data_7HHF
# 
_entry.id   7HHF 
# 
_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   7HHF         pdb_00007hhf 10.2210/pdb7hhf/pdb 
WWPDB D_1001407477 ?            ?                   
# 
_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.entry_id                        7HHF 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '1-(2-ethyl-1,3-thiazol-5-yl)-N-methylmethanamine' 156.249   1   ? ?    ? ? 
5 water       nat water                                              18.015    253 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                      SO4   
3 1,2-ETHANEDIOL                                     EDO   
4 '1-(2-ethyl-1,3-thiazol-5-yl)-N-methylmethanamine' A1A36 
5 water                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_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 
A1A36 non-polymer         . '1-(2-ethyl-1,3-thiazol-5-yl)-N-methylmethanamine' ?                 'C7 H12 N2 S'    156.249 
ALA   'L-peptide linking' y ALANINE                                            ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                           ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                         ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                    ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                           ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                     'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                                          ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                    ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                            ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                          ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                              ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                         ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                            ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                             ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                         ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                      ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                            ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                             ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                      ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                          ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                         ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                           ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                             ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  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 ?  ?   ?   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 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 31 GLY GLY C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER 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        A1A36 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A36 
_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 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 2 SO4   1   104 4   SO4   SO4 A . 
H 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1A36 1   103 101 A1A36 LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 202 HOH   HOH A . 
M 5 HOH   3   203 335 HOH   HOH A . 
M 5 HOH   4   204 84  HOH   HOH A . 
M 5 HOH   5   205 139 HOH   HOH A . 
M 5 HOH   6   206 346 HOH   HOH A . 
M 5 HOH   7   207 304 HOH   HOH A . 
M 5 HOH   8   208 334 HOH   HOH A . 
M 5 HOH   9   209 66  HOH   HOH A . 
M 5 HOH   10  210 293 HOH   HOH A . 
M 5 HOH   11  211 23  HOH   HOH A . 
M 5 HOH   12  212 87  HOH   HOH A . 
M 5 HOH   13  213 208 HOH   HOH A . 
M 5 HOH   14  214 97  HOH   HOH A . 
M 5 HOH   15  215 111 HOH   HOH A . 
M 5 HOH   16  216 91  HOH   HOH A . 
M 5 HOH   17  217 58  HOH   HOH A . 
M 5 HOH   18  218 47  HOH   HOH A . 
M 5 HOH   19  219 8   HOH   HOH A . 
M 5 HOH   20  220 12  HOH   HOH A . 
M 5 HOH   21  221 278 HOH   HOH A . 
M 5 HOH   22  222 93  HOH   HOH A . 
M 5 HOH   23  223 94  HOH   HOH A . 
M 5 HOH   24  224 86  HOH   HOH A . 
M 5 HOH   25  225 143 HOH   HOH A . 
M 5 HOH   26  226 292 HOH   HOH A . 
M 5 HOH   27  227 32  HOH   HOH A . 
M 5 HOH   28  228 26  HOH   HOH A . 
M 5 HOH   29  229 289 HOH   HOH A . 
M 5 HOH   30  230 190 HOH   HOH A . 
M 5 HOH   31  231 37  HOH   HOH A . 
M 5 HOH   32  232 85  HOH   HOH A . 
M 5 HOH   33  233 167 HOH   HOH A . 
M 5 HOH   34  234 41  HOH   HOH A . 
M 5 HOH   35  235 296 HOH   HOH A . 
M 5 HOH   36  236 333 HOH   HOH A . 
M 5 HOH   37  237 274 HOH   HOH A . 
M 5 HOH   38  238 7   HOH   HOH A . 
M 5 HOH   39  239 28  HOH   HOH A . 
M 5 HOH   40  240 188 HOH   HOH A . 
M 5 HOH   41  241 99  HOH   HOH A . 
M 5 HOH   42  242 55  HOH   HOH A . 
M 5 HOH   43  243 199 HOH   HOH A . 
M 5 HOH   44  244 18  HOH   HOH A . 
M 5 HOH   45  245 71  HOH   HOH A . 
M 5 HOH   46  246 1   HOH   HOH A . 
M 5 HOH   47  247 290 HOH   HOH A . 
M 5 HOH   48  248 95  HOH   HOH A . 
M 5 HOH   49  249 60  HOH   HOH A . 
M 5 HOH   50  250 203 HOH   HOH A . 
M 5 HOH   51  251 267 HOH   HOH A . 
M 5 HOH   52  252 2   HOH   HOH A . 
M 5 HOH   53  253 222 HOH   HOH A . 
M 5 HOH   54  254 297 HOH   HOH A . 
M 5 HOH   55  255 21  HOH   HOH A . 
M 5 HOH   56  256 31  HOH   HOH A . 
M 5 HOH   57  257 77  HOH   HOH A . 
M 5 HOH   58  258 179 HOH   HOH A . 
M 5 HOH   59  259 27  HOH   HOH A . 
M 5 HOH   60  260 34  HOH   HOH A . 
M 5 HOH   61  261 113 HOH   HOH A . 
M 5 HOH   62  262 260 HOH   HOH A . 
M 5 HOH   63  263 42  HOH   HOH A . 
M 5 HOH   64  264 300 HOH   HOH A . 
M 5 HOH   65  265 288 HOH   HOH A . 
M 5 HOH   66  266 20  HOH   HOH A . 
M 5 HOH   67  267 73  HOH   HOH A . 
M 5 HOH   68  268 78  HOH   HOH A . 
M 5 HOH   69  269 164 HOH   HOH A . 
M 5 HOH   70  270 14  HOH   HOH A . 
M 5 HOH   71  271 318 HOH   HOH A . 
M 5 HOH   72  272 301 HOH   HOH A . 
M 5 HOH   73  273 38  HOH   HOH A . 
M 5 HOH   74  274 116 HOH   HOH A . 
M 5 HOH   75  275 9   HOH   HOH A . 
M 5 HOH   76  276 115 HOH   HOH A . 
M 5 HOH   77  277 19  HOH   HOH A . 
M 5 HOH   78  278 347 HOH   HOH A . 
M 5 HOH   79  279 145 HOH   HOH A . 
M 5 HOH   80  280 270 HOH   HOH A . 
M 5 HOH   81  281 152 HOH   HOH A . 
M 5 HOH   82  282 109 HOH   HOH A . 
M 5 HOH   83  283 131 HOH   HOH A . 
M 5 HOH   84  284 259 HOH   HOH A . 
M 5 HOH   85  285 16  HOH   HOH A . 
M 5 HOH   86  286 22  HOH   HOH A . 
M 5 HOH   87  287 211 HOH   HOH A . 
M 5 HOH   88  288 337 HOH   HOH A . 
M 5 HOH   89  289 281 HOH   HOH A . 
M 5 HOH   90  290 218 HOH   HOH A . 
M 5 HOH   91  291 64  HOH   HOH A . 
M 5 HOH   92  292 351 HOH   HOH A . 
M 5 HOH   93  293 63  HOH   HOH A . 
M 5 HOH   94  294 171 HOH   HOH A . 
M 5 HOH   95  295 210 HOH   HOH A . 
M 5 HOH   96  296 108 HOH   HOH A . 
M 5 HOH   97  297 165 HOH   HOH A . 
M 5 HOH   98  298 352 HOH   HOH A . 
M 5 HOH   99  299 327 HOH   HOH A . 
M 5 HOH   100 300 83  HOH   HOH A . 
M 5 HOH   101 301 185 HOH   HOH A . 
M 5 HOH   102 302 219 HOH   HOH A . 
M 5 HOH   103 303 342 HOH   HOH A . 
M 5 HOH   104 304 75  HOH   HOH A . 
M 5 HOH   105 305 57  HOH   HOH A . 
M 5 HOH   106 306 205 HOH   HOH A . 
M 5 HOH   107 307 35  HOH   HOH A . 
M 5 HOH   108 308 283 HOH   HOH A . 
M 5 HOH   109 309 332 HOH   HOH A . 
M 5 HOH   110 310 156 HOH   HOH A . 
M 5 HOH   111 311 125 HOH   HOH A . 
N 5 HOH   1   201 258 HOH   HOH B . 
N 5 HOH   2   202 170 HOH   HOH B . 
N 5 HOH   3   203 89  HOH   HOH B . 
N 5 HOH   4   204 344 HOH   HOH B . 
N 5 HOH   5   205 247 HOH   HOH B . 
N 5 HOH   6   206 69  HOH   HOH B . 
N 5 HOH   7   207 249 HOH   HOH B . 
N 5 HOH   8   208 123 HOH   HOH B . 
N 5 HOH   9   209 72  HOH   HOH B . 
N 5 HOH   10  210 177 HOH   HOH B . 
N 5 HOH   11  211 17  HOH   HOH B . 
N 5 HOH   12  212 339 HOH   HOH B . 
N 5 HOH   13  213 272 HOH   HOH B . 
N 5 HOH   14  214 331 HOH   HOH B . 
N 5 HOH   15  215 242 HOH   HOH B . 
N 5 HOH   16  216 153 HOH   HOH B . 
N 5 HOH   17  217 150 HOH   HOH B . 
N 5 HOH   18  218 215 HOH   HOH B . 
N 5 HOH   19  219 25  HOH   HOH B . 
N 5 HOH   20  220 224 HOH   HOH B . 
N 5 HOH   21  221 6   HOH   HOH B . 
N 5 HOH   22  222 5   HOH   HOH B . 
N 5 HOH   23  223 137 HOH   HOH B . 
N 5 HOH   24  224 98  HOH   HOH B . 
N 5 HOH   25  225 46  HOH   HOH B . 
N 5 HOH   26  226 184 HOH   HOH B . 
N 5 HOH   27  227 10  HOH   HOH B . 
N 5 HOH   28  228 168 HOH   HOH B . 
N 5 HOH   29  229 117 HOH   HOH B . 
N 5 HOH   30  230 214 HOH   HOH B . 
N 5 HOH   31  231 261 HOH   HOH B . 
N 5 HOH   32  232 59  HOH   HOH B . 
N 5 HOH   33  233 68  HOH   HOH B . 
N 5 HOH   34  234 315 HOH   HOH B . 
N 5 HOH   35  235 329 HOH   HOH B . 
N 5 HOH   36  236 24  HOH   HOH B . 
N 5 HOH   37  237 320 HOH   HOH B . 
N 5 HOH   38  238 280 HOH   HOH B . 
N 5 HOH   39  239 175 HOH   HOH B . 
N 5 HOH   40  240 172 HOH   HOH B . 
N 5 HOH   41  241 96  HOH   HOH B . 
N 5 HOH   42  242 169 HOH   HOH B . 
N 5 HOH   43  243 101 HOH   HOH B . 
N 5 HOH   44  244 76  HOH   HOH B . 
N 5 HOH   45  245 120 HOH   HOH B . 
N 5 HOH   46  246 36  HOH   HOH B . 
N 5 HOH   47  247 61  HOH   HOH B . 
N 5 HOH   48  248 54  HOH   HOH B . 
N 5 HOH   49  249 279 HOH   HOH B . 
N 5 HOH   50  250 182 HOH   HOH B . 
N 5 HOH   51  251 291 HOH   HOH B . 
N 5 HOH   52  252 353 HOH   HOH B . 
N 5 HOH   53  253 223 HOH   HOH B . 
N 5 HOH   54  254 79  HOH   HOH B . 
N 5 HOH   55  255 197 HOH   HOH B . 
N 5 HOH   56  256 119 HOH   HOH B . 
N 5 HOH   57  257 157 HOH   HOH B . 
N 5 HOH   58  258 303 HOH   HOH B . 
N 5 HOH   59  259 74  HOH   HOH B . 
N 5 HOH   60  260 13  HOH   HOH B . 
N 5 HOH   61  261 217 HOH   HOH B . 
N 5 HOH   62  262 44  HOH   HOH B . 
N 5 HOH   63  263 104 HOH   HOH B . 
N 5 HOH   64  264 341 HOH   HOH B . 
N 5 HOH   65  265 316 HOH   HOH B . 
N 5 HOH   66  266 319 HOH   HOH B . 
N 5 HOH   67  267 163 HOH   HOH B . 
N 5 HOH   68  268 160 HOH   HOH B . 
N 5 HOH   69  269 201 HOH   HOH B . 
N 5 HOH   70  270 70  HOH   HOH B . 
N 5 HOH   71  271 322 HOH   HOH B . 
N 5 HOH   72  272 314 HOH   HOH B . 
N 5 HOH   73  273 345 HOH   HOH B . 
N 5 HOH   74  274 107 HOH   HOH B . 
N 5 HOH   75  275 312 HOH   HOH B . 
O 5 HOH   1   201 321 HOH   HOH C . 
O 5 HOH   2   202 338 HOH   HOH C . 
O 5 HOH   3   203 254 HOH   HOH C . 
O 5 HOH   4   204 49  HOH   HOH C . 
O 5 HOH   5   205 142 HOH   HOH C . 
O 5 HOH   6   206 330 HOH   HOH C . 
O 5 HOH   7   207 90  HOH   HOH C . 
O 5 HOH   8   208 269 HOH   HOH C . 
O 5 HOH   9   209 118 HOH   HOH C . 
O 5 HOH   10  210 302 HOH   HOH C . 
O 5 HOH   11  211 148 HOH   HOH C . 
O 5 HOH   12  212 15  HOH   HOH C . 
O 5 HOH   13  213 102 HOH   HOH C . 
O 5 HOH   14  214 189 HOH   HOH C . 
O 5 HOH   15  215 161 HOH   HOH C . 
O 5 HOH   16  216 209 HOH   HOH C . 
O 5 HOH   17  217 325 HOH   HOH C . 
O 5 HOH   18  218 295 HOH   HOH C . 
O 5 HOH   19  219 4   HOH   HOH C . 
O 5 HOH   20  220 309 HOH   HOH C . 
O 5 HOH   21  221 275 HOH   HOH C . 
O 5 HOH   22  222 134 HOH   HOH C . 
O 5 HOH   23  223 173 HOH   HOH C . 
O 5 HOH   24  224 40  HOH   HOH C . 
O 5 HOH   25  225 298 HOH   HOH C . 
O 5 HOH   26  226 53  HOH   HOH C . 
O 5 HOH   27  227 198 HOH   HOH C . 
O 5 HOH   28  228 287 HOH   HOH C . 
O 5 HOH   29  229 323 HOH   HOH C . 
O 5 HOH   30  230 45  HOH   HOH C . 
O 5 HOH   31  231 67  HOH   HOH C . 
O 5 HOH   32  232 271 HOH   HOH C . 
O 5 HOH   33  233 226 HOH   HOH C . 
O 5 HOH   34  234 350 HOH   HOH C . 
O 5 HOH   35  235 126 HOH   HOH C . 
O 5 HOH   36  236 317 HOH   HOH C . 
O 5 HOH   37  237 48  HOH   HOH C . 
O 5 HOH   38  238 132 HOH   HOH C . 
O 5 HOH   39  239 135 HOH   HOH C . 
O 5 HOH   40  240 43  HOH   HOH C . 
O 5 HOH   41  241 65  HOH   HOH C . 
O 5 HOH   42  242 294 HOH   HOH C . 
O 5 HOH   43  243 305 HOH   HOH C . 
O 5 HOH   44  244 62  HOH   HOH C . 
O 5 HOH   45  245 122 HOH   HOH C . 
O 5 HOH   46  246 151 HOH   HOH C . 
O 5 HOH   47  247 82  HOH   HOH C . 
O 5 HOH   48  248 284 HOH   HOH C . 
O 5 HOH   49  249 299 HOH   HOH C . 
O 5 HOH   50  250 326 HOH   HOH C . 
O 5 HOH   51  251 56  HOH   HOH C . 
O 5 HOH   52  252 130 HOH   HOH C . 
O 5 HOH   53  253 149 HOH   HOH C . 
O 5 HOH   54  254 246 HOH   HOH C . 
O 5 HOH   55  255 343 HOH   HOH C . 
O 5 HOH   56  256 241 HOH   HOH C . 
O 5 HOH   57  257 328 HOH   HOH C . 
O 5 HOH   58  258 146 HOH   HOH C . 
O 5 HOH   59  259 103 HOH   HOH C . 
O 5 HOH   60  260 336 HOH   HOH C . 
O 5 HOH   61  261 349 HOH   HOH C . 
O 5 HOH   62  262 324 HOH   HOH C . 
O 5 HOH   63  263 310 HOH   HOH C . 
O 5 HOH   64  264 313 HOH   HOH C . 
O 5 HOH   65  265 340 HOH   HOH C . 
O 5 HOH   66  266 92  HOH   HOH C . 
O 5 HOH   67  267 206 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 70 ? CE  ? A LYS 71 CE  
2  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
3  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
8  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
9  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
17 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
18 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
19 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
20 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
21 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
22 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
23 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
24 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
25 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
26 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
27 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
28 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
29 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
30 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
31 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
32 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
33 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
34 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
35 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
36 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
37 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
38 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
39 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
40 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
41 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
42 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
43 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
44 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
45 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
46 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
47 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
48 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
49 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
50 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
51 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
52 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
53 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
54 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
55 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
56 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHF 
_cell.length_a           41.710 
_cell.length_b           42.430 
_cell.length_c           160.420 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HHF 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          7HHF 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.0 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '28% PEG MME 2000; 0.15 M ammonium sulfate; 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2021-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918076 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.918076 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HHF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.47 
_reflns.d_resolution_high            1.86 
_reflns.number_obs                   24723 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.096 
_reflns.pdbx_netI_over_sigmaI        9.4 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.105 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     156058 
_reflns.pdbx_chi_squared             0.99 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.86 
_reflns_shell.d_res_low                   1.91 
_reflns_shell.number_measured_all         11710 
_reflns_shell.number_unique_obs           1772 
_reflns_shell.Rmerge_I_obs                2.320 
_reflns_shell.pdbx_chi_squared            0.82 
_reflns_shell.pdbx_redundancy             6.6 
_reflns_shell.percent_possible_obs        99.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.516 
_reflns_shell.pdbx_Rpim_I_all             0.965 
_reflns_shell.pdbx_CC_half                0.347 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HHF 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23397 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             41.05 
_refine.ls_d_res_high                            1.86 
_refine.ls_percent_reflns_obs                    99.47 
_refine.ls_R_factor_obs                          0.20176 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19903 
_refine.ls_R_factor_R_free                       0.24968 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1268 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               49.939 
_refine.aniso_B[1][1]                            0.57 
_refine.aniso_B[2][2]                            -0.08 
_refine.aniso_B[3][3]                            -0.50 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.160 
_refine.pdbx_overall_ESU_R_Free                  0.153 
_refine.overall_SU_ML                            0.156 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.727 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        2136 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               2437 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        41.05 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.012  ? 2276 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.662  1.834  ? 3091 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.213  5.000  ? 263  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.138  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.380 10.000 ? 305  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 283  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 1882 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.331  4.813  ? 1067 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.871  8.599  ? 1325 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.344  5.081  ? 1209 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       10.445 70.65  ? 3504 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.860 
_refine_ls_shell.d_res_low                        1.908 
_refine_ls_shell.number_reflns_R_work             1681 
_refine_ls_shell.R_factor_R_work                  0.351 
_refine_ls_shell.percent_reflns_obs               98.60 
_refine_ls_shell.R_factor_R_free                  0.362 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             82 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHF 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1267773633' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHF 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, 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 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHF A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHF B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHF 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 7HHF GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHF SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHF GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHF SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHF GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHF SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
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,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_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 LEU A 54 ? O LEU A 53 N TYR A 41 ? N TYR A 40 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHF 
_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 O   B HOH 238 ? ? O B HOH 271 ? ? 1.68 
2  1 CE  A LYS 39  ? ? O A HOH 278 ? ? 1.99 
3  1 O   C HOH 258 ? ? O C HOH 262 ? ? 2.05 
4  1 O   A HOH 263 ? ? O A HOH 278 ? ? 2.09 
5  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 2.09 
6  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.14 
7  1 O4  A SO4 104 ? ? O A HOH 202 ? ? 2.15 
8  1 OD1 A ASP 66  ? A O A HOH 203 ? ? 2.16 
9  1 NE2 C HIS 89  ? ? O C HOH 202 ? ? 2.19 
10 1 O   B HOH 258 ? ? O B HOH 271 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 226 ? ? 1_555 O A HOH 253 ? ? 4_545 1.94 
2 1 O A HOH 307 ? ? 1_555 O A HOH 308 ? ? 4_545 2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -152.85 66.67 
2 1 ASN B 87 ? ? -152.45 58.63 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL B 11 ? ? PHE B 12 ? ? 146.78 
2 1 VAL C 11 ? ? PHE C 12 ? ? 149.10 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
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 ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 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 
A1A36 N1   N N N 1   
A1A36 C4   C Y N 2   
A1A36 C5   C N N 3   
A1A36 C6   C N N 4   
A1A36 C3   C Y N 5   
A1A36 N    N Y N 6   
A1A36 S    S Y N 7   
A1A36 C2   C Y N 8   
A1A36 C1   C N N 9   
A1A36 C    C N N 10  
A1A36 H8   H N N 11  
A1A36 H7   H N N 12  
A1A36 H6   H N N 13  
A1A36 H9   H N N 14  
A1A36 H11  H N N 15  
A1A36 H10  H N N 16  
A1A36 H5   H N N 17  
A1A36 H3   H N N 18  
A1A36 H4   H N N 19  
A1A36 H    H N N 20  
A1A36 H1   H N N 21  
A1A36 H2   H N N 22  
ALA   N    N N N 23  
ALA   CA   C N S 24  
ALA   C    C N N 25  
ALA   O    O N N 26  
ALA   CB   C N N 27  
ALA   OXT  O N N 28  
ALA   H    H N N 29  
ALA   H2   H N N 30  
ALA   HA   H N N 31  
ALA   HB1  H N N 32  
ALA   HB2  H N N 33  
ALA   HB3  H N N 34  
ALA   HXT  H N N 35  
ARG   N    N N N 36  
ARG   CA   C N S 37  
ARG   C    C N N 38  
ARG   O    O N N 39  
ARG   CB   C N N 40  
ARG   CG   C N N 41  
ARG   CD   C N N 42  
ARG   NE   N N N 43  
ARG   CZ   C N N 44  
ARG   NH1  N N N 45  
ARG   NH2  N N N 46  
ARG   OXT  O N N 47  
ARG   H    H N N 48  
ARG   H2   H N N 49  
ARG   HA   H N N 50  
ARG   HB2  H N N 51  
ARG   HB3  H N N 52  
ARG   HG2  H N N 53  
ARG   HG3  H N N 54  
ARG   HD2  H N N 55  
ARG   HD3  H N N 56  
ARG   HE   H N N 57  
ARG   HH11 H N N 58  
ARG   HH12 H N N 59  
ARG   HH21 H N N 60  
ARG   HH22 H N N 61  
ARG   HXT  H N N 62  
ASN   N    N N N 63  
ASN   CA   C N S 64  
ASN   C    C N N 65  
ASN   O    O N N 66  
ASN   CB   C N N 67  
ASN   CG   C N N 68  
ASN   OD1  O N N 69  
ASN   ND2  N N N 70  
ASN   OXT  O N N 71  
ASN   H    H N N 72  
ASN   H2   H N N 73  
ASN   HA   H N N 74  
ASN   HB2  H N N 75  
ASN   HB3  H N N 76  
ASN   HD21 H N N 77  
ASN   HD22 H N N 78  
ASN   HXT  H N N 79  
ASP   N    N N N 80  
ASP   CA   C N S 81  
ASP   C    C N N 82  
ASP   O    O N N 83  
ASP   CB   C N N 84  
ASP   CG   C N N 85  
ASP   OD1  O N N 86  
ASP   OD2  O N N 87  
ASP   OXT  O N N 88  
ASP   H    H N N 89  
ASP   H2   H N N 90  
ASP   HA   H N N 91  
ASP   HB2  H N N 92  
ASP   HB3  H N N 93  
ASP   HD2  H N N 94  
ASP   HXT  H N N 95  
CYS   N    N N N 96  
CYS   CA   C N R 97  
CYS   C    C N N 98  
CYS   O    O N N 99  
CYS   CB   C N N 100 
CYS   SG   S N N 101 
CYS   OXT  O N N 102 
CYS   H    H N N 103 
CYS   H2   H N N 104 
CYS   HA   H N N 105 
CYS   HB2  H N N 106 
CYS   HB3  H N N 107 
CYS   HG   H N N 108 
CYS   HXT  H N N 109 
EDO   C1   C N N 110 
EDO   O1   O N N 111 
EDO   C2   C N N 112 
EDO   O2   O N N 113 
EDO   H11  H N N 114 
EDO   H12  H N N 115 
EDO   HO1  H N N 116 
EDO   H21  H N N 117 
EDO   H22  H N N 118 
EDO   HO2  H N N 119 
GLN   N    N N N 120 
GLN   CA   C N S 121 
GLN   C    C N N 122 
GLN   O    O N N 123 
GLN   CB   C N N 124 
GLN   CG   C N N 125 
GLN   CD   C N N 126 
GLN   OE1  O N N 127 
GLN   NE2  N N N 128 
GLN   OXT  O N N 129 
GLN   H    H N N 130 
GLN   H2   H N N 131 
GLN   HA   H N N 132 
GLN   HB2  H N N 133 
GLN   HB3  H N N 134 
GLN   HG2  H N N 135 
GLN   HG3  H N N 136 
GLN   HE21 H N N 137 
GLN   HE22 H N N 138 
GLN   HXT  H N N 139 
GLU   N    N N N 140 
GLU   CA   C N S 141 
GLU   C    C N N 142 
GLU   O    O N N 143 
GLU   CB   C N N 144 
GLU   CG   C N N 145 
GLU   CD   C N N 146 
GLU   OE1  O N N 147 
GLU   OE2  O N N 148 
GLU   OXT  O N N 149 
GLU   H    H N N 150 
GLU   H2   H N N 151 
GLU   HA   H N N 152 
GLU   HB2  H N N 153 
GLU   HB3  H N N 154 
GLU   HG2  H N N 155 
GLU   HG3  H N N 156 
GLU   HE2  H N N 157 
GLU   HXT  H N N 158 
GLY   N    N N N 159 
GLY   CA   C N N 160 
GLY   C    C N N 161 
GLY   O    O N N 162 
GLY   OXT  O N N 163 
GLY   H    H N N 164 
GLY   H2   H N N 165 
GLY   HA2  H N N 166 
GLY   HA3  H N N 167 
GLY   HXT  H N N 168 
HIS   N    N N N 169 
HIS   CA   C N S 170 
HIS   C    C N N 171 
HIS   O    O N N 172 
HIS   CB   C N N 173 
HIS   CG   C Y N 174 
HIS   ND1  N Y N 175 
HIS   CD2  C Y N 176 
HIS   CE1  C Y N 177 
HIS   NE2  N Y N 178 
HIS   OXT  O N N 179 
HIS   H    H N N 180 
HIS   H2   H N N 181 
HIS   HA   H N N 182 
HIS   HB2  H N N 183 
HIS   HB3  H N N 184 
HIS   HD1  H N N 185 
HIS   HD2  H N N 186 
HIS   HE1  H N N 187 
HIS   HE2  H N N 188 
HIS   HXT  H N N 189 
HOH   O    O N N 190 
HOH   H1   H N N 191 
HOH   H2   H N N 192 
ILE   N    N N N 193 
ILE   CA   C N S 194 
ILE   C    C N N 195 
ILE   O    O N N 196 
ILE   CB   C N S 197 
ILE   CG1  C N N 198 
ILE   CG2  C N N 199 
ILE   CD1  C N N 200 
ILE   OXT  O N N 201 
ILE   H    H N N 202 
ILE   H2   H N N 203 
ILE   HA   H N N 204 
ILE   HB   H N N 205 
ILE   HG12 H N N 206 
ILE   HG13 H N N 207 
ILE   HG21 H N N 208 
ILE   HG22 H N N 209 
ILE   HG23 H N N 210 
ILE   HD11 H N N 211 
ILE   HD12 H N N 212 
ILE   HD13 H N N 213 
ILE   HXT  H N N 214 
LEU   N    N N N 215 
LEU   CA   C N S 216 
LEU   C    C N N 217 
LEU   O    O N N 218 
LEU   CB   C N N 219 
LEU   CG   C N N 220 
LEU   CD1  C N N 221 
LEU   CD2  C N N 222 
LEU   OXT  O N N 223 
LEU   H    H N N 224 
LEU   H2   H N N 225 
LEU   HA   H N N 226 
LEU   HB2  H N N 227 
LEU   HB3  H N N 228 
LEU   HG   H N N 229 
LEU   HD11 H N N 230 
LEU   HD12 H N N 231 
LEU   HD13 H N N 232 
LEU   HD21 H N N 233 
LEU   HD22 H N N 234 
LEU   HD23 H N N 235 
LEU   HXT  H N N 236 
LYS   N    N N N 237 
LYS   CA   C N S 238 
LYS   C    C N N 239 
LYS   O    O N N 240 
LYS   CB   C N N 241 
LYS   CG   C N N 242 
LYS   CD   C N N 243 
LYS   CE   C N N 244 
LYS   NZ   N N N 245 
LYS   OXT  O N N 246 
LYS   H    H N N 247 
LYS   H2   H N N 248 
LYS   HA   H N N 249 
LYS   HB2  H N N 250 
LYS   HB3  H N N 251 
LYS   HG2  H N N 252 
LYS   HG3  H N N 253 
LYS   HD2  H N N 254 
LYS   HD3  H N N 255 
LYS   HE2  H N N 256 
LYS   HE3  H N N 257 
LYS   HZ1  H N N 258 
LYS   HZ2  H N N 259 
LYS   HZ3  H N N 260 
LYS   HXT  H N N 261 
MET   N    N N N 262 
MET   CA   C N S 263 
MET   C    C N N 264 
MET   O    O N N 265 
MET   CB   C N N 266 
MET   CG   C N N 267 
MET   SD   S N N 268 
MET   CE   C N N 269 
MET   OXT  O N N 270 
MET   H    H N N 271 
MET   H2   H N N 272 
MET   HA   H N N 273 
MET   HB2  H N N 274 
MET   HB3  H N N 275 
MET   HG2  H N N 276 
MET   HG3  H N N 277 
MET   HE1  H N N 278 
MET   HE2  H N N 279 
MET   HE3  H N N 280 
MET   HXT  H N N 281 
PHE   N    N N N 282 
PHE   CA   C N S 283 
PHE   C    C N N 284 
PHE   O    O N N 285 
PHE   CB   C N N 286 
PHE   CG   C Y N 287 
PHE   CD1  C Y N 288 
PHE   CD2  C Y N 289 
PHE   CE1  C Y N 290 
PHE   CE2  C Y N 291 
PHE   CZ   C Y N 292 
PHE   OXT  O N N 293 
PHE   H    H N N 294 
PHE   H2   H N N 295 
PHE   HA   H N N 296 
PHE   HB2  H N N 297 
PHE   HB3  H N N 298 
PHE   HD1  H N N 299 
PHE   HD2  H N N 300 
PHE   HE1  H N N 301 
PHE   HE2  H N N 302 
PHE   HZ   H N N 303 
PHE   HXT  H N N 304 
PRO   N    N N N 305 
PRO   CA   C N S 306 
PRO   C    C N N 307 
PRO   O    O N N 308 
PRO   CB   C N N 309 
PRO   CG   C N N 310 
PRO   CD   C N N 311 
PRO   OXT  O N N 312 
PRO   H    H N N 313 
PRO   HA   H N N 314 
PRO   HB2  H N N 315 
PRO   HB3  H N N 316 
PRO   HG2  H N N 317 
PRO   HG3  H N N 318 
PRO   HD2  H N N 319 
PRO   HD3  H N N 320 
PRO   HXT  H N N 321 
SER   N    N N N 322 
SER   CA   C N S 323 
SER   C    C N N 324 
SER   O    O N N 325 
SER   CB   C N N 326 
SER   OG   O N N 327 
SER   OXT  O N N 328 
SER   H    H N N 329 
SER   H2   H N N 330 
SER   HA   H N N 331 
SER   HB2  H N N 332 
SER   HB3  H N N 333 
SER   HG   H N N 334 
SER   HXT  H N N 335 
SO4   S    S N N 336 
SO4   O1   O N N 337 
SO4   O2   O N N 338 
SO4   O3   O N N 339 
SO4   O4   O N N 340 
THR   N    N N N 341 
THR   CA   C N S 342 
THR   C    C N N 343 
THR   O    O N N 344 
THR   CB   C N R 345 
THR   OG1  O N N 346 
THR   CG2  C N N 347 
THR   OXT  O N N 348 
THR   H    H N N 349 
THR   H2   H N N 350 
THR   HA   H N N 351 
THR   HB   H N N 352 
THR   HG1  H N N 353 
THR   HG21 H N N 354 
THR   HG22 H N N 355 
THR   HG23 H N N 356 
THR   HXT  H N N 357 
TRP   N    N N N 358 
TRP   CA   C N S 359 
TRP   C    C N N 360 
TRP   O    O N N 361 
TRP   CB   C N N 362 
TRP   CG   C Y N 363 
TRP   CD1  C Y N 364 
TRP   CD2  C Y N 365 
TRP   NE1  N Y N 366 
TRP   CE2  C Y N 367 
TRP   CE3  C Y N 368 
TRP   CZ2  C Y N 369 
TRP   CZ3  C Y N 370 
TRP   CH2  C Y N 371 
TRP   OXT  O N N 372 
TRP   H    H N N 373 
TRP   H2   H N N 374 
TRP   HA   H N N 375 
TRP   HB2  H N N 376 
TRP   HB3  H N N 377 
TRP   HD1  H N N 378 
TRP   HE1  H N N 379 
TRP   HE3  H N N 380 
TRP   HZ2  H N N 381 
TRP   HZ3  H N N 382 
TRP   HH2  H N N 383 
TRP   HXT  H N N 384 
TYR   N    N N N 385 
TYR   CA   C N S 386 
TYR   C    C N N 387 
TYR   O    O N N 388 
TYR   CB   C N N 389 
TYR   CG   C Y N 390 
TYR   CD1  C Y N 391 
TYR   CD2  C Y N 392 
TYR   CE1  C Y N 393 
TYR   CE2  C Y N 394 
TYR   CZ   C Y N 395 
TYR   OH   O N N 396 
TYR   OXT  O N N 397 
TYR   H    H N N 398 
TYR   H2   H N N 399 
TYR   HA   H N N 400 
TYR   HB2  H N N 401 
TYR   HB3  H N N 402 
TYR   HD1  H N N 403 
TYR   HD2  H N N 404 
TYR   HE1  H N N 405 
TYR   HE2  H N N 406 
TYR   HH   H N N 407 
TYR   HXT  H N N 408 
VAL   N    N N N 409 
VAL   CA   C N S 410 
VAL   C    C N N 411 
VAL   O    O N N 412 
VAL   CB   C N N 413 
VAL   CG1  C N N 414 
VAL   CG2  C N N 415 
VAL   OXT  O N N 416 
VAL   H    H N N 417 
VAL   H2   H N N 418 
VAL   HA   H N N 419 
VAL   HB   H N N 420 
VAL   HG11 H N N 421 
VAL   HG12 H N N 422 
VAL   HG13 H N N 423 
VAL   HG21 H N N 424 
VAL   HG22 H N N 425 
VAL   HG23 H N N 426 
VAL   HXT  H N N 427 
# 
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 
A1A36 C   C1   sing N N 1   
A1A36 C1  C2   sing N N 2   
A1A36 C2  N    doub Y N 3   
A1A36 N   C3   sing Y N 4   
A1A36 C3  C4   doub Y N 5   
A1A36 C4  C5   sing N N 6   
A1A36 C5  N1   sing N N 7   
A1A36 N1  C6   sing N N 8   
A1A36 S   C4   sing Y N 9   
A1A36 C2  S    sing Y N 10  
A1A36 N1  H8   sing N N 11  
A1A36 C5  H7   sing N N 12  
A1A36 C5  H6   sing N N 13  
A1A36 C6  H9   sing N N 14  
A1A36 C6  H11  sing N N 15  
A1A36 C6  H10  sing N N 16  
A1A36 C3  H5   sing N N 17  
A1A36 C1  H3   sing N N 18  
A1A36 C1  H4   sing N N 19  
A1A36 C   H    sing N N 20  
A1A36 C   H1   sing N N 21  
A1A36 C   H2   sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
CYS   N   CA   sing N N 92  
CYS   N   H    sing N N 93  
CYS   N   H2   sing N N 94  
CYS   CA  C    sing N N 95  
CYS   CA  CB   sing N N 96  
CYS   CA  HA   sing N N 97  
CYS   C   O    doub N N 98  
CYS   C   OXT  sing N N 99  
CYS   CB  SG   sing N N 100 
CYS   CB  HB2  sing N N 101 
CYS   CB  HB3  sing N N 102 
CYS   SG  HG   sing N N 103 
CYS   OXT HXT  sing N N 104 
EDO   C1  O1   sing N N 105 
EDO   C1  C2   sing N N 106 
EDO   C1  H11  sing N N 107 
EDO   C1  H12  sing N N 108 
EDO   O1  HO1  sing N N 109 
EDO   C2  O2   sing N N 110 
EDO   C2  H21  sing N N 111 
EDO   C2  H22  sing N N 112 
EDO   O2  HO2  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
SO4   S   O1   doub N N 321 
SO4   S   O2   doub N N 322 
SO4   S   O3   sing N N 323 
