data_7HHD
# 
_entry.id   7HHD 
# 
_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   7HHD         pdb_00007hhd 10.2210/pdb7hhd/pdb 
WWPDB D_1001407475 ?            ?                   
# 
_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                        7HHD 
_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 '(2R)-1-(cyclohexylamino)propan-2-ol'              157.253   1   ? ?    ? ? 
5 water       nat water                                              18.015    280 ? ?    ? ? 
# 
_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 '(2R)-1-(cyclohexylamino)propan-2-ol' A1A3V 
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 
A1A3V non-polymer         . '(2R)-1-(cyclohexylamino)propan-2-ol' ?                 'C9 H19 N O'     157.253 
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 ?  ?   ?   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        A1A3V 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3V 
_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 A1A3V 1   103 101 A1A3V 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   203 375 HOH   HOH A . 
M 5 HOH   4   204 342 HOH   HOH A . 
M 5 HOH   5   205 339 HOH   HOH A . 
M 5 HOH   6   206 208 HOH   HOH A . 
M 5 HOH   7   207 66  HOH   HOH A . 
M 5 HOH   8   208 304 HOH   HOH A . 
M 5 HOH   9   209 84  HOH   HOH A . 
M 5 HOH   10  210 95  HOH   HOH A . 
M 5 HOH   11  211 55  HOH   HOH A . 
M 5 HOH   12  212 86  HOH   HOH A . 
M 5 HOH   13  213 71  HOH   HOH A . 
M 5 HOH   14  214 293 HOH   HOH A . 
M 5 HOH   15  215 139 HOH   HOH A . 
M 5 HOH   16  216 289 HOH   HOH A . 
M 5 HOH   17  217 37  HOH   HOH A . 
M 5 HOH   18  218 278 HOH   HOH A . 
M 5 HOH   19  219 203 HOH   HOH A . 
M 5 HOH   20  220 290 HOH   HOH A . 
M 5 HOH   21  221 85  HOH   HOH A . 
M 5 HOH   22  222 259 HOH   HOH A . 
M 5 HOH   23  223 260 HOH   HOH A . 
M 5 HOH   24  224 28  HOH   HOH A . 
M 5 HOH   25  225 87  HOH   HOH A . 
M 5 HOH   26  226 21  HOH   HOH A . 
M 5 HOH   27  227 26  HOH   HOH A . 
M 5 HOH   28  228 42  HOH   HOH A . 
M 5 HOH   29  229 8   HOH   HOH A . 
M 5 HOH   30  230 99  HOH   HOH A . 
M 5 HOH   31  231 373 HOH   HOH A . 
M 5 HOH   32  232 179 HOH   HOH A . 
M 5 HOH   33  233 97  HOH   HOH A . 
M 5 HOH   34  234 111 HOH   HOH A . 
M 5 HOH   35  235 7   HOH   HOH A . 
M 5 HOH   36  236 23  HOH   HOH A . 
M 5 HOH   37  237 333 HOH   HOH A . 
M 5 HOH   38  238 12  HOH   HOH A . 
M 5 HOH   39  239 32  HOH   HOH A . 
M 5 HOH   40  240 349 HOH   HOH A . 
M 5 HOH   41  241 93  HOH   HOH A . 
M 5 HOH   42  242 91  HOH   HOH A . 
M 5 HOH   43  243 58  HOH   HOH A . 
M 5 HOH   44  244 34  HOH   HOH A . 
M 5 HOH   45  245 188 HOH   HOH A . 
M 5 HOH   46  246 31  HOH   HOH A . 
M 5 HOH   47  247 288 HOH   HOH A . 
M 5 HOH   48  248 267 HOH   HOH A . 
M 5 HOH   49  249 274 HOH   HOH A . 
M 5 HOH   50  250 60  HOH   HOH A . 
M 5 HOH   51  251 218 HOH   HOH A . 
M 5 HOH   52  252 1   HOH   HOH A . 
M 5 HOH   53  253 370 HOH   HOH A . 
M 5 HOH   54  254 113 HOH   HOH A . 
M 5 HOH   55  255 131 HOH   HOH A . 
M 5 HOH   56  256 368 HOH   HOH A . 
M 5 HOH   57  257 2   HOH   HOH A . 
M 5 HOH   58  258 109 HOH   HOH A . 
M 5 HOH   59  259 292 HOH   HOH A . 
M 5 HOH   60  260 297 HOH   HOH A . 
M 5 HOH   61  261 27  HOH   HOH A . 
M 5 HOH   62  262 190 HOH   HOH A . 
M 5 HOH   63  263 78  HOH   HOH A . 
M 5 HOH   64  264 77  HOH   HOH A . 
M 5 HOH   65  265 337 HOH   HOH A . 
M 5 HOH   66  266 377 HOH   HOH A . 
M 5 HOH   67  267 167 HOH   HOH A . 
M 5 HOH   68  268 300 HOH   HOH A . 
M 5 HOH   69  269 18  HOH   HOH A . 
M 5 HOH   70  270 211 HOH   HOH A . 
M 5 HOH   71  271 20  HOH   HOH A . 
M 5 HOH   72  272 145 HOH   HOH A . 
M 5 HOH   73  273 35  HOH   HOH A . 
M 5 HOH   74  274 64  HOH   HOH A . 
M 5 HOH   75  275 143 HOH   HOH A . 
M 5 HOH   76  276 116 HOH   HOH A . 
M 5 HOH   77  277 359 HOH   HOH A . 
M 5 HOH   78  278 164 HOH   HOH A . 
M 5 HOH   79  279 222 HOH   HOH A . 
M 5 HOH   80  280 73  HOH   HOH A . 
M 5 HOH   81  281 343 HOH   HOH A . 
M 5 HOH   82  282 165 HOH   HOH A . 
M 5 HOH   83  283 115 HOH   HOH A . 
M 5 HOH   84  284 19  HOH   HOH A . 
M 5 HOH   85  285 47  HOH   HOH A . 
M 5 HOH   86  286 287 HOH   HOH A . 
M 5 HOH   87  287 199 HOH   HOH A . 
M 5 HOH   88  288 9   HOH   HOH A . 
M 5 HOH   89  289 301 HOH   HOH A . 
M 5 HOH   90  290 152 HOH   HOH A . 
M 5 HOH   91  291 14  HOH   HOH A . 
M 5 HOH   92  292 75  HOH   HOH A . 
M 5 HOH   93  293 369 HOH   HOH A . 
M 5 HOH   94  294 16  HOH   HOH A . 
M 5 HOH   95  295 281 HOH   HOH A . 
M 5 HOH   96  296 318 HOH   HOH A . 
M 5 HOH   97  297 63  HOH   HOH A . 
M 5 HOH   98  298 327 HOH   HOH A . 
M 5 HOH   99  299 38  HOH   HOH A . 
M 5 HOH   100 300 185 HOH   HOH A . 
M 5 HOH   101 301 94  HOH   HOH A . 
M 5 HOH   102 302 22  HOH   HOH A . 
M 5 HOH   103 303 210 HOH   HOH A . 
M 5 HOH   104 304 296 HOH   HOH A . 
M 5 HOH   105 305 146 HOH   HOH A . 
M 5 HOH   106 306 348 HOH   HOH A . 
M 5 HOH   107 307 83  HOH   HOH A . 
M 5 HOH   108 308 108 HOH   HOH A . 
M 5 HOH   109 309 219 HOH   HOH A . 
M 5 HOH   110 310 205 HOH   HOH A . 
M 5 HOH   111 311 371 HOH   HOH A . 
M 5 HOH   112 312 283 HOH   HOH A . 
M 5 HOH   113 313 344 HOH   HOH A . 
M 5 HOH   114 314 57  HOH   HOH A . 
M 5 HOH   115 315 352 HOH   HOH A . 
M 5 HOH   116 316 156 HOH   HOH A . 
M 5 HOH   117 317 125 HOH   HOH A . 
M 5 HOH   118 318 358 HOH   HOH A . 
M 5 HOH   119 319 332 HOH   HOH A . 
N 5 HOH   1   201 272 HOH   HOH B . 
N 5 HOH   2   202 258 HOH   HOH B . 
N 5 HOH   3   203 247 HOH   HOH B . 
N 5 HOH   4   204 89  HOH   HOH B . 
N 5 HOH   5   205 69  HOH   HOH B . 
N 5 HOH   6   206 98  HOH   HOH B . 
N 5 HOH   7   207 376 HOH   HOH B . 
N 5 HOH   8   208 315 HOH   HOH B . 
N 5 HOH   9   209 123 HOH   HOH B . 
N 5 HOH   10  210 59  HOH   HOH B . 
N 5 HOH   11  211 242 HOH   HOH B . 
N 5 HOH   12  212 153 HOH   HOH B . 
N 5 HOH   13  213 10  HOH   HOH B . 
N 5 HOH   14  214 17  HOH   HOH B . 
N 5 HOH   15  215 335 HOH   HOH B . 
N 5 HOH   16  216 379 HOH   HOH B . 
N 5 HOH   17  217 223 HOH   HOH B . 
N 5 HOH   18  218 150 HOH   HOH B . 
N 5 HOH   19  219 137 HOH   HOH B . 
N 5 HOH   20  220 172 HOH   HOH B . 
N 5 HOH   21  221 6   HOH   HOH B . 
N 5 HOH   22  222 168 HOH   HOH B . 
N 5 HOH   23  223 249 HOH   HOH B . 
N 5 HOH   24  224 101 HOH   HOH B . 
N 5 HOH   25  225 5   HOH   HOH B . 
N 5 HOH   26  226 320 HOH   HOH B . 
N 5 HOH   27  227 24  HOH   HOH B . 
N 5 HOH   28  228 54  HOH   HOH B . 
N 5 HOH   29  229 224 HOH   HOH B . 
N 5 HOH   30  230 177 HOH   HOH B . 
N 5 HOH   31  231 261 HOH   HOH B . 
N 5 HOH   32  232 214 HOH   HOH B . 
N 5 HOH   33  233 96  HOH   HOH B . 
N 5 HOH   34  234 374 HOH   HOH B . 
N 5 HOH   35  235 25  HOH   HOH B . 
N 5 HOH   36  236 120 HOH   HOH B . 
N 5 HOH   37  237 366 HOH   HOH B . 
N 5 HOH   38  238 68  HOH   HOH B . 
N 5 HOH   39  239 169 HOH   HOH B . 
N 5 HOH   40  240 329 HOH   HOH B . 
N 5 HOH   41  241 361 HOH   HOH B . 
N 5 HOH   42  242 280 HOH   HOH B . 
N 5 HOH   43  243 117 HOH   HOH B . 
N 5 HOH   44  244 170 HOH   HOH B . 
N 5 HOH   45  245 61  HOH   HOH B . 
N 5 HOH   46  246 13  HOH   HOH B . 
N 5 HOH   47  247 217 HOH   HOH B . 
N 5 HOH   48  248 104 HOH   HOH B . 
N 5 HOH   49  249 74  HOH   HOH B . 
N 5 HOH   50  250 46  HOH   HOH B . 
N 5 HOH   51  251 372 HOH   HOH B . 
N 5 HOH   52  252 119 HOH   HOH B . 
N 5 HOH   53  253 36  HOH   HOH B . 
N 5 HOH   54  254 197 HOH   HOH B . 
N 5 HOH   55  255 79  HOH   HOH B . 
N 5 HOH   56  256 364 HOH   HOH B . 
N 5 HOH   57  257 182 HOH   HOH B . 
N 5 HOH   58  258 72  HOH   HOH B . 
N 5 HOH   59  259 76  HOH   HOH B . 
N 5 HOH   60  260 215 HOH   HOH B . 
N 5 HOH   61  261 44  HOH   HOH B . 
N 5 HOH   62  262 303 HOH   HOH B . 
N 5 HOH   63  263 157 HOH   HOH B . 
N 5 HOH   64  264 322 HOH   HOH B . 
N 5 HOH   65  265 279 HOH   HOH B . 
N 5 HOH   66  266 331 HOH   HOH B . 
N 5 HOH   67  267 175 HOH   HOH B . 
N 5 HOH   68  268 160 HOH   HOH B . 
N 5 HOH   69  269 291 HOH   HOH B . 
N 5 HOH   70  270 163 HOH   HOH B . 
N 5 HOH   71  271 201 HOH   HOH B . 
N 5 HOH   72  272 378 HOH   HOH B . 
N 5 HOH   73  273 314 HOH   HOH B . 
N 5 HOH   74  274 351 HOH   HOH B . 
N 5 HOH   75  275 107 HOH   HOH B . 
N 5 HOH   76  276 336 HOH   HOH B . 
N 5 HOH   77  277 316 HOH   HOH B . 
N 5 HOH   78  278 312 HOH   HOH B . 
N 5 HOH   79  279 313 HOH   HOH B . 
N 5 HOH   80  280 357 HOH   HOH B . 
O 5 HOH   1   201 254 HOH   HOH C . 
O 5 HOH   2   202 321 HOH   HOH C . 
O 5 HOH   3   203 365 HOH   HOH C . 
O 5 HOH   4   204 334 HOH   HOH C . 
O 5 HOH   5   205 226 HOH   HOH C . 
O 5 HOH   6   206 362 HOH   HOH C . 
O 5 HOH   7   207 323 HOH   HOH C . 
O 5 HOH   8   208 302 HOH   HOH C . 
O 5 HOH   9   209 325 HOH   HOH C . 
O 5 HOH   10  210 363 HOH   HOH C . 
O 5 HOH   11  211 350 HOH   HOH C . 
O 5 HOH   12  212 345 HOH   HOH C . 
O 5 HOH   13  213 330 HOH   HOH C . 
O 5 HOH   14  214 309 HOH   HOH C . 
O 5 HOH   15  215 317 HOH   HOH C . 
O 5 HOH   16  216 118 HOH   HOH C . 
O 5 HOH   17  217 271 HOH   HOH C . 
O 5 HOH   18  218 142 HOH   HOH C . 
O 5 HOH   19  219 126 HOH   HOH C . 
O 5 HOH   20  220 161 HOH   HOH C . 
O 5 HOH   21  221 90  HOH   HOH C . 
O 5 HOH   22  222 341 HOH   HOH C . 
O 5 HOH   23  223 173 HOH   HOH C . 
O 5 HOH   24  224 326 HOH   HOH C . 
O 5 HOH   25  225 15  HOH   HOH C . 
O 5 HOH   26  226 49  HOH   HOH C . 
O 5 HOH   27  227 82  HOH   HOH C . 
O 5 HOH   28  228 151 HOH   HOH C . 
O 5 HOH   29  229 189 HOH   HOH C . 
O 5 HOH   30  230 298 HOH   HOH C . 
O 5 HOH   31  231 269 HOH   HOH C . 
O 5 HOH   32  232 275 HOH   HOH C . 
O 5 HOH   33  233 41  HOH   HOH C . 
O 5 HOH   34  234 148 HOH   HOH C . 
O 5 HOH   35  235 48  HOH   HOH C . 
O 5 HOH   36  236 53  HOH   HOH C . 
O 5 HOH   37  237 45  HOH   HOH C . 
O 5 HOH   38  238 56  HOH   HOH C . 
O 5 HOH   39  239 4   HOH   HOH C . 
O 5 HOH   40  240 134 HOH   HOH C . 
O 5 HOH   41  241 130 HOH   HOH C . 
O 5 HOH   42  242 132 HOH   HOH C . 
O 5 HOH   43  243 40  HOH   HOH C . 
O 5 HOH   44  244 43  HOH   HOH C . 
O 5 HOH   45  245 284 HOH   HOH C . 
O 5 HOH   46  246 102 HOH   HOH C . 
O 5 HOH   47  247 122 HOH   HOH C . 
O 5 HOH   48  248 198 HOH   HOH C . 
O 5 HOH   49  249 299 HOH   HOH C . 
O 5 HOH   50  250 62  HOH   HOH C . 
O 5 HOH   51  251 340 HOH   HOH C . 
O 5 HOH   52  252 294 HOH   HOH C . 
O 5 HOH   53  253 209 HOH   HOH C . 
O 5 HOH   54  254 171 HOH   HOH C . 
O 5 HOH   55  255 184 HOH   HOH C . 
O 5 HOH   56  256 328 HOH   HOH C . 
O 5 HOH   57  257 65  HOH   HOH C . 
O 5 HOH   58  258 135 HOH   HOH C . 
O 5 HOH   59  259 67  HOH   HOH C . 
O 5 HOH   60  260 149 HOH   HOH C . 
O 5 HOH   61  261 354 HOH   HOH C . 
O 5 HOH   62  262 246 HOH   HOH C . 
O 5 HOH   63  263 347 HOH   HOH C . 
O 5 HOH   64  264 305 HOH   HOH C . 
O 5 HOH   65  265 241 HOH   HOH C . 
O 5 HOH   66  266 360 HOH   HOH C . 
O 5 HOH   67  267 355 HOH   HOH C . 
O 5 HOH   68  268 270 HOH   HOH C . 
O 5 HOH   69  269 70  HOH   HOH C . 
O 5 HOH   70  270 324 HOH   HOH C . 
O 5 HOH   71  271 367 HOH   HOH C . 
O 5 HOH   72  272 338 HOH   HOH C . 
O 5 HOH   73  273 346 HOH   HOH C . 
O 5 HOH   74  274 103 HOH   HOH C . 
O 5 HOH   75  275 353 HOH   HOH C . 
O 5 HOH   76  276 310 HOH   HOH C . 
O 5 HOH   77  277 92  HOH   HOH C . 
O 5 HOH   78  278 319 HOH   HOH C . 
O 5 HOH   79  279 295 HOH   HOH C . 
O 5 HOH   80  280 206 HOH   HOH C . 
