? 12  PHE B CD2 1 
ATOM   838  C  CE1 . PHE B 1 13 ? 12.270  -14.639 -35.502 1.00 27.03  ? 12  PHE B CE1 1 
ATOM   839  C  CE2 . PHE B 1 13 ? 12.807  -15.025 -37.803 1.00 30.43  ? 12  PHE B CE2 1 
ATOM   840  C  CZ  . PHE B 1 13 ? 11.987  -14.448 -36.846 1.00 27.64  ? 12  PHE B CZ  1 
ATOM   841  N  N   . ALA B 1 14 ? 17.992  -16.543 -33.467 1.00 21.89  ? 13  ALA B N   1 
ATOM   842  C  CA  . ALA B 1 14 ? 19.040  -17.242 -32.745 1.00 22.25  ? 13  ALA B CA  1 
ATOM   843  C  C   . ALA B 1 14 ? 18.380  -18.214 -31.774 1.00 21.00  ? 13  ALA B C   1 
ATOM   844  O  O   . ALA B 1 14 ? 17.447  -17.839 -31.052 1.00 24.15  ? 13  ALA B O   1 
ATOM   845  C  CB  . ALA B 1 14 ? 19.933  -16.273 -31.992 1.00 22.87  ? 13  ALA B CB  1 
ATOM   846  N  N   . LYS B 1 15 ? 18.820  -19.471 -31.809 1.00 25.57  ? 14  LYS B N   1 
ATOM   847  C  CA  . LYS B 1 15 ? 18.199  -20.524 -31.015 1.00 27.98  ? 14  LYS B CA  1 
ATOM   848  C  C   . LYS B 1 15 ? 19.068  -20.869 -29.817 1.00 26.25  ? 14  LYS B C   1 
ATOM   849  O  O   . LYS B 1 15 ? 20.249  -21.202 -29.970 1.00 29.54  ? 14  LYS B O   1 
ATOM   850  C  CB  . LYS B 1 15 ? 17.956  -21.776 -31.859 1.00 27.73  ? 14  LYS B CB  1 
ATOM   851  C  CG  . LYS B 1 15 ? 17.154  -22.855 -31.089 1.00 28.73  ? 14  LYS B CG  1 
ATOM   852  C  CD  . LYS B 1 15 ? 15.716  -22.358 -30.871 1.00 32.33  ? 14  LYS B CD  1 
ATOM   853  C  CE  . LYS B 1 15 ? 14.818  -23.442 -30.261 1.00 37.43  ? 14  LYS B CE  1 
ATOM   854  N  NZ  . LYS B 1 15 ? 15.172  -23.711 -28.842 1.00 28.57  ? 14  LYS B NZ  1 
ATOM   855  N  N   . MET B 1 16 ? 18.477  -20.797 -28.627 1.00 32.66  ? 15  MET B N   1 
ATOM   856  C  CA  . MET B 1 16 ? 19.123  -21.245 -27.405 1.00 35.78  ? 15  MET B CA  1 
ATOM   857  C  C   . MET B 1 16 ? 18.217  -22.239 -26.697 1.00 34.72  ? 15  MET B C   1 
ATOM   858  O  O   . MET B 1 16 ? 16.989  -22.121 -26.765 1.00 34.37  ? 15  MET B O   1 
ATOM   859  C  CB  . MET B 1 16 ? 19.432  -20.078 -26.500 1.00 30.81  ? 15  MET B CB  1 
ATOM   860  C  CG  . MET B 1 16 ? 20.422  -19.137 -27.126 1.00 36.10  ? 15  MET B CG  1 
ATOM   861  S  SD  . MET B 1 16 ? 21.362  -18.205 -25.936 1.00 44.35  ? 15  MET B SD  1 
ATOM   862  C  CE  . MET B 1 16 ? 20.067  -17.479 -24.960 1.00 43.35  ? 15  MET B CE  1 
ATOM   863  N  N   . LYS B 1 17 ? 18.826  -23.233 -26.047 1.00 42.74  ? 16  LYS B N   1 
ATOM   864  C  CA  . LYS B 1 17 ? 18.045  -24.277 -25.393 1.00 43.49  ? 16  LYS B CA  1 
ATOM   865  C  C   . LYS B 1 17 ? 17.127  -23.656 -24.352 1.00 31.63  ? 16  LYS B C   1 
ATOM   866  O  O   . LYS B 1 17 ? 17.537  -22.783 -23.585 1.00 34.29  ? 16  LYS B O   1 
ATOM   867  C  CB  . LYS B 1 17 ? 18.964  -25.322 -24.748 1.00 48.49  ? 16  LYS B CB  1 
ATOM   868  C  CG  . LYS B 1 17 ? 19.704  -26.249 -25.724 1.00 60.91  ? 16  LYS B CG  1 
ATOM   869  C  CD  . LYS B 1 17 ? 18.808  -26.718 -26.880 1.00 61.37  ? 16  LYS B CD  1 
ATOM   870  C  CE  . LYS B 1 17 ? 19.219  -26.061 -28.213 1.00 52.49  ? 16  LYS B CE  1 
ATOM   871  N  NZ  . LYS B 1 17 ? 18.113  -26.035 -29.213 1.00 52.51  ? 16  LYS B NZ  1 
ATOM   872  N  N   . GLY B 1 18 ? 15.859  -24.056 -24.379 1.00 36.22  ? 17  GLY B N   1 
ATOM   873  C  CA  . GLY B 1 18 ? 14.892  -23.514 -23.451 1.00 40.86  ? 17  GLY B CA  1 
ATOM   874  C  C   . GLY B 1 18 ? 14.148  -22.285 -23.923 1.00 40.69  ? 17  GLY B C   1 
ATOM   875  O  O   . GLY B 1 18 ? 13.262  -21.818 -23.202 1.00 35.20  ? 17  GLY B O   1 
ATOM   876  N  N   . TYR B 1 19 ? 14.467  -21.756 -25.111 1.00 34.80  ? 18  TYR B N   1 
ATOM   877  C  CA  . TYR B 1 19 ? 13.860  -20.564 -25.681 1.00 31.75  ? 18  TYR B CA  1 
ATOM   878  C  C   . TYR B 1 19 ? 13.499  -20.804 -27.139 1.00 26.98  ? 18  TYR B C   1 
ATOM   879  O  O   . TYR B 1 19 ? 14.224  -21.508 -27.851 1.00 32.59  ? 18  TYR B O   1 
ATOM   880  C  CB  . TYR B 1 19 ? 14.814  -19.365 -25.613 1.00 29.88  ? 18  TYR B CB  1 
ATOM   881  C  CG  . TYR B 1 19 ? 15.265  -19.053 -24.213 1.00 34.22  ? 18  TYR B CG  1 
ATOM   882  C  CD1 . TYR B 1 19 ? 14.434  -18.368 -23.345 1.00 34.28  ? 18  TYR B CD1 1 
ATOM   883  C  CD2 . TYR B 1 19 ? 16.519  -19.447 -23.766 1.00 35.45  ? 18  TYR B CD2 1 
ATOM   884  C  CE1 . TYR B 1 19 ? 14.836  -18.087 -22.052 1.00 40.60  ? 18  TYR B CE1 1 
ATOM   885  C  CE2 . TYR B 1 19 ? 16.932  -19.160 -22.472 1.00 43.59  ? 18  TYR B CE2 1 
ATOM   886  C  CZ  . TYR B 1 19 ? 16.085  -18.478 -21.623 1.00 40.43  ? 18  TYR B CZ  1 
ATOM   887  O  OH  . TYR B 1 19 ? 16.481  -18.193 -20.335 1.00 43.01  ? 18  TYR B OH  1 
ATOM   888  N  N   . PRO B 1 20 ? 12.387  -20.248 -27.604 1.00 26.21  ? 19  PRO B N   1 
ATOM   889  C  CA  . PRO B 1 20 ? 12.096  -20.289 -29.041 1.00 26.02  ? 19  PRO B CA  1 
ATOM   890  C  C   . PRO B 1 20 ? 13.149  -19.521 -29.824 1.00 29.12  ? 19  PRO B C   1 
ATOM   891  O  O   . PRO B 1 20 ? 13.843  -18.653 -29.284 1.00 24.58  ? 19  PRO B O   1 
ATOM   892  C  CB  . PRO B 1 20 ? 10.732  -19.608 -29.148 1.00 28.03  ? 19  PRO B CB  1 
ATOM   893  C  CG  . PRO B 1 20 ? 10.724  -18.631 -27.978 1.00 30.85  ? 19  PRO B CG  1 
ATOM   894  C  CD  . PRO B 1 20 ? 11.465  -19.355 -26.874 1.00 29.97  ? 19  PRO B CD  1 
ATOM   895  N  N   . HIS B 1 21 ? 13.270  -19.871 -31.109 1.00 28.81  ? 20  HIS B N   1 
ATOM   896  C  CA  . HIS B 1 21 ? 14.076  -19.087 -32.040 1.00 26.37  ? 20  HIS B CA  1 
ATOM   897  C  C   . HIS B 1 21 ? 13.770  -17.609 -31.861 1.00 20.92  ? 20  HIS B C   1 
ATOM   898  O  O   . HIS B 1 21 ? 12.615  -17.194 -31.928 1.00 23.34  ? 20  HIS B O   1 
ATOM   899  C  CB  . HIS B 1 21 ? 13.771  -19.536 -33.482 1.00 22.89  ? 20  HIS B CB  1 
ATOM   900  C  CG  . HIS B 1 21 ? 14.039  -20.995 -33.728 1.00 25.41  ? 20  HIS B CG  1 
ATOM   901  N  ND1 . HIS B 1 21 ? 13.177  -21.992 -33.321 1.00 28.85  ? 20  HIS B ND1 1 
ATOM   902  C  CD2 . HIS B 1 21 ? 15.081  -21.620 -34.325 1.00 29.08  ? 20  HIS B CD2 1 
ATOM   903  C  CE1 . HIS B 1 21 ? 13.665  -23.166 -33.676 1.00 29.19  ? 20  HIS B CE1 1 
ATOM   904  N  NE2 . HIS B 1 21 ? 14.824  -22.973 -34.278 1.00 28.68  ? 20  HIS B NE2 1 
ATOM   905  N  N   . TRP B 1 22 ? 14.803  -16.814 -31.616 1.00 23.73  ? 21  TRP B N   1 
ATOM   906  C  CA  . TRP B 1 22 ? 14.617  -15.483 -31.048 1.00 21.96  ? 21  TRP B CA  1 
ATOM   907  C  C   . TRP B 1 22 ? 15.167  -14.432 -31.999 1.00 23.89  ? 21  TRP B C   1 
ATOM   908  O  O   . TRP B 1 22 ? 16.312  -14.578 -32.454 1.00 24.57  ? 21  TRP B O   1 
ATOM   909  C  CB  . TRP B 1 22 ? 15.344  -15.398 -29.719 1.00 23.70  ? 21  TRP B CB  1 
ATOM   910  C  CG  . TRP B 1 22 ? 14.810  -14.308 -28.857 1.00 24.84  ? 21  TRP B CG  1 
ATOM   911  C  CD1 . TRP B 1 22 ? 15.110  -12.964 -28.945 1.00 26.58  ? 21  TRP B CD1 1 
ATOM   912  C  CD2 . TRP B 1 22 ? 13.874  -14.445 -27.780 1.00 23.41  ? 21  TRP B CD2 1 
ATOM   913  N  NE1 . TRP B 1 22 ? 14.404  -12.266 -27.985 1.00 27.33  ? 21  TRP B NE1 1 
ATOM   914  C  CE2 . TRP B 1 22 ? 13.641  -13.155 -27.260 1.00 25.01  ? 21  TRP B CE2 1 
ATOM   915  C  CE3 . TRP B 1 22 ? 13.210  -15.536 -27.207 1.00 27.40  ? 21  TRP B CE3 1 
ATOM   916  C  CZ2 . TRP B 1 22 ? 12.769  -12.925 -26.205 1.00 29.87  ? 21  TRP B CZ2 1 
ATOM   917  C  CZ3 . TRP B 1 22 ? 12.351  -15.301 -26.148 1.00 30.96  ? 21  TRP B CZ3 1 
ATOM   918  C  CH2 . TRP B 1 22 ? 12.141  -14.005 -25.658 1.00 29.19  ? 21  TRP B CH2 1 
ATOM   919  N  N   . PRO B 1 23 ? 14.410  -13.369 -32.299 1.00 23.24  ? 22  PRO B N   1 
ATOM   920  C  CA  . PRO B 1 23 ? 14.915  -12.303 -33.181 1.00 22.51  ? 22  PRO B CA  1 
ATOM   921  C  C   . PRO B 1 23 ? 16.191  -11.695 -32.619 1.00 24.71  ? 22  PRO B C   1 
ATOM   922  O  O   . PRO B 1 23 ? 16.261  -11.306 -31.446 1.00 23.14  ? 22  PRO B O   1 
ATOM   923  C  CB  . PRO B 1 23 ? 13.764  -11.290 -33.197 1.00 26.05  ? 22  PRO B CB  1 
ATOM   924  C  CG  . PRO B 1 23 ? 13.081  -11.499 -31.855 1.00 25.61  ? 22  PRO B CG  1 
ATOM   925  C  CD  . PRO B 1 23 ? 13.079  -13.036 -31.782 1.00 21.06  ? 22  PRO B CD  1 
ATOM   926  N  N   . ALA B 1 24 ? 17.215  -11.620 -33.459 1.00 22.07  ? 23  ALA B N   1 
ATOM   927  C  CA  . ALA B 1 24 ? 18.539  -11.243 -32.986 1.00 22.96  ? 23  ALA B CA  1 
ATOM   928  C  C   . ALA B 1 24 ? 19.343  -10.630 -34.137 1.00 22.74  ? 23  ALA B C   1 
ATOM   929  O  O   . ALA B 1 24 ? 18.932  -10.655 -35.299 1.00 24.67  ? 23  ALA B O   1 
ATOM   930  C  CB  . ALA B 1 24 ? 19.263  -12.440 -32.367 1.00 22.35  ? 23  ALA B CB  1 
ATOM   931  N  N   . ARG B 1 25 ? 20.527  -10.122 -33.803 1.00 26.45  ? 24  ARG B N   1 
ATOM   932  C  CA  . ARG B 1 25 ? 21.458  -9.662  -34.823 1.00 25.50  ? 24  ARG B CA  1 
ATOM   933  C  C   . ARG B 1 25 ? 22.871  -10.113 -34.485 1.00 22.42  ? 24  ARG B C   1 
ATOM   934  O  O   . ARG B 1 25 ? 23.213  -10.388 -33.327 1.00 28.30  ? 24  ARG B O   1 
ATOM   935  C  CB  . ARG B 1 25 ? 21.433  -8.123  -34.965 1.00 23.58  ? 24  ARG B CB  1 
ATOM   936  C  CG  . ARG B 1 25 ? 21.964  -7.411  -33.753 1.00 23.84  ? 24  ARG B CG  1 
ATOM   937  C  CD  . ARG B 1 25 ? 21.676  -5.889  -33.815 1.00 21.53  ? 24  ARG B CD  1 
ATOM   938  N  NE  . ARG B 1 25 ? 22.346  -5.223  -32.707 1.00 26.57  ? 24  ARG B NE  1 
ATOM   939  C  CZ  . ARG B 1 25 ? 22.088  -3.983  -32.312 1.00 29.38  ? 24  ARG B CZ  1 
ATOM   940  N  NH1 . ARG B 1 25 ? 21.127  -3.272  -32.877 1.00 29.45  ? 24  ARG B NH1 1 
ATOM   941  N  NH2 . ARG B 1 25 ? 22.809  -3.454  -31.330 1.00 26.84  ? 24  ARG B NH2 1 
ATOM   942  N  N   . ILE B 1 26 ? 23.689  -10.207 -35.529 1.00 26.79  ? 25  ILE B N   1 
ATOM   943  C  CA  . ILE B 1 26 ? 25.127  -10.365 -35.367 1.00 24.91  ? 25  ILE B CA  1 
ATOM   944  C  C   . ILE B 1 26 ? 25.699  -9.002  -35.008 1.00 34.72  ? 25  ILE B C   1 
ATOM   945  O  O   . ILE B 1 26 ? 25.586  -8.054  -35.792 1.00 33.15  ? 25  ILE B O   1 
ATOM   946  C  CB  . ILE B 1 26 ? 25.788  -10.892 -36.648 1.00 34.01  ? 25  ILE B CB  1 
ATOM   947  C  CG1 . ILE B 1 26 ? 25.042  -12.113 -37.186 1.00 36.47  ? 25  ILE B CG1 1 
ATOM   948  C  CG2 . ILE B 1 26 ? 27.279  -11.164 -36.387 1.00 30.72  ? 25  ILE B CG2 1 
ATOM   949  C  CD1 . ILE B 1 26 ? 25.279  -13.339 -36.390 1.00 33.96  ? 25  ILE B CD1 1 
ATOM   950  N  N   . ASP B 1 27 ? 26.324  -8.912  -33.840 1.00 31.05  ? 26  ASP B N   1 
ATOM   951  C  CA  . ASP B 1 27 ? 27.044  -7.725  -33.416 1.00 38.38  ? 26  ASP B CA  1 
ATOM   952  C  C   . ASP B 1 27 ? 28.462  -7.721  -33.978 1.00 44.34  ? 26  ASP B C   1 
ATOM   953  O  O   . ASP B 1 27 ? 28.957  -8.719  -34.513 1.00 44.82  ? 26  ASP B O   1 
ATOM   954  C  CB  . ASP B 1 27 ? 27.087  -7.645  -31.890 1.00 37.91  ? 26  ASP B CB  1 
ATOM   955  C  CG  . ASP B 1 27 ? 25.905  -6.909  -31.324 1.00 39.23  ? 26  ASP B CG  1 
ATOM   956  O  OD1 . ASP B 1 27 ? 25.135  -6.369  -32.143 1.00 36.50  ? 26  ASP B OD1 1 
ATOM   957  O  OD2 . ASP B 1 27 ? 25.749  -6.865  -30.081 1.00 36.99  ? 26  ASP B OD2 1 
ATOM   958  N  N   . ASP B 1 28 ? 29.124  -6.573  -33.846 1.00 50.31  ? 27  ASP B N   1 
ATOM   959  C  CA  . ASP B 1 28 ? 30.552  -6.530  -34.114 1.00 56.33  ? 27  ASP B CA  1 
ATOM   960  C  C   . ASP B 1 28 ? 31.325  -6.883  -32.850 1.00 52.77  ? 27  ASP B C   1 
ATOM   961  O  O   . ASP B 1 28 ? 30.789  -6.872  -31.740 1.00 51.11  ? 27  ASP B O   1 
ATOM   962  C  CB  . ASP B 1 28 ? 30.994  -5.165  -34.633 1.00 55.74  ? 27  ASP B CB  1 
ATOM   963  C  CG  . ASP B 1 28 ? 32.025  -5.287  -35.733 1.00 67.27  ? 27  ASP B CG  1 
ATOM   964  O  OD1 . ASP B 1 28 ? 32.086  -4.399  -36.604 1.00 68.93  ? 27  ASP B OD1 1 
ATOM   965  O  OD2 . ASP B 1 28 ? 32.763  -6.302  -35.746 1.00 71.19  ? 27  ASP B OD2 1 
ATOM   966  N  N   . ILE B 1 29 ? 32.610  -7.183  -33.036 1.00 57.24  ? 28  ILE B N   1 
ATOM   967  C  CA  . ILE B 1 29 ? 33.418  -7.693  -31.935 1.00 61.06  ? 28  ILE B CA  1 
ATOM   968  C  C   . ILE B 1 29 ? 33.980  -6.553  -31.086 1.00 69.91  ? 28  ILE B C   1 
ATOM   969  O  O   . ILE B 1 29 ? 33.991  -6.640  -29.852 1.00 78.32  ? 28  ILE B O   1 
ATOM   970  C  CB  . ILE B 1 29 ? 34.521  -8.621  -32.486 1.00 62.57  ? 28  ILE B CB  1 
ATOM   971  C  CG1 . ILE B 1 29 ? 33.929  -10.005 -32.796 1.00 70.13  ? 28  ILE B CG1 1 
ATOM   972  C  CG2 . ILE B 1 29 ? 35.679  -8.740  -31.505 1.00 70.71  ? 28  ILE B CG2 1 
ATOM   973  C  CD1 . ILE B 1 29 ? 34.864  -10.940 -33.553 1.00 69.88  ? 28  ILE B CD1 1 
ATOM   974  N  N   . ALA B 1 30 ? 34.425  -5.467  -31.719 1.00 64.16  ? 29  ALA B N   1 
ATOM   975  C  CA  . ALA B 1 30 ? 35.001  -4.316  -31.011 1.00 63.01  ? 29  ALA B CA  1 
ATOM   976  C  C   . ALA B 1 30 ? 36.179  -4.719  -30.115 1.00 59.59  ? 29  ALA B C   1 
ATOM   977  O  O   . ALA B 1 30 ? 36.021  -4.938  -28.909 1.00 75.40  ? 29  ALA B O   1 
ATOM   978  C  CB  . ALA B 1 30 ? 33.925  -3.597  -30.187 1.00 66.26  ? 29  ALA B CB  1 
ATOM   979  N  N   . LYS B 1 35 ? 36.939  -11.551 -27.388 1.00 73.98  ? 34  LYS B N   1 
ATOM   980  C  CA  . LYS B 1 35 ? 36.639  -12.263 -28.627 1.00 66.38  ? 34  LYS B CA  1 
ATOM   981  C  C   . LYS B 1 35 ? 35.801  -13.514 -28.351 1.00 62.43  ? 34  LYS B C   1 
ATOM   982  O  O   . LYS B 1 35 ? 35.882  -14.095 -27.268 1.00 57.14  ? 34  LYS B O   1 
ATOM   983  C  CB  . LYS B 1 35 ? 37.933  -12.638 -29.357 1.00 55.79  ? 34  LYS B CB  1 
ATOM   984  N  N   . PRO B 1 36 ? 34.987  -13.919 -29.322 1.00 70.66  ? 35  PRO B N   1 
ATOM   985  C  CA  . PRO B 1 36 ? 34.183  -15.147 -29.167 1.00 57.85  ? 35  PRO B CA  1 
ATOM   986  C  C   . PRO B 1 36 ? 35.032  -16.389 -29.368 1.00 56.93  ? 35  PRO B C   1 
ATOM   987  O  O   . PRO B 1 36 ? 36.095  -16.332 -30.005 1.00 55.92  ? 35  PRO B O   1 
ATOM   988  C  CB  . PRO B 1 36 ? 33.131  -15.018 -30.278 1.00 49.73  ? 35  PRO B CB  1 
ATOM   989  C  CG  . PRO B 1 36 ? 33.793  -14.160 -31.316 1.00 63.50  ? 35  PRO B CG  1 
ATOM   990  C  CD  . PRO B 1 36 ? 34.648  -13.183 -30.554 1.00 60.57  ? 35  PRO B CD  1 
ATOM   991  N  N   . PRO B 1 37 ? 34.598  -17.535 -28.846 1.00 51.83  ? 36  PRO B N   1 
ATOM   992  C  CA  . PRO B 1 37 ? 35.256  -18.787 -29.203 1.00 61.95  ? 36  PRO B CA  1 
ATOM   993  C  C   . PRO B 1 37 ? 35.216  -18.991 -30.704 1.00 64.04  ? 36  PRO B C   1 
ATOM   994  O  O   . PRO B 1 37 ? 34.327  -18.460 -31.396 1.00 59.55  ? 36  PRO B O   1 
ATOM   995  C  CB  . PRO B 1 37 ? 34.423  -19.846 -28.467 1.00 53.53  ? 36  PRO B CB  1 
ATOM   996  C  CG  . PRO B 1 37 ? 33.780  -19.113 -27.339 1.00 58.20  ? 36  PRO B CG  1 
ATOM   997  C  CD  . PRO B 1 37 ? 33.525  -17.728 -27.854 1.00 60.25  ? 36  PRO B CD  1 
ATOM   998  N  N   . PRO B 1 38 ? 36.168  -19.744 -31.258 1.00 65.56  ? 37  PRO B N   1 
ATOM   999  C  CA  . PRO B 1 38 ? 36.160  -19.972 -32.707 1.00 66.48  ? 37  PRO B CA  1 
ATOM   1000 C  C   . PRO B 1 38 ? 34.866  -20.648 -33.134 1.00 61.35  ? 37  PRO B C   1 
ATOM   1001 O  O   . PRO B 1 38 ? 34.236  -21.369 -32.357 1.00 62.43  ? 37  PRO B O   1 
ATOM   1002 C  CB  . PRO B 1 38 ? 37.376  -20.878 -32.935 1.00 70.19  ? 37  PRO B CB  1 
ATOM   1003 C  CG  . PRO B 1 38 ? 37.608  -21.538 -31.615 1.00 65.42  ? 37  PRO B CG  1 
ATOM   1004 C  CD  . PRO B 1 38 ? 37.228  -20.511 -30.584 1.00 64.38  ? 37  PRO B CD  1 
ATOM   1005 N  N   . ASN B 1 39 ? 34.463  -20.375 -34.377 1.00 62.00  ? 38  ASN B N   1 
ATOM   1006 C  CA  . ASN B 1 39 ? 33.203  -20.812 -34.974 1.00 63.78  ? 38  ASN B CA  1 
ATOM   1007 C  C   . ASN B 1 39 ? 31.985  -20.120 -34.373 1.00 49.75  ? 38  ASN B C   1 
ATOM   1008 O  O   . ASN B 1 39 ? 30.859  -20.493 -34.697 1.00 48.82  ? 38  ASN B O   1 
ATOM   1009 C  CB  . ASN B 1 39 ? 33.003  -22.331 -34.867 1.00 65.20  ? 38  ASN B CB  1 
ATOM   1010 C  CG  . ASN B 1 39 ? 34.211  -23.118 -35.340 1.00 80.07  ? 38  ASN B CG  1 
ATOM   1011 O  OD1 . ASN B 1 39 ? 34.719  -22.895 -36.441 1.00 92.18  ? 38  ASN B OD1 1 
ATOM   1012 N  ND2 . ASN B 1 39 ? 34.683  -24.041 -34.503 1.00 71.17  ? 38  ASN B ND2 1 
ATOM   1013 N  N   . LYS B 1 40 ? 32.165  -19.130 -33.505 1.00 47.29  ? 39  LYS B N   1 
ATOM   1014 C  CA  . LYS B 1 40 ? 31.034  -18.494 -32.853 1.00 40.99  ? 39  LYS B CA  1 
ATOM   1015 C  C   . LYS B 1 40 ? 31.050  -16.990 -33.094 1.00 45.54  ? 39  LYS B C   1 
ATOM   1016 O  O   . LYS B 1 40 ? 32.083  -16.397 -33.416 1.00 44.94  ? 39  LYS B O   1 
ATOM   1017 C  CB  . LYS B 1 40 ? 31.018  -18.804 -31.358 1.00 43.84  ? 39  LYS B CB  1 
ATOM   1018 C  CG  . LYS B 1 40 ? 30.754  -20.273 -31.060 1.00 38.80  ? 39  LYS B CG  1 
ATOM   1019 C  CD  . LYS B 1 40 ? 30.512  -20.494 -29.569 1.00 50.14  ? 39  LYS B CD  1 
ATOM   1020 C  CE  . LYS B 1 40 ? 29.792  -21.809 -29.325 1.00 56.08  ? 39  LYS B CE  1 
ATOM   1021 N  NZ  . LYS B 1 40 ? 30.330  -22.862 -30.213 1.00 52.16  ? 39  LYS B NZ  1 
ATOM   1022 N  N   . TYR B 1 41 ? 29.874  -16.389 -32.946 1.00 35.62  ? 40  TYR B N   1 
ATOM   1023 C  CA  . TYR B 1 41 ? 29.625  -14.984 -33.222 1.00 36.35  ? 40  TYR B CA  1 
ATOM   1024 C  C   . TYR B 1 41 ? 29.009  -14.317 -32.003 1.00 37.75  ? 40  TYR B C   1 
ATOM   1025 O  O   . TYR B 1 41 ? 28.264  -14.955 -31.253 1.00 33.11  ? 40  TYR B O   1 
ATOM   1026 C  CB  . TYR B 1 41 ? 28.668  -14.814 -34.410 1.00 34.39  ? 40  TYR B CB  1 
ATOM   1027 C  CG  . TYR B 1 41 ? 29.194  -15.280 -35.742 1.00 38.03  ? 40  TYR B CG  1 
ATOM   1028 C  CD1 . TYR B 1 41 ? 29.814  -14.394 -36.614 1.00 41.14  ? 40  TYR B CD1 1 
ATOM   1029 C  CD2 . TYR B 1 41 ? 29.034  -16.593 -36.149 1.00 38.01  ? 40  TYR B CD2 1 
ATOM   1030 C  CE1 . TYR B 1 41 ? 30.283  -14.806 -37.839 1.00 43.50  ? 40  TYR B CE1 1 
ATOM   1031 C  CE2 . TYR B 1 41 ? 29.508  -17.019 -37.383 1.00 35.32  ? 40  TYR B CE2 1 