SO4   S   O4   sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TRP   N   CA   sing N N 341 
TRP   N   H    sing N N 342 
TRP   N   H2   sing N N 343 
TRP   CA  C    sing N N 344 
TRP   CA  CB   sing N N 345 
TRP   CA  HA   sing N N 346 
TRP   C   O    doub N N 347 
TRP   C   OXT  sing N N 348 
TRP   CB  CG   sing N N 349 
TRP   CB  HB2  sing N N 350 
TRP   CB  HB3  sing N N 351 
TRP   CG  CD1  doub Y N 352 
TRP   CG  CD2  sing Y N 353 
TRP   CD1 NE1  sing Y N 354 
TRP   CD1 HD1  sing N N 355 
TRP   CD2 CE2  doub Y N 356 
TRP   CD2 CE3  sing Y N 357 
TRP   NE1 CE2  sing Y N 358 
TRP   NE1 HE1  sing N N 359 
TRP   CE2 CZ2  sing Y N 360 
TRP   CE3 CZ3  doub Y N 361 
TRP   CE3 HE3  sing N N 362 
TRP   CZ2 CH2  doub Y N 363 
TRP   CZ2 HZ2  sing N N 364 
TRP   CZ3 CH2  sing Y N 365 
TRP   CZ3 HZ3  sing N N 366 
TRP   CH2 HH2  sing N N 367 
TRP   OXT HXT  sing N N 368 
TYR   N   CA   sing N N 369 
TYR   N   H    sing N N 370 
TYR   N   H2   sing N N 371 
TYR   CA  C    sing N N 372 
TYR   CA  CB   sing N N 373 
TYR   CA  HA   sing N N 374 
TYR   C   O    doub N N 375 
TYR   C   OXT  sing N N 376 
TYR   CB  CG   sing N N 377 
TYR   CB  HB2  sing N N 378 
TYR   CB  HB3  sing N N 379 
TYR   CG  CD1  doub Y N 380 
TYR   CG  CD2  sing Y N 381 
TYR   CD1 CE1  sing Y N 382 
TYR   CD1 HD1  sing N N 383 
TYR   CD2 CE2  doub Y N 384 
TYR   CD2 HD2  sing N N 385 
TYR   CE1 CZ   doub Y N 386 
TYR   CE1 HE1  sing N N 387 
TYR   CE2 CZ   sing Y N 388 
TYR   CE2 HE2  sing N N 389 
TYR   CZ  OH   sing N N 390 
TYR   OH  HH   sing N N 391 
TYR   OXT HXT  sing N N 392 
VAL   N   CA   sing N N 393 
VAL   N   H    sing N N 394 
VAL   N   H2   sing N N 395 
VAL   CA  C    sing N N 396 
VAL   CA  CB   sing N N 397 
VAL   CA  HA   sing N N 398 
VAL   C   O    doub N N 399 
VAL   C   OXT  sing N N 400 
VAL   CB  CG1  sing N N 401 
VAL   CB  CG2  sing N N 402 
VAL   CB  HB   sing N N 403 
VAL   CG1 HG11 sing N N 404 
VAL   CG1 HG12 sing N N 405 
VAL   CG1 HG13 sing N N 406 
VAL   CG2 HG21 sing N N 407 
VAL   CG2 HG22 sing N N 408 
VAL   CG2 HG23 sing N N 409 
VAL   OXT HXT  sing N N 410 
# 
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_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HHF 
_atom_sites.fract_transf_matrix[1][1]   0.023975 
_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]   0.023568 
_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]   0.006234 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 2  ? 1.571   4.008   2.684   1.00 62.73  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? 0.436   3.560   1.835   1.00 66.68  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.921   2.539   0.803   1.00 68.73  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.987   2.705   0.212   1.00 71.57  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -0.295  4.755   1.209   1.00 73.56  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -1.334  5.370   2.140   1.00 92.65  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -2.781  4.337   2.473   1.00 112.76 ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.567  5.095   3.901   1.00 86.05  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? 0.177   1.423   0.599   1.00 63.41  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.646   0.307   -0.237  1.00 57.66  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.791   0.549   -1.740  1.00 52.27  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? 0.086   1.360   -2.319  1.00 49.64  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -0.384  -0.822  0.077   1.00 67.99  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.072  -0.376  1.375   1.00 60.90  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.112  1.140   1.259   1.00 62.57  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.720   -0.173  -2.371  1.00 59.57  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.908   -0.089  -3.815  1.00 58.58  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.347   -1.377  -4.409  1.00 52.21  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.914   -2.247  -3.658  1.00 49.21  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.396   0.141   -4.138  1.00 62.43  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.927   1.431   -3.589  1.00 74.33  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 4.235   1.624   -2.257  1.00 80.64  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.148   2.611   -4.189  1.00 79.35  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.641   2.873   -2.073  1.00 79.49  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.599   3.489   -3.236  1.00 78.79  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.350   -1.495  -5.742  1.00 49.44  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 1.174   -2.784  -6.399  1.00 44.34  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.284   -3.750  -5.989  1.00 37.71  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.337   -3.329  -5.530  1.00 39.85  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 1.141   -2.595  -7.895  1.00 48.63  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 2.037   -5.049  -6.159  1.00 35.77  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 3.046   -6.072  -5.928  1.00 39.38  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 4.198   -5.889  -6.918  1.00 41.07  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.967   -5.534  -8.072  1.00 43.73  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.445   -7.475  -6.039  1.00 37.31  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.673   -7.837  -4.772  1.00 37.91  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.344   -8.066  -3.573  1.00 34.50  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.288   -7.963  -4.790  1.00 37.36  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.663   -8.389  -2.408  1.00 34.25  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.388  -8.325  -3.627  1.00 33.25  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.297   -8.505  -2.440  1.00 35.96  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.431   -6.113  -6.444  1.00 38.99  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.613   -6.047  -7.300  1.00 40.50  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.537   -7.230  -6.979  1.00 35.30  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.456   -7.834  -5.911  1.00 32.04  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.205   -4.637  -7.161  1.00 38.23  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.870   -4.427  -5.810  1.00 46.48  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.575   -3.090  -5.603  1.00 54.86  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 9.274   -3.076  -4.271  1.00 55.60  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 8.340   -3.277  -3.157  1.00 46.42  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.419   -7.646  -7.917  1.00 34.80  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.377   -8.725  -7.668  1.00 33.26  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 10.141  -8.365  -6.402  1.00 31.26  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.485  -7.199  -6.224  1.00 36.43  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 10.284  -8.581  -8.931  1.00 34.27  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 9.289   -8.182  -10.020 1.00 37.58  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.485   -7.121  -9.301  1.00 37.39  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.350  -9.384  -5.552  1.00 29.72  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 11.081  -9.268  -4.309  1.00 29.65  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 10.094  -9.219  -3.140  1.00 31.44  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.459  -9.508  -2.005  1.00 30.11  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.825   -8.906  -3.421  1.00 28.29  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.862   -8.800  -2.309  1.00 31.34  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.616   -10.162 -1.659  1.00 27.34  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.472   -11.164 -2.350  1.00 30.09  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.538   -8.190  -2.765  1.00 27.85  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.511   -6.676  -2.913  1.00 34.06  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.431   -5.999  -2.396  1.00 37.60  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.583   -6.169  -3.556  1.00 32.14  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.505   -10.208 -0.320  1.00 26.96  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.346   -11.469 0.392   1.00 27.57  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.882   -11.587 0.790   1.00 30.45  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.317   -10.599 1.271   1.00 32.87  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.264   -11.523 1.623   1.00 27.82  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.751   -11.311 1.304   1.00 24.39  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.563  -11.443 2.639   1.00 27.56  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 10.121  -12.389 0.271   1.00 26.59  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.319   -12.791 0.638   1.00 28.44  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.891   -12.969 0.920   1.00 32.14  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.660   -14.325 1.553   1.00 32.13  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.579   -15.138 1.621   1.00 30.93  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 3.058   -12.858 -0.365  1.00 26.98  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 3.194   -11.461 -0.962  1.00 29.63  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.455   -13.941 -1.379  1.00 28.35  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.423   -14.545 2.030   1.00 32.28  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.889   -15.892 2.055   1.00 30.44  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.928   -16.002 0.869   1.00 33.13  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? 0.104   -15.126 0.689   1.00 31.85  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 1.088   -16.231 3.322   1.00 29.48  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.974   -16.362 4.550   1.00 30.77  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.326   -15.246 5.299   1.00 35.31  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.503   -17.600 4.909   1.00 35.96  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 3.185   -15.383 6.387   1.00 40.59  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.369   -17.729 6.002   1.00 37.18  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.700   -16.622 6.736   1.00 35.62  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 1.008   -17.098 0.109   1.00 34.05  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? 0.213   -17.227 -1.099  1.00 35.89  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -0.784  -18.375 -0.913  1.00 34.86  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.446  -19.409 -0.329  1.00 33.55  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 1.129   -17.420 -2.312  1.00 30.88  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.041  -18.163 -1.365  1.00 38.48  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.101  -19.124 -1.085  1.00 32.17  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.427  -19.871 -2.376  1.00 33.66  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -3.707  -19.216 -3.379  1.00 33.77  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.352  -18.458 -0.477  1.00 33.85  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.435  -19.456 -0.019  1.00 37.54  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.037  -20.424 1.097   1.00 40.33  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.147  -21.292 1.646   1.00 39.28  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.308  -22.520 0.852   1.00 43.33  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.305  -21.209 -2.350  1.00 36.10  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -3.826  -22.076 -3.399  1.00 40.14  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -4.889  -22.984 -2.766  1.00 48.80  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -4.742  -23.376 -1.608  1.00 40.89  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.765  -23.066 -3.878  1.00 42.88  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.415  -22.482 -4.239  1.00 50.31  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.443  -21.963 -5.962  1.00 50.66  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.042  -23.538 -6.722  1.00 45.54  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -5.920  -23.361 -3.539  1.00 54.47  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -6.984  -24.261 -3.095  1.00 52.44  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.381  -25.567 -2.591  1.00 49.73  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.520  -26.135 -3.249  1.00 44.42  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -7.776  -24.671 -4.342  1.00 60.61  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -8.907  -25.667 -4.138  1.00 58.63  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -9.415  -26.152 -5.494  1.00 65.01  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -10.738 -26.858 -5.460  1.00 79.46  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -11.852 -25.964 -5.113  1.00 88.56  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -6.833  -26.055 -1.429  1.00 48.04  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -6.339  -27.338 -0.962  1.00 47.75  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -5.035  -27.214 -0.174  1.00 58.22  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -4.561  -28.196 0.382   1.00 56.60  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -4.455  -26.010 -0.105  1.00 49.87  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -3.226  -25.852 0.649   1.00 42.96  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -3.403  -24.751 1.686   1.00 39.26  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -4.130  -23.802 1.457   1.00 41.76  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.095  -25.416 -0.286  1.00 47.42  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -1.521  -26.465 -1.227  1.00 47.41  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -0.388  -27.188 -0.877  1.00 56.77  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -2.087  -26.703 -2.477  1.00 55.56  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? 0.153   -28.136 -1.733  1.00 64.22  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -1.557  -27.646 -3.344  1.00 55.54  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -0.432  -28.366 -2.968  1.00 66.17  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? 0.123   -29.309 -3.796  1.00 71.33  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -2.649  -24.769 2.804   1.00 42.57  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -2.615  -23.619 3.717   1.00 39.94  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -1.897  -22.435 3.062   1.00 38.96  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -1.098  -22.636 2.159   1.00 40.45  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -1.842  -24.194 4.921   1.00 42.00  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -0.929  -25.252 4.312   1.00 49.38  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -1.751  -25.865 3.194   1.00 48.69  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -2.161  -21.216 3.545   1.00 35.07  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -1.423  -20.012 3.187   1.00 38.28  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? 0.081   -20.294 3.284   1.00 38.81  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? 0.561   -20.730 4.333   1.00 36.65  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -1.900  -18.850 4.064   1.00 40.99  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -3.374  -18.547 3.899   1.00 43.84  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -4.341  -19.269 4.570   1.00 39.47  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.032  -17.610 3.193   1.00 38.81  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -5.547  -18.793 4.263   1.00 40.63  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -5.389  -17.773 3.425   1.00 41.83  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? 0.810   -20.071 2.177   1.00 35.49  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 2.131   -20.672 2.027   1.00 33.48  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 3.231   -19.620 1.854   1.00 32.53  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 3.097   -18.727 1.030   1.00 31.68  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 2.116   -21.620 0.818   1.00 37.54  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 3.229   -22.629 0.844   1.00 37.44  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 4.553   -22.433 0.545   1.00 35.46  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 3.091   -24.019 1.201   1.00 39.07  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 5.244   -23.609 0.675   1.00 37.59  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 4.372   -24.602 1.076   1.00 39.08  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 2.009   -24.824 1.595   1.00 45.87  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 4.602   -25.954 1.357   1.00 44.13  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 2.242   -26.161 1.860   1.00 45.81  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 3.521   -26.720 1.739   1.00 45.97  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 4.392   -19.709 2.558   1.00 29.40  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 5.433   -18.688 2.410   1.00 31.67  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 5.936   -18.679 0.974   1.00 26.35  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 6.243   -19.744 0.409   1.00 32.82  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 6.519   -19.148 3.445   1.00 31.03  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 6.293   -20.654 3.546   1.00 30.50  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 4.749   -20.759 3.530   1.00 29.77  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 6.013   -17.463 0.407   1.00 28.62  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 6.295   -17.274 -1.004  1.00 30.41  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 6.865   -15.887 -1.265  1.00 28.03  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.860   -15.006 -0.405  1.00 32.28  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 5.025   -17.512 -1.817  1.00 29.09  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 7.376   -15.708 -2.490  1.00 26.95  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 7.775   -14.401 -2.937  1.00 26.78  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 7.253   -14.159 -4.347  1.00 29.53  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.946   -15.107 -5.094  1.00 30.80  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 9.297   -14.257 -2.893  1.00 27.03  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.946   -15.031 -4.028  1.00 27.71  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 11.490  -15.032 -3.809  1.00 30.42  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 12.225  -15.726 -4.879  1.00 32.49  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 13.476  -16.194 -4.782  1.00 35.53  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 14.179  -16.124 -3.637  1.00 33.10  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 14.001  -16.803 -5.836  1.00 34.69  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 7.171   -12.879 -4.694  1.00 29.31  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.892   -12.518 -6.087  1.00 31.50  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 8.220   -12.613 -6.839  1.00 34.01  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 9.183   -11.967 -6.430  1.00 31.86  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 6.359   -11.078 -6.231  1.00 34.56  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 5.238   -10.693 -5.236  1.00 39.07  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.998   -10.744 -7.695  1.00 30.16  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 3.906   -11.359 -5.454  1.00 43.71  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 8.249   -13.384 -7.930  1.00 33.32  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 9.473   -13.539 -8.709  1.00 37.31  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 9.597   -12.499 -9.822  1.00 41.25  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 8.627   -11.847 -10.220 1.00 33.43  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 9.611   -14.946 -9.262  1.00 36.56  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 10.552  -15.852 -8.492  1.00 39.73  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 11.104  -15.387 -7.464  1.00 43.48  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 10.740  -16.999 -8.931  1.00 37.68  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.838  -12.343 -10.315 1.00 38.04  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 11.101  -11.698 -11.587 1.00 43.66  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.742  -12.660 -12.717 1.00 39.61  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.588  -13.859 -12.507 1.00 41.95  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 12.561  -11.269 -11.673 1.00 47.87  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 12.887  -9.933  -11.010 1.00 57.13  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 12.457  -8.886  -11.545 1.00 58.13  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 13.556  -9.947  -9.949  1.00 65.23  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 10.563  -12.121 -13.924 1.00 39.43  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 10.553  -12.976 -15.100 1.00 43.08  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.895  -12.747 -15.800 1.00 43.57  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 12.265  -11.610 -16.064 1.00 43.51  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 9.361   -12.620 -16.006 1.00 49.65  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 8.023   -12.764 -15.236 1.00 50.28  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 9.382   -13.438 -17.304 1.00 42.59  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.941   -11.802 -15.705 1.00 47.35  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 12.638  -13.828 -16.026 1.00 40.80  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.906  -13.773 -16.741 1.00 44.72  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.670  -13.360 -18.197 1.00 39.19  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.663  -13.715 -18.815 1.00 38.25  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.565  -15.132 -16.667 1.00 42.17  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.635  -12.642 -18.777 1.00 43.37  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.634  -12.492 -20.227 1.00 41.23  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 14.503  -13.868 -20.862 1.00 34.65  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 15.162  -14.818 -20.440 1.00 39.62  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.872  -11.759 -20.725 1.00 46.81  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.889  -10.267 -20.434 1.00 49.67  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.799  -9.703  -20.215 1.00 57.30  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 16.999  -9.701  -20.362 1.00 54.11  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 13.593  -13.972 -21.835 1.00 39.01  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 13.416  -15.190 -22.615 1.00 38.08  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 12.479  -16.222 -21.982 1.00 43.77  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 12.256  -17.272 -22.573 1.00 45.07  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.980  -15.950 -20.768 1.00 43.04  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 11.209  -16.935 -20.019 1.00 47.34  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 9.723   -16.680 -20.268 1.00 44.51  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 9.350   -15.585 -20.687 1.00 41.29  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 11.563  -16.863 -18.536 1.00 39.73  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.898   -17.705 -20.017 1.00 47.25  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 7.444   -17.643 -20.131 1.00 49.57  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.860   -16.612 -19.170 1.00 44.72  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 7.089   -16.690 -17.970 1.00 48.63  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 6.854   -19.043 -19.861 1.00 53.07  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 5.330   -19.029 -19.857 1.00 55.74  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 7.375   -20.055 -20.874 1.00 58.43  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 6.065   -15.691 -19.731 1.00 50.05  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 5.386   -14.613 -19.025 1.00 48.35  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 4.117   -15.170 -18.389 1.00 47.13  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 3.569   -16.152 -18.882 1.00 41.43  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 5.001   -13.475 -19.980 1.00 46.98  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 6.141   -12.562 -20.438 1.00 55.08  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.758   -11.388 -21.329 1.00 57.53  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.418   -11.809 -22.723 1.00 55.48  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 5.193   -10.654 -23.592 1.00 55.39  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 3.613   -14.589 -17.277 1.00 50.23  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 2.370   -15.080 -16.663 1.00 49.60  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 1.181   -14.600 -17.485 1.00 45.71  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 1.313   -13.662 -18.261 1.00 49.29  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 2.365   -14.454 -15.273 1.00 44.33  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 3.155   -13.176 -15.463 1.00 52.02  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 4.181   -13.433 -16.567 1.00 49.63  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.026  -15.168 -17.290 1.00 44.99  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.226  -14.607 -17.906 1.00 47.93  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -1.390  -13.181 -17.400 1.00 51.09  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -0.775  -12.828 -16.387 1.00 43.14  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -2.390  -15.502 -17.468 1.00 48.08  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -1.764  -16.672 -16.742 1.00 43.95  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -0.296  -16.364 -16.481 1.00 42.15  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.192  -12.333 -18.100 1.00 49.94  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -2.505  -10.983 -17.632 1.00 50.60  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.048  -10.947 -16.208 1.00 48.33  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -3.824  -11.815 -15.811 1.00 48.98  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -3.550  -10.406 -18.622 1.00 53.34  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -3.720  -11.454 -19.690 1.00 47.72  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -2.815  -12.636 -19.403 1.00 55.95  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -2.625  -9.919  -15.466 1.00 47.48  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.084  -9.649  -14.119 1.00 48.90  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -2.652  -10.757 -13.163 1.00 43.03  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.141  -10.771 -12.041 1.00 48.32  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -4.606  -9.555  -14.052 1.00 60.87  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.145  -8.443  -14.920 1.00 64.99  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.086  -7.270  -14.540 1.00 65.08  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -5.683  -8.792  -16.075 1.00 62.26  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -1.786  -11.697 -13.589 1.00 41.11  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.251  -12.679 -12.641 1.00 32.45  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? 0.223   -12.397 -12.356 1.00 34.93  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.896   -11.730 -13.141 1.00 36.86  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -1.367  -14.130 -13.120 1.00 35.19  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -2.781  -14.603 -13.499 1.00 40.28  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -3.685  -14.581 -12.277 1.00 43.72  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.130  -14.879 -12.600 1.00 55.36  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -5.361  -16.318 -12.765 1.00 54.24  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.719   -12.923 -11.232 1.00 29.67  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 2.125   -12.751 -10.854 1.00 33.71  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 2.823   -14.105 -10.790 1.00 30.69  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 2.232   -15.101 -10.381 1.00 34.26  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 2.259   -12.076 -9.477  1.00 31.77  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.793   -10.627 -9.519  1.00 33.78  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? 0.433   -10.333 -9.492  1.00 38.74  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 2.684   -9.559  -9.597  1.00 39.74  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.017  -9.026  -9.570  1.00 42.64  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 2.252   -8.240  -9.654  1.00 42.31  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.887   -7.982  -9.617  1.00 46.58  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? 