O 5 HOH   81  281 356 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 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
19 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
20 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
21 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
22 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
23 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
24 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
25 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
26 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
27 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
28 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
29 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
30 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
31 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
32 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
33 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
34 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
35 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
36 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
37 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
38 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
39 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
40 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
41 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
42 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
43 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
44 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
45 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
46 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
47 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
48 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
49 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
50 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
51 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
52 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
53 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
54 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
55 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
56 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
57 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
58 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           7HHD 
_cell.length_a           41.730 
_cell.length_b           42.290 
_cell.length_c           159.860 
_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                         7HHD 
_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          7HHD 
_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                     7HHD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.29 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   40594 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.068 
_reflns.pdbx_netI_over_sigmaI        11.6 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.075 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     251973 
_reflns.pdbx_chi_squared             0.97 
_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                  1.57 
_reflns_shell.d_res_low                   1.61 
_reflns_shell.number_measured_all         15638 
_reflns_shell.number_unique_obs           2945 
_reflns_shell.Rmerge_I_obs                1.783 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             5.3 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.983 
_reflns_shell.pdbx_Rpim_I_all             0.858 
_reflns_shell.pdbx_CC_half                0.309 
_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                                 7HHD 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     38381 
_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                             40.92 
_refine.ls_d_res_high                            1.57 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_R_factor_obs                          0.21117 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20893 
_refine.ls_R_factor_R_free                       0.25108 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2139 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               44.625 
_refine.aniso_B[1][1]                            0.35 
_refine.aniso_B[2][2]                            -0.38 
_refine.aniso_B[3][3]                            0.03 
_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                       0.098 
_refine.pdbx_overall_ESU_R_Free                  0.102 
_refine.overall_SU_ML                            0.095 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.745 
_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        2130 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             280 
_refine_hist.number_atoms_total               2459 
_refine_hist.d_res_high                       1.57 
_refine_hist.d_res_low                        40.92 
# 
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             0.009  0.012  ? 2281 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.824  1.837  ? 3102 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.011  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.126  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.906 10.000 ? 301  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.136  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1866 '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                  3.738  4.230  ? 1069 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.969  7.583  ? 1332 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.914  4.519  ? 1212 '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       8.541  61.10  ? 3539 '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                       1.570 
_refine_ls_shell.d_res_low                        1.611 
_refine_ls_shell.number_reflns_R_work             2760 
_refine_ls_shell.R_factor_R_work                  0.343 
_refine_ls_shell.percent_reflns_obs               99.97 
_refine_ls_shell.R_factor_R_free                  0.359 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             178 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHD 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z90526999' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHD 
_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 7HHD A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHD B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHD 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 7HHD GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHD SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHD GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHD SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHD GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHD 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 ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHD 
_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   A HOH 265 ? ? O A HOH 291 ? ? 1.50 
2  1 O   C HOH 212 ? ? O C HOH 268 ? ? 1.78 
3  1 O   A HOH 231 ? ? O A HOH 263 ? ? 1.87 
4  1 O   B HOH 242 ? ? O B HOH 264 ? ? 1.87 
5  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.93 
6  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 1.95 
7  1 O2  C SO4 102 ? ? O C HOH 202 ? ? 1.98 
8  1 NE2 C HIS 89  ? ? O C HOH 203 ? ? 2.09 
9  1 O4  A SO4 104 ? ? O A HOH 202 ? ? 2.13 
10 1 O   C HOH 265 ? ? O C HOH 266 ? ? 2.14 
11 1 O   A HOH 273 ? ? O A HOH 312 ? ? 2.16 
# 
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 261 ? ? 1_555 O C HOH 272 ? ? 4_445 2.15 
2 1 O A HOH 259 ? ? 1_555 O A HOH 279 ? ? 4_545 2.15 
3 1 O A HOH 305 ? ? 1_555 O C HOH 270 ? ? 4_445 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -151.71 65.04 
2 1 ASN B 38 ? ? 80.08   -0.03 
3 1 ASN B 87 ? ? -157.73 62.00 
# 
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 GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 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 
A1A3V C4   C N N 1   
A1A3V C5   C N N 2   
A1A3V C6   C N N 3   
A1A3V C7   C N N 4   
A1A3V C8   C N N 5   
A1A3V O    O N N 6   
A1A3V C1   C N R 7   
A1A3V C    C N N 8   
A1A3V C2   C N N 9   
A1A3V N    N N N 10  
A1A3V C3   C N N 11  
A1A3V H9   H N N 12  
A1A3V H10  H N N 13  
A1A3V H12  H N N 14  
A1A3V H11  H N N 15  
A1A3V H13  H N N 16  
A1A3V H14  H N N 17  
A1A3V H15  H N N 18  
A1A3V H16  H N N 19  
A1A3V H18  H N N 20  
A1A3V H17  H N N 21  
A1A3V H4   H N N 22  
A1A3V H3   H N N 23  
A1A3V H    H N N 24  
A1A3V H1   H N N 25  
A1A3V H2   H N N 26  
A1A3V H5   H N N 27  
A1A3V H6   H N N 28  
A1A3V H19  H N N 29  
A1A3V H8   H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
EDO   C1   C N N 118 
EDO   O1   O N N 119 
EDO   C2   C N N 120 
EDO   O2   O N N 121 
EDO   H11  H N N 122 
EDO   H12  H N N 123 
EDO   HO1  H N N 124 
EDO   H21  H N N 125 
EDO   H22  H N N 126 
EDO   HO2  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
SO4   S    S N N 344 
SO4   O1   O N N 345 
SO4   O2   O N N 346 
SO4   O3   O N N 347 
SO4   O4   O N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TRP   N    N N N 366 
TRP   CA   C N S 367 
TRP   C    C N N 368 
TRP   O    O N N 369 
TRP   CB   C N N 370 
TRP   CG   C Y N 371 
TRP   CD1  C Y N 372 
TRP   CD2  C Y N 373 
TRP   NE1  N Y N 374 
TRP   CE2  C Y N 375 
TRP   CE3  C Y N 376 
TRP   CZ2  C Y N 377 
TRP   CZ3  C Y N 378 
TRP   CH2  C Y N 379 
TRP   OXT  O N N 380 
TRP   H    H N N 381 
TRP   H2   H N N 382 
TRP   HA   H N N 383 
TRP   HB2  H N N 384 
TRP   HB3  H N N 385 
TRP   HD1  H N N 386 
TRP   HE1  H N N 387 
TRP   HE3  H N N 388 
TRP   HZ2  H N N 389 
TRP   HZ3  H N N 390 
TRP   HH2  H N N 391 
TRP   HXT  H N N 392 
TYR   N    N N N 393 
TYR   CA   C N S 394 
TYR   C    C N N 395 
TYR   O    O N N 396 
TYR   CB   C N N 397 
TYR   CG   C Y N 398 
TYR   CD1  C Y N 399 
TYR   CD2  C Y N 400 
TYR   CE1  C Y N 401 
TYR   CE2  C Y N 402 
TYR   CZ   C Y N 403 
TYR   OH   O N N 404 
TYR   OXT  O N N 405 
TYR   H    H N N 406 
TYR   H2   H N N 407 
TYR   HA   H N N 408 
TYR   HB2  H N N 409 
TYR   HB3  H N N 410 
TYR   HD1  H N N 411 
TYR   HD2  H N N 412 
TYR   HE1  H N N 413 
TYR   HE2  H N N 414 
TYR   HH   H N N 415 
TYR   HXT  H N N 416 
VAL   N    N N N 417 
VAL   CA   C N S 418 
VAL   C    C N N 419 
VAL   O    O N N 420 
VAL   CB   C N N 421 
VAL   CG1  C N N 422 
VAL   CG2  C N N 423 
VAL   OXT  O N N 424 
VAL   H    H N N 425 
VAL   H2   H N N 426 
VAL   HA   H N N 427 
VAL   HB   H N N 428 
VAL   HG11 H N N 429 
VAL   HG12 H N N 430 
VAL   HG13 H N N 431 
VAL   HG21 H N N 432 
VAL   HG22 H N N 433 
VAL   HG23 H N N 434 
VAL   HXT  H N N 435 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A3V C   C1   sing N N 1   
A1A3V C1  O    sing N N 2   
A1A3V C2  C1   sing N N 3   
A1A3V N   C2   sing N N 4   
A1A3V C3  N    sing N N 5   
A1A3V C3  C4   sing N N 6   
A1A3V C4  C5   sing N N 7   
A1A3V C5  C6   sing N N 8   
A1A3V C6  C7   sing N N 9   
A1A3V C7  C8   sing N N 10  
A1A3V C8  C3   sing N N 11  
A1A3V C4  H9   sing N N 12  
A1A3V C4  H10  sing N N 13  
A1A3V C5  H12  sing N N 14  
A1A3V C5  H11  sing N N 15  
A1A3V C6  H13  sing N N 16  
A1A3V C6  H14  sing N N 17  
A1A3V C7  H15  sing N N 18  
A1A3V C7  H16  sing N N 19  
A1A3V C8  H18  sing N N 20  
A1A3V C8  H17  sing N N 21  
A1A3V O   H4   sing N N 22  
A1A3V C1  H3   sing N N 23  
A1A3V C   H    sing N N 24  
A1A3V C   H1   sing N N 25  
A1A3V C   H2   sing N N 26  
A1A3V C2  H5   sing N N 27  
A1A3V C2  H6   sing N N 28  
A1A3V N   H19  sing N N 29  
A1A3V C3  H8   sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
EDO   C1  O1   sing N N 113 
EDO   C1  C2   sing N N 114 
EDO   C1  H11  sing N N 115 
EDO   C1  H12  sing N N 116 
EDO   O1  HO1  sing N N 117 
EDO   C2  O2   sing N N 118 
EDO   C2  H21  sing N N 119 
EDO   C2  H22  sing N N 120 
EDO   O2  HO2  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
SO4   S   O1   doub N N 329 
SO4   S   O2   doub N N 330 
SO4   S   O3   sing N N 331 
SO4   S   O4   sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
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                    7HHD 
_atom_sites.fract_transf_matrix[1][1]   0.023964 
_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]   0.023646 
_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]   0.006255 
_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  ? 0.954   4.298   2.272   1.00 59.55  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.095  3.468   1.620   1.00 63.38  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.549   2.385   0.753   1.00 56.95  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.632   2.569   0.202   1.00 58.92  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.056  4.326   0.786   1.00 67.06  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.058  5.134   1.601   1.00 70.15  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.480  4.267   2.306   1.00 69.11  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.567  5.234   3.821   1.00 73.88  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.114  1.215   0.619   1.00 48.72  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.344   0.138   -0.261  1.00 46.97  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.526   0.518   -1.730  1.00 47.81  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.208  1.329   -2.295  1.00 47.28  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -0.840  -0.875  -0.102  1.00 46.84  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.343  -0.625  1.308   1.00 48.90  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.374  0.884   1.314   1.00 46.67  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.501   -0.132  -2.364  1.00 43.49  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.679   -0.028  -3.796  1.00 44.52  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.117   -1.318  -4.381  1.00 39.54  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.662   -2.192  -3.638  1.00 41.26  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.180   0.081   -4.116  1.00 52.35  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.816   1.378   -3.713  1.00 62.54  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.982   1.777   -2.404  1.00 67.80  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.313   2.374   -4.459  1.00 69.16  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.548   2.975   -2.373  1.00 70.34  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.762   3.355   -3.609  1.00 64.91  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.140   -1.445  -5.701  1.00 37.13  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.933   -2.748  -6.311  1.00 33.83  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.073   -3.691  -5.932  1.00 35.39  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.168   -3.244  -5.555  1.00 36.26  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.893   -2.599  -7.810  1.00 39.72  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.784   -4.986  -6.047  1.00 33.03  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.801   -6.030  -5.911  1.00 34.04  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.940   -5.797  -6.905  1.00 35.04  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.708   -5.377  -8.051  1.00 37.81  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.261   -7.465  -5.983  1.00 34.09  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.448   -7.815  -4.739  1.00 34.98  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.101   -8.030  -3.523  1.00 32.41  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.048   -7.950  -4.780  1.00 32.28  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.442   -8.381  -2.360  1.00 33.34  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.618  -8.329  -3.596  1.00 31.16  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.057   -8.508  -2.405  1.00 32.11  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.167   -6.078  -6.435  1.00 31.92  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.338   -5.987  -7.296  1.00 32.50  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.254   -7.176  -7.001  1.00 30.88  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.221   -7.769  -5.921  1.00 30.03  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.057   -4.662  -6.999  1.00 36.32  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.684   -4.586  -5.636  1.00 38.15  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.362   -3.243  -5.343  1.00 46.19  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.995   -3.277  -3.981  1.00 42.60  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.980   -3.226  -2.919  1.00 42.84  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.146   -7.543  -7.937  1.00 32.77  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.107   -8.610  -7.663  1.00 32.89  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.880   -8.354  -6.378  1.00 29.09  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.316  -7.222  -6.120  1.00 31.69  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 10.004  -8.559  -8.938  1.00 33.97  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 9.041   -8.034  -9.999  1.00 32.72  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.326   -6.890  -9.268  1.00 34.40  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.061  -9.420  -5.590  1.00 30.17  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.754  -9.364  -4.318  1.00 30.36  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.821   -9.218  -3.124  1.00 30.00  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.196  -9.486  -1.979  1.00 29.00  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.551   -8.829  -3.389  1.00 26.88  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.659   -8.770  -2.254  1.00 27.11  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.401   -10.160 -1.644  1.00 26.86  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.296   -11.129 -2.364  1.00 27.32  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.336   -8.184  -2.733  1.00 26.53  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.316   -6.670  -2.882  1.00 31.51  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.265   -5.999  -2.388  1.00 33.10  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.342   -6.163  -3.480  1.00 31.49  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.296   -10.212 -0.306  1.00 27.06  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.131   -11.457 0.450   1.00 25.45  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.660   -11.539 0.856   1.00 26.95  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.080   -10.529 1.304   1.00 31.21  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.031   -11.498 1.688   1.00 28.43  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.519   -11.289 1.348   1.00 28.27  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.389  -11.395 2.634   1.00 28.66  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 10.000  -12.243 0.232   1.00 29.06  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.113   -12.753 0.711   1.00 26.93  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.672   -12.953 0.948   1.00 27.03  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.430   -14.322 1.579   1.00 29.26  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.284   -15.204 1.619   1.00 28.52  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.872   -12.831 -0.367  1.00 27.05  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 3.048   -11.466 -1.036  1.00 28.94  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.299   -13.897 -1.387  1.00 28.90  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.176   -14.535 2.033   1.00 26.49  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.639   -15.878 2.045   1.00 28.45  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.665   -15.967 0.872   1.00 29.36  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.114  -15.026 0.685   1.00 29.23  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.874   -16.263 3.341   1.00 29.42  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.806   -16.359 4.537   1.00 29.72  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.144   -15.191 5.222   1.00 30.37  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.317   -17.602 4.946   1.00 32.17  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 3.027   -15.290 6.296   1.00 39.01  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.205   -17.680 6.029   1.00 33.87  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.540   -16.527 6.680   1.00 34.87  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.769   -17.051 0.081   1.00 27.97  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.006  -17.176 -1.140  1.00 28.23  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -0.983  -18.336 -0.927  1.00 31.23  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.612  -19.374 -0.375  1.00 30.14  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.907   -17.379 -2.345  1.00 29.39  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.257  -18.147 -1.330  1.00 30.87  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.260  -19.188 -1.118  1.00 31.15  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.583  -19.886 -2.441  1.00 33.02  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -3.932  -19.233 -3.405  1.00 36.86  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.487  -18.537 -0.455  1.00 33.00  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.621  -19.555 -0.107  1.00 36.39  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.168  -20.436 1.061   1.00 38.74  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.231  -21.188 1.815   1.00 41.71  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.572  -22.384 1.040   1.00 42.01  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.540  -21.226 -2.397  1.00 34.26  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -3.970  -22.128 -3.453  1.00 37.01  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.063  -23.018 -2.863  1.00 40.01  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.042  -23.325 -1.683  1.00 35.63  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.814  -23.087 -3.768  1.00 38.78  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.490  -22.411 -4.150  1.00 39.03  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.618  -21.851 -5.861  1.00 45.26  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.359  -23.368 -6.746  1.00 41.46  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -5.958  -23.500 -3.724  1.00 41.46  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.033  -24.378 -3.273  1.00 47.21  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.429  -25.627 -2.652  1.00 39.96  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.483  -26.200 -3.186  1.00 43.17  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -7.846  -24.818 -4.496  1.00 53.10  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.079  -25.655 -4.135  1.00 51.24  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.246 -24.729 -3.806  1.00 65.16  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -6.945  -26.008 -1.470  1.00 47.45  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.568  -27.257 -0.831  1.00 44.69  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.261  -27.160 -0.053  1.00 50.72  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -4.804  -28.143 0.521   1.00 50.73  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.634  -25.976 -0.053  1.00 42.35  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.382  -25.828 0.669   1.00 43.54  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.503  -24.714 1.697   1.00 37.62  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.257  -23.765 1.492   1.00 37.31  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.244  -25.409 -0.275  1.00 44.10  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -1.695  -26.454 -1.236  1.00 48.65  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -0.553  -27.180 -0.910  1.00 61.54  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.281  -26.676 -2.478  1.00 56.97  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.027  -28.120 -1.784  1.00 64.56  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -1.756  -27.607 -3.368  1.00 55.42  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -0.626  -28.328 -3.015  1.00 61.57  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.103  -29.264 -3.870  1.00 66.62  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -2.734  -24.768 2.807   1.00 38.86  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -2.699  -23.669 3.775   1.00 36.34  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.021  -22.465 3.101   1.00 34.80  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.277  -22.683 2.162   1.00 35.66  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -1.848  -24.257 4.915   1.00 39.38  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -0.967  -25.285 4.235   1.00 40.88  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -1.842  -25.893 3.166   1.00 41.11  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.319  -21.253 3.563   1.00 34.21  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.629  -20.021 3.146   1.00 30.62  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.118  -20.267 3.256   1.00 32.94  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? 0.360   -20.714 4.295   1.00 32.60  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.070  -18.842 4.029   1.00 31.99  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.516  -18.440 3.830   1.00 30.66  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.541  -19.120 4.471   1.00 37.56  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.107  -17.489 3.053   1.00 33.29  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -5.707  -18.582 4.106   1.00 38.65  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.486  -17.582 3.278   1.00 36.25  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.612   -20.087 2.137   1.00 30.27  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.949   -20.687 2.022   1.00 27.96  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.995   -19.573 1.897   1.00 30.32  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.844   -18.705 1.049   1.00 31.61  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 2.002   -21.550 0.764   1.00 30.15  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 3.114   -22.562 0.849   1.00 30.04  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.451   -22.394 0.605   1.00 32.65  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.912   -23.946 1.195   1.00 34.83  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 5.086   -23.615 0.757   1.00 32.98  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 4.177   -24.568 1.130   1.00 34.68  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.791   -24.702 1.569   1.00 39.67  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.359   -25.924 1.422   1.00 40.77  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.974   -26.050 1.850   1.00 42.69  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 3.239   -26.654 1.762   1.00 46.25  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 4.153   -19.648 2.607   1.00 29.21  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 5.215   -18.636 2.429   1.00 27.92  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.749   -18.590 0.985   1.00 27.30  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 6.063   -19.635 0.395   1.00 28.21  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 6.307   -19.123 3.386   1.00 29.84  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 6.086   -20.628 3.540   1.00 27.95  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.531   -20.728 3.541   1.00 29.32  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.822   -17.389 0.408   1.00 25.91  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 6.153   -17.266 -0.997  1.00 26.55  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.669   -15.864 -1.306  1.00 26.73  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.649   -14.977 -0.456  1.00 26.82  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.891   -17.582 -1.840  1.00 28.11  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 7.179   -15.677 -2.521  1.00 27.08  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.582   -14.352 -2.978  1.00 25.70  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 7.052   -14.077 -4.380  1.00 25.90  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.790   -15.017 -5.144  1.00 28.16  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 9.118   -14.241 -2.953  1.00 27.82  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.812   -15.108 -3.986  1.00 27.73  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 11.354  -14.932 -3.764  1.00 27.62  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 12.018  -15.686 -4.846  1.00 29.72  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 13.296  -16.100 -4.736  1.00 32.08  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.969  -15.985 -3.579  1.00 32.46  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.849  -16.704 -5.774  1.00 33.67  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.910   -12.791 -4.706  1.00 28.07  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.692   -12.423 -6.100  1.00 26.93  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 8.019   -12.543 -6.839  1.00 32.82  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.980   -11.912 -6.431  1.00 30.95  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 6.188   -10.974 -6.188  1.00 30.35  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 5.047   -10.689 -5.197  1.00 33.67  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.814   -10.647 -7.644  1.00 30.67  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.696   -11.268 -5.587  1.00 40.45  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 8.061   -13.369 -7.874  1.00 31.14  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 9.300   -13.548 -8.640  1.00 29.23  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.412   -12.534 -9.773  1.00 35.04  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.464   -11.902 -10.194 1.00 34.09  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.428   -14.943 -9.209  1.00 30.41  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.417  -15.855 -8.515  1.00 34.98  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.965  -15.457 -7.462  1.00 40.71  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.575  -16.968 -8.987  1.00 34.88  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.651  -12.378 -10.283 1.00 39.48  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.900  -11.735 -11.558 1.00 45.29  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.548  -12.723 -12.676 1.00 39.90  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.413  -13.919 -12.452 1.00 40.97  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.369  -11.332 -11.652 1.00 45.94  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.833  -10.166 -10.781 1.00 51.61  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.494  -9.011  -11.109 1.00 53.01  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.549  -10.419 -9.786  1.00 58.03  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.353  -12.206 -13.886 1.00 45.37  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.302  -13.072 -15.062 1.00 41.52  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.644  -12.857 -15.767 1.00 37.43  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 12.004  -11.722 -16.030 1.00 39.95  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 9.134   -12.629 -15.969 1.00 43.98  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.769   -12.656 -15.221 1.00 44.43  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 9.118   -13.454 -17.260 1.00 39.17  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.737   -11.681 -15.744 1.00 48.01  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.378  -13.948 -15.979 1.00 41.94  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.688  -13.891 -16.613 1.00 41.28  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.496  -13.523 -18.088 1.00 39.96  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.454  -13.812 -18.671 1.00 41.67  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.309  -15.259 -16.479 1.00 44.17  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.478  -12.856 -18.711 1.00 38.64  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.431  -12.739 -20.172 1.00 38.38  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.235  -14.133 -20.769 1.00 34.98  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.857  -15.079 -20.323 1.00 40.09  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.753  -12.163 -20.669 1.00 44.92  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 16.054  -10.710 -20.342 1.00 48.06  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 15.105  -9.961  -20.133 1.00 50.71  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 17.259  -10.331 -20.308 1.00 50.12  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.331  -14.237 -21.758 1.00 36.32  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.099  -15.451 -22.525 1.00 36.24  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.183  -16.461 -21.844 1.00 41.81  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.884  -17.491 -22.430 1.00 44.08  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.769  -16.172 -20.602 1.00 40.25  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.902  -17.079 -19.857 1.00 42.66  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.426   -16.814 -20.166 1.00 40.68  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 9.029   -15.713 -20.533 1.00 42.80  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 11.172  -16.869 -18.379 1.00 42.47  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.600   -17.852 -19.940 1.00 43.35  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 7.157   -17.781 -20.129 1.00 49.79  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.558   -16.755 -19.172 1.00 45.23  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.801   -16.854 -17.977 1.00 45.24  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.548   -19.171 -19.845 1.00 48.88  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 5.025   -19.111 -19.884 1.00 50.22  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 7.073   -20.215 -20.824 1.00 53.65  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.771   -15.816 -19.726 1.00 46.00  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 5.103   -14.754 -18.979 1.00 45.00  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.839   -15.300 -18.315 1.00 47.50  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.260   -16.288 -18.763 1.00 48.53  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.806   -13.519 -19.839 1.00 46.72  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 6.045   -12.862 -20.433 1.00 52.00  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.790   -11.582 -21.224 1.00 64.27  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.239   -11.847 -22.597 1.00 64.50  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 5.120   -10.612 -23.376 1.00 66.93  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.384   -14.679 -17.204 1.00 47.98  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 2.136   -15.090 -16.563 1.00 48.67  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.968   -14.627 -17.427 1.00 46.22  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 1.114   -13.721 -18.234 1.00 45.30  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 2.096   -14.362 -15.203 1.00 48.13  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 3.268   -13.389 -15.219 1.00 54.40  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 4.010   -13.520 -16.561 1.00 47.33  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.245  -15.160 -17.199 1.00 46.93  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.454  -14.555 -17.769 1.00 52.74  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.621  -13.095 -17.341 1.00 53.65  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.092  -12.699 -16.299 1.00 43.28  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.581  -15.441 -17.207 1.00 48.46  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -1.924  -16.742 -16.790 1.00 45.12  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.485  -16.399 -16.438 1.00 44.97  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.391  -12.239 -18.067 1.00 47.80  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.706  -10.898 -17.570 1.00 48.92  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.274  -10.903 -16.152 1.00 44.81  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -3.997  -11.818 -15.768 1.00 49.18  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.670  -10.260 -18.596 1.00 58.17  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -3.997  -11.396 -19.535 1.00 47.55  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -2.947  -12.487 -19.417 1.00 55.95  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -2.887  -9.875  -15.389 1.00 46.85  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.347  -9.631  -14.041 1.00 44.19  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -2.904  -10.744 -13.096 1.00 40.82  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.417  -10.791 -11.981 1.00 41.03  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -4.870  -9.521  -13.985 1.00 53.27  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.345  -8.345  -14.809 1.00 60.91  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.069  -7.188  -14.460 1.00 56.29  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.025  -8.625  -15.908 1.00 64.24  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -1.985  -11.632 -13.535 1.00 36.79  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.435  -12.633 -12.617 1.00 30.99  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? 0.071   -12.350 -12.423 1.00 31.02  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.697   -11.598 -13.184 1.00 36.34  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.564  -14.089 -13.072 1.00 36.28  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -2.956  -14.616 -13.546 1.00 41.06  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -3.870  -14.664 -12.336 1.00 42.70  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.311  -15.060 -12.640 1.00 49.08  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.475  -16.516 -12.698 1.00 56.25  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.586   -12.835 -11.294 1.00 30.44  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.975   -12.673 -10.873 1.00 31.46  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.619   -14.047 -10.802 1.00 30.09  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 2.017   -15.031 -10.423 1.00 29.24  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 2.132   -12.059 -9.449  1.00 30.33  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.615   -10.632 -9.443  1.00 33.64  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? 0.246   -10.394 -9.364  1.00 36.97  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.448   -9.550  -9.631  1.00 34.07  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.265  -9.111  -9.470  1.00 38.59  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.947   -8.253  -9.723  1.00 38.17  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.580   -8.037  -9.636  1.00 40.51  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.003  -6.787  -9.761  1.00 39.47  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.935   -14.167 -11.087 1.00 30.25  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.632   -15.435 -10.872 1.00 29.48  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.970   -15.552 -9.389  1.00 28.71  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.638   -14.650 -8.872  1.00 30.44  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.922   -15.285 -11.688 1.00 31.50  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 6.041   -13.840 -12.019 1.00 33.15  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.788   -13.067 -11.565 1.00 34.94  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.411   -16.581 -8.732  1.00 29.82  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.609   -16.787 -7.300  1.00 28.70  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.583   -17.945 -7.093  1.00 30.95  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 5.300   -19.084 -7.524  1.00 32.92  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 3.262   -17.060 -6.611  1.00 30.02  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 2.270   -15.940 -6.903  1.00 29.33  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.521   -17.242 -5.097  1.00 28.09  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.821   -14.557 -6.562  1.00 31.73  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.697   -17.681 -6.371  1.00 28.52  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.616   -18.734 -6.010  1.00 30.56  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 7.321   -19.157 -4.582  1.00 30.59  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.327   -18.332 -3.672  1.00 29.78  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 9.069   -18.228 -6.181  1.00 29.62  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 10.087  -19.265 -5.740  1.00 31.84  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.474  -20.290 -6.624  1.00 35.30  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.640  -19.241 -4.460  1.00 34.11  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.419  -21.241 -6.220  1.00 34.33  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.574  -20.220 -4.054  1.00 35.57  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.954  -21.215 -4.944  1.00 35.61  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 7.025   -20.444 -4.416  1.00 29.39  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.666   -20.971 -3.113  1.00 28.87  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.903   -21.491 -2.396  1.00 33.40  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.600   -22.393 -2.900  1.00 31.51  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.655   -22.113 -3.354  1.00 32.82  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 4.270   -21.623 -3.763  1.00 29.39  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.928   -21.500 -5.097  1.00 35.67  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 3.311   -21.345 -2.795  1.00 32.77  