ATOM   1032 C  CZ  . TYR B 1 41 ? 30.134  -16.121 -38.220 1.00 44.58  ? 40  TYR B CZ  1 
ATOM   1033 O  OH  . TYR B 1 41 ? 30.595  -16.537 -39.454 1.00 41.67  ? 40  TYR B OH  1 
ATOM   1034 N  N   . PRO B 1 42 ? 29.290  -13.031 -31.785 1.00 39.20  ? 41  PRO B N   1 
ATOM   1035 C  CA  . PRO B 1 42 ? 28.550  -12.285 -30.754 1.00 33.47  ? 41  PRO B CA  1 
ATOM   1036 C  C   . PRO B 1 42 ? 27.125  -12.020 -31.219 1.00 33.00  ? 41  PRO B C   1 
ATOM   1037 O  O   . PRO B 1 42 ? 26.907  -11.404 -32.266 1.00 30.59  ? 41  PRO B O   1 
ATOM   1038 C  CB  . PRO B 1 42 ? 29.350  -10.986 -30.606 1.00 34.73  ? 41  PRO B CB  1 
ATOM   1039 C  CG  . PRO B 1 42 ? 30.057  -10.827 -31.921 1.00 36.85  ? 41  PRO B CG  1 
ATOM   1040 C  CD  . PRO B 1 42 ? 30.303  -12.208 -32.468 1.00 36.89  ? 41  PRO B CD  1 
ATOM   1041 N  N   . ILE B 1 43 ? 26.149  -12.502 -30.445 1.00 32.38  ? 42  ILE B N   1 
ATOM   1042 C  CA  . ILE B 1 43 ? 24.731  -12.354 -30.770 1.00 29.59  ? 42  ILE B CA  1 
ATOM   1043 C  C   . ILE B 1 43 ? 24.095  -11.358 -29.804 1.00 31.12  ? 42  ILE B C   1 
ATOM   1044 O  O   . ILE B 1 43 ? 24.367  -11.392 -28.599 1.00 35.98  ? 42  ILE B O   1 
ATOM   1045 C  CB  . ILE B 1 43 ? 24.009  -13.719 -30.718 1.00 25.35  ? 42  ILE B CB  1 
ATOM   1046 C  CG1 . ILE B 1 43 ? 24.735  -14.736 -31.608 1.00 28.17  ? 42  ILE B CG1 1 
ATOM   1047 C  CG2 . ILE B 1 43 ? 22.540  -13.549 -31.104 1.00 30.86  ? 42  ILE B CG2 1 
ATOM   1048 C  CD1 . ILE B 1 43 ? 24.869  -14.345 -33.057 1.00 26.99  ? 42  ILE B CD1 1 
ATOM   1049 N  N   . PHE B 1 44 ? 23.267  -10.454 -30.341 1.00 28.07  ? 43  PHE B N   1 
ATOM   1050 C  CA  . PHE B 1 44 ? 22.460  -9.529  -29.547 1.00 26.76  ? 43  PHE B CA  1 
ATOM   1051 C  C   . PHE B 1 44 ? 20.989  -9.871  -29.750 1.00 23.97  ? 43  PHE B C   1 
ATOM   1052 O  O   . PHE B 1 44 ? 20.503  -9.903  -30.885 1.00 24.46  ? 43  PHE B O   1 
ATOM   1053 C  CB  . PHE B 1 44 ? 22.745  -8.069  -29.927 1.00 28.49  ? 43  PHE B CB  1 
ATOM   1054 C  CG  . PHE B 1 44 ? 21.787  -7.078  -29.307 1.00 27.78  ? 43  PHE B CG  1 
ATOM   1055 C  CD1 . PHE B 1 44 ? 20.624  -6.707  -29.965 1.00 26.45  ? 43  PHE B CD1 1 
ATOM   1056 C  CD2 . PHE B 1 44 ? 22.055  -6.528  -28.056 1.00 33.47  ? 43  PHE B CD2 1 
ATOM   1057 C  CE1 . PHE B 1 44 ? 19.740  -5.785  -29.395 1.00 31.87  ? 43  PHE B CE1 1 
ATOM   1058 C  CE2 . PHE B 1 44 ? 21.185  -5.606  -27.481 1.00 32.70  ? 43  PHE B CE2 1 
ATOM   1059 C  CZ  . PHE B 1 44 ? 20.028  -5.233  -28.149 1.00 28.66  ? 43  PHE B CZ  1 
ATOM   1060 N  N   . PHE B 1 45 ? 20.293  -10.184 -28.654 1.00 27.49  ? 44  PHE B N   1 
ATOM   1061 C  CA  . PHE B 1 45 ? 18.895  -10.597 -28.717 1.00 25.76  ? 44  PHE B CA  1 
ATOM   1062 C  C   . PHE B 1 45 ? 17.983  -9.380  -28.597 1.00 26.76  ? 44  PHE B C   1 
ATOM   1063 O  O   . PHE B 1 45 ? 18.051  -8.632  -27.612 1.00 27.63  ? 44  PHE B O   1 
ATOM   1064 C  CB  . PHE B 1 45 ? 18.590  -11.631 -27.620 1.00 23.31  ? 44  PHE B CB  1 
ATOM   1065 C  CG  . PHE B 1 45 ? 19.328  -12.935 -27.786 1.00 26.34  ? 44  PHE B CG  1 
ATOM   1066 C  CD1 . PHE B 1 45 ? 20.590  -13.114 -27.240 1.00 30.12  ? 44  PHE B CD1 1 
ATOM   1067 C  CD2 . PHE B 1 45 ? 18.749  -13.987 -28.475 1.00 29.66  ? 44  PHE B CD2 1 
ATOM   1068 C  CE1 . PHE B 1 45 ? 21.279  -14.317 -27.395 1.00 33.53  ? 44  PHE B CE1 1 
ATOM   1069 C  CE2 . PHE B 1 45 ? 19.429  -15.196 -28.637 1.00 28.24  ? 44  PHE B CE2 1 
ATOM   1070 C  CZ  . PHE B 1 45 ? 20.690  -15.365 -28.095 1.00 31.40  ? 44  PHE B CZ  1 
ATOM   1071 N  N   . PHE B 1 46 ? 17.109  -9.193  -29.580 1.00 24.32  ? 45  PHE B N   1 
ATOM   1072 C  CA  . PHE B 1 46 ? 16.164  -8.095  -29.509 1.00 26.74  ? 45  PHE B CA  1 
ATOM   1073 C  C   . PHE B 1 46 ? 15.141  -8.341  -28.401 1.00 33.91  ? 45  PHE B C   1 
ATOM   1074 O  O   . PHE B 1 46 ? 14.935  -9.470  -27.942 1.00 31.61  ? 45  PHE B O   1 
ATOM   1075 C  CB  . PHE B 1 46 ? 15.461  -7.890  -30.845 1.00 28.68  ? 45  PHE B CB  1 
ATOM   1076 C  CG  . PHE B 1 46 ? 16.368  -7.400  -31.922 1.00 29.08  ? 45  PHE B CG  1 
ATOM   1077 C  CD1 . PHE B 1 46 ? 16.901  -6.118  -31.871 1.00 26.45  ? 45  PHE B CD1 1 
ATOM   1078 C  CD2 . PHE B 1 46 ? 16.707  -8.219  -32.991 1.00 27.88  ? 45  PHE B CD2 1 
ATOM   1079 C  CE1 . PHE B 1 46 ? 17.750  -5.663  -32.871 1.00 24.90  ? 45  PHE B CE1 1 
ATOM   1080 C  CE2 . PHE B 1 46 ? 17.560  -7.772  -33.996 1.00 25.73  ? 45  PHE B CE2 1 
ATOM   1081 C  CZ  . PHE B 1 46 ? 18.060  -6.482  -33.950 1.00 23.97  ? 45  PHE B CZ  1 
ATOM   1082 N  N   . GLY B 1 47 ? 14.525  -7.251  -27.945 1.00 31.02  ? 46  GLY B N   1 
ATOM   1083 C  CA  . GLY B 1 47 ? 13.560  -7.317  -26.864 1.00 26.05  ? 46  GLY B CA  1 
ATOM   1084 C  C   . GLY B 1 47 ? 14.239  -7.432  -25.515 1.00 31.21  ? 46  GLY B C   1 
ATOM   1085 O  O   . GLY B 1 47 ? 14.124  -6.523  -24.682 1.00 37.93  ? 46  GLY B O   1 
ATOM   1086 N  N   . THR B 1 48 ? 14.958  -8.531  -25.281 1.00 27.70  ? 47  THR B N   1 
ATOM   1087 C  CA  . THR B 1 48 ? 15.638  -8.711  -24.005 1.00 32.45  ? 47  THR B CA  1 
ATOM   1088 C  C   . THR B 1 48 ? 16.951  -7.952  -23.947 1.00 38.53  ? 47  THR B C   1 
ATOM   1089 O  O   . THR B 1 48 ? 17.441  -7.654  -22.851 1.00 35.94  ? 47  THR B O   1 
ATOM   1090 C  CB  . THR B 1 48 ? 15.935  -10.189 -23.729 1.00 33.92  ? 47  THR B CB  1 
ATOM   1091 O  OG1 . THR B 1 48 ? 16.908  -10.673 -24.669 1.00 28.69  ? 47  THR B OG1 1 
ATOM   1092 C  CG2 . THR B 1 48 ? 14.671  -11.031 -23.794 1.00 31.42  ? 47  THR B CG2 1 
ATOM   1093 N  N   . HIS B 1 49 ? 17.539  -7.658  -25.105 1.00 30.27  ? 48  HIS B N   1 
ATOM   1094 C  CA  . HIS B 1 49 ? 18.847  -7.027  -25.219 1.00 33.59  ? 48  HIS B CA  1 
ATOM   1095 C  C   . HIS B 1 49 ? 19.946  -7.821  -24.534 1.00 28.86  ? 48  HIS B C   1 
ATOM   1096 O  O   . HIS B 1 49 ? 21.011  -7.262  -24.238 1.00 35.81  ? 48  HIS B O   1 
ATOM   1097 C  CB  . HIS B 1 49 ? 18.820  -5.588  -24.694 1.00 28.83  ? 48  HIS B CB  1 
ATOM   1098 C  CG  . HIS B 1 49 ? 17.606  -4.826  -25.110 1.00 34.33  ? 48  HIS B CG  1 
ATOM   1099 N  ND1 . HIS B 1 49 ? 17.071  -4.909  -26.376 1.00 33.11  ? 48  HIS B ND1 1 
ATOM   1100 C  CD2 . HIS B 1 49 ? 16.819  -3.958  -24.428 1.00 36.69  ? 48  HIS B CD2 1 
ATOM   1101 C  CE1 . HIS B 1 49 ? 16.008  -4.128  -26.457 1.00 32.64  ? 48  HIS B CE1 1 
ATOM   1102 N  NE2 . HIS B 1 49 ? 15.829  -3.547  -25.284 1.00 43.57  ? 48  HIS B NE2 1 
ATOM   1103 N  N   . GLU B 1 50 ? 19.727  -9.117  -24.288 1.00 29.58  ? 49  GLU B N   1 
ATOM   1104 C  CA  . GLU B 1 50 ? 20.807  -9.983  -23.842 1.00 30.34  ? 49  GLU B CA  1 
ATOM   1105 C  C   . GLU B 1 50 ? 21.776  -10.251 -24.988 1.00 36.07  ? 49  GLU B C   1 
ATOM   1106 O  O   . GLU B 1 50 ? 21.488  -9.970  -26.154 1.00 36.78  ? 49  GLU B O   1 
ATOM   1107 C  CB  . GLU B 1 50 ? 20.259  -11.299 -23.303 1.00 37.37  ? 49  GLU B CB  1 
ATOM   1108 C  CG  . GLU B 1 50 ? 19.160  -11.081 -22.285 1.00 44.53  ? 49  GLU B CG  1 
ATOM   1109 C  CD  . GLU B 1 50 ? 18.995  -12.231 -21.319 1.00 62.92  ? 49  GLU B CD  1 
ATOM   1110 O  OE1 . GLU B 1 50 ? 19.402  -13.375 -21.644 1.00 58.05  ? 49  GLU B OE1 1 
ATOM   1111 O  OE2 . GLU B 1 50 ? 18.441  -11.977 -20.228 1.00 48.15  ? 49  GLU B OE2 1 
ATOM   1112 N  N   . THR B 1 51 ? 22.949  -10.778 -24.631 1.00 36.70  ? 50  THR B N   1 
ATOM   1113 C  CA  . THR B 1 51 ? 23.988  -11.168 -25.575 1.00 36.94  ? 50  THR B CA  1 
ATOM   1114 C  C   . THR B 1 51 ? 24.489  -12.575 -25.257 1.00 44.37  ? 50  THR B C   1 
ATOM   1115 O  O   . THR B 1 51 ? 24.430  -13.035 -24.110 1.00 40.04  ? 50  THR B O   1 
ATOM   1116 C  CB  . THR B 1 51 ? 25.183  -10.195 -25.557 1.00 38.69  ? 50  THR B CB  1 
ATOM   1117 O  OG1 . THR B 1 51 ? 25.777  -10.192 -24.249 1.00 45.08  ? 50  THR B OG1 1 
ATOM   1118 C  CG2 . THR B 1 51 ? 24.741  -8.790  -25.897 1.00 33.25  ? 50  THR B CG2 1 
ATOM   1119 N  N   . ALA B 1 52 ? 24.999  -13.249 -26.284 1.00 39.28  ? 51  ALA B N   1 
ATOM   1120 C  CA  . ALA B 1 52 ? 25.594  -14.570 -26.139 1.00 38.45  ? 51  ALA B CA  1 
ATOM   1121 C  C   . ALA B 1 52 ? 26.475  -14.844 -27.347 1.00 35.46  ? 51  ALA B C   1 
ATOM   1122 O  O   . ALA B 1 52 ? 26.387  -14.162 -28.372 1.00 36.20  ? 51  ALA B O   1 
ATOM   1123 C  CB  . ALA B 1 52 ? 24.537  -15.668 -26.003 1.00 36.09  ? 51  ALA B CB  1 
ATOM   1124 N  N   . PHE B 1 53 ? 27.341  -15.842 -27.201 1.00 33.73  ? 52  PHE B N   1 
ATOM   1125 C  CA  . PHE B 1 53 ? 28.149  -16.362 -28.299 1.00 33.26  ? 52  PHE B CA  1 
ATOM   1126 C  C   . PHE B 1 53 ? 27.485  -17.630 -28.827 1.00 35.96  ? 52  PHE B C   1 
ATOM   1127 O  O   . PHE B 1 53 ? 27.292  -18.588 -28.073 1.00 35.90  ? 52  PHE B O   1 
ATOM   1128 C  CB  . PHE B 1 53 ? 29.575  -16.668 -27.842 1.00 37.62  ? 52  PHE B CB  1 
ATOM   1129 C  CG  . PHE B 1 53 ? 30.350  -15.458 -27.417 1.00 51.25  ? 52  PHE B CG  1 
ATOM   1130 C  CD1 . PHE B 1 53 ? 30.526  -14.395 -28.287 1.00 46.53  ? 52  PHE B CD1 1 
ATOM   1131 C  CD2 . PHE B 1 53 ? 30.905  -15.387 -26.150 1.00 51.05  ? 52  PHE B CD2 1 
ATOM   1132 C  CE1 . PHE B 1 53 ? 31.238  -13.280 -27.906 1.00 45.34  ? 52  PHE B CE1 1 
ATOM   1133 C  CE2 . PHE B 1 53 ? 31.621  -14.264 -25.757 1.00 50.89  ? 52  PHE B CE2 1 
ATOM   1134 C  CZ  . PHE B 1 53 ? 31.786  -13.210 -26.640 1.00 52.05  ? 52  PHE B CZ  1 
ATOM   1135 N  N   . LEU B 1 54 ? 27.146  -17.640 -30.113 1.00 33.96  ? 53  LEU B N   1 
ATOM   1136 C  CA  . LEU B 1 54 ? 26.528  -18.802 -30.732 1.00 30.45  ? 53  LEU B CA  1 
ATOM   1137 C  C   . LEU B 1 54 ? 27.194  -19.110 -32.068 1.00 30.84  ? 53  LEU B C   1 
ATOM   1138 O  O   . LEU B 1 54 ? 27.706  -18.216 -32.754 1.00 32.89  ? 53  LEU B O   1 
ATOM   1139 C  CB  . LEU B 1 54 ? 25.021  -18.596 -30.948 1.00 29.94  ? 53  LEU B CB  1 
ATOM   1140 C  CG  . LEU B 1 54 ? 24.128  -18.483 -29.715 1.00 31.12  ? 53  LEU B CG  1 
ATOM   1141 C  CD1 . LEU B 1 54 ? 22.737  -18.119 -30.159 1.00 29.69  ? 53  LEU B CD1 1 
ATOM   1142 C  CD2 . LEU B 1 54 ? 24.111  -19.816 -28.980 1.00 36.79  ? 53  LEU B CD2 1 
ATOM   1143 N  N   . GLY B 1 55 ? 27.164  -20.391 -32.438 1.00 29.21  ? 54  GLY B N   1 
ATOM   1144 C  CA  . GLY B 1 55 ? 27.646  -20.837 -33.725 1.00 28.26  ? 54  GLY B CA  1 
ATOM   1145 C  C   . GLY B 1 55 ? 26.562  -20.900 -34.786 1.00 27.02  ? 54  GLY B C   1 
ATOM   1146 O  O   . GLY B 1 55 ? 25.362  -20.849 -34.486 1.00 27.78  ? 54  GLY B O   1 
ATOM   1147 N  N   . PRO B 1 56 ? 26.977  -21.052 -36.053 1.00 28.81  ? 55  PRO B N   1 
ATOM   1148 C  CA  . PRO B 1 56 ? 26.011  -21.020 -37.165 1.00 25.60  ? 55  PRO B CA  1 
ATOM   1149 C  C   . PRO B 1 56 ? 24.887  -22.039 -37.072 1.00 25.11  ? 55  PRO B C   1 
ATOM   1150 O  O   . PRO B 1 56 ? 23.803  -21.792 -37.627 1.00 25.89  ? 55  PRO B O   1 
ATOM   1151 C  CB  . PRO B 1 56 ? 26.893  -21.279 -38.395 1.00 31.45  ? 55  PRO B CB  1 
ATOM   1152 C  CG  . PRO B 1 56 ? 28.237  -20.789 -37.994 1.00 38.77  ? 55  PRO B CG  1 
ATOM   1153 C  CD  . PRO B 1 56 ? 28.368  -21.070 -36.527 1.00 32.53  ? 55  PRO B CD  1 
ATOM   1154 N  N   . LYS B 1 57 ? 25.095  -23.184 -36.402 1.00 25.64  ? 56  LYS B N   1 
ATOM   1155 C  CA  . LYS B 1 57 ? 23.999  -24.148 -36.327 1.00 28.05  ? 56  LYS B CA  1 
ATOM   1156 C  C   . LYS B 1 57 ? 22.767  -23.578 -35.631 1.00 28.59  ? 56  LYS B C   1 
ATOM   1157 O  O   . LYS B 1 57 ? 21.653  -24.069 -35.865 1.00 26.69  ? 56  LYS B O   1 
ATOM   1158 C  CB  . LYS B 1 57 ? 24.445  -25.434 -35.598 1.00 26.60  ? 56  LYS B CB  1 
ATOM   1159 C  CG  . LYS B 1 57 ? 24.713  -25.242 -34.118 1.00 28.97  ? 56  LYS B CG  1 
ATOM   1160 C  CD  . LYS B 1 57 ? 24.955  -26.580 -33.433 1.00 33.75  ? 56  LYS B CD  1 
ATOM   1161 C  CE  . LYS B 1 57 ? 25.143  -26.414 -31.935 1.00 35.54  ? 56  LYS B CE  1 
ATOM   1162 N  NZ  . LYS B 1 57 ? 23.874  -26.075 -31.216 1.00 39.46  ? 56  LYS B NZ  1 
ATOM   1163 N  N   . ASP B 1 58 ? 22.932  -22.545 -34.799 1.00 24.93  ? 57  ASP B N   1 
ATOM   1164 C  CA  . ASP B 1 58 ? 21.820  -21.946 -34.081 1.00 24.76  ? 57  ASP B CA  1 
ATOM   1165 C  C   . ASP B 1 58 ? 21.389  -20.605 -34.667 1.00 25.09  ? 57  ASP B C   1 
ATOM   1166 O  O   . ASP B 1 58 ? 20.605  -19.893 -34.032 1.00 25.34  ? 57  ASP B O   1 
ATOM   1167 C  CB  . ASP B 1 58 ? 22.184  -21.771 -32.611 1.00 27.16  ? 57  ASP B CB  1 
ATOM   1168 C  CG  . ASP B 1 58 ? 22.327  -23.108 -31.897 1.00 36.35  ? 57  ASP B CG  1 
ATOM   1169 O  OD1 . ASP B 1 58 ? 21.393  -23.929 -32.007 1.00 30.10  ? 57  ASP B OD1 1 
ATOM   1170 O  OD2 . ASP B 1 58 ? 23.369  -23.333 -31.243 1.00 34.51  ? 57  ASP B OD2 1 
ATOM   1171 N  N   . LEU B 1 59 ? 21.824  -20.271 -35.881 1.00 23.08  ? 58  LEU B N   1 
ATOM   1172 C  CA  . LEU B 1 59 ? 21.583  -18.945 -36.456 1.00 25.45  ? 58  LEU B CA  1 
ATOM   1173 C  C   . LEU B 1 59 ? 20.838  -19.119 -37.765 1.00 25.60  ? 58  LEU B C   1 
ATOM   1174 O  O   . LEU B 1 59 ? 21.328  -19.802 -38.677 1.00 28.70  ? 58  LEU B O   1 
ATOM   1175 C  CB  . LEU B 1 59 ? 22.896  -18.206 -36.690 1.00 27.24  ? 58  LEU B CB  1 
ATOM   1176 C  CG  . LEU B 1 59 ? 23.766  -18.010 -35.460 1.00 29.01  ? 58  LEU B CG  1 
ATOM   1177 C  CD1 . LEU B 1 59 ? 25.039  -17.315 -35.864 1.00 29.15  ? 58  LEU B CD1 1 
ATOM   1178 C  CD2 . LEU B 1 59 ? 22.985  -17.211 -34.380 1.00 26.77  ? 58  LEU B CD2 1 
ATOM   1179 N  N   . PHE B 1 60 ? 19.638  -18.547 -37.840 1.00 21.37  ? 59  PHE B N   1 
ATOM   1180 C  CA  . PHE B 1 60 ? 18.740  -18.695 -38.982 1.00 21.48  ? 59  PHE B CA  1 
ATOM   1181 C  C   . PHE B 1 60 ? 18.482  -17.325 -39.607 1.00 25.38  ? 59  PHE B C   1 
ATOM   1182 O  O   . PHE B 1 60 ? 18.213  -16.363 -38.871 1.00 23.98  ? 59  PHE B O   1 
ATOM   1183 C  CB  . PHE B 1 60 ? 17.408  -19.329 -38.540 1.00 25.19  ? 59  PHE B CB  1 
ATOM   1184 C  CG  . PHE B 1 60 ? 17.557  -20.706 -37.920 1.00 22.74  ? 59  PHE B CG  1 
ATOM   1185 C  CD1 . PHE B 1 60 ? 17.997  -20.852 -36.602 1.00 25.26  ? 59  PHE B CD1 1 
ATOM   1186 C  CD2 . PHE B 1 60 ? 17.243  -21.842 -38.648 1.00 33.33  ? 59  PHE B CD2 1 
ATOM   1187 C  CE1 . PHE B 1 60 ? 18.129  -22.123 -36.030 1.00 28.91  ? 59  PHE B CE1 1 
ATOM   1188 C  CE2 . PHE B 1 60 ? 17.359  -23.109 -38.073 1.00 25.42  ? 59  PHE B CE2 1 
ATOM   1189 C  CZ  . PHE B 1 60 ? 17.809  -23.246 -36.775 1.00 28.13  ? 59  PHE B CZ  1 
ATOM   1190 N  N   . PRO B 1 61 ? 18.547  -17.180 -40.933 1.00 23.33  ? 60  PRO B N   1 
ATOM   1191 C  CA  . PRO B 1 61 ? 18.328  -15.842 -41.523 1.00 23.49  ? 60  PRO B CA  1 
ATOM   1192 C  C   . PRO B 1 61 ? 16.932  -15.314 -41.225 1.00 23.92  ? 60  PRO B C   1 
ATOM   1193 O  O   . PRO B 1 61 ? 15.938  -16.025 -41.310 1.00 27.19  ? 60  PRO B O   1 
ATOM   1194 C  CB  . PRO B 1 61 ? 18.539  -16.065 -43.023 1.00 29.50  ? 60  PRO B CB  1 
ATOM   1195 C  CG  . PRO B 1 61 ? 19.293  -17.370 -43.116 1.00 35.38  ? 60  PRO B CG  1 
ATOM   1196 C  CD  . PRO B 1 61 ? 18.800  -18.199 -41.960 1.00 30.20  ? 60  PRO B CD  1 
ATOM   1197 N  N   . TYR B 1 62 ? 16.864  -14.033 -40.836 1.00 22.51  ? 61  TYR B N   1 
ATOM   1198 C  CA  . TYR B 1 62 ? 15.582  -13.486 -40.415 1.00 26.63  ? 61  TYR B CA  1 
ATOM   1199 C  C   . TYR B 1 62 ? 14.574  -13.466 -41.555 1.00 28.85  ? 61  TYR B C   1 
ATOM   1200 O  O   . TYR B 1 62 ? 13.425  -13.886 -41.387 1.00 33.92  ? 61  TYR B O   1 
ATOM   1201 C  CB  . TYR B 1 62 ? 15.777  -12.079 -39.859 1.00 24.48  ? 61  TYR B CB  1 
ATOM   1202 C  CG  . TYR B 1 62 ? 14.487  -11.325 -39.669 1.00 28.62  ? 61  TYR B CG  1 
ATOM   1203 C  CD1 . TYR B 1 62 ? 13.644  -11.617 -38.607 1.00 29.37  ? 61  TYR B CD1 1 
ATOM   1204 C  CD2 . TYR B 1 62 ? 14.126  -10.294 -40.536 1.00 32.37  ? 61  TYR B CD2 1 
ATOM   1205 C  CE1 . TYR B 1 62 ? 12.460  -10.919 -38.423 1.00 32.28  ? 61  TYR B CE1 1 
ATOM   1206 C  CE2 . TYR B 1 62 ? 12.953  -9.584  -40.348 1.00 34.33  ? 61  TYR B CE2 1 
ATOM   1207 C  CZ  . TYR B 1 62 ? 12.129  -9.903  -39.293 1.00 40.96  ? 61  TYR B CZ  1 
ATOM   1208 O  OH  . TYR B 1 62 ? 10.961  -9.215  -39.101 1.00 40.14  ? 61  TYR B OH  1 
ATOM   1209 N  N   . ASP B 1 63 ? 14.968  -12.934 -42.711 1.00 31.56  ? 62  ASP B N   1 
ATOM   1210 C  CA  . ASP B 1 63 ? 13.995  -12.737 -43.776 1.00 36.08  ? 62  ASP B CA  1 
ATOM   1211 C  C   . ASP B 1 63 ? 13.536  -14.069 -44.334 1.00 32.88  ? 62  ASP B C   1 
ATOM   1212 O  O   . ASP B 1 63 ? 12.346  -14.255 -44.608 1.00 39.30  ? 62  ASP B O   1 
ATOM   1213 C  CB  . ASP B 1 63 ? 14.588  -11.872 -44.882 1.00 33.79  ? 62  ASP B CB  1 
ATOM   1214 C  CG  . ASP B 1 63 ? 14.255  -10.392 -44.711 1.00 57.87  ? 62  ASP B CG  1 
ATOM   1215 O  OD1 . ASP B 1 63 ? 13.389  -10.041 -43.871 1.00 57.02  ? 62  ASP B OD1 1 
ATOM   1216 O  OD2 . ASP B 1 63 ? 14.864  -9.572  -45.438 1.00 72.33  ? 62  ASP B OD2 1 
ATOM   1217 N  N   . LYS B 1 64 ? 14.467  -15.021 -44.463 1.00 34.61  ? 63  LYS B N   1 
ATOM   1218 C  CA  . LYS B 1 64 ? 14.123  -16.355 -44.951 1.00 35.34  ? 63  LYS B CA  1 
ATOM   1219 C  C   . LYS B 1 64 ? 13.139  -17.049 -44.018 1.00 35.80  ? 63  LYS B C   1 
ATOM   1220 O  O   . LYS B 1 64 ? 12.200  -17.714 -44.474 1.00 41.75  ? 63  LYS B O   1 
ATOM   1221 C  CB  . LYS B 1 64 ? 15.395  -17.195 -45.103 1.00 35.88  ? 63  LYS B CB  1 
ATOM   1222 C  CG  . LYS B 1 64 ? 15.176  -18.672 -45.551 1.00 37.58  ? 63  LYS B CG  1 
ATOM   1223 C  CD  . LYS B 1 64 ? 16.459  -19.520 -45.323 1.00 34.19  ? 63  LYS B CD  1 
ATOM   1224 C  CE  . LYS B 1 64 ? 16.381  -20.907 -45.957 1.00 34.33  ? 63  LYS B CE  1 