0.384   -6.718  -9.688  1.00 49.82  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 4.140   -14.203 -11.121 1.00 33.26  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 4.869   -15.449 -10.903 1.00 31.05  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 5.178   -15.571 -9.413  1.00 32.79  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 5.804   -14.667 -8.840  1.00 34.75  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 6.166   -15.297 -11.737 1.00 30.78  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 6.262   -13.850 -12.066 1.00 34.97  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.949   -13.133 -11.717 1.00 38.49  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 4.695   -16.648 -8.791  1.00 33.09  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.843   -16.821 -7.355  1.00 34.26  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 5.771   -17.999 -7.108  1.00 35.29  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 5.504   -19.102 -7.577  1.00 37.48  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 3.482   -17.034 -6.652  1.00 36.49  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 2.494   -15.928 -6.921  1.00 30.68  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.659   -17.297 -5.148  1.00 31.73  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.903   -14.524 -6.490  1.00 30.21  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.855   -17.752 -6.367  1.00 27.36  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 7.782   -18.805 -5.995  1.00 31.45  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 7.501   -19.239 -4.569  1.00 30.93  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 7.597   -18.414 -3.649  1.00 32.28  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 9.237   -18.307 -6.113  1.00 28.72  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 10.266  -19.328 -5.656  1.00 36.73  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 10.708  -20.331 -6.534  1.00 38.96  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 10.819  -19.273 -4.377  1.00 33.35  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 11.635  -21.271 -6.121  1.00 39.91  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 11.776  -20.207 -3.977  1.00 35.89  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 12.183  -21.199 -4.856  1.00 38.17  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 7.226   -20.541 -4.399  1.00 30.78  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 6.841   -21.042 -3.088  1.00 28.79  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 8.104   -21.551 -2.396  1.00 33.18  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 8.765   -22.465 -2.907  1.00 32.48  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 5.815   -22.170 -3.301  1.00 33.70  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 4.434   -21.677 -3.743  1.00 32.47  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 4.135   -21.527 -5.089  1.00 38.94  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 3.433   -21.394 -2.814  1.00 34.39  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.886   -21.064 -5.488  1.00 36.45  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 2.188   -20.918 -3.211  1.00 32.94  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.915   -20.758 -4.550  1.00 36.51  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 8.460   -20.940 -1.261  1.00 29.21  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 9.583   -21.446 -0.479  1.00 30.70  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 9.308   -22.888 -0.033  1.00 36.35  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 8.150   -23.299 0.118   1.00 35.93  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 9.801   -20.538 0.743   1.00 30.44  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 10.258  -19.134 0.363   1.00 31.83  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 11.509  -18.937 -0.213  1.00 32.14  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 9.436   -18.026 0.538   1.00 30.55  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 11.912  -17.664 -0.586  1.00 31.10  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 9.854   -16.745 0.212   1.00 29.74  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 11.112  -16.558 -0.338  1.00 32.08  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 10.398  -23.637 0.196   1.00 33.39  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 10.338  -25.010 0.663   1.00 36.44  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 10.135  -26.007 -0.489  1.00 43.06  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 10.991  -26.838 -0.723  1.00 46.49  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 9.011   -25.921 -1.217  1.00 41.86  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 8.754   -26.828 -2.334  1.00 39.90  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 9.526   -26.355 -3.561  1.00 40.51  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 9.767   -27.111 -4.494  1.00 44.22  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 7.257   -26.865 -2.655  1.00 41.19  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 6.933   -25.531 -3.020  1.00 41.62  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 6.362   -27.260 -1.498  1.00 38.80  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 9.837   -25.066 -3.588  1.00 36.68  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 10.475  -24.384 -4.702  1.00 40.69  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 9.631   -24.475 -5.976  1.00 40.99  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 10.194  -24.380 -7.063  1.00 39.78  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 11.936  -24.834 -4.881  1.00 41.17  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 12.698  -24.883 -3.596  1.00 43.79  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 13.462  -25.963 -3.220  1.00 45.86  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 12.786  -23.997 -2.586  1.00 44.67  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 14.002  -25.724 -2.033  1.00 54.50  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 13.609  -24.534 -1.628  1.00 48.44  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 8.298   -24.607 -5.856  1.00 43.68  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 7.430   -24.586 -7.040  1.00 44.92  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 7.064   -23.144 -7.426  1.00 44.46  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 7.214   -22.226 -6.618  1.00 41.44  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 6.193   -25.464 -6.830  1.00 46.46  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 6.547   -26.940 -6.682  1.00 53.22  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 5.517   -27.899 -6.104  1.00 62.45  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 4.357   -27.510 -5.824  1.00 62.67  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 5.922   -29.069 -5.891  1.00 67.43  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 6.584   -22.950 -8.674  1.00 40.09  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 6.113   -21.667 -9.173  1.00 37.84  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 4.668   -21.837 -9.642  1.00 39.40  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 4.342   -22.790 -10.342 1.00 43.64  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 6.990   -21.146 -10.311 1.00 39.50  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 8.292   -20.890 -9.804  1.00 38.83  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 6.501   -19.822 -10.890 1.00 44.94  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 3.797   -20.922 -9.233  1.00 38.97  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 2.451   -20.887 -9.781  1.00 36.62  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 2.121   -19.440 -10.108 1.00 39.04  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.864   -18.545 -9.725  1.00 37.30  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 1.452   -21.515 -8.829  1.00 33.57  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 1.043   -19.230 -10.872 1.00 34.18  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? 0.655   -17.900 -11.299 1.00 35.41  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -0.608  -17.525 -10.544 1.00 41.37  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -1.613  -18.237 -10.619 1.00 41.40  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? 0.315   -17.894 -12.790 1.00 40.80  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 1.515   -18.161 -13.686 1.00 40.23  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 2.660   -17.360 -13.609 1.00 44.53  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 1.510   -19.244 -14.565 1.00 42.50  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 3.770   -17.603 -14.422 1.00 48.74  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 2.628   -19.491 -15.368 1.00 42.11  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 3.746   -18.674 -15.305 1.00 45.54  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -0.535  -16.418 -9.798  1.00 33.87  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -1.633  -16.051 -8.911  1.00 31.61  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -1.929  -14.559 -9.041  1.00 35.45  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.048  -13.750 -9.380  1.00 36.02  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -1.183  -16.370 -7.483  1.00 31.69  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -1.275  -17.828 -7.018  1.00 35.84  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -0.827  -17.925 -5.545  1.00 35.45  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -2.705  -18.339 -7.195  1.00 33.84  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -3.167  -14.179 -8.705  1.00 33.55  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -3.538  -12.775 -8.686  1.00 30.12  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -3.578  -12.272 -7.236  1.00 27.88  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -3.509  -13.083 -6.303  1.00 31.37  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -3.668  -10.942 -7.024  1.00 27.73  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -3.597  -10.332 -5.686  1.00 27.60  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -4.580  -10.856 -4.636  1.00 32.00  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -4.294  -10.783 -3.441  1.00 27.83  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -3.933  -8.903  -6.008  1.00 28.66  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -3.283  -8.713  -7.348  1.00 32.06  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -3.718  -9.941  -8.107  1.00 29.77  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -5.727  -11.408 -5.072  1.00 28.51  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -6.670  -11.903 -4.066  1.00 31.01  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.088  -13.073 -3.267  1.00 33.41  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -6.578  -13.406 -2.191  1.00 30.72  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -7.965  -12.418 -4.713  1.00 34.34  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -7.881  -13.784 -5.394  1.00 39.42  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.169  -14.120 -6.154  1.00 48.10  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.150  -15.384 -6.965  1.00 47.28  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -8.837  -16.579 -6.172  1.00 52.11  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.072  -13.752 -3.817  1.00 29.83  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -4.490  -14.889 -3.141  1.00 30.35  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -3.139  -14.560 -2.505  1.00 29.30  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -2.454  -15.488 -2.078  1.00 35.27  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -4.357  -16.071 -4.073  1.00 32.26  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -5.721  -16.660 -4.397  1.00 39.89  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -6.548  -16.752 -3.431  1.00 34.20  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -5.943  -16.958 -5.586  1.00 37.02  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -2.796  -13.269 -2.455  1.00 31.67  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -1.492  -12.825 -1.965  1.00 31.30  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -1.666  -11.939 -0.719  1.00 26.87  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -2.303  -10.888 -0.769  1.00 29.85  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -0.744  -12.098 -3.092  1.00 28.35  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -0.599  -12.832 -4.429  1.00 31.09  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? 0.073   -11.924 -5.441  1.00 34.40  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? 0.184   -14.117 -4.311  1.00 32.79  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.039  -12.364 0.392   1.00 30.09  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.115  -11.657 1.655   1.00 29.48  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? 0.282   -11.211 2.085   1.00 34.26  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 1.126   -12.059 2.384   1.00 35.92  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -1.543  -12.790 2.592   1.00 29.04  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.002  -13.195 2.392   1.00 29.44  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -3.340  -14.163 1.442   1.00 29.99  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.013  -12.655 3.197   1.00 31.94  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -4.676  -14.518 1.226   1.00 37.00  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -5.345  -13.023 3.001   1.00 34.03  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -5.667  -13.968 2.032   1.00 31.90  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? 0.542   -9.891  2.157   1.00 37.99  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 1.837   -9.378  2.637   1.00 39.56  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 2.388   -10.095 3.869   1.00 38.94  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 1.673   -10.305 4.858   1.00 37.83  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 1.522   -7.887  2.879   1.00 34.59  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? 0.533   -7.567  1.754   1.00 41.37  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -0.373  -8.811  1.722   1.00 35.83  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 3.684   -10.455 3.795   1.00 32.09  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 4.287   -11.363 4.779   1.00 31.62  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 4.297   -10.759 6.184   1.00 32.34  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.888   -11.415 7.150   1.00 34.71  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 5.703   -11.766 4.353   1.00 31.47  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 6.471   -12.534 5.411   1.00 32.33  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 6.194   -13.869 5.668   1.00 32.17  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 7.488   -11.917 6.154   1.00 37.53  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.886   -14.581 6.632   1.00 33.85  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 8.178   -12.622 7.134   1.00 37.88  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.884   -13.950 7.362   1.00 36.84  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 8.570   -14.698 8.289   1.00 42.36  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 4.693   -9.494  6.270   1.00 31.44  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.852   -8.861  7.570   1.00 40.62  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 3.531   -8.839  8.339   1.00 39.45  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 3.485   -9.307  9.466   1.00 43.12  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 5.437   -7.461  7.497   1.00 44.64  ? 62  ASP   A CB  1 
ATOM   497  C CG  . ASP   A 1 63 ? 5.850   -6.938  8.867   1.00 65.93  ? 62  ASP   A CG  1 
ATOM   498  O OD1 . ASP   A 1 63 ? 6.659   -7.635  9.533   1.00 68.98  ? 62  ASP   A OD1 1 
ATOM   499  O OD2 . ASP   A 1 63 ? 5.316   -5.877  9.285   1.00 77.59  ? 62  ASP   A OD2 1 
ATOM   500  N N   . LYS   A 1 64 ? 2.466   -8.334  7.698   1.00 46.01  ? 63  LYS   A N   1 
ATOM   501  C CA  . LYS   A 1 64 ? 1.137   -8.256  8.307   1.00 46.14  ? 63  LYS   A CA  1 
ATOM   502  C C   . LYS   A 1 64 ? 0.575   -9.623  8.704   1.00 41.49  ? 63  LYS   A C   1 
ATOM   503  O O   . LYS   A 1 64 ? -0.191  -9.708  9.656   1.00 40.26  ? 63  LYS   A O   1 
ATOM   504  C CB  . LYS   A 1 64 ? 0.231   -7.498  7.326   1.00 47.18  ? 63  LYS   A CB  1 
ATOM   505  C CG  . LYS   A 1 64 ? -1.258  -7.466  7.635   1.00 54.68  ? 63  LYS   A CG  1 
ATOM   506  C CD  . LYS   A 1 64 ? -2.038  -6.699  6.569   1.00 47.91  ? 63  LYS   A CD  1 
ATOM   507  C CE  . LYS   A 1 64 ? -3.115  -5.881  7.225   1.00 52.76  ? 63  LYS   A CE  1 
ATOM   508  N NZ  . LYS   A 1 64 ? -4.324  -6.622  7.574   1.00 54.09  ? 63  LYS   A NZ  1 
ATOM   509  N N   . SER   A 1 65 ? 0.900   -10.695 7.962   1.00 38.29  ? 64  SER   A N   1 
ATOM   510  C CA  . SER   A 1 65 ? 0.180   -11.960 8.060   1.00 37.25  ? 64  SER   A CA  1 
ATOM   511  C C   . SER   A 1 65 ? 0.951   -13.039 8.818   1.00 37.79  ? 64  SER   A C   1 
ATOM   512  O O   . SER   A 1 65 ? 0.428   -14.136 9.005   1.00 40.46  ? 64  SER   A O   1 
ATOM   513  C CB  . SER   A 1 65 ? -0.190  -12.505 6.687   1.00 37.48  ? 64  SER   A CB  1 
ATOM   514  O OG  . SER   A 1 65 ? -0.943  -11.554 5.953   1.00 50.58  ? 64  SER   A OG  1 
ATOM   515  N N   . LYS   A 1 66 ? 2.212   -12.780 9.182   1.00 42.09  ? 65  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 66 ? 3.037   -13.880 9.663   1.00 42.97  ? 65  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 66 ? 2.559   -14.435 11.002  1.00 43.08  ? 65  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 66 ? 2.676   -15.642 11.241  1.00 43.21  ? 65  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 66 ? 4.537   -13.580 9.647   1.00 44.06  ? 65  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 66 ? 5.049   -12.490 10.531  1.00 45.41  ? 65  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 66 ? 6.517   -12.277 10.177  1.00 57.29  ? 65  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 66 ? 7.235   -11.458 11.201  1.00 61.34  ? 65  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 66 ? 6.335   -10.387 11.634  1.00 60.51  ? 65  LYS   A NZ  1 
ATOM   524  N N   A ASP   A 1 67 ? 2.022   -13.559 11.856  0.50 45.75  ? 66  ASP   A N   1 
ATOM   525  N N   B ASP   A 1 67 ? 2.059   -13.552 11.876  0.50 45.88  ? 66  ASP   A N   1 
ATOM   526  C CA  A ASP   A 1 67 ? 1.494   -13.966 13.154  0.50 50.18  ? 66  ASP   A CA  1 
ATOM   527  C CA  B ASP   A 1 67 ? 1.467   -13.963 13.145  0.50 50.52  ? 66  ASP   A CA  1 
ATOM   528  C C   A ASP   A 1 67 ? 0.393   -15.018 12.986  0.50 51.43  ? 66  ASP   A C   1 
ATOM   529  C C   B ASP   A 1 67 ? 0.487   -15.105 12.889  0.50 50.48  ? 66  ASP   A C   1 
ATOM   530  O O   A ASP   A 1 67 ? 0.305   -15.954 13.776  0.50 52.26  ? 66  ASP   A O   1 
ATOM   531  O O   B ASP   A 1 67 ? 0.578   -16.168 13.505  0.50 46.41  ? 66  ASP   A O   1 
ATOM   532  C CB  A ASP   A 1 67 ? 1.154   -12.765 14.028  0.50 50.43  ? 66  ASP   A CB  1 
ATOM   533  C CB  B ASP   A 1 67 ? 0.775   -12.804 13.850  0.50 53.18  ? 66  ASP   A CB  1 
ATOM   534  C CG  A ASP   A 1 67 ? 2.349   -12.094 14.695  0.50 52.32  ? 66  ASP   A CG  1 
ATOM   535  C CG  B ASP   A 1 67 ? 0.188   -13.107 15.226  0.50 57.32  ? 66  ASP   A CG  1 
ATOM   536  O OD1 A ASP   A 1 67 ? 3.480   -12.586 14.496  0.50 49.89  ? 66  ASP   A OD1 1 
ATOM   537  O OD1 B ASP   A 1 67 ? 0.947   -13.050 16.222  0.50 54.94  ? 66  ASP   A OD1 1 
ATOM   538  O OD2 A ASP   A 1 67 ? 2.150   -11.083 15.407  0.50 50.04  ? 66  ASP   A OD2 1 
ATOM   539  O OD2 B ASP   A 1 67 ? -1.023  -13.414 15.294  0.50 56.54  ? 66  ASP   A OD2 1 
ATOM   540  N N   . LYS   A 1 68 ? -0.416  -14.888 11.925  1.00 48.47  ? 67  LYS   A N   1 
ATOM   541  C CA  . LYS   A 1 68 ? -1.511  -15.807 11.669  1.00 45.34  ? 67  LYS   A CA  1 
ATOM   542  C C   . LYS   A 1 68 ? -1.050  -17.047 10.905  1.00 44.88  ? 67  LYS   A C   1 
ATOM   543  O O   . LYS   A 1 68 ? -1.500  -18.158 11.183  1.00 50.12  ? 67  LYS   A O   1 
ATOM   544  C CB  . LYS   A 1 68 ? -2.543  -15.012 10.864  1.00 50.95  ? 67  LYS   A CB  1 
ATOM   545  C CG  . LYS   A 1 68 ? -3.828  -15.731 10.565  1.00 52.13  ? 67  LYS   A CG  1 
ATOM   546  C CD  . LYS   A 1 68 ? -4.845  -14.777 9.950   1.00 50.80  ? 67  LYS   A CD  1 
ATOM   547  C CE  . LYS   A 1 68 ? -6.203  -15.402 9.909   1.00 52.69  ? 67  LYS   A CE  1 
ATOM   548  N NZ  . LYS   A 1 68 ? -7.212  -14.478 9.387   1.00 54.06  ? 67  LYS   A NZ  1 
ATOM   549  N N   . TYR   A 1 69 ? -0.176  -16.870 9.903   1.00 43.72  ? 68  TYR   A N   1 
ATOM   550  C CA  . TYR   A 1 69 ? 0.053   -17.957 8.966   1.00 36.75  ? 68  TYR   A CA  1 
ATOM   551  C C   . TYR   A 1 69 ? 1.448   -18.560 9.127   1.00 40.72  ? 68  TYR   A C   1 
ATOM   552  O O   . TYR   A 1 69 ? 1.712   -19.615 8.557   1.00 41.89  ? 68  TYR   A O   1 
ATOM   553  C CB  . TYR   A 1 69 ? -0.092  -17.497 7.510   1.00 36.34  ? 68  TYR   A CB  1 
ATOM   554  C CG  . TYR   A 1 69 ? -1.471  -17.004 7.112   1.00 41.03  ? 68  TYR   A CG  1 
ATOM   555  C CD1 . TYR   A 1 69 ? -2.622  -17.685 7.511   1.00 43.42  ? 68  TYR   A CD1 1 
ATOM   556  C CD2 . TYR   A 1 69 ? -1.618  -15.856 6.327   1.00 41.60  ? 68  TYR   A CD2 1 
ATOM   557  C CE1 . TYR   A 1 69 ? -3.881  -17.246 7.123   1.00 42.22  ? 68  TYR   A CE1 1 
ATOM   558  C CE2 . TYR   A 1 69 ? -2.875  -15.423 5.927   1.00 40.62  ? 68  TYR   A CE2 1 
ATOM   559  C CZ  . TYR   A 1 69 ? -4.011  -16.102 6.350   1.00 41.86  ? 68  TYR   A CZ  1 
ATOM   560  O OH  . TYR   A 1 69 ? -5.265  -15.665 5.980   1.00 40.98  ? 68  TYR   A OH  1 
ATOM   561  N N   . GLY   A 1 70 ? 2.303   -17.918 9.924   1.00 40.76  ? 69  GLY   A N   1 
ATOM   562  C CA  . GLY   A 1 70 ? 3.708   -18.302 9.995   1.00 41.13  ? 69  GLY   A CA  1 
ATOM   563  C C   . GLY   A 1 70 ? 4.005   -19.305 11.114  1.00 45.66  ? 69  GLY   A C   1 
ATOM   564  O O   . GLY   A 1 70 ? 4.965   -19.129 11.846  1.00 54.17  ? 69  GLY   A O   1 
ATOM   565  N N   . LYS   A 1 71 ? 3.202   -20.366 11.209  1.00 49.38  ? 70  LYS   A N   1 
ATOM   566  C CA  . LYS   A 1 71 ? 3.366   -21.412 12.205  1.00 52.88  ? 70  LYS   A CA  1 
ATOM   567  C C   . LYS   A 1 71 ? 3.646   -22.746 11.506  1.00 50.44  ? 70  LYS   A C   1 
ATOM   568  O O   . LYS   A 1 71 ? 3.267   -22.936 10.350  1.00 49.62  ? 70  LYS   A O   1 
ATOM   569  C CB  . LYS   A 1 71 ? 2.124   -21.424 13.108  1.00 52.77  ? 70  LYS   A CB  1 
ATOM   570  C CG  . LYS   A 1 71 ? 2.069   -20.293 14.125  1.00 49.16  ? 70  LYS   A CG  1 
ATOM   571  C CD  . LYS   A 1 71 ? 0.632   -19.932 14.483  1.00 55.74  ? 70  LYS   A CD  1 
ATOM   572  N N   . PRO   A 1 72 ? 4.354   -23.702 12.160  1.00 53.75  ? 71  PRO   A N   1 
ATOM   573  C CA  . PRO   A 1 72 ? 4.683   -24.988 11.531  1.00 49.99  ? 71  PRO   A CA  1 
ATOM   574  C C   . PRO   A 1 72 ? 3.503   -25.813 11.029  1.00 45.47  ? 71  PRO   A C   1 
ATOM   575  O O   . PRO   A 1 72 ? 2.409   -25.712 11.560  1.00 50.56  ? 71  PRO   A O   1 
ATOM   576  C CB  . PRO   A 1 72 ? 5.477   -25.724 12.621  1.00 55.57  ? 71  PRO   A CB  1 
ATOM   577  C CG  . PRO   A 1 72 ? 6.078   -24.598 13.430  1.00 59.34  ? 71  PRO   A CG  1 
ATOM   578  C CD  . PRO   A 1 72 ? 4.959   -23.557 13.498  1.00 54.83  ? 71  PRO   A CD  1 
ATOM   579  N N   . ASN   A 1 73 ? 3.761   -26.653 10.024  1.00 46.63  ? 72  ASN   A N   1 
ATOM   580  C CA  . ASN   A 1 73 ? 2.709   -27.326 9.286   1.00 58.74  ? 72  ASN   A CA  1 
ATOM   581  C C   . ASN   A 1 73 ? 3.226   -28.684 8.837   1.00 62.88  ? 72  ASN   A C   1 
ATOM   582  O O   . ASN   A 1 73 ? 4.384   -28.815 8.437   1.00 71.63  ? 72  ASN   A O   1 
ATOM   583  C CB  . ASN   A 1 73 ? 2.348   -26.511 8.051   1.00 59.90  ? 72  ASN   A CB  1 
ATOM   584  C CG  . ASN   A 1 73 ? 0.945   -26.766 7.570   1.00 76.83  ? 72  ASN   A CG  1 
ATOM   585  O OD1 . ASN   A 1 73 ? 0.707   -27.727 6.833   1.00 83.90  ? 72  ASN   A OD1 1 
ATOM   586  N ND2 . ASN   A 1 73 ? 0.017   -25.893 7.935   1.00 84.45  ? 72  ASN   A ND2 1 
ATOM   587  N N   . LYS   A 1 74 ? 2.338   -29.676 8.877   1.00 60.88  ? 73  LYS   A N   1 
ATOM   588  C CA  . LYS   A 1 74 ? 2.682   -31.041 8.519   1.00 64.45  ? 73  LYS   A CA  1 
ATOM   589  C C   . LYS   A 1 74 ? 3.047   -31.123 7.038   1.00 64.65  ? 73  LYS   A C   1 
ATOM   590  O O   . LYS   A 1 74 ? 3.750   -32.042 6.627   1.00 64.86  ? 73  LYS   A O   1 
ATOM   591  C CB  . LYS   A 1 74 ? 1.528   -31.974 8.918   1.00 75.98  ? 73  LYS   A CB  1 
ATOM   592  C CG  . LYS   A 1 74 ? 0.178   -31.754 8.231   1.00 78.35  ? 73  LYS   A CG  1 
ATOM   593  N N   . ARG   A 1 75 ? 2.589   -30.154 6.238   1.00 57.05  ? 74  ARG   A N   1 
ATOM   594  C CA  . ARG   A 1 75 ? 2.622   -30.329 4.795   1.00 57.88  ? 74  ARG   A CA  1 
ATOM   595  C C   . ARG   A 1 75 ? 4.055   -30.254 4.266   1.00 48.18  ? 74  ARG   A C   1 
ATOM   596  O O   . ARG   A 1 75 ? 4.869   -29.501 4.787   1.00 49.07  ? 74  ARG   A O   1 
ATOM   597  C CB  . ARG   A 1 75 ? 1.568   -29.444 4.120   1.00 59.22  ? 74  ARG   A CB  1 
ATOM   598  C CG  . ARG   A 1 75 ? 0.191   -29.993 4.456   1.00 56.68  ? 74  ARG   A CG  1 
ATOM   599  C CD  . ARG   A 1 75 ? -0.291  -30.898 3.345   1.00 55.02  ? 74  ARG   A CD  1 
ATOM   600  N NE  . ARG   A 1 75 ? -1.172  -30.183 2.414   1.00 71.46  ? 74  ARG   A NE  1 
ATOM   601  C CZ  . ARG   A 1 75 ? -2.309  -29.552 2.734   1.00 76.00  ? 74  ARG   A CZ  1 
ATOM   602  N NH1 . ARG   A 1 75 ? -3.101  -29.146 1.764   1.00 80.29  ? 74  ARG   A NH1 1 
ATOM   603  N NH2 . ARG   A 1 75 ? -2.687  -29.377 3.995   1.00 75.11  ? 74  ARG   A NH2 1 
ATOM   604  N N   . LYS   A 1 76 ? 4.340   -31.073 3.245   1.00 49.37  ? 75  LYS   A N   1 
ATOM   605  C CA  . LYS   A 1 76 ? 5.694   -31.310 2.765   1.00 53.53  ? 75  LYS   A CA  1 
ATOM   606  C C   . LYS   A 1 76 ? 6.289   -29.997 2.265   1.00 52.35  ? 75  LYS   A C   1 
ATOM   607  O O   . LYS   A 1 76 ? 5.683   -29.326 1.435   1.00 46.69  ? 75  LYS   A O   1 
ATOM   608  C CB  . LYS   A 1 76 ? 5.697   -32.327 1.618   1.00 50.98  ? 75  LYS   A CB  1 
ATOM   609  C CG  . LYS   A 1 76 ? 7.067   -32.620 0.988   1.00 57.29  ? 75  LYS   A CG  1 
ATOM   610  C CD  . LYS   A 1 76 ? 7.078   -33.743 -0.049  1.00 60.64  ? 75  LYS   A CD  1 
ATOM   611  C CE  . LYS   A 1 76 ? 8.464   -34.050 -0.556  1.00 58.34  ? 75  LYS   A CE  1 
ATOM   612  N N   . GLY   A 1 77 ? 7.480   -29.651 2.764   1.00 49.81  ? 76  GLY   A N   1 
ATOM   613  C CA  . GLY   A 1 77 ? 8.193   -28.468 2.313   1.00 45.03  ? 76  GLY   A CA  1 
ATOM   614  C C   . GLY   A 1 77 ? 7.848   -27.222 3.136   1.00 42.47  ? 76  GLY   A C   1 
ATOM   615  O O   . GLY   A 1 77 ? 8.573   -26.233 3.083   1.00 43.49  ? 76  GLY   A O   1 
ATOM   616  N N   . PHE   A 1 78 ? 6.773   -27.271 3.930   1.00 40.02  ? 77  PHE   A N   1 
ATOM   617  C CA  . PHE   A 1 78 ? 6.278   -26.064 4.562   1.00 37.92  ? 77  PHE   A CA  1 
ATOM   618  C C   . PHE   A 1 78 ? 7.295   -25.466 5.547   1.00 42.23  ? 77  PHE   A C   1 
ATOM   619  O O   . PHE   A 1 78 ? 7.543   -24.255 5.564   1.00 38.13  ? 77  PHE   A O   1 
ATOM   620  C CB  . PHE   A 1 78 ? 4.927   -26.366 5.210   1.00 39.44  ? 77  PHE   A CB  1 
ATOM   621  C CG  . PHE   A 1 78 ? 4.205   -25.089 5.607   1.00 42.06  ? 77  PHE   A CG  1 
ATOM   622  C CD1 . PHE   A 1 78 ? 4.504   -24.426 6.797   1.00 42.98  ? 77  PHE   A CD1 1 
ATOM   623  C CD2 . PHE   A 1 78 ? 3.216   -24.551 4.783   1.00 43.91  ? 77  PHE   A CD2 1 
ATOM   624  C CE1 . PHE   A 1 78 ? 3.839   -23.246 7.140   1.00 43.84  ? 77  PHE   A CE1 1 
ATOM   625  C CE2 . PHE   A 1 78 ? 2.545   -23.383 5.137   1.00 40.63  ? 77  PHE   A CE2 1 
ATOM   626  C CZ  . PHE   A 1 78 ? 2.862   -22.722 6.302   1.00 39.15  ? 77  PHE   A CZ  1 
ATOM   627  N N   . ASN   A 1 79 ? 7.851   -26.303 6.424   1.00 44.07  ? 78  ASN   A N   1 
ATOM   628  C CA  . ASN   A 1 79 ? 8.715   -25.830 7.498   1.00 38.55  ? 78  ASN   A CA  1 
ATOM   629  C C   . ASN   A 1 79 ? 10.038  -25.344 6.913   1.00 33.90  ? 78  ASN   A C   1 
ATOM   630  O O   . ASN   A 1 79 ? 10.620  -24.365 7.401   1.00 36.01  ? 78  ASN   A O   1 
ATOM   631  C CB  . ASN   A 1 79 ? 8.853   -26.914 8.564   1.00 40.56  ? 78  ASN   A CB  1 
ATOM   632  C CG  . ASN   A 1 79 ? 7.507   -27.202 9.191   1.00 50.11  ? 78  ASN   A CG  1 
ATOM   633  O OD1 . ASN   A 1 79 ? 6.601   -26.358 9.149   1.00 45.24  ? 78  ASN   A OD1 1 
ATOM   634  N ND2 . ASN   A 1 79 ? 7.360   -28.369 9.801   1.00 50.50  ? 78  ASN   A ND2 1 
ATOM   635  N N   . GLU   A 1 80 ? 10.511  -26.049 5.871   1.00 32.71  ? 79  GLU   A N   1 
ATOM   636  C CA  . GLU   A 1 80 ? 11.653  -25.563 5.106   1.00 39.53  ? 79  GLU   A CA  1 
ATOM   637  C C   . GLU   A 1 80 ? 11.330  -24.181 4.524   1.00 39.25  ? 79  GLU   A C   1 
ATOM   638  O O   . GLU   A 1 80 ? 12.131  -23.250 4.602   1.00 41.06  ? 79  GLU   A O   1 
ATOM   639  C CB  . GLU   A 1 80 ? 12.129  -26.550 4.036   1.00 37.71  ? 79  GLU   A CB  1 
ATOM   640  C CG  . GLU   A 1 80 ? 13.444  -26.107 3.404   1.00 34.47  ? 79  GLU   A CG  1 
ATOM   641  C CD  . GLU   A 1 80 ? 14.043  -27.049 2.360   1.00 54.88  ? 79  GLU   A CD  1 
ATOM   642  O OE1 . GLU   A 1 80 ? 13.373  -28.016 1.949   1.00 59.20  ? 79  GLU   A OE1 1 
ATOM   643  O OE2 . GLU   A 1 80 ? 15.205  -26.813 1.945   1.00 59.34  ? 79  GLU   A OE2 1 
ATOM   644  N N   . GLY   A 1 81 ? 10.133  -24.058 3.942   1.00 40.46  ? 80  GLY   A N   1 
ATOM   645  C CA  . GLY   A 1 81 ? 9.609   -22.786 3.468   1.00 39.61  ? 80  GLY   A CA  1 
ATOM   646  C C   . GLY   A 1 81 ? 9.666   -21.647 4.493   1.00 34.49  ? 80  GLY   A C   1 
ATOM   647  O O   . GLY   A 1 81 ? 10.049  -20.544 4.133   1.00 32.18  ? 80  GLY   A O   1 
ATOM   648  N N   . LEU   A 1 82 ? 9.272   -21.902 5.745   1.00 29.66  ? 81  LEU   A N   1 
ATOM   649  C CA  . LEU   A 1 82 ? 9.274   -20.897 6.794   1.00 35.54  ? 81  LEU   A CA  1 
ATOM   650  C C   . LEU   A 1 82 ? 10.707  -20.445 7.074   1.00 33.57  ? 81  LEU   A C   1 
ATOM   651  O O   . LEU   A 1 82 ? 10.916  -19.296 7.458   1.00 31.49  ? 81  LEU   A O   1 
ATOM   652  C CB  . LEU   A 1 82 ? 8.628   -21.400 8.084   1.00 38.01  ? 81  LEU   A CB  1 
ATOM   653  C CG  . LEU   A 1 82 ? 7.133   -21.747 8.006   1.00 40.83  ? 81  LEU   A CG  1 
ATOM   654  C CD1 . LEU   A 1 82 ? 6.806   -22.264 9.391   1.00 45.88  ? 81  LEU   A CD1 1 
ATOM   655  C CD2 . LEU   A 1 82 ? 6.212   -20.573 7.667   1.00 36.37  ? 81  LEU   A CD2 1 
ATOM   656  N N   . TRP   A 1 83 ? 11.673  -21.353 6.915   1.00 38.50  ? 82  TRP   A N   1 
ATOM   657  C CA  . TRP   A 1 83 ? 13.046  -21.009 7.286   1.00 40.21  ? 82  TRP   A CA  1 
ATOM   658  C C   . TRP   A 1 83 ? 13.596  -20.097 6.194   1.00 33.70  ? 82  TRP   A C   1 
ATOM   659  O O   . TRP   A 1 83 ? 14.266  -19.112 6.469   1.00 32.83  ? 82  TRP   A O   1 
ATOM   660  C CB  . TRP   A 1 83 ? 13.915  -22.268 7.458   1.00 39.47  ? 82  TRP   A CB  1 
ATOM   661  C CG  . TRP   A 1 83 ? 15.355  -21.972 7.775   1.00 35.50  ? 82  TRP   A CG  1 
ATOM   662  C CD1 . TRP   A 1 83 ? 15.931  -21.937 9.016   1.00 40.23  ? 82  TRP   A CD1 1 
ATOM   663  C CD2 . TRP   A 1 83 ? 16.396  -21.642 6.830   1.00 33.82  ? 82  TRP   A CD2 1 
ATOM   664  N NE1 . TRP   A 1 83 ? 17.253  -21.594 8.906   1.00 37.22  ? 82  TRP   A NE1 1 
ATOM   665  C CE2 . TRP   A 1 83 ? 17.564  -21.408 7.580   1.00 37.71  ? 82  TRP   A CE2 1 
ATOM   666  C CE3 . TRP   A 1 83 ? 16.445  -21.526 5.432   1.00 35.61  ? 82  TRP   A CE3 1 
ATOM   667  C CZ2 . TRP   A 1 83 ? 18.772  -21.086 6.972   1.00 35.34  ? 82  TRP   A CZ2 1 
ATOM   668  C CZ3 . TRP   A 1 83 ? 17.638  -21.201 4.832   1.00 37.75  ? 82  TRP   A CZ3 1 
ATOM   669  C CH2 . TRP   A 1 83 ? 18.781  -20.964 5.605   1.00 38.34  ? 82  TRP   A CH2 1 
ATOM   670  N N   . GLU   A 1 84 ? 13.235  -20.419 4.953   1.00 31.73  ? 83  GLU   A N   1 
ATOM   671  C CA  . GLU   A 1 84 ? 13.748  -19.708 3.798   1.00 29.88  ? 83  GLU   A CA  1 
ATOM   672  C C   . GLU   A 1 84 ? 13.240  -18.267 3.842   1.00 31.41  ? 83  GLU   A C   1 
ATOM   673  O O   . GLU   A 1 84 ? 14.008  -17.316 3.663   1.00 34.08  ? 83  GLU   A O   1 
ATOM   674  C CB  . GLU   A 1 84 ? 13.313  -20.451 2.528   1.00 31.43  ? 83  GLU   A CB  1 
ATOM   675  C CG  . GLU   A 1 84 ? 14.058  -21.766 2.288   1.00 34.85  ? 83  GLU   A CG  1 
ATOM   676  C CD  . GLU   A 1 84 ? 13.661  -22.489 1.008   1.00 38.38  ? 83  GLU   A CD  1 
ATOM   677  O OE1 . GLU   A 1 84 ? 12.820  -21.956 0.264   1.00 36.79  ? 83  GLU   A OE1 1 
ATOM   678  O OE2 . GLU   A 1 84 ? 14.165  -23.593 0.737   1.00 41.05  ? 83  GLU   A OE2 1 
ATOM   679  N N   . ILE   A 1 85 ? 11.929  -18.085 4.091   1.00 29.07  ? 84  ILE   A N   1 
ATOM   680  C CA  . ILE   A 1 85 ? 11.365  -16.734 3.974   1.00 26.26  ? 84  ILE   A CA  1 
ATOM   681  C C   . ILE   A 1 85 ? 11.886  -15.850 5.126   1.00 26.56  ? 84  ILE   A C   1 
ATOM   682  O O   . ILE   A 1 85 ? 11.975  -14.624 5.010   1.00 28.14  ? 84  ILE   A O   1 
ATOM   683  C CB  . ILE   A 1 85 ? 9.825   -16.750 3.881   1.00 28.05  ? 84  ILE   A CB  1 
ATOM   684  C CG1 . ILE   A 1 85 ? 9.268   -15.344 3.517   1.00 32.71  ? 84  ILE   A CG1 1 
ATOM   685  C CG2 . ILE   A 1 85 ? 9.229   -17.239 5.199   1.00 29.22  ? 84  ILE   A CG2 1 
ATOM   686  C CD1 . ILE   A 1 85 ? 7.843   -15.359 2.948   1.00 31.16  ? 84  ILE   A CD1 1 
ATOM   687  N N   . GLN   A 1 86 ? 12.300  -16.473 6.234   1.00 27.58  ? 85  GLN   A N   1 
ATOM   688  C CA  . GLN   A 1 86 ? 12.782  -15.719 7.395   1.00 29.88  ? 85  GLN   A CA  1 
ATOM   689  C C   . GLN   A 1 86 ? 14.281  -15.451 7.294   1.00 33.62  ? 85  GLN   A C   1 
ATOM   690  O O   . GLN   A 1 86 ? 14.746  -14.387 7.716   1.00 37.40  ? 85  GLN   A O   1 
ATOM   691  C CB  . GLN   A 1 86 ? 12.423  -16.479 8.682   1.00 37.20  ? 85  GLN   A CB  1 
ATOM   692  C CG  . GLN   A 1 86 ? 12.900  -15.853 9.993   1.00 43.88  ? 85  GLN   A CG  1 
ATOM   693  C CD  . GLN   A 1 86 ? 12.138  -16.398 11.200  1.00 51.36  ? 85  GLN   A CD  1 
ATOM   694  O OE1 . GLN   A 1 86 ? 11.953  -17.613 11.364  1.00 48.20  ? 85  GLN   A OE1 1 