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.654   -21.047 -5.461  1.00 35.41  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 2.031   -20.925 -3.162  1.00 32.97  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.726   -20.729 -4.487  1.00 34.43  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 8.185   -20.892 -1.237  1.00 31.42  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 9.322   -21.391 -0.460  1.00 29.80  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 9.099   -22.845 -0.041  1.00 32.36  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.970   -23.313 0.102   1.00 33.04  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.523   -20.456 0.744   1.00 31.06  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 10.005  -19.077 0.321   1.00 28.59  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 11.307  -18.890 -0.214  1.00 27.34  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 9.255   -17.923 0.586   1.00 30.08  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.699  -17.620 -0.631  1.00 27.06  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.710   -16.644 0.252   1.00 26.94  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.933  -16.493 -0.374  1.00 28.66  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 10.215  -23.550 0.171   1.00 32.05  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 10.185  -24.931 0.677   1.00 30.68  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.969   -25.896 -0.499  1.00 37.86  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.839  -26.698 -0.835  1.00 39.68  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.807   -25.803 -1.167  1.00 38.64  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.535   -26.646 -2.331  1.00 40.10  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 9.353   -26.186 -3.539  1.00 38.49  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.659   -26.967 -4.444  1.00 37.47  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 7.053   -26.705 -2.712  1.00 39.21  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.681   -25.399 -3.152  1.00 36.78  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 6.118   -27.205 -1.634  1.00 38.45  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.640   -24.875 -3.612  1.00 33.41  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 10.327  -24.282 -4.746  1.00 33.35  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.516   -24.415 -6.033  1.00 34.31  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 10.073  -24.338 -7.121  1.00 38.00  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.772  -24.799 -4.919  1.00 32.82  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.494  -24.792 -3.614  1.00 37.80  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 13.347  -25.815 -3.245  1.00 38.63  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.463  -23.925 -2.565  1.00 33.53  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.814  -25.567 -2.034  1.00 45.13  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 13.336  -24.414 -1.619  1.00 40.38  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 8.192   -24.491 -5.871  1.00 33.98  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 7.331   -24.543 -7.048  1.00 34.54  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.874   -23.143 -7.437  1.00 36.28  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 7.011   -22.172 -6.667  1.00 36.13  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 6.123   -25.438 -6.808  1.00 38.98  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 6.541   -26.903 -6.664  1.00 44.38  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 5.456   -27.814 -6.135  1.00 51.28  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 4.282   -27.411 -6.083  1.00 56.53  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.820   -28.948 -5.750  1.00 57.03  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.402   -23.017 -8.683  1.00 34.09  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.888   -21.733 -9.135  1.00 32.51  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.439   -21.929 -9.593  1.00 36.67  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 4.121   -22.933 -10.261 1.00 37.30  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.726   -21.156 -10.281 1.00 40.57  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 8.054   -20.780 -9.911  1.00 39.43  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 6.103   -19.925 -10.934 1.00 45.88  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.582   -20.952 -9.273  1.00 33.59  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 2.231   -20.861 -9.803  1.00 34.56  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.907   -19.402 -10.113 1.00 33.29  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.609   -18.476 -9.676  1.00 34.09  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 1.238   -21.462 -8.818  1.00 34.52  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.868   -19.172 -10.934 1.00 33.17  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.467   -17.829 -11.287 1.00 33.16  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -0.788  -17.476 -10.500 1.00 38.96  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -1.769  -18.224 -10.509 1.00 38.63  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? 0.156   -17.769 -12.787 1.00 37.91  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.339   -18.121 -13.663 1.00 38.35  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.468   -17.303 -13.679 1.00 41.80  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.283   -19.203 -14.535 1.00 42.44  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.563   -17.603 -14.499 1.00 54.07  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.374   -19.497 -15.342 1.00 45.10  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.498   -18.689 -15.348 1.00 43.89  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -0.722  -16.350 -9.779  1.00 31.20  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -1.828  -16.017 -8.878  1.00 29.90  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.117  -14.527 -8.975  1.00 30.98  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.280  -13.678 -9.293  1.00 31.52  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.485  -16.350 -7.417  1.00 34.13  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.420  -17.831 -7.049  1.00 33.24  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.027  -17.935 -5.590  1.00 33.47  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -2.851  -18.441 -7.292  1.00 37.66  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.389  -14.182 -8.725  1.00 28.53  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -3.684  -12.761 -8.655  1.00 29.15  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -3.763  -12.298 -7.190  1.00 26.45  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.740  -13.113 -6.242  1.00 27.21  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -3.887  -10.966 -6.992  1.00 29.29  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -3.811  -10.345 -5.658  1.00 29.46  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -4.783  -10.858 -4.612  1.00 28.67  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.507  -10.804 -3.420  1.00 27.68  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.061  -8.845  -5.951  1.00 30.12  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.473  -8.667  -7.346  1.00 32.96  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -3.867  -9.949  -8.069  1.00 30.31  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -5.934  -11.386 -5.088  1.00 30.04  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -6.886  -11.923 -4.116  1.00 28.92  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.327  -13.073 -3.266  1.00 29.08  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -6.798  -13.363 -2.168  1.00 30.08  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.171  -12.446 -4.794  1.00 33.20  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.016  -13.776 -5.524  1.00 36.48  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.338  -14.163 -6.201  1.00 42.43  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.222  -15.429 -6.986  1.00 43.74  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -8.860  -16.554 -6.124  1.00 50.24  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.253  -13.744 -3.772  1.00 28.89  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -4.693  -14.893 -3.106  1.00 30.44  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.330  -14.529 -2.511  1.00 29.62  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -2.628  -15.434 -2.077  1.00 29.94  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.608  -16.076 -4.075  1.00 30.10  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.013  -16.601 -4.405  1.00 33.04  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -6.833  -16.691 -3.448  1.00 34.86  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.245  -16.988 -5.555  1.00 36.26  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.015  -13.229 -2.459  1.00 27.30  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.684  -12.807 -1.963  1.00 27.40  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -1.843  -11.943 -0.713  1.00 25.24  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.460  -10.856 -0.727  1.00 28.70  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -0.949  -12.065 -3.078  1.00 27.71  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -0.839  -12.840 -4.383  1.00 28.62  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.146  -11.972 -5.417  1.00 30.86  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.019  -14.110 -4.239  1.00 29.25  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.246  -12.417 0.378   1.00 26.49  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.336  -11.733 1.684   1.00 26.82  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? 0.036   -11.222 2.083   1.00 30.67  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.929   -12.033 2.299   1.00 31.45  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -1.769  -12.790 2.708   1.00 28.46  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.227  -13.212 2.485   1.00 29.03  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.563  -14.125 1.498   1.00 31.20  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.226  -12.619 3.263   1.00 30.63  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -4.893  -14.424 1.220   1.00 35.07  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.544  -12.979 3.003   1.00 31.16  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -5.849  -13.876 2.019   1.00 31.29  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? 0.270   -9.908  2.199   1.00 33.08  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.616   -9.440  2.563   1.00 30.74  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 2.145   -10.107 3.831   1.00 29.96  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.464   -10.336 4.838   1.00 30.66  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.359   -7.935  2.692   1.00 32.39  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? 0.318   -7.654  1.587   1.00 34.22  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.659  -8.794  1.896   1.00 33.46  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.450   -10.506 3.812   1.00 30.69  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.966   -11.380 4.843   1.00 27.95  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 4.056   -10.721 6.234   1.00 28.52  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.685   -11.396 7.192   1.00 33.18  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.381   -11.781 4.372   1.00 31.25  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 6.187   -12.564 5.388   1.00 29.93  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.909   -13.906 5.644   1.00 29.56  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 7.221   -11.944 6.084   1.00 37.34  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.621   -14.643 6.592   1.00 34.06  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.934   -12.677 7.017   1.00 35.24  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.633   -13.997 7.279   1.00 34.81  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.383   -14.726 8.203   1.00 36.60  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.418   -9.437  6.253   1.00 32.92  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.631   -8.727  7.513   1.00 38.75  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 3.329   -8.744  8.305   1.00 35.54  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 3.323   -9.321  9.388   1.00 41.94  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.381   -7.408  7.372   1.00 40.65  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.905   -7.514  7.293   1.00 56.68  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 7.460   -8.498  7.838   1.00 66.20  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 7.540   -6.605  6.693   1.00 69.63  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 2.244   -8.302  7.649   1.00 39.72  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.912   -8.241  8.260   1.00 39.58  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? 0.374   -9.606  8.688   1.00 40.71  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.358  -9.682  9.679   1.00 37.06  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? 0.000   -7.641  7.191   1.00 37.84  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.455  -7.399  7.630   1.00 45.16  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.178  -6.654  6.514   1.00 46.17  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.645  -6.445  6.753   1.00 53.46  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.029  -5.987  8.095   1.00 65.97  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.711   -10.685 7.955   1.00 35.31  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? 0.024   -11.970 7.999   1.00 34.21  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.756   -13.087 8.771   1.00 35.17  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? 0.241   -14.197 8.917   1.00 35.98  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.269  -12.448 6.572   1.00 38.47  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.200  -11.547 5.978   1.00 45.22  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 2.030   -12.864 9.124   1.00 34.30  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.872   -13.936 9.619   1.00 37.77  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 2.406   -14.454 10.977  1.00 36.04  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 2.579   -15.631 11.272  1.00 38.35  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 4.355   -13.542 9.611   1.00 36.05  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.711   -12.294 10.375  1.00 38.25  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 6.195   -12.029 10.126  1.00 49.33  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.835   -11.207 11.210  1.00 58.43  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.196   -9.893  11.317  1.00 63.60  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.805   -13.565 11.781  0.50 41.56  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.844   -13.573 11.815  0.50 41.10  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 1.296   -13.923 13.100  0.50 43.76  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 1.321   -14.019 13.101  0.50 42.53  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? 0.178   -14.962 12.988  0.50 44.71  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? 0.294   -15.125 12.863  0.50 43.87  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? 0.040   -15.825 13.845  0.50 44.54  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? 0.346   -16.194 13.473  0.50 41.73  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.884   -12.686 13.884  0.50 45.94  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.739   -12.855 13.890  0.50 45.48  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 2.019   -11.938 14.569  0.50 50.68  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? 0.259   -13.179 15.300  0.50 49.57  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 3.154   -12.455 14.554  0.50 52.48  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 1.117   -13.311 16.204  0.50 54.82  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.766   -10.845 15.116  0.50 55.42  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -0.972  -13.303 15.483  0.50 54.92  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -0.617  -14.875 11.917  1.00 39.13  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -1.696  -15.803 11.657  1.00 36.38  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.210  -17.041 10.914  1.00 39.53  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -1.683  -18.144 11.195  1.00 45.01  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -2.744  -15.034 10.848  1.00 39.23  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -3.989  -15.802 10.589  1.00 39.74  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -4.987  -14.838 9.952   1.00 48.37  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.323  -15.445 9.670   1.00 49.51  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.233  -14.442 9.107   1.00 50.93  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.323  -16.856 9.911   1.00 37.26  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.103  -17.908 8.928   1.00 35.47  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 1.281   -18.556 9.081   1.00 34.39  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 1.530   -19.625 8.536   1.00 38.77  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.284  -17.389 7.486   1.00 33.39  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -1.691  -16.963 7.089   1.00 35.87  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -2.811  -17.711 7.472   1.00 37.12  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -1.888  -15.781 6.385   1.00 35.64  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.081  -17.311 7.105   1.00 38.06  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.162  -15.367 6.031   1.00 37.02  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.255  -16.138 6.393   1.00 38.63  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -5.490  -15.703 6.012   1.00 37.16  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 2.166   -17.920 9.844   1.00 35.65  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 3.550   -18.379 9.935   1.00 36.01  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.787   -19.320 11.113  1.00 40.52  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.652   -19.062 11.926  1.00 47.56  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 3.008   -20.395 11.168  1.00 42.29  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 3.169   -21.458 12.146  1.00 48.79  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 3.472   -22.774 11.428  1.00 39.12  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 3.060   -23.029 10.293  1.00 41.42  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.965   -21.451 13.099  1.00 52.84  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.864   -20.179 13.938  1.00 56.66  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.548   -20.004 14.686  1.00 62.83  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 4.269   -23.695 12.031  1.00 43.44  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 4.538   -24.966 11.370  1.00 41.55  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 3.300   -25.732 10.927  1.00 39.17  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 2.249   -25.624 11.559  1.00 52.96  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 5.403   -25.767 12.392  1.00 46.44  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.969   -24.712 13.315  1.00 49.88  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.968   -23.538 13.317  1.00 52.57  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 3.457   -26.512 9.857   1.00 44.39  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 2.391   -27.253 9.207   1.00 49.97  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 3.001   -28.578 8.765   1.00 57.85  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 4.195   -28.655 8.469   1.00 57.61  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.800   -26.400 8.078   1.00 52.05  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? 0.466   -26.863 7.537   1.00 62.40  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? 0.415   -27.768 6.700   1.00 59.47  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -0.617  -26.189 7.909   1.00 59.51  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 2.180   -29.629 8.731   1.00 56.84  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 2.677   -30.961 8.437   1.00 55.22  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.906   -31.150 6.939   1.00 54.42  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 3.520   -32.135 6.516   1.00 52.20  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 1.668   -31.974 8.994   1.00 67.42  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? 