ATOM   1225 N  NZ  . LYS B 1 64 ? 15.362  -21.757 -45.289 1.00 37.81  ? 63  LYS B NZ  1 
ATOM   1226 N  N   . CYS B 1 65 ? 13.317  -16.893 -42.706 1.00 30.29  ? 64  CYS B N   1 
ATOM   1227 C  CA  . CYS B 1 65 ? 12.643  -17.791 -41.776 1.00 38.56  ? 64  CYS B CA  1 
ATOM   1228 C  C   . CYS B 1 65 ? 11.646  -17.101 -40.849 1.00 32.53  ? 64  CYS B C   1 
ATOM   1229 O  O   . CYS B 1 65 ? 11.103  -17.763 -39.952 1.00 36.98  ? 64  CYS B O   1 
ATOM   1230 C  CB  . CYS B 1 65 ? 13.684  -18.571 -40.962 1.00 34.24  ? 64  CYS B CB  1 
ATOM   1231 S  SG  . CYS B 1 65 ? 14.726  -19.687 -41.975 1.00 38.48  ? 64  CYS B SG  1 
ATOM   1232 N  N   . LYS B 1 66 ? 11.354  -15.807 -41.058 1.00 35.48  ? 65  LYS B N   1 
ATOM   1233 C  CA  . LYS B 1 66 ? 10.430  -15.106 -40.164 1.00 40.96  ? 65  LYS B CA  1 
ATOM   1234 C  C   . LYS B 1 66 ? 9.005   -15.630 -40.287 1.00 43.01  ? 65  LYS B C   1 
ATOM   1235 O  O   . LYS B 1 66 ? 8.252   -15.603 -39.306 1.00 44.07  ? 65  LYS B O   1 
ATOM   1236 C  CB  . LYS B 1 66 ? 10.463  -13.598 -40.425 1.00 34.15  ? 65  LYS B CB  1 
ATOM   1237 C  CG  . LYS B 1 66 ? 10.001  -13.179 -41.814 1.00 35.23  ? 65  LYS B CG  1 
ATOM   1238 C  CD  . LYS B 1 66 ? 10.591  -11.847 -42.185 1.00 46.71  ? 65  LYS B CD  1 
ATOM   1239 C  CE  . LYS B 1 66 ? 9.734   -11.131 -43.205 1.00 53.10  ? 65  LYS B CE  1 
ATOM   1240 N  NZ  . LYS B 1 66 ? 9.835   -9.664  -42.966 1.00 57.26  ? 65  LYS B NZ  1 
ATOM   1241 N  N   . ASP B 1 67 ? 8.614   -16.098 -41.476 1.00 42.77  ? 66  ASP B N   1 
ATOM   1242 C  CA  . ASP B 1 67 ? 7.319   -16.753 -41.626 1.00 50.91  ? 66  ASP B CA  1 
ATOM   1243 C  C   . ASP B 1 67 ? 7.145   -17.864 -40.597 1.00 43.30  ? 66  ASP B C   1 
ATOM   1244 O  O   . ASP B 1 67 ? 6.049   -18.070 -40.061 1.00 51.04  ? 66  ASP B O   1 
ATOM   1245 C  CB  . ASP B 1 67 ? 7.187   -17.311 -43.047 1.00 55.39  ? 66  ASP B CB  1 
ATOM   1246 C  CG  . ASP B 1 67 ? 8.335   -18.252 -43.420 1.00 65.57  ? 66  ASP B CG  1 
ATOM   1247 O  OD1 . ASP B 1 67 ? 9.495   -17.985 -43.030 1.00 59.90  ? 66  ASP B OD1 1 
ATOM   1248 O  OD2 . ASP B 1 67 ? 8.074   -19.266 -44.105 1.00 72.26  ? 66  ASP B OD2 1 
ATOM   1249 N  N   . LYS B 1 68 ? 8.228   -18.572 -40.291 1.00 41.09  ? 67  LYS B N   1 
ATOM   1250 C  CA  . LYS B 1 68 ? 8.189   -19.719 -39.396 1.00 35.75  ? 67  LYS B CA  1 
ATOM   1251 C  C   . LYS B 1 68 ? 8.379   -19.330 -37.933 1.00 39.84  ? 67  LYS B C   1 
ATOM   1252 O  O   . LYS B 1 68 ? 7.617   -19.774 -37.070 1.00 45.10  ? 67  LYS B O   1 
ATOM   1253 C  CB  . LYS B 1 68 ? 9.267   -20.715 -39.817 1.00 40.93  ? 67  LYS B CB  1 
ATOM   1254 C  CG  . LYS B 1 68 ? 9.297   -21.989 -39.031 1.00 44.71  ? 67  LYS B CG  1 
ATOM   1255 C  CD  . LYS B 1 68 ? 10.563  -22.779 -39.368 1.00 52.75  ? 67  LYS B CD  1 
ATOM   1256 C  CE  . LYS B 1 68 ? 10.643  -23.197 -40.842 1.00 50.73  ? 67  LYS B CE  1 
ATOM   1257 N  NZ  . LYS B 1 68 ? 11.373  -22.272 -41.774 1.00 53.69  ? 67  LYS B NZ  1 
ATOM   1258 N  N   . TYR B 1 69 ? 9.392   -18.511 -37.639 1.00 35.56  ? 68  TYR B N   1 
ATOM   1259 C  CA  . TYR B 1 69 ? 9.800   -18.222 -36.267 1.00 29.30  ? 68  TYR B CA  1 
ATOM   1260 C  C   . TYR B 1 69 ? 9.250   -16.908 -35.741 1.00 32.79  ? 68  TYR B C   1 
ATOM   1261 O  O   . TYR B 1 69 ? 9.427   -16.616 -34.553 1.00 30.79  ? 68  TYR B O   1 
ATOM   1262 C  CB  . TYR B 1 69 ? 11.338  -18.195 -36.167 1.00 27.75  ? 68  TYR B CB  1 
ATOM   1263 C  CG  . TYR B 1 69 ? 11.982  -19.495 -36.605 1.00 30.06  ? 68  TYR B CG  1 
ATOM   1264 C  CD1 . TYR B 1 69 ? 11.596  -20.693 -36.033 1.00 31.73  ? 68  TYR B CD1 1 
ATOM   1265 C  CD2 . TYR B 1 69 ? 12.965  -19.521 -37.594 1.00 28.30  ? 68  TYR B CD2 1 
ATOM   1266 C  CE1 . TYR B 1 69 ? 12.162  -21.886 -36.426 1.00 28.18  ? 68  TYR B CE1 1 
ATOM   1267 C  CE2 . TYR B 1 69 ? 13.541  -20.724 -38.005 1.00 34.24  ? 68  TYR B CE2 1 
ATOM   1268 C  CZ  . TYR B 1 69 ? 13.132  -21.905 -37.407 1.00 33.69  ? 68  TYR B CZ  1 
ATOM   1269 O  OH  . TYR B 1 69 ? 13.664  -23.130 -37.780 1.00 31.14  ? 68  TYR B OH  1 
ATOM   1270 N  N   . GLY B 1 70 ? 8.600   -16.111 -36.585 1.00 38.30  ? 69  GLY B N   1 
ATOM   1271 C  CA  . GLY B 1 70 ? 8.255   -14.756 -36.197 1.00 38.00  ? 69  GLY B CA  1 
ATOM   1272 C  C   . GLY B 1 70 ? 6.888   -14.579 -35.562 1.00 47.32  ? 69  GLY B C   1 
ATOM   1273 O  O   . GLY B 1 70 ? 6.363   -13.459 -35.514 1.00 55.08  ? 69  GLY B O   1 
ATOM   1274 N  N   . LYS B 1 71 ? 6.311   -15.658 -35.059 1.00 45.17  ? 70  LYS B N   1 
ATOM   1275 C  CA  . LYS B 1 71 ? 4.958   -15.465 -34.557 1.00 44.08  ? 70  LYS B CA  1 
ATOM   1276 C  C   . LYS B 1 71 ? 4.987   -15.185 -33.063 1.00 52.86  ? 70  LYS B C   1 
ATOM   1277 O  O   . LYS B 1 71 ? 5.788   -15.783 -32.338 1.00 51.41  ? 70  LYS B O   1 
ATOM   1278 C  CB  . LYS B 1 71 ? 4.100   -16.688 -34.836 1.00 44.79  ? 70  LYS B CB  1 
ATOM   1279 C  CG  . LYS B 1 71 ? 4.838   -18.000 -34.617 1.00 65.21  ? 70  LYS B CG  1 
ATOM   1280 C  CD  . LYS B 1 71 ? 4.173   -19.156 -35.353 1.00 58.78  ? 70  LYS B CD  1 
ATOM   1281 C  CE  . LYS B 1 71 ? 4.122   -18.898 -36.857 1.00 69.32  ? 70  LYS B CE  1 
ATOM   1282 N  NZ  . LYS B 1 71 ? 3.423   -19.995 -37.606 1.00 70.21  ? 70  LYS B NZ  1 
ATOM   1283 N  N   . PRO B 1 72 ? 4.133   -14.282 -32.588 1.00 56.78  ? 71  PRO B N   1 
ATOM   1284 C  CA  . PRO B 1 72 ? 4.199   -13.881 -31.180 1.00 52.85  ? 71  PRO B CA  1 
ATOM   1285 C  C   . PRO B 1 72 ? 3.948   -15.051 -30.243 1.00 49.54  ? 71  PRO B C   1 
ATOM   1286 O  O   . PRO B 1 72 ? 3.329   -16.060 -30.589 1.00 50.47  ? 71  PRO B O   1 
ATOM   1287 C  CB  . PRO B 1 72 ? 3.097   -12.820 -31.056 1.00 47.71  ? 71  PRO B CB  1 
ATOM   1288 C  CG  . PRO B 1 72 ? 2.942   -12.286 -32.442 1.00 57.74  ? 71  PRO B CG  1 
ATOM   1289 C  CD  . PRO B 1 72 ? 3.173   -13.466 -33.351 1.00 55.16  ? 71  PRO B CD  1 
ATOM   1290 N  N   . ASN B 1 73 ? 4.471   -14.902 -29.035 1.00 53.46  ? 72  ASN B N   1 
ATOM   1291 C  CA  . ASN B 1 73 ? 4.250   -15.868 -27.978 1.00 43.66  ? 72  ASN B CA  1 
ATOM   1292 C  C   . ASN B 1 73 ? 4.211   -15.110 -26.655 1.00 40.56  ? 72  ASN B C   1 
ATOM   1293 O  O   . ASN B 1 73 ? 4.207   -13.872 -26.626 1.00 50.29  ? 72  ASN B O   1 
ATOM   1294 C  CB  . ASN B 1 73 ? 5.324   -16.965 -28.025 1.00 44.32  ? 72  ASN B CB  1 
ATOM   1295 C  CG  . ASN B 1 73 ? 6.726   -16.405 -27.894 1.00 37.50  ? 72  ASN B CG  1 
ATOM   1296 O  OD1 . ASN B 1 73 ? 7.016   -15.647 -26.975 1.00 37.14  ? 72  ASN B OD1 1 
ATOM   1297 N  ND2 . ASN B 1 73 ? 7.598   -16.752 -28.836 1.00 35.84  ? 72  ASN B ND2 1 
ATOM   1298 N  N   . LYS B 1 74 ? 4.231   -15.869 -25.567 1.00 43.15  ? 73  LYS B N   1 
ATOM   1299 C  CA  . LYS B 1 74 ? 4.081   -15.379 -24.207 1.00 46.41  ? 73  LYS B CA  1 
ATOM   1300 C  C   . LYS B 1 74 ? 5.413   -15.174 -23.495 1.00 52.96  ? 73  LYS B C   1 
ATOM   1301 O  O   . LYS B 1 74 ? 5.421   -14.832 -22.307 1.00 39.23  ? 73  LYS B O   1 
ATOM   1302 C  CB  . LYS B 1 74 ? 3.200   -16.343 -23.407 1.00 50.17  ? 73  LYS B CB  1 
ATOM   1303 C  CG  . LYS B 1 74 ? 3.777   -17.775 -23.223 1.00 55.21  ? 73  LYS B CG  1 
ATOM   1304 C  CD  . LYS B 1 74 ? 4.017   -18.526 -24.554 1.00 64.69  ? 73  LYS B CD  1 
ATOM   1305 C  CE  . LYS B 1 74 ? 4.622   -19.905 -24.413 1.00 49.00  ? 73  LYS B CE  1 
ATOM   1306 N  NZ  . LYS B 1 74 ? 5.025   -20.370 -25.767 1.00 59.50  ? 73  LYS B NZ  1 
ATOM   1307 N  N   . ARG B 1 75 ? 6.534   -15.389 -24.178 1.00 33.46  ? 74  ARG B N   1 
ATOM   1308 C  CA  . ARG B 1 75 ? 7.831   -15.211 -23.541 1.00 32.36  ? 74  ARG B CA  1 
ATOM   1309 C  C   . ARG B 1 75 ? 8.146   -13.728 -23.395 1.00 39.03  ? 74  ARG B C   1 
ATOM   1310 O  O   . ARG B 1 75 ? 7.905   -12.929 -24.306 1.00 34.51  ? 74  ARG B O   1 
ATOM   1311 C  CB  . ARG B 1 75 ? 8.936   -15.903 -24.349 1.00 36.76  ? 74  ARG B CB  1 
ATOM   1312 C  CG  . ARG B 1 75 ? 8.710   -17.395 -24.639 1.00 32.11  ? 74  ARG B CG  1 
ATOM   1313 C  CD  . ARG B 1 75 ? 8.555   -18.182 -23.371 1.00 40.61  ? 74  ARG B CD  1 
ATOM   1314 N  NE  . ARG B 1 75 ? 8.746   -19.610 -23.580 1.00 34.41  ? 74  ARG B NE  1 
ATOM   1315 C  CZ  . ARG B 1 75 ? 9.910   -20.237 -23.457 1.00 35.15  ? 74  ARG B CZ  1 
ATOM   1316 N  NH1 . ARG B 1 75 ? 11.018  -19.585 -23.152 1.00 34.49  ? 74  ARG B NH1 1 
ATOM   1317 N  NH2 . ARG B 1 75 ? 9.963   -21.556 -23.634 1.00 40.16  ? 74  ARG B NH2 1 
ATOM   1318 N  N   . LYS B 1 76 ? 8.709   -13.369 -22.244 1.00 34.14  ? 75  LYS B N   1 
ATOM   1319 C  CA  . LYS B 1 76 ? 9.001   -11.976 -21.941 1.00 35.51  ? 75  LYS B CA  1 
ATOM   1320 C  C   . LYS B 1 76 ? 10.089  -11.418 -22.859 1.00 32.89  ? 75  LYS B C   1 
ATOM   1321 O  O   . LYS B 1 76 ? 11.186  -11.980 -22.960 1.00 30.26  ? 75  LYS B O   1 
ATOM   1322 C  CB  . LYS B 1 76 ? 9.438   -11.844 -20.485 1.00 34.71  ? 75  LYS B CB  1 
ATOM   1323 C  CG  . LYS B 1 76 ? 9.696   -10.404 -20.086 1.00 34.69  ? 75  LYS B CG  1 
ATOM   1324 C  CD  . LYS B 1 76 ? 10.575  -10.332 -18.847 1.00 42.94  ? 75  LYS B CD  1 
ATOM   1325 C  CE  . LYS B 1 76 ? 10.738  -8.881  -18.418 1.00 39.62  ? 75  LYS B CE  1 
ATOM   1326 N  NZ  . LYS B 1 76 ? 11.688  -8.742  -17.274 1.00 62.54  ? 75  LYS B NZ  1 
ATOM   1327 N  N   . GLY B 1 77 ? 9.784   -10.288 -23.504 1.00 33.72  ? 76  GLY B N   1 
ATOM   1328 C  CA  . GLY B 1 77 ? 10.699  -9.628  -24.405 1.00 34.80  ? 76  GLY B CA  1 
ATOM   1329 C  C   . GLY B 1 77 ? 10.543  -10.026 -25.854 1.00 35.21  ? 76  GLY B C   1 
ATOM   1330 O  O   . GLY B 1 77 ? 11.161  -9.399  -26.725 1.00 31.89  ? 76  GLY B O   1 
ATOM   1331 N  N   . PHE B 1 78 ? 9.727   -11.040 -26.148 1.00 30.45  ? 77  PHE B N   1 
ATOM   1332 C  CA  . PHE B 1 78 ? 9.672   -11.561 -27.510 1.00 27.75  ? 77  PHE B CA  1 
ATOM   1333 C  C   . PHE B 1 78 ? 8.964   -10.604 -28.456 1.00 32.63  ? 77  PHE B C   1 
ATOM   1334 O  O   . PHE B 1 78 ? 9.485   -10.286 -29.535 1.00 30.88  ? 77  PHE B O   1 
ATOM   1335 C  CB  . PHE B 1 78 ? 8.981   -12.915 -27.536 1.00 28.38  ? 77  PHE B CB  1 
ATOM   1336 C  CG  . PHE B 1 78 ? 9.164   -13.630 -28.836 1.00 31.54  ? 77  PHE B CG  1 
ATOM   1337 C  CD1 . PHE B 1 78 ? 10.314  -14.385 -29.055 1.00 30.74  ? 77  PHE B CD1 1 
ATOM   1338 C  CD2 . PHE B 1 78 ? 8.214   -13.526 -29.847 1.00 32.48  ? 77  PHE B CD2 1 
ATOM   1339 C  CE1 . PHE B 1 78 ? 10.499  -15.039 -30.255 1.00 30.25  ? 77  PHE B CE1 1 
ATOM   1340 C  CE2 . PHE B 1 78 ? 8.407   -14.193 -31.049 1.00 31.14  ? 77  PHE B CE2 1 
ATOM   1341 C  CZ  . PHE B 1 78 ? 9.547   -14.932 -31.243 1.00 24.11  ? 77  PHE B CZ  1 
ATOM   1342 N  N   . ASN B 1 79 ? 7.760   -10.157 -28.100 1.00 31.19  ? 78  ASN B N   1 
ATOM   1343 C  CA  . ASN B 1 79 ? 7.047   -9.290  -29.023 1.00 34.54  ? 78  ASN B CA  1 
ATOM   1344 C  C   . ASN B 1 79 ? 7.750   -7.949  -29.145 1.00 37.42  ? 78  ASN B C   1 
ATOM   1345 O  O   . ASN B 1 79 ? 7.729   -7.338  -30.218 1.00 38.62  ? 78  ASN B O   1 
ATOM   1346 C  CB  . ASN B 1 79 ? 5.590   -9.110  -28.602 1.00 35.55  ? 78  ASN B CB  1 
ATOM   1347 C  CG  . ASN B 1 79 ? 4.823   -10.422 -28.570 1.00 49.55  ? 78  ASN B CG  1 
ATOM   1348 O  OD1 . ASN B 1 79 ? 5.248   -11.429 -29.140 1.00 52.66  ? 78  ASN B OD1 1 
ATOM   1349 N  ND2 . ASN B 1 79 ? 3.685   -10.415 -27.893 1.00 57.65  ? 78  ASN B ND2 1 
ATOM   1350 N  N   . GLU B 1 80 ? 8.396   -7.486  -28.076 1.00 35.58  ? 79  GLU B N   1 
ATOM   1351 C  CA  . GLU B 1 80 ? 9.220   -6.293  -28.209 1.00 38.19  ? 79  GLU B CA  1 
ATOM   1352 C  C   . GLU B 1 80 ? 10.401  -6.551  -29.141 1.00 30.94  ? 79  GLU B C   1 
ATOM   1353 O  O   . GLU B 1 80 ? 10.774  -5.672  -29.930 1.00 26.90  ? 79  GLU B O   1 
ATOM   1354 C  CB  . GLU B 1 80 ? 9.672   -5.810  -26.828 1.00 38.73  ? 79  GLU B CB  1 
ATOM   1355 C  CG  . GLU B 1 80 ? 8.547   -5.095  -26.063 1.00 44.45  ? 79  GLU B CG  1 
ATOM   1356 C  CD  . GLU B 1 80 ? 8.567   -5.339  -24.553 1.00 67.56  ? 79  GLU B CD  1 
ATOM   1357 O  OE1 . GLU B 1 80 ? 9.355   -6.196  -24.095 1.00 74.43  ? 79  GLU B OE1 1 
ATOM   1358 O  OE2 . GLU B 1 80 ? 7.788   -4.678  -23.820 1.00 71.37  ? 79  GLU B OE2 1 
ATOM   1359 N  N   . GLY B 1 81 ? 10.975  -7.762  -29.092 1.00 27.86  ? 80  GLY B N   1 
ATOM   1360 C  CA  . GLY B 1 81 ? 12.069  -8.092  -29.992 1.00 26.34  ? 80  GLY B CA  1 
ATOM   1361 C  C   . GLY B 1 81 ? 11.633  -8.176  -31.442 1.00 25.41  ? 80  GLY B C   1 
ATOM   1362 O  O   . GLY B 1 81 ? 12.386  -7.800  -32.347 1.00 27.17  ? 80  GLY B O   1 
ATOM   1363 N  N   . LEU B 1 82 ? 10.419  -8.678  -31.686 1.00 27.91  ? 81  LEU B N   1 
ATOM   1364 C  CA  . LEU B 1 82 ? 9.875   -8.646  -33.039 1.00 30.33  ? 81  LEU B CA  1 
ATOM   1365 C  C   . LEU B 1 82 ? 9.744   -7.215  -33.541 1.00 30.69  ? 81  LEU B C   1 
ATOM   1366 O  O   . LEU B 1 82 ? 10.069  -6.922  -34.696 1.00 31.30  ? 81  LEU B O   1 
ATOM   1367 C  CB  . LEU B 1 82 ? 8.524   -9.350  -33.081 1.00 31.04  ? 81  LEU B CB  1 
ATOM   1368 C  CG  . LEU B 1 82 ? 8.587   -10.845 -32.780 1.00 29.01  ? 81  LEU B CG  1 
ATOM   1369 C  CD1 . LEU B 1 82 ? 7.200   -11.444 -32.846 1.00 35.52  ? 81  LEU B CD1 1 
ATOM   1370 C  CD2 . LEU B 1 82 ? 9.506   -11.525 -33.791 1.00 31.14  ? 81  LEU B CD2 1 
ATOM   1371 N  N   . TRP B 1 83 ? 9.274   -6.303  -32.682 1.00 28.76  ? 82  TRP B N   1 
ATOM   1372 C  CA  . TRP B 1 83 ? 9.166   -4.904  -33.087 1.00 27.86  ? 82  TRP B CA  1 
ATOM   1373 C  C   . TRP B 1 83 ? 10.529  -4.339  -33.451 1.00 31.67  ? 82  TRP B C   1 
ATOM   1374 O  O   . TRP B 1 83 ? 10.691  -3.702  -34.498 1.00 32.19  ? 82  TRP B O   1 
ATOM   1375 C  CB  . TRP B 1 83 ? 8.532   -4.074  -31.965 1.00 32.94  ? 82  TRP B CB  1 
ATOM   1376 C  CG  . TRP B 1 83 ? 8.284   -2.643  -32.362 1.00 36.45  ? 82  TRP B CG  1 
ATOM   1377 C  CD1 . TRP B 1 83 ? 7.119   -2.117  -32.842 1.00 46.17  ? 82  TRP B CD1 1 
ATOM   1378 C  CD2 . TRP B 1 83 ? 9.226   -1.561  -32.327 1.00 43.27  ? 82  TRP B CD2 1 
ATOM   1379 N  NE1 . TRP B 1 83 ? 7.275   -0.777  -33.100 1.00 48.99  ? 82  TRP B NE1 1 
ATOM   1380 C  CE2 . TRP B 1 83 ? 8.558   -0.411  -32.791 1.00 41.39  ? 82  TRP B CE2 1 
ATOM   1381 C  CE3 . TRP B 1 83 ? 10.568  -1.453  -31.942 1.00 43.00  ? 82  TRP B CE3 1 
ATOM   1382 C  CZ2 . TRP B 1 83 ? 9.187   0.833   -32.894 1.00 47.73  ? 82  TRP B CZ2 1 
ATOM   1383 C  CZ3 . TRP B 1 83 ? 11.195  -0.207  -32.044 1.00 44.72  ? 82  TRP B CZ3 1 
ATOM   1384 C  CH2 . TRP B 1 83 ? 10.500  0.914   -32.514 1.00 47.73  ? 82  TRP B CH2 1 
ATOM   1385 N  N   . GLU B 1 84 ? 11.523  -4.574  -32.593 1.00 26.51  ? 83  GLU B N   1 
ATOM   1386 C  CA  . GLU B 1 84 ? 12.854  -4.007  -32.782 1.00 26.24  ? 83  GLU B CA  1 
ATOM   1387 C  C   . GLU B 1 84 ? 13.498  -4.486  -34.079 1.00 27.68  ? 83  GLU B C   1 
ATOM   1388 O  O   . GLU B 1 84 ? 14.034  -3.682  -34.851 1.00 27.61  ? 83  GLU B O   1 
ATOM   1389 C  CB  . GLU B 1 84 ? 13.729  -4.351  -31.588 1.00 27.92  ? 83  GLU B CB  1 
ATOM   1390 C  CG  . GLU B 1 84 ? 13.216  -3.691  -30.296 1.00 30.86  ? 83  GLU B CG  1 
ATOM   1391 C  CD  . GLU B 1 84 ? 14.094  -3.965  -29.105 1.00 36.83  ? 83  GLU B CD  1 
ATOM   1392 O  OE1 . GLU B 1 84 ? 15.014  -4.804  -29.216 1.00 28.16  ? 83  GLU B OE1 1 
ATOM   1393 O  OE2 . GLU B 1 84 ? 13.854  -3.320  -28.052 1.00 34.38  ? 83  GLU B OE2 1 
ATOM   1394 N  N   . ILE B 1 85 ? 13.462  -5.794  -34.340 1.00 24.28  ? 84  ILE B N   1 
ATOM   1395 C  CA  . ILE B 1 85 ? 14.146  -6.289  -35.536 1.00 26.77  ? 84  ILE B CA  1 
ATOM   1396 C  C   . ILE B 1 85 ? 13.474  -5.759  -36.801 1.00 29.67  ? 84  ILE B C   1 
ATOM   1397 O  O   . ILE B 1 85 ? 14.134  -5.561  -37.833 1.00 28.13  ? 84  ILE B O   1 
ATOM   1398 C  CB  . ILE B 1 85 ? 14.195  -7.832  -35.506 1.00 25.12  ? 84  ILE B CB  1 
ATOM   1399 C  CG1 . ILE B 1 85 ? 15.168  -8.352  -36.578 1.00 24.88  ? 84  ILE B CG1 1 
ATOM   1400 C  CG2 . ILE B 1 85 ? 12.782  -8.411  -35.688 1.00 26.82  ? 84  ILE B CG2 1 
ATOM   1401 C  CD1 . ILE B 1 85 ? 15.646  -9.782  -36.324 1.00 26.27  ? 84  ILE B CD1 1 
ATOM   1402 N  N   . GLN B 1 86 ? 12.166  -5.488  -36.738 1.00 29.87  ? 85  GLN B N   1 
ATOM   1403 C  CA  . GLN B 1 86 ? 11.427  -4.971  -37.887 1.00 37.08  ? 85  GLN B CA  1 
ATOM   1404 C  C   . GLN B 1 86 ? 11.638  -3.474  -38.068 1.00 33.92  ? 85  GLN B C   1 
ATOM   1405 O  O   . GLN B 1 86 ? 11.802  -2.996  -39.199 1.00 35.32  ? 85  GLN B O   1 
ATOM   1406 C  CB  . GLN B 1 86 ? 9.936   -5.257  -37.725 1.00 36.25  ? 85  GLN B CB  1 
ATOM   1407 C  CG  . GLN B 1 86 ? 9.112   -5.006  -38.984 1.00 57.33  ? 85  GLN B CG  1 
ATOM   1408 C  CD  . GLN B 1 86 ? 9.050   -6.220  -39.908 1.00 76.98  ? 85  GLN B CD  1 
ATOM   1409 O  OE1 . GLN B 1 86 ? 10.038  -6.586  -40.557 1.00 69.67  ? 85  GLN B OE1 1 
ATOM   1410 N  NE2 . GLN B 1 86 ? 7.880   -6.851  -39.970 1.00 77.17  ? 85  GLN B NE2 1 
ATOM   1411 N  N   . ASN B 1 87 ? 11.647  -2.725  -36.971 1.00 32.42  ? 86  ASN B N   1 
ATOM   1412 C  CA  . ASN B 1 87 ? 11.549  -1.268  -37.036 1.00 30.18  ? 86  ASN B CA  1 
ATOM   1413 C  C   . ASN B 1 87 ? 12.862  -0.532  -36.816 1.00 31.90  ? 86  ASN B C   1 
ATOM   1414 O  O   . ASN B 1 87 ? 13.042  0.549   -37.385 1.00 31.53  ? 86  ASN B O   1 
ATOM   1415 C  CB  . ASN B 1 87 ? 10.517  -0.749  -36.025 1.00 32.47  ? 86  ASN B CB  1 
ATOM   1416 C  CG  . ASN B 1 87 ? 9.104   -1.079  -36.423 1.00 46.08  ? 86  ASN B CG  1 
ATOM   1417 O  OD1 . ASN B 1 87 ? 8.484   -0.352  -37.202 1.00 47.32  ? 86  ASN B OD1 1 
ATOM   1418 N  ND2 . ASN B 1 87 ? 8.585   -2.189  -35.907 1.00 39.34  ? 86  ASN B ND2 1 