ATOM   695  N NE2 . GLN   A 1 86 ? 11.648  -15.510 12.057  1.00 49.98  ? 85  GLN   A NE2 1 
ATOM   696  N N   . ASN   A 1 87 ? 15.011  -16.363 6.656   1.00 32.15  ? 86  ASN   A N   1 
ATOM   697  C CA  . ASN   A 1 87 ? 16.461  -16.407 6.791   1.00 32.35  ? 86  ASN   A CA  1 
ATOM   698  C C   . ASN   A 1 87 ? 17.191  -15.993 5.513   1.00 36.80  ? 86  ASN   A C   1 
ATOM   699  O O   . ASN   A 1 87 ? 18.276  -15.424 5.645   1.00 34.83  ? 86  ASN   A O   1 
ATOM   700  C CB  . ASN   A 1 87 ? 16.914  -17.714 7.443   1.00 32.04  ? 86  ASN   A CB  1 
ATOM   701  C CG  . ASN   A 1 87 ? 16.392  -17.804 8.857   1.00 38.57  ? 86  ASN   A CG  1 
ATOM   702  O OD1 . ASN   A 1 87 ? 16.729  -16.959 9.702   1.00 38.99  ? 86  ASN   A OD1 1 
ATOM   703  N ND2 . ASN   A 1 87 ? 15.490  -18.738 9.117   1.00 36.27  ? 86  ASN   A ND2 1 
ATOM   704  N N   . ASN   A 1 88 ? 16.666  -16.324 4.305   1.00 30.19  ? 87  ASN   A N   1 
ATOM   705  C CA  . ASN   A 1 88 ? 17.299  -15.887 3.067   1.00 32.33  ? 87  ASN   A CA  1 
ATOM   706  C C   . ASN   A 1 88 ? 16.231  -15.784 1.966   1.00 31.39  ? 87  ASN   A C   1 
ATOM   707  O O   . ASN   A 1 88 ? 16.159  -16.609 1.046   1.00 32.85  ? 87  ASN   A O   1 
ATOM   708  C CB  . ASN   A 1 88 ? 18.404  -16.863 2.680   1.00 35.00  ? 87  ASN   A CB  1 
ATOM   709  C CG  . ASN   A 1 88 ? 19.488  -16.234 1.847   1.00 35.25  ? 87  ASN   A CG  1 
ATOM   710  O OD1 . ASN   A 1 88 ? 19.268  -15.226 1.172   1.00 34.94  ? 87  ASN   A OD1 1 
ATOM   711  N ND2 . ASN   A 1 88 ? 20.669  -16.841 1.850   1.00 38.58  ? 87  ASN   A ND2 1 
ATOM   712  N N   . PRO   A 1 89 ? 15.277  -14.842 2.087   1.00 32.07  ? 88  PRO   A N   1 
ATOM   713  C CA  . PRO   A 1 89 ? 14.155  -14.833 1.149   1.00 31.35  ? 88  PRO   A CA  1 
ATOM   714  C C   . PRO   A 1 89 ? 14.501  -14.437 -0.285  1.00 32.37  ? 88  PRO   A C   1 
ATOM   715  O O   . PRO   A 1 89 ? 13.688  -14.656 -1.187  1.00 31.05  ? 88  PRO   A O   1 
ATOM   716  C CB  . PRO   A 1 89 ? 13.158  -13.922 1.812   1.00 26.52  ? 88  PRO   A CB  1 
ATOM   717  C CG  . PRO   A 1 89 ? 13.983  -12.937 2.644   1.00 27.49  ? 88  PRO   A CG  1 
ATOM   718  C CD  . PRO   A 1 89 ? 15.162  -13.807 3.140   1.00 26.84  ? 88  PRO   A CD  1 
ATOM   719  N N   . HIS   A 1 90 ? 15.710  -13.898 -0.499  1.00 31.34  ? 89  HIS   A N   1 
ATOM   720  C CA  . HIS   A 1 90 ? 16.058  -13.347 -1.800  1.00 30.38  ? 89  HIS   A CA  1 
ATOM   721  C C   . HIS   A 1 90 ? 17.149  -14.160 -2.499  1.00 31.65  ? 89  HIS   A C   1 
ATOM   722  O O   . HIS   A 1 90 ? 17.660  -13.696 -3.521  1.00 29.12  ? 89  HIS   A O   1 
ATOM   723  C CB  . HIS   A 1 90 ? 16.424  -11.871 -1.652  1.00 29.39  ? 89  HIS   A CB  1 
ATOM   724  C CG  . HIS   A 1 90 ? 15.339  -11.015 -1.086  1.00 34.41  ? 89  HIS   A CG  1 
ATOM   725  N ND1 . HIS   A 1 90 ? 14.049  -10.953 -1.597  1.00 32.28  ? 89  HIS   A ND1 1 
ATOM   726  C CD2 . HIS   A 1 90 ? 15.374  -10.193 -0.020  1.00 32.24  ? 89  HIS   A CD2 1 
ATOM   727  C CE1 . HIS   A 1 90 ? 13.335  -10.094 -0.866  1.00 28.40  ? 89  HIS   A CE1 1 
ATOM   728  N NE2 . HIS   A 1 90 ? 14.117  -9.631  0.112   1.00 31.96  ? 89  HIS   A NE2 1 
ATOM   729  N N   . ALA   A 1 91 ? 17.437  -15.356 -1.960  1.00 33.19  ? 90  ALA   A N   1 
ATOM   730  C CA  . ALA   A 1 91 ? 18.451  -16.296 -2.435  1.00 36.61  ? 90  ALA   A CA  1 
ATOM   731  C C   . ALA   A 1 91 ? 17.990  -16.991 -3.709  1.00 39.90  ? 90  ALA   A C   1 
ATOM   732  O O   . ALA   A 1 91 ? 16.783  -17.125 -3.984  1.00 38.01  ? 90  ALA   A O   1 
ATOM   733  C CB  . ALA   A 1 91 ? 18.758  -17.337 -1.372  1.00 36.25  ? 90  ALA   A CB  1 
ATOM   734  N N   . SER   A 1 92 ? 18.985  -17.390 -4.514  1.00 36.00  ? 91  SER   A N   1 
ATOM   735  C CA  . SER   A 1 92 ? 18.706  -18.294 -5.617  1.00 40.47  ? 91  SER   A CA  1 
ATOM   736  C C   . SER   A 1 92 ? 18.391  -19.673 -5.057  1.00 41.19  ? 91  SER   A C   1 
ATOM   737  O O   . SER   A 1 92 ? 19.207  -20.216 -4.315  1.00 46.67  ? 91  SER   A O   1 
ATOM   738  C CB  . SER   A 1 92 ? 19.898  -18.374 -6.527  1.00 46.77  ? 91  SER   A CB  1 
ATOM   739  O OG  . SER   A 1 92 ? 19.635  -19.414 -7.457  1.00 53.38  ? 91  SER   A OG  1 
ATOM   740  N N   . TYR   A 1 93 ? 17.231  -20.245 -5.412  1.00 43.73  ? 92  TYR   A N   1 
ATOM   741  C CA  . TYR   A 1 93 ? 16.870  -21.589 -4.971  1.00 41.42  ? 92  TYR   A CA  1 
ATOM   742  C C   . TYR   A 1 93 ? 16.850  -22.553 -6.161  1.00 51.14  ? 92  TYR   A C   1 
ATOM   743  O O   . TYR   A 1 93 ? 16.255  -23.623 -6.085  1.00 55.06  ? 92  TYR   A O   1 
ATOM   744  C CB  . TYR   A 1 93 ? 15.567  -21.659 -4.162  1.00 39.07  ? 92  TYR   A CB  1 
ATOM   745  C CG  . TYR   A 1 93 ? 15.723  -21.087 -2.762  1.00 40.24  ? 92  TYR   A CG  1 
ATOM   746  C CD1 . TYR   A 1 93 ? 16.182  -21.889 -1.725  1.00 39.63  ? 92  TYR   A CD1 1 
ATOM   747  C CD2 . TYR   A 1 93 ? 15.435  -19.744 -2.489  1.00 39.75  ? 92  TYR   A CD2 1 
ATOM   748  C CE1 . TYR   A 1 93 ? 16.348  -21.351 -0.453  1.00 47.24  ? 92  TYR   A CE1 1 
ATOM   749  C CE2 . TYR   A 1 93 ? 15.579  -19.206 -1.219  1.00 35.59  ? 92  TYR   A CE2 1 
ATOM   750  C CZ  . TYR   A 1 93 ? 16.048  -20.020 -0.200  1.00 41.49  ? 92  TYR   A CZ  1 
ATOM   751  O OH  . TYR   A 1 93 ? 16.236  -19.534 1.059   1.00 45.31  ? 92  TYR   A OH  1 
ATOM   752  N N   . SER   A 1 94 ? 17.515  -22.183 -7.258  1.00 61.80  ? 93  SER   A N   1 
ATOM   753  C CA  . SER   A 1 94 ? 17.716  -23.113 -8.360  1.00 81.43  ? 93  SER   A CA  1 
ATOM   754  C C   . SER   A 1 94 ? 18.766  -24.175 -7.986  1.00 89.35  ? 93  SER   A C   1 
ATOM   755  O O   . SER   A 1 94 ? 19.970  -23.828 -7.994  1.00 85.97  ? 93  SER   A O   1 
ATOM   756  C CB  . SER   A 1 94 ? 18.069  -22.396 -9.635  1.00 80.21  ? 93  SER   A CB  1 
ATOM   757  O OG  . SER   A 1 94 ? 16.882  -21.907 -10.240 1.00 80.93  ? 93  SER   A OG  1 
ATOM   758  O OXT . SER   A 1 94 ? 18.343  -25.317 -7.689  1.00 103.93 ? 93  SER   A OXT 1 
ATOM   759  N N   . MET   B 1 2  ? 38.641  -10.943 -42.833 1.00 103.19 ? 1   MET   B N   1 
ATOM   760  C CA  . MET   B 1 2  ? 38.417  -11.954 -43.900 1.00 98.46  ? 1   MET   B CA  1 
ATOM   761  C C   . MET   B 1 2  ? 36.936  -12.326 -43.917 1.00 86.66  ? 1   MET   B C   1 
ATOM   762  O O   . MET   B 1 2  ? 36.451  -12.903 -42.948 1.00 94.68  ? 1   MET   B O   1 
ATOM   763  C CB  . MET   B 1 2  ? 39.271  -13.202 -43.642 1.00 102.95 ? 1   MET   B CB  1 
ATOM   764  C CG  . MET   B 1 2  ? 39.414  -14.128 -44.844 1.00 115.67 ? 1   MET   B CG  1 
ATOM   765  S SD  . MET   B 1 2  ? 40.328  -13.481 -46.261 1.00 97.45  ? 1   MET   B SD  1 
ATOM   766  C CE  . MET   B 1 2  ? 41.783  -12.814 -45.442 1.00 86.94  ? 1   MET   B CE  1 
ATOM   767  N N   . PRO   B 1 3  ? 36.173  -12.005 -44.995 1.00 81.47  ? 2   PRO   B N   1 
ATOM   768  C CA  . PRO   B 1 3  ? 34.733  -12.288 -45.032 1.00 74.97  ? 2   PRO   B CA  1 
ATOM   769  C C   . PRO   B 1 3  ? 34.424  -13.744 -44.682 1.00 70.86  ? 2   PRO   B C   1 
ATOM   770  O O   . PRO   B 1 3  ? 35.084  -14.646 -45.188 1.00 66.96  ? 2   PRO   B O   1 
ATOM   771  C CB  . PRO   B 1 3  ? 34.278  -11.925 -46.465 1.00 71.85  ? 2   PRO   B CB  1 
ATOM   772  C CG  . PRO   B 1 3  ? 35.386  -11.046 -47.016 1.00 67.54  ? 2   PRO   B CG  1 
ATOM   773  C CD  . PRO   B 1 3  ? 36.649  -11.340 -46.219 1.00 67.69  ? 2   PRO   B CD  1 
ATOM   774  N N   . HIS   B 1 4  ? 33.437  -13.956 -43.795 1.00 67.41  ? 3   HIS   B N   1 
ATOM   775  C CA  . HIS   B 1 4  ? 32.922  -15.287 -43.506 1.00 63.65  ? 3   HIS   B CA  1 
ATOM   776  C C   . HIS   B 1 4  ? 31.532  -15.437 -44.131 1.00 59.43  ? 3   HIS   B C   1 
ATOM   777  O O   . HIS   B 1 4  ? 31.039  -14.502 -44.758 1.00 51.63  ? 3   HIS   B O   1 
ATOM   778  C CB  . HIS   B 1 4  ? 33.015  -15.594 -42.009 1.00 66.30  ? 3   HIS   B CB  1 
ATOM   779  C CG  . HIS   B 1 4  ? 34.402  -15.502 -41.472 1.00 76.07  ? 3   HIS   B CG  1 
ATOM   780  N ND1 . HIS   B 1 4  ? 35.481  -16.115 -42.073 1.00 75.29  ? 3   HIS   B ND1 1 
ATOM   781  C CD2 . HIS   B 1 4  ? 34.882  -14.888 -40.378 1.00 71.01  ? 3   HIS   B CD2 1 
ATOM   782  C CE1 . HIS   B 1 4  ? 36.577  -15.857 -41.369 1.00 78.05  ? 3   HIS   B CE1 1 
ATOM   783  N NE2 . HIS   B 1 4  ? 36.236  -15.113 -40.334 1.00 79.21  ? 3   HIS   B NE2 1 
ATOM   784  N N   . ALA   B 1 5  ? 30.934  -16.632 -43.993 1.00 52.18  ? 4   ALA   B N   1 
ATOM   785  C CA  . ALA   B 1 5  ? 29.605  -16.929 -44.506 1.00 55.25  ? 4   ALA   B CA  1 
ATOM   786  C C   . ALA   B 1 5  ? 28.609  -15.889 -43.998 1.00 51.85  ? 4   ALA   B C   1 
ATOM   787  O O   . ALA   B 1 5  ? 27.716  -15.473 -44.735 1.00 52.67  ? 4   ALA   B O   1 
ATOM   788  C CB  . ALA   B 1 5  ? 29.198  -18.311 -44.047 1.00 55.20  ? 4   ALA   B CB  1 
ATOM   789  N N   . PHE   B 1 6  ? 28.764  -15.535 -42.716 1.00 52.05  ? 5   PHE   B N   1 
ATOM   790  C CA  . PHE   B 1 6  ? 27.978  -14.523 -42.022 1.00 61.11  ? 5   PHE   B CA  1 
ATOM   791  C C   . PHE   B 1 6  ? 28.878  -13.316 -41.771 1.00 61.72  ? 5   PHE   B C   1 
ATOM   792  O O   . PHE   B 1 6  ? 30.001  -13.465 -41.288 1.00 57.74  ? 5   PHE   B O   1 
ATOM   793  C CB  . PHE   B 1 6  ? 27.448  -14.982 -40.652 1.00 55.75  ? 5   PHE   B CB  1 
ATOM   794  C CG  . PHE   B 1 6  ? 26.392  -16.078 -40.699 1.00 51.90  ? 5   PHE   B CG  1 
ATOM   795  C CD1 . PHE   B 1 6  ? 25.066  -15.774 -41.002 1.00 46.70  ? 5   PHE   B CD1 1 
ATOM   796  C CD2 . PHE   B 1 6  ? 26.726  -17.405 -40.455 1.00 49.68  ? 5   PHE   B CD2 1 
ATOM   797  C CE1 . PHE   B 1 6  ? 24.100  -16.766 -41.079 1.00 45.39  ? 5   PHE   B CE1 1 
ATOM   798  C CE2 . PHE   B 1 6  ? 25.754  -18.400 -40.534 1.00 50.65  ? 5   PHE   B CE2 1 
ATOM   799  C CZ  . PHE   B 1 6  ? 24.444  -18.078 -40.834 1.00 50.59  ? 5   PHE   B CZ  1 
ATOM   800  N N   . LYS   B 1 7  ? 28.375  -12.123 -42.103 1.00 56.03  ? 6   LYS   B N   1 
ATOM   801  C CA  . LYS   B 1 7  ? 29.118  -10.902 -41.836 1.00 51.35  ? 6   LYS   B CA  1 
ATOM   802  C C   . LYS   B 1 7  ? 28.310  -10.047 -40.859 1.00 53.17  ? 6   LYS   B C   1 
ATOM   803  O O   . LYS   B 1 7  ? 27.076  -10.162 -40.812 1.00 46.34  ? 6   LYS   B O   1 
ATOM   804  C CB  . LYS   B 1 7  ? 29.274  -10.164 -43.165 1.00 56.09  ? 6   LYS   B CB  1 
ATOM   805  C CG  . LYS   B 1 7  ? 27.942  -9.913  -43.872 1.00 56.99  ? 6   LYS   B CG  1 
ATOM   806  C CD  . LYS   B 1 7  ? 28.047  -9.208  -45.222 1.00 65.77  ? 6   LYS   B CD  1 
ATOM   807  C CE  . LYS   B 1 7  ? 26.716  -9.046  -45.885 1.00 56.37  ? 6   LYS   B CE  1 
ATOM   808  N NZ  . LYS   B 1 7  ? 26.168  -10.344 -46.280 1.00 66.62  ? 6   LYS   B NZ  1 
ATOM   809  N N   . PRO   B 1 8  ? 28.972  -9.139  -40.097 1.00 53.56  ? 7   PRO   B N   1 
ATOM   810  C CA  . PRO   B 1 8  ? 28.290  -8.255  -39.148 1.00 50.18  ? 7   PRO   B CA  1 
ATOM   811  C C   . PRO   B 1 8  ? 27.131  -7.555  -39.838 1.00 50.65  ? 7   PRO   B C   1 
ATOM   812  O O   . PRO   B 1 8  ? 27.285  -7.010  -40.933 1.00 56.99  ? 7   PRO   B O   1 
ATOM   813  C CB  . PRO   B 1 8  ? 29.436  -7.309  -38.858 1.00 47.83  ? 7   PRO   B CB  1 
ATOM   814  C CG  . PRO   B 1 8  ? 30.612  -8.254  -38.791 1.00 51.12  ? 7   PRO   B CG  1 
ATOM   815  C CD  . PRO   B 1 8  ? 30.419  -8.879  -40.147 1.00 51.72  ? 7   PRO   B CD  1 
ATOM   816  N N   . GLY   B 1 9  ? 25.945  -7.686  -39.234 1.00 46.91  ? 8   GLY   B N   1 
ATOM   817  C CA  . GLY   B 1 9  ? 24.779  -6.956  -39.691 1.00 41.62  ? 8   GLY   B CA  1 
ATOM   818  C C   . GLY   B 1 9  ? 23.793  -7.868  -40.406 1.00 42.27  ? 8   GLY   B C   1 
ATOM   819  O O   . GLY   B 1 9  ? 22.667  -7.442  -40.678 1.00 44.04  ? 8   GLY   B O   1 
ATOM   820  N N   . ASP   B 1 10 ? 24.219  -9.118  -40.695 1.00 42.28  ? 9   ASP   B N   1 
ATOM   821  C CA  . ASP   B 1 10 ? 23.285  -10.133 -41.181 1.00 39.51  ? 9   ASP   B CA  1 
ATOM   822  C C   . ASP   B 1 10 ? 22.225  -10.359 -40.097 1.00 33.52  ? 9   ASP   B C   1 
ATOM   823  O O   . ASP   B 1 10 ? 22.561  -10.384 -38.921 1.00 35.93  ? 9   ASP   B O   1 
ATOM   824  C CB  . ASP   B 1 10 ? 23.988  -11.442 -41.518 1.00 37.70  ? 9   ASP   B CB  1 
ATOM   825  C CG  . ASP   B 1 10 ? 24.927  -11.401 -42.723 1.00 50.55  ? 9   ASP   B CG  1 
ATOM   826  O OD1 . ASP   B 1 10 ? 24.594  -10.694 -43.695 1.00 47.33  ? 9   ASP   B OD1 1 
ATOM   827  O OD2 . ASP   B 1 10 ? 25.979  -12.087 -42.688 1.00 53.28  ? 9   ASP   B OD2 1 
ATOM   828  N N   . LEU   B 1 11 ? 20.962  -10.433 -40.495 1.00 38.64  ? 10  LEU   B N   1 
ATOM   829  C CA  . LEU   B 1 11 ? 19.880  -10.718 -39.560 1.00 41.01  ? 10  LEU   B CA  1 
ATOM   830  C C   . LEU   B 1 11 ? 19.580  -12.217 -39.619 1.00 43.40  ? 10  LEU   B C   1 
ATOM   831  O O   . LEU   B 1 11 ? 19.593  -12.783 -40.719 1.00 39.47  ? 10  LEU   B O   1 
ATOM   832  C CB  . LEU   B 1 11 ? 18.695  -9.879  -40.038 1.00 37.29  ? 10  LEU   B CB  1 
ATOM   833  C CG  . LEU   B 1 11 ? 18.978  -8.390  -40.263 1.00 40.26  ? 10  LEU   B CG  1 
ATOM   834  C CD1 . LEU   B 1 11 ? 17.677  -7.655  -40.590 1.00 34.84  ? 10  LEU   B CD1 1 
ATOM   835  C CD2 . LEU   B 1 11 ? 19.659  -7.833  -39.017 1.00 34.32  ? 10  LEU   B CD2 1 
ATOM   836  N N   . VAL   B 1 12 ? 19.351  -12.836 -38.440 1.00 41.49  ? 11  VAL   B N   1 
ATOM   837  C CA  . VAL   B 1 12 ? 19.132  -14.272 -38.262 1.00 38.41  ? 11  VAL   B CA  1 
ATOM   838  C C   . VAL   B 1 12 ? 17.998  -14.540 -37.263 1.00 40.69  ? 11  VAL   B C   1 
ATOM   839  O O   . VAL   B 1 12 ? 17.522  -13.645 -36.562 1.00 35.69  ? 11  VAL   B O   1 
ATOM   840  C CB  . VAL   B 1 12 ? 20.409  -15.038 -37.860 1.00 40.84  ? 11  VAL   B CB  1 
ATOM   841  C CG1 . VAL   B 1 12 ? 21.498  -14.882 -38.930 1.00 43.76  ? 11  VAL   B CG1 1 
ATOM   842  C CG2 . VAL   B 1 12 ? 20.967  -14.629 -36.493 1.00 36.84  ? 11  VAL   B CG2 1 
ATOM   843  N N   . PHE   B 1 13 ? 17.525  -15.785 -37.243 1.00 40.69  ? 12  PHE   B N   1 
ATOM   844  C CA  . PHE   B 1 13 ? 17.044  -16.367 -35.991 1.00 38.64  ? 12  PHE   B CA  1 
ATOM   845  C C   . PHE   B 1 13 ? 18.159  -17.237 -35.438 1.00 37.83  ? 12  PHE   B C   1 
ATOM   846  O O   . PHE   B 1 13 ? 18.737  -18.020 -36.199 1.00 37.16  ? 12  PHE   B O   1 
ATOM   847  C CB  . PHE   B 1 13 ? 15.814  -17.228 -36.249 1.00 35.16  ? 12  PHE   B CB  1 
ATOM   848  C CG  . PHE   B 1 13 ? 14.618  -16.377 -36.610 1.00 38.86  ? 12  PHE   B CG  1 
ATOM   849  C CD1 . PHE   B 1 13 ? 14.393  -15.994 -37.929 1.00 40.89  ? 12  PHE   B CD1 1 
ATOM   850  C CD2 . PHE   B 1 13 ? 13.736  -15.944 -35.623 1.00 36.05  ? 12  PHE   B CD2 1 
ATOM   851  C CE1 . PHE   B 1 13 ? 13.300  -15.213 -38.257 1.00 42.93  ? 12  PHE   B CE1 1 
ATOM   852  C CE2 . PHE   B 1 13 ? 12.644  -15.150 -35.961 1.00 42.51  ? 12  PHE   B CE2 1 
ATOM   853  C CZ  . PHE   B 1 13 ? 12.433  -14.784 -37.272 1.00 46.34  ? 12  PHE   B CZ  1 
ATOM   854  N N   . ALA   B 1 14 ? 18.482  -17.028 -34.144 1.00 35.88  ? 13  ALA   B N   1 
ATOM   855  C CA  . ALA   B 1 14 ? 19.509  -17.746 -33.417 1.00 34.17  ? 13  ALA   B CA  1 
ATOM   856  C C   . ALA   B 1 14 ? 18.843  -18.699 -32.425 1.00 38.17  ? 13  ALA   B C   1 
ATOM   857  O O   . ALA   B 1 14 ? 17.901  -18.307 -31.739 1.00 39.14  ? 13  ALA   B O   1 
ATOM   858  C CB  . ALA   B 1 14 ? 20.419  -16.764 -32.699 1.00 32.48  ? 13  ALA   B CB  1 
ATOM   859  N N   . LYS   B 1 15 ? 19.362  -19.927 -32.344 1.00 38.10  ? 14  LYS   B N   1 
ATOM   860  C CA  . LYS   B 1 15 ? 18.796  -21.001 -31.523 1.00 43.11  ? 14  LYS   B CA  1 
ATOM   861  C C   . LYS   B 1 15 ? 19.711  -21.274 -30.330 1.00 39.36  ? 14  LYS   B C   1 
ATOM   862  O O   . LYS   B 1 15 ? 20.900  -21.542 -30.481 1.00 40.51  ? 14  LYS   B O   1 
ATOM   863  C CB  . LYS   B 1 15 ? 18.484  -22.284 -32.326 1.00 39.29  ? 14  LYS   B CB  1 
ATOM   864  C CG  . LYS   B 1 15 ? 17.677  -23.407 -31.602 1.00 40.55  ? 14  LYS   B CG  1 
ATOM   865  C CD  . LYS   B 1 15 ? 16.285  -22.989 -31.117 1.00 43.11  ? 14  LYS   B CD  1 
ATOM   866  C CE  . LYS   B 1 15 ? 15.432  -24.098 -30.472 1.00 40.99  ? 14  LYS   B CE  1 
ATOM   867  N NZ  . LYS   B 1 15 ? 16.058  -24.523 -29.219 1.00 36.63  ? 14  LYS   B NZ  1 
ATOM   868  N N   . MET   B 1 16 ? 19.139  -21.153 -29.128 1.00 43.95  ? 15  MET   B N   1 
ATOM   869  C CA  . MET   B 1 16 ? 19.781  -21.581 -27.893 1.00 47.42  ? 15  MET   B CA  1 
ATOM   870  C C   . MET   B 1 16 ? 18.865  -22.576 -27.182 1.00 43.80  ? 15  MET   B C   1 
ATOM   871  O O   . MET   B 1 16 ? 17.634  -22.425 -27.189 1.00 41.00  ? 15  MET   B O   1 
ATOM   872  C CB  . MET   B 1 16 ? 19.964  -20.427 -26.894 1.00 46.67  ? 15  MET   B CB  1 
ATOM   873  C CG  . MET   B 1 16 ? 20.539  -19.143 -27.456 1.00 51.12  ? 15  MET   B CG  1 
ATOM   874  S SD  . MET   B 1 16 ? 22.227  -18.773 -26.951 1.00 59.12  ? 15  MET   B SD  1 
ATOM   875  C CE  . MET   B 1 16 ? 22.337  -18.969 -25.167 1.00 60.32  ? 15  MET   B CE  1 
ATOM   876  N N   . LYS   B 1 17 ? 19.487  -23.540 -26.496 1.00 44.55  ? 16  LYS   B N   1 
ATOM   877  C CA  . LYS   B 1 17 ? 18.725  -24.573 -25.800 1.00 44.12  ? 16  LYS   B CA  1 
ATOM   878  C C   . LYS   B 1 17 ? 17.827  -23.883 -24.772 1.00 41.77  ? 16  LYS   B C   1 
ATOM   879  O O   . LYS   B 1 17 ? 18.285  -23.013 -24.034 1.00 42.49  ? 16  LYS   B O   1 
ATOM   880  C CB  . LYS   B 1 17 ? 19.688  -25.586 -25.162 1.00 46.43  ? 16  LYS   B CB  1 
ATOM   881  C CG  . LYS   B 1 17 ? 19.018  -26.679 -24.301 1.00 55.88  ? 16  LYS   B CG  1 
ATOM   882  C CD  . LYS   B 1 17 ? 19.907  -27.736 -23.653 1.00 57.88  ? 16  LYS   B CD  1 
ATOM   883  N N   . GLY   B 1 18 ? 16.546  -24.244 -24.746 1.00 47.63  ? 17  GLY   B N   1 
ATOM   884  C CA  . GLY   B 1 18 ? 15.624  -23.638 -23.798 1.00 50.38  ? 17  GLY   B CA  1 
ATOM   885  C C   . GLY   B 1 18 ? 14.681  -22.623 -24.444 1.00 53.79  ? 17  GLY   B C   1 
ATOM   886  O O   . GLY   B 1 18 ? 13.646  -22.292 -23.868 1.00 47.87  ? 17  GLY   B O   1 
ATOM   887  N N   . TYR   B 1 19 ? 15.046  -22.112 -25.632 1.00 44.60  ? 18  TYR   B N   1 
ATOM   888  C CA  . TYR   B 1 19 ? 14.405  -20.901 -26.138 1.00 44.30  ? 18  TYR   B CA  1 
ATOM   889  C C   . TYR   B 1 19 ? 13.963  -21.137 -27.577 1.00 37.58  ? 18  TYR   B C   1 
ATOM   890  O O   . TYR   B 1 19 ? 14.602  -21.891 -28.301 1.00 42.86  ? 18  TYR   B O   1 
ATOM   891  C CB  . TYR   B 1 19 ? 15.433  -19.765 -26.041 1.00 42.43  ? 18  TYR   B CB  1 
ATOM   892  C CG  . TYR   B 1 19 ? 15.891  -19.500 -24.612 1.00 46.20  ? 18  TYR   B CG  1 
ATOM   893  C CD1 . TYR   B 1 19 ? 15.090  -18.777 -23.733 1.00 37.91  ? 18  TYR   B CD1 1 
ATOM   894  C CD2 . TYR   B 1 19 ? 17.093  -20.009 -24.118 1.00 48.59  ? 18  TYR   B CD2 1 
ATOM   895  C CE1 . TYR   B 1 19 ? 15.475  -18.562 -22.419 1.00 38.63  ? 18  TYR   B CE1 1 
ATOM   896  C CE2 . TYR   B 1 19 ? 17.494  -19.780 -22.805 1.00 53.70  ? 18  TYR   B CE2 1 
ATOM   897  C CZ  . TYR   B 1 19 ? 16.668  -19.075 -21.945 1.00 44.23  ? 18  TYR   B CZ  1 
ATOM   898  O OH  . TYR   B 1 19 ? 17.031  -18.827 -20.652 1.00 51.03  ? 18  TYR   B OH  1 
ATOM   899  N N   . PRO   B 1 20 ? 12.895  -20.520 -28.101 1.00 38.38  ? 19  PRO   B N   1 
ATOM   900  C CA  . PRO   B 1 20 ? 12.596  -20.729 -29.513 1.00 41.21  ? 19  PRO   B CA  1 
ATOM   901  C C   . PRO   B 1 20 ? 13.617  -19.932 -30.329 1.00 38.03  ? 19  PRO   B C   1 
ATOM   902  O O   . PRO   B 1 20 ? 14.321  -19.068 -29.805 1.00 35.32  ? 19  PRO   B O   1 
ATOM   903  C CB  . PRO   B 1 20 ? 11.195  -20.193 -29.662 1.00 35.25  ? 19  PRO   B CB  1 
ATOM   904  C CG  . PRO   B 1 20 ? 11.125  -19.097 -28.625 1.00 39.40  ? 19  PRO   B CG  1 
ATOM   905  C CD  . PRO   B 1 20 ? 11.963  -19.589 -27.453 1.00 38.84  ? 19  PRO   B CD  1 
ATOM   906  N N   . HIS   B 1 21 ? 13.720  -20.294 -31.599 1.00 35.29  ? 20  HIS   B N   1 
ATOM   907  C CA  . HIS   B 1 21 ? 14.497  -19.526 -32.570 1.00 39.64  ? 20  HIS   B CA  1 
ATOM   908  C C   . HIS   B 1 21 ? 14.215  -18.032 -32.399 1.00 35.82  ? 20  HIS   B C   1 
ATOM   909  O O   . HIS   B 1 21 ? 13.072  -17.596 -32.509 1.00 39.11  ? 20  HIS   B O   1 
ATOM   910  C CB  . HIS   B 1 21 ? 14.140  -20.024 -33.971 1.00 34.81  ? 20  HIS   B CB  1 
ATOM   911  C CG  . HIS   B 1 21 ? 14.410  -21.494 -34.166 1.00 41.30  ? 20  HIS   B CG  1 
ATOM   912  N ND1 . HIS   B 1 21 ? 13.586  -22.502 -33.683 1.00 43.56  ? 20  HIS   B ND1 1 
ATOM   913  C CD2 . HIS   B 1 21 ? 15.447  -22.114 -34.760 1.00 42.84  ? 20  HIS   B CD2 1 
ATOM   914  C CE1 . HIS   B 1 21 ? 14.097  -23.687 -34.015 1.00 42.38  ? 20  HIS   B CE1 1 
ATOM   915  N NE2 . HIS   B 1 21 ? 15.224  -23.474 -34.681 1.00 40.08  ? 20  HIS   B NE2 1 
ATOM   916  N N   . TRP   B 1 22 ? 15.266  -17.259 -32.127 1.00 35.00  ? 21  TRP   B N   1 
ATOM   917  C CA  . TRP   B 1 22 ? 15.091  -15.933 -31.565 1.00 33.59  ? 21  TRP   B CA  1 
ATOM   918  C C   . TRP   B 1 22 ? 15.614  -14.871 -32.539 1.00 39.52  ? 21  TRP   B C   1 
ATOM   919  O O   . TRP   B 1 22 ? 16.765  -14.954 -32.985 1.00 37.57  ? 21  TRP   B O   1 
ATOM   920  C CB  . TRP   B 1 22 ? 15.843  -15.876 -30.231 1.00 34.18  ? 21  TRP   B CB  1 
ATOM   921  C CG  . TRP   B 1 22 ? 15.346  -14.734 -29.377 1.00 39.15  ? 21  TRP   B CG  1 
ATOM   922  C CD1 . TRP   B 1 22 ? 15.635  -13.406 -29.533 1.00 38.40  ? 21  TRP   B CD1 1 
ATOM   923  C CD2 . TRP   B 1 22 ? 14.426  -14.820 -28.258 1.00 36.46  ? 21  TRP   B CD2 1 
ATOM   924  N NE1 . TRP   B 1 22 ? 14.970  -12.662 -28.583 1.00 40.11  ? 21  TRP   B NE1 1 
ATOM   925  C CE2 . TRP   B 1 22 ? 14.234  -13.500 -27.785 1.00 38.22  ? 21  TRP   B CE2 1 
ATOM   926  C CE3 . TRP   B 1 22 ? 13.760  -15.875 -27.613 1.00 42.79  ? 21  TRP   B CE3 1 
ATOM   927  C CZ2 . TRP   B 1 22 ? 13.397  -13.212 -26.703 1.00 40.78  ? 21  TRP   B CZ2 1 
ATOM   928  C CZ3 . TRP   B 1 22 ? 12.930  -15.597 -26.542 1.00 37.67  ? 21  TRP   B CZ3 1 
ATOM   929  C CH2 . TRP   B 1 22 ? 12.754  -14.279 -26.105 1.00 41.31  ? 21  TRP   B CH2 1 
ATOM   930  N N   . PRO   B 1 23 ? 14.827  -13.821 -32.875 1.00 35.94  ? 22  PRO   B N   1 
ATOM   931  C CA  . PRO   B 1 23 ? 15.282  -12.778 -33.820 1.00 36.45  ? 22  PRO   B CA  1 
ATOM   932  C C   . PRO   B 1 23 ? 16.576  -12.112 -33.370 1.00 37.94  ? 22  PRO   B C   1 
ATOM   933  O O   . PRO   B 1 23 ? 16.695  -11.736 -32.209 1.00 39.82  ? 22  PRO   B O   1 
ATOM   934  C CB  . PRO   B 1 23 ? 14.092  -11.797 -33.892 1.00 37.64  ? 22  PRO   B CB  1 
ATOM   935  C CG  . PRO   B 1 23 ? 13.342  -12.058 -32.586 1.00 35.46  ? 22  PRO   B CG  1 
ATOM   936  C CD  . PRO   B 1 23 ? 13.479  -13.562 -32.356 1.00 33.80  ? 22  PRO   B CD  1 
ATOM   937  N N   . ALA   B 1 24 ? 17.601  -12.065 -34.245 1.00 34.23  ? 23  ALA   B N   1 
ATOM   938  C CA  . ALA   B 1 24 ? 18.923  -11.651 -33.791 1.00 34.12  ? 23  ALA   B CA  1 
ATOM   939  C C   . ALA   B 1 24 ? 19.781  -11.103 -34.945 1.00 34.19  ? 23  ALA   B C   1 
ATOM   940  O O   . ALA   B 1 24 ? 19.348  -11.067 -36.111 1.00 36.15  ? 23  ALA   B O   1 
ATOM   941  C CB  . ALA   B 1 24 ? 19.586  -12.823 -33.105 1.00 35.21  ? 23  ALA   B CB  1 
ATOM   942  N N   . ARG   B 1 25 ? 20.972  -10.609 -34.604 1.00 34.17  ? 24  ARG   B N   1 
ATOM   943  C CA  . ARG   B 1 25 ? 21.867  -10.133 -35.655 1.00 39.02  ? 24  ARG   B CA  1 
ATOM   944  C C   . ARG   B 1 25 ? 23.290  -10.564 -35.327 1.00 37.79  ? 24  ARG   B C   1 
ATOM   945  O O   . ARG   B 1 25 ? 23.593  -10.853 -34.175 1.00 40.66  ? 24  ARG   B O   1 
ATOM   946  C CB  . ARG   B 1 25 ? 21.805  -8.618  -35.872 1.00 36.31  ? 24  ARG   B CB  1 
ATOM   947  C CG  . ARG   B 1 25 ? 22.522  -7.821  -34.791 1.00 37.76  ? 24  ARG   B CG  1 
ATOM   948  C CD  . ARG   B 1 25 ? 22.255  -6.318  -34.822 1.00 36.58  ? 24  ARG   B CD  1 
ATOM   949  N NE  . ARG   B 1 25 ? 22.880  -5.597  -33.709 1.00 41.15  ? 24  ARG   B NE  1 
ATOM   950  C CZ  . ARG   B 1 25 ? 22.551  -4.359  -33.278 1.00 45.49  ? 24  ARG   B CZ  1 
ATOM   951  N NH1 . ARG   B 1 25 ? 21.572  -3.691  -33.856 1.00 40.99  ? 24  ARG   B NH1 1 
ATOM   952  N NH2 . ARG   B 1 25 ? 23.179  -3.808  -32.250 1.00 37.35  ? 24  ARG   B NH2 1 
ATOM   953  N N   . ILE   B 1 26 ? 24.145  -10.620 -36.366 1.00 41.05  ? 25  ILE   B N   1 
ATOM   954  C CA  . ILE   B 1 26 ? 25.573  -10.797 -36.168 1.00 42.92  ? 25  ILE   B CA  1 
ATOM   955  C C   . ILE   B 1 26 ? 26.153  -9.434  -35.808 1.00 47.25  ? 25  ILE   B C   1 
ATOM   956  O O   . ILE   B 1 26 ? 25.908  -8.460  -36.529 1.00 47.90  ? 25  ILE   B O   1 
ATOM   957  C CB  . ILE   B 1 26 ? 26.261  -11.316 -37.443 1.00 46.06  ? 25  ILE   B CB  1 
ATOM   958  C CG1 . ILE   B 1 26 ? 25.580  -12.558 -38.011 1.00 42.15  ? 25  ILE   B CG1 1 
ATOM   959  C CG2 . ILE   B 1 26 ? 27.749  -11.545 -37.169 1.00 46.21  ? 25  ILE   B CG2 1 
ATOM   960  C CD1 . ILE   B 1 26 ? 25.699  -13.777 -37.114 1.00 45.73  ? 25  ILE   B CD1 1 
ATOM   961  N N   . ASP   B 1 27 ? 26.973  -9.404  -34.750 1.00 46.12  ? 26  ASP   B N   1 
ATOM   962  C CA  . ASP   B 1 27 ? 27.620  -8.178  -34.295 1.00 53.60  ? 26  ASP   B CA  1 
ATOM   963  C C   . ASP   B 1 27 ? 29.053  -8.083  -34.819 1.00 52.64  ? 26  ASP   B C   1 
ATOM   964  O O   . ASP   B 1 27 ? 29.573  -9.060  -35.346 1.00 54.12  ? 26  ASP   B O   1 
ATOM   965  C CB  . ASP   B 1 27 ? 27.576  -8.065  -32.784 1.00 49.00  ? 26  ASP   B CB  1 
ATOM   966  C CG  . ASP   B 1 27 ? 26.389  -7.289  -32.236 1.00 53.52  ? 26  ASP   B CG  1 
ATOM   967  O OD1 . ASP   B 1 27 ? 25.556  -6.825  -33.049 1.00 60.14  ? 26  ASP   B OD1 1 
ATOM   968  O OD2 . ASP   B 1 27 ? 26.335  -7.118  -31.007 1.00 51.84  ? 26  ASP   B OD2 1 
ATOM   969  N N   . ASP   B 1 28 ? 29.652  -6.887  -34.681 1.00 65.04  ? 27  ASP   B N   1 
ATOM   970  C CA  . ASP   B 1 28 ? 31.079  -6.622  -34.832 1.00 73.68  ? 27  ASP   B CA  1 
ATOM   971  C C   . ASP   B 1 28 ? 31.826  -7.031  -33.564 1.00 73.06  ? 27  ASP   B C   1 
ATOM   972  O O   . ASP   B 1 28 ? 31.214  -7.251  -32.523 1.00 80.59  ? 27  ASP   B O   1 
ATOM   973  C CB  . ASP   B 1 28 ? 31.336  -5.150  -35.120 1.00 81.56  ? 27  ASP   B CB  1 
ATOM   974  C CG  . ASP   B 1 28 ? 30.997  -4.679  -36.530 1.00 90.45  ? 27  ASP   B CG  1 
ATOM   975  O OD1 . ASP   B 1 28 ? 31.715  -5.094  -37.473 1.00 87.09  ? 27  ASP   B OD1 1 
ATOM   976  O OD2 . ASP   B 1 28 ? 30.018  -3.904  -36.675 1.00 82.84  ? 27  ASP   B OD2 1 
ATOM   977  N N   . ILE   B 1 29 ? 33.158  -7.129  -33.656 1.00 79.83  ? 28  ILE   B N   1 
ATOM   978  C CA  . ILE   B 1 29 ? 33.983  -7.553  -32.535 1.00 80.11  ? 28  ILE   B CA  1 
ATOM   979  C C   . ILE   B 1 29 ? 34.968  -6.423  -32.188 1.00 83.94  ? 28  ILE   B C   1 
ATOM   980  O O   . ILE   B 1 29 ? 34.486  -5.353  -31.746 1.00 86.10  ? 28  ILE   B O   1 
ATOM   981  C CB  . ILE   B 1 29 ? 34.713  -8.872  -32.857 1.00 80.74  ? 28  ILE   B CB  1 
ATOM   982  N N   . LYS   B 1 35 ? 37.356  -11.893 -27.996 1.00 81.63  ? 34  LYS   B N   1 
ATOM   983  C CA  . LYS   B 1 35 ? 37.125  -12.344 -29.396 1.00 73.74  ? 34  LYS   B CA  1 
ATOM   984  C C   . LYS   B 1 35 ? 36.376  -13.681 -29.381 1.00 76.48  ? 34  LYS   B C   1 
ATOM   985  O O   . LYS   B 1 35 ? 36.627  -14.511 -28.505 1.00 82.81  ? 34  LYS   B O   1 
ATOM   986  C CB  . LYS   B 1 35 ? 38.460  -12.377 -30.153 1.00 64.46  ? 34  LYS   B CB  1 
ATOM   987  N N   . PRO   B 1 36 ? 35.429  -13.938 -30.327 1.00 74.32  ? 35  PRO   B N   1 
ATOM   988  C CA  . PRO   B 1 36 ? 34.673  -15.201 -30.354 1.00 66.88  ? 35  PRO   B CA  1 
ATOM   989  C C   . PRO   B 1 36 ? 35.548  -16.453 -30.349 1.00 60.93  ? 35  PRO   B C   1 
ATOM   990  O O   . PRO   B 1 36 ? 36.658  -16.414 -30.864 1.00 69.67  ? 35  PRO   B O   1 
ATOM   991  C CB  . PRO   B 1 36 ? 33.775  -15.150 -31.609 1.00 67.75  ? 35  PRO   B CB  1 
ATOM   992  C CG  . PRO   B 1 36 ? 34.087  -13.827 -32.283 1.00 74.67  ? 35  PRO   B CG  1 
ATOM   993  C CD  . PRO   B 1 36 ? 35.028  -13.015 -31.404 1.00 72.53  ? 35  PRO   B CD  1 
ATOM   994  N N   . PRO   B 1 37 ? 35.090  -17.594 -29.780 1.00 57.40  ? 36  PRO   B N   1 
ATOM   995  C CA  . PRO   B 1 37 ? 35.819  -18.862 -29.885 1.00 62.20  ? 36  PRO   B CA  1 
ATOM   996  C C   . PRO   B 1 37 ? 35.817  -19.265 -31.356 1.00 71.78  ? 36  PRO   B C   1 
ATOM   997  O O   . PRO   B 1 37 ? 35.015  -18.743 -32.130 1.00 80.64  ? 36  PRO   B O   1 
ATOM   998  C CB  . PRO   B 1 37 ? 35.038  -19.858 -29.009 1.00 57.35  ? 36  PRO   B CB  1 
ATOM   999  C CG  . PRO   B 1 37 ? 34.122  -18.988 -28.175 1.00 57.11  ? 36  PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 1 37 ? 33.861  -17.725 -28.985 1.00 62.30  ? 36  PRO   B CD  1 
ATOM   1001 N N   . PRO   B 1 38 ? 36.728  -20.163 -31.803 1.00 79.74  ? 37  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 38 ? 36.771  -20.566 -33.213 1.00 78.26  ? 37  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 38 ? 35.404  -21.013 -33.742 1.00 68.79  ? 37  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 38 ? 34.635  -21.663 -33.031 1.00 70.67  ? 37  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 38 ? 37.811  -21.710 -33.215 1.00 75.46  ? 37  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 38 ? 38.696  -21.415 -32.018 1.00 78.14  ? 37  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 38 ? 37.758  -20.824 -30.982 1.00 81.12  ? 37  PRO   B CD  1 
ATOM   1008 N N   . ASN   B 1 39 ? 35.100  -20.619 -34.985 1.00 67.72  ? 38  ASN   B N   1 
ATOM   1009 C CA  . ASN   B 1 39 ? 33.909  -21.052 -35.712 1.00 70.56  ? 38  ASN   B CA  1 
ATOM   1010 C C   . ASN   B 1 39 ? 32.619  -20.401 -35.194 1.00 64.43  ? 38  ASN   B C   1 
ATOM   1011 O O   . ASN   B 1 39 ? 31.549  -20.793 -35.631 1.00 54.00  ? 38  ASN   B O   1 
ATOM   1012 C CB  . ASN   B 1 39 ? 33.723  -22.567 -35.672 1.00 74.95  ? 38  ASN   B CB  1 
ATOM   1013 C CG  . ASN   B 1 39 ? 34.986  -23.331 -35.996 1.00 86.83  ? 38  ASN   B CG  1 
ATOM   1014 O OD1 . ASN   B 1 39 ? 35.310  -24.301 -35.300 1.00 85.83  ? 38  ASN   B OD1 1 
ATOM   1015 N ND2 . ASN   B 1 39 ? 35.694  -22.930 -37.047 1.00 81.79  ? 38  ASN   B ND2 1 
ATOM   1016 N N   . LYS   B 1 40 ? 32.710  -19.407 -34.291 1.00 62.22  ? 39  LYS   B N   1 
ATOM   1017 C CA  . LYS   B 1 40 ? 31.548  -18.861 -33.605 1.00 53.81  ? 39  LYS   B CA  1 
ATOM   1018 C C   . LYS   B 1 40 ? 31.445  -17.369 -33.900 1.00 59.10  ? 39  LYS   B C   1 
ATOM   1019 O O   . LYS   B 1 40 ? 32.436  -16.742 -34.269 1.00 56.02  ? 39  LYS   B O   1 
ATOM   1020 C CB  . LYS   B 1 40 ? 31.556  -19.330 -32.144 1.00 52.96  ? 39  LYS   B CB  1 
ATOM   1021 C CG  . LYS   B 1 40 ? 31.456  -20.851 -32.056 1.00 50.35  ? 39  LYS   B CG  1 
ATOM   1022 C CD  . LYS   B 1 40 ? 31.515  -21.546 -30.705 1.00 54.81  ? 39  LYS   B CD  1 
ATOM   1023 C CE  . LYS   B 1 40 ? 30.185  -21.688 -30.072 1.00 66.06  ? 39  LYS   B CE  1 
ATOM   1024 N NZ  . LYS   B 1 40 ? 30.220  -22.671 -28.983 1.00 73.03  ? 39  LYS   B NZ  1 
ATOM   1025 N N   . TYR   B 1 41 ? 30.221  -16.832 -33.838 1.00 47.55  ? 40  TYR   B N   1 
ATOM   1026 C CA  . TYR   B 1 41 ? 29.995  -15.434 -34.161 1.00 42.76  ? 40  TYR   B CA  1 
ATOM   1027 C C   . TYR   B 1 41 ? 29.424  -14.720 -32.932 1.00 48.59  ? 40  TYR   B C   1 
ATOM   1028 O O   . TYR   B 1 41 ? 28.776  -15.369 -32.104 1.00 43.32  ? 40  TYR   B O   1 
ATOM   1029 C CB  . TYR   B 1 41 ? 28.970  -15.365 -35.297 1.00 43.54  ? 40  TYR   B CB  1 
ATOM   1030 C CG  . TYR   B 1 41 ? 29.419  -15.861 -36.665 1.00 46.65  ? 40  TYR   B CG  1 
ATOM   1031 C CD1 . TYR   B 1 41 ? 29.977  -14.988 -37.594 1.00 49.70  ? 40  TYR   B CD1 1 
ATOM   1032 C CD2 . TYR   B 1 41 ? 29.246  -17.188 -37.043 1.00 49.43  ? 40  TYR   B CD2 1 
ATOM   1033 C CE1 . TYR   B 1 41 ? 30.379  -15.430 -38.845 1.00 53.95  ? 40  TYR   B CE1 1 
ATOM   1034 C CE2 . TYR   B 1 41 ? 29.637  -17.642 -38.292 1.00 52.26  ? 40  TYR   B CE2 1 
ATOM   1035 C CZ  . TYR   B 1 41 ? 30.214  -16.762 -39.195 1.00 53.33  ? 40  TYR   B CZ  1 
ATOM   1036 O OH  . TYR   B 1 41 ? 30.573  -17.194 -40.442 1.00 54.29  ? 40  TYR   B OH  1 
ATOM   1037 N N   . PRO   B 1 42 ? 29.628  -13.380 -32.793 1.00 52.96  ? 41  PRO   B N   1 
ATOM   1038 C CA  . PRO   B 1 42 ? 28.954  -12.583 -31.765 1.00 47.34  ? 41  PRO   B CA  1 
ATOM   1039 C C   . PRO   B 1 42 ? 27.507  -12.395 -32.208 1.00 47.48  ? 41  PRO   B C   1 
ATOM   1040 O O   . PRO   B 1 42 ? 27.240  -11.874 -33.296 1.00 47.56  ? 41  PRO   B O   1 
ATOM   1041 C CB  . PRO   B 1 42 ? 29.700  -11.230 -31.704 1.00 48.23  ? 41  PRO   B CB  1 
ATOM   1042 C CG  . PRO   B 1 42 ? 30.737  -11.287 -32.825 1.00 46.21  ? 41  PRO   B CG  1 
ATOM   1043 C CD  . PRO   B 1 42 ? 30.514  -12.553 -33.633 1.00 49.64  ? 41  PRO   B CD  1 
ATOM   1044 N N   . ILE   B 1 43 ? 26.588  -12.851 -31.349 1.00 47.37  ? 42  ILE   B N   1 
ATOM   1045 C CA  . ILE   B 1 43 ? 25.167  -12.752 -31.622 1.00 45.44  ? 42  ILE   B CA  1 