0.312   -32.003 8.292   1.00 63.66  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 2.443   -30.187 6.130   1.00 47.10  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 2.495   -30.356 4.693   1.00 47.65  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.944   -30.281 4.220   1.00 44.34  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 4.733   -29.494 4.755   1.00 43.62  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 1.598   -29.323 3.998   1.00 49.49  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? 0.117   -29.507 4.300   1.00 57.39  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -0.530  -30.742 3.662   1.00 52.91  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -1.024  -30.480 2.306   1.00 61.40  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -2.094  -29.748 1.980   1.00 61.37  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -2.359  -29.537 0.705   1.00 61.91  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -2.890  -29.239 2.906   1.00 57.87  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 4.241   -31.106 3.210   1.00 44.66  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 5.567   -31.274 2.638   1.00 47.29  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 6.124   -29.922 2.186   1.00 43.73  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 5.522   -29.258 1.341   1.00 38.80  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 5.479   -32.283 1.491   1.00 51.86  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.794   -32.605 0.817   1.00 52.92  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.704   -33.711 -0.224  1.00 60.29  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 8.033   -33.919 -0.885  1.00 64.14  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 7.295   -29.573 2.721   1.00 41.84  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 8.001   -28.362 2.313   1.00 38.89  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 7.652   -27.131 3.151   1.00 39.41  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 8.391   -26.151 3.083   1.00 37.86  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 6.563   -27.174 3.931   1.00 36.55  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 6.053   -25.980 4.603   1.00 34.20  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 7.079   -25.403 5.592   1.00 42.27  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 7.362   -24.205 5.601   1.00 37.97  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 4.668   -26.229 5.221   1.00 37.26  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.962   -24.938 5.598   1.00 41.09  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 4.223   -24.274 6.790   1.00 40.43  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 3.009   -24.390 4.734   1.00 42.04  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 3.562   -23.092 7.115   1.00 41.67  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 2.350   -23.214 5.069   1.00 34.25  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 2.626   -22.555 6.245   1.00 36.18  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 7.648   -26.262 6.444   1.00 39.80  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 8.514   -25.776 7.517   1.00 38.84  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.850   -25.301 6.934   1.00 32.94  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 10.415  -24.308 7.439   1.00 36.59  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 8.650   -26.841 8.608   1.00 39.01  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 7.318   -27.114 9.272   1.00 47.28  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 6.426   -26.257 9.258   1.00 40.47  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 7.173   -28.281 9.889   1.00 43.01  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 10.329  -25.946 5.861   1.00 34.22  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 11.513  -25.476 5.161   1.00 33.59  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 11.184  -24.097 4.582   1.00 32.91  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.993  -23.161 4.628   1.00 31.36  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.992  -26.407 4.034   1.00 36.73  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 13.242  -25.933 3.290   1.00 35.85  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 13.766  -26.950 2.260   1.00 44.47  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 13.096  -27.958 1.951   1.00 55.29  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 14.891  -26.757 1.791   1.00 44.65  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.979   -23.987 4.012   1.00 33.11  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 9.579   -22.695 3.462   1.00 34.27  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 9.517   -21.581 4.513   1.00 31.04  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.817   -20.432 4.168   1.00 32.59  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 9.084   -21.874 5.766   1.00 30.27  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 9.090   -20.861 6.810   1.00 32.48  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 10.512  -20.370 7.071   1.00 32.29  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.703  -19.183 7.332   1.00 31.29  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 8.447   -21.339 8.119   1.00 35.61  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.954   -21.680 8.003   1.00 35.68  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 6.543   -22.290 9.334   1.00 39.06  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 6.144   -20.397 7.765   1.00 34.51  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 11.484  -21.305 7.000   1.00 31.90  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.853  -20.933 7.318   1.00 34.54  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 13.343  -20.012 6.204   1.00 30.88  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 14.012  -19.028 6.479   1.00 31.09  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.749  -22.189 7.501   1.00 34.36  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 15.205  -21.848 7.756   1.00 31.50  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.822  -21.768 8.969   1.00 35.20  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 16.189  -21.499 6.761   1.00 33.59  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 17.134  -21.407 8.791   1.00 34.49  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 17.383  -21.223 7.457   1.00 34.71  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 16.191  -21.406 5.361   1.00 34.18  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 18.556  -20.870 6.795   1.00 34.77  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 17.347  -21.025 4.711   1.00 36.83  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 18.514  -20.761 5.425   1.00 37.28  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 13.001  -20.349 4.945   1.00 28.78  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 13.519  -19.612 3.801   1.00 28.28  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 13.002  -18.173 3.837   1.00 30.96  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.753  -17.247 3.609   1.00 28.88  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 13.116  -20.312 2.511   1.00 27.83  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.885  -21.633 2.416   1.00 28.08  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 13.494  -22.367 1.125   1.00 36.87  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 12.584  -21.915 0.404   1.00 34.32  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 14.047  -23.447 0.823   1.00 34.66  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 11.703  -18.011 4.113   1.00 28.36  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 11.134  -16.659 3.991   1.00 28.07  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.649  -15.750 5.131   1.00 27.47  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.805  -14.534 4.940   1.00 30.46  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 9.584   -16.744 3.969   1.00 27.24  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.990   -15.382 3.557   1.00 28.11  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 9.060   -17.090 5.358   1.00 29.57  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 7.540   -15.495 3.059   1.00 27.49  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 12.012  -16.366 6.274   1.00 29.15  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 12.537  -15.594 7.414   1.00 30.24  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 14.038  -15.309 7.278   1.00 31.91  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 14.511  -14.206 7.673   1.00 33.91  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 12.224  -16.347 8.711   1.00 34.54  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 12.739  -15.678 9.979   1.00 41.26  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 12.079  -16.260 11.221  1.00 44.10  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 11.797  -17.471 11.310  1.00 44.65  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.774  -15.378 12.163  1.00 48.91  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.769  -16.262 6.702   1.00 29.36  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 16.220  -16.261 6.820   1.00 27.91  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.951  -15.892 5.533   1.00 30.85  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 18.056  -15.339 5.601   1.00 32.27  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.720  -17.572 7.429   1.00 29.50  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 16.268  -17.660 8.869   1.00 35.80  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 16.648  -16.804 9.690   1.00 36.87  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 15.300  -18.524 9.156   1.00 34.84  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 16.442  -16.269 4.359   1.00 30.02  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 17.070  -15.900 3.111   1.00 29.83  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 16.024  -15.813 1.996   1.00 28.68  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 16.015  -16.585 1.020   1.00 29.76  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 18.238  -16.835 2.758   1.00 30.95  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 19.287  -16.181 1.876   1.00 32.31  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 19.059  -15.193 1.169   1.00 30.98  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 20.494  -16.747 1.861   1.00 35.33  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 15.075  -14.850 2.105   1.00 28.22  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.933  -14.846 1.180   1.00 26.55  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 14.272  -14.406 -0.236  1.00 31.20  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 13.483  -14.625 -1.140  1.00 29.05  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.969  -13.855 1.868   1.00 29.29  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.907  -12.882 2.572   1.00 28.68  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.971  -13.811 3.137   1.00 27.30  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 15.483  -13.831 -0.432  1.00 26.95  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.836  -13.293 -1.743  1.00 27.53  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.941  -14.111 -2.442  1.00 28.13  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 17.396  -13.710 -3.512  1.00 30.90  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 16.231  -11.806 -1.629  1.00 26.60  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 15.137  -10.966 -1.074  1.00 28.72  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.884  -10.878 -1.664  1.00 28.35  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 15.105  -10.261 0.040   1.00 29.25  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 13.133  -10.052 -0.917  1.00 29.47  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.862  -9.673  0.124   1.00 29.34  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 17.217  -15.295 -1.894  1.00 28.54  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 18.292  -16.120 -2.473  1.00 30.43  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.826  -16.874 -3.711  1.00 37.06  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 16.635  -17.037 -3.969  1.00 33.21  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.783  -17.082 -1.449  1.00 30.66  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.819  -17.394 -4.452  1.00 34.52  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 18.543  -18.294 -5.551  1.00 36.33  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 18.287  -19.687 -4.999  1.00 37.55  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 19.124  -20.217 -4.267  1.00 38.45  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.714  -18.285 -6.505  1.00 38.78  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 19.614  -19.459 -7.285  1.00 46.00  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 17.135  -20.271 -5.367  1.00 35.81  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 16.749  -21.595 -4.931  1.00 34.80  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 16.662  -22.505 -6.153  1.00 44.26  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 16.021  -23.540 -6.085  1.00 51.43  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 15.410  -21.587 -4.154  1.00 33.51  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 15.587  -21.013 -2.754  1.00 31.49  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.949  -21.801 -1.662  1.00 32.86  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 15.275  -19.678 -2.514  1.00 31.80  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 16.120  -21.244 -0.396  1.00 37.98  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 15.410  -19.118 -1.265  1.00 32.88  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.805  -19.910 -0.203  1.00 34.14  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.992  -19.370 1.029   1.00 35.73  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 17.383  -22.139 -7.218  1.00 57.75  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 17.427  -22.903 -8.459  1.00 71.32  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 18.636  -23.853 -8.480  1.00 77.87  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 19.476  -23.739 -7.563  1.00 77.33  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.432  -21.996 -9.665  1.00 68.01  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 16.109  -21.567 -9.957  1.00 70.47  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 18.697  -24.677 -9.427  1.00 88.47  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 38.732  -11.213 -42.542 1.00 71.11  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.429  -12.124 -43.675 1.00 65.83  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 36.922  -12.383 -43.677 1.00 64.37  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.376  -12.785 -42.651 1.00 70.54  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.267  -13.406 -43.549 1.00 71.20  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.241  -14.373 -44.738 1.00 82.86  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.073  -13.971 -46.294 1.00 80.63  ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.415  -12.923 -45.723 1.00 55.94  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.199  -12.112 -44.797 1.00 54.69  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 34.749  -12.314 -44.855 1.00 53.74  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.425  -13.765 -44.525 1.00 58.83  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.197  -14.644 -44.873 1.00 57.45  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.389  -11.969 -46.288 1.00 55.82  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.482  -11.016 -46.704 1.00 51.79  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 36.738  -11.563 -46.051 1.00 51.86  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.316  -13.980 -43.806 1.00 55.66  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.872  -15.308 -43.415 1.00 51.77  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.494  -15.554 -44.018 1.00 48.17  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 30.919  -14.661 -44.640 1.00 45.90  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 32.962  -15.449 -41.890 1.00 57.23  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.361  -15.475 -41.358 1.00 63.33  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.360  -16.288 -41.863 1.00 60.69  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 34.909  -14.821 -40.320 1.00 62.82  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.478  -16.098 -41.170 1.00 53.82  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.224  -15.213 -40.227 1.00 68.17  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 30.977  -16.782 -43.854 1.00 44.01  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.638  -17.123 -44.310 1.00 47.96  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.625  -16.101 -43.802 1.00 42.98  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.731  -15.684 -44.534 1.00 48.53  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.289  -18.503 -43.804 1.00 49.57  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.756  -15.738 -42.529 1.00 50.18  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.951  -14.680 -41.937 1.00 51.40  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.824  -13.445 -41.722 1.00 45.52  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.968  -13.553 -41.279 1.00 49.33  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.366  -15.082 -40.577 1.00 48.49  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.317  -16.185 -40.629 1.00 47.30  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 24.973  -15.880 -40.778 1.00 40.83  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.672  -17.528 -40.556 1.00 46.58  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.999  -16.868 -40.834 1.00 46.00  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.692  -18.511 -40.611 1.00 40.06  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.359  -18.195 -40.745 1.00 40.07  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.251  -12.284 -42.051 1.00 48.08  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 28.947  -11.018 -41.860 1.00 43.30  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.212  -10.200 -40.801 1.00 43.32  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 26.982  -10.299 -40.678 1.00 39.58  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 28.992  -10.230 -43.172 1.00 48.40  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.671  -9.878  -43.842 1.00 53.43  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 27.840  -9.309  -45.253 1.00 55.46  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 26.524  -8.946  -45.874 1.00 58.13  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 25.731  -10.138 -46.189 1.00 63.44  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.922  -9.299  -40.083 1.00 47.95  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.279  -8.296  -39.223 1.00 42.51  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.109  -7.606  -39.910 1.00 42.93  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.219  -7.125  -41.050 1.00 44.00  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.483  -7.378  -38.994 1.00 45.01  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.618  -8.366  -38.823 1.00 47.87  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.392  -9.172  -40.084 1.00 52.32  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 25.963  -7.603  -39.206 1.00 39.24  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.725  -6.959  -39.626 1.00 37.26  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.725  -7.927  -40.246 1.00 34.63  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.576  -7.558  -40.487 1.00 38.49  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.186  -9.149  -40.551 1.00 37.56  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.275  -10.160 -41.057 1.00 38.71  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.236  -10.475 -39.967 1.00 32.45  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.579  -10.544 -38.786 1.00 35.86  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 23.973  -11.473 -41.382 1.00 36.49  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.751  -11.528 -42.695 1.00 49.32  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.497  -10.645 -43.547 1.00 44.70  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.610  -12.453 -42.828 1.00 47.12  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.014  -10.653 -40.412 1.00 34.59  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.883  -10.879 -39.517 1.00 33.06  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.604  -12.371 -39.522 1.00 35.09  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.618  -12.967 -40.599 1.00 37.06  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.679  -10.066 -39.959 1.00 34.68  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 18.947  -8.558  -40.097 1.00 36.29  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.631  -7.872  -40.406 1.00 35.87  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.639  -8.025  -38.835 1.00 37.46  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.220  -12.931 -38.353 1.00 34.97  