ATOM   1419 N  N   . ASN B 1 88 ? 13.784  -1.048  -36.009 1.00 27.46  ? 87  ASN B N   1 
ATOM   1420 C  CA  . ASN B 1 88 ? 15.103  -0.428  -35.861 1.00 32.06  ? 87  ASN B CA  1 
ATOM   1421 C  C   . ASN B 1 88 ? 16.120  -1.483  -35.458 1.00 26.60  ? 87  ASN B C   1 
ATOM   1422 O  O   . ASN B 1 88 ? 16.687  -1.448  -34.361 1.00 28.08  ? 87  ASN B O   1 
ATOM   1423 C  CB  . ASN B 1 88 ? 15.067  0.720   -34.854 1.00 34.21  ? 87  ASN B CB  1 
ATOM   1424 C  CG  . ASN B 1 88 ? 16.132  1.768   -35.140 1.00 38.04  ? 87  ASN B CG  1 
ATOM   1425 O  OD1 . ASN B 1 88 ? 17.162  1.479   -35.755 1.00 33.49  ? 87  ASN B OD1 1 
ATOM   1426 N  ND2 . ASN B 1 88 ? 15.890  2.999   -34.686 1.00 42.95  ? 87  ASN B ND2 1 
ATOM   1427 N  N   . PRO B 1 89 ? 16.421  -2.416  -36.365 1.00 28.02  ? 88  PRO B N   1 
ATOM   1428 C  CA  . PRO B 1 89 ? 17.347  -3.512  -36.031 1.00 28.14  ? 88  PRO B CA  1 
ATOM   1429 C  C   . PRO B 1 89 ? 18.772  -3.067  -35.744 1.00 26.26  ? 88  PRO B C   1 
ATOM   1430 O  O   . PRO B 1 89 ? 19.490  -3.799  -35.053 1.00 26.00  ? 88  PRO B O   1 
ATOM   1431 C  CB  . PRO B 1 89 ? 17.288  -4.408  -37.281 1.00 31.74  ? 88  PRO B CB  1 
ATOM   1432 C  CG  . PRO B 1 89 ? 16.874  -3.485  -38.392 1.00 26.42  ? 88  PRO B CG  1 
ATOM   1433 C  CD  . PRO B 1 89 ? 15.911  -2.514  -37.745 1.00 28.40  ? 88  PRO B CD  1 
ATOM   1434 N  N   . HIS B 1 90 ? 19.232  -1.909  -36.250 1.00 22.93  ? 89  HIS B N   1 
ATOM   1435 C  CA  . HIS B 1 90 ? 20.642  -1.560  -36.104 1.00 22.93  ? 89  HIS B CA  1 
ATOM   1436 C  C   . HIS B 1 90 ? 20.875  -0.460  -35.078 1.00 26.27  ? 89  HIS B C   1 
ATOM   1437 O  O   . HIS B 1 90 ? 22.008  0.010   -34.935 1.00 26.59  ? 89  HIS B O   1 
ATOM   1438 C  CB  . HIS B 1 90 ? 21.222  -1.140  -37.453 1.00 26.23  ? 89  HIS B CB  1 
ATOM   1439 C  CG  . HIS B 1 90 ? 21.007  -2.164  -38.522 1.00 27.51  ? 89  HIS B CG  1 
ATOM   1440 N  ND1 . HIS B 1 90 ? 21.490  -3.452  -38.413 1.00 29.23  ? 89  HIS B ND1 1 
ATOM   1441 C  CD2 . HIS B 1 90 ? 20.326  -2.112  -39.691 1.00 24.93  ? 89  HIS B CD2 1 
ATOM   1442 C  CE1 . HIS B 1 90 ? 21.148  -4.139  -39.486 1.00 26.21  ? 89  HIS B CE1 1 
ATOM   1443 N  NE2 . HIS B 1 90 ? 20.422  -3.359  -40.266 1.00 28.06  ? 89  HIS B NE2 1 
ATOM   1444 N  N   . ALA B 1 91 ? 19.850  -0.102  -34.314 1.00 26.27  ? 90  ALA B N   1 
ATOM   1445 C  CA  . ALA B 1 91 ? 19.974  0.942   -33.310 1.00 29.50  ? 90  ALA B CA  1 
ATOM   1446 C  C   . ALA B 1 91 ? 20.893  0.507   -32.172 1.00 35.15  ? 90  ALA B C   1 
ATOM   1447 O  O   . ALA B 1 91 ? 21.159  -0.682  -31.950 1.00 33.84  ? 90  ALA B O   1 
ATOM   1448 C  CB  . ALA B 1 91 ? 18.598  1.302   -32.753 1.00 29.31  ? 90  ALA B CB  1 
ATOM   1449 N  N   . SER B 1 92 ? 21.389  1.496   -31.440 1.00 35.08  ? 91  SER B N   1 
ATOM   1450 C  CA  . SER B 1 92 ? 22.017  1.213   -30.162 1.00 37.03  ? 91  SER B CA  1 
ATOM   1451 C  C   . SER B 1 92 ? 20.927  1.008   -29.119 1.00 43.75  ? 91  SER B C   1 
ATOM   1452 O  O   . SER B 1 92 ? 20.007  1.828   -29.002 1.00 41.38  ? 91  SER B O   1 
ATOM   1453 C  CB  . SER B 1 92 ? 22.940  2.355   -29.738 1.00 53.47  ? 91  SER B CB  1 
ATOM   1454 O  OG  . SER B 1 92 ? 22.987  2.414   -28.323 1.00 59.36  ? 91  SER B OG  1 
ATOM   1455 N  N   . TYR B 1 93 ? 21.021  -0.104  -28.388 1.00 39.23  ? 92  TYR B N   1 
ATOM   1456 C  CA  . TYR B 1 93 ? 20.108  -0.433  -27.306 1.00 49.03  ? 92  TYR B CA  1 
ATOM   1457 C  C   . TYR B 1 93 ? 20.793  -0.420  -25.948 1.00 58.26  ? 92  TYR B C   1 
ATOM   1458 O  O   . TYR B 1 93 ? 20.110  -0.539  -24.922 1.00 56.58  ? 92  TYR B O   1 
ATOM   1459 C  CB  . TYR B 1 93 ? 19.456  -1.806  -27.565 1.00 39.82  ? 92  TYR B CB  1 
ATOM   1460 C  CG  . TYR B 1 93 ? 18.474  -1.748  -28.709 1.00 32.70  ? 92  TYR B CG  1 
ATOM   1461 C  CD1 . TYR B 1 93 ? 17.193  -1.280  -28.514 1.00 28.80  ? 92  TYR B CD1 1 
ATOM   1462 C  CD2 . TYR B 1 93 ? 18.837  -2.147  -30.000 1.00 30.81  ? 92  TYR B CD2 1 
ATOM   1463 C  CE1 . TYR B 1 93 ? 16.287  -1.184  -29.553 1.00 33.09  ? 92  TYR B CE1 1 
ATOM   1464 C  CE2 . TYR B 1 93 ? 17.921  -2.083  -31.051 1.00 28.28  ? 92  TYR B CE2 1 
ATOM   1465 C  CZ  . TYR B 1 93 ? 16.651  -1.600  -30.819 1.00 30.42  ? 92  TYR B CZ  1 
ATOM   1466 O  OH  . TYR B 1 93 ? 15.730  -1.501  -31.833 1.00 32.61  ? 92  TYR B OH  1 
ATOM   1467 N  N   . SER B 1 94 ? 22.116  -0.266  -25.923 1.00 60.47  ? 93  SER B N   1 
ATOM   1468 C  CA  . SER B 1 94 ? 22.876  -0.078  -24.698 1.00 74.23  ? 93  SER B CA  1 
ATOM   1469 C  C   . SER B 1 94 ? 22.680  1.351   -24.184 1.00 78.49  ? 93  SER B C   1 
ATOM   1470 O  O   . SER B 1 94 ? 22.803  2.329   -24.933 1.00 67.65  ? 93  SER B O   1 
ATOM   1471 C  CB  . SER B 1 94 ? 24.366  -0.378  -24.934 1.00 65.23  ? 93  SER B CB  1 
ATOM   1472 O  OG  . SER B 1 94 ? 24.872  0.313   -26.068 1.00 60.45  ? 93  SER B OG  1 
ATOM   1473 O  OXT . SER B 1 94 ? 22.383  1.557   -23.003 1.00 80.31  ? 93  SER B OXT 1 
ATOM   1474 N  N   . HIS C 1 4  ? 32.011  -22.981 27.205  1.00 82.52  ? 3   HIS C N   1 
ATOM   1475 C  CA  . HIS C 1 4  ? 31.002  -22.171 27.884  1.00 79.37  ? 3   HIS C CA  1 
ATOM   1476 C  C   . HIS C 1 4  ? 29.845  -23.052 28.347  1.00 77.17  ? 3   HIS C C   1 
ATOM   1477 O  O   . HIS C 1 4  ? 28.909  -23.309 27.584  1.00 79.25  ? 3   HIS C O   1 
ATOM   1478 C  CB  . HIS C 1 4  ? 30.492  -21.062 26.956  1.00 87.50  ? 3   HIS C CB  1 
ATOM   1479 C  CG  . HIS C 1 4  ? 29.705  -19.989 27.652  1.00 87.31  ? 3   HIS C CG  1 
ATOM   1480 N  ND1 . HIS C 1 4  ? 28.646  -20.262 28.498  1.00 79.41  ? 3   HIS C ND1 1 
ATOM   1481 C  CD2 . HIS C 1 4  ? 29.810  -18.638 27.605  1.00 63.88  ? 3   HIS C CD2 1 
ATOM   1482 C  CE1 . HIS C 1 4  ? 28.143  -19.126 28.948  1.00 71.73  ? 3   HIS C CE1 1 
ATOM   1483 N  NE2 . HIS C 1 4  ? 28.827  -18.126 28.418  1.00 64.73  ? 3   HIS C NE2 1 
ATOM   1484 N  N   . ALA C 1 5  ? 29.913  -23.508 29.598  1.00 73.96  ? 4   ALA C N   1 
ATOM   1485 C  CA  . ALA C 1 5  ? 28.886  -24.398 30.126  1.00 76.57  ? 4   ALA C CA  1 
ATOM   1486 C  C   . ALA C 1 5  ? 27.518  -23.725 30.082  1.00 69.32  ? 4   ALA C C   1 
ATOM   1487 O  O   . ALA C 1 5  ? 27.367  -22.551 30.432  1.00 75.28  ? 4   ALA C O   1 
ATOM   1488 C  CB  . ALA C 1 5  ? 29.224  -24.826 31.558  1.00 64.27  ? 4   ALA C CB  1 
ATOM   1489 N  N   . PHE C 1 6  ? 26.521  -24.479 29.641  1.00 71.22  ? 5   PHE C N   1 
ATOM   1490 C  CA  . PHE C 1 6  ? 25.188  -23.956 29.401  1.00 66.35  ? 5   PHE C CA  1 
ATOM   1491 C  C   . PHE C 1 6  ? 24.299  -24.163 30.626  1.00 74.73  ? 5   PHE C C   1 
ATOM   1492 O  O   . PHE C 1 6  ? 24.544  -25.039 31.462  1.00 72.24  ? 5   PHE C O   1 
ATOM   1493 C  CB  . PHE C 1 6  ? 24.569  -24.632 28.173  1.00 68.03  ? 5   PHE C CB  1 
ATOM   1494 C  CG  . PHE C 1 6  ? 25.480  -24.681 26.966  1.00 56.25  ? 5   PHE C CG  1 
ATOM   1495 C  CD1 . PHE C 1 6  ? 25.494  -23.645 26.044  1.00 70.89  ? 5   PHE C CD1 1 
ATOM   1496 C  CD2 . PHE C 1 6  ? 26.299  -25.776 26.738  1.00 62.55  ? 5   PHE C CD2 1 
ATOM   1497 C  CE1 . PHE C 1 6  ? 26.320  -23.695 24.924  1.00 66.31  ? 5   PHE C CE1 1 
ATOM   1498 C  CE2 . PHE C 1 6  ? 27.127  -25.831 25.622  1.00 55.77  ? 5   PHE C CE2 1 
ATOM   1499 C  CZ  . PHE C 1 6  ? 27.136  -24.790 24.715  1.00 50.15  ? 5   PHE C CZ  1 
ATOM   1500 N  N   . LYS C 1 7  ? 23.258  -23.339 30.723  1.00 68.66  ? 6   LYS C N   1 
ATOM   1501 C  CA  . LYS C 1 7  ? 22.263  -23.398 31.784  1.00 72.16  ? 6   LYS C CA  1 
ATOM   1502 C  C   . LYS C 1 7  ? 20.882  -23.665 31.192  1.00 71.45  ? 6   LYS C C   1 
ATOM   1503 O  O   . LYS C 1 7  ? 20.642  -23.376 30.014  1.00 66.22  ? 6   LYS C O   1 
ATOM   1504 C  CB  . LYS C 1 7  ? 22.247  -22.086 32.579  1.00 60.41  ? 6   LYS C CB  1 
ATOM   1505 C  CG  . LYS C 1 7  ? 22.725  -20.906 31.761  1.00 69.91  ? 6   LYS C CG  1 
ATOM   1506 C  CD  . LYS C 1 7  ? 22.402  -19.587 32.423  1.00 68.51  ? 6   LYS C CD  1 
ATOM   1507 C  CE  . LYS C 1 7  ? 22.670  -18.441 31.469  1.00 65.04  ? 6   LYS C CE  1 
ATOM   1508 N  NZ  . LYS C 1 7  ? 21.971  -18.638 30.163  1.00 75.18  ? 6   LYS C NZ  1 
ATOM   1509 N  N   . PRO C 1 8  ? 19.937  -24.243 31.987  1.00 74.12  ? 7   PRO C N   1 
ATOM   1510 C  CA  . PRO C 1 8  ? 18.600  -24.553 31.445  1.00 73.08  ? 7   PRO C CA  1 
ATOM   1511 C  C   . PRO C 1 8  ? 17.945  -23.364 30.747  1.00 69.23  ? 7   PRO C C   1 
ATOM   1512 O  O   . PRO C 1 8  ? 17.819  -22.288 31.337  1.00 71.75  ? 7   PRO C O   1 
ATOM   1513 C  CB  . PRO C 1 8  ? 17.808  -24.971 32.689  1.00 62.38  ? 7   PRO C CB  1 
ATOM   1514 C  CG  . PRO C 1 8  ? 18.828  -25.492 33.622  1.00 63.59  ? 7   PRO C CG  1 
ATOM   1515 C  CD  . PRO C 1 8  ? 20.076  -24.682 33.388  1.00 70.45  ? 7   PRO C CD  1 
ATOM   1516 N  N   . GLY C 1 9  ? 17.544  -23.543 29.486  1.00 61.11  ? 8   GLY C N   1 
ATOM   1517 C  CA  . GLY C 1 9  ? 16.980  -22.482 28.677  1.00 58.69  ? 8   GLY C CA  1 
ATOM   1518 C  C   . GLY C 1 9  ? 17.850  -22.038 27.516  1.00 59.03  ? 8   GLY C C   1 
ATOM   1519 O  O   . GLY C 1 9  ? 17.320  -21.471 26.550  1.00 64.41  ? 8   GLY C O   1 
ATOM   1520 N  N   . ASP C 1 10 ? 19.163  -22.269 27.578  1.00 58.03  ? 9   ASP C N   1 
ATOM   1521 C  CA  . ASP C 1 10 ? 20.052  -21.864 26.493  1.00 47.84  ? 9   ASP C CA  1 
ATOM   1522 C  C   . ASP C 1 10 ? 19.745  -22.645 25.221  1.00 56.36  ? 9   ASP C C   1 
ATOM   1523 O  O   . ASP C 1 10 ? 19.432  -23.838 25.267  1.00 48.09  ? 9   ASP C O   1 
ATOM   1524 C  CB  . ASP C 1 10 ? 21.520  -22.080 26.867  1.00 49.87  ? 9   ASP C CB  1 
ATOM   1525 C  CG  . ASP C 1 10 ? 21.914  -21.372 28.142  1.00 64.64  ? 9   ASP C CG  1 
ATOM   1526 O  OD1 . ASP C 1 10 ? 21.232  -20.393 28.519  1.00 70.47  ? 9   ASP C OD1 1 
ATOM   1527 O  OD2 . ASP C 1 10 ? 22.912  -21.804 28.764  1.00 53.87  ? 9   ASP C OD2 1 
ATOM   1528 N  N   . LEU C 1 11 ? 19.879  -21.969 24.083  1.00 51.09  ? 10  LEU C N   1 
ATOM   1529 C  CA  . LEU C 1 11 ? 19.547  -22.514 22.771  1.00 53.77  ? 10  LEU C CA  1 
ATOM   1530 C  C   . LEU C 1 11 ? 20.811  -22.961 22.044  1.00 47.91  ? 10  LEU C C   1 
ATOM   1531 O  O   . LEU C 1 11 ? 21.793  -22.214 21.982  1.00 45.50  ? 10  LEU C O   1 
ATOM   1532 C  CB  . LEU C 1 11 ? 18.815  -21.466 21.932  1.00 51.30  ? 10  LEU C CB  1 
ATOM   1533 C  CG  . LEU C 1 11 ? 17.614  -20.787 22.585  1.00 45.16  ? 10  LEU C CG  1 
ATOM   1534 C  CD1 . LEU C 1 11 ? 17.058  -19.770 21.606  1.00 55.03  ? 10  LEU C CD1 1 
ATOM   1535 C  CD2 . LEU C 1 11 ? 16.549  -21.797 23.011  1.00 40.22  ? 10  LEU C CD2 1 
ATOM   1536 N  N   . VAL C 1 12 ? 20.770  -24.167 21.461  1.00 39.73  ? 11  VAL C N   1 
ATOM   1537 C  CA  . VAL C 1 12 ? 21.920  -24.761 20.783  1.00 47.08  ? 11  VAL C CA  1 
ATOM   1538 C  C   . VAL C 1 12 ? 21.455  -25.521 19.543  1.00 35.56  ? 11  VAL C C   1 
ATOM   1539 O  O   . VAL C 1 12 ? 20.261  -25.714 19.307  1.00 34.52  ? 11  VAL C O   1 
ATOM   1540 C  CB  . VAL C 1 12 ? 22.705  -25.727 21.704  1.00 45.81  ? 11  VAL C CB  1 
ATOM   1541 C  CG1 . VAL C 1 12 ? 23.475  -24.958 22.782  1.00 46.93  ? 11  VAL C CG1 1 
ATOM   1542 C  CG2 . VAL C 1 12 ? 21.759  -26.767 22.315  1.00 35.79  ? 11  VAL C CG2 1 
ATOM   1543 N  N   . PHE C 1 13 ? 22.427  -25.945 18.740  1.00 35.12  ? 12  PHE C N   1 
ATOM   1544 C  CA  . PHE C 1 13 ? 22.272  -27.127 17.899  1.00 33.35  ? 12  PHE C CA  1 
ATOM   1545 C  C   . PHE C 1 13 ? 22.930  -28.292 18.629  1.00 37.66  ? 12  PHE C C   1 
ATOM   1546 O  O   . PHE C 1 13 ? 24.044  -28.151 19.147  1.00 38.21  ? 12  PHE C O   1 
ATOM   1547 C  CB  . PHE C 1 13 ? 22.891  -26.928 16.508  1.00 35.67  ? 12  PHE C CB  1 
ATOM   1548 C  CG  . PHE C 1 13 ? 22.164  -25.911 15.665  1.00 36.44  ? 12  PHE C CG  1 
ATOM   1549 C  CD1 . PHE C 1 13 ? 22.488  -24.565 15.746  1.00 48.54  ? 12  PHE C CD1 1 
ATOM   1550 C  CD2 . PHE C 1 13 ? 21.141  -26.299 14.811  1.00 37.14  ? 12  PHE C CD2 1 
ATOM   1551 C  CE1 . PHE C 1 13 ? 21.804  -23.624 14.980  1.00 39.76  ? 12  PHE C CE1 1 
ATOM   1552 C  CE2 . PHE C 1 13 ? 20.462  -25.367 14.045  1.00 42.75  ? 12  PHE C CE2 1 
ATOM   1553 C  CZ  . PHE C 1 13 ? 20.797  -24.027 14.131  1.00 37.73  ? 12  PHE C CZ  1 
ATOM   1554 N  N   . ALA C 1 14 ? 22.226  -29.418 18.714  1.00 25.34  ? 13  ALA C N   1 
ATOM   1555 C  CA  . ALA C 1 14 ? 22.721  -30.582 19.430  1.00 25.51  ? 13  ALA C CA  1 
ATOM   1556 C  C   . ALA C 1 14 ? 22.905  -31.718 18.438  1.00 27.21  ? 13  ALA C C   1 
ATOM   1557 O  O   . ALA C 1 14 ? 22.017  -31.975 17.618  1.00 26.77  ? 13  ALA C O   1 
ATOM   1558 C  CB  . ALA C 1 14 ? 21.752  -31.002 20.552  1.00 26.42  ? 13  ALA C CB  1 
ATOM   1559 N  N   . LYS C 1 15 ? 24.050  -32.385 18.506  1.00 31.03  ? 14  LYS C N   1 
ATOM   1560 C  CA  . LYS C 1 15 ? 24.389  -33.441 17.555  1.00 31.41  ? 14  LYS C CA  1 
ATOM   1561 C  C   . LYS C 1 15 ? 24.320  -34.790 18.253  1.00 32.70  ? 14  LYS C C   1 
ATOM   1562 O  O   . LYS C 1 15 ? 25.127  -35.077 19.144  1.00 36.98  ? 14  LYS C O   1 
ATOM   1563 C  CB  . LYS C 1 15 ? 25.778  -33.215 16.969  1.00 30.57  ? 14  LYS C CB  1 
ATOM   1564 C  CG  . LYS C 1 15 ? 26.178  -34.269 15.962  1.00 39.92  ? 14  LYS C CG  1 
ATOM   1565 C  CD  . LYS C 1 15 ? 25.426  -34.063 14.651  1.00 35.61  ? 14  LYS C CD  1 
ATOM   1566 C  CE  . LYS C 1 15 ? 25.964  -34.992 13.582  1.00 38.54  ? 14  LYS C CE  1 
ATOM   1567 N  NZ  . LYS C 1 15 ? 25.631  -36.402 13.929  1.00 31.42  ? 14  LYS C NZ  1 
ATOM   1568 N  N   . MET C 1 16 ? 23.364  -35.618 17.851  1.00 28.68  ? 15  MET C N   1 
ATOM   1569 C  CA  . MET C 1 16 ? 23.321  -37.003 18.280  1.00 27.33  ? 15  MET C CA  1 
ATOM   1570 C  C   . MET C 1 16 ? 23.693  -37.902 17.115  1.00 36.78  ? 15  MET C C   1 
ATOM   1571 O  O   . MET C 1 16 ? 23.396  -37.597 15.952  1.00 30.83  ? 15  MET C O   1 
ATOM   1572 C  CB  . MET C 1 16 ? 21.943  -37.398 18.777  1.00 31.18  ? 15  MET C CB  1 
ATOM   1573 C  CG  . MET C 1 16 ? 21.492  -36.614 19.970  1.00 52.93  ? 15  MET C CG  1 
ATOM   1574 S  SD  . MET C 1 16 ? 20.295  -37.545 20.926  1.00 53.02  ? 15  MET C SD  1 
ATOM   1575 C  CE  . MET C 1 16 ? 19.755  -38.786 19.764  1.00 42.59  ? 15  MET C CE  1 
ATOM   1576 N  N   . LYS C 1 17 ? 24.325  -39.024 17.439  1.00 27.97  ? 16  LYS C N   1 
ATOM   1577 C  CA  . LYS C 1 17 ? 24.688  -39.966 16.390  1.00 32.07  ? 16  LYS C CA  1 
ATOM   1578 C  C   . LYS C 1 17 ? 23.443  -40.423 15.630  1.00 28.15  ? 16  LYS C C   1 
ATOM   1579 O  O   . LYS C 1 17 ? 22.423  -40.781 16.232  1.00 29.63  ? 16  LYS C O   1 
ATOM   1580 C  CB  . LYS C 1 17 ? 25.418  -41.171 16.994  1.00 32.61  ? 16  LYS C CB  1 
ATOM   1581 C  CG  . LYS C 1 17 ? 26.079  -42.064 15.931  1.00 37.20  ? 16  LYS C CG  1 
ATOM   1582 C  CD  . LYS C 1 17 ? 27.281  -41.359 15.304  1.00 34.66  ? 16  LYS C CD  1 
ATOM   1583 C  CE  . LYS C 1 17 ? 28.021  -42.277 14.308  1.00 48.07  ? 16  LYS C CE  1 
ATOM   1584 N  NZ  . LYS C 1 17 ? 29.294  -41.635 13.850  1.00 45.55  ? 16  LYS C NZ  1 
ATOM   1585 N  N   . GLY C 1 18 ? 23.532  -40.383 14.297  1.00 33.68  ? 17  GLY C N   1 
ATOM   1586 C  CA  . GLY C 1 18 ? 22.446  -40.758 13.415  1.00 32.71  ? 17  GLY C CA  1 
ATOM   1587 C  C   . GLY C 1 18 ? 21.528  -39.626 13.001  1.00 33.99  ? 17  GLY C C   1 
ATOM   1588 O  O   . GLY C 1 18 ? 20.550  -39.873 12.279  1.00 32.85  ? 17  GLY C O   1 
ATOM   1589 N  N   . TYR C 1 19 ? 21.793  -38.403 13.446  1.00 28.36  ? 18  TYR C N   1 
ATOM   1590 C  CA  . TYR C 1 19 ? 20.946  -37.250 13.163  1.00 35.95  ? 18  TYR C CA  1 
ATOM   1591 C  C   . TYR C 1 19 ? 21.795  -36.039 12.818  1.00 31.41  ? 18  TYR C C   1 
ATOM   1592 O  O   . TYR C 1 19 ? 22.941  -35.931 13.271  1.00 32.95  ? 18  TYR C O   1 
ATOM   1593 C  CB  . TYR C 1 19 ? 20.059  -36.918 14.373  1.00 34.78  ? 18  TYR C CB  1 
ATOM   1594 C  CG  . TYR C 1 19 ? 19.127  -38.040 14.725  1.00 32.76  ? 18  TYR C CG  1 
ATOM   1595 C  CD1 . TYR C 1 19 ? 17.862  -38.108 14.163  1.00 35.86  ? 18  TYR C CD1 1 
ATOM   1596 C  CD2 . TYR C 1 19 ? 19.503  -39.032 15.633  1.00 36.05  ? 18  TYR C CD2 1 
ATOM   1597 C  CE1 . TYR C 1 19 ? 16.996  -39.125 14.481  1.00 49.05  ? 18  TYR C CE1 1 
ATOM   1598 C  CE2 . TYR C 1 19 ? 18.642  -40.063 15.954  1.00 39.26  ? 18  TYR C CE2 1 
ATOM   1599 C  CZ  . TYR C 1 19 ? 17.384  -40.097 15.374  1.00 53.92  ? 18  TYR C CZ  1 
ATOM   1600 O  OH  . TYR C 1 19 ? 16.493  -41.101 15.668  1.00 57.59  ? 18  TYR C OH  1 
ATOM   1601 N  N   . PRO C 1 20 ? 21.264  -35.110 12.021  1.00 33.37  ? 19  PRO C N   1 
ATOM   1602 C  CA  . PRO C 1 20 ? 21.986  -33.865 11.745  1.00 33.00  ? 19  PRO C CA  1 
ATOM   1603 C  C   . PRO C 1 20 ? 21.953  -32.950 12.959  1.00 32.23  ? 19  PRO C C   1 
ATOM   1604 O  O   . PRO C 1 20 ? 21.199  -33.168 13.908  1.00 32.07  ? 19  PRO C O   1 
ATOM   1605 C  CB  . PRO C 1 20 ? 21.205  -33.269 10.571  1.00 38.30  ? 19  PRO C CB  1 
ATOM   1606 C  CG  . PRO C 1 20 ? 19.803  -33.734 10.821  1.00 30.74  ? 19  PRO C CG  1 
ATOM   1607 C  CD  . PRO C 1 20 ? 19.933  -35.126 11.384  1.00 37.44  ? 19  PRO C CD  1 
ATOM   1608 N  N   . HIS C 1 21 ? 22.793  -31.914 12.926  1.00 34.20  ? 20  HIS C N   1 
ATOM   1609 C  CA  . HIS C 1 21 ? 22.809  -30.951 14.022  1.00 33.62  ? 20  HIS C CA  1 
ATOM   1610 C  C   . HIS C 1 21 ? 21.413  -30.360 14.184  1.00 34.64  ? 20  HIS C C   1 
ATOM   1611 O  O   . HIS C 1 21 ? 20.837  -29.836 13.224  1.00 33.24  ? 20  HIS C O   1 
ATOM   1612 C  CB  . HIS C 1 21 ? 23.845  -29.857 13.764  1.00 39.21  ? 20  HIS C CB  1 