ATOM   1046 C C   . ILE   B 1 43 ? 24.574  -11.712 -30.677 1.00 44.59  ? 42  ILE   B C   1 
ATOM   1047 O O   . ILE   B 1 43 ? 24.883  -11.736 -29.502 1.00 41.68  ? 42  ILE   B O   1 
ATOM   1048 C CB  . ILE   B 1 43 ? 24.517  -14.140 -31.478 1.00 39.69  ? 42  ILE   B CB  1 
ATOM   1049 C CG1 . ILE   B 1 43 ? 25.234  -15.166 -32.380 1.00 38.00  ? 42  ILE   B CG1 1 
ATOM   1050 C CG2 . ILE   B 1 43 ? 23.020  -14.063 -31.799 1.00 36.24  ? 42  ILE   B CG2 1 
ATOM   1051 C CD1 . ILE   B 1 43 ? 25.300  -14.742 -33.835 1.00 37.70  ? 42  ILE   B CD1 1 
ATOM   1052 N N   . PHE   B 1 44 ? 23.754  -10.795 -31.214 1.00 47.25  ? 43  PHE   B N   1 
ATOM   1053 C CA  . PHE   B 1 44 ? 22.937  -9.900  -30.411 1.00 43.61  ? 43  PHE   B CA  1 
ATOM   1054 C C   . PHE   B 1 44 ? 21.483  -10.333 -30.561 1.00 41.50  ? 43  PHE   B C   1 
ATOM   1055 O O   . PHE   B 1 44 ? 20.983  -10.417 -31.676 1.00 39.65  ? 43  PHE   B O   1 
ATOM   1056 C CB  . PHE   B 1 44 ? 23.187  -8.448  -30.852 1.00 44.16  ? 43  PHE   B CB  1 
ATOM   1057 C CG  . PHE   B 1 44 ? 22.268  -7.430  -30.185 1.00 45.64  ? 43  PHE   B CG  1 
ATOM   1058 C CD1 . PHE   B 1 44 ? 21.054  -7.072  -30.771 1.00 48.17  ? 43  PHE   B CD1 1 
ATOM   1059 C CD2 . PHE   B 1 44 ? 22.608  -6.840  -28.966 1.00 47.25  ? 43  PHE   B CD2 1 
ATOM   1060 C CE1 . PHE   B 1 44 ? 20.204  -6.165  -30.153 1.00 41.89  ? 43  PHE   B CE1 1 
ATOM   1061 C CE2 . PHE   B 1 44 ? 21.759  -5.920  -28.361 1.00 40.27  ? 43  PHE   B CE2 1 
ATOM   1062 C CZ  . PHE   B 1 44 ? 20.563  -5.595  -28.951 1.00 42.30  ? 43  PHE   B CZ  1 
ATOM   1063 N N   . PHE   B 1 45 ? 20.785  -10.574 -29.437 1.00 42.15  ? 44  PHE   B N   1 
ATOM   1064 C CA  . PHE   B 1 45 ? 19.374  -10.942 -29.458 1.00 36.29  ? 44  PHE   B CA  1 
ATOM   1065 C C   . PHE   B 1 45 ? 18.498  -9.698  -29.327 1.00 40.25  ? 44  PHE   B C   1 
ATOM   1066 O O   . PHE   B 1 45 ? 18.585  -8.986  -28.322 1.00 42.39  ? 44  PHE   B O   1 
ATOM   1067 C CB  . PHE   B 1 45 ? 19.061  -11.935 -28.323 1.00 33.17  ? 44  PHE   B CB  1 
ATOM   1068 C CG  . PHE   B 1 45 ? 19.753  -13.283 -28.492 1.00 36.00  ? 44  PHE   B CG  1 
ATOM   1069 C CD1 . PHE   B 1 45 ? 21.026  -13.504 -27.985 1.00 35.07  ? 44  PHE   B CD1 1 
ATOM   1070 C CD2 . PHE   B 1 45 ? 19.121  -14.332 -29.164 1.00 34.34  ? 44  PHE   B CD2 1 
ATOM   1071 C CE1 . PHE   B 1 45 ? 21.663  -14.724 -28.156 1.00 38.12  ? 44  PHE   B CE1 1 
ATOM   1072 C CE2 . PHE   B 1 45 ? 19.733  -15.571 -29.284 1.00 36.98  ? 44  PHE   B CE2 1 
ATOM   1073 C CZ  . PHE   B 1 45 ? 21.013  -15.759 -28.792 1.00 35.06  ? 44  PHE   B CZ  1 
ATOM   1074 N N   . PHE   B 1 46 ? 17.657  -9.442  -30.347 1.00 34.40  ? 45  PHE   B N   1 
ATOM   1075 C CA  . PHE   B 1 46 ? 16.698  -8.354  -30.302 1.00 35.10  ? 45  PHE   B CA  1 
ATOM   1076 C C   . PHE   B 1 46 ? 15.727  -8.593  -29.130 1.00 42.71  ? 45  PHE   B C   1 
ATOM   1077 O O   . PHE   B 1 46 ? 15.566  -9.727  -28.692 1.00 38.87  ? 45  PHE   B O   1 
ATOM   1078 C CB  . PHE   B 1 46 ? 15.947  -8.261  -31.629 1.00 37.60  ? 45  PHE   B CB  1 
ATOM   1079 C CG  . PHE   B 1 46 ? 16.847  -7.782  -32.769 1.00 39.89  ? 45  PHE   B CG  1 
ATOM   1080 C CD1 . PHE   B 1 46 ? 17.375  -6.486  -32.771 1.00 40.81  ? 45  PHE   B CD1 1 
ATOM   1081 C CD2 . PHE   B 1 46 ? 17.163  -8.627  -33.829 1.00 37.84  ? 45  PHE   B CD2 1 
ATOM   1082 C CE1 . PHE   B 1 46 ? 18.187  -6.040  -33.818 1.00 40.72  ? 45  PHE   B CE1 1 
ATOM   1083 C CE2 . PHE   B 1 46 ? 17.981  -8.178  -34.877 1.00 39.55  ? 45  PHE   B CE2 1 
ATOM   1084 C CZ  . PHE   B 1 46 ? 18.477  -6.891  -34.871 1.00 41.39  ? 45  PHE   B CZ  1 
ATOM   1085 N N   . GLY   B 1 47 ? 15.089  -7.529  -28.615 1.00 43.04  ? 46  GLY   B N   1 
ATOM   1086 C CA  . GLY   B 1 47 ? 14.119  -7.665  -27.528 1.00 39.31  ? 46  GLY   B CA  1 
ATOM   1087 C C   . GLY   B 1 47 ? 14.820  -7.794  -26.175 1.00 37.34  ? 46  GLY   B C   1 
ATOM   1088 O O   . GLY   B 1 47 ? 14.738  -6.895  -25.358 1.00 44.45  ? 46  GLY   B O   1 
ATOM   1089 N N   . THR   B 1 48 ? 15.560  -8.880  -25.943 1.00 40.01  ? 47  THR   B N   1 
ATOM   1090 C CA  . THR   B 1 48 ? 16.261  -9.032  -24.677 1.00 42.87  ? 47  THR   B CA  1 
ATOM   1091 C C   . THR   B 1 48 ? 17.569  -8.249  -24.660 1.00 46.68  ? 47  THR   B C   1 
ATOM   1092 O O   . THR   B 1 48 ? 18.123  -7.992  -23.589 1.00 44.39  ? 47  THR   B O   1 
ATOM   1093 C CB  . THR   B 1 48 ? 16.519  -10.503 -24.340 1.00 41.16  ? 47  THR   B CB  1 
ATOM   1094 O OG1 . THR   B 1 48 ? 17.421  -10.991 -25.340 1.00 41.41  ? 47  THR   B OG1 1 
ATOM   1095 C CG2 . THR   B 1 48 ? 15.234  -11.307 -24.263 1.00 38.11  ? 47  THR   B CG2 1 
ATOM   1096 N N   . HIS   B 1 49 ? 18.119  -7.951  -25.843 1.00 43.01  ? 48  HIS   B N   1 
ATOM   1097 C CA  . HIS   B 1 49 ? 19.425  -7.299  -25.940 1.00 43.20  ? 48  HIS   B CA  1 
ATOM   1098 C C   . HIS   B 1 49 ? 20.516  -8.104  -25.250 1.00 38.99  ? 48  HIS   B C   1 
ATOM   1099 O O   . HIS   B 1 49 ? 21.527  -7.534  -24.869 1.00 49.90  ? 48  HIS   B O   1 
ATOM   1100 C CB  . HIS   B 1 49 ? 19.416  -5.848  -25.427 1.00 41.70  ? 48  HIS   B CB  1 
ATOM   1101 C CG  . HIS   B 1 49 ? 18.253  -5.083  -25.970 1.00 46.21  ? 48  HIS   B CG  1 
ATOM   1102 N ND1 . HIS   B 1 49 ? 17.543  -4.157  -25.241 1.00 51.17  ? 48  HIS   B ND1 1 
ATOM   1103 C CD2 . HIS   B 1 49 ? 17.645  -5.153  -27.169 1.00 47.99  ? 48  HIS   B CD2 1 
ATOM   1104 C CE1 . HIS   B 1 49 ? 16.549  -3.680  -25.988 1.00 53.82  ? 48  HIS   B CE1 1 
ATOM   1105 N NE2 . HIS   B 1 49 ? 16.589  -4.283  -27.169 1.00 50.13  ? 48  HIS   B NE2 1 
ATOM   1106 N N   . GLU   B 1 50 ? 20.340  -9.422  -25.129 1.00 37.66  ? 49  GLU   B N   1 
ATOM   1107 C CA  . GLU   B 1 50 ? 21.377  -10.309 -24.610 1.00 44.04  ? 49  GLU   B CA  1 
ATOM   1108 C C   . GLU   B 1 50 ? 22.386  -10.597 -25.734 1.00 42.96  ? 49  GLU   B C   1 
ATOM   1109 O O   . GLU   B 1 50 ? 22.098  -10.327 -26.910 1.00 39.05  ? 49  GLU   B O   1 
ATOM   1110 C CB  . GLU   B 1 50 ? 20.636  -11.588 -24.219 1.00 54.67  ? 49  GLU   B CB  1 
ATOM   1111 C CG  . GLU   B 1 50 ? 21.449  -12.567 -23.379 1.00 77.77  ? 49  GLU   B CG  1 
ATOM   1112 C CD  . GLU   B 1 50 ? 21.239  -12.374 -21.888 1.00 85.60  ? 49  GLU   B CD  1 
ATOM   1113 O OE1 . GLU   B 1 50 ? 20.511  -13.204 -21.313 1.00 90.43  ? 49  GLU   B OE1 1 
ATOM   1114 O OE2 . GLU   B 1 50 ? 21.781  -11.414 -21.301 1.00 92.67  ? 49  GLU   B OE2 1 
ATOM   1115 N N   . THR   B 1 51 ? 23.546  -11.171 -25.386 1.00 41.73  ? 50  THR   B N   1 
ATOM   1116 C CA  . THR   B 1 51 ? 24.557  -11.563 -26.369 1.00 47.68  ? 50  THR   B CA  1 
ATOM   1117 C C   . THR   B 1 51 ? 25.053  -12.966 -26.038 1.00 49.29  ? 50  THR   B C   1 
ATOM   1118 O O   . THR   B 1 51 ? 25.059  -13.359 -24.874 1.00 52.56  ? 50  THR   B O   1 
ATOM   1119 C CB  . THR   B 1 51 ? 25.734  -10.578 -26.478 1.00 47.85  ? 50  THR   B CB  1 
ATOM   1120 O OG1 . THR   B 1 51 ? 26.407  -10.560 -25.227 1.00 50.69  ? 50  THR   B OG1 1 
ATOM   1121 C CG2 . THR   B 1 51 ? 25.342  -9.155  -26.838 1.00 48.41  ? 50  THR   B CG2 1 
ATOM   1122 N N   . ALA   B 1 52 ? 25.447  -13.717 -27.077 1.00 49.97  ? 51  ALA   B N   1 
ATOM   1123 C CA  . ALA   B 1 52 ? 26.135  -14.992 -26.930 1.00 45.64  ? 51  ALA   B CA  1 
ATOM   1124 C C   . ALA   B 1 52 ? 27.023  -15.237 -28.152 1.00 45.62  ? 51  ALA   B C   1 
ATOM   1125 O O   . ALA   B 1 52 ? 26.958  -14.489 -29.130 1.00 42.93  ? 51  ALA   B O   1 
ATOM   1126 C CB  . ALA   B 1 52 ? 25.159  -16.140 -26.726 1.00 45.78  ? 51  ALA   B CB  1 
ATOM   1127 N N   . PHE   B 1 53 ? 27.867  -16.274 -28.048 1.00 43.78  ? 52  PHE   B N   1 
ATOM   1128 C CA  . PHE   B 1 53 ? 28.622  -16.813 -29.167 1.00 47.43  ? 52  PHE   B CA  1 
ATOM   1129 C C   . PHE   B 1 53 ? 27.960  -18.106 -29.655 1.00 51.55  ? 52  PHE   B C   1 
ATOM   1130 O O   . PHE   B 1 53 ? 27.738  -19.049 -28.887 1.00 55.46  ? 52  PHE   B O   1 
ATOM   1131 C CB  . PHE   B 1 53 ? 30.027  -17.046 -28.601 1.00 47.02  ? 52  PHE   B CB  1 
ATOM   1132 C CG  . PHE   B 1 53 ? 30.840  -15.793 -28.296 1.00 46.93  ? 52  PHE   B CG  1 
ATOM   1133 C CD1 . PHE   B 1 53 ? 30.983  -14.777 -29.241 1.00 53.51  ? 52  PHE   B CD1 1 
ATOM   1134 C CD2 . PHE   B 1 53 ? 31.437  -15.626 -27.054 1.00 47.96  ? 52  PHE   B CD2 1 
ATOM   1135 C CE1 . PHE   B 1 53 ? 31.738  -13.643 -28.964 1.00 52.97  ? 52  PHE   B CE1 1 
ATOM   1136 C CE2 . PHE   B 1 53 ? 32.173  -14.477 -26.768 1.00 54.72  ? 52  PHE   B CE2 1 
ATOM   1137 C CZ  . PHE   B 1 53 ? 32.329  -13.491 -27.722 1.00 51.03  ? 52  PHE   B CZ  1 
ATOM   1138 N N   . LEU   B 1 54 ? 27.617  -18.146 -30.945 1.00 48.30  ? 53  LEU   B N   1 
ATOM   1139 C CA  . LEU   B 1 54 ? 27.000  -19.331 -31.516 1.00 38.93  ? 53  LEU   B CA  1 
ATOM   1140 C C   . LEU   B 1 54 ? 27.736  -19.703 -32.804 1.00 42.94  ? 53  LEU   B C   1 
ATOM   1141 O O   . LEU   B 1 54 ? 28.269  -18.819 -33.479 1.00 43.23  ? 53  LEU   B O   1 
ATOM   1142 C CB  . LEU   B 1 54 ? 25.523  -19.074 -31.816 1.00 42.99  ? 53  LEU   B CB  1 
ATOM   1143 C CG  . LEU   B 1 54 ? 24.585  -18.828 -30.628 1.00 43.98  ? 53  LEU   B CG  1 
ATOM   1144 C CD1 . LEU   B 1 54 ? 23.211  -18.450 -31.170 1.00 38.76  ? 53  LEU   B CD1 1 
ATOM   1145 C CD2 . LEU   B 1 54 ? 24.514  -20.116 -29.820 1.00 42.82  ? 53  LEU   B CD2 1 
ATOM   1146 N N   . GLY   B 1 55 ? 27.688  -21.002 -33.143 1.00 44.05  ? 54  GLY   B N   1 
ATOM   1147 C CA  . GLY   B 1 55 ? 28.176  -21.560 -34.395 1.00 38.81  ? 54  GLY   B CA  1 
ATOM   1148 C C   . GLY   B 1 55 ? 27.086  -21.531 -35.465 1.00 38.85  ? 54  GLY   B C   1 
ATOM   1149 O O   . GLY   B 1 55 ? 25.908  -21.356 -35.153 1.00 37.95  ? 54  GLY   B O   1 
ATOM   1150 N N   . PRO   B 1 56 ? 27.440  -21.707 -36.757 1.00 41.37  ? 55  PRO   B N   1 
ATOM   1151 C CA  . PRO   B 1 56 ? 26.449  -21.726 -37.846 1.00 39.32  ? 55  PRO   B CA  1 
ATOM   1152 C C   . PRO   B 1 56 ? 25.249  -22.663 -37.724 1.00 38.93  ? 55  PRO   B C   1 
ATOM   1153 O O   . PRO   B 1 56 ? 24.217  -22.374 -38.312 1.00 38.04  ? 55  PRO   B O   1 
ATOM   1154 C CB  . PRO   B 1 56 ? 27.239  -22.005 -39.148 1.00 41.92  ? 55  PRO   B CB  1 
ATOM   1155 C CG  . PRO   B 1 56 ? 28.689  -22.097 -38.726 1.00 43.06  ? 55  PRO   B CG  1 
ATOM   1156 C CD  . PRO   B 1 56 ? 28.822  -21.903 -37.231 1.00 41.61  ? 55  PRO   B CD  1 
ATOM   1157 N N   . LYS   B 1 57 ? 25.385  -23.792 -37.005 1.00 39.37  ? 56  LYS   B N   1 
ATOM   1158 C CA  . LYS   B 1 57 ? 24.319  -24.792 -36.922 1.00 42.23  ? 56  LYS   B CA  1 
ATOM   1159 C C   . LYS   B 1 57 ? 23.079  -24.204 -36.243 1.00 41.28  ? 56  LYS   B C   1 
ATOM   1160 O O   . LYS   B 1 57 ? 21.962  -24.697 -36.422 1.00 38.43  ? 56  LYS   B O   1 
ATOM   1161 C CB  . LYS   B 1 57 ? 24.735  -26.103 -36.235 1.00 44.74  ? 56  LYS   B CB  1 
ATOM   1162 C CG  . LYS   B 1 57 ? 24.903  -26.051 -34.729 1.00 55.30  ? 56  LYS   B CG  1 
ATOM   1163 C CD  . LYS   B 1 57 ? 24.923  -27.428 -34.071 1.00 59.23  ? 56  LYS   B CD  1 
ATOM   1164 C CE  . LYS   B 1 57 ? 25.299  -27.403 -32.612 1.00 62.61  ? 56  LYS   B CE  1 
ATOM   1165 N NZ  . LYS   B 1 57 ? 24.293  -26.708 -31.807 1.00 57.83  ? 56  LYS   B NZ  1 
ATOM   1166 N N   . ASP   B 1 58 ? 23.292  -23.141 -35.459 1.00 37.70  ? 57  ASP   B N   1 
ATOM   1167 C CA  . ASP   B 1 58 ? 22.212  -22.521 -34.720 1.00 36.86  ? 57  ASP   B CA  1 
ATOM   1168 C C   . ASP   B 1 58 ? 21.863  -21.140 -35.274 1.00 44.15  ? 57  ASP   B C   1 
ATOM   1169 O O   . ASP   B 1 58 ? 21.187  -20.369 -34.573 1.00 38.58  ? 57  ASP   B O   1 
ATOM   1170 C CB  . ASP   B 1 58 ? 22.648  -22.329 -33.286 1.00 37.79  ? 57  ASP   B CB  1 
ATOM   1171 C CG  . ASP   B 1 58 ? 22.916  -23.609 -32.512 1.00 46.22  ? 57  ASP   B CG  1 
ATOM   1172 O OD1 . ASP   B 1 58 ? 22.039  -24.501 -32.545 1.00 41.60  ? 57  ASP   B OD1 1 
ATOM   1173 O OD2 . ASP   B 1 58 ? 23.976  -23.664 -31.848 1.00 42.46  ? 57  ASP   B OD2 1 
ATOM   1174 N N   . LEU   B 1 59 ? 22.333  -20.816 -36.500 1.00 40.69  ? 58  LEU   B N   1 
ATOM   1175 C CA  . LEU   B 1 59 ? 22.058  -19.520 -37.126 1.00 40.29  ? 58  LEU   B CA  1 
ATOM   1176 C C   . LEU   B 1 59 ? 21.242  -19.706 -38.400 1.00 37.29  ? 58  LEU   B C   1 
ATOM   1177 O O   . LEU   B 1 59 ? 21.646  -20.445 -39.298 1.00 38.35  ? 58  LEU   B O   1 
ATOM   1178 C CB  . LEU   B 1 59 ? 23.361  -18.786 -37.414 1.00 39.18  ? 58  LEU   B CB  1 
ATOM   1179 C CG  . LEU   B 1 59 ? 24.196  -18.455 -36.175 1.00 43.93  ? 58  LEU   B CG  1 
ATOM   1180 C CD1 . LEU   B 1 59 ? 25.486  -17.756 -36.548 1.00 40.44  ? 58  LEU   B CD1 1 
ATOM   1181 C CD2 . LEU   B 1 59 ? 23.380  -17.624 -35.161 1.00 40.89  ? 58  LEU   B CD2 1 
ATOM   1182 N N   . PHE   B 1 60 ? 20.061  -19.085 -38.430 1.00 34.73  ? 59  PHE   B N   1 
ATOM   1183 C CA  . PHE   B 1 60 ? 19.111  -19.249 -39.518 1.00 38.76  ? 59  PHE   B CA  1 
ATOM   1184 C C   . PHE   B 1 60 ? 18.907  -17.910 -40.225 1.00 41.60  ? 59  PHE   B C   1 
ATOM   1185 O O   . PHE   B 1 60 ? 18.351  -16.995 -39.640 1.00 39.28  ? 59  PHE   B O   1 
ATOM   1186 C CB  . PHE   B 1 60 ? 17.779  -19.772 -38.959 1.00 36.45  ? 59  PHE   B CB  1 
ATOM   1187 C CG  . PHE   B 1 60 ? 17.875  -21.193 -38.416 1.00 39.40  ? 59  PHE   B CG  1 
ATOM   1188 C CD1 . PHE   B 1 60 ? 18.429  -21.443 -37.167 1.00 33.41  ? 59  PHE   B CD1 1 
ATOM   1189 C CD2 . PHE   B 1 60 ? 17.395  -22.273 -39.156 1.00 36.28  ? 59  PHE   B CD2 1 
ATOM   1190 C CE1 . PHE   B 1 60 ? 18.523  -22.743 -36.680 1.00 35.28  ? 59  PHE   B CE1 1 
ATOM   1191 C CE2 . PHE   B 1 60 ? 17.480  -23.566 -38.668 1.00 38.92  ? 59  PHE   B CE2 1 
ATOM   1192 C CZ  . PHE   B 1 60 ? 18.063  -23.808 -37.443 1.00 37.79  ? 59  PHE   B CZ  1 
ATOM   1193 N N   . PRO   B 1 61 ? 19.361  -17.733 -41.490 1.00 46.82  ? 60  PRO   B N   1 
ATOM   1194 C CA  . PRO   B 1 61 ? 19.156  -16.466 -42.202 1.00 46.62  ? 60  PRO   B CA  1 
ATOM   1195 C C   . PRO   B 1 61 ? 17.718  -15.944 -42.152 1.00 45.89  ? 60  PRO   B C   1 
ATOM   1196 O O   . PRO   B 1 61 ? 16.779  -16.681 -42.424 1.00 43.29  ? 60  PRO   B O   1 
ATOM   1197 C CB  . PRO   B 1 61 ? 19.659  -16.735 -43.632 1.00 46.34  ? 60  PRO   B CB  1 
ATOM   1198 C CG  . PRO   B 1 61 ? 20.679  -17.840 -43.428 1.00 51.99  ? 60  PRO   B CG  1 
ATOM   1199 C CD  . PRO   B 1 61 ? 20.144  -18.708 -42.276 1.00 47.86  ? 60  PRO   B CD  1 
ATOM   1200 N N   . TYR   B 1 62 ? 17.564  -14.659 -41.773 1.00 43.11  ? 61  TYR   B N   1 
ATOM   1201 C CA  . TYR   B 1 62 ? 16.276  -14.094 -41.412 1.00 38.34  ? 61  TYR   B CA  1 
ATOM   1202 C C   . TYR   B 1 62 ? 15.269  -14.185 -42.555 1.00 43.35  ? 61  TYR   B C   1 
ATOM   1203 O O   . TYR   B 1 62 ? 14.101  -14.507 -42.323 1.00 43.94  ? 61  TYR   B O   1 
ATOM   1204 C CB  . TYR   B 1 62 ? 16.412  -12.687 -40.816 1.00 43.98  ? 61  TYR   B CB  1 
ATOM   1205 C CG  . TYR   B 1 62 ? 15.111  -11.921 -40.603 1.00 48.59  ? 61  TYR   B CG  1 
ATOM   1206 C CD1 . TYR   B 1 62 ? 14.328  -12.140 -39.477 1.00 49.78  ? 61  TYR   B CD1 1 
ATOM   1207 C CD2 . TYR   B 1 62 ? 14.700  -10.926 -41.496 1.00 56.79  ? 61  TYR   B CD2 1 
ATOM   1208 C CE1 . TYR   B 1 62 ? 13.162  -11.422 -39.259 1.00 52.15  ? 61  TYR   B CE1 1 
ATOM   1209 C CE2 . TYR   B 1 62 ? 13.533  -10.201 -41.291 1.00 55.65  ? 61  TYR   B CE2 1 
ATOM   1210 C CZ  . TYR   B 1 62 ? 12.771  -10.445 -40.161 1.00 53.89  ? 61  TYR   B CZ  1 
ATOM   1211 O OH  . TYR   B 1 62 ? 11.611  -9.767  -39.951 1.00 47.67  ? 61  TYR   B OH  1 
ATOM   1212 N N   . ASP   B 1 63 ? 15.699  -13.848 -43.776 1.00 52.20  ? 62  ASP   B N   1 
ATOM   1213 C CA  . ASP   B 1 63 ? 14.763  -13.751 -44.891 1.00 56.44  ? 62  ASP   B CA  1 
ATOM   1214 C C   . ASP   B 1 63 ? 14.129  -15.105 -45.193 1.00 48.41  ? 62  ASP   B C   1 
ATOM   1215 O O   . ASP   B 1 63 ? 12.904  -15.247 -45.176 1.00 58.28  ? 62  ASP   B O   1 
ATOM   1216 C CB  . ASP   B 1 63 ? 15.402  -13.130 -46.119 1.00 67.73  ? 62  ASP   B CB  1 
ATOM   1217 C CG  . ASP   B 1 63 ? 14.839  -11.767 -46.487 1.00 83.51  ? 62  ASP   B CG  1 
ATOM   1218 O OD1 . ASP   B 1 63 ? 14.884  -10.850 -45.629 1.00 76.51  ? 62  ASP   B OD1 1 
ATOM   1219 O OD2 . ASP   B 1 63 ? 14.327  -11.655 -47.620 1.00 94.70  ? 62  ASP   B OD2 1 
ATOM   1220 N N   . LYS   B 1 64 ? 14.986  -16.096 -45.436 1.00 51.86  ? 63  LYS   B N   1 
ATOM   1221 C CA  . LYS   B 1 64 ? 14.561  -17.471 -45.663 1.00 53.23  ? 63  LYS   B CA  1 
ATOM   1222 C C   . LYS   B 1 64 ? 13.608  -17.954 -44.566 1.00 51.14  ? 63  LYS   B C   1 
ATOM   1223 O O   . LYS   B 1 64 ? 12.650  -18.666 -44.861 1.00 55.04  ? 63  LYS   B O   1 
ATOM   1224 C CB  . LYS   B 1 64 ? 15.805  -18.370 -45.723 1.00 58.28  ? 63  LYS   B CB  1 
ATOM   1225 C CG  . LYS   B 1 64 ? 15.557  -19.845 -46.039 1.00 59.49  ? 63  LYS   B CG  1 
ATOM   1226 C CD  . LYS   B 1 64 ? 16.817  -20.701 -45.986 1.00 61.79  ? 63  LYS   B CD  1 
ATOM   1227 C CE  . LYS   B 1 64 ? 16.681  -21.961 -46.812 1.00 63.03  ? 63  LYS   B CE  1 
ATOM   1228 N NZ  . LYS   B 1 64 ? 15.582  -22.834 -46.400 1.00 58.09  ? 63  LYS   B NZ  1 
ATOM   1229 N N   . SER   B 1 65 ? 13.854  -17.581 -43.302 1.00 50.01  ? 64  SER   B N   1 
ATOM   1230 C CA  . SER   B 1 65 ? 13.196  -18.283 -42.199 1.00 52.33  ? 64  SER   B CA  1 
ATOM   1231 C C   . SER   B 1 65 ? 12.137  -17.475 -41.439 1.00 53.39  ? 64  SER   B C   1 
ATOM   1232 O O   . SER   B 1 65 ? 11.570  -17.969 -40.461 1.00 52.94  ? 64  SER   B O   1 
ATOM   1233 C CB  . SER   B 1 65 ? 14.202  -18.904 -41.271 1.00 55.57  ? 64  SER   B CB  1 
ATOM   1234 O OG  . SER   B 1 65 ? 15.070  -17.914 -40.750 1.00 64.78  ? 64  SER   B OG  1 
ATOM   1235 N N   . LYS   B 1 66 ? 11.787  -16.276 -41.915 1.00 52.17  ? 65  LYS   B N   1 
ATOM   1236 C CA  . LYS   B 1 66 ? 10.956  -15.410 -41.088 1.00 52.60  ? 65  LYS   B CA  1 
ATOM   1237 C C   . LYS   B 1 66 ? 9.522   -15.927 -40.990 1.00 57.27  ? 65  LYS   B C   1 
ATOM   1238 O O   . LYS   B 1 66 ? 8.858   -15.715 -39.975 1.00 60.30  ? 65  LYS   B O   1 
ATOM   1239 C CB  . LYS   B 1 66 ? 11.000  -13.929 -41.486 1.00 55.62  ? 65  LYS   B CB  1 
ATOM   1240 C CG  . LYS   B 1 66 ? 10.181  -13.563 -42.717 1.00 55.97  ? 65  LYS   B CG  1 
ATOM   1241 C CD  . LYS   B 1 66 ? 10.545  -12.194 -43.276 1.00 71.55  ? 65  LYS   B CD  1 
ATOM   1242 C CE  . LYS   B 1 66 ? 10.169  -12.055 -44.718 1.00 76.20  ? 65  LYS   B CE  1 
ATOM   1243 N NZ  . LYS   B 1 66 ? 10.955  -10.977 -45.321 1.00 86.29  ? 65  LYS   B NZ  1 
ATOM   1244 N N   . ASP   B 1 67 ? 9.024   -16.594 -42.036 1.00 54.07  ? 66  ASP   B N   1 
ATOM   1245 C CA  . ASP   B 1 67 ? 7.619   -16.966 -41.991 1.00 57.80  ? 66  ASP   B CA  1 
ATOM   1246 C C   . ASP   B 1 67 ? 7.424   -18.145 -41.037 1.00 55.99  ? 66  ASP   B C   1 
ATOM   1247 O O   . ASP   B 1 67 ? 6.367   -18.274 -40.418 1.00 61.15  ? 66  ASP   B O   1 
ATOM   1248 C CB  . ASP   B 1 67 ? 6.947   -16.957 -43.358 1.00 71.20  ? 66  ASP   B CB  1 
ATOM   1249 C CG  . ASP   B 1 67 ? 7.360   -18.039 -44.343 1.00 84.29  ? 66  ASP   B CG  1 
ATOM   1250 O OD1 . ASP   B 1 67 ? 7.821   -17.681 -45.450 1.00 99.47  ? 66  ASP   B OD1 1 
ATOM   1251 O OD2 . ASP   B 1 67 ? 7.191   -19.231 -44.009 1.00 98.48  ? 66  ASP   B OD2 1 
ATOM   1252 N N   . LYS   B 1 68 ? 8.480   -18.952 -40.883 1.00 50.47  ? 67  LYS   B N   1 
ATOM   1253 C CA  . LYS   B 1 68 ? 8.490   -20.131 -40.028 1.00 51.82  ? 67  LYS   B CA  1 
ATOM   1254 C C   . LYS   B 1 68 ? 8.729   -19.758 -38.558 1.00 54.93  ? 67  LYS   B C   1 
ATOM   1255 O O   . LYS   B 1 68 ? 8.018   -20.248 -37.677 1.00 56.21  ? 67  LYS   B O   1 
ATOM   1256 C CB  . LYS   B 1 68 ? 9.495   -21.132 -40.613 1.00 55.43  ? 67  LYS   B CB  1 
ATOM   1257 C CG  . LYS   B 1 68 ? 9.787   -22.380 -39.809 1.00 59.84  ? 67  LYS   B CG  1 
ATOM   1258 C CD  . LYS   B 1 68 ? 10.593  -23.363 -40.654 1.00 71.55  ? 67  LYS   B CD  1 
ATOM   1259 C CE  . LYS   B 1 68 ? 10.956  -24.611 -39.907 1.00 69.21  ? 67  LYS   B CE  1 
ATOM   1260 N NZ  . LYS   B 1 68 ? 9.745   -25.308 -39.462 1.00 64.10  ? 67  LYS   B NZ  1 
ATOM   1261 N N   . TYR   B 1 69 ? 9.693   -18.862 -38.292 1.00 42.01  ? 68  TYR   B N   1 
ATOM   1262 C CA  . TYR   B 1 69 ? 10.117  -18.573 -36.929 1.00 44.03  ? 68  TYR   B CA  1 
ATOM   1263 C C   . TYR   B 1 69 ? 9.661   -17.191 -36.462 1.00 45.78  ? 68  TYR   B C   1 
ATOM   1264 O O   . TYR   B 1 69 ? 9.790   -16.876 -35.283 1.00 47.62  ? 68  TYR   B O   1 
ATOM   1265 C CB  . TYR   B 1 69 ? 11.631  -18.711 -36.771 1.00 44.56  ? 68  TYR   B CB  1 
ATOM   1266 C CG  . TYR   B 1 69 ? 12.222  -20.095 -37.031 1.00 50.19  ? 68  TYR   B CG  1 
ATOM   1267 C CD1 . TYR   B 1 69 ? 11.718  -21.245 -36.423 1.00 50.05  ? 68  TYR   B CD1 1 
ATOM   1268 C CD2 . TYR   B 1 69 ? 13.304  -20.241 -37.896 1.00 50.77  ? 68  TYR   B CD2 1 
ATOM   1269 C CE1 . TYR   B 1 69 ? 12.265  -22.499 -36.678 1.00 52.22  ? 68  TYR   B CE1 1 
ATOM   1270 C CE2 . TYR   B 1 69 ? 13.857  -21.482 -38.159 1.00 52.96  ? 68  TYR   B CE2 1 
ATOM   1271 C CZ  . TYR   B 1 69 ? 13.343  -22.612 -37.545 1.00 53.36  ? 68  TYR   B CZ  1 
ATOM   1272 O OH  . TYR   B 1 69 ? 13.923  -23.807 -37.835 1.00 49.68  ? 68  TYR   B OH  1 
ATOM   1273 N N   . GLY   B 1 70 ? 9.125   -16.364 -37.367 1.00 46.68  ? 69  GLY   B N   1 
ATOM   1274 C CA  . GLY   B 1 70 ? 8.841   -14.978 -37.030 1.00 54.78  ? 69  GLY   B CA  1 
ATOM   1275 C C   . GLY   B 1 70 ? 7.426   -14.772 -36.486 1.00 60.80  ? 69  GLY   B C   1 
ATOM   1276 O O   . GLY   B 1 70 ? 6.753   -13.809 -36.865 1.00 57.93  ? 69  GLY   B O   1 
ATOM   1277 N N   . LYS   B 1 71 ? 6.979   -15.683 -35.608 1.00 55.94  ? 70  LYS   B N   1 
ATOM   1278 C CA  . LYS   B 1 71 ? 5.634   -15.610 -35.070 1.00 55.72  ? 70  LYS   B CA  1 
ATOM   1279 C C   . LYS   B 1 71 ? 5.719   -15.137 -33.631 1.00 60.98  ? 70  LYS   B C   1 
ATOM   1280 O O   . LYS   B 1 71 ? 6.650   -15.513 -32.919 1.00 58.66  ? 70  LYS   B O   1 
ATOM   1281 C CB  . LYS   B 1 71 ? 4.840   -16.919 -35.106 1.00 57.96  ? 70  LYS   B CB  1 
ATOM   1282 C CG  . LYS   B 1 71 ? 3.951   -17.107 -36.332 1.00 63.81  ? 70  LYS   B CG  1 
ATOM   1283 C CD  . LYS   B 1 71 ? 4.644   -17.814 -37.490 1.00 70.56  ? 70  LYS   B CD  1 
ATOM   1284 C CE  . LYS   B 1 71 ? 3.691   -18.247 -38.569 1.00 81.40  ? 70  LYS   B CE  1 
ATOM   1285 N NZ  . LYS   B 1 71 ? 4.269   -19.289 -39.426 1.00 75.57  ? 70  LYS   B NZ  1 
ATOM   1286 N N   . PRO   B 1 72 ? 4.770   -14.286 -33.171 1.00 58.87  ? 71  PRO   B N   1 
ATOM   1287 C CA  . PRO   B 1 72 ? 4.750   -13.866 -31.769 1.00 58.92  ? 71  PRO   B CA  1 
ATOM   1288 C C   . PRO   B 1 72 ? 4.541   -15.077 -30.864 1.00 57.84  ? 71  PRO   B C   1 
ATOM   1289 O O   . PRO   B 1 72 ? 3.917   -16.064 -31.269 1.00 54.26  ? 71  PRO   B O   1 
ATOM   1290 C CB  . PRO   B 1 72 ? 3.606   -12.837 -31.679 1.00 57.42  ? 71  PRO   B CB  1 
ATOM   1291 C CG  . PRO   B 1 72 ? 3.354   -12.444 -33.114 1.00 58.86  ? 71  PRO   B CG  1 
ATOM   1292 C CD  . PRO   B 1 72 ? 3.706   -13.659 -33.969 1.00 54.45  ? 71  PRO   B CD  1 
ATOM   1293 N N   . ASN   B 1 73 ? 5.130   -15.000 -29.661 1.00 58.89  ? 72  ASN   B N   1 
ATOM   1294 C CA  . ASN   B 1 73 ? 4.899   -15.970 -28.602 1.00 55.45  ? 72  ASN   B CA  1 
ATOM   1295 C C   . ASN   B 1 73 ? 4.949   -15.239 -27.256 1.00 57.16  ? 72  ASN   B C   1 
ATOM   1296 O O   . ASN   B 1 73 ? 5.011   -14.007 -27.210 1.00 55.07  ? 72  ASN   B O   1 
ATOM   1297 C CB  . ASN   B 1 73 ? 5.849   -17.160 -28.692 1.00 48.50  ? 72  ASN   B CB  1 
ATOM   1298 C CG  . ASN   B 1 73 ? 7.279   -16.775 -28.375 1.00 51.25  ? 72  ASN   B CG  1 
ATOM   1299 O OD1 . ASN   B 1 73 ? 7.528   -16.028 -27.422 1.00 45.32  ? 72  ASN   B OD1 1 
ATOM   1300 N ND2 . ASN   B 1 73 ? 8.232   -17.207 -29.191 1.00 46.03  ? 72  ASN   B ND2 1 
ATOM   1301 N N   . LYS   B 1 74 ? 4.954   -16.020 -26.170 1.00 48.81  ? 73  LYS   B N   1 
ATOM   1302 C CA  . LYS   B 1 74 ? 4.758   -15.510 -24.824 1.00 56.90  ? 73  LYS   B CA  1 
ATOM   1303 C C   . LYS   B 1 74 ? 6.084   -15.372 -24.072 1.00 57.93  ? 73  LYS   B C   1 
ATOM   1304 O O   . LYS   B 1 74 ? 6.056   -15.019 -22.894 1.00 59.14  ? 73  LYS   B O   1 
ATOM   1305 C CB  . LYS   B 1 74 ? 3.742   -16.366 -24.044 1.00 56.06  ? 73  LYS   B CB  1 
ATOM   1306 N N   . ARG   B 1 75 ? 7.236   -15.631 -24.728 1.00 44.61  ? 74  ARG   B N   1 
ATOM   1307 C CA  . ARG   B 1 75 ? 8.507   -15.472 -24.023 1.00 41.06  ? 74  ARG   B CA  1 
ATOM   1308 C C   . ARG   B 1 75 ? 8.812   -13.980 -23.858 1.00 42.28  ? 74  ARG   B C   1 
ATOM   1309 O O   . ARG   B 1 75 ? 8.613   -13.190 -24.794 1.00 41.41  ? 74  ARG   B O   1 
ATOM   1310 C CB  . ARG   B 1 75 ? 9.669   -16.204 -24.705 1.00 46.08  ? 74  ARG   B CB  1 
ATOM   1311 C CG  . ARG   B 1 75 ? 9.518   -17.698 -24.967 1.00 39.84  ? 74  ARG   B CG  1 
ATOM   1312 C CD  . ARG   B 1 75 ? 9.295   -18.472 -23.670 1.00 45.56  ? 74  ARG   B CD  1 
ATOM   1313 N NE  . ARG   B 1 75 ? 9.518   -19.898 -23.910 1.00 43.93  ? 74  ARG   B NE  1 
ATOM   1314 C CZ  . ARG   B 1 75 ? 10.623  -20.560 -23.625 1.00 47.33  ? 74  ARG   B CZ  1 
ATOM   1315 N NH1 . ARG   B 1 75 ? 11.652  -19.975 -23.031 1.00 51.21  ? 74  ARG   B NH1 1 
ATOM   1316 N NH2 . ARG   B 1 75 ? 10.713  -21.812 -24.009 1.00 45.73  ? 74  ARG   B NH2 1 
ATOM   1317 N N   . LYS   B 1 76 ? 9.325   -13.602 -22.673 1.00 41.88  ? 75  LYS   B N   1 
ATOM   1318 C CA  . LYS   B 1 76 ? 9.627   -12.212 -22.352 1.00 36.08  ? 75  LYS   B CA  1 
ATOM   1319 C C   . LYS   B 1 76 ? 10.703  -11.664 -23.297 1.00 38.58  ? 75  LYS   B C   1 
ATOM   1320 O O   . LYS   B 1 76 ? 11.814  -12.213 -23.376 1.00 39.04  ? 75  LYS   B O   1 
ATOM   1321 C CB  . LYS   B 1 76 ? 10.256  -12.073 -20.959 1.00 35.58  ? 75  LYS   B CB  1 
ATOM   1322 C CG  . LYS   B 1 76 ? 10.388  -10.620 -20.514 1.00 37.39  ? 75  LYS   B CG  1 
ATOM   1323 C CD  . LYS   B 1 76 ? 11.024  -10.490 -19.135 1.00 42.74  ? 75  LYS   B CD  1 
ATOM   1324 C CE  . LYS   B 1 76 ? 11.068  -9.072  -18.648 1.00 46.84  ? 75  LYS   B CE  1 
ATOM   1325 N NZ  . LYS   B 1 76 ? 11.598  -9.028  -17.278 1.00 57.03  ? 75  LYS   B NZ  1 
ATOM   1326 N N   . GLY   B 1 77 ? 10.374  -10.551 -23.965 1.00 40.78  ? 76  GLY   B N   1 
ATOM   1327 C CA  . GLY   B 1 77 ? 11.325  -9.857  -24.826 1.00 40.18  ? 76  GLY   B CA  1 
ATOM   1328 C C   . GLY   B 1 77 ? 11.178  -10.252 -26.298 1.00 40.34  ? 76  GLY   B C   1 
ATOM   1329 O O   . GLY   B 1 77 ? 11.746  -9.595  -27.163 1.00 39.75  ? 76  GLY   B O   1 
ATOM   1330 N N   . PHE   B 1 78 ? 10.365  -11.274 -26.598 1.00 41.24  ? 77  PHE   B N   1 
ATOM   1331 C CA  . PHE   B 1 78 ? 10.304  -11.860 -27.934 1.00 40.47  ? 77  PHE   B CA  1 
ATOM   1332 C C   . PHE   B 1 78 ? 9.567   -10.949 -28.912 1.00 46.88  ? 77  PHE   B C   1 
ATOM   1333 O O   . PHE   B 1 78 ? 10.064  -10.653 -30.005 1.00 39.74  ? 77  PHE   B O   1 
ATOM   1334 C CB  . PHE   B 1 78 ? 9.611   -13.224 -27.980 1.00 40.35  ? 77  PHE   B CB  1 
ATOM   1335 C CG  . PHE   B 1 78 ? 9.836   -13.978 -29.284 1.00 37.04  ? 77  PHE   B CG  1 
ATOM   1336 C CD1 . PHE   B 1 78 ? 10.956  -14.786 -29.453 1.00 41.18  ? 77  PHE   B CD1 1 
ATOM   1337 C CD2 . PHE   B 1 78 ? 8.941   -13.853 -30.342 1.00 41.71  ? 77  PHE   B CD2 1 
ATOM   1338 C CE1 . PHE   B 1 78 ? 11.162  -15.488 -30.634 1.00 39.86  ? 77  PHE   B CE1 1 
ATOM   1339 C CE2 . PHE   B 1 78 ? 9.159   -14.548 -31.527 1.00 42.76  ? 77  PHE   B CE2 1 
ATOM   1340 C CZ  . PHE   B 1 78 ? 10.261  -15.368 -31.661 1.00 40.80  ? 77  PHE   B CZ  1 
ATOM   1341 N N   . ASN   B 1 79 ? 8.369   -10.522 -28.518 1.00 42.65  ? 78  ASN   B N   1 
ATOM   1342 C CA  . ASN   B 1 79 ? 7.537   -9.711  -29.379 1.00 42.18  ? 78  ASN   B CA  1 
ATOM   1343 C C   . ASN   B 1 79 ? 8.242   -8.374  -29.617 1.00 49.19  ? 78  ASN   B C   1 
ATOM   1344 O O   . ASN   B 1 79 ? 8.103   -7.783  -30.682 1.00 47.28  ? 78  ASN   B O   1 
ATOM   1345 C CB  . ASN   B 1 79 ? 6.087   -9.657  -28.875 1.00 46.19  ? 78  ASN   B CB  1 
ATOM   1346 C CG  . ASN   B 1 79 ? 5.322   -10.956 -29.047 1.00 51.37  ? 78  ASN   B CG  1 
ATOM   1347 O OD1 . ASN   B 1 79 ? 5.747   -11.861 -29.770 1.00 52.09  ? 78  ASN   B OD1 1 
ATOM   1348 N ND2 . ASN   B 1 79 ? 4.166   -11.082 -28.409 1.00 49.03  ? 78  ASN   B ND2 1 
ATOM   1349 N N   . GLU   B 1 80 ? 9.036   -7.915  -28.639 1.00 44.24  ? 79  GLU   B N   1 
ATOM   1350 C CA  . GLU   B 1 80 ? 9.771   -6.676  -28.808 1.00 46.71  ? 79  GLU   B CA  1 
ATOM   1351 C C   . GLU   B 1 80 ? 10.915  -6.908  -29.801 1.00 50.66  ? 79  GLU   B C   1 
ATOM   1352 O O   . GLU   B 1 80 ? 11.220  -6.022  -30.607 1.00 47.01  ? 79  GLU   B O   1 
ATOM   1353 C CB  . GLU   B 1 80 ? 10.328  -6.130  -27.491 1.00 44.08  ? 79  GLU   B CB  1 
ATOM   1354 C CG  . GLU   B 1 80 ? 9.301   -5.357  -26.669 1.00 49.52  ? 79  GLU   B CG  1 
ATOM   1355 N N   . GLY   B 1 81 ? 11.537  -8.100  -29.721 1.00 45.55  ? 80  GLY   B N   1 
ATOM   1356 C CA  . GLY   B 1 81 ? 12.594  -8.540  -30.637 1.00 43.06  ? 80  GLY   B CA  1 
ATOM   1357 C C   . GLY   B 1 81 ? 12.115  -8.538  -32.087 1.00 41.54  ? 80  GLY   B C   1 
ATOM   1358 O O   . GLY   B 1 81 ? 12.849  -8.114  -32.980 1.00 45.62  ? 80  GLY   B O   1 
ATOM   1359 N N   . LEU   B 1 82 ? 10.888  -9.022  -32.311 1.00 38.23  ? 81  LEU   B N   1 
ATOM   1360 C CA  . LEU   B 1 82 ? 10.276  -9.017  -33.629 1.00 43.61  ? 81  LEU   B CA  1 
ATOM   1361 C C   . LEU   B 1 82 ? 10.143  -7.578  -34.119 1.00 44.03  ? 81  LEU   B C   1 
ATOM   1362 O O   . LEU   B 1 82 ? 10.474  -7.288  -35.261 1.00 43.40  ? 81  LEU   B O   1 
ATOM   1363 C CB  . LEU   B 1 82 ? 8.936   -9.754  -33.691 1.00 45.74  ? 81  LEU   B CB  1 
ATOM   1364 C CG  . LEU   B 1 82 ? 8.967   -11.264 -33.429 1.00 41.96  ? 81  LEU   B CG  1 
ATOM   1365 C CD1 . LEU   B 1 82 ? 7.568   -11.879 -33.524 1.00 42.51  ? 81  LEU   B CD1 1 
ATOM   1366 C CD2 . LEU   B 1 82 ? 9.899   -11.922 -34.418 1.00 38.02  ? 81  LEU   B CD2 1 
ATOM   1367 N N   . TRP   B 1 83 ? 9.692   -6.674  -33.242 1.00 45.07  ? 82  TRP   B N   1 
ATOM   1368 C CA  . TRP   B 1 83 ? 9.581   -5.264  -33.582 1.00 44.22  ? 82  TRP   B CA  1 
ATOM   1369 C C   . TRP   B 1 83 ? 10.929  -4.682  -34.032 1.00 42.89  ? 82  TRP   B C   1 
ATOM   1370 O O   . TRP   B 1 83 ? 10.974  -3.968  -35.035 1.00 42.88  ? 82  TRP   B O   1 
ATOM   1371 C CB  . TRP   B 1 83 ? 8.963   -4.423  -32.448 1.00 46.77  ? 82  TRP   B CB  1 
ATOM   1372 C CG  . TRP   B 1 83 ? 8.652   -3.030  -32.928 1.00 44.13  ? 82  TRP   B CG  1 
ATOM   1373 C CD1 . TRP   B 1 83 ? 7.486   -2.622  -33.505 1.00 51.18  ? 82  TRP   B CD1 1 
ATOM   1374 C CD2 . TRP   B 1 83 ? 9.562   -1.907  -33.005 1.00 46.08  ? 82  TRP   B CD2 1 
ATOM   1375 N NE1 . TRP   B 1 83 ? 7.595   -1.314  -33.903 1.00 55.77  ? 82  TRP   B NE1 1 
ATOM   1376 C CE2 . TRP   B 1 83 ? 8.858   -0.853  -33.619 1.00 51.69  ? 82  TRP   B CE2 1 
ATOM   1377 C CE3 . TRP   B 1 83 ? 10.898  -1.690  -32.627 1.00 45.78  ? 82  TRP   B CE3 1 
ATOM   1378 C CZ2 . TRP   B 1 83 ? 9.438   0.397   -33.841 1.00 46.19  ? 82  TRP   B CZ2 1 
ATOM   1379 C CZ3 . TRP   B 1 83 ? 11.473  -0.459  -32.855 1.00 51.07  ? 82  TRP   B CZ3 1 
ATOM   1380 C CH2 . TRP   B 1 83 ? 10.748  0.569   -33.464 1.00 48.20  ? 82  TRP   B CH2 1 
ATOM   1381 N N   . GLU   B 1 84 ? 12.004  -4.951  -33.274 1.00 38.52  ? 83  GLU   B N   1 
ATOM   1382 C CA  . GLU   B 1 84 ? 13.308  -4.382  -33.547 1.00 40.43  ? 83  GLU   B CA  1 
ATOM   1383 C C   . GLU   B 1 84 ? 13.830  -4.860  -34.900 1.00 42.59  ? 83  GLU   B C   1 
ATOM   1384 O O   . GLU   B 1 84 ? 14.224  -4.041  -35.736 1.00 45.68  ? 83  GLU   B O   1 
ATOM   1385 C CB  . GLU   B 1 84 ? 14.336  -4.654  -32.447 1.00 40.32  ? 83  GLU   B CB  1 
ATOM   1386 C CG  . GLU   B 1 84 ? 13.902  -4.065  -31.105 1.00 48.20  ? 83  GLU   B CG  1 
ATOM   1387 C CD  . GLU   B 1 84 ? 14.832  -4.308  -29.937 1.00 47.71  ? 83  GLU   B CD  1 
ATOM   1388 O OE1 . GLU   B 1 84 ? 15.787  -5.105  -30.095 1.00 45.99  ? 83  GLU   B OE1 1 
ATOM   1389 O OE2 . GLU   B 1 84 ? 14.644  -3.656  -28.877 1.00 42.07  ? 83  GLU   B OE2 1 
ATOM   1390 N N   . ILE   B 1 85 ? 13.851  -6.182  -35.097 1.00 40.17  ? 84  ILE   B N   1 
ATOM   1391 C CA  . ILE   B 1 85 ? 14.437  -6.774  -36.303 1.00 42.64  ? 84  ILE   B CA  1 
ATOM   1392 C C   . ILE   B 1 85 ? 13.732  -6.238  -37.545 1.00 39.58  ? 84  ILE   B C   1 
ATOM   1393 O O   . ILE   B 1 85 ? 14.345  -6.103  -38.610 1.00 38.34  ? 84  ILE   B O   1 
ATOM   1394 C CB  . ILE   B 1 85 ? 14.422  -8.319  -36.262 1.00 38.04  ? 84  ILE   B CB  1 
ATOM   1395 C CG1 . ILE   B 1 85 ? 15.376  -8.896  -37.306 1.00 37.06  ? 84  ILE   B CG1 1 
ATOM   1396 C CG2 . ILE   B 1 85 ? 13.018  -8.888  -36.462 1.00 37.58  ? 84  ILE   B CG2 1 
ATOM   1397 C CD1 . ILE   B 1 85 ? 15.947  -10.264 -36.956 1.00 39.44  ? 84  ILE   B CD1 1 
ATOM   1398 N N   . GLN   B 1 86 ? 12.433  -5.966  -37.406 1.00 43.91  ? 85  GLN   B N   1 