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 19.023  -14.379 -38.252 1.00 32.95  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.944  -14.652 -37.209 1.00 36.18  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.575  -13.750 -36.461 1.00 33.83  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.341  -15.049 -37.806 1.00 33.04  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.446  -14.907 -38.866 1.00 34.22  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.837  -14.626 -36.409 1.00 37.63  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.502  -15.927 -37.138 1.00 34.46  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.995  -16.456 -35.877 1.00 33.72  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 18.106  -17.319 -35.290 1.00 32.28  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.724  -18.083 -36.059 1.00 34.61  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.756  -17.287 -36.166 1.00 33.75  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.545  -16.433 -36.517 1.00 33.47  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.276  -16.095 -37.843 1.00 36.86  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.666  -16.008 -35.519 1.00 34.61  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.153  -15.330 -38.155 1.00 40.36  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.533  -15.258 -35.836 1.00 38.23  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.281  -14.918 -37.155 1.00 40.30  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.370  -17.150 -33.979 1.00 30.74  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.422  -17.868 -33.296 1.00 31.97  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.807  -18.837 -32.282 1.00 35.50  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.848  -18.494 -31.589 1.00 33.60  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.393  -16.904 -32.646 1.00 35.05  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.352  -20.054 -32.227 1.00 32.47  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.776  -21.102 -31.384 1.00 36.93  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.668  -21.306 -30.165 1.00 36.46  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.876  -21.579 -30.276 1.00 35.60  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.594  -22.400 -32.202 1.00 35.28  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 18.002  -23.596 -31.373 1.00 35.22  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 16.553  -23.222 -31.050 1.00 34.47  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.684  -24.241 -30.228 1.00 40.53  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 16.195  -24.382 -28.869 1.00 39.92  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 19.028  -21.188 -28.990 1.00 34.27  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.625  -21.440 -27.685 1.00 39.61  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.839  -22.548 -26.978 1.00 37.31  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.612  -22.591 -27.052 1.00 38.56  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.618  -20.166 -26.826 1.00 40.15  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.485  -19.037 -27.364 1.00 43.86  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 22.259  -19.144 -27.041 1.00 48.66  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 22.328  -18.737 -25.293 1.00 48.53  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.550  -23.435 -26.277 1.00 41.11  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.863  -24.526 -25.588 1.00 42.45  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.872  -23.933 -24.584 1.00 39.23  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 18.231  -23.042 -23.814 1.00 43.23  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.879  -25.351 -24.791 1.00 49.78  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 19.292  -26.568 -24.052 1.00 50.41  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 20.185  -27.057 -22.914 1.00 55.44  ? 16  LYS   B CD  1 
ATOM   881  N N   . GLY   B 1 18 ? 16.627  -24.416 -24.639 1.00 43.41  ? 17  GLY   B N   1 
ATOM   882  C CA  . GLY   B 1 18 ? 15.585  -23.970 -23.719 1.00 44.49  ? 17  GLY   B CA  1 
ATOM   883  C C   . GLY   B 1 18 ? 14.716  -22.849 -24.293 1.00 44.02  ? 17  GLY   B C   1 
ATOM   884  O O   . GLY   B 1 18 ? 13.705  -22.482 -23.694 1.00 43.07  ? 17  GLY   B O   1 
ATOM   885  N N   . TYR   B 1 19 ? 15.087  -22.309 -25.476 1.00 39.04  ? 18  TYR   B N   1 
ATOM   886  C CA  . TYR   B 1 19 ? 14.388  -21.138 -26.003 1.00 36.71  ? 18  TYR   B CA  1 
ATOM   887  C C   . TYR   B 1 19 ? 13.987  -21.376 -27.458 1.00 36.14  ? 18  TYR   B C   1 
ATOM   888  O O   . TYR   B 1 19 ? 14.664  -22.117 -28.167 1.00 38.24  ? 18  TYR   B O   1 
ATOM   889  C CB  . TYR   B 1 19 ? 15.274  -19.882 -26.000 1.00 36.79  ? 18  TYR   B CB  1 
ATOM   890  C CG  . TYR   B 1 19 ? 15.671  -19.581 -24.563 1.00 39.26  ? 18  TYR   B CG  1 
ATOM   891  C CD1 . TYR   B 1 19 ? 14.790  -18.918 -23.709 1.00 42.14  ? 18  TYR   B CD1 1 
ATOM   892  C CD2 . TYR   B 1 19 ? 16.825  -20.130 -24.014 1.00 40.90  ? 18  TYR   B CD2 1 
ATOM   893  C CE1 . TYR   B 1 19 ? 15.110  -18.723 -22.368 1.00 39.85  ? 18  TYR   B CE1 1 
ATOM   894  C CE2 . TYR   B 1 19 ? 17.159  -19.924 -22.684 1.00 45.58  ? 18  TYR   B CE2 1 
ATOM   895  C CZ  . TYR   B 1 19 ? 16.286  -19.241 -21.858 1.00 39.99  ? 18  TYR   B CZ  1 
ATOM   896  O OH  . TYR   B 1 19 ? 16.593  -19.052 -20.539 1.00 45.63  ? 18  TYR   B OH  1 
ATOM   897  N N   . PRO   B 1 20 ? 12.917  -20.725 -27.963 1.00 36.33  ? 19  PRO   B N   1 
ATOM   898  C CA  . PRO   B 1 20 ? 12.541  -20.843 -29.371 1.00 33.09  ? 19  PRO   B CA  1 
ATOM   899  C C   . PRO   B 1 20 ? 13.570  -20.076 -30.198 1.00 32.79  ? 19  PRO   B C   1 
ATOM   900  O O   . PRO   B 1 20 ? 14.235  -19.202 -29.664 1.00 34.68  ? 19  PRO   B O   1 
ATOM   901  C CB  . PRO   B 1 20 ? 11.181  -20.194 -29.498 1.00 36.27  ? 19  PRO   B CB  1 
ATOM   902  C CG  . PRO   B 1 20 ? 11.114  -19.258 -28.308 1.00 37.34  ? 19  PRO   B CG  1 
ATOM   903  C CD  . PRO   B 1 20 ? 12.022  -19.832 -27.219 1.00 36.73  ? 19  PRO   B CD  1 
ATOM   904  N N   . HIS   B 1 21 ? 13.726  -20.489 -31.458 1.00 34.22  ? 20  HIS   B N   1 
ATOM   905  C CA  . HIS   B 1 21 ? 14.541  -19.717 -32.403 1.00 33.70  ? 20  HIS   B CA  1 
ATOM   906  C C   . HIS   B 1 21 ? 14.241  -18.221 -32.234 1.00 31.83  ? 20  HIS   B C   1 
ATOM   907  O O   . HIS   B 1 21 ? 13.087  -17.821 -32.322 1.00 33.17  ? 20  HIS   B O   1 
ATOM   908  C CB  . HIS   B 1 21 ? 14.283  -20.189 -33.842 1.00 33.10  ? 20  HIS   B CB  1 
ATOM   909  C CG  . HIS   B 1 21 ? 14.522  -21.648 -34.056 1.00 34.67  ? 20  HIS   B CG  1 
ATOM   910  N ND1 . HIS   B 1 21 ? 13.645  -22.635 -33.610 1.00 38.25  ? 20  HIS   B ND1 1 
ATOM   911  C CD2 . HIS   B 1 21 ? 15.570  -22.289 -34.572 1.00 37.67  ? 20  HIS   B CD2 1 
ATOM   912  C CE1 . HIS   B 1 21 ? 14.131  -23.833 -33.925 1.00 41.15  ? 20  HIS   B CE1 1 
ATOM   913  N NE2 . HIS   B 1 21 ? 15.297  -23.656 -34.514 1.00 37.13  ? 20  HIS   B NE2 1 
ATOM   914  N N   . TRP   B 1 22 ? 15.292  -17.398 -32.067 1.00 33.99  ? 21  TRP   B N   1 
ATOM   915  C CA  . TRP   B 1 22 ? 15.087  -16.063 -31.491 1.00 31.52  ? 21  TRP   B CA  1 
ATOM   916  C C   . TRP   B 1 22 ? 15.584  -14.993 -32.459 1.00 33.72  ? 21  TRP   B C   1 
ATOM   917  O O   . TRP   B 1 22 ? 16.700  -15.149 -32.952 1.00 32.62  ? 21  TRP   B O   1 
ATOM   918  C CB  . TRP   B 1 22 ? 15.874  -15.922 -30.173 1.00 35.03  ? 21  TRP   B CB  1 
ATOM   919  C CG  . TRP   B 1 22 ? 15.348  -14.797 -29.315 1.00 35.85  ? 21  TRP   B CG  1 
ATOM   920  C CD1 . TRP   B 1 22 ? 15.627  -13.453 -29.404 1.00 34.01  ? 21  TRP   B CD1 1 
ATOM   921  C CD2 . TRP   B 1 22 ? 14.396  -14.937 -28.226 1.00 36.25  ? 21  TRP   B CD2 1 
ATOM   922  N NE1 . TRP   B 1 22 ? 14.884  -12.747 -28.471 1.00 34.48  ? 21  TRP   B NE1 1 
ATOM   923  C CE2 . TRP   B 1 22 ? 14.148  -13.639 -27.722 1.00 34.17  ? 21  TRP   B CE2 1 
ATOM   924  C CE3 . TRP   B 1 22 ? 13.742  -16.040 -27.637 1.00 37.80  ? 21  TRP   B CE3 1 
ATOM   925  C CZ2 . TRP   B 1 22 ? 13.270  -13.408 -26.654 1.00 36.90  ? 21  TRP   B CZ2 1 
ATOM   926  C CZ3 . TRP   B 1 22 ? 12.891  -15.813 -26.571 1.00 36.61  ? 21  TRP   B CZ3 1 
ATOM   927  C CH2 . TRP   B 1 22 ? 12.629  -14.508 -26.114 1.00 37.47  ? 21  TRP   B CH2 1 
ATOM   928  N N   . PRO   B 1 23 ? 14.837  -13.884 -32.733 1.00 32.68  ? 22  PRO   B N   1 
ATOM   929  C CA  . PRO   B 1 23 ? 15.305  -12.879 -33.705 1.00 31.05  ? 22  PRO   B CA  1 
ATOM   930  C C   . PRO   B 1 23 ? 16.610  -12.293 -33.191 1.00 33.83  ? 22  PRO   B C   1 
ATOM   931  O O   . PRO   B 1 23 ? 16.727  -11.891 -32.025 1.00 34.08  ? 22  PRO   B O   1 
ATOM   932  C CB  . PRO   B 1 23 ? 14.168  -11.805 -33.758 1.00 30.65  ? 22  PRO   B CB  1 
ATOM   933  C CG  . PRO   B 1 23 ? 13.456  -12.024 -32.409 1.00 33.04  ? 22  PRO   B CG  1 
ATOM   934  C CD  . PRO   B 1 23 ? 13.513  -13.547 -32.178 1.00 32.51  ? 22  PRO   B CD  1 
ATOM   935  N N   . ALA   B 1 24 ? 17.606  -12.194 -34.079 1.00 31.01  ? 23  ALA   B N   1 
ATOM   936  C CA  . ALA   B 1 24 ? 18.933  -11.811 -33.618 1.00 30.56  ? 23  ALA   B CA  1 
ATOM   937  C C   . ALA   B 1 24 ? 19.751  -11.278 -34.795 1.00 31.77  ? 23  ALA   B C   1 
ATOM   938  O O   . ALA   B 1 24 ? 19.296  -11.338 -35.931 1.00 32.82  ? 23  ALA   B O   1 
ATOM   939  C CB  . ALA   B 1 24 ? 19.653  -12.985 -32.954 1.00 33.09  ? 23  ALA   B CB  1 
ATOM   940  N N   . ARG   B 1 25 ? 20.941  -10.756 -34.485 1.00 35.83  ? 24  ARG   B N   1 
ATOM   941  C CA  . ARG   B 1 25 ? 21.842  -10.280 -35.527 1.00 36.14  ? 24  ARG   B CA  1 
ATOM   942  C C   . ARG   B 1 25 ? 23.263  -10.741 -35.226 1.00 33.11  ? 24  ARG   B C   1 
ATOM   943  O O   . ARG   B 1 25 ? 23.661  -10.975 -34.095 1.00 34.44  ? 24  ARG   B O   1 
ATOM   944  C CB  . ARG   B 1 25 ? 21.822  -8.752  -35.661 1.00 37.77  ? 24  ARG   B CB  1 
ATOM   945  C CG  . ARG   B 1 25 ? 22.374  -7.991  -34.460 1.00 36.45  ? 24  ARG   B CG  1 
ATOM   946  C CD  . ARG   B 1 25 ? 22.159  -6.480  -34.624 1.00 35.52  ? 24  ARG   B CD  1 
ATOM   947  N NE  . ARG   B 1 25 ? 22.829  -5.773  -33.533 1.00 38.15  ? 24  ARG   B NE  1 
ATOM   948  C CZ  . ARG   B 1 25 ? 22.547  -4.515  -33.139 1.00 36.92  ? 24  ARG   B CZ  1 
ATOM   949  N NH1 . ARG   B 1 25 ? 21.539  -3.844  -33.699 1.00 38.43  ? 24  ARG   B NH1 1 
ATOM   950  N NH2 . ARG   B 1 25 ? 23.242  -3.996  -32.143 1.00 39.27  ? 24  ARG   B NH2 1 
ATOM   951  N N   . ILE   B 1 26 ? 24.086  -10.786 -36.282 1.00 32.56  ? 25  ILE   B N   1 
ATOM   952  C CA  . ILE   B 1 26 ? 25.511  -10.977 -36.107 1.00 35.17  ? 25  ILE   B CA  1 
ATOM   953  C C   . ILE   B 1 26 ? 26.085  -9.601  -35.760 1.00 40.97  ? 25  ILE   B C   1 
ATOM   954  O O   . ILE   B 1 26 ? 25.809  -8.655  -36.483 1.00 41.89  ? 25  ILE   B O   1 
ATOM   955  C CB  . ILE   B 1 26 ? 26.129  -11.437 -37.438 1.00 41.73  ? 25  ILE   B CB  1 
ATOM   956  C CG1 . ILE   B 1 26 ? 25.369  -12.599 -38.042 1.00 39.43  ? 25  ILE   B CG1 1 
ATOM   957  C CG2 . ILE   B 1 26 ? 27.617  -11.753 -37.289 1.00 44.51  ? 25  ILE   B CG2 1 
ATOM   958  C CD1 . ILE   B 1 26 ? 25.269  -13.804 -37.117 1.00 39.62  ? 25  ILE   B CD1 1 
ATOM   959  N N   . ASP   B 1 27 ? 26.810  -9.528  -34.640 1.00 38.20  ? 26  ASP   B N   1 
ATOM   960  C CA  . ASP   B 1 27 ? 27.479  -8.287  -34.240 1.00 45.81  ? 26  ASP   B CA  1 
ATOM   961  C C   . ASP   B 1 27 ? 28.909  -8.207  -34.783 1.00 50.67  ? 26  ASP   B C   1 
ATOM   962  O O   . ASP   B 1 27 ? 29.453  -9.188  -35.272 1.00 50.90  ? 26  ASP   B O   1 
ATOM   963  C CB  . ASP   B 1 27 ? 27.520  -8.140  -32.729 1.00 41.63  ? 26  ASP   B CB  1 
ATOM   964  C CG  . ASP   B 1 27 ? 26.333  -7.440  -32.097 1.00 46.81  ? 26  ASP   B CG  1 
ATOM   965  O OD1 . ASP   B 1 27 ? 25.464  -6.966  -32.869 1.00 51.34  ? 26  ASP   B OD1 1 
ATOM   966  O OD2 . ASP   B 1 27 ? 26.297  -7.377  -30.838 1.00 45.34  ? 26  ASP   B OD2 1 
ATOM   967  N N   A ASP   B 1 28 ? 29.504  -7.012  -34.660 0.50 58.28  ? 27  ASP   B N   1 
ATOM   968  N N   B ASP   B 1 28 ? 29.508  -7.012  -34.687 0.50 57.12  ? 27  ASP   B N   1 
ATOM   969  C CA  A ASP   B 1 28 ? 30.909  -6.778  -34.948 0.50 62.96  ? 27  ASP   B CA  1 
ATOM   970  C CA  B ASP   B 1 28 ? 30.916  -6.814  -34.991 0.50 60.91  ? 27  ASP   B CA  1 
ATOM   971  C C   A ASP   B 1 28 ? 31.746  -7.249  -33.759 0.50 64.22  ? 27  ASP   B C   1 
ATOM   972  C C   B ASP   B 1 28 ? 31.709  -6.941  -33.690 0.50 63.58  ? 27  ASP   B C   1 
ATOM   973  O O   A ASP   B 1 28 ? 31.237  -7.884  -32.836 0.50 61.90  ? 27  ASP   B O   1 
ATOM   974  O O   B ASP   B 1 28 ? 31.119  -7.033  -32.616 0.50 62.41  ? 27  ASP   B O   1 
ATOM   975  C CB  A ASP   B 1 28 ? 31.175  -5.305  -35.227 0.50 61.68  ? 27  ASP   B CB  1 
ATOM   976  C CB  B ASP   B 1 28 ? 31.146  -5.477  -35.680 0.50 56.83  ? 27  ASP   B CB  1 
ATOM   977  C CG  A ASP   B 1 28 ? 30.015  -4.516  -35.820 0.50 61.30  ? 27  ASP   B CG  1 
ATOM   978  C CG  B ASP   B 1 28 ? 31.995  -5.526  -36.943 0.50 54.18  ? 27  ASP   B CG  1 
ATOM   979  O OD1 A ASP   B 1 28 ? 30.033  -4.272  -37.047 0.50 61.51  ? 27  ASP   B OD1 1 
ATOM   980  O OD1 B ASP   B 1 28 ? 32.973  -6.300  -36.964 0.50 56.74  ? 27  ASP   B OD1 1 
ATOM   981  O OD2 A ASP   B 1 28 ? 29.106  -4.141  -35.047 0.50 60.82  ? 27  ASP   B OD2 1 
ATOM   982  O OD2 B ASP   B 1 28 ? 31.675  -4.777  -37.892 0.50 49.54  ? 27  ASP   B OD2 1 
ATOM   983  N N   . ILE   B 1 29 ? 33.045  -6.935  -33.795 1.00 70.00  ? 28  ILE   B N   1 
ATOM   984  C CA  . ILE   B 1 29 ? 33.916  -7.148  -32.648 1.00 78.60  ? 28  ILE   B CA  1 
ATOM   985  C C   . ILE   B 1 29 ? 34.517  -5.796  -32.223 1.00 86.71  ? 28  ILE   B C   1 
ATOM   986  O O   . ILE   B 1 29 ? 33.765  -5.007  -31.606 1.00 81.46  ? 28  ILE   B O   1 
ATOM   987  C CB  . ILE   B 1 29 ? 35.007  -8.193  -32.950 1.00 86.01  ? 28  ILE   B CB  1 
ATOM   988  N N   . LYS   B 1 35 ? 37.743  -12.300 -28.188 1.00 81.69  ? 34  LYS   B N   1 
ATOM   989  C CA  . LYS   B 1 35 ? 37.141  -12.635 -29.505 1.00 74.77  ? 34  LYS   B CA  1 
ATOM   990  C C   . LYS   B 1 35 ? 36.227  -13.851 -29.350 1.00 76.05  ? 34  LYS   B C   1 
ATOM   991  O O   . LYS   B 1 35 ? 36.291  -14.559 -28.339 1.00 69.38  ? 34  LYS   B O   1 
ATOM   992  C CB  . LYS   B 1 35 ? 38.261  -12.820 -30.535 1.00 81.96  ? 34  LYS   B CB  1 
ATOM   993  N N   . PRO   B 1 36 ? 35.311  -14.107 -30.319 1.00 67.70  ? 35  PRO   B N   1 
ATOM   994  C CA  . PRO   B 1 36 ? 34.542  -15.354 -30.332 1.00 67.72  ? 35  PRO   B CA  1 
ATOM   995  C C   . PRO   B 1 36 ? 35.444  -16.577 -30.186 1.00 62.32  ? 35  PRO   B C   1 
ATOM   996  O O   . PRO   B 1 36 ? 36.614  -16.518 -30.545 1.00 75.27  ? 35  PRO   B O   1 
ATOM   997  C CB  . PRO   B 1 36 ? 33.798  -15.357 -31.679 1.00 65.63  ? 35  PRO   B CB  1 
ATOM   998  C CG  . PRO   B 1 36 ? 33.868  -13.928 -32.185 1.00 66.56  ? 35  PRO   B CG  1 
ATOM   999  C CD  . PRO   B 1 36 ? 34.936  -13.179 -31.399 1.00 62.74  ? 35  PRO   B CD  1 
ATOM   1000 N N   . PRO   B 1 37 ? 34.946  -17.713 -29.641 1.00 62.11  ? 36  PRO   B N   1 
ATOM   1001 C CA  . PRO   B 1 37 ? 35.665  -18.984 -29.738 1.00 58.61  ? 36  PRO   B CA  1 
ATOM   1002 C C   . PRO   B 1 37 ? 35.734  -19.365 -31.216 1.00 64.81  ? 36  PRO   B C   1 
ATOM   1003 O O   . PRO   B 1 37 ? 34.893  -18.929 -32.001 1.00 63.27  ? 36  PRO   B O   1 
ATOM   1004 C CB  . PRO   B 1 37 ? 34.783  -19.947 -28.923 1.00 61.89  ? 36  PRO   B CB  1 
ATOM   1005 C CG  . PRO   B 1 37 ? 33.950  -19.044 -28.030 1.00 60.59  ? 36  PRO   B CG  1 
ATOM   1006 C CD  . PRO   B 1 37 ? 33.685  -17.831 -28.892 1.00 63.80  ? 36  PRO   B CD  1 
ATOM   1007 N N   . PRO   B 1 38 ? 36.727  -20.172 -31.662 1.00 71.15  ? 37  PRO   B N   1 
ATOM   1008 C CA  . PRO   B 1 38 ? 36.757  -20.651 -33.052 1.00 72.86  ? 37  PRO   B CA  1 
ATOM   1009 C C   . PRO   B 1 38 ? 35.407  -21.166 -33.560 1.00 59.55  ? 37  PRO   B C   1 
ATOM   1010 O O   . PRO   B 1 38 ? 34.677  -21.834 -32.829 1.00 65.75  ? 37  PRO   B O   1 
ATOM   1011 C CB  . PRO   B 1 38 ? 37.848  -21.754 -33.074 1.00 64.90  ? 37  PRO   B CB  1 
ATOM   1012 C CG  . PRO   B 1 38 ? 38.292  -21.911 -31.627 1.00 67.42  ? 37  PRO   B CG  1 
ATOM   1013 C CD  . PRO   B 1 38 ? 37.868  -20.656 -30.868 1.00 70.93  ? 37  PRO   B CD  1 
ATOM   1014 N N   . ASN   B 1 39 ? 35.080  -20.841 -34.816 1.00 61.46  ? 38  ASN   B N   1 
ATOM   1015 C CA  . ASN   B 1 39 ? 33.898  -21.370 -35.496 1.00 64.99  ? 38  ASN   B CA  1 
ATOM   1016 C C   . ASN   B 1 39 ? 32.608  -20.636 -35.096 1.00 54.62  ? 38  ASN   B C   1 
ATOM   1017 O O   . ASN   B 1 39 ? 31.537  -20.980 -35.571 1.00 49.87  ? 38  ASN   B O   1 
ATOM   1018 C CB  . ASN   B 1 39 ? 33.708  -22.876 -35.279 1.00 58.28  ? 38  ASN   B CB  1 
ATOM   1019 C CG  . ASN   B 1 39 ? 34.920  -23.725 -35.606 1.00 66.52  ? 38  ASN   B CG  1 
ATOM   1020 O OD1 . ASN   B 1 39 ? 35.158  -24.743 -34.943 1.00 67.94  ? 38  ASN   B OD1 1 
ATOM   1021 N ND2 . ASN   B 1 39 ? 35.671  -23.364 -36.639 1.00 59.97  ? 38  ASN   B ND2 1 
ATOM   1022 N N   . LYS   B 1 40 ? 32.690  -19.636 -34.209 1.00 58.87  ? 39  LYS   B N   1 
ATOM   1023 C CA  . LYS   B 1 40 ? 31.489  -19.074 -33.608 1.00 49.87  ? 39  LYS   B CA  1 
ATOM   1024 C C   . LYS   B 1 40 ? 31.430  -17.581 -33.901 1.00 46.71  ? 39  LYS   B C   1 
ATOM   1025 O O   . LYS   B 1 40 ? 32.438  -16.996 -34.290 1.00 50.37  ? 39  LYS   B O   1 
ATOM   1026 C CB  . LYS   B 1 40 ? 31.478  -19.407 -32.109 1.00 53.03  ? 39  LYS   B CB  1 
ATOM   1027 C CG  . LYS   B 1 40 ? 31.231  -20.887 -31.838 1.00 50.75  ? 39  LYS   B CG  1 
ATOM   1028 C CD  . LYS   B 1 40 ? 31.029  -21.336 -30.396 1.00 58.75  ? 39  LYS   B CD  1 
ATOM   1029 C CE  . LYS   B 1 40 ? 30.589  -22.764 -30.344 1.00 59.47  ? 39  LYS   B CE  1 
ATOM   1030 N NZ  . LYS   B 1 40 ? 31.350  -23.605 -31.275 1.00 68.38  ? 39  LYS   B NZ  1 
ATOM   1031 N N   . TYR   B 1 41 ? 30.220  -17.000 -33.795 1.00 43.91  ? 40  TYR   B N   1 
ATOM   1032 C CA  . TYR   B 1 41 ? 29.960  -15.603 -34.118 1.00 39.89  ? 40  TYR   B CA  1 
ATOM   1033 C C   . TYR   B 1 41 ? 29.407  -14.884 -32.891 1.00 42.63  ? 40  TYR   B C   1 
ATOM   1034 O O   . TYR   B 1 41 ? 28.670  -15.463 -32.096 1.00 40.05  ? 40  TYR   B O   1 
ATOM   1035 C CB  . TYR   B 1 41 ? 28.896  -15.471 -35.206 1.00 38.85  ? 40  TYR   B CB  1 
ATOM   1036 C CG  . TYR   B 1 41 ? 29.358  -15.945 -36.575 1.00 39.77  ? 40  TYR   B CG  1 
ATOM   1037 C CD1 . TYR   B 1 41 ? 29.987  -15.080 -37.465 1.00 43.26  ? 40  TYR   B CD1 1 
ATOM   1038 C CD2 . TYR   B 1 41 ? 29.118  -17.255 -36.985 1.00 40.04  ? 40  TYR   B CD2 1 
ATOM   1039 C CE1 . TYR   B 1 41 ? 30.376  -15.517 -38.726 1.00 47.31  ? 40  TYR   B CE1 1 
ATOM   1040 C CE2 . TYR   B 1 41 ? 29.515  -17.701 -38.234 1.00 45.99  ? 40  TYR   B CE2 1 
ATOM   1041 C CZ  . TYR   B 1 41 ? 30.154  -16.830 -39.106 1.00 47.68  ? 40  TYR   B CZ  1 
ATOM   1042 O OH  . TYR   B 1 41 ? 30.509  -17.284 -40.351 1.00 42.84  ? 40  TYR   B OH  1 
ATOM   1043 N N   . PRO   B 1 42 ? 29.652  -13.562 -32.743 1.00 43.60  ? 41  PRO   B N   1 
ATOM   1044 C CA  . PRO   B 1 42 ? 28.954  -12.799 -31.706 1.00 40.88  ? 41  PRO   B CA  1 
ATOM   1045 C C   . PRO   B 1 42 ? 27.523  -12.513 -32.130 1.00 38.00  ? 41  PRO   B C   1 
ATOM   1046 O O   . PRO   B 1 42 ? 27.287  -11.917 -33.183 1.00 38.00  ? 41  PRO   B O   1 
ATOM   1047 C CB  . PRO   B 1 42 ? 29.805  -11.517 -31.535 1.00 45.94  ? 41  PRO   B CB  1 
ATOM   1048 C CG  . PRO   B 1 42 ? 30.579  -11.377 -32.837 1.00 46.31  ? 41  PRO   B CG  1 
ATOM   1049 C CD  . PRO   B 1 42 ? 30.613  -12.749 -33.527 1.00 42.83  ? 41  PRO   B CD  1 
ATOM   1050 N N   . ILE   B 1 43 ? 26.568  -12.953 -31.290 1.00 38.06  ? 42  ILE   B N   1 
ATOM   1051 C CA  . ILE   B 1 43 ? 25.138  -12.787 -31.550 1.00 36.99  ? 42  ILE   B CA  1 
ATOM   1052 C C   . ILE   B 1 43 ? 24.558  -11.750 -30.594 1.00 36.72  ? 42  ILE   B C   1 
ATOM   1053 O O   . ILE   B 1 43 ? 24.825  -11.796 -29.417 1.00 41.80  ? 42  ILE   B O   1 
ATOM   1054 C CB  . ILE   B 1 43 ? 24.404  -14.134 -31.386 1.00 36.46  ? 42  ILE   B CB  1 
ATOM   1055 C CG1 . ILE   B 1 43 ? 25.141  -15.230 -32.212 1.00 41.78  ? 42  ILE   B CG1 1 
ATOM   1056 C CG2 . ILE   B 1 43 ? 22.923  -13.995 -31.796 1.00 35.77  ? 42  ILE   B CG2 1 
ATOM   1057 C CD1 . ILE   B 1 43 ? 25.327  -14.890 -33.677 1.00 37.52  ? 42  ILE   B CD1 1 
ATOM   1058 N N   . PHE   B 1 44 ? 23.724  -10.860 -31.112 1.00 35.76  ? 43  PHE   B N   1 
ATOM   1059 C CA  . PHE   B 1 44 ? 22.908  -10.018 -30.247 1.00 35.37  ? 43  PHE   B CA  1 
ATOM   1060 C C   . PHE   B 1 44 ? 21.460  -10.458 -30.427 1.00 36.42  ? 43  PHE   B C   1 
ATOM   1061 O O   . PHE   B 1 44 ? 20.954  -10.481 -31.543 1.00 34.21  ? 43  PHE   B O   1 
ATOM   1062 C CB  . PHE   B 1 44 ? 23.137  -8.555  -30.659 1.00 36.43  ? 43  PHE   B CB  1 
ATOM   1063 C CG  . PHE   B 1 44 ? 22.167  -7.554  -30.027 1.00 38.79  ? 43  PHE   B CG  1 
ATOM   1064 C CD1 . PHE   B 1 44 ? 21.019  -7.155  -30.696 1.00 36.57  ? 43  PHE   B CD1 1 
ATOM   1065 C CD2 . PHE   B 1 44 ? 22.434  -6.963  -28.801 1.00 47.39  ? 43  PHE   B CD2 1 
ATOM   1066 C CE1 . PHE   B 1 44 ? 20.125  -6.253  -30.142 1.00 42.87  ? 43  PHE   B CE1 1 
ATOM   1067 C CE2 . PHE   B 1 44 ? 21.546  -6.037  -28.257 1.00 40.49  ? 43  PHE   B CE2 1 
ATOM   1068 C CZ  . PHE   B 1 44 ? 20.403  -5.690  -28.923 1.00 44.11  ? 43  PHE   B CZ  1 
ATOM   1069 N N   . PHE   B 1 45 ? 20.768  -10.711 -29.310 1.00 35.21  ? 44  PHE   B N   1 
ATOM   1070 C CA  . PHE   B 1 45 ? 19.372  -11.107 -29.337 1.00 36.12  ? 44  PHE   B CA  1 