ATOM   1613 C  CG  . HIS C 1 21 ? 25.261  -30.356 13.735  1.00 42.76  ? 20  HIS C CG  1 
ATOM   1614 N  ND1 . HIS C 1 21 ? 25.774  -31.089 12.683  1.00 42.45  ? 20  HIS C ND1 1 
ATOM   1615 C  CD2 . HIS C 1 21 ? 26.272  -30.222 14.627  1.00 46.04  ? 20  HIS C CD2 1 
ATOM   1616 C  CE1 . HIS C 1 21 ? 27.037  -31.388 12.933  1.00 42.48  ? 20  HIS C CE1 1 
ATOM   1617 N  NE2 . HIS C 1 21 ? 27.364  -30.873 14.105  1.00 45.82  ? 20  HIS C NE2 1 
ATOM   1618 N  N   . TRP C 1 22 ? 20.856  -30.465 15.389  1.00 28.72  ? 21  TRP C N   1 
ATOM   1619 C  CA  . TRP C 1 22 ? 19.419  -30.300 15.576  1.00 27.25  ? 21  TRP C CA  1 
ATOM   1620 C  C   . TRP C 1 22 ? 19.119  -29.107 16.479  1.00 25.19  ? 21  TRP C C   1 
ATOM   1621 O  O   . TRP C 1 22 ? 19.725  -28.994 17.553  1.00 26.62  ? 21  TRP C O   1 
ATOM   1622 C  CB  . TRP C 1 22 ? 18.823  -31.569 16.205  1.00 25.67  ? 21  TRP C CB  1 
ATOM   1623 C  CG  . TRP C 1 22 ? 17.363  -31.736 15.959  1.00 28.31  ? 21  TRP C CG  1 
ATOM   1624 C  CD1 . TRP C 1 22 ? 16.329  -31.098 16.599  1.00 27.14  ? 21  TRP C CD1 1 
ATOM   1625 C  CD2 . TRP C 1 22 ? 16.769  -32.599 14.996  1.00 33.53  ? 21  TRP C CD2 1 
ATOM   1626 N  NE1 . TRP C 1 22 ? 15.125  -31.532 16.088  1.00 27.65  ? 21  TRP C NE1 1 
ATOM   1627 C  CE2 . TRP C 1 22 ? 15.370  -32.459 15.112  1.00 30.19  ? 21  TRP C CE2 1 
ATOM   1628 C  CE3 . TRP C 1 22 ? 17.285  -33.489 14.049  1.00 32.81  ? 21  TRP C CE3 1 
ATOM   1629 C  CZ2 . TRP C 1 22 ? 14.483  -33.170 14.304  1.00 34.74  ? 21  TRP C CZ2 1 
ATOM   1630 C  CZ3 . TRP C 1 22 ? 16.405  -34.194 13.254  1.00 32.93  ? 21  TRP C CZ3 1 
ATOM   1631 C  CH2 . TRP C 1 22 ? 15.020  -34.035 13.391  1.00 32.47  ? 21  TRP C CH2 1 
ATOM   1632 N  N   . PRO C 1 23 ? 18.179  -28.232 16.116  1.00 27.57  ? 22  PRO C N   1 
ATOM   1633 C  CA  . PRO C 1 23 ? 17.863  -27.097 16.996  1.00 30.05  ? 22  PRO C CA  1 
ATOM   1634 C  C   . PRO C 1 23 ? 17.355  -27.599 18.342  1.00 29.17  ? 22  PRO C C   1 
ATOM   1635 O  O   . PRO C 1 23 ? 16.417  -28.399 18.414  1.00 27.33  ? 22  PRO C O   1 
ATOM   1636 C  CB  . PRO C 1 23 ? 16.781  -26.331 16.219  1.00 25.21  ? 22  PRO C CB  1 
ATOM   1637 C  CG  . PRO C 1 23 ? 16.201  -27.344 15.264  1.00 31.20  ? 22  PRO C CG  1 
ATOM   1638 C  CD  . PRO C 1 23 ? 17.368  -28.213 14.884  1.00 28.88  ? 22  PRO C CD  1 
ATOM   1639 N  N   . ALA C 1 24 ? 17.991  -27.127 19.415  1.00 30.28  ? 23  ALA C N   1 
ATOM   1640 C  CA  . ALA C 1 24 ? 17.708  -27.657 20.737  1.00 31.94  ? 23  ALA C CA  1 
ATOM   1641 C  C   . ALA C 1 24 ? 17.934  -26.585 21.790  1.00 38.17  ? 23  ALA C C   1 
ATOM   1642 O  O   . ALA C 1 24 ? 18.428  -25.493 21.507  1.00 33.24  ? 23  ALA C O   1 
ATOM   1643 C  CB  . ALA C 1 24 ? 18.580  -28.874 21.049  1.00 33.67  ? 23  ALA C CB  1 
ATOM   1644 N  N   . ARG C 1 25 ? 17.571  -26.933 23.023  1.00 46.10  ? 24  ARG C N   1 
ATOM   1645 C  CA  . ARG C 1 25 ? 17.859  -26.099 24.176  1.00 45.74  ? 24  ARG C CA  1 
ATOM   1646 C  C   . ARG C 1 25 ? 18.106  -26.988 25.386  1.00 40.12  ? 24  ARG C C   1 
ATOM   1647 O  O   . ARG C 1 25 ? 17.702  -28.157 25.423  1.00 41.88  ? 24  ARG C O   1 
ATOM   1648 C  CB  . ARG C 1 25 ? 16.720  -25.117 24.467  1.00 44.12  ? 24  ARG C CB  1 
ATOM   1649 C  CG  . ARG C 1 25 ? 15.412  -25.782 24.814  1.00 48.15  ? 24  ARG C CG  1 
ATOM   1650 C  CD  . ARG C 1 25 ? 14.735  -25.046 25.955  1.00 58.60  ? 24  ARG C CD  1 
ATOM   1651 N  NE  . ARG C 1 25 ? 13.399  -25.573 26.208  1.00 65.15  ? 24  ARG C NE  1 
ATOM   1652 C  CZ  . ARG C 1 25 ? 12.294  -24.848 26.140  1.00 67.41  ? 24  ARG C CZ  1 
ATOM   1653 N  NH1 . ARG C 1 25 ? 12.338  -23.553 25.882  1.00 56.70  ? 24  ARG C NH1 1 
ATOM   1654 N  NH2 . ARG C 1 25 ? 11.117  -25.436 26.339  1.00 70.42  ? 24  ARG C NH2 1 
ATOM   1655 N  N   . ILE C 1 26 ? 18.759  -26.401 26.385  1.00 48.27  ? 25  ILE C N   1 
ATOM   1656 C  CA  . ILE C 1 26 ? 19.046  -27.082 27.643  1.00 58.59  ? 25  ILE C CA  1 
ATOM   1657 C  C   . ILE C 1 26 ? 17.772  -27.185 28.476  1.00 59.27  ? 25  ILE C C   1 
ATOM   1658 O  O   . ILE C 1 26 ? 17.080  -26.186 28.712  1.00 56.24  ? 25  ILE C O   1 
ATOM   1659 C  CB  . ILE C 1 26 ? 20.146  -26.338 28.415  1.00 55.47  ? 25  ILE C CB  1 
ATOM   1660 C  CG1 . ILE C 1 26 ? 21.227  -25.829 27.456  1.00 49.76  ? 25  ILE C CG1 1 
ATOM   1661 C  CG2 . ILE C 1 26 ? 20.755  -27.245 29.471  1.00 58.78  ? 25  ILE C CG2 1 
ATOM   1662 C  CD1 . ILE C 1 26 ? 22.179  -26.902 26.970  1.00 55.80  ? 25  ILE C CD1 1 
ATOM   1663 N  N   . ASP C 1 27 ? 17.464  -28.395 28.933  1.00 64.83  ? 26  ASP C N   1 
ATOM   1664 C  CA  . ASP C 1 27 ? 16.298  -28.627 29.779  1.00 68.48  ? 26  ASP C CA  1 
ATOM   1665 C  C   . ASP C 1 27 ? 16.620  -28.338 31.246  1.00 75.60  ? 26  ASP C C   1 
ATOM   1666 O  O   . ASP C 1 27 ? 17.756  -28.005 31.592  1.00 77.93  ? 26  ASP C O   1 
ATOM   1667 C  CB  . ASP C 1 27 ? 15.797  -30.067 29.621  1.00 63.86  ? 26  ASP C CB  1 
ATOM   1668 N  N   . PRO C 1 36 ? 21.118  -37.800 35.587  1.00 75.37  ? 35  PRO C N   1 
ATOM   1669 C  CA  . PRO C 1 36 ? 21.990  -37.099 34.636  1.00 70.42  ? 35  PRO C CA  1 
ATOM   1670 C  C   . PRO C 1 36 ? 23.406  -37.670 34.630  1.00 80.49  ? 35  PRO C C   1 
ATOM   1671 O  O   . PRO C 1 36 ? 24.148  -37.437 35.584  1.00 81.27  ? 35  PRO C O   1 
ATOM   1672 C  CB  . PRO C 1 36 ? 21.979  -35.653 35.143  1.00 66.59  ? 35  PRO C CB  1 
ATOM   1673 C  CG  . PRO C 1 36 ? 21.593  -35.755 36.587  1.00 74.91  ? 35  PRO C CG  1 
ATOM   1674 C  CD  . PRO C 1 36 ? 20.665  -36.924 36.679  1.00 74.44  ? 35  PRO C CD  1 
ATOM   1675 N  N   . PRO C 1 37 ? 23.764  -38.407 33.576  1.00 78.19  ? 36  PRO C N   1 
ATOM   1676 C  CA  . PRO C 1 37 ? 25.087  -39.033 33.535  1.00 69.58  ? 36  PRO C CA  1 
ATOM   1677 C  C   . PRO C 1 37 ? 26.180  -37.995 33.677  1.00 64.07  ? 36  PRO C C   1 
ATOM   1678 O  O   . PRO C 1 37 ? 25.964  -36.799 33.409  1.00 60.02  ? 36  PRO C O   1 
ATOM   1679 C  CB  . PRO C 1 37 ? 25.118  -39.701 32.153  1.00 61.96  ? 36  PRO C CB  1 
ATOM   1680 C  CG  . PRO C 1 37 ? 23.684  -39.960 31.838  1.00 65.24  ? 36  PRO C CG  1 
ATOM   1681 C  CD  . PRO C 1 37 ? 22.920  -38.818 32.438  1.00 73.17  ? 36  PRO C CD  1 
ATOM   1682 N  N   . PRO C 1 38 ? 27.366  -38.401 34.129  1.00 60.29  ? 37  PRO C N   1 
ATOM   1683 C  CA  . PRO C 1 38 ? 28.435  -37.430 34.397  1.00 54.05  ? 37  PRO C CA  1 
ATOM   1684 C  C   . PRO C 1 38 ? 28.781  -36.592 33.173  1.00 57.76  ? 37  PRO C C   1 
ATOM   1685 O  O   . PRO C 1 38 ? 28.918  -37.105 32.060  1.00 49.21  ? 37  PRO C O   1 
ATOM   1686 C  CB  . PRO C 1 38 ? 29.609  -38.318 34.825  1.00 53.24  ? 37  PRO C CB  1 
ATOM   1687 C  CG  . PRO C 1 38 ? 28.938  -39.515 35.446  1.00 53.45  ? 37  PRO C CG  1 
ATOM   1688 C  CD  . PRO C 1 38 ? 27.719  -39.754 34.597  1.00 55.27  ? 37  PRO C CD  1 
ATOM   1689 N  N   . ASN C 1 39 ? 28.900  -35.280 33.395  1.00 55.86  ? 38  ASN C N   1 
ATOM   1690 C  CA  . ASN C 1 39 ? 29.275  -34.292 32.384  1.00 59.90  ? 38  ASN C CA  1 
ATOM   1691 C  C   . ASN C 1 39 ? 28.262  -34.206 31.244  1.00 54.85  ? 38  ASN C C   1 
ATOM   1692 O  O   . ASN C 1 39 ? 28.582  -33.694 30.166  1.00 55.00  ? 38  ASN C O   1 
ATOM   1693 C  CB  . ASN C 1 39 ? 30.681  -34.568 31.832  1.00 57.88  ? 38  ASN C CB  1 
ATOM   1694 C  CG  . ASN C 1 39 ? 31.330  -33.326 31.232  1.00 65.97  ? 38  ASN C CG  1 
ATOM   1695 O  OD1 . ASN C 1 39 ? 30.901  -32.198 31.489  1.00 64.86  ? 38  ASN C OD1 1 
ATOM   1696 N  ND2 . ASN C 1 39 ? 32.372  -33.530 30.427  1.00 58.72  ? 38  ASN C ND2 1 
ATOM   1697 N  N   . LYS C 1 40 ? 27.036  -34.681 31.460  1.00 53.48  ? 39  LYS C N   1 
ATOM   1698 C  CA  . LYS C 1 40 ? 25.996  -34.675 30.439  1.00 45.49  ? 39  LYS C CA  1 
ATOM   1699 C  C   . LYS C 1 40 ? 24.918  -33.663 30.797  1.00 56.71  ? 39  LYS C C   1 
ATOM   1700 O  O   . LYS C 1 40 ? 24.428  -33.646 31.933  1.00 47.69  ? 39  LYS C O   1 
ATOM   1701 C  CB  . LYS C 1 40 ? 25.366  -36.063 30.275  1.00 51.86  ? 39  LYS C CB  1 
ATOM   1702 C  CG  . LYS C 1 40 ? 26.335  -37.142 29.838  1.00 51.76  ? 39  LYS C CG  1 
ATOM   1703 C  CD  . LYS C 1 40 ? 27.161  -36.719 28.631  1.00 46.99  ? 39  LYS C CD  1 
ATOM   1704 C  CE  . LYS C 1 40 ? 27.867  -37.925 28.000  1.00 45.14  ? 39  LYS C CE  1 
ATOM   1705 N  NZ  . LYS C 1 40 ? 28.934  -37.553 27.014  1.00 48.06  ? 39  LYS C NZ  1 
ATOM   1706 N  N   . TYR C 1 41 ? 24.526  -32.810 29.789  1.00 46.26  ? 40  TYR C N   1 
ATOM   1707 C  CA  . TYR C 1 41 ? 23.433  -31.848 29.877  1.00 53.67  ? 40  TYR C CA  1 
ATOM   1708 C  C   . TYR C 1 41 ? 22.107  -32.498 29.484  1.00 55.09  ? 40  TYR C C   1 
ATOM   1709 O  O   . TYR C 1 41 ? 22.070  -33.387 28.621  1.00 48.28  ? 40  TYR C O   1 
ATOM   1710 C  CB  . TYR C 1 41 ? 23.684  -30.657 28.958  1.00 46.13  ? 40  TYR C CB  1 
ATOM   1711 C  CG  . TYR C 1 41 ? 24.927  -29.830 29.230  1.00 51.49  ? 40  TYR C CG  1 
ATOM   1712 C  CD1 . TYR C 1 41 ? 26.111  -30.068 28.544  1.00 55.94  ? 40  TYR C CD1 1 
ATOM   1713 C  CD2 . TYR C 1 41 ? 24.901  -28.777 30.139  1.00 58.78  ? 40  TYR C CD2 1 
ATOM   1714 C  CE1 . TYR C 1 41 ? 27.242  -29.301 28.771  1.00 47.32  ? 40  TYR C CE1 1 
ATOM   1715 C  CE2 . TYR C 1 41 ? 26.029  -28.005 30.377  1.00 58.71  ? 40  TYR C CE2 1 
ATOM   1716 C  CZ  . TYR C 1 41 ? 27.194  -28.271 29.692  1.00 64.97  ? 40  TYR C CZ  1 
ATOM   1717 O  OH  . TYR C 1 41 ? 28.309  -27.501 29.934  1.00 63.22  ? 40  TYR C OH  1 
ATOM   1718 N  N   . PRO C 1 42 ? 20.998  -32.075 30.094  1.00 61.03  ? 41  PRO C N   1 
ATOM   1719 C  CA  . PRO C 1 42 ? 19.680  -32.484 29.588  1.00 55.28  ? 41  PRO C CA  1 
ATOM   1720 C  C   . PRO C 1 42 ? 19.322  -31.631 28.378  1.00 48.26  ? 41  PRO C C   1 
ATOM   1721 O  O   . PRO C 1 42 ? 19.403  -30.403 28.430  1.00 47.21  ? 41  PRO C O   1 
ATOM   1722 C  CB  . PRO C 1 42 ? 18.744  -32.212 30.770  1.00 51.92  ? 41  PRO C CB  1 
ATOM   1723 C  CG  . PRO C 1 42 ? 19.389  -31.068 31.474  1.00 59.41  ? 41  PRO C CG  1 
ATOM   1724 C  CD  . PRO C 1 42 ? 20.888  -31.186 31.265  1.00 58.46  ? 41  PRO C CD  1 
ATOM   1725 N  N   . ILE C 1 43 ? 18.955  -32.283 27.278  1.00 50.25  ? 42  ILE C N   1 
ATOM   1726 C  CA  . ILE C 1 43 ? 18.710  -31.588 26.020  1.00 46.81  ? 42  ILE C CA  1 
ATOM   1727 C  C   . ILE C 1 43 ? 17.270  -31.815 25.596  1.00 39.57  ? 42  ILE C C   1 
ATOM   1728 O  O   . ILE C 1 43 ? 16.787  -32.955 25.583  1.00 55.06  ? 42  ILE C O   1 
ATOM   1729 C  CB  . ILE C 1 43 ? 19.685  -32.038 24.917  1.00 43.29  ? 42  ILE C CB  1 
ATOM   1730 C  CG1 . ILE C 1 43 ? 21.104  -31.615 25.300  1.00 38.60  ? 42  ILE C CG1 1 
ATOM   1731 C  CG2 . ILE C 1 43 ? 19.277  -31.438 23.553  1.00 40.78  ? 42  ILE C CG2 1 
ATOM   1732 C  CD1 . ILE C 1 43 ? 21.227  -30.148 25.640  1.00 40.81  ? 42  ILE C CD1 1 
ATOM   1733 N  N   . PHE C 1 44 ? 16.595  -30.726 25.238  1.00 46.61  ? 43  PHE C N   1 
ATOM   1734 C  CA  . PHE C 1 44 ? 15.267  -30.748 24.646  1.00 49.50  ? 43  PHE C CA  1 
ATOM   1735 C  C   . PHE C 1 44 ? 15.417  -30.391 23.171  1.00 33.55  ? 43  PHE C C   1 
ATOM   1736 O  O   . PHE C 1 44 ? 15.994  -29.348 22.844  1.00 37.23  ? 43  PHE C O   1 
ATOM   1737 C  CB  . PHE C 1 44 ? 14.346  -29.755 25.358  1.00 55.08  ? 43  PHE C CB  1 
ATOM   1738 C  CG  . PHE C 1 44 ? 12.961  -29.687 24.782  1.00 57.86  ? 43  PHE C CG  1 
ATOM   1739 C  CD1 . PHE C 1 44 ? 12.531  -28.554 24.100  1.00 57.20  ? 43  PHE C CD1 1 
ATOM   1740 C  CD2 . PHE C 1 44 ? 12.089  -30.760 24.921  1.00 49.56  ? 43  PHE C CD2 1 
ATOM   1741 C  CE1 . PHE C 1 44 ? 11.253  -28.494 23.570  1.00 57.16  ? 43  PHE C CE1 1 
ATOM   1742 C  CE2 . PHE C 1 44 ? 10.813  -30.704 24.396  1.00 54.28  ? 43  PHE C CE2 1 
ATOM   1743 C  CZ  . PHE C 1 44 ? 10.396  -29.571 23.718  1.00 59.58  ? 43  PHE C CZ  1 
ATOM   1744 N  N   . PHE C 1 45 ? 14.943  -31.272 22.297  1.00 35.60  ? 44  PHE C N   1 
ATOM   1745 C  CA  . PHE C 1 45 ? 15.069  -31.069 20.857  1.00 42.39  ? 44  PHE C CA  1 
ATOM   1746 C  C   . PHE C 1 45 ? 13.818  -30.380 20.333  1.00 42.55  ? 44  PHE C C   1 
ATOM   1747 O  O   . PHE C 1 45 ? 12.715  -30.931 20.431  1.00 39.70  ? 44  PHE C O   1 
ATOM   1748 C  CB  . PHE C 1 45 ? 15.282  -32.398 20.135  1.00 38.40  ? 44  PHE C CB  1 
ATOM   1749 C  CG  . PHE C 1 45 ? 16.600  -33.025 20.427  1.00 40.18  ? 44  PHE C CG  1 
ATOM   1750 C  CD1 . PHE C 1 45 ? 17.703  -32.732 19.657  1.00 32.83  ? 44  PHE C CD1 1 
ATOM   1751 C  CD2 . PHE C 1 45 ? 16.740  -33.913 21.487  1.00 44.97  ? 44  PHE C CD2 1 
ATOM   1752 C  CE1 . PHE C 1 45 ? 18.933  -33.312 19.927  1.00 31.62  ? 44  PHE C CE1 1 
ATOM   1753 C  CE2 . PHE C 1 45 ? 17.957  -34.490 21.761  1.00 41.42  ? 44  PHE C CE2 1 
ATOM   1754 C  CZ  . PHE C 1 45 ? 19.057  -34.192 20.987  1.00 36.14  ? 44  PHE C CZ  1 
ATOM   1755 N  N   . PHE C 1 46 ? 13.987  -29.188 19.761  1.00 35.55  ? 45  PHE C N   1 
ATOM   1756 C  CA  . PHE C 1 46 ? 12.847  -28.511 19.161  1.00 31.22  ? 45  PHE C CA  1 
ATOM   1757 C  C   . PHE C 1 46 ? 12.241  -29.358 18.045  1.00 36.89  ? 45  PHE C C   1 
ATOM   1758 O  O   . PHE C 1 46 ? 12.910  -30.183 17.415  1.00 31.00  ? 45  PHE C O   1 
ATOM   1759 C  CB  . PHE C 1 46 ? 13.266  -27.143 18.626  1.00 33.03  ? 45  PHE C CB  1 
ATOM   1760 C  CG  . PHE C 1 46 ? 13.605  -26.152 19.696  1.00 31.20  ? 45  PHE C CG  1 
ATOM   1761 C  CD1 . PHE C 1 46 ? 12.621  -25.676 20.551  1.00 40.32  ? 45  PHE C CD1 1 
ATOM   1762 C  CD2 . PHE C 1 46 ? 14.891  -25.665 19.822  1.00 31.03  ? 45  PHE C CD2 1 
ATOM   1763 C  CE1 . PHE C 1 46 ? 12.930  -24.743 21.536  1.00 37.66  ? 45  PHE C CE1 1 
ATOM   1764 C  CE2 . PHE C 1 46 ? 15.207  -24.731 20.804  1.00 35.32  ? 45  PHE C CE2 1 
ATOM   1765 C  CZ  . PHE C 1 46 ? 14.224  -24.272 21.660  1.00 39.61  ? 45  PHE C CZ  1 
ATOM   1766 N  N   . GLY C 1 47 ? 10.955  -29.147 17.798  1.00 37.35  ? 46  GLY C N   1 
ATOM   1767 C  CA  . GLY C 1 47 ? 10.282  -29.886 16.751  1.00 40.65  ? 46  GLY C CA  1 
ATOM   1768 C  C   . GLY C 1 47 ? 9.775   -31.238 17.204  1.00 52.42  ? 46  GLY C C   1 
ATOM   1769 O  O   . GLY C 1 47 ? 8.575   -31.398 17.452  1.00 56.01  ? 46  GLY C O   1 
ATOM   1770 N  N   . THR C 1 48 ? 10.677  -32.222 17.316  1.00 44.54  ? 47  THR C N   1 
ATOM   1771 C  CA  . THR C 1 48 ? 10.255  -33.549 17.766  1.00 57.33  ? 47  THR C CA  1 
ATOM   1772 C  C   . THR C 1 48 ? 9.883   -33.549 19.241  1.00 47.93  ? 47  THR C C   1 
ATOM   1773 O  O   . THR C 1 48 ? 9.078   -34.383 19.674  1.00 61.04  ? 47  THR C O   1 
ATOM   1774 C  CB  . THR C 1 48 ? 11.350  -34.589 17.522  1.00 40.10  ? 47  THR C CB  1 
ATOM   1775 O  OG1 . THR C 1 48 ? 12.465  -34.323 18.387  1.00 39.61  ? 47  THR C OG1 1 
ATOM   1776 C  CG2 . THR C 1 48 ? 11.800  -34.585 16.058  1.00 44.71  ? 47  THR C CG2 1 
ATOM   1777 N  N   . HIS C 1 49 ? 10.469  -32.642 20.017  1.00 38.64  ? 48  HIS C N   1 
ATOM   1778 C  CA  . HIS C 1 49 ? 10.216  -32.436 21.442  1.00 55.28  ? 48  HIS C CA  1 
ATOM   1779 C  C   . HIS C 1 49 ? 10.731  -33.573 22.313  1.00 58.00  ? 48  HIS C C   1 
ATOM   1780 O  O   . HIS C 1 49 ? 10.356  -33.658 23.491  1.00 66.73  ? 48  HIS C O   1 
ATOM   1781 C  CB  . HIS C 1 49 ? 8.730   -32.198 21.730  1.00 55.55  ? 48  HIS C CB  1 
ATOM   1782 C  CG  . HIS C 1 49 ? 8.162   -31.017 21.005  1.00 60.07  ? 48  HIS C CG  1 
ATOM   1783 N  ND1 . HIS C 1 49 ? 8.572   -29.723 21.255  1.00 55.51  ? 48  HIS C ND1 1 
ATOM   1784 C  CD2 . HIS C 1 49 ? 7.218   -30.934 20.038  1.00 59.51  ? 48  HIS C CD2 1 
ATOM   1785 C  CE1 . HIS C 1 49 ? 7.906   -28.894 20.472  1.00 57.60  ? 48  HIS C CE1 1 
ATOM   1786 N  NE2 . HIS C 1 49 ? 7.081   -29.604 19.721  1.00 60.10  ? 48  HIS C NE2 1 
ATOM   1787 N  N   . GLU C 1 50 ? 11.584  -34.444 21.776  1.00 52.85  ? 49  GLU C N   1 
ATOM   1788 C  CA  . GLU C 1 50 ? 12.159  -35.517 22.570  1.00 49.13  ? 49  GLU C CA  1 
ATOM   1789 C  C   . GLU C 1 50 ? 13.275  -34.974 23.459  1.00 54.89  ? 49  GLU C C   1 
ATOM   1790 O  O   . GLU C 1 50 ? 13.662  -33.805 23.381  1.00 45.63  ? 49  GLU C O   1 
ATOM   1791 C  CB  . GLU C 1 50 ? 12.672  -36.633 21.667  1.00 47.21  ? 49  GLU C CB  1 
ATOM   1792 C  CG  . GLU C 1 50 ? 11.681  -37.016 20.576  1.00 58.60  ? 49  GLU C CG  1 
ATOM   1793 C  CD  . GLU C 1 50 ? 11.620  -38.506 20.329  1.00 63.81  ? 49  GLU C CD  1 
ATOM   1794 O  OE1 . GLU C 1 50 ? 12.543  -39.040 19.677  1.00 71.23  ? 49  GLU C OE1 1 
ATOM   1795 O  OE2 . GLU C 1 50 ? 10.651  -39.141 20.795  1.00 68.45  ? 49  GLU C OE2 1 
ATOM   1796 N  N   . THR C 1 51 ? 13.785  -35.836 24.335  1.00 52.95  ? 50  THR C N   1 
ATOM   1797 C  CA  . THR C 1 51 ? 14.854  -35.462 25.246  1.00 52.62  ? 50  THR C CA  1 
ATOM   1798 C  C   . THR C 1 51 ? 15.974  -36.491 25.162  1.00 40.23  ? 50  THR C C   1 
ATOM   1799 O  O   . THR C 1 51 ? 15.782  -37.622 24.701  1.00 51.88  ? 50  THR C O   1 
ATOM   1800 C  CB  . THR C 1 51 ? 14.364  -35.336 26.700  1.00 59.90  ? 50  THR C CB  1 
ATOM   1801 O  OG1 . THR C 1 51 ? 13.443  -36.397 26.986  1.00 52.99  ? 50  THR C OG1 1 
ATOM   1802 C  CG2 . THR C 1 51 ? 13.687  -33.983 26.937  1.00 50.27  ? 50  THR C CG2 1 
ATOM   1803 N  N   . ALA C 1 52 ? 17.153  -36.068 25.610  1.00 44.25  ? 51  ALA C N   1 
ATOM   1804 C  CA  . ALA C 1 52 ? 18.360  -36.879 25.582  1.00 44.34  ? 51  ALA C CA  1 
ATOM   1805 C  C   . ALA C 1 52 ? 19.409  -36.190 26.438  1.00 53.09  ? 51  ALA C C   1 
ATOM   1806 O  O   . ALA C 1 52 ? 19.288  -35.006 26.763  1.00 50.13  ? 51  ALA C O   1 