ATOM   1399 C CA  . GLN   B 1 86 ? 11.594  -5.435  -38.470 1.00 44.99  ? 85  GLN   B CA  1 
ATOM   1400 C C   . GLN   B 1 86 ? 11.811  -3.935  -38.726 1.00 45.17  ? 85  GLN   B C   1 
ATOM   1401 O O   . GLN   B 1 86 ? 11.722  -3.487  -39.862 1.00 51.70  ? 85  GLN   B O   1 
ATOM   1402 C CB  . GLN   B 1 86 ? 10.143  -5.764  -38.114 1.00 53.24  ? 85  GLN   B CB  1 
ATOM   1403 C CG  . GLN   B 1 86 ? 9.698   -7.144  -38.598 1.00 67.54  ? 85  GLN   B CG  1 
ATOM   1404 C CD  . GLN   B 1 86 ? 8.584   -7.797  -37.803 1.00 66.73  ? 85  GLN   B CD  1 
ATOM   1405 O OE1 . GLN   B 1 86 ? 7.441   -7.324  -37.754 1.00 72.35  ? 85  GLN   B OE1 1 
ATOM   1406 N NE2 . GLN   B 1 86 ? 8.910   -8.938  -37.210 1.00 60.02  ? 85  GLN   B NE2 1 
ATOM   1407 N N   . ASN   B 1 87 ? 12.061  -3.130  -37.693 1.00 42.59  ? 86  ASN   B N   1 
ATOM   1408 C CA  . ASN   B 1 87 ? 11.877  -1.692  -37.846 1.00 40.85  ? 86  ASN   B CA  1 
ATOM   1409 C C   . ASN   B 1 87 ? 13.186  -0.937  -37.706 1.00 40.50  ? 86  ASN   B C   1 
ATOM   1410 O O   . ASN   B 1 87 ? 13.317  0.168   -38.233 1.00 49.05  ? 86  ASN   B O   1 
ATOM   1411 C CB  . ASN   B 1 87 ? 10.989  -1.119  -36.745 1.00 43.27  ? 86  ASN   B CB  1 
ATOM   1412 C CG  . ASN   B 1 87 ? 9.572   -1.577  -36.947 1.00 52.38  ? 86  ASN   B CG  1 
ATOM   1413 O OD1 . ASN   B 1 87 ? 8.850   -0.980  -37.750 1.00 59.68  ? 86  ASN   B OD1 1 
ATOM   1414 N ND2 . ASN   B 1 87 ? 9.184   -2.655  -36.281 1.00 60.61  ? 86  ASN   B ND2 1 
ATOM   1415 N N   . ASN   B 1 88 ? 14.107  -1.494  -36.918 1.00 37.97  ? 87  ASN   B N   1 
ATOM   1416 C CA  . ASN   B 1 88 ? 15.387  -0.852  -36.703 1.00 38.48  ? 87  ASN   B CA  1 
ATOM   1417 C C   . ASN   B 1 88 ? 16.464  -1.888  -36.383 1.00 39.54  ? 87  ASN   B C   1 
ATOM   1418 O O   . ASN   B 1 88 ? 17.139  -1.811  -35.344 1.00 40.26  ? 87  ASN   B O   1 
ATOM   1419 C CB  . ASN   B 1 88 ? 15.261  0.384   -35.805 1.00 45.97  ? 87  ASN   B CB  1 
ATOM   1420 C CG  . ASN   B 1 88 ? 16.453  1.308   -35.951 1.00 44.86  ? 87  ASN   B CG  1 
ATOM   1421 O OD1 . ASN   B 1 88 ? 17.399  1.005   -36.687 1.00 45.13  ? 87  ASN   B OD1 1 
ATOM   1422 N ND2 . ASN   B 1 88 ? 16.453  2.439   -35.258 1.00 51.68  ? 87  ASN   B ND2 1 
ATOM   1423 N N   . PRO   B 1 89 ? 16.714  -2.872  -37.288 1.00 41.02  ? 88  PRO   B N   1 
ATOM   1424 C CA  . PRO   B 1 89 ? 17.704  -3.912  -37.014 1.00 36.83  ? 88  PRO   B CA  1 
ATOM   1425 C C   . PRO   B 1 89 ? 19.106  -3.437  -36.684 1.00 37.78  ? 88  PRO   B C   1 
ATOM   1426 O O   . PRO   B 1 89 ? 19.850  -4.194  -36.063 1.00 37.87  ? 88  PRO   B O   1 
ATOM   1427 C CB  . PRO   B 1 89 ? 17.720  -4.800  -38.290 1.00 36.31  ? 88  PRO   B CB  1 
ATOM   1428 C CG  . PRO   B 1 89 ? 17.043  -3.948  -39.355 1.00 35.55  ? 88  PRO   B CG  1 
ATOM   1429 C CD  . PRO   B 1 89 ? 16.008  -3.105  -38.560 1.00 35.08  ? 88  PRO   B CD  1 
ATOM   1430 N N   . HIS   B 1 90 ? 19.484  -2.235  -37.177 1.00 37.12  ? 89  HIS   B N   1 
ATOM   1431 C CA  . HIS   B 1 90 ? 20.883  -1.841  -37.141 1.00 39.52  ? 89  HIS   B CA  1 
ATOM   1432 C C   . HIS   B 1 90 ? 21.164  -0.813  -36.038 1.00 42.93  ? 89  HIS   B C   1 
ATOM   1433 O O   . HIS   B 1 90 ? 22.309  -0.381  -35.899 1.00 41.76  ? 89  HIS   B O   1 
ATOM   1434 C CB  . HIS   B 1 90 ? 21.373  -1.421  -38.538 1.00 39.27  ? 89  HIS   B CB  1 
ATOM   1435 C CG  . HIS   B 1 90 ? 21.222  -2.530  -39.548 1.00 34.40  ? 89  HIS   B CG  1 
ATOM   1436 N ND1 . HIS   B 1 90 ? 21.808  -3.764  -39.432 1.00 35.15  ? 89  HIS   B ND1 1 
ATOM   1437 C CD2 . HIS   B 1 90 ? 20.552  -2.548  -40.702 1.00 38.87  ? 89  HIS   B CD2 1 
ATOM   1438 C CE1 . HIS   B 1 90 ? 21.480  -4.501  -40.473 1.00 32.03  ? 89  HIS   B CE1 1 
ATOM   1439 N NE2 . HIS   B 1 90 ? 20.708  -3.782  -41.259 1.00 37.48  ? 89  HIS   B NE2 1 
ATOM   1440 N N   . ALA   B 1 91 ? 20.154  -0.473  -35.217 1.00 42.73  ? 90  ALA   B N   1 
ATOM   1441 C CA  . ALA   B 1 91 ? 20.324  0.544   -34.177 1.00 39.04  ? 90  ALA   B CA  1 
ATOM   1442 C C   . ALA   B 1 91 ? 21.351  0.125   -33.133 1.00 45.47  ? 90  ALA   B C   1 
ATOM   1443 O O   . ALA   B 1 91 ? 21.569  -1.066  -32.928 1.00 42.61  ? 90  ALA   B O   1 
ATOM   1444 C CB  . ALA   B 1 91 ? 18.982  0.857   -33.539 1.00 36.56  ? 90  ALA   B CB  1 
ATOM   1445 N N   . SER   B 1 92 ? 21.980  1.117   -32.470 1.00 46.00  ? 91  SER   B N   1 
ATOM   1446 C CA  . SER   B 1 92 ? 22.666  0.882   -31.210 1.00 50.37  ? 91  SER   B CA  1 
ATOM   1447 C C   . SER   B 1 92 ? 21.617  0.610   -30.136 1.00 58.63  ? 91  SER   B C   1 
ATOM   1448 O O   . SER   B 1 92 ? 20.625  1.336   -30.056 1.00 58.68  ? 91  SER   B O   1 
ATOM   1449 C CB  . SER   B 1 92 ? 23.506  2.073   -30.816 1.00 61.53  ? 91  SER   B CB  1 
ATOM   1450 O OG  . SER   B 1 92 ? 23.976  1.934   -29.480 1.00 60.36  ? 91  SER   B OG  1 
ATOM   1451 N N   . TYR   B 1 93 ? 21.844  -0.437  -29.327 1.00 59.23  ? 92  TYR   B N   1 
ATOM   1452 C CA  . TYR   B 1 93 ? 20.920  -0.818  -28.266 1.00 58.48  ? 92  TYR   B CA  1 
ATOM   1453 C C   . TYR   B 1 93 ? 21.643  -0.712  -26.922 1.00 66.01  ? 92  TYR   B C   1 
ATOM   1454 O O   . TYR   B 1 93 ? 21.148  -1.206  -25.914 1.00 69.82  ? 92  TYR   B O   1 
ATOM   1455 C CB  . TYR   B 1 93 ? 20.201  -2.152  -28.544 1.00 47.31  ? 92  TYR   B CB  1 
ATOM   1456 C CG  . TYR   B 1 93 ? 19.125  -2.070  -29.620 1.00 47.25  ? 92  TYR   B CG  1 
ATOM   1457 C CD1 . TYR   B 1 93 ? 17.852  -1.603  -29.332 1.00 42.24  ? 92  TYR   B CD1 1 
ATOM   1458 C CD2 . TYR   B 1 93 ? 19.374  -2.473  -30.931 1.00 48.75  ? 92  TYR   B CD2 1 
ATOM   1459 C CE1 . TYR   B 1 93 ? 16.873  -1.490  -30.303 1.00 45.65  ? 92  TYR   B CE1 1 
ATOM   1460 C CE2 . TYR   B 1 93 ? 18.395  -2.369  -31.912 1.00 42.73  ? 92  TYR   B CE2 1 
ATOM   1461 C CZ  . TYR   B 1 93 ? 17.146  -1.879  -31.599 1.00 40.08  ? 92  TYR   B CZ  1 
ATOM   1462 O OH  . TYR   B 1 93 ? 16.180  -1.788  -32.564 1.00 41.74  ? 92  TYR   B OH  1 
ATOM   1463 N N   . SER   B 1 94 ? 22.811  -0.046  -26.931 1.00 84.47  ? 93  SER   B N   1 
ATOM   1464 C CA  . SER   B 1 94 ? 23.608  0.254   -25.747 1.00 85.03  ? 93  SER   B CA  1 
ATOM   1465 C C   . SER   B 1 94 ? 22.750  0.998   -24.716 1.00 98.93  ? 93  SER   B C   1 
ATOM   1466 O O   . SER   B 1 94 ? 21.946  1.858   -25.150 1.00 92.67  ? 93  SER   B O   1 
ATOM   1467 C CB  . SER   B 1 94 ? 24.823  1.090   -26.078 1.00 84.30  ? 93  SER   B CB  1 
ATOM   1468 O OG  . SER   B 1 94 ? 25.647  0.488   -27.066 1.00 86.83  ? 93  SER   B OG  1 
ATOM   1469 O OXT . SER   B 1 94 ? 22.935  0.712   -23.511 1.00 116.96 ? 93  SER   B OXT 1 
ATOM   1470 N N   . HIS   C 1 4  ? 32.884  -24.124 26.715  1.00 73.57  ? 3   HIS   C N   1 
ATOM   1471 C CA  . HIS   C 1 4  ? 32.029  -23.050 27.292  1.00 85.62  ? 3   HIS   C CA  1 
ATOM   1472 C C   . HIS   C 1 4  ? 31.529  -23.512 28.660  1.00 94.46  ? 3   HIS   C C   1 
ATOM   1473 O O   . HIS   C 1 4  ? 32.278  -24.127 29.421  1.00 95.98  ? 3   HIS   C O   1 
ATOM   1474 C CB  . HIS   C 1 4  ? 30.918  -22.659 26.305  1.00 82.30  ? 3   HIS   C CB  1 
ATOM   1475 N N   . ALA   C 1 5  ? 30.263  -23.197 28.961  1.00 88.69  ? 4   ALA   C N   1 
ATOM   1476 C CA  . ALA   C 1 5  ? 29.555  -23.747 30.105  1.00 82.97  ? 4   ALA   C CA  1 
ATOM   1477 C C   . ALA   C 1 5  ? 28.067  -23.466 29.957  1.00 89.77  ? 4   ALA   C C   1 
ATOM   1478 O O   . ALA   C 1 5  ? 27.657  -22.358 29.605  1.00 95.47  ? 4   ALA   C O   1 
ATOM   1479 C CB  . ALA   C 1 5  ? 30.079  -23.159 31.379  1.00 88.77  ? 4   ALA   C CB  1 
ATOM   1480 N N   . PHE   C 1 6  ? 27.266  -24.490 30.241  1.00 78.48  ? 5   PHE   C N   1 
ATOM   1481 C CA  . PHE   C 1 6  ? 25.868  -24.439 29.870  1.00 69.50  ? 5   PHE   C CA  1 
ATOM   1482 C C   . PHE   C 1 6  ? 25.046  -24.448 31.148  1.00 71.52  ? 5   PHE   C C   1 
ATOM   1483 O O   . PHE   C 1 6  ? 25.378  -25.181 32.077  1.00 83.24  ? 5   PHE   C O   1 
ATOM   1484 C CB  . PHE   C 1 6  ? 25.585  -25.582 28.885  1.00 66.73  ? 5   PHE   C CB  1 
ATOM   1485 C CG  . PHE   C 1 6  ? 26.384  -25.513 27.586  1.00 64.27  ? 5   PHE   C CG  1 
ATOM   1486 C CD1 . PHE   C 1 6  ? 27.485  -26.341 27.374  1.00 67.86  ? 5   PHE   C CD1 1 
ATOM   1487 C CD2 . PHE   C 1 6  ? 26.049  -24.605 26.584  1.00 64.34  ? 5   PHE   C CD2 1 
ATOM   1488 C CE1 . PHE   C 1 6  ? 28.223  -26.273 26.195  1.00 65.28  ? 5   PHE   C CE1 1 
ATOM   1489 C CE2 . PHE   C 1 6  ? 26.782  -24.547 25.403  1.00 67.31  ? 5   PHE   C CE2 1 
ATOM   1490 C CZ  . PHE   C 1 6  ? 27.861  -25.382 25.204  1.00 60.44  ? 5   PHE   C CZ  1 
ATOM   1491 N N   . LYS   C 1 7  ? 24.011  -23.597 31.186  1.00 70.50  ? 6   LYS   C N   1 
ATOM   1492 C CA  . LYS   C 1 7  ? 23.003  -23.613 32.238  1.00 78.18  ? 6   LYS   C CA  1 
ATOM   1493 C C   . LYS   C 1 7  ? 21.669  -23.923 31.567  1.00 81.33  ? 6   LYS   C C   1 
ATOM   1494 O O   . LYS   C 1 7  ? 21.548  -23.726 30.360  1.00 94.88  ? 6   LYS   C O   1 
ATOM   1495 C CB  . LYS   C 1 7  ? 22.959  -22.297 33.029  1.00 72.02  ? 6   LYS   C CB  1 
ATOM   1496 N N   . PRO   C 1 8  ? 20.646  -24.447 32.287  1.00 79.11  ? 7   PRO   C N   1 
ATOM   1497 C CA  . PRO   C 1 8  ? 19.359  -24.756 31.658  1.00 77.57  ? 7   PRO   C CA  1 
ATOM   1498 C C   . PRO   C 1 8  ? 18.815  -23.546 30.902  1.00 81.20  ? 7   PRO   C C   1 
ATOM   1499 O O   . PRO   C 1 8  ? 19.008  -22.407 31.328  1.00 80.90  ? 7   PRO   C O   1 
ATOM   1500 C CB  . PRO   C 1 8  ? 18.459  -25.187 32.821  1.00 76.67  ? 7   PRO   C CB  1 
ATOM   1501 C CG  . PRO   C 1 8  ? 19.434  -25.675 33.874  1.00 78.62  ? 7   PRO   C CG  1 
ATOM   1502 C CD  . PRO   C 1 8  ? 20.677  -24.805 33.715  1.00 85.02  ? 7   PRO   C CD  1 
ATOM   1503 N N   . GLY   C 1 9  ? 18.180  -23.808 29.754  1.00 75.71  ? 8   GLY   C N   1 
ATOM   1504 C CA  . GLY   C 1 9  ? 17.591  -22.752 28.949  1.00 66.88  ? 8   GLY   C CA  1 
ATOM   1505 C C   . GLY   C 1 9  ? 18.481  -22.347 27.775  1.00 66.66  ? 8   GLY   C C   1 
ATOM   1506 O O   . GLY   C 1 9  ? 17.967  -21.863 26.768  1.00 77.08  ? 8   GLY   C O   1 
ATOM   1507 N N   . ASP   C 1 10 ? 19.803  -22.535 27.907  1.00 57.96  ? 9   ASP   C N   1 
ATOM   1508 C CA  . ASP   C 1 10 ? 20.742  -22.191 26.846  1.00 63.22  ? 9   ASP   C CA  1 
ATOM   1509 C C   . ASP   C 1 10 ? 20.418  -22.992 25.576  1.00 61.64  ? 9   ASP   C C   1 
ATOM   1510 O O   . ASP   C 1 10 ? 20.013  -24.158 25.633  1.00 60.64  ? 9   ASP   C O   1 
ATOM   1511 C CB  . ASP   C 1 10 ? 22.198  -22.328 27.281  1.00 67.81  ? 9   ASP   C CB  1 
ATOM   1512 C CG  . ASP   C 1 10 ? 22.649  -21.561 28.524  1.00 74.44  ? 9   ASP   C CG  1 
ATOM   1513 O OD1 . ASP   C 1 10 ? 21.836  -20.803 29.097  1.00 79.23  ? 9   ASP   C OD1 1 
ATOM   1514 O OD2 . ASP   C 1 10 ? 23.817  -21.738 28.932  1.00 74.36  ? 9   ASP   C OD2 1 
ATOM   1515 N N   . LEU   C 1 11 ? 20.600  -22.337 24.424  1.00 61.00  ? 10  LEU   C N   1 
ATOM   1516 C CA  . LEU   C 1 11 ? 20.242  -22.889 23.128  1.00 61.64  ? 10  LEU   C CA  1 
ATOM   1517 C C   . LEU   C 1 11 ? 21.511  -23.344 22.408  1.00 60.46  ? 10  LEU   C C   1 
ATOM   1518 O O   . LEU   C 1 11 ? 22.504  -22.613 22.356  1.00 54.08  ? 10  LEU   C O   1 
ATOM   1519 C CB  . LEU   C 1 11 ? 19.458  -21.854 22.316  1.00 60.00  ? 10  LEU   C CB  1 
ATOM   1520 C CG  . LEU   C 1 11 ? 18.216  -21.239 22.973  1.00 56.24  ? 10  LEU   C CG  1 
ATOM   1521 C CD1 . LEU   C 1 11 ? 17.657  -20.182 22.036  1.00 60.49  ? 10  LEU   C CD1 1 
ATOM   1522 C CD2 . LEU   C 1 11 ? 17.134  -22.258 23.320  1.00 55.37  ? 10  LEU   C CD2 1 
ATOM   1523 N N   . VAL   C 1 12 ? 21.455  -24.566 21.857  1.00 54.08  ? 11  VAL   C N   1 
ATOM   1524 C CA  . VAL   C 1 12 ? 22.623  -25.234 21.302  1.00 52.59  ? 11  VAL   C CA  1 
ATOM   1525 C C   . VAL   C 1 12 ? 22.250  -25.926 19.983  1.00 50.71  ? 11  VAL   C C   1 
ATOM   1526 O O   . VAL   C 1 12 ? 21.074  -26.123 19.692  1.00 49.39  ? 11  VAL   C O   1 
ATOM   1527 C CB  . VAL   C 1 12 ? 23.171  -26.272 22.314  1.00 47.52  ? 11  VAL   C CB  1 
ATOM   1528 C CG1 . VAL   C 1 12 ? 23.523  -25.658 23.670  1.00 43.07  ? 11  VAL   C CG1 1 
ATOM   1529 C CG2 . VAL   C 1 12 ? 22.227  -27.453 22.503  1.00 41.98  ? 11  VAL   C CG2 1 
ATOM   1530 N N   . PHE   C 1 13 ? 23.277  -26.301 19.210  1.00 42.72  ? 12  PHE   C N   1 
ATOM   1531 C CA  . PHE   C 1 13 ? 23.235  -27.463 18.329  1.00 42.08  ? 12  PHE   C CA  1 
ATOM   1532 C C   . PHE   C 1 13 ? 23.831  -28.646 19.083  1.00 41.55  ? 12  PHE   C C   1 
ATOM   1533 O O   . PHE   C 1 13 ? 24.847  -28.492 19.760  1.00 48.62  ? 12  PHE   C O   1 
ATOM   1534 C CB  . PHE   C 1 13 ? 23.947  -27.182 17.004  1.00 45.14  ? 12  PHE   C CB  1 
ATOM   1535 C CG  . PHE   C 1 13 ? 23.144  -26.204 16.161  1.00 48.16  ? 12  PHE   C CG  1 
ATOM   1536 C CD1 . PHE   C 1 13 ? 22.150  -26.660 15.283  1.00 48.05  ? 12  PHE   C CD1 1 
ATOM   1537 C CD2 . PHE   C 1 13 ? 23.360  -24.834 16.271  1.00 44.75  ? 12  PHE   C CD2 1 
ATOM   1538 C CE1 . PHE   C 1 13 ? 21.413  -25.758 14.522  1.00 46.47  ? 12  PHE   C CE1 1 
ATOM   1539 C CE2 . PHE   C 1 13 ? 22.607  -23.936 15.522  1.00 47.96  ? 12  PHE   C CE2 1 
ATOM   1540 C CZ  . PHE   C 1 13 ? 21.648  -24.397 14.643  1.00 49.48  ? 12  PHE   C CZ  1 
ATOM   1541 N N   . ALA   C 1 14 ? 23.120  -29.782 19.074  1.00 43.27  ? 13  ALA   C N   1 
ATOM   1542 C CA  . ALA   C 1 14 ? 23.550  -30.971 19.799  1.00 41.03  ? 13  ALA   C CA  1 
ATOM   1543 C C   . ALA   C 1 14 ? 23.839  -32.080 18.791  1.00 45.79  ? 13  ALA   C C   1 
ATOM   1544 O O   . ALA   C 1 14 ? 22.995  -32.366 17.927  1.00 36.24  ? 13  ALA   C O   1 
ATOM   1545 C CB  . ALA   C 1 14 ? 22.491  -31.386 20.787  1.00 38.12  ? 13  ALA   C CB  1 
ATOM   1546 N N   . LYS   C 1 15 ? 25.042  -32.670 18.898  1.00 40.53  ? 14  LYS   C N   1 
ATOM   1547 C CA  . LYS   C 1 15 ? 25.495  -33.645 17.920  1.00 39.14  ? 14  LYS   C CA  1 
ATOM   1548 C C   . LYS   C 1 15 ? 25.464  -35.042 18.529  1.00 44.37  ? 14  LYS   C C   1 
ATOM   1549 O O   . LYS   C 1 15 ? 26.182  -35.315 19.480  1.00 42.38  ? 14  LYS   C O   1 
ATOM   1550 C CB  . LYS   C 1 15 ? 26.871  -33.269 17.351  1.00 44.55  ? 14  LYS   C CB  1 
ATOM   1551 C CG  . LYS   C 1 15 ? 27.419  -34.202 16.276  1.00 42.22  ? 14  LYS   C CG  1 
ATOM   1552 C CD  . LYS   C 1 15 ? 26.596  -34.210 14.995  1.00 42.89  ? 14  LYS   C CD  1 
ATOM   1553 C CE  . LYS   C 1 15 ? 27.146  -35.108 13.904  1.00 45.21  ? 14  LYS   C CE  1 
ATOM   1554 N NZ  . LYS   C 1 15 ? 26.822  -36.523 14.121  1.00 39.80  ? 14  LYS   C NZ  1 
ATOM   1555 N N   . MET   C 1 16 ? 24.635  -35.926 17.961  1.00 41.47  ? 15  MET   C N   1 
ATOM   1556 C CA  . MET   C 1 16 ? 24.685  -37.347 18.273  1.00 39.48  ? 15  MET   C CA  1 
ATOM   1557 C C   . MET   C 1 16 ? 25.173  -38.142 17.060  1.00 48.98  ? 15  MET   C C   1 
ATOM   1558 O O   . MET   C 1 16 ? 24.967  -37.737 15.907  1.00 42.11  ? 15  MET   C O   1 
ATOM   1559 C CB  . MET   C 1 16 ? 23.302  -37.859 18.675  1.00 41.17  ? 15  MET   C CB  1 
ATOM   1560 C CG  . MET   C 1 16 ? 22.692  -37.071 19.810  1.00 48.10  ? 15  MET   C CG  1 
ATOM   1561 S SD  . MET   C 1 16 ? 21.177  -37.871 20.359  1.00 53.92  ? 15  MET   C SD  1 
ATOM   1562 C CE  . MET   C 1 16 ? 20.158  -37.632 18.896  1.00 60.02  ? 15  MET   C CE  1 
ATOM   1563 N N   . LYS   C 1 17 ? 25.793  -39.299 17.347  1.00 47.70  ? 16  LYS   C N   1 
ATOM   1564 C CA  . LYS   C 1 17 ? 26.224  -40.233 16.313  1.00 51.30  ? 16  LYS   C CA  1 
ATOM   1565 C C   . LYS   C 1 17 ? 25.000  -40.610 15.477  1.00 50.30  ? 16  LYS   C C   1 
ATOM   1566 O O   . LYS   C 1 17 ? 23.985  -41.045 16.015  1.00 43.85  ? 16  LYS   C O   1 
ATOM   1567 C CB  . LYS   C 1 17 ? 26.862  -41.490 16.926  1.00 44.13  ? 16  LYS   C CB  1 
ATOM   1568 C CG  . LYS   C 1 17 ? 27.515  -42.502 15.967  1.00 47.49  ? 16  LYS   C CG  1 
ATOM   1569 C CD  . LYS   C 1 17 ? 28.803  -41.945 15.368  1.00 49.46  ? 16  LYS   C CD  1 
ATOM   1570 C CE  . LYS   C 1 17 ? 29.425  -42.887 14.381  1.00 60.61  ? 16  LYS   C CE  1 
ATOM   1571 N NZ  . LYS   C 1 17 ? 30.685  -42.353 13.855  1.00 58.63  ? 16  LYS   C NZ  1 
ATOM   1572 N N   . GLY   C 1 18 ? 25.100  -40.424 14.159  1.00 48.56  ? 17  GLY   C N   1 
ATOM   1573 C CA  . GLY   C 1 18 ? 24.013  -40.869 13.303  1.00 51.99  ? 17  GLY   C CA  1 
ATOM   1574 C C   . GLY   C 1 18 ? 23.031  -39.745 12.982  1.00 50.73  ? 17  GLY   C C   1 
ATOM   1575 O O   . GLY   C 1 18 ? 22.005  -39.994 12.350  1.00 43.89  ? 17  GLY   C O   1 
ATOM   1576 N N   . TYR   C 1 19 ? 23.346  -38.515 13.425  1.00 47.63  ? 18  TYR   C N   1 
ATOM   1577 C CA  . TYR   C 1 19 ? 22.435  -37.396 13.207  1.00 49.04  ? 18  TYR   C CA  1 
ATOM   1578 C C   . TYR   C 1 19 ? 23.200  -36.107 12.925  1.00 39.95  ? 18  TYR   C C   1 
ATOM   1579 O O   . TYR   C 1 19 ? 24.295  -35.898 13.433  1.00 39.05  ? 18  TYR   C O   1 
ATOM   1580 C CB  . TYR   C 1 19 ? 21.501  -37.109 14.381  1.00 42.56  ? 18  TYR   C CB  1 
ATOM   1581 C CG  . TYR   C 1 19 ? 20.671  -38.304 14.797  1.00 44.85  ? 18  TYR   C CG  1 
ATOM   1582 C CD1 . TYR   C 1 19 ? 21.228  -39.345 15.541  1.00 47.24  ? 18  TYR   C CD1 1 
ATOM   1583 C CD2 . TYR   C 1 19 ? 19.333  -38.390 14.441  1.00 50.47  ? 18  TYR   C CD2 1 
ATOM   1584 C CE1 . TYR   C 1 19 ? 20.473  -40.443 15.921  1.00 44.09  ? 18  TYR   C CE1 1 
ATOM   1585 C CE2 . TYR   C 1 19 ? 18.575  -39.490 14.806  1.00 51.18  ? 18  TYR   C CE2 1 
ATOM   1586 C CZ  . TYR   C 1 19 ? 19.141  -40.508 15.557  1.00 52.53  ? 18  TYR   C CZ  1 
ATOM   1587 O OH  . TYR   C 1 19 ? 18.367  -41.578 15.915  1.00 60.62  ? 18  TYR   C OH  1 
ATOM   1588 N N   . PRO   C 1 20 ? 22.580  -35.193 12.152  1.00 39.19  ? 19  PRO   C N   1 
ATOM   1589 C CA  . PRO   C 1 20 ? 23.172  -33.883 11.872  1.00 41.43  ? 19  PRO   C CA  1 
ATOM   1590 C C   . PRO   C 1 20 ? 23.135  -33.052 13.163  1.00 41.70  ? 19  PRO   C C   1 
ATOM   1591 O O   . PRO   C 1 20 ? 22.363  -33.361 14.091  1.00 40.15  ? 19  PRO   C O   1 
ATOM   1592 C CB  . PRO   C 1 20 ? 22.207  -33.373 10.769  1.00 43.25  ? 19  PRO   C CB  1 
ATOM   1593 C CG  . PRO   C 1 20 ? 20.867  -33.934 11.184  1.00 43.70  ? 19  PRO   C CG  1 
ATOM   1594 C CD  . PRO   C 1 20 ? 21.217  -35.367 11.592  1.00 41.86  ? 19  PRO   C CD  1 
ATOM   1595 N N   . HIS   C 1 21 ? 23.986  -32.018 13.230  1.00 43.96  ? 20  HIS   C N   1 
ATOM   1596 C CA  . HIS   C 1 21 ? 23.977  -31.116 14.379  1.00 46.41  ? 20  HIS   C CA  1 
ATOM   1597 C C   . HIS   C 1 21 ? 22.561  -30.576 14.539  1.00 42.87  ? 20  HIS   C C   1 
ATOM   1598 O O   . HIS   C 1 21 ? 22.021  -29.976 13.604  1.00 42.43  ? 20  HIS   C O   1 
ATOM   1599 C CB  . HIS   C 1 21 ? 24.998  -29.984 14.220  1.00 49.48  ? 20  HIS   C CB  1 
ATOM   1600 C CG  . HIS   C 1 21 ? 26.405  -30.463 14.246  1.00 53.36  ? 20  HIS   C CG  1 
ATOM   1601 N ND1 . HIS   C 1 21 ? 27.015  -31.029 13.146  1.00 54.07  ? 20  HIS   C ND1 1 
ATOM   1602 C CD2 . HIS   C 1 21 ? 27.301  -30.515 15.244  1.00 54.79  ? 20  HIS   C CD2 1 
ATOM   1603 C CE1 . HIS   C 1 21 ? 28.246  -31.398 13.471  1.00 59.35  ? 20  HIS   C CE1 1 
ATOM   1604 N NE2 . HIS   C 1 21 ? 28.443  -31.081 14.735  1.00 59.31  ? 20  HIS   C NE2 1 
ATOM   1605 N N   . TRP   C 1 22 ? 21.968  -30.787 15.727  1.00 42.46  ? 21  TRP   C N   1 
ATOM   1606 C CA  . TRP   C 1 22 ? 20.524  -30.633 15.842  1.00 39.15  ? 21  TRP   C CA  1 
ATOM   1607 C C   . TRP   C 1 22 ? 20.170  -29.447 16.751  1.00 43.16  ? 21  TRP   C C   1 
ATOM   1608 O O   . TRP   C 1 22 ? 20.725  -29.313 17.842  1.00 40.30  ? 21  TRP   C O   1 
ATOM   1609 C CB  . TRP   C 1 22 ? 19.940  -31.934 16.408  1.00 39.80  ? 21  TRP   C CB  1 
ATOM   1610 C CG  . TRP   C 1 22 ? 18.509  -32.152 16.015  1.00 36.44  ? 21  TRP   C CG  1 
ATOM   1611 C CD1 . TRP   C 1 22 ? 17.405  -31.573 16.566  1.00 38.08  ? 21  TRP   C CD1 1 
ATOM   1612 C CD2 . TRP   C 1 22 ? 18.039  -33.037 14.970  1.00 34.16  ? 21  TRP   C CD2 1 
ATOM   1613 N NE1 . TRP   C 1 22 ? 16.279  -32.002 15.899  1.00 39.45  ? 21  TRP   C NE1 1 
ATOM   1614 C CE2 . TRP   C 1 22 ? 16.634  -32.917 14.935  1.00 34.61  ? 21  TRP   C CE2 1 
ATOM   1615 C CE3 . TRP   C 1 22 ? 18.659  -33.911 14.074  1.00 35.23  ? 21  TRP   C CE3 1 
ATOM   1616 C CZ2 . TRP   C 1 22 ? 15.849  -33.641 14.042  1.00 35.26  ? 21  TRP   C CZ2 1 
ATOM   1617 C CZ3 . TRP   C 1 22 ? 17.882  -34.626 13.180  1.00 42.38  ? 21  TRP   C CZ3 1 
ATOM   1618 C CH2 . TRP   C 1 22 ? 16.492  -34.496 13.174  1.00 37.93  ? 21  TRP   C CH2 1 
ATOM   1619 N N   . PRO   C 1 23 ? 19.211  -28.566 16.384  1.00 40.15  ? 22  PRO   C N   1 
ATOM   1620 C CA  . PRO   C 1 23 ? 18.830  -27.464 17.275  1.00 41.80  ? 22  PRO   C CA  1 
ATOM   1621 C C   . PRO   C 1 23 ? 18.215  -28.026 18.554  1.00 43.92  ? 22  PRO   C C   1 
ATOM   1622 O O   . PRO   C 1 23 ? 17.344  -28.889 18.503  1.00 40.70  ? 22  PRO   C O   1 
ATOM   1623 C CB  . PRO   C 1 23 ? 17.791  -26.711 16.441  1.00 41.71  ? 22  PRO   C CB  1 
ATOM   1624 C CG  . PRO   C 1 23 ? 17.170  -27.772 15.545  1.00 37.68  ? 22  PRO   C CG  1 
ATOM   1625 C CD  . PRO   C 1 23 ? 18.388  -28.609 15.151  1.00 39.72  ? 22  PRO   C CD  1 
ATOM   1626 N N   . ALA   C 1 24 ? 18.680  -27.542 19.714  1.00 44.17  ? 23  ALA   C N   1 
ATOM   1627 C CA  . ALA   C 1 24 ? 18.269  -28.146 20.972  1.00 47.17  ? 23  ALA   C CA  1 
ATOM   1628 C C   . ALA   C 1 24 ? 18.424  -27.119 22.091  1.00 49.03  ? 23  ALA   C C   1 
ATOM   1629 O O   . ALA   C 1 24 ? 18.938  -26.016 21.856  1.00 49.11  ? 23  ALA   C O   1 
ATOM   1630 C CB  . ALA   C 1 24 ? 19.127  -29.382 21.241  1.00 43.40  ? 23  ALA   C CB  1 
ATOM   1631 N N   . ARG   C 1 25 ? 18.031  -27.513 23.310  1.00 51.24  ? 24  ARG   C N   1 
ATOM   1632 C CA  . ARG   C 1 25 ? 18.299  -26.683 24.482  1.00 54.11  ? 24  ARG   C CA  1 
ATOM   1633 C C   . ARG   C 1 25 ? 18.759  -27.531 25.675  1.00 49.26  ? 24  ARG   C C   1 
ATOM   1634 O O   . ARG   C 1 25 ? 18.461  -28.724 25.733  1.00 50.09  ? 24  ARG   C O   1 
ATOM   1635 C CB  . ARG   C 1 25 ? 17.051  -25.874 24.842  1.00 47.45  ? 24  ARG   C CB  1 
ATOM   1636 C CG  . ARG   C 1 25 ? 15.869  -26.661 25.383  1.00 52.40  ? 24  ARG   C CG  1 
ATOM   1637 C CD  . ARG   C 1 25 ? 14.842  -25.739 26.044  1.00 61.60  ? 24  ARG   C CD  1 
ATOM   1638 N NE  . ARG   C 1 25 ? 13.620  -26.489 26.365  1.00 69.92  ? 24  ARG   C NE  1 
ATOM   1639 C CZ  . ARG   C 1 25 ? 12.382  -26.201 25.972  1.00 69.47  ? 24  ARG   C CZ  1 
ATOM   1640 N NH1 . ARG   C 1 25 ? 12.118  -25.098 25.286  1.00 67.04  ? 24  ARG   C NH1 1 
ATOM   1641 N NH2 . ARG   C 1 25 ? 11.402  -27.027 26.284  1.00 71.73  ? 24  ARG   C NH2 1 
ATOM   1642 N N   . ILE   C 1 26 ? 19.473  -26.900 26.626  1.00 52.65  ? 25  ILE   C N   1 
ATOM   1643 C CA  . ILE   C 1 26 ? 19.791  -27.524 27.911  1.00 59.17  ? 25  ILE   C CA  1 
ATOM   1644 C C   . ILE   C 1 26 ? 18.524  -27.608 28.763  1.00 61.09  ? 25  ILE   C C   1 
ATOM   1645 O O   . ILE   C 1 26 ? 17.791  -26.632 28.894  1.00 70.32  ? 25  ILE   C O   1 
ATOM   1646 C CB  . ILE   C 1 26 ? 20.897  -26.757 28.666  1.00 57.63  ? 25  ILE   C CB  1 
ATOM   1647 C CG1 . ILE   C 1 26 ? 22.065  -26.337 27.774  1.00 51.31  ? 25  ILE   C CG1 1 
ATOM   1648 C CG2 . ILE   C 1 26 ? 21.372  -27.541 29.895  1.00 60.60  ? 25  ILE   C CG2 1 
ATOM   1649 C CD1 . ILE   C 1 26 ? 22.883  -27.487 27.214  1.00 49.05  ? 25  ILE   C CD1 1 
ATOM   1650 N N   . ASP   C 1 27 ? 18.267  -28.785 29.341  1.00 70.59  ? 26  ASP   C N   1 
ATOM   1651 C CA  . ASP   C 1 27 ? 17.181  -28.954 30.298  1.00 79.07  ? 26  ASP   C CA  1 
ATOM   1652 C C   . ASP   C 1 27 ? 17.722  -28.822 31.723  1.00 77.82  ? 26  ASP   C C   1 
ATOM   1653 O O   . ASP   C 1 27 ? 18.922  -28.979 31.939  1.00 79.70  ? 26  ASP   C O   1 
ATOM   1654 C CB  . ASP   C 1 27 ? 16.452  -30.275 30.096  1.00 81.59  ? 26  ASP   C CB  1 
ATOM   1655 C CG  . ASP   C 1 27 ? 15.152  -30.212 29.304  1.00 89.82  ? 26  ASP   C CG  1 
ATOM   1656 O OD1 . ASP   C 1 27 ? 14.930  -29.184 28.616  1.00 88.36  ? 26  ASP   C OD1 1 
ATOM   1657 O OD2 . ASP   C 1 27 ? 14.350  -31.177 29.423  1.00 74.80  ? 26  ASP   C OD2 1 
ATOM   1658 N N   . ASP   C 1 28 ? 16.834  -28.510 32.683  1.00 82.25  ? 27  ASP   C N   1 
ATOM   1659 C CA  . ASP   C 1 28 ? 17.146  -28.640 34.102  1.00 84.61  ? 27  ASP   C CA  1 
ATOM   1660 C C   . ASP   C 1 28 ? 16.831  -30.078 34.496  1.00 88.17  ? 27  ASP   C C   1 
ATOM   1661 O O   . ASP   C 1 28 ? 16.028  -30.726 33.832  1.00 84.74  ? 27  ASP   C O   1 
ATOM   1662 C CB  . ASP   C 1 28 ? 16.447  -27.595 34.962  1.00 78.85  ? 27  ASP   C CB  1 
ATOM   1663 N N   . ILE   C 1 29 ? 17.482  -30.575 35.555  1.00 92.60  ? 28  ILE   C N   1 
ATOM   1664 C CA  . ILE   C 1 29 ? 17.413  -31.990 35.882  1.00 83.96  ? 28  ILE   C CA  1 
ATOM   1665 C C   . ILE   C 1 29 ? 16.328  -32.207 36.948  1.00 83.53  ? 28  ILE   C C   1 
ATOM   1666 O O   . ILE   C 1 29 ? 16.360  -31.466 37.949  1.00 85.24  ? 28  ILE   C O   1 
ATOM   1667 C CB  . ILE   C 1 29 ? 18.788  -32.534 36.318  1.00 75.72  ? 28  ILE   C CB  1 
ATOM   1668 N N   . GLY   C 1 32 ? 15.787  -35.357 41.358  1.00 103.48 ? 31  GLY   C N   1 
ATOM   1669 C CA  . GLY   C 1 32 ? 16.332  -36.680 40.985  1.00 102.87 ? 31  GLY   C CA  1 
ATOM   1670 C C   . GLY   C 1 32 ? 15.222  -37.682 40.713  1.00 89.37  ? 31  GLY   C C   1 
ATOM   1671 O O   . GLY   C 1 32 ? 14.738  -38.280 41.705  1.00 78.34  ? 31  GLY   C O   1 
ATOM   1672 N N   . LYS   C 1 35 ? 19.778  -39.426 37.960  1.00 80.26  ? 34  LYS   C N   1 
ATOM   1673 C CA  . LYS   C 1 35 ? 20.881  -38.436 37.809  1.00 78.14  ? 34  LYS   C CA  1 
ATOM   1674 C C   . LYS   C 1 35 ? 21.597  -38.699 36.485  1.00 72.50  ? 34  LYS   C C   1 
ATOM   1675 O O   . LYS   C 1 35 ? 21.763  -39.853 36.084  1.00 62.31  ? 34  LYS   C O   1 
ATOM   1676 C CB  . LYS   C 1 35 ? 21.854  -38.489 38.997  1.00 76.22  ? 34  LYS   C CB  1 
ATOM   1677 N N   . PRO   C 1 36 ? 22.062  -37.649 35.769  1.00 71.02  ? 35  PRO   C N   1 
ATOM   1678 C CA  . PRO   C 1 36 ? 22.770  -37.854 34.503  1.00 75.39  ? 35  PRO   C CA  1 
ATOM   1679 C C   . PRO   C 1 36 ? 23.969  -38.791 34.675  1.00 77.94  ? 35  PRO   C C   1 
ATOM   1680 O O   . PRO   C 1 36 ? 24.480  -38.975 35.784  1.00 72.92  ? 35  PRO   C O   1 
ATOM   1681 C CB  . PRO   C 1 36 ? 23.201  -36.427 34.076  1.00 75.26  ? 35  PRO   C CB  1 
ATOM   1682 C CG  . PRO   C 1 36 ? 22.272  -35.501 34.843  1.00 75.88  ? 35  PRO   C CG  1 
ATOM   1683 C CD  . PRO   C 1 36 ? 21.960  -36.227 36.151  1.00 77.45  ? 35  PRO   C CD  1 
ATOM   1684 N N   . PRO   C 1 37 ? 24.460  -39.437 33.596  1.00 72.72  ? 36  PRO   C N   1 
ATOM   1685 C CA  . PRO   C 1 37 ? 25.838  -39.930 33.601  1.00 70.78  ? 36  PRO   C CA  1 
ATOM   1686 C C   . PRO   C 1 37 ? 26.776  -38.787 34.001  1.00 67.40  ? 36  PRO   C C   1 
ATOM   1687 O O   . PRO   C 1 37 ? 26.445  -37.615 33.811  1.00 63.44  ? 36  PRO   C O   1 
ATOM   1688 C CB  . PRO   C 1 37 ? 26.020  -40.408 32.153  1.00 67.89  ? 36  PRO   C CB  1 
ATOM   1689 C CG  . PRO   C 1 37 ? 24.622  -40.840 31.763  1.00 70.66  ? 36  PRO   C CG  1 
ATOM   1690 C CD  . PRO   C 1 37 ? 23.719  -39.773 32.366  1.00 71.00  ? 36  PRO   C CD  1 
ATOM   1691 N N   . PRO   C 1 38 ? 27.950  -39.084 34.611  1.00 63.57  ? 37  PRO   C N   1 
ATOM   1692 C CA  . PRO   C 1 38 ? 28.895  -38.039 35.009  1.00 60.04  ? 37  PRO   C CA  1 
ATOM   1693 C C   . PRO   C 1 38 ? 29.262  -37.139 33.835  1.00 53.08  ? 37  PRO   C C   1 
ATOM   1694 O O   . PRO   C 1 38 ? 29.525  -37.622 32.730  1.00 53.86  ? 37  PRO   C O   1 
ATOM   1695 C CB  . PRO   C 1 38 ? 30.112  -38.849 35.498  1.00 62.75  ? 37  PRO   C CB  1 
ATOM   1696 C CG  . PRO   C 1 38 ? 29.516  -40.163 35.947  1.00 64.07  ? 37  PRO   C CG  1 
ATOM   1697 C CD  . PRO   C 1 38 ? 28.424  -40.440 34.938  1.00 63.14  ? 37  PRO   C CD  1 
ATOM   1698 N N   . ASN   C 1 39 ? 29.269  -35.826 34.096  1.00 55.28  ? 38  ASN   C N   1 
ATOM   1699 C CA  . ASN   C 1 39 ? 29.729  -34.830 33.145  1.00 53.32  ? 38  ASN   C CA  1 
ATOM   1700 C C   . ASN   C 1 39 ? 28.808  -34.767 31.920  1.00 54.82  ? 38  ASN   C C   1 
ATOM   1701 O O   . ASN   C 1 39 ? 29.274  -34.353 30.855  1.00 52.11  ? 38  ASN   C O   1 
ATOM   1702 C CB  . ASN   C 1 39 ? 31.177  -35.088 32.724  1.00 62.50  ? 38  ASN   C CB  1 
ATOM   1703 C CG  . ASN   C 1 39 ? 31.866  -33.865 32.154  1.00 76.96  ? 38  ASN   C CG  1 
ATOM   1704 O OD1 . ASN   C 1 39 ? 31.772  -32.775 32.727  1.00 86.57  ? 38  ASN   C OD1 1 
ATOM   1705 N ND2 . ASN   C 1 39 ? 32.564  -34.009 31.036  1.00 75.86  ? 38  ASN   C ND2 1 
ATOM   1706 N N   . LYS   C 1 40 ? 27.521  -35.152 32.065  1.00 49.51  ? 39  LYS   C N   1 
ATOM   1707 C CA  . LYS   C 1 40 ? 26.561  -35.089 30.957  1.00 47.10  ? 39  LYS   C CA  1 
ATOM   1708 C C   . LYS   C 1 40 ? 25.438  -34.098 31.257  1.00 52.58  ? 39  LYS   C C   1 
ATOM   1709 O O   . LYS   C 1 40 ? 24.977  -34.011 32.391  1.00 52.30  ? 39  LYS   C O   1 
ATOM   1710 C CB  . LYS   C 1 40 ? 25.862  -36.427 30.677  1.00 45.61  ? 39  LYS   C CB  1 
ATOM   1711 C CG  . LYS   C 1 40 ? 26.735  -37.579 30.236  1.00 45.98  ? 39  LYS   C CG  1 
ATOM   1712 C CD  . LYS   C 1 40 ? 27.427  -37.429 28.889  1.00 52.65  ? 39  LYS   C CD  1 
ATOM   1713 C CE  . LYS   C 1 40 ? 28.226  -38.646 28.534  1.00 58.18  ? 39  LYS   C CE  1 
ATOM   1714 N NZ  . LYS   C 1 40 ? 29.438  -38.282 27.789  1.00 62.06  ? 39  LYS   C NZ  1 
ATOM   1715 N N   . TYR   C 1 41 ? 24.972  -33.398 30.211  1.00 48.15  ? 40  TYR   C N   1 
ATOM   1716 C CA  . TYR   C 1 41 ? 23.885  -32.429 30.296  1.00 49.24  ? 40  TYR   C CA  1 
ATOM   1717 C C   . TYR   C 1 41 ? 22.594  -33.048 29.759  1.00 52.45  ? 40  TYR   C C   1 
ATOM   1718 O O   . TYR   C 1 41 ? 22.639  -33.769 28.759  1.00 45.48  ? 40  TYR   C O   1 
ATOM   1719 C CB  . TYR   C 1 41 ? 24.154  -31.179 29.442  1.00 47.10  ? 40  TYR   C CB  1 
ATOM   1720 C CG  . TYR   C 1 41 ? 25.326  -30.297 29.853  1.00 56.19  ? 40  TYR   C CG  1 
ATOM   1721 C CD1 . TYR   C 1 41 ? 26.598  -30.475 29.304  1.00 46.70  ? 40  TYR   C CD1 1 
ATOM   1722 C CD2 . TYR   C 1 41 ? 25.157  -29.270 30.787  1.00 60.42  ? 40  TYR   C CD2 1 
ATOM   1723 C CE1 . TYR   C 1 41 ? 27.663  -29.679 29.707  1.00 58.48  ? 40  TYR   C CE1 1 
ATOM   1724 C CE2 . TYR   C 1 41 ? 26.215  -28.461 31.182  1.00 63.55  ? 40  TYR   C CE2 1 
ATOM   1725 C CZ  . TYR   C 1 41 ? 27.471  -28.671 30.645  1.00 60.28  ? 40  TYR   C CZ  1 
ATOM   1726 O OH  . TYR   C 1 41 ? 28.516  -27.887 31.037  1.00 65.67  ? 40  TYR   C OH  1 
ATOM   1727 N N   . PRO   C 1 42 ? 21.409  -32.754 30.365  1.00 48.50  ? 41  PRO   C N   1 
ATOM   1728 C CA  . PRO   C 1 42 ? 20.124  -33.189 29.807  1.00 49.71  ? 41  PRO   C CA  1 
ATOM   1729 C C   . PRO   C 1 42 ? 19.810  -32.265 28.631  1.00 51.65  ? 41  PRO   C C   1 
ATOM   1730 O O   . PRO   C 1 42 ? 19.796  -31.045 28.799  1.00 47.15  ? 41  PRO   C O   1 
ATOM   1731 C CB  . PRO   C 1 42 ? 19.093  -33.046 30.958  1.00 48.50  ? 41  PRO   C CB  1 
ATOM   1732 C CG  . PRO   C 1 42 ? 19.810  -32.203 32.011  1.00 53.50  ? 41  PRO   C CG  1 
ATOM   1733 C CD  . PRO   C 1 42 ? 21.238  -31.917 31.569  1.00 46.59  ? 41  PRO   C CD  1 
ATOM   1734 N N   . ILE   C 1 43 ? 19.605  -32.864 27.447  1.00 48.65  ? 42  ILE   C N   1 
ATOM   1735 C CA  . ILE   C 1 43 ? 19.272  -32.137 26.225  1.00 44.53  ? 42  ILE   C CA  1 
ATOM   1736 C C   . ILE   C 1 43 ? 17.816  -32.422 25.856  1.00 45.59  ? 42  ILE   C C   1 
ATOM   1737 O O   . ILE   C 1 43 ? 17.327  -33.551 25.997  1.00 50.70  ? 42  ILE   C O   1 
ATOM   1738 C CB  . ILE   C 1 43 ? 20.237  -32.513 25.076  1.00 44.35  ? 42  ILE   C CB  1 
ATOM   1739 C CG1 . ILE   C 1 43 ? 21.704  -32.333 25.499  1.00 42.47  ? 42  ILE   C CG1 1 
ATOM   1740 C CG2 . ILE   C 1 43 ? 19.947  -31.724 23.786  1.00 44.77  ? 42  ILE   C CG2 1 
ATOM   1741 C CD1 . ILE   C 1 43 ? 22.065  -30.921 25.940  1.00 39.65  ? 42  ILE   C CD1 1 
ATOM   1742 N N   . PHE   C 1 44 ? 17.127  -31.373 25.385  1.00 47.12  ? 43  PHE   C N   1 
ATOM   1743 C CA  . PHE   C 1 44 ? 15.833  -31.491 24.728  1.00 45.15  ? 43  PHE   C CA  1 
ATOM   1744 C C   . PHE   C 1 44 ? 16.016  -31.047 23.273  1.00 47.20  ? 43  PHE   C C   1 
ATOM   1745 O O   . PHE   C 1 44 ? 16.610  -30.004 23.022  1.00 47.03  ? 43  PHE   C O   1 
ATOM   1746 C CB  . PHE   C 1 44 ? 14.828  -30.632 25.495  1.00 42.16  ? 43  PHE   C CB  1 
ATOM   1747 C CG  . PHE   C 1 44 ? 13.487  -30.452 24.800  1.00 50.43  ? 43  PHE   C CG  1 
ATOM   1748 C CD1 . PHE   C 1 44 ? 12.487  -31.410 24.937  1.00 48.76  ? 43  PHE   C CD1 1 
ATOM   1749 C CD2 . PHE   C 1 44 ? 13.228  -29.319 24.025  1.00 56.51  ? 43  PHE   C CD2 1 
ATOM   1750 C CE1 . PHE   C 1 44 ? 11.264  -31.250 24.293  1.00 54.24  ? 43  PHE   C CE1 1 