ATOM   1071 C C   . PHE   B 1 45 ? 18.472  -9.897  -29.197 1.00 32.40  ? 44  PHE   B C   1 
ATOM   1072 O O   . PHE   B 1 45 ? 18.510  -9.177  -28.185 1.00 37.10  ? 44  PHE   B O   1 
ATOM   1073 C CB  . PHE   B 1 45 ? 19.098  -12.121 -28.213 1.00 34.14  ? 44  PHE   B CB  1 
ATOM   1074 C CG  . PHE   B 1 45 ? 19.884  -13.422 -28.351 1.00 33.01  ? 44  PHE   B CG  1 
ATOM   1075 C CD1 . PHE   B 1 45 ? 21.123  -13.577 -27.756 1.00 35.81  ? 44  PHE   B CD1 1 
ATOM   1076 C CD2 . PHE   B 1 45 ? 19.365  -14.494 -29.085 1.00 32.05  ? 44  PHE   B CD2 1 
ATOM   1077 C CE1 . PHE   B 1 45 ? 21.839  -14.753 -27.941 1.00 41.56  ? 44  PHE   B CE1 1 
ATOM   1078 C CE2 . PHE   B 1 45 ? 20.056  -15.681 -29.208 1.00 35.54  ? 44  PHE   B CE2 1 
ATOM   1079 C CZ  . PHE   B 1 45 ? 21.300  -15.800 -28.648 1.00 37.68  ? 44  PHE   B CZ  1 
ATOM   1080 N N   . PHE   B 1 46 ? 17.645  -9.681  -30.226 1.00 33.29  ? 45  PHE   B N   1 
ATOM   1081 C CA  . PHE   B 1 46 ? 16.698  -8.580  -30.166 1.00 32.15  ? 45  PHE   B CA  1 
ATOM   1082 C C   . PHE   B 1 46 ? 15.715  -8.816  -29.003 1.00 36.10  ? 45  PHE   B C   1 
ATOM   1083 O O   . PHE   B 1 46 ? 15.355  -9.947  -28.629 1.00 36.20  ? 45  PHE   B O   1 
ATOM   1084 C CB  . PHE   B 1 46 ? 15.904  -8.341  -31.446 1.00 33.11  ? 45  PHE   B CB  1 
ATOM   1085 C CG  . PHE   B 1 46 ? 16.806  -7.916  -32.595 1.00 36.12  ? 45  PHE   B CG  1 
ATOM   1086 C CD1 . PHE   B 1 46 ? 17.324  -6.613  -32.616 1.00 35.93  ? 45  PHE   B CD1 1 
ATOM   1087 C CD2 . PHE   B 1 46 ? 17.106  -8.791  -33.642 1.00 33.75  ? 45  PHE   B CD2 1 
ATOM   1088 C CE1 . PHE   B 1 46 ? 18.142  -6.216  -33.674 1.00 34.50  ? 45  PHE   B CE1 1 
ATOM   1089 C CE2 . PHE   B 1 46 ? 17.919  -8.382  -34.702 1.00 36.23  ? 45  PHE   B CE2 1 
ATOM   1090 C CZ  . PHE   B 1 46 ? 18.417  -7.087  -34.704 1.00 35.23  ? 45  PHE   B CZ  1 
ATOM   1091 N N   . GLY   B 1 47 ? 15.222  -7.710  -28.465 1.00 35.58  ? 46  GLY   B N   1 
ATOM   1092 C CA  . GLY   B 1 47 ? 14.210  -7.807  -27.416 1.00 34.41  ? 46  GLY   B CA  1 
ATOM   1093 C C   . GLY   B 1 47 ? 14.866  -7.862  -26.039 1.00 38.06  ? 46  GLY   B C   1 
ATOM   1094 O O   . GLY   B 1 47 ? 14.571  -7.015  -25.196 1.00 46.46  ? 46  GLY   B O   1 
ATOM   1095 N N   . THR   B 1 48 ? 15.716  -8.872  -25.793 1.00 38.32  ? 47  THR   B N   1 
ATOM   1096 C CA  . THR   B 1 48 ? 16.372  -9.078  -24.508 1.00 44.14  ? 47  THR   B CA  1 
ATOM   1097 C C   . THR   B 1 48 ? 17.666  -8.275  -24.456 1.00 42.10  ? 47  THR   B C   1 
ATOM   1098 O O   . THR   B 1 48 ? 18.203  -7.984  -23.374 1.00 42.37  ? 47  THR   B O   1 
ATOM   1099 C CB  . THR   B 1 48 ? 16.605  -10.553 -24.127 1.00 44.94  ? 47  THR   B CB  1 
ATOM   1100 O OG1 . THR   B 1 48 ? 17.715  -11.109 -24.830 1.00 41.49  ? 47  THR   B OG1 1 
ATOM   1101 C CG2 . THR   B 1 48 ? 15.396  -11.464 -24.302 1.00 38.51  ? 47  THR   B CG2 1 
ATOM   1102 N N   . HIS   B 1 49 ? 18.196  -7.990  -25.650 1.00 42.07  ? 48  HIS   B N   1 
ATOM   1103 C CA  . HIS   B 1 49 ? 19.433  -7.244  -25.826 1.00 46.18  ? 48  HIS   B CA  1 
ATOM   1104 C C   . HIS   B 1 49 ? 20.604  -7.970  -25.179 1.00 48.13  ? 48  HIS   B C   1 
ATOM   1105 O O   . HIS   B 1 49 ? 21.573  -7.336  -24.799 1.00 50.22  ? 48  HIS   B O   1 
ATOM   1106 C CB  . HIS   B 1 49 ? 19.276  -5.787  -25.372 1.00 43.86  ? 48  HIS   B CB  1 
ATOM   1107 C CG  . HIS   B 1 49 ? 18.038  -5.152  -25.895 1.00 44.38  ? 48  HIS   B CG  1 
ATOM   1108 N ND1 . HIS   B 1 49 ? 17.251  -4.350  -25.102 1.00 44.26  ? 48  HIS   B ND1 1 
ATOM   1109 C CD2 . HIS   B 1 49 ? 17.427  -5.206  -27.092 1.00 42.37  ? 48  HIS   B CD2 1 
ATOM   1110 C CE1 . HIS   B 1 49 ? 16.196  -3.948  -25.800 1.00 52.54  ? 48  HIS   B CE1 1 
ATOM   1111 N NE2 . HIS   B 1 49 ? 16.284  -4.456  -27.020 1.00 48.33  ? 48  HIS   B NE2 1 
ATOM   1112 N N   . GLU   B 1 50 ? 20.518  -9.295  -25.055 1.00 44.34  ? 49  GLU   B N   1 
ATOM   1113 C CA  . GLU   B 1 50 ? 21.639  -10.062 -24.537 1.00 39.36  ? 49  GLU   B CA  1 
ATOM   1114 C C   . GLU   B 1 50 ? 22.541  -10.500 -25.698 1.00 38.81  ? 49  GLU   B C   1 
ATOM   1115 O O   . GLU   B 1 50 ? 22.152  -10.373 -26.869 1.00 39.32  ? 49  GLU   B O   1 
ATOM   1116 C CB  . GLU   B 1 50 ? 21.123  -11.320 -23.840 1.00 45.14  ? 49  GLU   B CB  1 
ATOM   1117 C CG  . GLU   B 1 50 ? 20.319  -10.995 -22.584 1.00 47.44  ? 49  GLU   B CG  1 
ATOM   1118 C CD  . GLU   B 1 50 ? 19.632  -12.243 -22.077 1.00 46.68  ? 49  GLU   B CD  1 
ATOM   1119 O OE1 . GLU   B 1 50 ? 18.649  -12.621 -22.713 1.00 45.59  ? 49  GLU   B OE1 1 
ATOM   1120 O OE2 . GLU   B 1 50 ? 20.062  -12.843 -21.082 1.00 50.61  ? 49  GLU   B OE2 1 
ATOM   1121 N N   . THR   B 1 51 ? 23.680  -11.095 -25.328 1.00 39.51  ? 50  THR   B N   1 
ATOM   1122 C CA  . THR   B 1 51 ? 24.674  -11.552 -26.289 1.00 39.60  ? 50  THR   B CA  1 
ATOM   1123 C C   . THR   B 1 51 ? 25.153  -12.953 -25.939 1.00 47.66  ? 50  THR   B C   1 
ATOM   1124 O O   . THR   B 1 51 ? 25.146  -13.353 -24.785 1.00 49.14  ? 50  THR   B O   1 
ATOM   1125 C CB  . THR   B 1 51 ? 25.829  -10.557 -26.459 1.00 43.90  ? 50  THR   B CB  1 
ATOM   1126 O OG1 . THR   B 1 51 ? 26.402  -10.377 -25.169 1.00 48.01  ? 50  THR   B OG1 1 
ATOM   1127 C CG2 . THR   B 1 51 ? 25.388  -9.178  -26.909 1.00 42.33  ? 50  THR   B CG2 1 
ATOM   1128 N N   . ALA   B 1 52 ? 25.579  -13.697 -26.966 1.00 44.34  ? 51  ALA   B N   1 
ATOM   1129 C CA  . ALA   B 1 52 ? 26.204  -14.995 -26.784 1.00 44.84  ? 51  ALA   B CA  1 
ATOM   1130 C C   . ALA   B 1 52 ? 27.073  -15.281 -27.999 1.00 41.82  ? 51  ALA   B C   1 
ATOM   1131 O O   . ALA   B 1 52 ? 27.012  -14.551 -28.992 1.00 42.00  ? 51  ALA   B O   1 
ATOM   1132 C CB  . ALA   B 1 52 ? 25.176  -16.093 -26.590 1.00 44.45  ? 51  ALA   B CB  1 
ATOM   1133 N N   . PHE   B 1 53 ? 27.865  -16.345 -27.889 1.00 42.79  ? 52  PHE   B N   1 
ATOM   1134 C CA  . PHE   B 1 53 ? 28.558  -16.860 -29.055 1.00 44.58  ? 52  PHE   B CA  1 
ATOM   1135 C C   . PHE   B 1 53 ? 27.885  -18.147 -29.537 1.00 40.63  ? 52  PHE   B C   1 
ATOM   1136 O O   . PHE   B 1 53 ? 27.663  -19.092 -28.776 1.00 43.43  ? 52  PHE   B O   1 
ATOM   1137 C CB  . PHE   B 1 53 ? 30.034  -17.086 -28.711 1.00 42.03  ? 52  PHE   B CB  1 
ATOM   1138 C CG  . PHE   B 1 53 ? 30.840  -15.850 -28.323 1.00 47.17  ? 52  PHE   B CG  1 
ATOM   1139 C CD1 . PHE   B 1 53 ? 31.130  -14.867 -29.262 1.00 52.25  ? 52  PHE   B CD1 1 
ATOM   1140 C CD2 . PHE   B 1 53 ? 31.366  -15.719 -27.041 1.00 52.03  ? 52  PHE   B CD2 1 
ATOM   1141 C CE1 . PHE   B 1 53 ? 31.882  -13.751 -28.922 1.00 50.50  ? 52  PHE   B CE1 1 
ATOM   1142 C CE2 . PHE   B 1 53 ? 32.126  -14.601 -26.701 1.00 52.75  ? 52  PHE   B CE2 1 
ATOM   1143 C CZ  . PHE   B 1 53 ? 32.386  -13.631 -27.642 1.00 54.82  ? 52  PHE   B CZ  1 
ATOM   1144 N N   . LEU   B 1 54 ? 27.574  -18.192 -30.835 1.00 40.91  ? 53  LEU   B N   1 
ATOM   1145 C CA  . LEU   B 1 54 ? 26.921  -19.345 -31.422 1.00 37.16  ? 53  LEU   B CA  1 
ATOM   1146 C C   . LEU   B 1 54 ? 27.653  -19.706 -32.706 1.00 39.94  ? 53  LEU   B C   1 
ATOM   1147 O O   . LEU   B 1 54 ? 28.186  -18.822 -33.385 1.00 41.96  ? 53  LEU   B O   1 
ATOM   1148 C CB  . LEU   B 1 54 ? 25.432  -19.176 -31.729 1.00 38.48  ? 53  LEU   B CB  1 
ATOM   1149 C CG  . LEU   B 1 54 ? 24.502  -19.108 -30.524 1.00 37.93  ? 53  LEU   B CG  1 
ATOM   1150 C CD1 . LEU   B 1 54 ? 23.108  -18.797 -31.001 1.00 36.80  ? 53  LEU   B CD1 1 
ATOM   1151 C CD2 . LEU   B 1 54 ? 24.604  -20.471 -29.830 1.00 41.42  ? 53  LEU   B CD2 1 
ATOM   1152 N N   . GLY   B 1 55 ? 27.594  -21.006 -33.021 1.00 39.89  ? 54  GLY   B N   1 
ATOM   1153 C CA  . GLY   B 1 55 ? 28.121  -21.586 -34.246 1.00 40.80  ? 54  GLY   B CA  1 
ATOM   1154 C C   . GLY   B 1 55 ? 27.048  -21.618 -35.327 1.00 37.89  ? 54  GLY   B C   1 
ATOM   1155 O O   . GLY   B 1 55 ? 25.851  -21.477 -35.050 1.00 38.63  ? 54  GLY   B O   1 
ATOM   1156 N N   . PRO   B 1 56 ? 27.430  -21.790 -36.613 1.00 38.97  ? 55  PRO   B N   1 
ATOM   1157 C CA  . PRO   B 1 56 ? 26.437  -21.925 -37.681 1.00 35.37  ? 55  PRO   B CA  1 
ATOM   1158 C C   . PRO   B 1 56 ? 25.238  -22.860 -37.556 1.00 34.43  ? 55  PRO   B C   1 
ATOM   1159 O O   . PRO   B 1 56 ? 24.180  -22.562 -38.094 1.00 36.09  ? 55  PRO   B O   1 
ATOM   1160 C CB  . PRO   B 1 56 ? 27.283  -22.193 -38.966 1.00 39.82  ? 55  PRO   B CB  1 
ATOM   1161 C CG  . PRO   B 1 56 ? 28.722  -21.961 -38.589 1.00 46.97  ? 55  PRO   B CG  1 
ATOM   1162 C CD  . PRO   B 1 56 ? 28.828  -21.828 -37.093 1.00 41.77  ? 55  PRO   B CD  1 
ATOM   1163 N N   . LYS   B 1 57 ? 25.390  -23.993 -36.852 1.00 34.27  ? 56  LYS   B N   1 
ATOM   1164 C CA  . LYS   B 1 57 ? 24.292  -24.940 -36.776 1.00 37.06  ? 56  LYS   B CA  1 
ATOM   1165 C C   . LYS   B 1 57 ? 23.087  -24.314 -36.088 1.00 37.64  ? 56  LYS   B C   1 
ATOM   1166 O O   . LYS   B 1 57 ? 21.977  -24.814 -36.213 1.00 36.59  ? 56  LYS   B O   1 
ATOM   1167 C CB  . LYS   B 1 57 ? 24.735  -26.187 -35.998 1.00 44.17  ? 56  LYS   B CB  1 
ATOM   1168 C CG  . LYS   B 1 57 ? 24.895  -26.031 -34.487 1.00 50.32  ? 56  LYS   B CG  1 
ATOM   1169 C CD  . LYS   B 1 57 ? 25.106  -27.376 -33.793 1.00 57.18  ? 56  LYS   B CD  1 
ATOM   1170 C CE  . LYS   B 1 57 ? 25.411  -27.292 -32.326 1.00 57.11  ? 56  LYS   B CE  1 
ATOM   1171 N NZ  . LYS   B 1 57 ? 24.262  -26.911 -31.505 1.00 54.95  ? 56  LYS   B NZ  1 
ATOM   1172 N N   . ASP   B 1 58 ? 23.325  -23.205 -35.358 1.00 35.00  ? 57  ASP   B N   1 
ATOM   1173 C CA  . ASP   B 1 58 ? 22.277  -22.610 -34.540 1.00 34.92  ? 57  ASP   B CA  1 
ATOM   1174 C C   . ASP   B 1 58 ? 21.818  -21.279 -35.139 1.00 35.13  ? 57  ASP   B C   1 
ATOM   1175 O O   . ASP   B 1 58 ? 21.085  -20.533 -34.477 1.00 34.74  ? 57  ASP   B O   1 
ATOM   1176 C CB  . ASP   B 1 58 ? 22.773  -22.477 -33.110 1.00 36.47  ? 57  ASP   B CB  1 
ATOM   1177 C CG  . ASP   B 1 58 ? 22.929  -23.807 -32.376 1.00 41.75  ? 57  ASP   B CG  1 
ATOM   1178 O OD1 . ASP   B 1 58 ? 21.986  -24.641 -32.494 1.00 39.61  ? 57  ASP   B OD1 1 
ATOM   1179 O OD2 . ASP   B 1 58 ? 23.941  -23.945 -31.657 1.00 44.64  ? 57  ASP   B OD2 1 
ATOM   1180 N N   . LEU   B 1 59 ? 22.294  -20.971 -36.374 1.00 35.65  ? 58  LEU   B N   1 
ATOM   1181 C CA  . LEU   B 1 59 ? 22.026  -19.667 -36.993 1.00 35.10  ? 58  LEU   B CA  1 
ATOM   1182 C C   . LEU   B 1 59 ? 21.250  -19.853 -38.294 1.00 33.92  ? 58  LEU   B C   1 
ATOM   1183 O O   . LEU   B 1 59 ? 21.718  -20.529 -39.231 1.00 36.01  ? 58  LEU   B O   1 
ATOM   1184 C CB  . LEU   B 1 59 ? 23.342  -18.932 -37.227 1.00 34.84  ? 58  LEU   B CB  1 
ATOM   1185 C CG  . LEU   B 1 59 ? 24.171  -18.620 -35.977 1.00 34.12  ? 58  LEU   B CG  1 
ATOM   1186 C CD1 . LEU   B 1 59 ? 25.464  -17.917 -36.396 1.00 37.01  ? 58  LEU   B CD1 1 
ATOM   1187 C CD2 . LEU   B 1 59 ? 23.432  -17.784 -34.899 1.00 37.03  ? 58  LEU   B CD2 1 
ATOM   1188 N N   . PHE   B 1 60 ? 20.053  -19.267 -38.347 1.00 31.98  ? 59  PHE   B N   1 
ATOM   1189 C CA  . PHE   B 1 60 ? 19.109  -19.447 -39.435 1.00 34.48  ? 59  PHE   B CA  1 
ATOM   1190 C C   . PHE   B 1 60 ? 18.889  -18.098 -40.116 1.00 33.76  ? 59  PHE   B C   1 
ATOM   1191 O O   . PHE   B 1 60 ? 18.277  -17.195 -39.535 1.00 33.25  ? 59  PHE   B O   1 
ATOM   1192 C CB  . PHE   B 1 60 ? 17.776  -19.989 -38.898 1.00 32.10  ? 59  PHE   B CB  1 
ATOM   1193 C CG  . PHE   B 1 60 ? 17.914  -21.399 -38.307 1.00 33.89  ? 59  PHE   B CG  1 
ATOM   1194 C CD1 . PHE   B 1 60 ? 18.475  -21.569 -37.040 1.00 34.94  ? 59  PHE   B CD1 1 
ATOM   1195 C CD2 . PHE   B 1 60 ? 17.454  -22.505 -39.012 1.00 36.33  ? 59  PHE   B CD2 1 
ATOM   1196 C CE1 . PHE   B 1 60 ? 18.620  -22.838 -36.491 1.00 38.05  ? 59  PHE   B CE1 1 
ATOM   1197 C CE2 . PHE   B 1 60 ? 17.594  -23.781 -38.457 1.00 36.20  ? 59  PHE   B CE2 1 
ATOM   1198 C CZ  . PHE   B 1 60 ? 18.194  -23.937 -37.217 1.00 38.47  ? 59  PHE   B CZ  1 
ATOM   1199 N N   . PRO   B 1 61 ? 19.349  -17.907 -41.373 1.00 36.57  ? 60  PRO   B N   1 
ATOM   1200 C CA  . PRO   B 1 61 ? 19.127  -16.616 -42.048 1.00 36.01  ? 60  PRO   B CA  1 
ATOM   1201 C C   . PRO   B 1 61 ? 17.677  -16.113 -41.983 1.00 32.46  ? 60  PRO   B C   1 
ATOM   1202 O O   . PRO   B 1 61 ? 16.711  -16.853 -42.208 1.00 36.20  ? 60  PRO   B O   1 
ATOM   1203 C CB  . PRO   B 1 61 ? 19.668  -16.877 -43.497 1.00 36.84  ? 60  PRO   B CB  1 
ATOM   1204 C CG  . PRO   B 1 61 ? 20.671  -17.996 -43.323 1.00 47.28  ? 60  PRO   B CG  1 
ATOM   1205 C CD  . PRO   B 1 61 ? 20.151  -18.876 -42.159 1.00 39.12  ? 60  PRO   B CD  1 
ATOM   1206 N N   . TYR   B 1 62 ? 17.509  -14.809 -41.627 1.00 36.06  ? 61  TYR   B N   1 
ATOM   1207 C CA  . TYR   B 1 62 ? 16.210  -14.270 -41.298 1.00 37.67  ? 61  TYR   B CA  1 
ATOM   1208 C C   . TYR   B 1 62 ? 15.200  -14.357 -42.431 1.00 36.78  ? 61  TYR   B C   1 
ATOM   1209 O O   . TYR   B 1 62 ? 14.081  -14.798 -42.190 1.00 38.05  ? 61  TYR   B O   1 
ATOM   1210 C CB  . TYR   B 1 62 ? 16.393  -12.826 -40.800 1.00 39.51  ? 61  TYR   B CB  1 
ATOM   1211 C CG  . TYR   B 1 62 ? 15.067  -12.116 -40.568 1.00 43.80  ? 61  TYR   B CG  1 
ATOM   1212 C CD1 . TYR   B 1 62 ? 14.315  -12.372 -39.432 1.00 43.74  ? 61  TYR   B CD1 1 
ATOM   1213 C CD2 . TYR   B 1 62 ? 14.619  -11.132 -41.444 1.00 51.18  ? 61  TYR   B CD2 1 
ATOM   1214 C CE1 . TYR   B 1 62 ? 13.124  -11.713 -39.194 1.00 42.77  ? 61  TYR   B CE1 1 
ATOM   1215 C CE2 . TYR   B 1 62 ? 13.435  -10.451 -41.216 1.00 52.67  ? 61  TYR   B CE2 1 
ATOM   1216 C CZ  . TYR   B 1 62 ? 12.684  -10.753 -40.091 1.00 50.84  ? 61  TYR   B CZ  1 
ATOM   1217 O OH  . TYR   B 1 62 ? 11.513  -10.104 -39.888 1.00 47.57  ? 61  TYR   B OH  1 
ATOM   1218 N N   . ASP   B 1 63 ? 15.579  -13.908 -43.648 1.00 43.14  ? 62  ASP   B N   1 
ATOM   1219 C CA  . ASP   B 1 63 ? 14.706  -13.934 -44.823 1.00 50.98  ? 62  ASP   B CA  1 
ATOM   1220 C C   . ASP   B 1 63 ? 14.153  -15.334 -45.115 1.00 40.33  ? 62  ASP   B C   1 
ATOM   1221 O O   . ASP   B 1 63 ? 12.935  -15.524 -45.195 1.00 49.49  ? 62  ASP   B O   1 
ATOM   1222 C CB  . ASP   B 1 63 ? 15.356  -13.265 -46.024 1.00 57.23  ? 62  ASP   B CB  1 
ATOM   1223 C CG  . ASP   B 1 63 ? 15.311  -11.743 -46.028 1.00 75.34  ? 62  ASP   B CG  1 
ATOM   1224 O OD1 . ASP   B 1 63 ? 14.466  -11.172 -45.292 1.00 76.43  ? 62  ASP   B OD1 1 
ATOM   1225 O OD2 . ASP   B 1 63 ? 16.134  -11.137 -46.757 1.00 86.18  ? 62  ASP   B OD2 1 
ATOM   1226 N N   . LYS   B 1 64 ? 15.050  -16.302 -45.248 1.00 46.83  ? 63  LYS   B N   1 
ATOM   1227 C CA  . LYS   B 1 64 ? 14.665  -17.686 -45.456 1.00 49.21  ? 63  LYS   B CA  1 
ATOM   1228 C C   . LYS   B 1 64 ? 13.704  -18.168 -44.369 1.00 47.90  ? 63  LYS   B C   1 
ATOM   1229 O O   . LYS   B 1 64 ? 12.768  -18.911 -44.667 1.00 47.69  ? 63  LYS   B O   1 
ATOM   1230 C CB  . LYS   B 1 64 ? 15.914  -18.570 -45.552 1.00 52.49  ? 63  LYS   B CB  1 
ATOM   1231 C CG  . LYS   B 1 64 ? 15.598  -20.024 -45.862 1.00 50.30  ? 63  LYS   B CG  1 
ATOM   1232 C CD  . LYS   B 1 64 ? 16.811  -20.943 -45.829 1.00 55.79  ? 63  LYS   B CD  1 
ATOM   1233 C CE  . LYS   B 1 64 ? 16.589  -22.321 -46.439 1.00 49.59  ? 63  LYS   B CE  1 
ATOM   1234 N NZ  . LYS   B 1 64 ? 15.310  -22.974 -46.140 1.00 54.57  ? 63  LYS   B NZ  1 
ATOM   1235 N N   . SER   B 1 65 ? 13.900  -17.734 -43.114 1.00 43.65  ? 64  SER   B N   1 
ATOM   1236 C CA  . SER   B 1 65 ? 13.275  -18.480 -42.010 1.00 43.48  ? 64  SER   B CA  1 
ATOM   1237 C C   . SER   B 1 65 ? 12.136  -17.755 -41.274 1.00 42.52  ? 64  SER   B C   1 
ATOM   1238 O O   . SER   B 1 65 ? 11.518  -18.343 -40.386 1.00 44.93  ? 64  SER   B O   1 
ATOM   1239 C CB  . SER   B 1 65 ? 14.325  -19.015 -41.063 1.00 46.30  ? 64  SER   B CB  1 
ATOM   1240 O OG  . SER   B 1 65 ? 15.046  -17.959 -40.445 1.00 64.25  ? 64  SER   B OG  1 
ATOM   1241 N N   . LYS   B 1 66 ? 11.779  -16.520 -41.677 1.00 43.86  ? 65  LYS   B N   1 
ATOM   1242 C CA  . LYS   B 1 66 ? 10.907  -15.692 -40.842 1.00 41.47  ? 65  LYS   B CA  1 
ATOM   1243 C C   . LYS   B 1 66 ? 9.457   -16.175 -40.853 1.00 48.95  ? 65  LYS   B C   1 
ATOM   1244 O O   . LYS   B 1 66 ? 8.719   -15.975 -39.891 1.00 50.23  ? 65  LYS   B O   1 
ATOM   1245 C CB  . LYS   B 1 66 ? 10.944  -14.209 -41.240 1.00 41.93  ? 65  LYS   B CB  1 
ATOM   1246 C CG  . LYS   B 1 66 ? 10.405  -13.834 -42.624 1.00 47.40  ? 65  LYS   B CG  1 
ATOM   1247 C CD  . LYS   B 1 66 ? 10.710  -12.372 -42.950 1.00 58.04  ? 65  LYS   B CD  1 
ATOM   1248 C CE  . LYS   B 1 66 ? 10.315  -11.996 -44.351 1.00 65.38  ? 65  LYS   B CE  1 
ATOM   1249 N NZ  . LYS   B 1 66 ? 11.186  -10.927 -44.851 1.00 77.93  ? 65  LYS   B NZ  1 
ATOM   1250 N N   . ASP   B 1 67 ? 9.050   -16.799 -41.956 1.00 47.68  ? 66  ASP   B N   1 
ATOM   1251 C CA  . ASP   B 1 67 ? 7.720   -17.376 -42.094 1.00 56.01  ? 66  ASP   B CA  1 
ATOM   1252 C C   . ASP   B 1 67 ? 7.502   -18.436 -41.010 1.00 53.61  ? 66  ASP   B C   1 
ATOM   1253 O O   . ASP   B 1 67 ? 6.449   -18.483 -40.376 1.00 56.70  ? 66  ASP   B O   1 
ATOM   1254 C CB  . ASP   B 1 67 ? 7.532   -17.920 -43.505 1.00 62.31  ? 66  ASP   B CB  1 
ATOM   1255 C CG  . ASP   B 1 67 ? 6.604   -19.122 -43.635 1.00 80.59  ? 66  ASP   B CG  1 
ATOM   1256 O OD1 . ASP   B 1 67 ? 7.126   -20.261 -43.738 1.00 86.44  ? 66  ASP   B OD1 1 
ATOM   1257 O OD2 . ASP   B 1 67 ? 5.370   -18.907 -43.650 1.00 78.77  ? 66  ASP   B OD2 1 
ATOM   1258 N N   . LYS   B 1 68 ? 8.529   -19.265 -40.809 1.00 50.87  ? 67  LYS   B N   1 
ATOM   1259 C CA  . LYS   B 1 68 ? 8.513   -20.395 -39.902 1.00 47.42  ? 67  LYS   B CA  1 
ATOM   1260 C C   . LYS   B 1 68 ? 8.716   -19.977 -38.446 1.00 47.22  ? 67  LYS   B C   1 
ATOM   1261 O O   . LYS   B 1 68 ? 8.009   -20.490 -37.583 1.00 48.00  ? 67  LYS   B O   1 
ATOM   1262 C CB  . LYS   B 1 68 ? 9.653   -21.335 -40.303 1.00 50.06  ? 67  LYS   B CB  1 
ATOM   1263 C CG  . LYS   B 1 68 ? 9.747   -22.596 -39.461 1.00 53.22  ? 67  LYS   B CG  1 
ATOM   1264 C CD  . LYS   B 1 68 ? 10.793  -23.580 -39.976 1.00 58.37  ? 67  LYS   B CD  1 
ATOM   1265 C CE  . LYS   B 1 68 ? 10.757  -24.891 -39.258 1.00 63.51  ? 67  LYS   B CE  1 
ATOM   1266 N NZ  . LYS   B 1 68 ? 9.519   -25.630 -39.526 1.00 66.66  ? 67  LYS   B NZ  1 
ATOM   1267 N N   . TYR   B 1 69 ? 9.690   -19.089 -38.174 1.00 41.65  ? 68  TYR   B N   1 
ATOM   1268 C CA  . TYR   B 1 69 ? 10.128  -18.803 -36.808 1.00 35.10  ? 68  TYR   B CA  1 
ATOM   1269 C C   . TYR   B 1 69 ? 9.618   -17.452 -36.310 1.00 39.00  ? 68  TYR   B C   1 
ATOM   1270 O O   . TYR   B 1 69 ? 9.758   -17.166 -35.120 1.00 45.52  ? 68  TYR   B O   1 
ATOM   1271 C CB  . TYR   B 1 69 ? 11.650  -18.897 -36.605 1.00 37.13  ? 68  TYR   B CB  1 
ATOM   1272 C CG  . TYR   B 1 69 ? 12.303  -20.249 -36.867 1.00 38.80  ? 68  TYR   B CG  1 
ATOM   1273 C CD1 . TYR   B 1 69 ? 11.803  -21.418 -36.296 1.00 40.66  ? 68  TYR   B CD1 1 
ATOM   1274 C CD2 . TYR   B 1 69 ? 13.374  -20.363 -37.746 1.00 42.71  ? 68  TYR   B CD2 1 
ATOM   1275 C CE1 . TYR   B 1 69 ? 12.378  -22.653 -36.557 1.00 40.70  ? 68  TYR   B CE1 1 
ATOM   1276 C CE2 . TYR   B 1 69 ? 13.948  -21.595 -38.032 1.00 42.52  ? 68  TYR   B CE2 1 
ATOM   1277 C CZ  . TYR   B 1 69 ? 13.462  -22.736 -37.407 1.00 39.53  ? 68  TYR   B CZ  1 
ATOM   1278 O OH  . TYR   B 1 69 ? 13.960  -23.968 -37.668 1.00 43.33  ? 68  TYR   B OH  1 
ATOM   1279 N N   . GLY   B 1 70 ? 9.127   -16.597 -37.222 1.00 44.78  ? 69  GLY   B N   1 
ATOM   1280 C CA  . GLY   B 1 70 ? 8.848   -15.209 -36.879 1.00 48.39  ? 69  GLY   B CA  1 
ATOM   1281 C C   . GLY   B 1 70 ? 7.430   -14.976 -36.352 1.00 48.72  ? 69  GLY   B C   1 
ATOM   1282 O O   . GLY   B 1 70 ? 6.833   -13.928 -36.616 1.00 54.99  ? 69  GLY   B O   1 
ATOM   1283 N N   . LYS   B 1 71 ? 6.886   -15.955 -35.618 1.00 51.23  ? 70  LYS   B N   1 
ATOM   1284 C CA  . LYS   B 1 71 ? 5.533   -15.848 -35.096 1.00 53.68  ? 70  LYS   B CA  1 
ATOM   1285 C C   . LYS   B 1 71 ? 5.605   -15.410 -33.642 1.00 56.23  ? 70  LYS   B C   1 
ATOM   1286 O O   . LYS   B 1 71 ? 6.459   -15.878 -32.890 1.00 47.53  ? 70  LYS   B O   1 
ATOM   1287 C CB  . LYS   B 1 71 ? 4.722   -17.151 -35.137 1.00 56.57  ? 70  LYS   B CB  1 
ATOM   1288 C CG  . LYS   B 1 71 ? 3.806   -17.356 -36.342 1.00 67.09  ? 70  LYS   B CG  1 
ATOM   1289 C CD  . LYS   B 1 71 ? 4.512   -17.599 -37.669 1.00 68.52  ? 70  LYS   B CD  1 
ATOM   1290 C CE  . LYS   B 1 71 ? 3.565   -17.905 -38.797 1.00 77.09  ? 70  LYS   B CE  1 
ATOM   1291 N NZ  . LYS   B 1 71 ? 4.213   -17.715 -40.099 1.00 73.42  ? 70  LYS   B NZ  1 
ATOM   1292 N N   . PRO   B 1 72 ? 4.719   -14.492 -33.192 1.00 55.46  ? 71  PRO   B N   1 
ATOM   1293 C CA  . PRO   B 1 72 ? 4.692   -14.137 -31.776 1.00 54.62  ? 71  PRO   B CA  1 
ATOM   1294 C C   . PRO   B 1 72 ? 4.477   -15.339 -30.859 1.00 47.45  ? 71  PRO   B C   1 
ATOM   1295 O O   . PRO   B 1 72 ? 3.878   -16.345 -31.248 1.00 49.97  ? 71  PRO   B O   1 
ATOM   1296 C CB  . PRO   B 1 72 ? 3.604   -13.060 -31.682 1.00 50.18  ? 71  PRO   B CB  1 
ATOM   1297 C CG  . PRO   B 1 72 ? 3.573   -12.479 -33.086 1.00 53.45  ? 71  PRO   B CG  1 
ATOM   1298 C CD  . PRO   B 1 72 ? 3.806   -13.677 -34.010 1.00 52.67  ? 71  PRO   B CD  1 
ATOM   1299 N N   . ASN   B 1 73 ? 5.033   -15.218 -29.653 1.00 51.77  ? 72  ASN   B N   1 
ATOM   1300 C CA  . ASN   B 1 73 ? 4.802   -16.138 -28.553 1.00 46.66  ? 72  ASN   B CA  1 
ATOM   1301 C C   . ASN   B 1 73 ? 4.738   -15.351 -27.237 1.00 54.26  ? 72  ASN   B C   1 
ATOM   1302 O O   . ASN   B 1 73 ? 4.770   -14.109 -27.219 1.00 53.53  ? 72  ASN   B O   1 
ATOM   1303 C CB  . ASN   B 1 73 ? 5.832   -17.266 -28.508 1.00 45.80  ? 72  ASN   B CB  1 
ATOM   1304 C CG  . ASN   B 1 73 ? 7.252   -16.799 -28.261 1.00 43.74  ? 72  ASN   B CG  1 
ATOM   1305 O OD1 . ASN   B 1 73 ? 7.522   -16.088 -27.282 1.00 44.30  ? 72  ASN   B OD1 1 