ATOM   1807 C  CB  . ALA C 1 52 ? 18.875  -37.078 24.155  1.00 50.96  ? 51  ALA C CB  1 
ATOM   1808 N  N   . PHE C 1 53 ? 20.443  -36.948 26.801  1.00 52.23  ? 52  PHE C N   1 
ATOM   1809 C  CA  . PHE C 1 53 ? 21.565  -36.432 27.579  1.00 51.27  ? 52  PHE C CA  1 
ATOM   1810 C  C   . PHE C 1 53 ? 22.789  -36.353 26.678  1.00 50.22  ? 52  PHE C C   1 
ATOM   1811 O  O   . PHE C 1 53 ? 23.214  -37.368 26.112  1.00 48.17  ? 52  PHE C O   1 
ATOM   1812 C  CB  . PHE C 1 53 ? 21.838  -37.312 28.802  1.00 52.08  ? 52  PHE C CB  1 
ATOM   1813 C  CG  . PHE C 1 53 ? 20.995  -36.958 29.995  1.00 55.06  ? 52  PHE C CG  1 
ATOM   1814 C  CD1 . PHE C 1 53 ? 20.979  -35.661 30.482  1.00 58.31  ? 52  PHE C CD1 1 
ATOM   1815 C  CD2 . PHE C 1 53 ? 20.193  -37.909 30.609  1.00 67.01  ? 52  PHE C CD2 1 
ATOM   1816 C  CE1 . PHE C 1 53 ? 20.199  -35.321 31.579  1.00 64.13  ? 52  PHE C CE1 1 
ATOM   1817 C  CE2 . PHE C 1 53 ? 19.409  -37.572 31.704  1.00 60.38  ? 52  PHE C CE2 1 
ATOM   1818 C  CZ  . PHE C 1 53 ? 19.412  -36.276 32.185  1.00 60.69  ? 52  PHE C CZ  1 
ATOM   1819 N  N   . LEU C 1 54 ? 23.342  -35.153 26.537  1.00 40.03  ? 53  LEU C N   1 
ATOM   1820 C  CA  . LEU C 1 54 ? 24.485  -34.933 25.669  1.00 41.03  ? 53  LEU C CA  1 
ATOM   1821 C  C   . LEU C 1 54 ? 25.592  -34.225 26.430  1.00 36.08  ? 53  LEU C C   1 
ATOM   1822 O  O   . LEU C 1 54 ? 25.354  -33.509 27.406  1.00 42.34  ? 53  LEU C O   1 
ATOM   1823 C  CB  . LEU C 1 54 ? 24.115  -34.106 24.420  1.00 40.57  ? 53  LEU C CB  1 
ATOM   1824 C  CG  . LEU C 1 54 ? 23.350  -34.875 23.345  1.00 36.25  ? 53  LEU C CG  1 
ATOM   1825 C  CD1 . LEU C 1 54 ? 23.049  -34.006 22.117  1.00 31.48  ? 53  LEU C CD1 1 
ATOM   1826 C  CD2 . LEU C 1 54 ? 24.132  -36.128 22.932  1.00 40.99  ? 53  LEU C CD2 1 
ATOM   1827 N  N   . GLY C 1 55 ? 26.811  -34.425 25.945  1.00 39.25  ? 54  GLY C N   1 
ATOM   1828 C  CA  . GLY C 1 55 ? 27.971  -33.783 26.500  1.00 45.73  ? 54  GLY C CA  1 
ATOM   1829 C  C   . GLY C 1 55 ? 28.386  -32.557 25.713  1.00 53.44  ? 54  GLY C C   1 
ATOM   1830 O  O   . GLY C 1 55 ? 27.851  -32.252 24.636  1.00 42.18  ? 54  GLY C O   1 
ATOM   1831 N  N   . PRO C 1 56 ? 29.376  -31.838 26.252  1.00 49.11  ? 55  PRO C N   1 
ATOM   1832 C  CA  . PRO C 1 56 ? 29.808  -30.575 25.629  1.00 45.55  ? 55  PRO C CA  1 
ATOM   1833 C  C   . PRO C 1 56 ? 30.161  -30.659 24.159  1.00 53.38  ? 55  PRO C C   1 
ATOM   1834 O  O   . PRO C 1 56 ? 29.757  -29.785 23.384  1.00 47.51  ? 55  PRO C O   1 
ATOM   1835 C  CB  . PRO C 1 56 ? 31.034  -30.195 26.470  1.00 57.42  ? 55  PRO C CB  1 
ATOM   1836 C  CG  . PRO C 1 56 ? 30.750  -30.769 27.798  1.00 48.32  ? 55  PRO C CG  1 
ATOM   1837 C  CD  . PRO C 1 56 ? 30.023  -32.060 27.556  1.00 46.36  ? 55  PRO C CD  1 
ATOM   1838 N  N   . LYS C 1 57 ? 30.916  -31.678 23.748  1.00 56.22  ? 56  LYS C N   1 
ATOM   1839 C  CA  . LYS C 1 57 ? 31.402  -31.689 22.374  1.00 53.10  ? 56  LYS C CA  1 
ATOM   1840 C  C   . LYS C 1 57 ? 30.300  -31.941 21.360  1.00 55.75  ? 56  LYS C C   1 
ATOM   1841 O  O   . LYS C 1 57 ? 30.570  -31.889 20.156  1.00 54.05  ? 56  LYS C O   1 
ATOM   1842 C  CB  . LYS C 1 57 ? 32.518  -32.726 22.217  1.00 63.37  ? 56  LYS C CB  1 
ATOM   1843 C  CG  . LYS C 1 57 ? 32.293  -34.018 22.981  1.00 64.69  ? 56  LYS C CG  1 
ATOM   1844 C  CD  . LYS C 1 57 ? 31.615  -35.081 22.134  1.00 63.58  ? 56  LYS C CD  1 
ATOM   1845 C  CE  . LYS C 1 57 ? 31.109  -36.220 23.017  1.00 66.65  ? 56  LYS C CE  1 
ATOM   1846 N  NZ  . LYS C 1 57 ? 30.468  -37.316 22.227  1.00 68.04  ? 56  LYS C NZ  1 
ATOM   1847 N  N   . ASP C 1 58 ? 29.074  -32.202 21.807  1.00 48.00  ? 57  ASP C N   1 
ATOM   1848 C  CA  . ASP C 1 58 ? 27.942  -32.380 20.913  1.00 43.68  ? 57  ASP C CA  1 
ATOM   1849 C  C   . ASP C 1 58 ? 27.037  -31.157 20.856  1.00 45.26  ? 57  ASP C C   1 
ATOM   1850 O  O   . ASP C 1 58 ? 25.947  -31.235 20.278  1.00 38.09  ? 57  ASP C O   1 
ATOM   1851 C  CB  . ASP C 1 58 ? 27.128  -33.597 21.337  1.00 44.61  ? 57  ASP C CB  1 
ATOM   1852 C  CG  . ASP C 1 58 ? 27.899  -34.890 21.189  1.00 46.51  ? 57  ASP C CG  1 
ATOM   1853 O  OD1 . ASP C 1 58 ? 28.484  -35.117 20.106  1.00 53.44  ? 57  ASP C OD1 1 
ATOM   1854 O  OD2 . ASP C 1 58 ? 27.911  -35.675 22.158  1.00 56.79  ? 57  ASP C OD2 1 
ATOM   1855 N  N   . LEU C 1 59 ? 27.454  -30.039 21.445  1.00 43.56  ? 58  LEU C N   1 
ATOM   1856 C  CA  . LEU C 1 59 ? 26.623  -28.849 21.546  1.00 49.94  ? 58  LEU C CA  1 
ATOM   1857 C  C   . LEU C 1 59 ? 27.310  -27.678 20.867  1.00 51.97  ? 58  LEU C C   1 
ATOM   1858 O  O   . LEU C 1 59 ? 28.535  -27.527 20.944  1.00 53.37  ? 58  LEU C O   1 
ATOM   1859 C  CB  . LEU C 1 59 ? 26.317  -28.502 23.008  1.00 45.64  ? 58  LEU C CB  1 
ATOM   1860 C  CG  . LEU C 1 59 ? 25.672  -29.624 23.825  1.00 42.48  ? 58  LEU C CG  1 
ATOM   1861 C  CD1 . LEU C 1 59 ? 25.384  -29.178 25.255  1.00 43.07  ? 58  LEU C CD1 1 
ATOM   1862 C  CD2 . LEU C 1 59 ? 24.406  -30.143 23.156  1.00 36.08  ? 58  LEU C CD2 1 
ATOM   1863 N  N   . PHE C 1 60 ? 26.507  -26.856 20.201  1.00 59.20  ? 59  PHE C N   1 
ATOM   1864 C  CA  . PHE C 1 60 ? 26.947  -25.679 19.468  1.00 49.95  ? 59  PHE C CA  1 
ATOM   1865 C  C   . PHE C 1 60 ? 25.927  -24.575 19.716  1.00 56.56  ? 59  PHE C C   1 
ATOM   1866 O  O   . PHE C 1 60 ? 24.741  -24.767 19.423  1.00 53.83  ? 59  PHE C O   1 
ATOM   1867 C  CB  . PHE C 1 60 ? 27.071  -25.985 17.975  1.00 48.92  ? 59  PHE C CB  1 
ATOM   1868 C  CG  . PHE C 1 60 ? 27.907  -27.196 17.667  1.00 53.38  ? 59  PHE C CG  1 
ATOM   1869 C  CD1 . PHE C 1 60 ? 27.350  -28.469 17.675  1.00 50.36  ? 59  PHE C CD1 1 
ATOM   1870 C  CD2 . PHE C 1 60 ? 29.252  -27.064 17.366  1.00 52.22  ? 59  PHE C CD2 1 
ATOM   1871 C  CE1 . PHE C 1 60 ? 28.122  -29.582 17.397  1.00 48.69  ? 59  PHE C CE1 1 
ATOM   1872 C  CE2 . PHE C 1 60 ? 30.026  -28.172 17.082  1.00 59.08  ? 59  PHE C CE2 1 
ATOM   1873 C  CZ  . PHE C 1 60 ? 29.460  -29.432 17.096  1.00 59.36  ? 59  PHE C CZ  1 
ATOM   1874 N  N   . PRO C 1 61 ? 26.330  -23.426 20.267  1.00 61.06  ? 60  PRO C N   1 
ATOM   1875 C  CA  . PRO C 1 61 ? 25.339  -22.396 20.614  1.00 53.43  ? 60  PRO C CA  1 
ATOM   1876 C  C   . PRO C 1 61 ? 24.621  -21.880 19.372  1.00 52.18  ? 60  PRO C C   1 
ATOM   1877 O  O   . PRO C 1 61 ? 25.207  -21.754 18.294  1.00 47.53  ? 60  PRO C O   1 
ATOM   1878 C  CB  . PRO C 1 61 ? 26.179  -21.303 21.289  1.00 59.69  ? 60  PRO C CB  1 
ATOM   1879 C  CG  . PRO C 1 61 ? 27.558  -21.499 20.741  1.00 60.49  ? 60  PRO C CG  1 
ATOM   1880 C  CD  . PRO C 1 61 ? 27.711  -22.983 20.529  1.00 63.88  ? 60  PRO C CD  1 
ATOM   1881 N  N   . TYR C 1 62 ? 23.328  -21.600 19.539  1.00 50.61  ? 61  TYR C N   1 
ATOM   1882 C  CA  . TYR C 1 62 ? 22.431  -21.304 18.427  1.00 45.80  ? 61  TYR C CA  1 
ATOM   1883 C  C   . TYR C 1 62 ? 22.831  -20.042 17.670  1.00 59.69  ? 61  TYR C C   1 
ATOM   1884 O  O   . TYR C 1 62 ? 23.223  -20.110 16.501  1.00 60.61  ? 61  TYR C O   1 
ATOM   1885 C  CB  . TYR C 1 62 ? 20.995  -21.178 18.951  1.00 45.22  ? 61  TYR C CB  1 
ATOM   1886 C  CG  . TYR C 1 62 ? 19.978  -20.786 17.904  1.00 57.73  ? 61  TYR C CG  1 
ATOM   1887 C  CD1 . TYR C 1 62 ? 19.130  -19.697 18.110  1.00 62.67  ? 61  TYR C CD1 1 
ATOM   1888 C  CD2 . TYR C 1 62 ? 19.860  -21.494 16.716  1.00 54.88  ? 61  TYR C CD2 1 
ATOM   1889 C  CE1 . TYR C 1 62 ? 18.184  -19.337 17.159  1.00 60.20  ? 61  TYR C CE1 1 
ATOM   1890 C  CE2 . TYR C 1 62 ? 18.921  -21.134 15.754  1.00 63.91  ? 61  TYR C CE2 1 
ATOM   1891 C  CZ  . TYR C 1 62 ? 18.086  -20.051 15.985  1.00 56.92  ? 61  TYR C CZ  1 
ATOM   1892 O  OH  . TYR C 1 62 ? 17.156  -19.674 15.040  1.00 50.96  ? 61  TYR C OH  1 
ATOM   1893 N  N   . ASP C 1 63 ? 22.737  -18.886 18.335  1.00 68.08  ? 62  ASP C N   1 
ATOM   1894 C  CA  . ASP C 1 63 ? 23.030  -17.610 17.685  1.00 69.76  ? 62  ASP C CA  1 
ATOM   1895 C  C   . ASP C 1 63 ? 24.449  -17.559 17.137  1.00 63.82  ? 62  ASP C C   1 
ATOM   1896 O  O   . ASP C 1 63 ? 24.697  -16.908 16.115  1.00 58.81  ? 62  ASP C O   1 
ATOM   1897 C  CB  . ASP C 1 63 ? 22.800  -16.466 18.671  1.00 66.22  ? 62  ASP C CB  1 
ATOM   1898 C  CG  . ASP C 1 63 ? 21.339  -16.285 19.009  1.00 69.55  ? 62  ASP C CG  1 
ATOM   1899 O  OD1 . ASP C 1 63 ? 20.572  -15.884 18.106  1.00 75.45  ? 62  ASP C OD1 1 
ATOM   1900 O  OD2 . ASP C 1 63 ? 20.952  -16.567 20.165  1.00 70.27  ? 62  ASP C OD2 1 
ATOM   1901 N  N   . LYS C 1 64 ? 25.389  -18.239 17.792  1.00 54.65  ? 63  LYS C N   1 
ATOM   1902 C  CA  . LYS C 1 64 ? 26.772  -18.214 17.336  1.00 59.17  ? 63  LYS C CA  1 
ATOM   1903 C  C   . LYS C 1 64 ? 27.003  -19.117 16.122  1.00 61.96  ? 63  LYS C C   1 
ATOM   1904 O  O   . LYS C 1 64 ? 27.897  -18.838 15.312  1.00 51.40  ? 63  LYS C O   1 
ATOM   1905 C  CB  . LYS C 1 64 ? 27.695  -18.607 18.493  1.00 56.13  ? 63  LYS C CB  1 
ATOM   1906 C  CG  . LYS C 1 64 ? 29.082  -17.993 18.436  1.00 70.23  ? 63  LYS C CG  1 
ATOM   1907 C  CD  . LYS C 1 64 ? 29.809  -18.146 19.766  1.00 70.90  ? 63  LYS C CD  1 
ATOM   1908 C  CE  . LYS C 1 64 ? 31.189  -17.501 19.717  1.00 79.43  ? 63  LYS C CE  1 
ATOM   1909 N  NZ  . LYS C 1 64 ? 31.126  -16.072 19.293  1.00 74.09  ? 63  LYS C NZ  1 
ATOM   1910 N  N   . CYS C 1 65 ? 26.211  -20.187 15.963  1.00 57.01  ? 64  CYS C N   1 
ATOM   1911 C  CA  . CYS C 1 65 ? 26.446  -21.172 14.910  1.00 50.07  ? 64  CYS C CA  1 
ATOM   1912 C  C   . CYS C 1 65 ? 25.270  -21.392 13.963  1.00 51.26  ? 64  CYS C C   1 
ATOM   1913 O  O   . CYS C 1 65 ? 25.391  -22.214 13.043  1.00 44.55  ? 64  CYS C O   1 
ATOM   1914 C  CB  . CYS C 1 65 ? 26.841  -22.523 15.527  1.00 58.97  ? 64  CYS C CB  1 
ATOM   1915 S  SG  . CYS C 1 65 ? 28.508  -22.578 16.214  1.00 66.06  ? 64  CYS C SG  1 
ATOM   1916 N  N   . LYS C 1 66 ? 24.146  -20.688 14.150  1.00 52.05  ? 65  LYS C N   1 
ATOM   1917 C  CA  . LYS C 1 66 ? 22.962  -20.909 13.320  1.00 53.19  ? 65  LYS C CA  1 
ATOM   1918 C  C   . LYS C 1 66 ? 23.239  -20.727 11.837  1.00 51.43  ? 65  LYS C C   1 
ATOM   1919 O  O   . LYS C 1 66 ? 22.516  -21.291 11.008  1.00 47.61  ? 65  LYS C O   1 
ATOM   1920 C  CB  . LYS C 1 66 ? 21.835  -19.957 13.732  1.00 52.91  ? 65  LYS C CB  1 
ATOM   1921 C  CG  . LYS C 1 66 ? 22.232  -18.486 13.691  1.00 52.86  ? 65  LYS C CG  1 
ATOM   1922 C  CD  . LYS C 1 66 ? 21.024  -17.572 13.780  1.00 64.30  ? 65  LYS C CD  1 
ATOM   1923 C  CE  . LYS C 1 66 ? 20.288  -17.761 15.084  1.00 63.62  ? 65  LYS C CE  1 
ATOM   1924 N  NZ  . LYS C 1 66 ? 19.079  -16.885 15.208  1.00 68.56  ? 65  LYS C NZ  1 
ATOM   1925 N  N   . ASP C 1 67 ? 24.264  -19.953 11.476  1.00 66.23  ? 66  ASP C N   1 
ATOM   1926 C  CA  . ASP C 1 67 ? 24.497  -19.688 10.063  1.00 58.45  ? 66  ASP C CA  1 
ATOM   1927 C  C   . ASP C 1 67 ? 24.940  -20.934 9.305   1.00 60.32  ? 66  ASP C C   1 
ATOM   1928 O  O   . ASP C 1 67 ? 24.767  -20.987 8.085   1.00 59.65  ? 66  ASP C O   1 
ATOM   1929 C  CB  . ASP C 1 67 ? 25.509  -18.544 9.888   1.00 57.28  ? 66  ASP C CB  1 
ATOM   1930 C  CG  . ASP C 1 67 ? 26.591  -18.527 10.966  1.00 64.14  ? 66  ASP C CG  1 
ATOM   1931 O  OD1 . ASP C 1 67 ? 26.589  -19.410 11.856  1.00 72.03  ? 66  ASP C OD1 1 
ATOM   1932 O  OD2 . ASP C 1 67 ? 27.448  -17.612 10.918  1.00 59.96  ? 66  ASP C OD2 1 
ATOM   1933 N  N   . LYS C 1 68 ? 25.469  -21.951 9.986   1.00 56.77  ? 67  LYS C N   1 
ATOM   1934 C  CA  . LYS C 1 68 ? 25.820  -23.193 9.303   1.00 57.02  ? 67  LYS C CA  1 
ATOM   1935 C  C   . LYS C 1 68 ? 24.791  -24.298 9.525   1.00 63.09  ? 67  LYS C C   1 
ATOM   1936 O  O   . LYS C 1 68 ? 24.400  -24.988 8.577   1.00 55.70  ? 67  LYS C O   1 
ATOM   1937 C  CB  . LYS C 1 68 ? 27.213  -23.670 9.745   1.00 58.42  ? 67  LYS C CB  1 
ATOM   1938 C  CG  . LYS C 1 68 ? 27.544  -25.103 9.334   1.00 63.90  ? 67  LYS C CG  1 
ATOM   1939 C  CD  . LYS C 1 68 ? 27.315  -25.370 7.840   1.00 72.13  ? 67  LYS C CD  1 
ATOM   1940 C  CE  . LYS C 1 68 ? 27.041  -26.853 7.603   1.00 81.10  ? 67  LYS C CE  1 
ATOM   1941 N  NZ  . LYS C 1 68 ? 26.155  -27.119 6.430   1.00 78.61  ? 67  LYS C NZ  1 
ATOM   1942 N  N   . TYR C 1 69 ? 24.338  -24.487 10.759  1.00 52.78  ? 68  TYR C N   1 
ATOM   1943 C  CA  . TYR C 1 69 ? 23.427  -25.588 11.029  1.00 50.83  ? 68  TYR C CA  1 
ATOM   1944 C  C   . TYR C 1 69 ? 21.962  -25.197 10.901  1.00 45.61  ? 68  TYR C C   1 
ATOM   1945 O  O   . TYR C 1 69 ? 21.110  -26.081 10.747  1.00 41.99  ? 68  TYR C O   1 
ATOM   1946 C  CB  . TYR C 1 69 ? 23.719  -26.157 12.419  1.00 44.63  ? 68  TYR C CB  1 
ATOM   1947 C  CG  . TYR C 1 69 ? 25.140  -26.671 12.526  1.00 46.78  ? 68  TYR C CG  1 
ATOM   1948 C  CD1 . TYR C 1 69 ? 25.597  -27.671 11.673  1.00 50.27  ? 68  TYR C CD1 1 
ATOM   1949 C  CD2 . TYR C 1 69 ? 26.021  -26.158 13.472  1.00 54.83  ? 68  TYR C CD2 1 
ATOM   1950 C  CE1 . TYR C 1 69 ? 26.893  -28.149 11.759  1.00 51.95  ? 68  TYR C CE1 1 
ATOM   1951 C  CE2 . TYR C 1 69 ? 27.325  -26.633 13.565  1.00 50.48  ? 68  TYR C CE2 1 
ATOM   1952 C  CZ  . TYR C 1 69 ? 27.752  -27.624 12.703  1.00 55.10  ? 68  TYR C CZ  1 
ATOM   1953 O  OH  . TYR C 1 69 ? 29.043  -28.098 12.787  1.00 66.09  ? 68  TYR C OH  1 
ATOM   1954 N  N   . GLY C 1 70 ? 21.651  -23.903 10.939  1.00 45.35  ? 69  GLY C N   1 
ATOM   1955 C  CA  . GLY C 1 70 ? 20.281  -23.461 10.790  1.00 47.42  ? 69  GLY C CA  1 
ATOM   1956 C  C   . GLY C 1 70 ? 19.861  -23.445 9.337   1.00 54.43  ? 69  GLY C C   1 
ATOM   1957 O  O   . GLY C 1 70 ? 19.745  -22.381 8.718   1.00 52.96  ? 69  GLY C O   1 
ATOM   1958 N  N   . LYS C 1 71 ? 19.644  -24.631 8.778   1.00 40.68  ? 70  LYS C N   1 
ATOM   1959 C  CA  . LYS C 1 71 ? 19.269  -24.766 7.386   1.00 45.93  ? 70  LYS C CA  1 
ATOM   1960 C  C   . LYS C 1 71 ? 18.275  -25.915 7.313   1.00 45.86  ? 70  LYS C C   1 
ATOM   1961 O  O   . LYS C 1 71 ? 18.427  -26.911 8.040   1.00 45.83  ? 70  LYS C O   1 
ATOM   1962 C  CB  . LYS C 1 71 ? 20.487  -25.042 6.490   1.00 49.83  ? 70  LYS C CB  1 
ATOM   1963 C  CG  . LYS C 1 71 ? 20.182  -25.117 4.999   1.00 51.47  ? 70  LYS C CG  1 
ATOM   1964 C  CD  . LYS C 1 71 ? 21.373  -25.622 4.205   1.00 60.19  ? 70  LYS C CD  1 
ATOM   1965 C  CE  . LYS C 1 71 ? 20.995  -25.965 2.759   1.00 58.58  ? 70  LYS C CE  1 
ATOM   1966 N  NZ  . LYS C 1 71 ? 20.572  -27.388 2.596   1.00 52.45  ? 70  LYS C NZ  1 
ATOM   1967 N  N   . PRO C 1 72 ? 17.239  -25.800 6.480   1.00 37.76  ? 71  PRO C N   1 
ATOM   1968 C  CA  . PRO C 1 72 ? 16.239  -26.868 6.407   1.00 32.08  ? 71  PRO C CA  1 
ATOM   1969 C  C   . PRO C 1 72 ? 16.845  -28.197 5.988   1.00 41.30  ? 71  PRO C C   1 
ATOM   1970 O  O   . PRO C 1 72 ? 17.888  -28.261 5.334   1.00 45.77  ? 71  PRO C O   1 
ATOM   1971 C  CB  . PRO C 1 72 ? 15.251  -26.363 5.349   1.00 40.01  ? 71  PRO C CB  1 
ATOM   1972 C  CG  . PRO C 1 72 ? 15.376  -24.900 5.399   1.00 32.99  ? 71  PRO C CG  1 
ATOM   1973 C  CD  . PRO C 1 72 ? 16.815  -24.604 5.729   1.00 37.24  ? 71  PRO C CD  1 
ATOM   1974 N  N   . ASN C 1 73 ? 16.171  -29.264 6.391   1.00 39.52  ? 72  ASN C N   1 
ATOM   1975 C  CA  . ASN C 1 73 ? 16.376  -30.579 5.814   1.00 48.64  ? 72  ASN C CA  1 
ATOM   1976 C  C   . ASN C 1 73 ? 15.107  -31.373 6.058   1.00 41.54  ? 72  ASN C C   1 
ATOM   1977 O  O   . ASN C 1 73 ? 14.201  -30.938 6.776   1.00 41.02  ? 72  ASN C O   1 
ATOM   1978 C  CB  . ASN C 1 73 ? 17.597  -31.298 6.394   1.00 48.58  ? 72  ASN C CB  1 
ATOM   1979 C  CG  . ASN C 1 73 ? 17.406  -31.701 7.841   1.00 39.28  ? 72  ASN C CG  1 
ATOM   1980 O  OD1 . ASN C 1 73 ? 16.550  -32.527 8.172   1.00 43.92  ? 72  ASN C OD1 1 
ATOM   1981 N  ND2 . ASN C 1 73 ? 18.210  -31.121 8.713   1.00 49.87  ? 72  ASN C ND2 1 
ATOM   1982 N  N   . LYS C 1 74 ? 15.069  -32.567 5.489   1.00 38.48  ? 73  LYS C N   1 
ATOM   1983 C  CA  . LYS C 1 74 ? 13.823  -33.294 5.356   1.00 40.37  ? 73  LYS C CA  1 
ATOM   1984 C  C   . LYS C 1 74 ? 13.534  -34.208 6.532   1.00 50.40  ? 73  LYS C C   1 
ATOM   1985 O  O   . LYS C 1 74 ? 12.427  -34.758 6.606   1.00 61.18  ? 73  LYS C O   1 
ATOM   1986 C  CB  . LYS C 1 74 ? 13.858  -34.108 4.059   1.00 38.48  ? 73  LYS C CB  1 
ATOM   1987 C  CG  . LYS C 1 74 ? 14.337  -33.308 2.854   1.00 58.37  ? 73  LYS C CG  1 
ATOM   1988 C  CD  . LYS C 1 74 ? 13.370  -32.169 2.531   1.00 52.40  ? 73  LYS C CD  1 
ATOM   1989 C  CE  . LYS C 1 74 ? 13.913  -31.222 1.465   1.00 59.92  ? 73  LYS C CE  1 
ATOM   1990 N  NZ  . LYS C 1 74 ? 13.554  -31.643 0.074   1.00 58.50  ? 73  LYS C NZ  1 
ATOM   1991 N  N   . ARG C 1 75 ? 14.494  -34.380 7.442   1.00 45.94  ? 74  ARG C N   1 
ATOM   1992 C  CA  . ARG C 1 75 ? 14.318  -35.297 8.559   1.00 40.05  ? 74  ARG C CA  1 
ATOM   1993 C  C   . ARG C 1 75 ? 13.118  -34.880 9.398   1.00 43.43  ? 74  ARG C C   1 
ATOM   1994 O  O   . ARG C 1 75 ? 12.836  -33.690 9.573   1.00 40.33  ? 74  ARG C O   1 
ATOM   1995 C  CB  . ARG C 1 75 ? 15.590  -35.345 9.413   1.00 42.12  ? 74  ARG C CB  1 
ATOM   1996 C  CG  . ARG C 1 75 ? 16.872  -35.511 8.593   1.00 49.81  ? 74  ARG C CG  1 
ATOM   1997 C  CD  . ARG C 1 75 ? 17.041  -36.929 8.060   1.00 41.79  ? 74  ARG C CD  1 
ATOM   1998 N  NE  . ARG C 1 75 ? 17.318  -37.836 9.162   1.00 46.26  ? 74  ARG C NE  1 
ATOM   1999 C  CZ  . ARG C 1 75 ? 18.532  -38.173 9.572   1.00 53.54  ? 74  ARG C CZ  1 