ATOM   1751 C CE2 . PHE   C 1 44 ? 12.001  -29.159 23.389  1.00 52.37  ? 43  PHE   C CE2 1 
ATOM   1752 C CZ  . PHE   C 1 44 ? 11.024  -30.124 23.532  1.00 53.21  ? 43  PHE   C CZ  1 
ATOM   1753 N N   . PHE   C 1 45 ? 15.574  -31.887 22.332  1.00 46.09  ? 44  PHE   C N   1 
ATOM   1754 C CA  . PHE   C 1 45 ? 15.816  -31.648 20.915  1.00 46.13  ? 44  PHE   C CA  1 
ATOM   1755 C C   . PHE   C 1 45 ? 14.554  -31.000 20.359  1.00 45.52  ? 44  PHE   C C   1 
ATOM   1756 O O   . PHE   C 1 45 ? 13.471  -31.555 20.538  1.00 46.68  ? 44  PHE   C O   1 
ATOM   1757 C CB  . PHE   C 1 45 ? 16.149  -32.946 20.164  1.00 40.42  ? 44  PHE   C CB  1 
ATOM   1758 C CG  . PHE   C 1 45 ? 17.494  -33.554 20.522  1.00 42.93  ? 44  PHE   C CG  1 
ATOM   1759 C CD1 . PHE   C 1 45 ? 18.645  -33.212 19.806  1.00 41.46  ? 44  PHE   C CD1 1 
ATOM   1760 C CD2 . PHE   C 1 45 ? 17.607  -34.470 21.574  1.00 41.80  ? 44  PHE   C CD2 1 
ATOM   1761 C CE1 . PHE   C 1 45 ? 19.887  -33.766 20.140  1.00 39.40  ? 44  PHE   C CE1 1 
ATOM   1762 C CE2 . PHE   C 1 45 ? 18.847  -35.014 21.913  1.00 44.16  ? 44  PHE   C CE2 1 
ATOM   1763 C CZ  . PHE   C 1 45 ? 19.980  -34.653 21.197  1.00 40.03  ? 44  PHE   C CZ  1 
ATOM   1764 N N   . PHE   C 1 46 ? 14.695  -29.817 19.735  1.00 44.84  ? 45  PHE   C N   1 
ATOM   1765 C CA  . PHE   C 1 46 ? 13.539  -29.191 19.105  1.00 40.70  ? 45  PHE   C CA  1 
ATOM   1766 C C   . PHE   C 1 46 ? 13.071  -30.045 17.930  1.00 43.90  ? 45  PHE   C C   1 
ATOM   1767 O O   . PHE   C 1 46 ? 13.863  -30.777 17.315  1.00 41.18  ? 45  PHE   C O   1 
ATOM   1768 C CB  . PHE   C 1 46 ? 13.759  -27.738 18.661  1.00 43.56  ? 45  PHE   C CB  1 
ATOM   1769 C CG  . PHE   C 1 46 ? 14.071  -26.754 19.783  1.00 49.07  ? 45  PHE   C CG  1 
ATOM   1770 C CD1 . PHE   C 1 46 ? 13.063  -26.267 20.602  1.00 51.16  ? 45  PHE   C CD1 1 
ATOM   1771 C CD2 . PHE   C 1 46 ? 15.370  -26.298 19.998  1.00 46.56  ? 45  PHE   C CD2 1 
ATOM   1772 C CE1 . PHE   C 1 46 ? 13.349  -25.367 21.622  1.00 47.84  ? 45  PHE   C CE1 1 
ATOM   1773 C CE2 . PHE   C 1 46 ? 15.648  -25.406 21.024  1.00 50.84  ? 45  PHE   C CE2 1 
ATOM   1774 C CZ  . PHE   C 1 46 ? 14.634  -24.934 21.828  1.00 45.36  ? 45  PHE   C CZ  1 
ATOM   1775 N N   . GLY   C 1 47 ? 11.791  -29.873 17.576  1.00 42.69  ? 46  GLY   C N   1 
ATOM   1776 C CA  . GLY   C 1 47 ? 11.240  -30.599 16.449  1.00 41.39  ? 46  GLY   C CA  1 
ATOM   1777 C C   . GLY   C 1 47 ? 10.767  -31.979 16.883  1.00 51.37  ? 46  GLY   C C   1 
ATOM   1778 O O   . GLY   C 1 47 ? 9.569   -32.234 16.878  1.00 48.65  ? 46  GLY   C O   1 
ATOM   1779 N N   . THR   C 1 48 ? 11.714  -32.843 17.288  1.00 50.64  ? 47  THR   C N   1 
ATOM   1780 C CA  . THR   C 1 48 ? 11.371  -34.206 17.667  1.00 48.82  ? 47  THR   C CA  1 
ATOM   1781 C C   . THR   C 1 48 ? 10.775  -34.220 19.066  1.00 45.13  ? 47  THR   C C   1 
ATOM   1782 O O   . THR   C 1 48 ? 9.910   -35.045 19.332  1.00 52.81  ? 47  THR   C O   1 
ATOM   1783 C CB  . THR   C 1 48 ? 12.545  -35.177 17.535  1.00 44.81  ? 47  THR   C CB  1 
ATOM   1784 O OG1 . THR   C 1 48 ? 13.498  -34.721 18.491  1.00 45.74  ? 47  THR   C OG1 1 
ATOM   1785 C CG2 . THR   C 1 48 ? 13.100  -35.207 16.126  1.00 42.95  ? 47  THR   C CG2 1 
ATOM   1786 N N   . HIS   C 1 49 ? 11.234  -33.299 19.927  1.00 47.34  ? 48  HIS   C N   1 
ATOM   1787 C CA  . HIS   C 1 49 ? 10.808  -33.175 21.320  1.00 54.68  ? 48  HIS   C CA  1 
ATOM   1788 C C   . HIS   C 1 49 ? 11.349  -34.336 22.164  1.00 54.42  ? 48  HIS   C C   1 
ATOM   1789 O O   . HIS   C 1 49 ? 10.793  -34.669 23.205  1.00 56.75  ? 48  HIS   C O   1 
ATOM   1790 C CB  . HIS   C 1 49 ? 9.291   -32.932 21.434  1.00 50.82  ? 48  HIS   C CB  1 
ATOM   1791 C CG  . HIS   C 1 49 ? 8.786   -31.795 20.598  1.00 59.66  ? 48  HIS   C CG  1 
ATOM   1792 N ND1 . HIS   C 1 49 ? 7.691   -31.901 19.766  1.00 64.63  ? 48  HIS   C ND1 1 
ATOM   1793 C CD2 . HIS   C 1 49 ? 9.249   -30.544 20.435  1.00 61.31  ? 48  HIS   C CD2 1 
ATOM   1794 C CE1 . HIS   C 1 49 ? 7.503   -30.747 19.137  1.00 68.20  ? 48  HIS   C CE1 1 
ATOM   1795 N NE2 . HIS   C 1 49 ? 8.433   -29.907 19.533  1.00 64.41  ? 48  HIS   C NE2 1 
ATOM   1796 N N   . GLU   C 1 50 ? 12.445  -34.955 21.718  1.00 50.76  ? 49  GLU   C N   1 
ATOM   1797 C CA  . GLU   C 1 50 ? 13.043  -36.051 22.465  1.00 52.40  ? 49  GLU   C CA  1 
ATOM   1798 C C   . GLU   C 1 50 ? 14.086  -35.497 23.440  1.00 49.32  ? 49  GLU   C C   1 
ATOM   1799 O O   . GLU   C 1 50 ? 14.401  -34.309 23.420  1.00 49.69  ? 49  GLU   C O   1 
ATOM   1800 C CB  . GLU   C 1 50 ? 13.585  -37.074 21.467  1.00 60.66  ? 49  GLU   C CB  1 
ATOM   1801 C CG  . GLU   C 1 50 ? 12.488  -37.753 20.652  1.00 61.70  ? 49  GLU   C CG  1 
ATOM   1802 C CD  . GLU   C 1 50 ? 13.049  -38.609 19.531  1.00 71.34  ? 49  GLU   C CD  1 
ATOM   1803 O OE1 . GLU   C 1 50 ? 14.292  -38.690 19.395  1.00 78.82  ? 49  GLU   C OE1 1 
ATOM   1804 O OE2 . GLU   C 1 50 ? 12.238  -39.188 18.778  1.00 74.79  ? 49  GLU   C OE2 1 
ATOM   1805 N N   . THR   C 1 51 ? 14.559  -36.341 24.367  1.00 59.00  ? 50  THR   C N   1 
ATOM   1806 C CA  . THR   C 1 51 ? 15.622  -35.940 25.284  1.00 53.14  ? 50  THR   C CA  1 
ATOM   1807 C C   . THR   C 1 51 ? 16.756  -36.958 25.204  1.00 47.37  ? 50  THR   C C   1 
ATOM   1808 O O   . THR   C 1 51 ? 16.560  -38.064 24.706  1.00 51.40  ? 50  THR   C O   1 
ATOM   1809 C CB  . THR   C 1 51 ? 15.137  -35.783 26.728  1.00 57.03  ? 50  THR   C CB  1 
ATOM   1810 O OG1 . THR   C 1 51 ? 14.513  -37.019 27.069  1.00 61.20  ? 50  THR   C OG1 1 
ATOM   1811 C CG2 . THR   C 1 51 ? 14.231  -34.586 26.948  1.00 57.81  ? 50  THR   C CG2 1 
ATOM   1812 N N   . ALA   C 1 52 ? 17.934  -36.540 25.683  1.00 46.65  ? 51  ALA   C N   1 
ATOM   1813 C CA  . ALA   C 1 52 ? 19.130  -37.364 25.788  1.00 49.21  ? 51  ALA   C CA  1 
ATOM   1814 C C   . ALA   C 1 52 ? 20.147  -36.641 26.663  1.00 52.79  ? 51  ALA   C C   1 
ATOM   1815 O O   . ALA   C 1 52 ? 20.009  -35.448 26.925  1.00 50.64  ? 51  ALA   C O   1 
ATOM   1816 C CB  . ALA   C 1 52 ? 19.725  -37.647 24.418  1.00 53.46  ? 51  ALA   C CB  1 
ATOM   1817 N N   . PHE   C 1 53 ? 21.162  -37.390 27.111  1.00 53.07  ? 52  PHE   C N   1 
ATOM   1818 C CA  . PHE   C 1 53 ? 22.302  -36.833 27.820  1.00 51.17  ? 52  PHE   C CA  1 
ATOM   1819 C C   . PHE   C 1 53 ? 23.469  -36.741 26.859  1.00 47.11  ? 52  PHE   C C   1 
ATOM   1820 O O   . PHE   C 1 53 ? 23.766  -37.717 26.169  1.00 53.33  ? 52  PHE   C O   1 
ATOM   1821 C CB  . PHE   C 1 53 ? 22.709  -37.773 28.953  1.00 50.70  ? 52  PHE   C CB  1 
ATOM   1822 C CG  . PHE   C 1 53 ? 21.649  -37.733 30.041  1.00 58.73  ? 52  PHE   C CG  1 
ATOM   1823 C CD1 . PHE   C 1 53 ? 21.469  -36.588 30.813  1.00 52.66  ? 52  PHE   C CD1 1 
ATOM   1824 C CD2 . PHE   C 1 53 ? 20.819  -38.827 30.267  1.00 65.73  ? 52  PHE   C CD2 1 
ATOM   1825 C CE1 . PHE   C 1 53 ? 20.496  -36.552 31.799  1.00 60.36  ? 52  PHE   C CE1 1 
ATOM   1826 C CE2 . PHE   C 1 53 ? 19.848  -38.783 31.258  1.00 62.55  ? 52  PHE   C CE2 1 
ATOM   1827 C CZ  . PHE   C 1 53 ? 19.693  -37.649 32.022  1.00 56.33  ? 52  PHE   C CZ  1 
ATOM   1828 N N   . LEU   C 1 54 ? 24.105  -35.564 26.816  1.00 43.62  ? 53  LEU   C N   1 
ATOM   1829 C CA  . LEU   C 1 54 ? 25.262  -35.372 25.953  1.00 44.40  ? 53  LEU   C CA  1 
ATOM   1830 C C   . LEU   C 1 54 ? 26.382  -34.683 26.727  1.00 44.88  ? 53  LEU   C C   1 
ATOM   1831 O O   . LEU   C 1 54 ? 26.121  -33.906 27.639  1.00 48.03  ? 53  LEU   C O   1 
ATOM   1832 C CB  . LEU   C 1 54 ? 24.864  -34.568 24.717  1.00 47.13  ? 53  LEU   C CB  1 
ATOM   1833 C CG  . LEU   C 1 54 ? 24.049  -35.321 23.659  1.00 48.36  ? 53  LEU   C CG  1 
ATOM   1834 C CD1 . LEU   C 1 54 ? 23.741  -34.332 22.576  1.00 45.21  ? 53  LEU   C CD1 1 
ATOM   1835 C CD2 . LEU   C 1 54 ? 24.780  -36.526 23.070  1.00 53.37  ? 53  LEU   C CD2 1 
ATOM   1836 N N   . GLY   C 1 55 ? 27.628  -34.960 26.329  1.00 50.57  ? 54  GLY   C N   1 
ATOM   1837 C CA  . GLY   C 1 55 ? 28.782  -34.303 26.926  1.00 49.23  ? 54  GLY   C CA  1 
ATOM   1838 C C   . GLY   C 1 55 ? 29.041  -32.972 26.225  1.00 54.71  ? 54  GLY   C C   1 
ATOM   1839 O O   . GLY   C 1 55 ? 28.499  -32.734 25.138  1.00 52.29  ? 54  GLY   C O   1 
ATOM   1840 N N   . PRO   C 1 56 ? 29.854  -32.066 26.819  1.00 56.80  ? 55  PRO   C N   1 
ATOM   1841 C CA  . PRO   C 1 56 ? 30.053  -30.725 26.267  1.00 62.04  ? 55  PRO   C CA  1 
ATOM   1842 C C   . PRO   C 1 56 ? 30.714  -30.675 24.896  1.00 55.70  ? 55  PRO   C C   1 
ATOM   1843 O O   . PRO   C 1 56 ? 30.504  -29.717 24.158  1.00 68.89  ? 55  PRO   C O   1 
ATOM   1844 C CB  . PRO   C 1 56 ? 30.849  -29.947 27.347  1.00 62.61  ? 55  PRO   C CB  1 
ATOM   1845 C CG  . PRO   C 1 56 ? 31.489  -31.034 28.182  1.00 57.77  ? 55  PRO   C CG  1 
ATOM   1846 C CD  . PRO   C 1 56 ? 30.590  -32.259 28.079  1.00 60.91  ? 55  PRO   C CD  1 
ATOM   1847 N N   . LYS   C 1 57 ? 31.479  -31.719 24.550  1.00 56.49  ? 56  LYS   C N   1 
ATOM   1848 C CA  . LYS   C 1 57 ? 32.111  -31.779 23.237  1.00 61.56  ? 56  LYS   C CA  1 
ATOM   1849 C C   . LYS   C 1 57 ? 31.050  -31.943 22.145  1.00 66.20  ? 56  LYS   C C   1 
ATOM   1850 O O   . LYS   C 1 57 ? 31.354  -31.805 20.960  1.00 58.33  ? 56  LYS   C O   1 
ATOM   1851 C CB  . LYS   C 1 57 ? 33.123  -32.924 23.100  1.00 58.83  ? 56  LYS   C CB  1 
ATOM   1852 N N   . ASP   C 1 58 ? 29.809  -32.251 22.541  1.00 58.56  ? 57  ASP   C N   1 
ATOM   1853 C CA  . ASP   C 1 58 ? 28.793  -32.557 21.546  1.00 63.14  ? 57  ASP   C CA  1 
ATOM   1854 C C   . ASP   C 1 58 ? 27.890  -31.349 21.346  1.00 54.45  ? 57  ASP   C C   1 
ATOM   1855 O O   . ASP   C 1 58 ? 26.906  -31.436 20.610  1.00 60.05  ? 57  ASP   C O   1 
ATOM   1856 C CB  . ASP   C 1 58 ? 27.959  -33.777 21.911  1.00 59.20  ? 57  ASP   C CB  1 
ATOM   1857 C CG  . ASP   C 1 58 ? 28.729  -35.078 22.088  1.00 58.31  ? 57  ASP   C CG  1 
ATOM   1858 O OD1 . ASP   C 1 58 ? 29.638  -35.340 21.273  1.00 58.03  ? 57  ASP   C OD1 1 
ATOM   1859 O OD2 . ASP   C 1 58 ? 28.388  -35.828 23.022  1.00 60.09  ? 57  ASP   C OD2 1 
ATOM   1860 N N   . LEU   C 1 59 ? 28.227  -30.244 22.020  1.00 47.22  ? 58  LEU   C N   1 
ATOM   1861 C CA  . LEU   C 1 59 ? 27.315  -29.119 22.170  1.00 50.65  ? 58  LEU   C CA  1 
ATOM   1862 C C   . LEU   C 1 59 ? 27.952  -27.852 21.601  1.00 56.07  ? 58  LEU   C C   1 
ATOM   1863 O O   . LEU   C 1 59 ? 29.144  -27.619 21.758  1.00 62.03  ? 58  LEU   C O   1 
ATOM   1864 C CB  . LEU   C 1 59 ? 26.900  -28.939 23.634  1.00 49.08  ? 58  LEU   C CB  1 
ATOM   1865 C CG  . LEU   C 1 59 ? 26.173  -30.115 24.300  1.00 52.16  ? 58  LEU   C CG  1 
ATOM   1866 C CD1 . LEU   C 1 59 ? 25.884  -29.793 25.762  1.00 48.94  ? 58  LEU   C CD1 1 
ATOM   1867 C CD2 . LEU   C 1 59 ? 24.883  -30.544 23.599  1.00 44.39  ? 58  LEU   C CD2 1 
ATOM   1868 N N   . PHE   C 1 60 ? 27.147  -27.040 20.916  1.00 57.22  ? 59  PHE   C N   1 
ATOM   1869 C CA  . PHE   C 1 60 ? 27.631  -25.816 20.293  1.00 59.60  ? 59  PHE   C CA  1 
ATOM   1870 C C   . PHE   C 1 60 ? 26.626  -24.704 20.591  1.00 64.09  ? 59  PHE   C C   1 
ATOM   1871 O O   . PHE   C 1 60 ? 25.422  -24.885 20.390  1.00 64.22  ? 59  PHE   C O   1 
ATOM   1872 C CB  . PHE   C 1 60 ? 27.920  -26.041 18.803  1.00 58.39  ? 59  PHE   C CB  1 
ATOM   1873 C CG  . PHE   C 1 60 ? 28.863  -27.201 18.519  1.00 54.25  ? 59  PHE   C CG  1 
ATOM   1874 C CD1 . PHE   C 1 60 ? 28.398  -28.511 18.474  1.00 49.57  ? 59  PHE   C CD1 1 
ATOM   1875 C CD2 . PHE   C 1 60 ? 30.223  -26.982 18.306  1.00 63.71  ? 59  PHE   C CD2 1 
ATOM   1876 C CE1 . PHE   C 1 60 ? 29.263  -29.572 18.227  1.00 53.07  ? 59  PHE   C CE1 1 
ATOM   1877 C CE2 . PHE   C 1 60 ? 31.090  -28.044 18.056  1.00 59.47  ? 59  PHE   C CE2 1 
ATOM   1878 C CZ  . PHE   C 1 60 ? 30.609  -29.339 18.022  1.00 55.30  ? 59  PHE   C CZ  1 
ATOM   1879 N N   . PRO   C 1 61 ? 27.078  -23.534 21.112  1.00 64.39  ? 60  PRO   C N   1 
ATOM   1880 C CA  . PRO   C 1 61 ? 26.160  -22.439 21.439  1.00 62.86  ? 60  PRO   C CA  1 
ATOM   1881 C C   . PRO   C 1 61 ? 25.470  -21.981 20.154  1.00 60.15  ? 60  PRO   C C   1 
ATOM   1882 O O   . PRO   C 1 61 ? 26.094  -21.915 19.094  1.00 60.97  ? 60  PRO   C O   1 
ATOM   1883 C CB  . PRO   C 1 61 ? 27.070  -21.351 22.067  1.00 65.06  ? 60  PRO   C CB  1 
ATOM   1884 C CG  . PRO   C 1 61 ? 28.365  -22.083 22.401  1.00 57.01  ? 60  PRO   C CG  1 
ATOM   1885 C CD  . PRO   C 1 61 ? 28.489  -23.204 21.380  1.00 59.72  ? 60  PRO   C CD  1 
ATOM   1886 N N   . TYR   C 1 62 ? 24.161  -21.724 20.260  1.00 68.21  ? 61  TYR   C N   1 
ATOM   1887 C CA  . TYR   C 1 62 ? 23.290  -21.505 19.114  1.00 67.80  ? 61  TYR   C CA  1 
ATOM   1888 C C   . TYR   C 1 62 ? 23.713  -20.260 18.346  1.00 76.50  ? 61  TYR   C C   1 
ATOM   1889 O O   . TYR   C 1 62 ? 23.936  -20.327 17.137  1.00 80.31  ? 61  TYR   C O   1 
ATOM   1890 C CB  . TYR   C 1 62 ? 21.858  -21.233 19.571  1.00 59.45  ? 61  TYR   C CB  1 
ATOM   1891 C CG  . TYR   C 1 62 ? 20.893  -20.905 18.441  1.00 59.74  ? 61  TYR   C CG  1 
ATOM   1892 C CD1 . TYR   C 1 62 ? 20.828  -21.691 17.290  1.00 63.79  ? 61  TYR   C CD1 1 
ATOM   1893 C CD2 . TYR   C 1 62 ? 20.060  -19.793 18.521  1.00 59.57  ? 61  TYR   C CD2 1 
ATOM   1894 C CE1 . TYR   C 1 62 ? 19.939  -21.386 16.267  1.00 68.87  ? 61  TYR   C CE1 1 
ATOM   1895 C CE2 . TYR   C 1 62 ? 19.175  -19.474 17.501  1.00 63.03  ? 61  TYR   C CE2 1 
ATOM   1896 C CZ  . TYR   C 1 62 ? 19.112  -20.276 16.373  1.00 63.15  ? 61  TYR   C CZ  1 
ATOM   1897 O OH  . TYR   C 1 62 ? 18.223  -19.966 15.382  1.00 68.84  ? 61  TYR   C OH  1 
ATOM   1898 N N   . ASP   C 1 63 ? 23.781  -19.129 19.064  1.00 76.10  ? 62  ASP   C N   1 
ATOM   1899 C CA  . ASP   C 1 63 ? 24.091  -17.844 18.461  1.00 73.41  ? 62  ASP   C CA  1 
ATOM   1900 C C   . ASP   C 1 63 ? 25.455  -17.879 17.783  1.00 64.87  ? 62  ASP   C C   1 
ATOM   1901 O O   . ASP   C 1 63 ? 25.633  -17.252 16.739  1.00 76.20  ? 62  ASP   C O   1 
ATOM   1902 C CB  . ASP   C 1 63 ? 23.810  -16.676 19.393  1.00 77.60  ? 62  ASP   C CB  1 
ATOM   1903 C CG  . ASP   C 1 63 ? 22.409  -16.096 19.252  1.00 93.50  ? 62  ASP   C CG  1 
ATOM   1904 O OD1 . ASP   C 1 63 ? 21.634  -16.161 20.238  1.00 85.22  ? 62  ASP   C OD1 1 
ATOM   1905 O OD2 . ASP   C 1 63 ? 22.093  -15.597 18.145  1.00 96.13  ? 62  ASP   C OD2 1 
ATOM   1906 N N   . LYS   C 1 64 ? 26.398  -18.641 18.348  1.00 60.64  ? 63  LYS   C N   1 
ATOM   1907 C CA  . LYS   C 1 64 ? 27.752  -18.671 17.812  1.00 58.10  ? 63  LYS   C CA  1 
ATOM   1908 C C   . LYS   C 1 64 ? 27.822  -19.473 16.512  1.00 59.70  ? 63  LYS   C C   1 
ATOM   1909 O O   . LYS   C 1 64 ? 28.622  -19.135 15.639  1.00 61.92  ? 63  LYS   C O   1 
ATOM   1910 C CB  . LYS   C 1 64 ? 28.798  -19.117 18.844  1.00 62.08  ? 63  LYS   C CB  1 
ATOM   1911 N N   . SER   C 1 65 ? 26.973  -20.511 16.367  1.00 62.44  ? 64  SER   C N   1 
ATOM   1912 C CA  . SER   C 1 65 ? 27.158  -21.474 15.286  1.00 54.90  ? 64  SER   C CA  1 
ATOM   1913 C C   . SER   C 1 65 ? 25.930  -21.650 14.382  1.00 54.27  ? 64  SER   C C   1 
ATOM   1914 O O   . SER   C 1 65 ? 25.967  -22.454 13.451  1.00 51.61  ? 64  SER   C O   1 
ATOM   1915 C CB  . SER   C 1 65 ? 27.670  -22.788 15.818  1.00 58.39  ? 64  SER   C CB  1 
ATOM   1916 O OG  . SER   C 1 65 ? 26.641  -23.442 16.544  1.00 54.64  ? 64  SER   C OG  1 
ATOM   1917 N N   . LYS   C 1 66 ? 24.860  -20.877 14.608  1.00 54.80  ? 65  LYS   C N   1 
ATOM   1918 C CA  . LYS   C 1 66 ? 23.681  -21.000 13.759  1.00 62.28  ? 65  LYS   C CA  1 
ATOM   1919 C C   . LYS   C 1 66 ? 24.042  -20.735 12.302  1.00 69.26  ? 65  LYS   C C   1 
ATOM   1920 O O   . LYS   C 1 66 ? 23.455  -21.343 11.405  1.00 66.01  ? 65  LYS   C O   1 
ATOM   1921 C CB  . LYS   C 1 66 ? 22.463  -20.164 14.171  1.00 61.54  ? 65  LYS   C CB  1 
ATOM   1922 C CG  . LYS   C 1 66 ? 22.593  -18.649 14.130  1.00 61.45  ? 65  LYS   C CG  1 
ATOM   1923 C CD  . LYS   C 1 66 ? 21.380  -18.025 14.805  1.00 68.16  ? 65  LYS   C CD  1 
ATOM   1924 C CE  . LYS   C 1 66 ? 21.384  -16.532 14.866  1.00 79.36  ? 65  LYS   C CE  1 
ATOM   1925 N NZ  . LYS   C 1 66 ? 20.095  -16.037 15.353  1.00 81.95  ? 65  LYS   C NZ  1 
ATOM   1926 N N   . ASP   C 1 67 ? 25.018  -19.845 12.072  1.00 68.04  ? 66  ASP   C N   1 
ATOM   1927 C CA  . ASP   C 1 67 ? 25.345  -19.491 10.696  1.00 73.61  ? 66  ASP   C CA  1 
ATOM   1928 C C   . ASP   C 1 67 ? 25.774  -20.747 9.937   1.00 68.10  ? 66  ASP   C C   1 
ATOM   1929 O O   . ASP   C 1 67 ? 25.546  -20.831 8.734   1.00 57.14  ? 66  ASP   C O   1 
ATOM   1930 C CB  . ASP   C 1 67 ? 26.151  -18.200 10.552  1.00 74.82  ? 66  ASP   C CB  1 
ATOM   1931 C CG  . ASP   C 1 67 ? 27.675  -18.267 10.573  1.00 83.85  ? 66  ASP   C CG  1 
ATOM   1932 O OD1 . ASP   C 1 67 ? 28.243  -19.238 10.013  1.00 77.91  ? 66  ASP   C OD1 1 
ATOM   1933 O OD2 . ASP   C 1 67 ? 28.290  -17.289 11.070  1.00 76.97  ? 66  ASP   C OD2 1 
ATOM   1934 N N   . LYS   C 1 68 ? 26.306  -21.738 10.677  1.00 59.78  ? 67  LYS   C N   1 
ATOM   1935 C CA  . LYS   C 1 68 ? 26.905  -22.952 10.133  1.00 57.83  ? 67  LYS   C CA  1 
ATOM   1936 C C   . LYS   C 1 68 ? 25.921  -24.135 10.150  1.00 54.38  ? 67  LYS   C C   1 
ATOM   1937 O O   . LYS   C 1 68 ? 25.866  -24.912 9.198   1.00 56.87  ? 67  LYS   C O   1 
ATOM   1938 C CB  . LYS   C 1 68 ? 28.165  -23.178 10.983  1.00 51.03  ? 67  LYS   C CB  1 
ATOM   1939 C CG  . LYS   C 1 68 ? 29.122  -24.325 10.686  1.00 56.52  ? 67  LYS   C CG  1 
ATOM   1940 C CD  . LYS   C 1 68 ? 30.282  -24.137 11.666  1.00 67.12  ? 67  LYS   C CD  1 
ATOM   1941 C CE  . LYS   C 1 68 ? 31.152  -25.302 12.045  1.00 72.12  ? 67  LYS   C CE  1 
ATOM   1942 N NZ  . LYS   C 1 68 ? 32.233  -25.638 11.113  1.00 69.52  ? 67  LYS   C NZ  1 
ATOM   1943 N N   . TYR   C 1 69 ? 25.154  -24.292 11.237  1.00 54.54  ? 68  TYR   C N   1 
ATOM   1944 C CA  . TYR   C 1 69 ? 24.337  -25.487 11.426  1.00 54.36  ? 68  TYR   C CA  1 
ATOM   1945 C C   . TYR   C 1 69 ? 22.845  -25.184 11.263  1.00 53.00  ? 68  TYR   C C   1 
ATOM   1946 O O   . TYR   C 1 69 ? 22.049  -26.109 11.104  1.00 46.91  ? 68  TYR   C O   1 
ATOM   1947 C CB  . TYR   C 1 69 ? 24.558  -26.097 12.819  1.00 48.97  ? 68  TYR   C CB  1 
ATOM   1948 C CG  . TYR   C 1 69 ? 25.959  -26.599 13.145  1.00 46.72  ? 68  TYR   C CG  1 
ATOM   1949 C CD1 . TYR   C 1 69 ? 26.723  -27.318 12.226  1.00 54.12  ? 68  TYR   C CD1 1 
ATOM   1950 C CD2 . TYR   C 1 69 ? 26.510  -26.365 14.398  1.00 54.48  ? 68  TYR   C CD2 1 
ATOM   1951 C CE1 . TYR   C 1 69 ? 27.997  -27.768 12.541  1.00 49.66  ? 68  TYR   C CE1 1 
ATOM   1952 C CE2 . TYR   C 1 69 ? 27.783  -26.804 14.723  1.00 54.67  ? 68  TYR   C CE2 1 
ATOM   1953 C CZ  . TYR   C 1 69 ? 28.523  -27.509 13.795  1.00 53.24  ? 68  TYR   C CZ  1 
ATOM   1954 O OH  . TYR   C 1 69 ? 29.768  -27.926 14.173  1.00 65.80  ? 68  TYR   C OH  1 
ATOM   1955 N N   . GLY   C 1 70 ? 22.467  -23.902 11.365  1.00 49.57  ? 69  GLY   C N   1 
ATOM   1956 C CA  . GLY   C 1 70 ? 21.077  -23.493 11.228  1.00 55.95  ? 69  GLY   C CA  1 
ATOM   1957 C C   . GLY   C 1 70 ? 20.706  -23.342 9.757   1.00 55.56  ? 69  GLY   C C   1 
ATOM   1958 O O   . GLY   C 1 70 ? 20.684  -22.229 9.240   1.00 51.93  ? 69  GLY   C O   1 
ATOM   1959 N N   . LYS   C 1 71 ? 20.470  -24.482 9.097   1.00 48.44  ? 70  LYS   C N   1 
ATOM   1960 C CA  . LYS   C 1 71 ? 20.133  -24.566 7.678   1.00 52.30  ? 70  LYS   C CA  1 
ATOM   1961 C C   . LYS   C 1 71 ? 19.262  -25.803 7.496   1.00 50.50  ? 70  LYS   C C   1 
ATOM   1962 O O   . LYS   C 1 71 ? 19.403  -26.779 8.234   1.00 55.74  ? 70  LYS   C O   1 
ATOM   1963 C CB  . LYS   C 1 71 ? 21.367  -24.735 6.774   1.00 49.86  ? 70  LYS   C CB  1 
ATOM   1964 C CG  . LYS   C 1 71 ? 22.251  -25.911 7.158   1.00 55.35  ? 70  LYS   C CG  1 
ATOM   1965 C CD  . LYS   C 1 71 ? 23.472  -26.227 6.305   1.00 63.82  ? 70  LYS   C CD  1 
ATOM   1966 C CE  . LYS   C 1 71 ? 24.192  -27.436 6.851   1.00 62.03  ? 70  LYS   C CE  1 
ATOM   1967 N N   . PRO   C 1 72 ? 18.284  -25.802 6.568   1.00 44.72  ? 71  PRO   C N   1 
ATOM   1968 C CA  . PRO   C 1 72 ? 17.361  -26.924 6.496   1.00 42.84  ? 71  PRO   C CA  1 
ATOM   1969 C C   . PRO   C 1 72 ? 18.034  -28.251 6.180   1.00 44.56  ? 71  PRO   C C   1 
ATOM   1970 O O   . PRO   C 1 72 ? 19.128  -28.299 5.608   1.00 47.04  ? 71  PRO   C O   1 
ATOM   1971 C CB  . PRO   C 1 72 ? 16.405  -26.462 5.393   1.00 42.52  ? 71  PRO   C CB  1 
ATOM   1972 C CG  . PRO   C 1 72 ? 16.449  -24.967 5.541   1.00 42.05  ? 71  PRO   C CG  1 
ATOM   1973 C CD  . PRO   C 1 72 ? 17.930  -24.697 5.662   1.00 41.13  ? 71  PRO   C CD  1 
ATOM   1974 N N   . ASN   C 1 73 ? 17.355  -29.321 6.573   1.00 43.74  ? 72  ASN   C N   1 
ATOM   1975 C CA  . ASN   C 1 73 ? 17.669  -30.624 6.023   1.00 52.33  ? 72  ASN   C CA  1 
ATOM   1976 C C   . ASN   C 1 73 ? 16.446  -31.518 6.139   1.00 47.20  ? 72  ASN   C C   1 
ATOM   1977 O O   . ASN   C 1 73 ? 15.465  -31.169 6.791   1.00 47.15  ? 72  ASN   C O   1 
ATOM   1978 C CB  . ASN   C 1 73 ? 19.001  -31.193 6.518   1.00 56.84  ? 72  ASN   C CB  1 
ATOM   1979 C CG  . ASN   C 1 73 ? 18.887  -31.860 7.864   1.00 53.21  ? 72  ASN   C CG  1 
ATOM   1980 O OD1 . ASN   C 1 73 ? 18.299  -32.941 7.983   1.00 47.84  ? 72  ASN   C OD1 1 
ATOM   1981 N ND2 . ASN   C 1 73 ? 19.493  -31.259 8.871   1.00 57.84  ? 72  ASN   C ND2 1 
ATOM   1982 N N   . LYS   C 1 74 ? 16.542  -32.681 5.493   1.00 52.89  ? 73  LYS   C N   1 
ATOM   1983 C CA  . LYS   C 1 74 ? 15.376  -33.491 5.208   1.00 48.97  ? 73  LYS   C CA  1 
ATOM   1984 C C   . LYS   C 1 74 ? 15.075  -34.391 6.400   1.00 44.13  ? 73  LYS   C C   1 
ATOM   1985 O O   . LYS   C 1 74 ? 13.994  -34.969 6.447   1.00 53.06  ? 73  LYS   C O   1 
ATOM   1986 C CB  . LYS   C 1 74 ? 15.652  -34.264 3.909   1.00 49.02  ? 73  LYS   C CB  1 
ATOM   1987 N N   . ARG   C 1 75 ? 16.015  -34.515 7.359   1.00 40.73  ? 74  ARG   C N   1 
ATOM   1988 C CA  . ARG   C 1 75 ? 15.814  -35.468 8.453   1.00 42.50  ? 74  ARG   C CA  1 
ATOM   1989 C C   . ARG   C 1 75 ? 14.550  -35.087 9.228   1.00 45.10  ? 74  ARG   C C   1 
ATOM   1990 O O   . ARG   C 1 75 ? 14.257  -33.901 9.431   1.00 43.81  ? 74  ARG   C O   1 
ATOM   1991 C CB  . ARG   C 1 75 ? 16.987  -35.666 9.440   1.00 39.96  ? 74  ARG   C CB  1 
ATOM   1992 C CG  . ARG   C 1 75 ? 18.351  -35.872 8.787   1.00 52.42  ? 74  ARG   C CG  1 
ATOM   1993 C CD  . ARG   C 1 75 ? 18.648  -37.207 8.112   1.00 53.91  ? 74  ARG   C CD  1 
ATOM   1994 N NE  . ARG   C 1 75 ? 18.631  -38.175 9.209   1.00 50.45  ? 74  ARG   C NE  1 
ATOM   1995 C CZ  . ARG   C 1 75 ? 19.750  -38.562 9.829   1.00 45.08  ? 74  ARG   C CZ  1 
ATOM   1996 N NH1 . ARG   C 1 75 ? 19.674  -39.194 10.975  1.00 44.98  ? 74  ARG   C NH1 1 
ATOM   1997 N NH2 . ARG   C 1 75 ? 20.923  -38.236 9.337   1.00 46.37  ? 74  ARG   C NH2 1 
ATOM   1998 N N   . LYS   C 1 76 ? 13.821  -36.120 9.672   1.00 46.83  ? 75  LYS   C N   1 
ATOM   1999 C CA  . LYS   C 1 76 ? 12.512  -35.997 10.291  1.00 51.26  ? 75  LYS   C CA  1 
ATOM   2000 C C   . LYS   C 1 76 ? 12.601  -35.047 11.479  1.00 50.79  ? 75  LYS   C C   1 
ATOM   2001 O O   . LYS   C 1 76 ? 13.371  -35.302 12.410  1.00 49.00  ? 75  LYS   C O   1 
ATOM   2002 C CB  . LYS   C 1 76 ? 11.984  -37.366 10.759  1.00 52.11  ? 75  LYS   C CB  1 
ATOM   2003 C CG  . LYS   C 1 76 ? 10.456  -37.495 10.795  1.00 51.13  ? 75  LYS   C CG  1 
ATOM   2004 C CD  . LYS   C 1 76 ? 9.873   -38.458 11.825  1.00 61.81  ? 75  LYS   C CD  1 
ATOM   2005 N N   . GLY   C 1 77 ? 11.805  -33.967 11.423  1.00 47.05  ? 76  GLY   C N   1 
ATOM   2006 C CA  . GLY   C 1 77 ? 11.545  -33.104 12.568  1.00 44.32  ? 76  GLY   C CA  1 
ATOM   2007 C C   . GLY   C 1 77 ? 12.519  -31.930 12.646  1.00 40.43  ? 76  GLY   C C   1 
ATOM   2008 O O   . GLY   C 1 77 ? 12.362  -31.040 13.480  1.00 44.18  ? 76  GLY   C O   1 
ATOM   2009 N N   . PHE   C 1 78 ? 13.526  -31.938 11.762  1.00 40.40  ? 77  PHE   C N   1 
ATOM   2010 C CA  . PHE   C 1 78 ? 14.592  -30.955 11.774  1.00 41.83  ? 77  PHE   C CA  1 
ATOM   2011 C C   . PHE   C 1 78 ? 14.055  -29.554 11.468  1.00 44.37  ? 77  PHE   C C   1 
ATOM   2012 O O   . PHE   C 1 78 ? 14.375  -28.594 12.182  1.00 36.34  ? 77  PHE   C O   1 
ATOM   2013 C CB  . PHE   C 1 78 ? 15.765  -31.321 10.855  1.00 41.26  ? 77  PHE   C CB  1 
ATOM   2014 C CG  . PHE   C 1 78 ? 17.071  -30.574 11.133  1.00 43.58  ? 77  PHE   C CG  1 
ATOM   2015 C CD1 . PHE   C 1 78 ? 17.332  -29.329 10.552  1.00 46.66  ? 77  PHE   C CD1 1 
ATOM   2016 C CD2 . PHE   C 1 78 ? 18.079  -31.143 11.912  1.00 40.13  ? 77  PHE   C CD2 1 
ATOM   2017 C CE1 . PHE   C 1 78 ? 18.540  -28.665 10.776  1.00 44.46  ? 77  PHE   C CE1 1 
ATOM   2018 C CE2 . PHE   C 1 78 ? 19.290  -30.477 12.129  1.00 41.61  ? 77  PHE   C CE2 1 
ATOM   2019 C CZ  . PHE   C 1 78 ? 19.525  -29.243 11.560  1.00 42.21  ? 77  PHE   C CZ  1 
ATOM   2020 N N   . ASN   C 1 79 ? 13.292  -29.421 10.376  1.00 42.56  ? 78  ASN   C N   1 
ATOM   2021 C CA  . ASN   C 1 79 ? 12.923  -28.085 9.932   1.00 45.87  ? 78  ASN   C CA  1 
ATOM   2022 C C   . ASN   C 1 79 ? 11.994  -27.436 10.959  1.00 42.99  ? 78  ASN   C C   1 
ATOM   2023 O O   . ASN   C 1 79 ? 12.123  -26.252 11.292  1.00 40.77  ? 78  ASN   C O   1 
ATOM   2024 C CB  . ASN   C 1 79 ? 12.526  -28.051 8.459   1.00 46.04  ? 78  ASN   C CB  1 
ATOM   2025 C CG  . ASN   C 1 79 ? 13.710  -28.410 7.594   1.00 45.89  ? 78  ASN   C CG  1 
ATOM   2026 O OD1 . ASN   C 1 79 ? 14.843  -28.060 7.934   1.00 46.23  ? 78  ASN   C OD1 1 
ATOM   2027 N ND2 . ASN   C 1 79 ? 13.502  -29.158 6.519   1.00 43.21  ? 78  ASN   C ND2 1 
ATOM   2028 N N   . GLU   C 1 80 ? 11.096  -28.234 11.526  1.00 44.52  ? 79  GLU   C N   1 
ATOM   2029 C CA  . GLU   C 1 80 ? 10.299  -27.705 12.620  1.00 48.36  ? 79  GLU   C CA  1 
ATOM   2030 C C   . GLU   C 1 80 ? 11.211  -27.310 13.780  1.00 47.66  ? 79  GLU   C C   1 
ATOM   2031 O O   . GLU   C 1 80 ? 10.991  -26.278 14.420  1.00 45.08  ? 79  GLU   C O   1 
ATOM   2032 C CB  . GLU   C 1 80 ? 9.234   -28.720 13.024  1.00 49.50  ? 79  GLU   C CB  1 
ATOM   2033 C CG  . GLU   C 1 80 ? 8.216   -28.142 13.999  1.00 49.73  ? 79  GLU   C CG  1 
ATOM   2034 C CD  . GLU   C 1 80 ? 7.069   -29.115 14.164  1.00 56.68  ? 79  GLU   C CD  1 
ATOM   2035 O OE1 . GLU   C 1 80 ? 7.175   -30.257 13.669  1.00 66.38  ? 79  GLU   C OE1 1 
ATOM   2036 O OE2 . GLU   C 1 80 ? 6.053   -28.711 14.744  1.00 52.43  ? 79  GLU   C OE2 1 
ATOM   2037 N N   . GLY   C 1 81 ? 12.249  -28.130 14.039  1.00 47.26  ? 80  GLY   C N   1 
ATOM   2038 C CA  . GLY   C 1 81 ? 13.203  -27.803 15.090  1.00 42.71  ? 80  GLY   C CA  1 
ATOM   2039 C C   . GLY   C 1 81 ? 13.795  -26.407 14.902  1.00 45.63  ? 80  GLY   C C   1 
ATOM   2040 O O   . GLY   C 1 81 ? 13.923  -25.655 15.866  1.00 41.76  ? 80  GLY   C O   1 
ATOM   2041 N N   . LEU   C 1 82 ? 14.226  -26.105 13.659  1.00 47.81  ? 81  LEU   C N   1 
ATOM   2042 C CA  . LEU   C 1 82 ? 14.753  -24.794 13.282  1.00 44.56  ? 81  LEU   C CA  1 
ATOM   2043 C C   . LEU   C 1 82 ? 13.746  -23.675 13.573  1.00 44.87  ? 81  LEU   C C   1 
ATOM   2044 O O   . LEU   C 1 82 ? 14.128  -22.628 14.082  1.00 48.43  ? 81  LEU   C O   1 
ATOM   2045 C CB  . LEU   C 1 82 ? 15.225  -24.710 11.830  1.00 45.75  ? 81  LEU   C CB  1 
ATOM   2046 C CG  . LEU   C 1 82 ? 16.437  -25.564 11.463  1.00 40.85  ? 81  LEU   C CG  1 
ATOM   2047 C CD1 . LEU   C 1 82 ? 16.821  -25.381 10.001  1.00 47.48  ? 81  LEU   C CD1 1 
ATOM   2048 C CD2 . LEU   C 1 82 ? 17.582  -25.152 12.340  1.00 45.48  ? 81  LEU   C CD2 1 
ATOM   2049 N N   . TRP   C 1 83 ? 12.478  -23.869 13.202  1.00 43.16  ? 82  TRP   C N   1 
ATOM   2050 C CA  . TRP   C 1 83 ? 11.473  -22.856 13.476  1.00 55.84  ? 82  TRP   C CA  1 
ATOM   2051 C C   . TRP   C 1 83 ? 11.369  -22.600 14.984  1.00 58.85  ? 82  TRP   C C   1 
ATOM   2052 O O   . TRP   C 1 83 ? 11.351  -21.446 15.425  1.00 56.17  ? 82  TRP   C O   1 
ATOM   2053 C CB  . TRP   C 1 83 ? 10.103  -23.236 12.894  1.00 53.20  ? 82  TRP   C CB  1 
ATOM   2054 C CG  . TRP   C 1 83 ? 9.141   -22.081 12.962  1.00 54.31  ? 82  TRP   C CG  1 
ATOM   2055 C CD1 . TRP   C 1 83 ? 9.015   -21.077 12.045  1.00 52.22  ? 82  TRP   C CD1 1 
ATOM   2056 C CD2 . TRP   C 1 83 ? 8.234   -21.763 14.041  1.00 64.07  ? 82  TRP   C CD2 1 
ATOM   2057 N NE1 . TRP   C 1 83 ? 8.067   -20.177 12.457  1.00 54.20  ? 82  TRP   C NE1 1 
ATOM   2058 C CE2 . TRP   C 1 83 ? 7.569   -20.567 13.673  1.00 58.23  ? 82  TRP   C CE2 1 
ATOM   2059 C CE3 . TRP   C 1 83 ? 7.910   -22.371 15.264  1.00 65.35  ? 82  TRP   C CE3 1 
ATOM   2060 C CZ2 . TRP   C 1 83 ? 6.599   -19.977 14.482  1.00 62.40  ? 82  TRP   C CZ2 1 
ATOM   2061 C CZ3 . TRP   C 1 83 ? 6.954   -21.782 16.066  1.00 66.76  ? 82  TRP   C CZ3 1 
ATOM   2062 C CH2 . TRP   C 1 83 ? 6.314   -20.601 15.678  1.00 69.41  ? 82  TRP   C CH2 1 
ATOM   2063 N N   . GLU   C 1 84 ? 11.311  -23.687 15.765  1.00 50.78  ? 83  GLU   C N   1 
ATOM   2064 C CA  . GLU   C 1 84 ? 11.157  -23.582 17.205  1.00 50.58  ? 83  GLU   C CA  1 
ATOM   2065 C C   . GLU   C 1 84 ? 12.341  -22.853 17.835  1.00 47.83  ? 83  GLU   C C   1 
ATOM   2066 O O   . GLU   C 1 84 ? 12.144  -21.980 18.681  1.00 49.70  ? 83  GLU   C O   1 
ATOM   2067 C CB  . GLU   C 1 84 ? 10.958  -24.921 17.911  1.00 49.30  ? 83  GLU   C CB  1 
ATOM   2068 C CG  . GLU   C 1 84 ? 9.614   -25.582 17.627  1.00 51.07  ? 83  GLU   C CG  1 
ATOM   2069 C CD  . GLU   C 1 84 ? 9.538   -27.043 18.046  1.00 54.53  ? 83  GLU   C CD  1 
ATOM   2070 O OE1 . GLU   C 1 84 ? 10.499  -27.573 18.661  1.00 50.30  ? 83  GLU   C OE1 1 
ATOM   2071 O OE2 . GLU   C 1 84 ? 8.514   -27.678 17.713  1.00 58.78  ? 83  GLU   C OE2 1 
ATOM   2072 N N   . ILE   C 1 85 ? 13.572  -23.207 17.453  1.00 47.84  ? 84  ILE   C N   1 
ATOM   2073 C CA  . ILE   C 1 85 ? 14.712  -22.621 18.141  1.00 52.85  ? 84  ILE   C CA  1 
ATOM   2074 C C   . ILE   C 1 85 ? 14.814  -21.122 17.834  1.00 57.88  ? 84  ILE   C C   1 
ATOM   2075 O O   . ILE   C 1 85 ? 15.378  -20.377 18.636  1.00 51.64  ? 84  ILE   C O   1 
ATOM   2076 C CB  . ILE   C 1 85 ? 16.026  -23.371 17.846  1.00 50.78  ? 84  ILE   C CB  1 
ATOM   2077 C CG1 . ILE   C 1 85 ? 17.104  -22.995 18.861  1.00 45.40  ? 84  ILE   C CG1 1 
ATOM   2078 C CG2 . ILE   C 1 85 ? 16.489  -23.163 16.400  1.00 46.34  ? 84  ILE   C CG2 1 
ATOM   2079 C CD1 . ILE   C 1 85 ? 18.474  -23.608 18.612  1.00 52.77  ? 84  ILE   C CD1 1 
ATOM   2080 N N   . GLN   C 1 86 ? 14.265  -20.686 16.686  1.00 52.91  ? 85  GLN   C N   1 
ATOM   2081 C CA  . GLN   C 1 86 ? 14.337  -19.288 16.262  1.00 62.03  ? 85  GLN   C CA  1 
ATOM   2082 C C   . GLN   C 1 86 ? 13.193  -18.435 16.829  1.00 54.33  ? 85  GLN   C C   1 
ATOM   2083 O O   . GLN   C 1 86 ? 13.424  -17.291 17.216  1.00 59.26  ? 85  GLN   C O   1 
ATOM   2084 C CB  . GLN   C 1 86 ? 14.370  -19.107 14.741  1.00 58.24  ? 85  GLN   C CB  1 
ATOM   2085 C CG  . GLN   C 1 86 ? 14.695  -17.685 14.281  1.00 53.12  ? 85  GLN   C CG  1 
ATOM   2086 C CD  . GLN   C 1 86 ? 15.048  -17.590 12.807  1.00 58.08  ? 85  GLN   C CD  1 
ATOM   2087 O OE1 . GLN   C 1 86 ? 14.805  -18.509 12.010  1.00 56.78  ? 85  GLN   C OE1 1 
ATOM   2088 N NE2 . GLN   C 1 86 ? 15.628  -16.460 12.421  1.00 50.68  ? 85  GLN   C NE2 1 
ATOM   2089 N N   . ASN   C 1 87 ? 11.985  -19.001 16.897  1.00 52.28  ? 86  ASN   C N   1 
ATOM   2090 C CA  . ASN   C 1 87 ? 10.747  -18.259 17.103  1.00 57.02  ? 86  ASN   C CA  1 
ATOM   2091 C C   . ASN   C 1 87 ? 10.105  -18.555 18.462  1.00 61.92  ? 86  ASN   C C   1 
ATOM   2092 O O   . ASN   C 1 87 ? 9.528   -17.654 19.075  1.00 62.94  ? 86  ASN   C O   1 
ATOM   2093 C CB  . ASN   C 1 87 ? 9.745   -18.537 15.987  1.00 50.59  ? 86  ASN   C CB  1 
ATOM   2094 C CG  . ASN   C 1 87 ? 10.281  -18.055 14.665  1.00 62.36  ? 86  ASN   C CG  1 
ATOM   2095 O OD1 . ASN   C 1 87 ? 10.519  -16.853 14.488  1.00 68.47  ? 86  ASN   C OD1 1 
ATOM   2096 N ND2 . ASN   C 1 87 ? 10.537  -18.975 13.750  1.00 51.85  ? 86  ASN   C ND2 1 
ATOM   2097 N N   . ASN   C 1 88 ? 10.188  -19.813 18.924  1.00 61.56  ? 87  ASN   C N   1 
ATOM   2098 C CA  . ASN   C 1 88 ? 9.496   -20.207 20.143  1.00 59.50  ? 87  ASN   C CA  1 
ATOM   2099 C C   . ASN   C 1 88 ? 10.385  -21.074 21.042  1.00 60.12  ? 87  ASN   C C   1 
ATOM   2100 O O   . ASN   C 1 88 ? 9.989   -22.177 21.432  1.00 59.11  ? 87  ASN   C O   1 
ATOM   2101 C CB  . ASN   C 1 88 ? 8.159   -20.855 19.804  1.00 68.21  ? 87  ASN   C CB  1 
ATOM   2102 C CG  . ASN   C 1 88 ? 7.280   -21.047 21.020  1.00 71.88  ? 87  ASN   C CG  1 
ATOM   2103 O OD1 . ASN   C 1 88 ? 7.438   -20.363 22.041  1.00 73.74  ? 87  ASN   C OD1 1 