ATOM   2000 N  NH1 . ARG C 1 75 ? 19.621  -37.767 8.932   1.00 45.09  ? 74  ARG C NH1 1 
ATOM   2001 N  NH2 . ARG C 1 75 ? 18.657  -38.924 10.657  1.00 40.91  ? 74  ARG C NH2 1 
ATOM   2002 N  N   . LYS C 1 76 ? 12.410  -35.877 9.922   1.00 41.00  ? 75  LYS C N   1 
ATOM   2003 C  CA  . LYS C 1 76 ? 11.116  -35.635 10.547  1.00 43.19  ? 75  LYS C CA  1 
ATOM   2004 C  C   . LYS C 1 76 ? 11.245  -34.667 11.713  1.00 47.17  ? 75  LYS C C   1 
ATOM   2005 O  O   . LYS C 1 76 ? 12.108  -34.831 12.583  1.00 41.40  ? 75  LYS C O   1 
ATOM   2006 C  CB  . LYS C 1 76 ? 10.498  -36.955 11.022  1.00 44.21  ? 75  LYS C CB  1 
ATOM   2007 C  CG  . LYS C 1 76 ? 8.966   -36.927 11.144  1.00 55.38  ? 75  LYS C CG  1 
ATOM   2008 C  CD  . LYS C 1 76 ? 8.494   -36.292 12.459  1.00 60.05  ? 75  LYS C CD  1 
ATOM   2009 C  CE  . LYS C 1 76 ? 7.194   -35.502 12.277  1.00 64.24  ? 75  LYS C CE  1 
ATOM   2010 N  NZ  . LYS C 1 76 ? 6.882   -34.627 13.457  1.00 66.04  ? 75  LYS C NZ  1 
ATOM   2011 N  N   . GLY C 1 77 ? 10.379  -33.651 11.723  1.00 45.67  ? 76  GLY C N   1 
ATOM   2012 C  CA  . GLY C 1 77 ? 10.326  -32.692 12.801  1.00 38.72  ? 76  GLY C CA  1 
ATOM   2013 C  C   . GLY C 1 77 ? 11.355  -31.590 12.727  1.00 31.36  ? 76  GLY C C   1 
ATOM   2014 O  O   . GLY C 1 77 ? 11.264  -30.636 13.502  1.00 31.60  ? 76  GLY C O   1 
ATOM   2015 N  N   . PHE C 1 78 ? 12.330  -31.690 11.823  1.00 29.67  ? 77  PHE C N   1 
ATOM   2016 C  CA  . PHE C 1 78 ? 13.447  -30.755 11.835  1.00 29.88  ? 77  PHE C CA  1 
ATOM   2017 C  C   . PHE C 1 78 ? 12.976  -29.341 11.534  1.00 28.49  ? 77  PHE C C   1 
ATOM   2018 O  O   . PHE C 1 78 ? 13.340  -28.391 12.235  1.00 28.21  ? 77  PHE C O   1 
ATOM   2019 C  CB  . PHE C 1 78 ? 14.507  -31.182 10.819  1.00 33.43  ? 77  PHE C CB  1 
ATOM   2020 C  CG  . PHE C 1 78 ? 15.809  -30.459 10.976  1.00 31.30  ? 77  PHE C CG  1 
ATOM   2021 C  CD1 . PHE C 1 78 ? 16.790  -30.958 11.796  1.00 28.11  ? 77  PHE C CD1 1 
ATOM   2022 C  CD2 . PHE C 1 78 ? 16.035  -29.256 10.323  1.00 28.01  ? 77  PHE C CD2 1 
ATOM   2023 C  CE1 . PHE C 1 78 ? 17.981  -30.306 11.963  1.00 26.85  ? 77  PHE C CE1 1 
ATOM   2024 C  CE2 . PHE C 1 78 ? 17.238  -28.582 10.486  1.00 37.32  ? 77  PHE C CE2 1 
ATOM   2025 C  CZ  . PHE C 1 78 ? 18.213  -29.104 11.314  1.00 34.98  ? 77  PHE C CZ  1 
ATOM   2026 N  N   . ASN C 1 79 ? 12.169  -29.183 10.484  1.00 31.33  ? 78  ASN C N   1 
ATOM   2027 C  CA  . ASN C 1 79 ? 11.817  -27.831 10.065  1.00 26.75  ? 78  ASN C CA  1 
ATOM   2028 C  C   . ASN C 1 79 ? 10.850  -27.166 11.035  1.00 32.09  ? 78  ASN C C   1 
ATOM   2029 O  O   . ASN C 1 79 ? 10.916  -25.941 11.231  1.00 30.90  ? 78  ASN C O   1 
ATOM   2030 C  CB  . ASN C 1 79 ? 11.251  -27.856 8.648   1.00 29.41  ? 78  ASN C CB  1 
ATOM   2031 C  CG  . ASN C 1 79 ? 12.287  -28.268 7.625   1.00 36.38  ? 78  ASN C CG  1 
ATOM   2032 O  OD1 . ASN C 1 79 ? 13.483  -28.012 7.790   1.00 31.77  ? 78  ASN C OD1 1 
ATOM   2033 N  ND2 . ASN C 1 79 ? 11.831  -28.902 6.550   1.00 30.94  ? 78  ASN C ND2 1 
ATOM   2034 N  N   . GLU C 1 80 ? 9.955   -27.931 11.661  1.00 33.45  ? 79  GLU C N   1 
ATOM   2035 C  CA  . GLU C 1 80 ? 9.188   -27.351 12.754  1.00 32.08  ? 79  GLU C CA  1 
ATOM   2036 C  C   . GLU C 1 80 ? 10.104  -26.938 13.897  1.00 32.81  ? 79  GLU C C   1 
ATOM   2037 O  O   . GLU C 1 80 ? 9.901   -25.885 14.505  1.00 30.70  ? 79  GLU C O   1 
ATOM   2038 C  CB  . GLU C 1 80 ? 8.113   -28.325 13.236  1.00 34.67  ? 79  GLU C CB  1 
ATOM   2039 C  CG  . GLU C 1 80 ? 7.210   -27.753 14.307  1.00 42.97  ? 79  GLU C CG  1 
ATOM   2040 C  CD  . GLU C 1 80 ? 5.875   -28.468 14.363  1.00 45.27  ? 79  GLU C CD  1 
ATOM   2041 O  OE1 . GLU C 1 80 ? 5.744   -29.514 13.688  1.00 51.40  ? 79  GLU C OE1 1 
ATOM   2042 O  OE2 . GLU C 1 80 ? 4.961   -27.984 15.068  1.00 46.15  ? 79  GLU C OE2 1 
ATOM   2043 N  N   . GLY C 1 81 ? 11.149  -27.730 14.179  1.00 32.02  ? 80  GLY C N   1 
ATOM   2044 C  CA  . GLY C 1 81 ? 12.106  -27.332 15.204  1.00 29.34  ? 80  GLY C CA  1 
ATOM   2045 C  C   . GLY C 1 81 ? 12.828  -26.038 14.871  1.00 29.03  ? 80  GLY C C   1 
ATOM   2046 O  O   . GLY C 1 81 ? 13.083  -25.209 15.752  1.00 31.44  ? 80  GLY C O   1 
ATOM   2047 N  N   . LEU C 1 82 ? 13.183  -25.859 13.593  1.00 28.06  ? 81  LEU C N   1 
ATOM   2048 C  CA  . LEU C 1 82 ? 13.779  -24.604 13.160  1.00 28.25  ? 81  LEU C CA  1 
ATOM   2049 C  C   . LEU C 1 82 ? 12.844  -23.435 13.431  1.00 27.09  ? 81  LEU C C   1 
ATOM   2050 O  O   . LEU C 1 82 ? 13.295  -22.349 13.798  1.00 31.20  ? 81  LEU C O   1 
ATOM   2051 C  CB  . LEU C 1 82 ? 14.134  -24.663 11.674  1.00 26.45  ? 81  LEU C CB  1 
ATOM   2052 C  CG  . LEU C 1 82 ? 15.348  -25.497 11.258  1.00 30.33  ? 81  LEU C CG  1 
ATOM   2053 C  CD1 . LEU C 1 82 ? 15.481  -25.507 9.717   1.00 30.78  ? 81  LEU C CD1 1 
ATOM   2054 C  CD2 . LEU C 1 82 ? 16.629  -25.005 11.910  1.00 30.81  ? 81  LEU C CD2 1 
ATOM   2055 N  N   . TRP C 1 83 ? 11.538  -23.631 13.237  1.00 27.31  ? 82  TRP C N   1 
ATOM   2056 C  CA  . TRP C 1 83 ? 10.604  -22.539 13.499  1.00 31.52  ? 82  TRP C CA  1 
ATOM   2057 C  C   . TRP C 1 83 ? 10.553  -22.216 14.989  1.00 31.90  ? 82  TRP C C   1 
ATOM   2058 O  O   . TRP C 1 83 ? 10.557  -21.044 15.380  1.00 31.86  ? 82  TRP C O   1 
ATOM   2059 C  CB  . TRP C 1 83 ? 9.210   -22.889 12.974  1.00 34.36  ? 82  TRP C CB  1 
ATOM   2060 C  CG  . TRP C 1 83 ? 8.215   -21.746 13.119  1.00 34.74  ? 82  TRP C CG  1 
ATOM   2061 C  CD1 . TRP C 1 83 ? 7.904   -20.800 12.174  1.00 32.02  ? 82  TRP C CD1 1 
ATOM   2062 C  CD2 . TRP C 1 83 ? 7.429   -21.425 14.282  1.00 34.20  ? 82  TRP C CD2 1 
ATOM   2063 N  NE1 . TRP C 1 83 ? 6.963   -19.924 12.675  1.00 34.88  ? 82  TRP C NE1 1 
ATOM   2064 C  CE2 . TRP C 1 83 ? 6.660   -20.284 13.966  1.00 34.78  ? 82  TRP C CE2 1 
ATOM   2065 C  CE3 . TRP C 1 83 ? 7.300   -21.998 15.554  1.00 42.68  ? 82  TRP C CE3 1 
ATOM   2066 C  CZ2 . TRP C 1 83 ? 5.780   -19.702 14.878  1.00 43.65  ? 82  TRP C CZ2 1 
ATOM   2067 C  CZ3 . TRP C 1 83 ? 6.422   -21.416 16.458  1.00 41.30  ? 82  TRP C CZ3 1 
ATOM   2068 C  CH2 . TRP C 1 83 ? 5.674   -20.281 16.116  1.00 41.27  ? 82  TRP C CH2 1 
ATOM   2069 N  N   . GLU C 1 84 ? 10.541  -23.248 15.831  1.00 35.01  ? 83  GLU C N   1 
ATOM   2070 C  CA  . GLU C 1 84 ? 10.443  -23.039 17.273  1.00 31.04  ? 83  GLU C CA  1 
ATOM   2071 C  C   . GLU C 1 84 ? 11.661  -22.301 17.814  1.00 38.61  ? 83  GLU C C   1 
ATOM   2072 O  O   . GLU C 1 84 ? 11.521  -21.328 18.561  1.00 38.57  ? 83  GLU C O   1 
ATOM   2073 C  CB  . GLU C 1 84 ? 10.261  -24.378 17.977  1.00 32.94  ? 83  GLU C CB  1 
ATOM   2074 C  CG  . GLU C 1 84 ? 8.933   -25.023 17.670  1.00 35.60  ? 83  GLU C CG  1 
ATOM   2075 C  CD  . GLU C 1 84 ? 8.792   -26.358 18.330  1.00 46.40  ? 83  GLU C CD  1 
ATOM   2076 O  OE1 . GLU C 1 84 ? 9.821   -26.857 18.827  1.00 42.68  ? 83  GLU C OE1 1 
ATOM   2077 O  OE2 . GLU C 1 84 ? 7.670   -26.909 18.338  1.00 51.81  ? 83  GLU C OE2 1 
ATOM   2078 N  N   . ILE C 1 85 ? 12.867  -22.727 17.428  1.00 33.61  ? 84  ILE C N   1 
ATOM   2079 C  CA  . ILE C 1 85 ? 14.073  -22.131 18.001  1.00 36.68  ? 84  ILE C CA  1 
ATOM   2080 C  C   . ILE C 1 85 ? 14.177  -20.654 17.653  1.00 44.66  ? 84  ILE C C   1 
ATOM   2081 O  O   . ILE C 1 85 ? 14.670  -19.851 18.457  1.00 41.31  ? 84  ILE C O   1 
ATOM   2082 C  CB  . ILE C 1 85 ? 15.332  -22.912 17.567  1.00 43.29  ? 84  ILE C CB  1 
ATOM   2083 C  CG1 . ILE C 1 85 ? 16.520  -22.550 18.466  1.00 38.39  ? 84  ILE C CG1 1 
ATOM   2084 C  CG2 . ILE C 1 85 ? 15.667  -22.672 16.099  1.00 30.44  ? 84  ILE C CG2 1 
ATOM   2085 C  CD1 . ILE C 1 85 ? 17.669  -23.561 18.422  1.00 33.55  ? 84  ILE C CD1 1 
ATOM   2086 N  N   . GLN C 1 86 ? 13.695  -20.262 16.477  1.00 31.35  ? 85  GLN C N   1 
ATOM   2087 C  CA  . GLN C 1 86 ? 13.754  -18.869 16.066  1.00 42.17  ? 85  GLN C CA  1 
ATOM   2088 C  C   . GLN C 1 86 ? 12.605  -18.042 16.618  1.00 43.84  ? 85  GLN C C   1 
ATOM   2089 O  O   . GLN C 1 86 ? 12.807  -16.868 16.958  1.00 40.44  ? 85  GLN C O   1 
ATOM   2090 C  CB  . GLN C 1 86 ? 13.756  -18.774 14.543  1.00 37.07  ? 85  GLN C CB  1 
ATOM   2091 C  CG  . GLN C 1 86 ? 14.063  -17.379 14.042  1.00 41.17  ? 85  GLN C CG  1 
ATOM   2092 C  CD  . GLN C 1 86 ? 14.399  -17.345 12.574  1.00 44.39  ? 85  GLN C CD  1 
ATOM   2093 O  OE1 . GLN C 1 86 ? 14.297  -18.363 11.871  1.00 44.15  ? 85  GLN C OE1 1 
ATOM   2094 N  NE2 . GLN C 1 86 ? 14.814  -16.172 12.096  1.00 48.69  ? 85  GLN C NE2 1 
ATOM   2095 N  N   . ASN C 1 87 ? 11.419  -18.636 16.754  1.00 32.20  ? 86  ASN C N   1 
ATOM   2096 C  CA  . ASN C 1 87 ? 10.213  -17.871 17.037  1.00 42.18  ? 86  ASN C CA  1 
ATOM   2097 C  C   . ASN C 1 87 ? 9.640   -18.071 18.426  1.00 45.26  ? 86  ASN C C   1 
ATOM   2098 O  O   . ASN C 1 87 ? 9.100   -17.113 18.982  1.00 48.47  ? 86  ASN C O   1 
ATOM   2099 C  CB  . ASN C 1 87 ? 9.133   -18.197 16.007  1.00 35.97  ? 86  ASN C CB  1 
ATOM   2100 C  CG  . ASN C 1 87 ? 9.490   -17.660 14.652  1.00 40.42  ? 86  ASN C CG  1 
ATOM   2101 O  OD1 . ASN C 1 87 ? 9.477   -16.451 14.442  1.00 37.55  ? 86  ASN C OD1 1 
ATOM   2102 N  ND2 . ASN C 1 87 ? 9.859   -18.546 13.734  1.00 34.54  ? 86  ASN C ND2 1 
ATOM   2103 N  N   . ASN C 1 88 ? 9.722   -19.276 18.996  1.00 47.62  ? 87  ASN C N   1 
ATOM   2104 C  CA  . ASN C 1 88 ? 9.162   -19.560 20.322  1.00 46.05  ? 87  ASN C CA  1 
ATOM   2105 C  C   . ASN C 1 88 ? 10.114  -20.475 21.090  1.00 45.76  ? 87  ASN C C   1 
ATOM   2106 O  O   . ASN C 1 88 ? 9.790   -21.630 21.397  1.00 54.11  ? 87  ASN C O   1 
ATOM   2107 C  CB  . ASN C 1 88 ? 7.767   -20.180 20.198  1.00 47.94  ? 87  ASN C CB  1 
ATOM   2108 C  CG  . ASN C 1 88 ? 6.972   -20.099 21.500  1.00 57.97  ? 87  ASN C CG  1 
ATOM   2109 O  OD1 . ASN C 1 88 ? 7.325   -19.342 22.409  1.00 62.55  ? 87  ASN C OD1 1 
ATOM   2110 N  ND2 . ASN C 1 88 ? 5.898   -20.877 21.591  1.00 58.27  ? 87  ASN C ND2 1 
ATOM   2111 N  N   . PRO C 1 89 ? 11.306  -19.976 21.434  1.00 41.89  ? 88  PRO C N   1 
ATOM   2112 C  CA  . PRO C 1 89 ? 12.348  -20.871 21.958  1.00 44.02  ? 88  PRO C CA  1 
ATOM   2113 C  C   . PRO C 1 89 ? 12.213  -21.218 23.430  1.00 59.58  ? 88  PRO C C   1 
ATOM   2114 O  O   . PRO C 1 89 ? 12.735  -22.262 23.845  1.00 54.23  ? 88  PRO C O   1 
ATOM   2115 C  CB  . PRO C 1 89 ? 13.635  -20.079 21.702  1.00 42.54  ? 88  PRO C CB  1 
ATOM   2116 C  CG  . PRO C 1 89 ? 13.206  -18.651 21.795  1.00 55.08  ? 88  PRO C CG  1 
ATOM   2117 C  CD  . PRO C 1 89 ? 11.798  -18.597 21.262  1.00 50.78  ? 88  PRO C CD  1 
ATOM   2118 N  N   . HIS C 1 90 ? 11.548  -20.388 24.235  1.00 65.47  ? 89  HIS C N   1 
ATOM   2119 C  CA  . HIS C 1 90 ? 11.476  -20.613 25.674  1.00 54.99  ? 89  HIS C CA  1 
ATOM   2120 C  C   . HIS C 1 90 ? 10.069  -20.951 26.148  1.00 51.01  ? 89  HIS C C   1 
ATOM   2121 O  O   . HIS C 1 90 ? 9.795   -20.891 27.350  1.00 68.12  ? 89  HIS C O   1 
ATOM   2122 C  CB  . HIS C 1 90 ? 12.036  -19.407 26.420  1.00 52.04  ? 89  HIS C CB  1 
ATOM   2123 C  CG  . HIS C 1 90 ? 13.466  -19.120 26.084  1.00 52.10  ? 89  HIS C CG  1 
ATOM   2124 N  ND1 . HIS C 1 90 ? 13.859  -18.001 25.377  1.00 61.23  ? 89  HIS C ND1 1 
ATOM   2125 C  CD2 . HIS C 1 90 ? 14.596  -19.823 26.334  1.00 61.17  ? 89  HIS C CD2 1 
ATOM   2126 C  CE1 . HIS C 1 90 ? 15.170  -18.020 25.217  1.00 51.15  ? 89  HIS C CE1 1 
ATOM   2127 N  NE2 . HIS C 1 90 ? 15.642  -19.114 25.790  1.00 61.03  ? 89  HIS C NE2 1 
ATOM   2128 N  N   . ALA C 1 91 ? 9.173   -21.315 25.233  1.00 55.99  ? 90  ALA C N   1 
ATOM   2129 C  CA  . ALA C 1 91 ? 7.921   -21.928 25.646  1.00 63.22  ? 90  ALA C CA  1 
ATOM   2130 C  C   . ALA C 1 91 ? 8.229   -23.160 26.482  1.00 81.89  ? 90  ALA C C   1 
ATOM   2131 O  O   . ALA C 1 91 ? 9.150   -23.921 26.174  1.00 82.90  ? 90  ALA C O   1 
ATOM   2132 C  CB  . ALA C 1 91 ? 7.073   -22.308 24.432  1.00 60.86  ? 90  ALA C CB  1 
ATOM   2133 N  N   . SER C 1 92 ? 7.472   -23.349 27.565  1.00 78.06  ? 91  SER C N   1 
ATOM   2134 C  CA  . SER C 1 92 ? 7.718   -24.509 28.413  1.00 80.83  ? 91  SER C CA  1 
ATOM   2135 C  C   . SER C 1 92 ? 7.549   -25.821 27.651  1.00 82.33  ? 91  SER C C   1 
ATOM   2136 O  O   . SER C 1 92 ? 8.105   -26.842 28.074  1.00 83.51  ? 91  SER C O   1 
ATOM   2137 C  CB  . SER C 1 92 ? 6.797   -24.475 29.634  1.00 71.95  ? 91  SER C CB  1 
ATOM   2138 O  OG  . SER C 1 92 ? 5.486   -24.889 29.295  1.00 78.61  ? 91  SER C OG  1 
ATOM   2139 N  N   . TYR C 1 93 ? 6.820   -25.806 26.531  1.00 79.62  ? 92  TYR C N   1 
ATOM   2140 C  CA  . TYR C 1 93 ? 6.579   -26.983 25.683  1.00 75.17  ? 92  TYR C CA  1 
ATOM   2141 C  C   . TYR C 1 93 ? 6.212   -28.226 26.487  1.00 74.25  ? 92  TYR C C   1 
ATOM   2142 O  O   . TYR C 1 93 ? 6.201   -29.335 25.957  1.00 82.07  ? 92  TYR C O   1 
ATOM   2143 C  CB  . TYR C 1 93 ? 7.800   -27.278 24.796  1.00 70.06  ? 92  TYR C CB  1 
ATOM   2144 C  CG  . TYR C 1 93 ? 7.989   -26.290 23.660  1.00 66.10  ? 92  TYR C CG  1 
ATOM   2145 C  CD1 . TYR C 1 93 ? 7.041   -26.170 22.649  1.00 71.87  ? 92  TYR C CD1 1 
ATOM   2146 C  CD2 . TYR C 1 93 ? 9.116   -25.481 23.595  1.00 64.27  ? 92  TYR C CD2 1 
ATOM   2147 C  CE1 . TYR C 1 93 ? 7.207   -25.260 21.607  1.00 67.19  ? 92  TYR C CE1 1 
ATOM   2148 C  CE2 . TYR C 1 93 ? 9.290   -24.567 22.560  1.00 62.85  ? 92  TYR C CE2 1 
ATOM   2149 C  CZ  . TYR C 1 93 ? 8.333   -24.463 21.569  1.00 65.05  ? 92  TYR C CZ  1 
ATOM   2150 O  OH  . TYR C 1 93 ? 8.501   -23.555 20.546  1.00 62.11  ? 92  TYR C OH  1 
HETATM 2151 BR BR4 . BYZ D 2 .  ? -0.162  -23.649 -1.842  0.62 80.42  ? 101 BYZ A BR4 1 
HETATM 2152 C  C4  . BYZ D 2 .  ? 1.263   -24.356 -2.843  0.62 29.22  ? 101 BYZ A C4  1 
HETATM 2153 C  C5  . BYZ D 2 .  ? 2.578   -24.559 -2.448  0.62 25.96  ? 101 BYZ A C5  1 
HETATM 2154 N  N1  . BYZ D 2 .  ? 3.279   -25.089 -3.444  0.62 31.25  ? 101 BYZ A N1  1 
HETATM 2155 N  N2  . BYZ D 2 .  ? 2.408   -25.225 -4.473  0.62 42.81  ? 101 BYZ A N2  1 
HETATM 2156 C  C3  . BYZ D 2 .  ? 1.188   -24.792 -4.141  0.62 33.45  ? 101 BYZ A C3  1 
HETATM 2157 S  S   . SO4 E 3 .  ? 8.067   -29.434 5.744   0.70 32.74  ? 102 SO4 A S   1 
HETATM 2158 O  O1  . SO4 E 3 .  ? 7.712   -30.612 4.878   0.70 33.53  ? 102 SO4 A O1  1 
HETATM 2159 O  O2  . SO4 E 3 .  ? 8.686   -28.398 4.865   0.70 33.10  ? 102 SO4 A O2  1 
HETATM 2160 O  O3  . SO4 E 3 .  ? 6.841   -28.951 6.473   0.70 30.31  ? 102 SO4 A O3  1 
HETATM 2161 O  O4  . SO4 E 3 .  ? 9.101   -29.810 6.758   0.70 37.75  ? 102 SO4 A O4  1 
HETATM 2162 S  S   . SO4 F 3 .  ? 0.369   -32.952 1.592   1.00 86.54  ? 103 SO4 A S   1 
HETATM 2163 O  O1  . SO4 F 3 .  ? 1.402   -33.732 0.829   1.00 53.31  ? 103 SO4 A O1  1 
HETATM 2164 O  O2  . SO4 F 3 .  ? 0.898   -31.595 1.954   1.00 61.44  ? 103 SO4 A O2  1 
HETATM 2165 O  O3  . SO4 F 3 .  ? -0.848  -32.792 0.729   1.00 75.82  ? 103 SO4 A O3  1 
HETATM 2166 O  O4  . SO4 F 3 .  ? -0.001  -33.675 2.856   1.00 66.63  ? 103 SO4 A O4  1 
HETATM 2167 S  S   . SO4 G 3 .  ? -10.403 -23.957 1.369   1.00 87.92  ? 104 SO4 A S   1 
HETATM 2168 O  O1  . SO4 G 3 .  ? -10.685 -23.287 0.052   1.00 62.54  ? 104 SO4 A O1  1 
HETATM 2169 O  O2  . SO4 G 3 .  ? -10.234 -22.921 2.440   1.00 66.75  ? 104 SO4 A O2  1 
HETATM 2170 O  O3  . SO4 G 3 .  ? -11.533 -24.887 1.715   1.00 76.19  ? 104 SO4 A O3  1 
HETATM 2171 O  O4  . SO4 G 3 .  ? -9.128  -24.745 1.302   1.00 62.51  ? 104 SO4 A O4  1 
HETATM 2172 S  S   . SO4 H 3 .  ? 6.852   -8.464  -24.595 1.00 58.55  ? 101 SO4 B S   1 
HETATM 2173 O  O1  . SO4 H 3 .  ? 8.085   -8.209  -25.417 1.00 41.56  ? 101 SO4 B O1  1 
HETATM 2174 O  O2  . SO4 H 3 .  ? 5.990   -9.455  -25.320 1.00 58.20  ? 101 SO4 B O2  1 
HETATM 2175 O  O3  . SO4 H 3 .  ? 7.225   -8.990  -23.232 1.00 46.78  ? 101 SO4 B O3  1 
HETATM 2176 O  O4  . SO4 H 3 .  ? 6.079   -7.188  -24.421 1.00 69.13  ? 101 SO4 B O4  1 
HETATM 2177 S  S   . SO4 I 3 .  ? 13.955  -26.494 -26.380 0.81 60.85  ? 102 SO4 B S   1 
HETATM 2178 O  O1  . SO4 I 3 .  ? 15.426  -26.447 -26.103 0.81 47.65  ? 102 SO4 B O1  1 
HETATM 2179 O  O2  . SO4 I 3 .  ? 13.639  -25.994 -27.758 0.81 64.24  ? 102 SO4 B O2  1 
HETATM 2180 O  O3  . SO4 I 3 .  ? 13.469  -27.907 -26.267 0.81 65.40  ? 102 SO4 B O3  1 
HETATM 2181 O  O4  . SO4 I 3 .  ? 13.268  -25.640 -25.360 0.81 63.00  ? 102 SO4 B O4  1 
HETATM 2182 S  S   . DMS J 4 .  ? 16.617  -14.184 -25.315 1.00 45.82  ? 103 DMS B S   1 
HETATM 2183 O  O   . DMS J 4 .  ? 17.665  -13.531 -24.442 1.00 47.95  ? 103 DMS B O   1 
HETATM 2184 C  C1  . DMS J 4 .  ? 15.487  -14.862 -24.095 1.00 47.93  ? 103 DMS B C1  1 
HETATM 2185 C  C2  . DMS J 4 .  ? 17.238  -15.792 -25.868 1.00 44.10  ? 103 DMS B C2  1 
HETATM 2186 BR BR4 . BYZ K 2 .  ? 18.439  -35.601 17.427  0.63 88.06  ? 101 BYZ C BR4 1 
HETATM 2187 C  C4  . BYZ K 2 .  ? 16.599  -35.637 17.817  0.63 34.75  ? 101 BYZ C C4  1 
HETATM 2188 C  C5  . BYZ K 2 .  ? 15.532  -35.388 16.968  0.63 32.63  ? 101 BYZ C C5  1 
HETATM 2189 N  N1  . BYZ K 2 .  ? 14.383  -35.530 17.617  0.63 42.69  ? 101 BYZ C N1  1 
HETATM 2190 N  N2  . BYZ K 2 .  ? 14.720  -35.870 18.883  0.63 46.55  ? 101 BYZ C N2  1 
HETATM 2191 C  C3  . BYZ K 2 .  ? 16.044  -35.943 19.035  0.63 52.36  ? 101 BYZ C C3  1 
HETATM 2192 S  S   . SO4 L 3 .  ? 27.084  -39.297 24.471  1.00 91.21  ? 102 SO4 C S   1 
HETATM 2193 O  O1  . SO4 L 3 .  ? 26.582  -39.667 23.101  1.00 73.54  ? 102 SO4 C O1  1 
HETATM 2194 O  O2  . SO4 L 3 .  ? 27.371  -37.822 24.587  1.00 63.07  ? 102 SO4 C O2  1 
HETATM 2195 O  O3  . SO4 L 3 .  ? 26.055  -39.671 25.504  1.00 79.69  ? 102 SO4 C O3  1 
HETATM 2196 O  O4  . SO4 L 3 .  ? 28.349  -40.062 24.726  1.00 80.22  ? 102 SO4 C O4  1 
HETATM 2197 S  S   . SO4 M 3 .  ? 14.223  -39.599 10.454  1.00 93.69  ? 103 SO4 C S   1 
HETATM 2198 O  O1  . SO4 M 3 .  ? 14.393  -40.803 9.572   1.00 84.71  ? 103 SO4 C O1  1 
HETATM 2199 O  O2  . SO4 M 3 .  ? 14.726  -38.388 9.722   1.00 70.52  ? 103 SO4 C O2  1 
HETATM 2200 O  O3  . SO4 M 3 .  ? 12.767  -39.434 10.795  1.00 81.62  ? 103 SO4 C O3  1 
HETATM 2201 O  O4  . SO4 M 3 .  ? 15.010  -39.773 11.723  1.00 77.05  ? 103 SO4 C O4  1 
HETATM 2202 S  S   . SO4 N 3 .  ? 28.936  -38.347 12.393  1.00 72.63  ? 104 SO4 C S   1 
HETATM 2203 O  O1  . SO4 N 3 .  ? 30.219  -38.882 11.828  1.00 72.31  ? 104 SO4 C O1  1 
HETATM 2204 O  O2  . SO4 N 3 .  ? 28.190  -39.494 13.007  1.00 47.05  ? 104 SO4 C O2  1 
HETATM 2205 O  O3  . SO4 N 3 .  ? 29.201  -37.308 13.453  1.00 69.05  ? 104 SO4 C O3  1 
HETATM 2206 O  O4  . SO4 N 3 .  ? 28.146  -37.746 11.264  1.00 63.93  ? 104 SO4 C O4  1 
HETATM 2207 O  O   . HOH O 5 .  ? -0.962  -33.216 4.875   1.00 62.13  ? 201 HOH A O   1 
HETATM 2208 O  O   . HOH O 5 .  ? 1.702   -4.327  -9.909  1.00 36.40  ? 202 HOH A O   1 
HETATM 2209 O  O   . HOH O 5 .  ? 9.904   -29.739 3.238   1.00 47.19  ? 203 HOH A O   1 
HETATM 2210 O  O   . HOH O 5 .  ? 14.252  -19.084 -7.138  1.00 44.98  ? 204 HOH A O   1 
HETATM 2211 O  O   . HOH O 5 .  ? 8.422   -17.822 -11.108 1.00 36.01  ? 205 HOH A O   1 
HETATM 2212 O  O   . HOH O 5 .  ? 19.413  -15.654 7.049   1.00 31.51  ? 206 HOH A O   1 
HETATM 2213 O  O   . HOH O 5 .  ? 4.404   -3.346  -3.239  1.00 41.40  ? 207 HOH A O   1 
HETATM 2214 O  O   . HOH O 5 .  ? 12.176  -13.419 -9.239  1.00 52.34  ? 208 HOH A O   1 
HETATM 2215 O  O   . HOH O 5 .  ? 10.607  -23.700 9.675   1.00 33.34  ? 209 HOH A O   1 
HETATM 2216 O  O   . HOH O 5 .  ? 1.793   -1.458  -0.403  1.00 46.19  ? 210 HOH A O   1 
HETATM 2217 O  O   . HOH O 5 .  ? 12.723  -11.983 7.811   1.00 45.73  ? 211 HOH A O   1 
HETATM 2218 O  O   . HOH O 5 .  ? 6.744   -10.253 -11.974 1.00 38.87  ? 212 HOH A O   1 
HETATM 2219 O  O   . HOH O 5 .  ? -1.097  -20.539 7.073   1.00 33.52  ? 213 HOH A O   1 
HETATM 2220 O  O   . HOH O 5 .  ? 1.956   -24.633 -10.031 1.00 38.06  ? 214 HOH A O   1 
HETATM 2221 O  O   . HOH O 5 .  ? 11.805  -18.231 -8.210  1.00 39.69  ? 215 HOH A O   1 
HETATM 2222 O  O   . HOH O 5 .  ? 10.499  -4.941  -7.497  1.00 41.21  ? 216 HOH A O   1 
HETATM 2223 O  O   . HOH O 5 .  ? 11.160  -12.238 6.188   1.00 42.35  ? 217 HOH A O   1 
HETATM 2224 O  O   . HOH O 5 .  ? 4.477   -7.613  1.156   1.00 34.19  ? 218 HOH A O   1 
HETATM 2225 O  O   . HOH O 5 .  ? 15.316  -24.625 1.693   1.00 43.81  ? 219 HOH A O   1 
HETATM 2226 O  O   . HOH O 5 .  ? 8.844   -22.269 -9.442  1.00 33.47  ? 220 HOH A O   1 
HETATM 2227 O  O   . HOH O 5 .  ? -2.318  -21.475 -0.461  1.00 29.61  ? 221 HOH A O   1 
HETATM 2228 O  O   . HOH O 5 .  ? 2.987   -11.833 -24.837 1.00 54.87  ? 222 HOH A O   1 
HETATM 2229 O  O   . HOH O 5 .  ? 16.773  -13.098 1.213   1.00 26.57  ? 223 HOH A O   1 
HETATM 2230 O  O   . HOH O 5 .  ? -8.853  -20.705 -1.448  1.00 51.02  ? 224 HOH A O   1 
HETATM 2231 O  O   . HOH O 5 .  ? 3.535   -16.618 13.687  1.00 51.35  ? 225 HOH A O   1 
HETATM 2232 O  O   . HOH O 5 .  ? 5.114   -7.931  4.069   1.00 41.83  ? 226 HOH A O   1 
HETATM 2233 O  O   . HOH O 5 .  ? -6.246  -24.723 -5.816  1.00 38.62  ? 227 HOH A O   1 
HETATM 2234 O  O   . HOH O 5 .  ? -0.240  -22.425 9.343   1.00 43.70  ? 228 HOH A O   1 
HETATM 2235 O  O   . HOH O 5 .  ? -3.007  3.725   -2.027  1.00 51.45  ? 229 HOH A O   1 
HETATM 2236 O  O   . HOH O 5 .  ? 7.870   -7.809  1.334   1.00 32.02  ? 230 HOH A O   1 
HETATM 2237 O  O   . HOH O 5 .  ? -4.754  -20.837 6.389   1.00 43.19  ? 231 HOH A O   1 
HETATM 2238 O  O   . HOH O 5 .  ? -6.026  -15.323 -8.107  1.00 35.14  ? 232 HOH A O   1 
HETATM 2239 O  O   . HOH O 5 .  ? -5.771  -16.799 -10.209 1.00 59.04  ? 233 HOH A O   1 
HETATM 2240 O  O   . HOH O 5 .  ? 1.613   -24.006 -6.944  0.58 47.57  ? 234 HOH A O   1 
HETATM 2241 O  O   . HOH O 5 .  ? 1.677   -10.296 12.026  1.00 40.83  ? 235 HOH A O   1 
HETATM 2242 O  O   . HOH O 5 .  ? 12.828  -11.868 -4.494  1.00 26.68  ? 236 HOH A O   1 
HETATM 2243 O  O   . HOH O 5 .  ? 1.662   1.505   -6.637  1.00 53.36  ? 237 HOH A O   1 
HETATM 2244 O  O   . HOH O 5 .  ? -1.182  -11.302 11.670  1.00 41.57  ? 238 HOH A O   1 
HETATM 2245 O  O   . HOH O 5 .  ? -6.070  -19.207 -5.925  1.00 48.41  ? 239 HOH A O   1 
HETATM 2246 O  O   . HOH O 5 .  ? -8.202  -15.352 -0.757  1.00 36.85  ? 240 HOH A O   1 
HETATM 2247 O  O   . HOH O 5 .  ? 9.692   -6.059  -1.612  1.00 40.08  ? 241 HOH A O   1 
HETATM 2248 O  O   . HOH O 5 .  ? 2.252   -29.654 -0.288  1.00 50.40  ? 242 HOH A O   1 
HETATM 2249 O  O   . HOH O 5 .  ? -7.244  -12.440 7.015   1.00 52.68  ? 243 HOH A O   1 
HETATM 2250 O  O   . HOH O 5 .  ? 10.995  -16.335 -14.588 1.00 47.50  ? 244 HOH A O   1 
HETATM 2251 O  O   . HOH O 5 .  ? 0.408   -17.536 -18.831 1.00 48.99  ? 245 HOH A O   1 
HETATM 2252 O  O   . HOH O 5 .  ? 8.342   -16.038 -13.213 1.00 38.40  ? 246 HOH A O   1 
HETATM 2253 O  O   . HOH O 5 .  ? 14.431  -28.433 -0.846  1.00 61.72  ? 247 HOH A O   1 
HETATM 2254 O  O   . HOH O 5 .  ? 6.711   -5.737  0.550   1.00 41.76  ? 248 HOH A O   1 
HETATM 2255 O  O   . HOH O 5 .  ? 0.723   -7.953  -13.183 1.00 52.41  ? 249 HOH A O   1 
HETATM 2256 O  O   . HOH O 5 .  ? -8.254  -18.983 -3.239  1.00 49.20  ? 250 HOH A O   1 
HETATM 2257 O  O   . HOH O 5 .  ? -8.487  -16.142 2.024   1.00 43.35  ? 251 HOH A O   1 
HETATM 2258 O  O   . HOH O 5 .  ? -9.812  -13.040 -0.456  1.00 26.97  ? 252 HOH A O   1 
HETATM 2259 O  O   . HOH O 5 .  ? -7.338  -10.806 -7.941  1.00 41.96  ? 253 HOH A O   1 
HETATM 2260 O  O   . HOH O 5 .  ? -6.293  -16.006 -15.665 1.00 63.95  ? 254 HOH A O   1 
HETATM 2261 O  O   . HOH O 5 .  ? 7.163   -17.371 9.376   1.00 41.83  ? 255 HOH A O   1 
HETATM 2262 O  O   . HOH O 5 .  ? -7.856  -20.742 -5.704  1.00 48.66  ? 256 HOH A O   1 
HETATM 2263 O  O   . HOH O 5 .  ? 20.736  -16.773 -3.345  1.00 41.31  ? 257 HOH A O   1 
HETATM 2264 O  O   . HOH O 5 .  ? 15.242  -11.803 -5.693  1.00 52.40  ? 258 HOH A O   1 
HETATM 2265 O  O   . HOH O 5 .  ? 16.761  -12.466 -16.680 1.00 49.25  ? 259 HOH A O   1 
HETATM 2266 O  O   . HOH O 5 .  ? 9.084   -35.973 1.218   1.00 61.91  ? 260 HOH A O   1 
HETATM 2267 O  O   . HOH O 5 .  ? 10.057  -12.093 10.105  1.00 48.41  ? 261 HOH A O   1 
HETATM 2268 O  O   . HOH O 5 .  ? 8.555   -8.822  -13.529 1.00 38.47  ? 262 HOH A O   1 
HETATM 2269 O  O   . HOH O 5 .  ? -4.050  -7.040  -10.460 1.00 42.57  ? 263 HOH A O   1 
HETATM 2270 O  O   . HOH O 5 .  ? 11.625  -12.341 -6.166  1.00 40.91  ? 264 HOH A O   1 
HETATM 2271 O  O   . HOH O 5 .  ? 11.991  -16.037 -11.756 1.00 48.74  ? 265 HOH A O   1 
HETATM 2272 O  O   . HOH O 5 .  ? -6.515  -25.927 3.485   1.00 46.50  ? 266 HOH A O   1 
HETATM 2273 O  O   . HOH O 5 .  ? -3.738  -9.335  11.062  1.00 62.18  ? 267 HOH A O   1 
HETATM 2274 O  O   . HOH O 5 .  ? -9.263  -15.296 -10.958 1.00 59.69  ? 268 HOH A O   1 
HETATM 2275 O  O   . HOH O 5 .  ? -1.358  -27.513 11.432  1.00 56.88  ? 269 HOH A O   1 
HETATM 2276 O  O   . HOH O 5 .  ? -7.120  -18.099 8.326   1.00 65.08  ? 270 HOH A O   1 
HETATM 2277 O  O   . HOH O 5 .  ? -6.655  -22.063 5.969   1.00 48.01  ? 271 HOH A O   1 
HETATM 2278 O  O   . HOH O 5 .  ? 7.870   -8.022  4.487   1.00 39.91  ? 272 HOH A O   1 
HETATM 2279 O  O   . HOH O 5 .  ? 9.057   -9.790  6.463   1.00 46.63  ? 273 HOH A O   1 
HETATM 2280 O  O   . HOH P 5 .  ? 16.175  -25.321 -28.210 1.00 77.38  ? 201 HOH B O   1 
HETATM 2281 O  O   . HOH P 5 .  ? 30.621  -7.766  -29.658 1.00 54.74  ? 202 HOH B O   1 
HETATM 2282 O  O   . HOH P 5 .  ? 11.280  -28.439 -25.955 1.00 60.51  ? 203 HOH B O   1 
HETATM 2283 O  O   . HOH P 5 .  ? 5.931   -11.940 -25.782 1.00 46.20  ? 204 HOH B O   1 
HETATM 2284 O  O   . HOH P 5 .  ? 25.726  -22.460 -30.780 1.00 37.42  ? 205 HOH B O   1 
HETATM 2285 O  O   . HOH P 5 .  ? 30.204  -19.023 -40.063 1.00 40.82  ? 206 HOH B O   1 
HETATM 2286 O  O   . HOH P 5 .  ? 24.195  -1.079  -35.814 1.00 40.28  ? 207 HOH B O   1 
HETATM 2287 O  O   . HOH P 5 .  ? 10.107  -18.296 -32.676 1.00 29.66  ? 208 HOH B O   1 
HETATM 2288 O  O   . HOH P 5 .  ? 22.730  -5.312  -24.592 1.00 50.57  ? 209 HOH B O   1 
HETATM 2289 O  O   . HOH P 5 .  ? 24.494  -4.664  -29.377 1.00 42.07  ? 210 HOH B O   1 
HETATM 2290 O  O   . HOH P 5 .  ? 28.299  -4.736  -41.488 1.00 38.74  ? 211 HOH B O   1 
HETATM 2291 O  O   . HOH P 5 .  ? 12.972  -21.192 -46.262 1.00 48.68  ? 212 HOH B O   1 
HETATM 2292 O  O   . HOH P 5 .  ? 29.708  -23.840 -32.642 1.00 56.93  ? 213 HOH B O   1 
HETATM 2293 O  O   . HOH P 5 .  ? 16.224  -25.292 -34.465 1.00 42.72  ? 214 HOH B O   1 
HETATM 2294 O  O   . HOH P 5 .  ? 20.433  -9.364  -42.336 1.00 43.12  ? 215 HOH B O   1 
HETATM 2295 O  O   . HOH P 5 .  ? 14.590  -23.243 -40.381 1.00 37.25  ? 216 HOH B O   1 
HETATM 2296 O  O   . HOH P 5 .  ? 16.513  -18.676 -28.563 1.00 30.45  ? 217 HOH B O   1 
HETATM 2297 O  O   . HOH P 5 .  ? 25.090  -5.385  -35.095 1.00 39.28  ? 218 HOH B O   1 
HETATM 2298 O  O   . HOH P 5 .  ? 17.843  -0.073  -38.005 1.00 26.52  ? 219 HOH B O   1 
HETATM 2299 O  O   . HOH P 5 .  ? 10.926  -20.325 -43.783 1.00 64.62  ? 220 HOH B O   1 
HETATM 2300 O  O   . HOH P 5 .  ? 26.284  -3.819  -32.701 1.00 48.30  ? 221 HOH B O   1 
HETATM 2301 O  O   . HOH P 5 .  ? 7.462   -18.093 -31.356 1.00 44.88  ? 222 HOH B O   1 
HETATM 2302 O  O   . HOH P 5 .  ? 19.708  -25.162 -33.973 1.00 36.38  ? 223 HOH B O   1 
HETATM 2303 O  O   . HOH P 5 .  ? 13.962  -5.696  -40.697 1.00 42.03  ? 224 HOH B O   1 
HETATM 2304 O  O   . HOH P 5 .  ? 21.440  -2.997  -24.215 1.00 62.28  ? 225 HOH B O   1 
HETATM 2305 O  O   . HOH P 5 .  ? 31.050  -11.486 -38.297 1.00 47.82  ? 226 HOH B O   1 
HETATM 2306 O  O   . HOH P 5 .  ? 21.232  -15.369 -22.730 1.00 53.90  ? 227 HOH B O   1 
HETATM 2307 O  O   . HOH P 5 .  ? 20.960  -5.957  -42.107 1.00 33.70  ? 228 HOH B O   1 
HETATM 2308 O  O   . HOH P 5 .  ? 23.476  -3.671  -36.240 1.00 29.98  ? 229 HOH B O   1 
HETATM 2309 O  O   . HOH P 5 .  ? 30.898  -10.504 -35.844 1.00 43.58  ? 230 HOH B O   1 
HETATM 2310 O  O   . HOH P 5 .  ? 17.576  -11.547 -42.758 1.00 38.08  ? 231 HOH B O   1 
HETATM 2311 O  O   . HOH P 5 .  ? 22.343  -22.697 -28.468 1.00 42.51  ? 232 HOH B O   1 
HETATM 2312 O  O   . HOH P 5 .  ? 20.855  -13.157 -42.270 1.00 45.05  ? 233 HOH B O   1 
HETATM 2313 O  O   . HOH P 5 .  ? 23.443  -1.813  -28.839 1.00 40.83  ? 234 HOH B O   1 
HETATM 2314 O  O   . HOH P 5 .  ? 20.644  4.280   -32.278 1.00 35.96  ? 235 HOH B O   1 
HETATM 2315 O  O   . HOH P 5 .  ? 14.571  -7.575  -42.618 1.00 42.80  ? 236 HOH B O   1 
HETATM 2316 O  O   . HOH P 5 .  ? 10.302  -21.289 -32.579 1.00 36.84  ? 237 HOH B O   1 
HETATM 2317 O  O   . HOH P 5 .  ? 23.485  -11.020 -21.632 1.00 44.85  ? 238 HOH B O   1 
HETATM 2318 O  O   . HOH P 5 .  ? 21.872  -22.821 -25.950 1.00 55.00  ? 239 HOH B O   1 
HETATM 2319 O  O   . HOH P 5 .  ? 27.673  -24.137 -34.959 1.00 38.40  ? 240 HOH B O   1 
HETATM 2320 O  O   . HOH P 5 .  ? 24.650  -6.383  -42.194 1.00 39.65  ? 241 HOH B O   1 
HETATM 2321 O  O   . HOH P 5 .  ? 28.985  -25.773 -30.003 1.00 51.13  ? 242 HOH B O   1 
HETATM 2322 O  O   . HOH P 5 .  ? 8.732   -8.337  -16.049 1.00 43.71  ? 243 HOH B O   1 
HETATM 2323 O  O   . HOH P 5 .  ? 17.318  -8.903  -43.344 1.00 38.19  ? 244 HOH B O   1 
HETATM 2324 O  O   . HOH P 5 .  ? 18.250  5.336   -34.460 1.00 50.17  ? 245 HOH B O   1 
HETATM 2325 O  O   . HOH P 5 .  ? 16.698  -0.154  -24.744 1.00 49.28  ? 246 HOH B O   1 
HETATM 2326 O  O   . HOH P 5 .  ? 31.929  -20.809 -38.003 1.00 49.12  ? 247 HOH B O   1 
HETATM 2327 O  O   . HOH P 5 .  ? 0.438   -10.913 -29.510 1.00 59.83  ? 248 HOH B O   1 
HETATM 2328 O  O   . HOH P 5 .  ? 12.565  -19.990 -19.612 1.00 52.95  ? 249 HOH B O   1 
HETATM 2329 O  O   . HOH P 5 .  ? 14.555  -25.212 -20.586 1.00 51.43  ? 250 HOH B O   1 
HETATM 2330 O  O   . HOH P 5 .  ? 33.627  -10.386 -25.028 1.00 55.08  ? 251 HOH B O   1 
HETATM 2331 O  O   . HOH P 5 .  ? 18.490  -14.895 -46.106 1.00 53.84  ? 252 HOH B O   1 
HETATM 2332 O  O   . HOH P 5 .  ? 7.206   -21.008 -29.715 1.00 41.50  ? 253 HOH B O   1 
HETATM 2333 O  O   . HOH P 5 .  ? 6.836   -9.373  -17.947 1.00 51.79  ? 254 HOH B O   1 
HETATM 2334 O  O   . HOH Q 5 .  ? 26.140  -37.859 10.629  1.00 38.15  ? 201 HOH C O   1 
HETATM 2335 O  O   . HOH Q 5 .  ? 13.964  -20.621 11.602  1.00 47.06  ? 202 HOH C O   1 
HETATM 2336 O  O   . HOH Q 5 .  ? 15.314  -17.844 19.429  1.00 54.41  ? 203 HOH C O   1 
HETATM 2337 O  O   . HOH Q 5 .  ? 25.220  -17.823 14.013  1.00 54.62  ? 204 HOH C O   1 
HETATM 2338 O  O   . HOH Q 5 .  ? 23.274  -18.904 20.735  1.00 72.56  ? 205 HOH C O   1 
HETATM 2339 O  O   . HOH Q 5 .  ? 24.414  -31.248 10.598  1.00 51.26  ? 206 HOH C O   1 
HETATM 2340 O  O   . HOH Q 5 .  ? 30.826  -43.045 12.427  1.00 47.76  ? 207 HOH C O   1 
HETATM 2341 O  O   . HOH Q 5 .  ? 25.210  -19.738 5.865   1.00 46.20  ? 208 HOH C O   1 
HETATM 2342 O  O   . HOH Q 5 .  ? 29.810  -16.512 11.190  1.00 55.89  ? 209 HOH C O   1 
HETATM 2343 O  O   . HOH Q 5 .  ? 25.431  -39.371 12.784  1.00 36.57  ? 210 HOH C O   1 
HETATM 2344 O  O   . HOH Q 5 .  ? 29.103  -33.509 35.361  1.00 58.83  ? 211 HOH C O   1 
HETATM 2345 O  O   . HOH Q 5 .  ? 9.506   -18.307 23.532  1.00 50.89  ? 212 HOH C O   1 
HETATM 2346 O  O   . HOH Q 5 .  ? 19.932  -29.100 8.227   1.00 41.88  ? 213 HOH C O   1 
HETATM 2347 O  O   . HOH Q 5 .  ? 19.887  -19.349 24.617  1.00 47.33  ? 214 HOH C O   1 
HETATM 2348 O  O   . HOH Q 5 .  ? 12.893  -29.610 4.195   1.00 51.92  ? 215 HOH C O   1 
HETATM 2349 O  O   . HOH Q 5 .  ? 22.049  -41.684 18.732  1.00 37.67  ? 216 HOH C O   1 
HETATM 2350 O  O   . HOH Q 5 .  ? 13.847  -39.678 7.170   1.00 52.12  ? 217 HOH C O   1 
HETATM 2351 O  O   . HOH Q 5 .  ? 21.237  -34.403 16.336  1.00 28.45  ? 218 HOH C O   1 
HETATM 2352 O  O   . HOH Q 5 .  ? 11.881  -31.372 8.399   1.00 43.45  ? 219 HOH C O   1 
HETATM 2353 O  O   . HOH Q 5 .  ? 22.264  -20.517 24.142  1.00 54.40  ? 220 HOH C O   1 
HETATM 2354 O  O   . HOH Q 5 .  ? 20.901  -29.590 4.284   1.00 54.30  ? 221 HOH C O   1 
HETATM 2355 O  O   . HOH Q 5 .  ? 27.151  -37.651 15.917  1.00 47.23  ? 222 HOH C O   1 
HETATM 2356 O  O   . HOH Q 5 .  ? 30.769  -35.728 28.075  1.00 53.57  ? 223 HOH C O   1 
HETATM 2357 O  O   . HOH Q 5 .  ? 18.831  -42.081 12.257  1.00 38.48  ? 224 HOH C O   1 
HETATM 2358 O  O   . HOH Q 5 .  ? 21.704  -28.945 10.699  1.00 42.33  ? 225 HOH C O   1 
HETATM 2359 O  O   . HOH Q 5 .  ? 29.159  -33.541 17.859  1.00 52.88  ? 226 HOH C O   1 
HETATM 2360 O  O   . HOH Q 5 .  ? 25.740  -20.934 28.777  1.00 71.14  ? 227 HOH C O   1 
HETATM 2361 O  O   . HOH Q 5 .  ? 17.980  -43.417 14.957  1.00 40.64  ? 228 HOH C O   1 
HETATM 2362 O  O   . HOH Q 5 .  ? 8.506   -36.787 18.205  1.00 55.04  ? 229 HOH C O   1 
HETATM 2363 O  O   . HOH Q 5 .  ? 28.549  -41.531 27.201  1.00 46.43  ? 230 HOH C O   1 
HETATM 2364 O  O   . HOH Q 5 .  ? 13.887  -41.190 14.418  1.00 52.38  ? 231 HOH C O   1 
HETATM 2365 O  O   . HOH Q 5 .  ? 29.486  -39.765 31.066  1.00 39.26  ? 232 HOH C O   1 
HETATM 2366 O  O   . HOH Q 5 .  ? 29.834  -17.946 9.231   1.00 49.59  ? 233 HOH C O   1 
HETATM 2367 O  O   . HOH Q 5 .  ? 11.025  -14.032 15.084  1.00 50.79  ? 234 HOH C O   1 
HETATM 2368 O  O   . HOH Q 5 .  ? 31.095  -39.551 26.884  1.00 46.13  ? 235 HOH C O   1 
HETATM 2369 O  O   . HOH Q 5 .  ? 17.598  -27.342 2.513   1.00 51.06  ? 236 HOH C O   1 
HETATM 2370 O  O   . HOH Q 5 .  ? 27.399  -37.331 18.435  1.00 51.54  ? 237 HOH C O   1 
HETATM 2371 O  O   . HOH Q 5 .  ? 25.145  -39.401 20.300  1.00 40.13  ? 238 HOH C O   1 
HETATM 2372 O  O   . HOH Q 5 .  ? 18.497  -20.504 10.770  1.00 57.04  ? 239 HOH C O   1 
HETATM 2373 O  O   . HOH Q 5 .  ? 20.934  -35.676 7.130   1.00 54.80  ? 240 HOH C O   1 
HETATM 2374 O  O   . HOH Q 5 .  ? 16.921  -21.144 12.328  1.00 44.20  ? 241 HOH C O   1 
HETATM 2375 O  O   . HOH Q 5 .  ? 20.613  -18.662 10.887  1.00 61.08  ? 242 HOH C O   1 
HETATM 2376 O  O   . HOH Q 5 .  ? 7.151   -15.999 21.438  1.00 57.50  ? 243 HOH C O   1 
HETATM 2377 O  O   . HOH Q 5 .  ? 22.056  -18.681 22.529  1.00 55.09  ? 244 HOH C O   1 
HETATM 2378 O  O   . HOH Q 5 .  ? 31.837  -41.361 9.948   1.00 51.13  ? 245 HOH C O   1 
HETATM 2379 O  O   . HOH Q 5 .  ? 16.336  -38.957 21.427  1.00 44.67  ? 246 HOH C O   1 
HETATM 2380 O  O   . HOH Q 5 .  ? 11.486  -21.109 10.569  1.00 38.55  ? 247 HOH C O   1 
HETATM 2381 O  O   . HOH Q 5 .  ? 29.273  -34.980 37.115  1.00 56.09  ? 248 HOH C O   1 
HETATM 2382 O  O   . HOH Q 5 .  ? 13.875  -22.097 29.259  1.00 61.12  ? 249 HOH C O   1 
HETATM 2383 O  O   . HOH Q 5 .  ? 31.512  -38.924 29.691  1.00 45.74  ? 250 HOH C O   1 
HETATM 2384 O  O   . HOH Q 5 .  ? 18.959  -43.280 18.004  1.00 52.73  ? 251 HOH C O   1 
HETATM 2385 O  O   . HOH Q 5 .  ? 25.427  -14.015 11.195  1.00 42.15  ? 252 HOH C O   1 
HETATM 2386 O  O   . HOH Q 5 .  ? 29.153  -40.139 19.088  1.00 50.26  ? 253 HOH C O   1 
HETATM 2387 O  O   . HOH Q 5 .  ? 33.006  -43.789 15.642  1.00 57.29  ? 254 HOH C O   1 
# 