ATOM   2104 N ND2 . ASN   C 1 88 ? 6.329   -21.956 20.912  1.00 66.13  ? 87  ASN   C ND2 1 
ATOM   2105 N N   . PRO   C 1 89 ? 11.580  -20.587 21.456  1.00 55.89  ? 88  PRO   C N   1 
ATOM   2106 C CA  . PRO   C 1 89 ? 12.587  -21.434 22.105  1.00 65.93  ? 88  PRO   C CA  1 
ATOM   2107 C C   . PRO   C 1 89 ? 12.415  -21.932 23.540  1.00 68.89  ? 88  PRO   C C   1 
ATOM   2108 O O   . PRO   C 1 89 ? 13.214  -22.768 23.963  1.00 64.81  ? 88  PRO   C O   1 
ATOM   2109 C CB  . PRO   C 1 89 ? 13.920  -20.670 21.950  1.00 57.00  ? 88  PRO   C CB  1 
ATOM   2110 C CG  . PRO   C 1 89 ? 13.547  -19.398 21.198  1.00 62.09  ? 88  PRO   C CG  1 
ATOM   2111 C CD  . PRO   C 1 89 ? 12.041  -19.204 21.290  1.00 56.99  ? 88  PRO   C CD  1 
ATOM   2112 N N   . HIS   C 1 90 ? 11.403  -21.414 24.262  1.00 66.38  ? 89  HIS   C N   1 
ATOM   2113 C CA  . HIS   C 1 90 ? 11.183  -21.716 25.675  1.00 60.92  ? 89  HIS   C CA  1 
ATOM   2114 C C   . HIS   C 1 90 ? 9.733   -22.083 25.973  1.00 65.70  ? 89  HIS   C C   1 
ATOM   2115 O O   . HIS   C 1 90 ? 9.294   -21.985 27.115  1.00 73.36  ? 89  HIS   C O   1 
ATOM   2116 C CB  . HIS   C 1 90 ? 11.579  -20.542 26.572  1.00 46.01  ? 89  HIS   C CB  1 
ATOM   2117 C CG  . HIS   C 1 90 ? 12.985  -20.105 26.352  1.00 49.92  ? 89  HIS   C CG  1 
ATOM   2118 N ND1 . HIS   C 1 90 ? 14.056  -20.900 26.713  1.00 55.03  ? 89  HIS   C ND1 1 
ATOM   2119 C CD2 . HIS   C 1 90 ? 13.509  -19.001 25.788  1.00 49.56  ? 89  HIS   C CD2 1 
ATOM   2120 C CE1 . HIS   C 1 90 ? 15.187  -20.280 26.402  1.00 54.03  ? 89  HIS   C CE1 1 
ATOM   2121 N NE2 . HIS   C 1 90 ? 14.876  -19.117 25.843  1.00 52.69  ? 89  HIS   C NE2 1 
ATOM   2122 N N   . ALA   C 1 91 ? 8.999   -22.525 24.950  1.00 70.80  ? 90  ALA   C N   1 
ATOM   2123 C CA  . ALA   C 1 91 ? 7.678   -23.097 25.150  1.00 72.80  ? 90  ALA   C CA  1 
ATOM   2124 C C   . ALA   C 1 91 ? 7.806   -24.479 25.790  1.00 73.87  ? 90  ALA   C C   1 
ATOM   2125 O O   . ALA   C 1 91 ? 8.892   -25.054 25.830  1.00 77.25  ? 90  ALA   C O   1 
ATOM   2126 C CB  . ALA   C 1 91 ? 6.942   -23.158 23.826  1.00 68.40  ? 90  ALA   C CB  1 
ATOM   2127 N N   . SER   C 1 92 ? 6.665   -25.018 26.239  1.00 85.54  ? 91  SER   C N   1 
ATOM   2128 C CA  . SER   C 1 92 ? 6.579   -26.252 27.008  1.00 85.71  ? 91  SER   C CA  1 
ATOM   2129 C C   . SER   C 1 92 ? 6.853   -27.482 26.145  1.00 82.20  ? 91  SER   C C   1 
ATOM   2130 O O   . SER   C 1 92 ? 7.633   -28.347 26.532  1.00 92.32  ? 91  SER   C O   1 
ATOM   2131 C CB  . SER   C 1 92 ? 5.229   -26.377 27.675  1.00 79.53  ? 91  SER   C CB  1 
ATOM   2132 O OG  . SER   C 1 92 ? 5.043   -25.329 28.610  1.00 82.91  ? 91  SER   C OG  1 
ATOM   2133 N N   . TYR   C 1 93 ? 6.148   -27.581 25.014  1.00 79.92  ? 92  TYR   C N   1 
ATOM   2134 C CA  . TYR   C 1 93 ? 6.185   -28.755 24.154  1.00 84.45  ? 92  TYR   C CA  1 
ATOM   2135 C C   . TYR   C 1 93 ? 5.828   -30.001 24.981  1.00 85.67  ? 92  TYR   C C   1 
ATOM   2136 O O   . TYR   C 1 93 ? 6.206   -31.120 24.563  1.00 97.84  ? 92  TYR   C O   1 
ATOM   2137 C CB  . TYR   C 1 93 ? 7.520   -28.851 23.401  1.00 82.15  ? 92  TYR   C CB  1 
ATOM   2138 C CG  . TYR   C 1 93 ? 7.886   -27.604 22.602  1.00 76.52  ? 92  TYR   C CG  1 
ATOM   2139 C CD1 . TYR   C 1 93 ? 7.203   -27.280 21.430  1.00 68.72  ? 92  TYR   C CD1 1 
ATOM   2140 C CD2 . TYR   C 1 93 ? 8.920   -26.766 23.009  1.00 68.04  ? 92  TYR   C CD2 1 
ATOM   2141 C CE1 . TYR   C 1 93 ? 7.517   -26.148 20.700  1.00 71.32  ? 92  TYR   C CE1 1 
ATOM   2142 C CE2 . TYR   C 1 93 ? 9.249   -25.633 22.280  1.00 71.51  ? 92  TYR   C CE2 1 
ATOM   2143 C CZ  . TYR   C 1 93 ? 8.544   -25.323 21.128  1.00 74.23  ? 92  TYR   C CZ  1 
ATOM   2144 O OH  . TYR   C 1 93 ? 8.859   -24.208 20.403  1.00 82.62  ? 92  TYR   C OH  1 
HETATM 2145 S S   . SO4   D 2 .  ? 1.693   -33.735 2.027   1.00 110.51 ? 101 SO4   A S   1 
HETATM 2146 O O1  . SO4   D 2 .  ? 2.467   -34.656 1.230   1.00 102.40 ? 101 SO4   A O1  1 
HETATM 2147 O O2  . SO4   D 2 .  ? 1.472   -32.519 1.287   1.00 104.80 ? 101 SO4   A O2  1 
HETATM 2148 O O3  . SO4   D 2 .  ? 0.424   -34.330 2.355   1.00 121.46 ? 101 SO4   A O3  1 
HETATM 2149 O O4  . SO4   D 2 .  ? 2.406   -33.436 3.239   1.00 111.61 ? 101 SO4   A O4  1 
HETATM 2150 S S   . SO4   E 2 .  ? -8.895  -25.007 1.472   1.00 93.30  ? 102 SO4   A S   1 
HETATM 2151 O O1  . SO4   E 2 .  ? -9.417  -24.400 0.262   1.00 80.72  ? 102 SO4   A O1  1 
HETATM 2152 O O2  . SO4   E 2 .  ? -8.842  -24.024 2.529   1.00 81.57  ? 102 SO4   A O2  1 
HETATM 2153 O O3  . SO4   E 2 .  ? -9.735  -26.108 1.876   1.00 95.36  ? 102 SO4   A O3  1 
HETATM 2154 O O4  . SO4   E 2 .  ? -7.573  -25.507 1.225   1.00 107.78 ? 102 SO4   A O4  1 
HETATM 2155 C C1  . EDO   F 3 .  ? 14.391  -19.688 -7.538  1.00 46.21  ? 103 EDO   A C1  1 
HETATM 2156 O O1  . EDO   F 3 .  ? 15.594  -18.966 -7.189  1.00 43.59  ? 103 EDO   A O1  1 
HETATM 2157 C C2  . EDO   F 3 .  ? 13.459  -18.992 -8.495  1.00 44.52  ? 103 EDO   A C2  1 
HETATM 2158 O O2  . EDO   F 3 .  ? 13.068  -17.684 -8.077  1.00 43.32  ? 103 EDO   A O2  1 
HETATM 2159 S S   . SO4   G 2 .  ? 9.471   -29.483 5.766   1.00 86.54  ? 104 SO4   A S   1 
HETATM 2160 O O1  . SO4   G 2 .  ? 10.315  -28.748 4.878   1.00 81.04  ? 104 SO4   A O1  1 
HETATM 2161 O O2  . SO4   G 2 .  ? 8.886   -30.597 5.062   1.00 94.15  ? 104 SO4   A O2  1 
HETATM 2162 O O3  . SO4   G 2 .  ? 10.244  -29.967 6.886   1.00 90.68  ? 104 SO4   A O3  1 
HETATM 2163 O O4  . SO4   G 2 .  ? 8.418   -28.624 6.228   1.00 98.52  ? 104 SO4   A O4  1 
HETATM 2164 S S   . SO4   H 2 .  ? 7.664   -8.304  -25.037 1.00 91.52  ? 101 SO4   B S   1 
HETATM 2165 O O1  . SO4   H 2 .  ? 8.795   -8.233  -25.927 1.00 57.01  ? 101 SO4   B O1  1 
HETATM 2166 O O2  . SO4   H 2 .  ? 6.570   -9.026  -25.656 1.00 69.11  ? 101 SO4   B O2  1 
HETATM 2167 O O3  . SO4   H 2 .  ? 8.026   -9.004  -23.816 1.00 67.85  ? 101 SO4   B O3  1 
HETATM 2168 O O4  . SO4   H 2 .  ? 7.268   -6.949  -24.743 1.00 80.76  ? 101 SO4   B O4  1 
HETATM 2169 S S   . SO4   I 2 .  ? 14.631  -26.879 -26.722 1.00 83.64  ? 102 SO4   B S   1 
HETATM 2170 O O1  . SO4   I 2 .  ? 15.852  -26.304 -26.221 1.00 75.06  ? 102 SO4   B O1  1 
HETATM 2171 O O2  . SO4   I 2 .  ? 14.894  -28.208 -27.219 1.00 94.83  ? 102 SO4   B O2  1 
HETATM 2172 O O3  . SO4   I 2 .  ? 13.673  -26.954 -25.654 1.00 91.57  ? 102 SO4   B O3  1 
HETATM 2173 O O4  . SO4   I 2 .  ? 14.102  -26.060 -27.794 1.00 72.32  ? 102 SO4   B O4  1 
HETATM 2174 N N1  . A1A36 J 4 .  ? 19.771  -15.739 -20.822 0.76 56.28  ? 103 A1A36 B N1  1 
HETATM 2175 C C4  . A1A36 J 4 .  ? 18.171  -14.872 -22.490 0.76 46.79  ? 103 A1A36 B C4  1 
HETATM 2176 C C5  . A1A36 J 4 .  ? 18.425  -15.189 -21.030 0.76 51.56  ? 103 A1A36 B C5  1 
HETATM 2177 C C6  . A1A36 J 4 .  ? 19.851  -17.162 -21.163 0.76 59.13  ? 103 A1A36 B C6  1 
HETATM 2178 C C3  . A1A36 J 4 .  ? 18.098  -13.663 -23.092 0.76 54.26  ? 103 A1A36 B C3  1 
HETATM 2179 N N   . A1A36 J 4 .  ? 17.806  -13.645 -24.448 0.76 42.66  ? 103 A1A36 B N   1 
HETATM 2180 S S   . A1A36 J 4 .  ? 17.868  -16.108 -23.667 0.76 45.86  ? 103 A1A36 B S   1 
HETATM 2181 C C2  . A1A36 J 4 .  ? 17.660  -14.854 -24.878 0.76 43.75  ? 103 A1A36 B C2  1 
HETATM 2182 C C1  . A1A36 J 4 .  ? 17.337  -15.187 -26.288 0.76 44.26  ? 103 A1A36 B C1  1 
HETATM 2183 C C   . A1A36 J 4 .  ? 17.483  -16.648 -26.603 0.76 36.93  ? 103 A1A36 B C   1 
HETATM 2184 C C1  . EDO   K 3 .  ? 17.346  -36.548 16.356  1.00 57.51  ? 101 EDO   C C1  1 
HETATM 2185 O O1  . EDO   K 3 .  ? 16.251  -37.222 15.766  1.00 66.30  ? 101 EDO   C O1  1 
HETATM 2186 C C2  . EDO   K 3 .  ? 16.977  -35.595 17.430  1.00 53.33  ? 101 EDO   C C2  1 
HETATM 2187 O O2  . EDO   K 3 .  ? 15.930  -36.112 18.206  1.00 47.69  ? 101 EDO   C O2  1 
HETATM 2188 S S   . SO4   L 2 .  ? 29.876  -39.135 12.222  1.00 110.72 ? 102 SO4   C S   1 
HETATM 2189 O O1  . SO4   L 2 .  ? 31.084  -38.770 11.535  1.00 116.75 ? 102 SO4   C O1  1 
HETATM 2190 O O2  . SO4   L 2 .  ? 28.746  -38.583 11.522  1.00 89.61  ? 102 SO4   C O2  1 
HETATM 2191 O O3  . SO4   L 2 .  ? 29.761  -40.570 12.257  1.00 97.00  ? 102 SO4   C O3  1 
HETATM 2192 O O4  . SO4   L 2 .  ? 29.926  -38.620 13.569  1.00 113.31 ? 102 SO4   C O4  1 
HETATM 2193 O O   . HOH   M 5 .  ? 9.734   -32.220 3.953   1.00 59.78  ? 201 HOH   A O   1 
HETATM 2194 O O   . HOH   M 5 .  ? 6.400   -29.120 6.763   1.00 55.94  ? 202 HOH   A O   1 
HETATM 2195 O O   . HOH   M 5 .  ? 4.364   -10.761 13.765  1.00 59.58  ? 203 HOH   A O   1 
HETATM 2196 O O   . HOH   M 5 .  ? -5.100  -13.553 -16.590 1.00 58.49  ? 204 HOH   A O   1 
HETATM 2197 O O   . HOH   M 5 .  ? 0.814   -10.729 -15.202 1.00 56.50  ? 205 HOH   A O   1 
HETATM 2198 O O   . HOH   M 5 .  ? -0.752  -31.273 0.346   1.00 61.55  ? 206 HOH   A O   1 
HETATM 2199 O O   . HOH   M 5 .  ? -1.767  -30.816 -4.019  1.00 53.67  ? 207 HOH   A O   1 
HETATM 2200 O O   . HOH   M 5 .  ? 15.532  -16.988 -19.372 1.00 45.34  ? 208 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 11.488  -29.722 2.929   1.00 53.32  ? 209 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? -3.259  -11.092 6.736   1.00 53.08  ? 210 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? 12.011  -12.305 5.929   1.00 44.19  ? 211 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? 7.291   -10.689 -12.023 1.00 55.56  ? 212 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? 1.717   -24.989 13.879  1.00 63.80  ? 213 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? 11.214  -5.325  -7.758  1.00 40.80  ? 214 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 3.769   -29.631 -0.192  1.00 55.29  ? 215 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? -1.698  3.135   -2.011  1.00 52.63  ? 216 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 8.605   -17.232 8.582   1.00 60.42  ? 217 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 9.745   -19.776 -18.743 1.00 62.23  ? 218 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 20.324  -15.543 7.257   1.00 37.18  ? 219 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? -5.191  -16.054 -7.918  1.00 38.49  ? 220 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 2.778   -25.527 -6.471  1.00 57.23  ? 221 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? -4.549  -25.918 -5.670  1.00 73.30  ? 222 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? -7.214  -21.328 -4.561  1.00 80.35  ? 223 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 16.437  -24.268 1.873   1.00 50.28  ? 224 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 7.068   -6.040  0.207   1.00 57.39  ? 225 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 13.498  -9.348  -7.387  1.00 55.40  ? 226 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? -7.533  -16.025 -1.086  1.00 42.26  ? 227 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 11.674  -23.984 9.798   1.00 53.24  ? 228 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 14.444  -15.731 -9.232  1.00 49.33  ? 229 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 10.419  -13.321 9.615   1.00 48.46  ? 230 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 5.148   -7.947  1.108   1.00 43.25  ? 231 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 10.130  -22.988 -9.337  1.00 64.24  ? 232 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 0.444   -29.503 10.758  1.00 84.31  ? 233 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 1.919   0.395   -7.550  1.00 51.05  ? 234 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? -0.939  -28.763 -6.194  1.00 108.36 ? 235 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 7.609   -7.914  7.043   1.00 56.79  ? 236 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 11.824  -12.419 -6.163  1.00 39.04  ? 237 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -0.184  -20.827 6.925   1.00 39.51  ? 238 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 4.887   -3.571  -3.292  1.00 46.95  ? 239 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? -3.815  -21.393 6.167   1.00 56.98  ? 240 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 1.762   -18.170 -18.657 1.00 59.88  ? 241 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 9.543   -18.068 -11.132 1.00 47.81  ? 242 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 8.764   -17.912 -16.199 1.00 69.87  ? 243 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 2.110   -10.610 11.428  1.00 50.41  ? 244 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 0.342   -33.762 5.032   1.00 63.32  ? 245 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 17.760  -12.967 1.531   1.00 31.00  ? 246 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 2.990   -25.145 -9.946  1.00 51.77  ? 247 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 13.500  -11.969 8.082   1.00 63.96  ? 248 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -5.255  -19.840 -5.581  1.00 57.09  ? 249 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 0.723   -23.602 9.329   1.00 58.50  ? 250 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 13.759  -12.010 -4.147  1.00 28.99  ? 251 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? -1.285  -22.109 -0.566  1.00 36.82  ? 252 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? -6.026  -13.063 6.632   1.00 51.29  ? 253 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 3.212   -6.605  5.630   1.00 50.53  ? 254 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 9.188   -16.207 -13.210 1.00 44.56  ? 255 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -5.371  -27.281 2.943   1.00 59.53  ? 256 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 16.903  -12.159 -17.131 1.00 49.42  ? 257 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 14.049  -28.352 -4.674  1.00 71.51  ? 258 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 2.417   -4.709  -10.338 1.00 53.91  ? 259 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 10.238  -6.087  -1.814  1.00 53.05  ? 260 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -7.989  -19.237 -3.232  1.00 62.56  ? 261 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? -7.553  -17.311 6.583   1.00 49.61  ? 262 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? -5.853  -11.554 -11.372 1.00 45.48  ? 263 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? -1.291  -11.901 11.205  1.00 54.82  ? 264 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 16.123  -11.960 -5.271  1.00 44.36  ? 265 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 8.262   -7.870  1.229   1.00 40.89  ? 266 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? -10.561 -16.318 -3.827  1.00 62.11  ? 267 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -7.561  -16.713 1.713   1.00 47.93  ? 268 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 13.265  -13.578 -8.393  1.00 52.21  ? 269 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 5.633   -7.641  4.090   1.00 45.22  ? 270 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -3.120  -7.269  10.263  1.00 59.25  ? 271 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 17.882  -18.061 -9.508  1.00 61.26  ? 272 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? -7.941  -21.434 -1.446  1.00 49.01  ? 273 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 3.263   -9.762  -13.345 1.00 89.28  ? 274 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 11.489  -7.859  0.392   1.00 36.89  ? 275 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 7.072   -15.898 -14.987 1.00 66.09  ? 276 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 21.910  -16.751 -3.720  1.00 46.51  ? 277 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -6.257  -13.592 -11.590 1.00 60.69  ? 278 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? -1.179  -7.387  11.495  1.00 53.18  ? 279 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 12.521  -20.594 10.606  1.00 56.59  ? 280 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 8.931   -1.819  -0.444  1.00 93.39  ? 281 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? 11.929  -5.636  -3.816  1.00 59.55  ? 282 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -3.124  -7.750  -10.945 1.00 59.69  ? 283 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 4.531   -35.621 4.286   1.00 75.06  ? 284 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -6.915  -11.663 -8.065  1.00 38.56  ? 285 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 9.264   -9.157  -14.009 1.00 46.67  ? 286 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 15.889  -28.336 -0.829  1.00 64.66  ? 287 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -8.577  -15.849 -13.090 1.00 56.90  ? 288 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 22.868  -16.878 -0.596  1.00 46.57  ? 289 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -0.164  -21.318 10.658  1.00 74.26  ? 290 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 10.427  -27.622 -7.681  1.00 66.13  ? 291 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 18.096  -21.358 12.146  1.00 64.00  ? 292 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -5.297  -23.467 -6.891  1.00 55.89  ? 293 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 2.720   -29.711 12.275  1.00 70.69  ? 294 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -3.434  -11.051 9.643   1.00 57.48  ? 295 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 5.288   -7.011  -11.145 1.00 52.36  ? 296 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 14.102  -14.791 -11.735 1.00 70.03  ? 297 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 5.222   3.249   2.817   1.00 66.20  ? 298 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -3.645  -26.582 7.577   1.00 76.17  ? 299 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -6.923  -14.271 -9.192  1.00 48.44  ? 300 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -9.899  -28.443 -1.462  1.00 73.91  ? 301 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 11.813  -1.871  -1.987  1.00 68.25  ? 302 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 23.397  -19.555 -6.076  1.00 60.87  ? 303 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? 8.569   -30.636 -1.066  1.00 73.07  ? 304 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 5.250   -9.614  -11.164 1.00 63.18  ? 305 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -5.504  -23.112 5.713   1.00 62.75  ? 306 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 8.540   -8.433  4.489   1.00 42.10  ? 307 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? -10.945 -13.737 -3.130  1.00 55.72  ? 308 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 6.138   -3.394  1.099   1.00 76.01  ? 309 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -7.123  -19.046 8.559   1.00 72.28  ? 310 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? -4.438  -21.143 -8.210  1.00 54.38  ? 311 HOH   A O   1 
HETATM 2304 O O   . HOH   N 5 .  ? 27.783  -7.848  -29.407 1.00 52.30  ? 201 HOH   B O   1 
HETATM 2305 O O   . HOH   N 5 .  ? 31.256  -12.347 -39.646 1.00 65.26  ? 202 HOH   B O   1 
HETATM 2306 O O   . HOH   N 5 .  ? 6.934   -12.392 -26.256 1.00 49.66  ? 203 HOH   B O   1 
HETATM 2307 O O   . HOH   N 5 .  ? 2.133   -16.401 -32.787 1.00 72.62  ? 204 HOH   B O   1 
HETATM 2308 O O   . HOH   N 5 .  ? 30.553  -8.259  -30.362 1.00 68.98  ? 205 HOH   B O   1 
HETATM 2309 O O   . HOH   N 5 .  ? 11.516  1.427   -39.383 1.00 50.02  ? 206 HOH   B O   1 
HETATM 2310 O O   . HOH   N 5 .  ? 24.351  -1.514  -36.743 1.00 63.39  ? 207 HOH   B O   1 
HETATM 2311 O O   . HOH   N 5 .  ? 26.309  -4.570  -33.788 1.00 74.47  ? 208 HOH   B O   1 
HETATM 2312 O O   . HOH   N 5 .  ? 23.871  -11.051 -22.635 1.00 75.28  ? 209 HOH   B O   1 
HETATM 2313 O O   . HOH   N 5 .  ? 18.761  -0.404  -25.755 1.00 58.80  ? 210 HOH   B O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 26.397  -22.992 -31.613 1.00 48.77  ? 211 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 11.030  -7.869  -41.523 1.00 64.31  ? 212 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 10.201  -11.125 -38.338 1.00 61.70  ? 213 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 20.581  -21.978 -23.594 1.00 57.69  ? 214 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 6.201   -7.899  -32.488 1.00 64.93  ? 215 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 21.053  -25.335 -30.251 1.00 62.35  ? 216 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 23.898  -2.042  -29.711 1.00 77.43  ? 217 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 35.195  -22.525 -30.602 1.00 83.26  ? 218 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 23.643  -3.892  -37.534 1.00 46.69  ? 219 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 21.157  -2.944  -23.917 1.00 90.52  ? 220 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 10.757  -18.703 -33.194 1.00 39.97  ? 221 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 18.141  -0.251  -38.930 1.00 44.91  ? 222 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 20.502  -13.096 -43.221 1.00 54.56  ? 223 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 25.231  -4.745  -30.409 1.00 50.13  ? 224 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 16.605  -9.270  -44.288 1.00 54.40  ? 225 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 29.645  -12.245 -45.304 1.00 82.36  ? 226 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 16.988  -19.137 -29.248 1.00 34.71  ? 227 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 8.491   -27.552 -38.495 1.00 66.73  ? 228 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 27.770  -17.669 -25.664 1.00 68.82  ? 229 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 17.679  -15.716 -46.094 1.00 66.78  ? 230 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 22.705  -23.155 -29.063 1.00 63.45  ? 231 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 8.860   -8.774  -16.680 1.00 54.53  ? 232 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 10.284  -16.563 -44.651 1.00 62.40  ? 233 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 7.289   -19.125 -35.186 1.00 70.56  ? 234 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 10.080  -19.107 -43.218 1.00 73.84  ? 235 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 14.172  -6.281  -41.436 1.00 48.49  ? 236 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 17.477  -19.602 -42.518 1.00 65.82  ? 237 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 21.890  3.876   -33.178 1.00 46.98  ? 238 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 27.449  -10.481 -29.307 1.00 77.06  ? 239 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 13.086  -4.496  -42.191 1.00 68.10  ? 240 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 20.070  -25.517 -34.393 1.00 50.16  ? 241 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 13.994  -22.086 -20.963 1.00 59.25  ? 242 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 7.614   -18.222 -31.884 1.00 67.55  ? 243 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 7.852   -8.088  -21.021 1.00 66.65  ? 244 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 18.752  -25.753 -29.108 1.00 59.08  ? 245 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 21.263  -6.218  -43.001 1.00 47.48  ? 246 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 20.450  -10.078 -43.430 1.00 53.57  ? 247 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 25.226  -5.537  -36.370 1.00 62.69  ? 248 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 26.430  -0.038  -29.925 1.00 59.34  ? 249 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 6.980   -20.486 -25.420 1.00 65.84  ? 250 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 9.773   -5.396  -41.148 1.00 71.17  ? 251 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 26.574  -12.215 -22.507 1.00 57.99  ? 252 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 3.462   -8.269  -27.488 1.00 66.60  ? 253 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 18.779  -2.589  -22.916 1.00 68.24  ? 254 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 1.582   -12.725 -28.695 1.00 63.37  ? 255 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 32.904  -18.841 -43.102 1.00 63.22  ? 256 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 7.257   -12.960 -39.828 1.00 90.22  ? 257 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 18.497  4.735   -34.658 1.00 51.50  ? 258 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 14.694  -24.498 -40.822 1.00 51.85  ? 259 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 10.553  -21.864 -33.010 1.00 56.43  ? 260 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 32.293  -21.684 -38.632 1.00 60.52  ? 261 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 24.931  -6.304  -43.032 1.00 59.49  ? 262 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 28.099  -24.804 -35.435 1.00 48.12  ? 263 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 25.345  -8.152  -23.075 1.00 57.64  ? 264 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 39.004  -13.216 -39.618 1.00 87.13  ? 265 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 7.783   -23.759 -24.302 1.00 63.31  ? 266 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 13.281  -20.009 -19.871 1.00 57.73  ? 267 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 16.720  -26.081 -21.647 1.00 69.93  ? 268 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 14.945  -7.937  -43.327 1.00 50.23  ? 269 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 8.599   -21.387 -27.256 1.00 55.96  ? 270 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 20.304  4.364   -33.470 1.00 43.60  ? 271 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 15.312  -21.755 -42.036 1.00 61.63  ? 272 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 39.166  -16.650 -43.840 1.00 74.69  ? 273 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 7.203   -9.955  -18.704 1.00 63.24  ? 274 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 22.916  -29.342 -35.921 1.00 54.51  ? 275 HOH   B O   1 
HETATM 2379 O O   . HOH   O 5 .  ? 27.283  -38.202 10.079  1.00 57.93  ? 201 HOH   C O   1 
HETATM 2380 O O   . HOH   O 5 .  ? 17.045  -18.803 25.771  1.00 59.04  ? 202 HOH   C O   1 
HETATM 2381 O O   . HOH   O 5 .  ? 26.961  -39.633 12.726  1.00 47.49  ? 203 HOH   C O   1 
HETATM 2382 O O   . HOH   O 5 .  ? 28.346  -37.679 15.709  1.00 55.78  ? 204 HOH   C O   1 
HETATM 2383 O O   . HOH   O 5 .  ? 25.889  -19.609 6.575   1.00 54.92  ? 205 HOH   C O   1 
HETATM 2384 O O   . HOH   O 5 .  ? 13.697  -22.900 28.193  1.00 68.40  ? 206 HOH   C O   1 
HETATM 2385 O O   . HOH   O 5 .  ? 13.391  -31.610 8.142   1.00 43.82  ? 207 HOH   C O   1 
HETATM 2386 O O   . HOH   O 5 .  ? 15.772  -21.423 12.581  1.00 47.47  ? 208 HOH   C O   1 
HETATM 2387 O O   . HOH   O 5 .  ? 17.672  -17.471 15.362  1.00 62.63  ? 209 HOH   C O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 32.117  -33.790 25.907  1.00 69.36  ? 210 HOH   C O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 9.328   -19.280 23.385  1.00 62.88  ? 211 HOH   C O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 20.629  -42.147 12.142  1.00 44.10  ? 212 HOH   C O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 25.937  -31.549 10.876  1.00 46.71  ? 213 HOH   C O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 14.517  -37.425 13.287  1.00 59.98  ? 214 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 9.155   -36.946 17.753  1.00 76.40  ? 215 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 29.623  -15.880 12.778  1.00 72.94  ? 216 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 15.385  -39.451 16.757  1.00 54.40  ? 217 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 18.597  -41.468 39.057  1.00 71.92  ? 218 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 22.705  -34.810 16.588  1.00 38.98  ? 219 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 33.545  -24.867 31.594  1.00 63.12  ? 220 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 25.899  -17.826 14.182  1.00 56.61  ? 221 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 23.339  -41.904 18.457  1.00 52.53  ? 222 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 6.370   -26.474 16.562  1.00 54.11  ? 223 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 7.342   -18.070 10.888  1.00 49.41  ? 224 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 30.512  -36.127 29.080  1.00 65.36  ? 225 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 23.609  -18.746 21.770  1.00 69.39  ? 226 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 22.604  -20.437 24.056  1.00 68.47  ? 227 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 14.854  -29.652 4.147   1.00 63.57  ? 228 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 22.568  -19.465 31.425  1.00 95.88  ? 229 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 22.824  -28.783 11.166  1.00 42.01  ? 230 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 26.372  -18.166 21.093  1.00 58.26  ? 231 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 19.874  -19.980 10.674  1.00 59.55  ? 232 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 8.949   -31.022 11.647  1.00 80.00  ? 233 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 6.348   -34.348 20.034  1.00 67.76  ? 234 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 16.340  -17.793 19.254  1.00 61.75  ? 235 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 11.661  -29.429 27.791  1.00 73.00  ? 236 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 30.074  -40.156 31.544  1.00 57.97  ? 237 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 20.766  -26.865 3.763   1.00 70.21  ? 238 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 31.999  -43.615 16.067  1.00 62.73  ? 239 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 21.016  -40.215 26.609  1.00 54.92  ? 240 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 30.914  -33.040 18.393  1.00 58.62  ? 241 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 28.124  -37.759 25.221  1.00 60.01  ? 242 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 29.193  -25.672 32.843  1.00 70.10  ? 243 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 26.043  -39.936 20.224  1.00 52.98  ? 244 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 21.429  -29.048 8.533   1.00 43.14  ? 245 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 31.047  -16.989 10.038  1.00 63.37  ? 246 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 26.474  -34.840 34.847  1.00 78.97  ? 247 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 30.842  -32.325 15.976  1.00 60.58  ? 248 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 10.221  -30.565 9.844   1.00 45.01  ? 249 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 17.096  -38.362 20.499  1.00 74.60  ? 250 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 31.573  -40.443 27.801  1.00 55.23  ? 251 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 21.639  -29.975 4.655   1.00 76.57  ? 252 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 32.729  -44.219 11.820  1.00 62.99  ? 253 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 5.054   -24.019 18.442  1.00 77.71  ? 254 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 28.383  -44.960 13.516  1.00 78.17  ? 255 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 17.266  -37.022 29.263  1.00 71.02  ? 256 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 13.958  -39.685 9.126   1.00 68.48  ? 257 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 21.116  -13.195 13.320  1.00 47.52  ? 258 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 32.089  -39.501 30.104  1.00 64.40  ? 259 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 8.434   -18.460 25.992  1.00 58.84  ? 260 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 24.430  -15.971 12.196  1.00 62.10  ? 261 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 23.030  -13.861 13.621  1.00 67.05  ? 262 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 36.945  -24.434 27.648  1.00 72.22  ? 263 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 28.911  -41.034 19.538  1.00 80.43  ? 264 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 14.791  -34.714 35.655  1.00 59.14  ? 265 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 28.582  -41.941 29.897  1.00 52.45  ? 266 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 33.934  -44.968 15.394  1.00 49.12  ? 267 HOH   C O   1 
# 