ATOM   1306 N ND2 . ASN   B 1 73 ? 8.178   -17.187 -29.136 1.00 42.79  ? 72  ASN   B ND2 1 
ATOM   1307 N N   . LYS   B 1 74 ? 4.699   -16.100 -26.128 1.00 50.69  ? 73  LYS   B N   1 
ATOM   1308 C CA  . LYS   B 1 74 ? 4.523   -15.527 -24.799 1.00 54.29  ? 73  LYS   B CA  1 
ATOM   1309 C C   . LYS   B 1 74 ? 5.835   -15.502 -24.004 1.00 52.44  ? 73  LYS   B C   1 
ATOM   1310 O O   . LYS   B 1 74 ? 5.801   -15.269 -22.793 1.00 56.13  ? 73  LYS   B O   1 
ATOM   1311 C CB  . LYS   B 1 74 ? 3.404   -16.269 -24.044 1.00 49.86  ? 73  LYS   B CB  1 
ATOM   1312 N N   . ARG   B 1 75 ? 6.989   -15.740 -24.662 1.00 43.20  ? 74  ARG   B N   1 
ATOM   1313 C CA  . ARG   B 1 75 ? 8.278   -15.565 -24.000 1.00 43.91  ? 74  ARG   B CA  1 
ATOM   1314 C C   . ARG   B 1 75 ? 8.629   -14.072 -23.872 1.00 42.62  ? 74  ARG   B C   1 
ATOM   1315 O O   . ARG   B 1 75 ? 8.477   -13.276 -24.807 1.00 43.90  ? 74  ARG   B O   1 
ATOM   1316 C CB  . ARG   B 1 75 ? 9.406   -16.375 -24.652 1.00 44.81  ? 74  ARG   B CB  1 
ATOM   1317 C CG  . ARG   B 1 75 ? 9.320   -17.883 -24.885 1.00 44.40  ? 74  ARG   B CG  1 
ATOM   1318 C CD  . ARG   B 1 75 ? 9.176   -18.694 -23.617 1.00 50.53  ? 74  ARG   B CD  1 
ATOM   1319 N NE  . ARG   B 1 75 ? 9.411   -20.125 -23.863 1.00 45.22  ? 74  ARG   B NE  1 
ATOM   1320 C CZ  . ARG   B 1 75 ? 10.528  -20.756 -23.557 1.00 45.21  ? 74  ARG   B CZ  1 
ATOM   1321 N NH1 . ARG   B 1 75 ? 11.530  -20.102 -22.993 1.00 48.54  ? 74  ARG   B NH1 1 
ATOM   1322 N NH2 . ARG   B 1 75 ? 10.674  -22.029 -23.892 1.00 49.92  ? 74  ARG   B NH2 1 
ATOM   1323 N N   . LYS   B 1 76 ? 9.087   -13.698 -22.673 1.00 43.49  ? 75  LYS   B N   1 
ATOM   1324 C CA  . LYS   B 1 76 ? 9.499   -12.349 -22.317 1.00 37.39  ? 75  LYS   B CA  1 
ATOM   1325 C C   . LYS   B 1 76 ? 10.590  -11.834 -23.269 1.00 36.17  ? 75  LYS   B C   1 
ATOM   1326 O O   . LYS   B 1 76 ? 11.668  -12.429 -23.332 1.00 36.52  ? 75  LYS   B O   1 
ATOM   1327 C CB  . LYS   B 1 76 ? 10.077  -12.304 -20.897 1.00 41.31  ? 75  LYS   B CB  1 
ATOM   1328 C CG  . LYS   B 1 76 ? 10.353  -10.858 -20.502 1.00 41.66  ? 75  LYS   B CG  1 
ATOM   1329 C CD  . LYS   B 1 76 ? 10.882  -10.667 -19.085 1.00 46.11  ? 75  LYS   B CD  1 
ATOM   1330 C CE  . LYS   B 1 76 ? 10.967  -9.208  -18.728 1.00 48.92  ? 75  LYS   B CE  1 
ATOM   1331 N NZ  . LYS   B 1 76 ? 11.225  -9.058  -17.290 1.00 58.68  ? 75  LYS   B NZ  1 
ATOM   1332 N N   . GLY   B 1 77 ? 10.268  -10.742 -23.977 1.00 36.94  ? 76  GLY   B N   1 
ATOM   1333 C CA  . GLY   B 1 77 ? 11.211  -10.062 -24.874 1.00 35.98  ? 76  GLY   B CA  1 
ATOM   1334 C C   . GLY   B 1 77 ? 11.088  -10.513 -26.332 1.00 39.42  ? 76  GLY   B C   1 
ATOM   1335 O O   . GLY   B 1 77 ? 11.673  -9.907  -27.228 1.00 40.24  ? 76  GLY   B O   1 
ATOM   1336 N N   . PHE   B 1 78 ? 10.363  -11.601 -26.583 1.00 34.94  ? 77  PHE   B N   1 
ATOM   1337 C CA  . PHE   B 1 78 ? 10.217  -12.115 -27.950 1.00 35.58  ? 77  PHE   B CA  1 
ATOM   1338 C C   . PHE   B 1 78 ? 9.464   -11.168 -28.904 1.00 39.28  ? 77  PHE   B C   1 
ATOM   1339 O O   . PHE   B 1 78 ? 9.911   -10.903 -30.021 1.00 36.38  ? 77  PHE   B O   1 
ATOM   1340 C CB  . PHE   B 1 78 ? 9.496   -13.468 -27.952 1.00 36.24  ? 77  PHE   B CB  1 
ATOM   1341 C CG  . PHE   B 1 78 ? 9.696   -14.193 -29.275 1.00 38.16  ? 77  PHE   B CG  1 
ATOM   1342 C CD1 . PHE   B 1 78 ? 10.799  -15.025 -29.460 1.00 34.48  ? 77  PHE   B CD1 1 
ATOM   1343 C CD2 . PHE   B 1 78 ? 8.776   -14.068 -30.314 1.00 37.73  ? 77  PHE   B CD2 1 
ATOM   1344 C CE1 . PHE   B 1 78 ? 10.997  -15.691 -30.688 1.00 35.12  ? 77  PHE   B CE1 1 
ATOM   1345 C CE2 . PHE   B 1 78 ? 8.963   -14.748 -31.528 1.00 37.33  ? 77  PHE   B CE2 1 
ATOM   1346 C CZ  . PHE   B 1 78 ? 10.073  -15.566 -31.698 1.00 38.88  ? 77  PHE   B CZ  1 
ATOM   1347 N N   . ASN   B 1 79 ? 8.284   -10.669 -28.524 1.00 39.29  ? 78  ASN   B N   1 
ATOM   1348 C CA  . ASN   B 1 79 ? 7.522   -9.823  -29.441 1.00 42.37  ? 78  ASN   B CA  1 
ATOM   1349 C C   . ASN   B 1 79 ? 8.246   -8.484  -29.671 1.00 38.67  ? 78  ASN   B C   1 
ATOM   1350 O O   . ASN   B 1 79 ? 8.178   -7.944  -30.781 1.00 41.25  ? 78  ASN   B O   1 
ATOM   1351 C CB  . ASN   B 1 79 ? 6.051   -9.712  -29.038 1.00 46.60  ? 78  ASN   B CB  1 
ATOM   1352 C CG  . ASN   B 1 79 ? 5.293   -11.018 -29.153 1.00 49.18  ? 78  ASN   B CG  1 
ATOM   1353 O OD1 . ASN   B 1 79 ? 5.764   -11.968 -29.785 1.00 45.88  ? 78  ASN   B OD1 1 
ATOM   1354 N ND2 . ASN   B 1 79 ? 4.113   -11.105 -28.552 1.00 49.42  ? 78  ASN   B ND2 1 
ATOM   1355 N N   . GLU   B 1 80 ? 8.964   -7.994  -28.655 1.00 36.75  ? 79  GLU   B N   1 
ATOM   1356 C CA  . GLU   B 1 80 ? 9.717   -6.756  -28.789 1.00 40.77  ? 79  GLU   B CA  1 
ATOM   1357 C C   . GLU   B 1 80 ? 10.854  -7.013  -29.777 1.00 40.09  ? 79  GLU   B C   1 
ATOM   1358 O O   . GLU   B 1 80 ? 11.192  -6.141  -30.582 1.00 39.31  ? 79  GLU   B O   1 
ATOM   1359 C CB  . GLU   B 1 80 ? 10.366  -6.316  -27.477 1.00 43.28  ? 79  GLU   B CB  1 
ATOM   1360 C CG  . GLU   B 1 80 ? 9.371   -5.765  -26.460 1.00 54.58  ? 79  GLU   B CG  1 
ATOM   1361 N N   . GLY   B 1 81 ? 11.440  -8.220  -29.668 1.00 38.67  ? 80  GLY   B N   1 
ATOM   1362 C CA  . GLY   B 1 81 ? 12.524  -8.677  -30.543 1.00 40.20  ? 80  GLY   B CA  1 
ATOM   1363 C C   . GLY   B 1 81 ? 12.081  -8.754  -32.001 1.00 35.73  ? 80  GLY   B C   1 
ATOM   1364 O O   . GLY   B 1 81 ? 12.841  -8.391  -32.923 1.00 35.41  ? 80  GLY   B O   1 
ATOM   1365 N N   . LEU   B 1 82 ? 10.861  -9.218  -32.202 1.00 35.69  ? 81  LEU   B N   1 
ATOM   1366 C CA  . LEU   B 1 82 ? 10.254  -9.267  -33.524 1.00 40.37  ? 81  LEU   B CA  1 
ATOM   1367 C C   . LEU   B 1 82 ? 10.156  -7.834  -34.055 1.00 37.10  ? 81  LEU   B C   1 
ATOM   1368 O O   . LEU   B 1 82 ? 10.430  -7.576  -35.231 1.00 38.02  ? 81  LEU   B O   1 
ATOM   1369 C CB  . LEU   B 1 82 ? 8.902   -9.995  -33.534 1.00 39.20  ? 81  LEU   B CB  1 
ATOM   1370 C CG  . LEU   B 1 82 ? 8.934   -11.524 -33.380 1.00 37.08  ? 81  LEU   B CG  1 
ATOM   1371 C CD1 . LEU   B 1 82 ? 7.500   -12.101 -33.485 1.00 40.96  ? 81  LEU   B CD1 1 
ATOM   1372 C CD2 . LEU   B 1 82 ? 9.898   -12.187 -34.365 1.00 37.32  ? 81  LEU   B CD2 1 
ATOM   1373 N N   . TRP   B 1 83 ? 9.750   -6.910  -33.171 1.00 37.54  ? 82  TRP   B N   1 
ATOM   1374 C CA  . TRP   B 1 83 ? 9.525   -5.529  -33.560 1.00 40.44  ? 82  TRP   B CA  1 
ATOM   1375 C C   . TRP   B 1 83 ? 10.838  -4.932  -34.047 1.00 38.83  ? 82  TRP   B C   1 
ATOM   1376 O O   . TRP   B 1 83 ? 10.871  -4.307  -35.113 1.00 38.21  ? 82  TRP   B O   1 
ATOM   1377 C CB  . TRP   B 1 83 ? 8.937   -4.674  -32.423 1.00 43.59  ? 82  TRP   B CB  1 
ATOM   1378 C CG  . TRP   B 1 83 ? 8.595   -3.293  -32.927 1.00 42.08  ? 82  TRP   B CG  1 
ATOM   1379 C CD1 . TRP   B 1 83 ? 7.423   -2.891  -33.500 1.00 50.40  ? 82  TRP   B CD1 1 
ATOM   1380 C CD2 . TRP   B 1 83 ? 9.482   -2.158  -32.974 1.00 43.80  ? 82  TRP   B CD2 1 
ATOM   1381 N NE1 . TRP   B 1 83 ? 7.516   -1.579  -33.898 1.00 50.14  ? 82  TRP   B NE1 1 
ATOM   1382 C CE2 . TRP   B 1 83 ? 8.764   -1.106  -33.592 1.00 43.47  ? 82  TRP   B CE2 1 
ATOM   1383 C CE3 . TRP   B 1 83 ? 10.810  -1.935  -32.578 1.00 41.70  ? 82  TRP   B CE3 1 
ATOM   1384 C CZ2 . TRP   B 1 83 ? 9.330   0.155   -33.800 1.00 44.18  ? 82  TRP   B CZ2 1 
ATOM   1385 C CZ3 . TRP   B 1 83 ? 11.358  -0.682  -32.761 1.00 49.68  ? 82  TRP   B CZ3 1 
ATOM   1386 C CH2 . TRP   B 1 83 ? 10.625  0.337   -33.380 1.00 39.82  ? 82  TRP   B CH2 1 
ATOM   1387 N N   . GLU   B 1 84 ? 11.911  -5.203  -33.278 1.00 35.03  ? 83  GLU   B N   1 
ATOM   1388 C CA  . GLU   B 1 84 ? 13.206  -4.610  -33.525 1.00 37.39  ? 83  GLU   B CA  1 
ATOM   1389 C C   . GLU   B 1 84 ? 13.825  -5.148  -34.819 1.00 37.70  ? 83  GLU   B C   1 
ATOM   1390 O O   . GLU   B 1 84 ? 14.410  -4.369  -35.566 1.00 37.32  ? 83  GLU   B O   1 
ATOM   1391 C CB  . GLU   B 1 84 ? 14.139  -4.853  -32.353 1.00 34.24  ? 83  GLU   B CB  1 
ATOM   1392 C CG  . GLU   B 1 84 ? 13.686  -4.157  -31.063 1.00 38.05  ? 83  GLU   B CG  1 
ATOM   1393 C CD  . GLU   B 1 84 ? 14.543  -4.496  -29.874 1.00 40.38  ? 83  GLU   B CD  1 
ATOM   1394 O OE1 . GLU   B 1 84 ? 15.463  -5.358  -29.953 1.00 37.41  ? 83  GLU   B OE1 1 
ATOM   1395 O OE2 . GLU   B 1 84 ? 14.315  -3.876  -28.801 1.00 42.45  ? 83  GLU   B OE2 1 
ATOM   1396 N N   . ILE   B 1 85 ? 13.728  -6.457  -35.067 1.00 37.95  ? 84  ILE   B N   1 
ATOM   1397 C CA  . ILE   B 1 85 ? 14.391  -7.022  -36.248 1.00 35.74  ? 84  ILE   B CA  1 
ATOM   1398 C C   . ILE   B 1 85 ? 13.740  -6.485  -37.530 1.00 36.67  ? 84  ILE   B C   1 
ATOM   1399 O O   . ILE   B 1 85 ? 14.423  -6.306  -38.551 1.00 36.67  ? 84  ILE   B O   1 
ATOM   1400 C CB  . ILE   B 1 85 ? 14.491  -8.562  -36.201 1.00 34.70  ? 84  ILE   B CB  1 
ATOM   1401 C CG1 . ILE   B 1 85 ? 15.562  -9.073  -37.209 1.00 35.23  ? 84  ILE   B CG1 1 
ATOM   1402 C CG2 . ILE   B 1 85 ? 13.132  -9.203  -36.469 1.00 34.87  ? 84  ILE   B CG2 1 
ATOM   1403 C CD1 . ILE   B 1 85 ? 16.046  -10.496 -36.895 1.00 37.80  ? 84  ILE   B CD1 1 
ATOM   1404 N N   . GLN   B 1 86 ? 12.440  -6.195  -37.422 1.00 36.52  ? 85  GLN   B N   1 
ATOM   1405 C CA  . GLN   B 1 86 ? 11.593  -5.659  -38.480 1.00 38.52  ? 85  GLN   B CA  1 
ATOM   1406 C C   . GLN   B 1 86 ? 11.873  -4.175  -38.709 1.00 42.28  ? 85  GLN   B C   1 
ATOM   1407 O O   . GLN   B 1 86 ? 12.009  -3.741  -39.858 1.00 42.54  ? 85  GLN   B O   1 
ATOM   1408 C CB  . GLN   B 1 86 ? 10.134  -5.919  -38.094 1.00 40.77  ? 85  GLN   B CB  1 
ATOM   1409 N N   . ASN   B 1 87 ? 11.956  -3.388  -37.624 1.00 39.47  ? 86  ASN   B N   1 
ATOM   1410 C CA  . ASN   B 1 87 ? 11.853  -1.939  -37.772 1.00 38.75  ? 86  ASN   B CA  1 
ATOM   1411 C C   . ASN   B 1 87 ? 13.177  -1.212  -37.574 1.00 38.74  ? 86  ASN   B C   1 
ATOM   1412 O O   . ASN   B 1 87 ? 13.309  -0.083  -38.059 1.00 41.45  ? 86  ASN   B O   1 
ATOM   1413 C CB  . ASN   B 1 87 ? 10.914  -1.353  -36.713 1.00 41.96  ? 86  ASN   B CB  1 
ATOM   1414 C CG  . ASN   B 1 87 ? 9.504   -1.837  -36.944 1.00 50.65  ? 86  ASN   B CG  1 
ATOM   1415 O OD1 . ASN   B 1 87 ? 8.767   -1.241  -37.736 1.00 61.18  ? 86  ASN   B OD1 1 
ATOM   1416 N ND2 . ASN   B 1 87 ? 9.123   -2.927  -36.294 1.00 56.63  ? 86  ASN   B ND2 1 
ATOM   1417 N N   . ASN   B 1 88 ? 14.116  -1.762  -36.797 1.00 37.75  ? 87  ASN   B N   1 
ATOM   1418 C CA  . ASN   B 1 88 ? 15.387  -1.073  -36.581 1.00 39.22  ? 87  ASN   B CA  1 
ATOM   1419 C C   . ASN   B 1 88 ? 16.473  -2.062  -36.157 1.00 39.89  ? 87  ASN   B C   1 
ATOM   1420 O O   . ASN   B 1 88 ? 17.087  -1.978  -35.078 1.00 36.94  ? 87  ASN   B O   1 
ATOM   1421 C CB  . ASN   B 1 88 ? 15.230  0.156   -35.681 1.00 42.02  ? 87  ASN   B CB  1 
ATOM   1422 C CG  . ASN   B 1 88 ? 16.369  1.145   -35.804 1.00 38.78  ? 87  ASN   B CG  1 
ATOM   1423 O OD1 . ASN   B 1 88 ? 17.352  0.925   -36.524 1.00 43.03  ? 87  ASN   B OD1 1 
ATOM   1424 N ND2 . ASN   B 1 88 ? 16.256  2.255   -35.085 1.00 45.45  ? 87  ASN   B ND2 1 
ATOM   1425 N N   . PRO   B 1 89 ? 16.777  -3.036  -37.062 1.00 38.20  ? 88  PRO   B N   1 
ATOM   1426 C CA  . PRO   B 1 89 ? 17.715  -4.116  -36.753 1.00 35.06  ? 88  PRO   B CA  1 
ATOM   1427 C C   . PRO   B 1 89 ? 19.161  -3.687  -36.518 1.00 31.66  ? 88  PRO   B C   1 
ATOM   1428 O O   . PRO   B 1 89 ? 19.978  -4.420  -35.980 1.00 34.39  ? 88  PRO   B O   1 
ATOM   1429 C CB  . PRO   B 1 89 ? 17.542  -5.032  -38.012 1.00 34.61  ? 88  PRO   B CB  1 
ATOM   1430 C CG  . PRO   B 1 89 ? 17.150  -4.099  -39.155 1.00 33.39  ? 88  PRO   B CG  1 
ATOM   1431 C CD  . PRO   B 1 89 ? 16.209  -3.125  -38.424 1.00 36.23  ? 88  PRO   B CD  1 
ATOM   1432 N N   . HIS   B 1 90 ? 19.508  -2.473  -37.011 1.00 33.88  ? 89  HIS   B N   1 
ATOM   1433 C CA  . HIS   B 1 90 ? 20.907  -2.081  -36.971 1.00 34.48  ? 89  HIS   B CA  1 
ATOM   1434 C C   . HIS   B 1 90 ? 21.192  -1.005  -35.913 1.00 40.86  ? 89  HIS   B C   1 
ATOM   1435 O O   . HIS   B 1 90 ? 22.312  -0.486  -35.857 1.00 36.91  ? 89  HIS   B O   1 
ATOM   1436 C CB  . HIS   B 1 90 ? 21.361  -1.609  -38.370 1.00 36.09  ? 89  HIS   B CB  1 
ATOM   1437 C CG  . HIS   B 1 90 ? 21.221  -2.691  -39.409 1.00 38.00  ? 89  HIS   B CG  1 
ATOM   1438 N ND1 . HIS   B 1 90 ? 21.816  -3.927  -39.300 1.00 35.50  ? 89  HIS   B ND1 1 
ATOM   1439 C CD2 . HIS   B 1 90 ? 20.551  -2.710  -40.560 1.00 36.14  ? 89  HIS   B CD2 1 
ATOM   1440 C CE1 . HIS   B 1 90 ? 21.495  -4.652  -40.360 1.00 34.67  ? 89  HIS   B CE1 1 
ATOM   1441 N NE2 . HIS   B 1 90 ? 20.708  -3.931  -41.119 1.00 34.68  ? 89  HIS   B NE2 1 
ATOM   1442 N N   . ALA   B 1 91 ? 20.186  -0.692  -35.083 1.00 37.54  ? 90  ALA   B N   1 
ATOM   1443 C CA  . ALA   B 1 91 ? 20.351  0.319   -34.033 1.00 39.57  ? 90  ALA   B CA  1 
ATOM   1444 C C   . ALA   B 1 91 ? 21.294  -0.102  -32.905 1.00 43.30  ? 90  ALA   B C   1 
ATOM   1445 O O   . ALA   B 1 91 ? 21.567  -1.281  -32.659 1.00 38.41  ? 90  ALA   B O   1 
ATOM   1446 C CB  . ALA   B 1 91 ? 18.999  0.762   -33.516 1.00 37.76  ? 90  ALA   B CB  1 
ATOM   1447 N N   . SER   B 1 92 ? 21.806  0.919   -32.197 1.00 44.39  ? 91  SER   B N   1 
ATOM   1448 C CA  . SER   B 1 92 ? 22.461  0.749   -30.916 1.00 48.18  ? 91  SER   B CA  1 
ATOM   1449 C C   . SER   B 1 92 ? 21.387  0.519   -29.859 1.00 48.51  ? 91  SER   B C   1 
ATOM   1450 O O   . SER   B 1 92 ? 20.470  1.339   -29.706 1.00 51.58  ? 91  SER   B O   1 
ATOM   1451 C CB  . SER   B 1 92 ? 23.293  1.986   -30.573 1.00 52.99  ? 91  SER   B CB  1 
ATOM   1452 O OG  . SER   B 1 92 ? 23.855  1.874   -29.277 1.00 59.45  ? 91  SER   B OG  1 
ATOM   1453 N N   . TYR   B 1 93 ? 21.504  -0.632  -29.194 1.00 46.55  ? 92  TYR   B N   1 
ATOM   1454 C CA  . TYR   B 1 93 ? 20.687  -1.022  -28.061 1.00 49.44  ? 92  TYR   B CA  1 
ATOM   1455 C C   . TYR   B 1 93 ? 21.534  -0.928  -26.797 1.00 60.76  ? 92  TYR   B C   1 
ATOM   1456 O O   . TYR   B 1 93 ? 21.161  -1.476  -25.764 1.00 66.53  ? 92  TYR   B O   1 
ATOM   1457 C CB  . TYR   B 1 93 ? 20.107  -2.417  -28.321 1.00 42.47  ? 92  TYR   B CB  1 
ATOM   1458 C CG  . TYR   B 1 93 ? 19.107  -2.349  -29.456 1.00 37.18  ? 92  TYR   B CG  1 
ATOM   1459 C CD1 . TYR   B 1 93 ? 17.812  -1.925  -29.207 1.00 41.95  ? 92  TYR   B CD1 1 
ATOM   1460 C CD2 . TYR   B 1 93 ? 19.438  -2.705  -30.772 1.00 41.01  ? 92  TYR   B CD2 1 
ATOM   1461 C CE1 . TYR   B 1 93 ? 16.880  -1.792  -30.213 1.00 41.67  ? 92  TYR   B CE1 1 
ATOM   1462 C CE2 . TYR   B 1 93 ? 18.509  -2.533  -31.787 1.00 37.56  ? 92  TYR   B CE2 1 
ATOM   1463 C CZ  . TYR   B 1 93 ? 17.222  -2.117  -31.511 1.00 40.71  ? 92  TYR   B CZ  1 
ATOM   1464 O OH  . TYR   B 1 93 ? 16.236  -1.979  -32.435 1.00 40.63  ? 92  TYR   B OH  1 
ATOM   1465 N N   . SER   B 1 94 ? 22.658  -0.202  -26.906 1.00 74.40  ? 93  SER   B N   1 
ATOM   1466 C CA  . SER   B 1 94 ? 23.642  -0.038  -25.845 1.00 78.84  ? 93  SER   B CA  1 
ATOM   1467 C C   . SER   B 1 94 ? 22.994  -0.268  -24.471 1.00 88.49  ? 93  SER   B C   1 
ATOM   1468 O O   . SER   B 1 94 ? 22.276  0.651   -24.006 1.00 93.45  ? 93  SER   B O   1 
ATOM   1469 C CB  . SER   B 1 94 ? 24.326  1.314   -25.922 1.00 72.04  ? 93  SER   B CB  1 
ATOM   1470 O OG  . SER   B 1 94 ? 25.338  1.329   -26.923 1.00 70.83  ? 93  SER   B OG  1 
ATOM   1471 O OXT . SER   B 1 94 ? 23.213  -1.369  -23.924 1.00 99.43  ? 93  SER   B OXT 1 
ATOM   1472 N N   . HIS   C 1 4  ? 33.230  -24.261 27.325  1.00 87.04  ? 3   HIS   C N   1 
ATOM   1473 C CA  . HIS   C 1 4  ? 32.250  -23.158 27.524  1.00 86.08  ? 3   HIS   C CA  1 
ATOM   1474 C C   . HIS   C 1 4  ? 31.506  -23.380 28.841  1.00 84.85  ? 3   HIS   C C   1 
ATOM   1475 O O   . HIS   C 1 4  ? 32.053  -23.952 29.783  1.00 78.41  ? 3   HIS   C O   1 
ATOM   1476 C CB  . HIS   C 1 4  ? 31.334  -23.039 26.299  1.00 84.34  ? 3   HIS   C CB  1 
ATOM   1477 N N   . ALA   C 1 5  ? 30.256  -22.913 28.890  1.00 86.22  ? 4   ALA   C N   1 
ATOM   1478 C CA  . ALA   C 1 5  ? 29.368  -23.142 30.017  1.00 84.86  ? 4   ALA   C CA  1 
ATOM   1479 C C   . ALA   C 1 5  ? 27.935  -23.248 29.511  1.00 86.02  ? 4   ALA   C C   1 
ATOM   1480 O O   . ALA   C 1 5  ? 27.560  -22.583 28.545  1.00 89.05  ? 4   ALA   C O   1 
ATOM   1481 C CB  . ALA   C 1 5  ? 29.485  -21.998 30.988  1.00 86.89  ? 4   ALA   C CB  1 
ATOM   1482 N N   . PHE   C 1 6  ? 27.142  -24.085 30.182  1.00 69.94  ? 5   PHE   C N   1 
ATOM   1483 C CA  . PHE   C 1 6  ? 25.741  -24.219 29.838  1.00 57.96  ? 5   PHE   C CA  1 
ATOM   1484 C C   . PHE   C 1 6  ? 24.947  -24.341 31.127  1.00 61.79  ? 5   PHE   C C   1 
ATOM   1485 O O   . PHE   C 1 6  ? 25.409  -24.971 32.076  1.00 73.71  ? 5   PHE   C O   1 
ATOM   1486 C CB  . PHE   C 1 6  ? 25.505  -25.415 28.898  1.00 60.24  ? 5   PHE   C CB  1 
ATOM   1487 C CG  . PHE   C 1 6  ? 26.263  -25.342 27.578  1.00 53.15  ? 5   PHE   C CG  1 
ATOM   1488 C CD1 . PHE   C 1 6  ? 27.421  -26.082 27.377  1.00 56.16  ? 5   PHE   C CD1 1 
ATOM   1489 C CD2 . PHE   C 1 6  ? 25.845  -24.496 26.551  1.00 58.14  ? 5   PHE   C CD2 1 
ATOM   1490 C CE1 . PHE   C 1 6  ? 28.124  -26.006 26.180  1.00 61.94  ? 5   PHE   C CE1 1 
ATOM   1491 C CE2 . PHE   C 1 6  ? 26.550  -24.427 25.356  1.00 57.99  ? 5   PHE   C CE2 1 
ATOM   1492 C CZ  . PHE   C 1 6  ? 27.679  -25.184 25.166  1.00 52.47  ? 5   PHE   C CZ  1 
ATOM   1493 N N   . LYS   C 1 7  ? 23.761  -23.731 31.139  1.00 55.93  ? 6   LYS   C N   1 
ATOM   1494 C CA  . LYS   C 1 7  ? 22.824  -23.847 32.246  1.00 64.53  ? 6   LYS   C CA  1 
ATOM   1495 C C   . LYS   C 1 7  ? 21.442  -24.026 31.630  1.00 55.71  ? 6   LYS   C C   1 
ATOM   1496 O O   . LYS   C 1 7  ? 21.297  -23.817 30.424  1.00 59.91  ? 6   LYS   C O   1 
ATOM   1497 C CB  . LYS   C 1 7  ? 22.944  -22.633 33.179  1.00 65.26  ? 6   LYS   C CB  1 
ATOM   1498 N N   . PRO   C 1 8  ? 20.398  -24.448 32.385  1.00 62.03  ? 7   PRO   C N   1 
ATOM   1499 C CA  . PRO   C 1 8  ? 19.081  -24.660 31.785  1.00 62.35  ? 7   PRO   C CA  1 
ATOM   1500 C C   . PRO   C 1 8  ? 18.617  -23.427 31.011  1.00 65.96  ? 7   PRO   C C   1 
ATOM   1501 O O   . PRO   C 1 8  ? 18.842  -22.295 31.441  1.00 71.40  ? 7   PRO   C O   1 
ATOM   1502 C CB  . PRO   C 1 8  ? 18.189  -24.980 32.987  1.00 69.71  ? 7   PRO   C CB  1 
ATOM   1503 C CG  . PRO   C 1 8  ? 19.144  -25.571 33.999  1.00 66.48  ? 7   PRO   C CG  1 
ATOM   1504 C CD  . PRO   C 1 8  ? 20.426  -24.757 33.829  1.00 57.20  ? 7   PRO   C CD  1 
ATOM   1505 N N   . GLY   C 1 9  ? 18.008  -23.662 29.844  1.00 65.42  ? 8   GLY   C N   1 
ATOM   1506 C CA  . GLY   C 1 9  ? 17.421  -22.592 29.052  1.00 59.46  ? 8   GLY   C CA  1 
ATOM   1507 C C   . GLY   C 1 9  ? 18.281  -22.194 27.855  1.00 59.08  ? 8   GLY   C C   1 
ATOM   1508 O O   . GLY   C 1 9  ? 17.742  -21.714 26.861  1.00 65.67  ? 8   GLY   C O   1 
ATOM   1509 N N   . ASP   C 1 10 ? 19.601  -22.412 27.950  1.00 51.79  ? 9   ASP   C N   1 
ATOM   1510 C CA  . ASP   C 1 10 ? 20.535  -22.091 26.886  1.00 47.27  ? 9   ASP   C CA  1 
ATOM   1511 C C   . ASP   C 1 10 ? 20.162  -22.812 25.585  1.00 49.28  ? 9   ASP   C C   1 
ATOM   1512 O O   . ASP   C 1 10 ? 19.817  -23.995 25.593  1.00 47.60  ? 9   ASP   C O   1 
ATOM   1513 C CB  . ASP   C 1 10 ? 21.971  -22.384 27.278  1.00 48.58  ? 9   ASP   C CB  1 
ATOM   1514 C CG  . ASP   C 1 10 ? 22.578  -21.464 28.335  1.00 63.49  ? 9   ASP   C CG  1 
ATOM   1515 O OD1 . ASP   C 1 10 ? 22.077  -20.334 28.482  1.00 61.23  ? 9   ASP   C OD1 1 
ATOM   1516 O OD2 . ASP   C 1 10 ? 23.537  -21.890 29.017  1.00 62.79  ? 9   ASP   C OD2 1 
ATOM   1517 N N   . LEU   C 1 11 ? 20.256  -22.071 24.475  1.00 48.75  ? 10  LEU   C N   1 
ATOM   1518 C CA  . LEU   C 1 11 ? 19.934  -22.603 23.159  1.00 45.62  ? 10  LEU   C CA  1 
ATOM   1519 C C   . LEU   C 1 11 ? 21.213  -23.065 22.470  1.00 40.32  ? 10  LEU   C C   1 
ATOM   1520 O O   . LEU   C 1 11 ? 22.207  -22.349 22.420  1.00 46.55  ? 10  LEU   C O   1 
ATOM   1521 C CB  . LEU   C 1 11 ? 19.198  -21.527 22.354  1.00 43.94  ? 10  LEU   C CB  1 
ATOM   1522 C CG  . LEU   C 1 11 ? 17.934  -20.960 22.997  1.00 42.99  ? 10  LEU   C CG  1 
ATOM   1523 C CD1 . LEU   C 1 11 ? 17.266  -20.000 22.020  1.00 47.93  ? 10  LEU   C CD1 1 
ATOM   1524 C CD2 . LEU   C 1 11 ? 16.989  -22.094 23.397  1.00 41.99  ? 10  LEU   C CD2 1 
ATOM   1525 N N   . VAL   C 1 12 ? 21.160  -24.261 21.837  1.00 39.85  ? 11  VAL   C N   1 
ATOM   1526 C CA  . VAL   C 1 12 ? 22.340  -24.887 21.279  1.00 40.73  ? 11  VAL   C CA  1 
ATOM   1527 C C   . VAL   C 1 12 ? 21.964  -25.609 19.976  1.00 37.57  ? 11  VAL   C C   1 
ATOM   1528 O O   . VAL   C 1 12 ? 20.772  -25.824 19.725  1.00 40.27  ? 11  VAL   C O   1 
ATOM   1529 C CB  . VAL   C 1 12 ? 22.999  -25.911 22.239  1.00 43.63  ? 11  VAL   C CB  1 
ATOM   1530 C CG1 . VAL   C 1 12 ? 23.507  -25.275 23.546  1.00 46.25  ? 11  VAL   C CG1 1 
ATOM   1531 C CG2 . VAL   C 1 12 ? 22.106  -27.121 22.510  1.00 42.66  ? 11  VAL   C CG2 1 
ATOM   1532 N N   . PHE   C 1 13 ? 23.007  -25.996 19.228  1.00 38.02  ? 12  PHE   C N   1 
ATOM   1533 C CA  . PHE   C 1 13 ? 22.943  -27.170 18.354  1.00 39.38  ? 12  PHE   C CA  1 
ATOM   1534 C C   . PHE   C 1 13 ? 23.608  -28.351 19.057  1.00 37.44  ? 12  PHE   C C   1 
ATOM   1535 O O   . PHE   C 1 13 ? 24.695  -28.230 19.623  1.00 39.91  ? 12  PHE   C O   1 
ATOM   1536 C CB  . PHE   C 1 13 ? 23.674  -26.947 17.025  1.00 43.83  ? 12  PHE   C CB  1 
ATOM   1537 C CG  . PHE   C 1 13 ? 22.912  -25.948 16.175  1.00 44.44  ? 12  PHE   C CG  1 
ATOM   1538 C CD1 . PHE   C 1 13 ? 21.883  -26.384 15.333  1.00 43.54  ? 12  PHE   C CD1 1 
ATOM   1539 C CD2 . PHE   C 1 13 ? 23.212  -24.588 16.231  1.00 45.18  ? 12  PHE   C CD2 1 
ATOM   1540 C CE1 . PHE   C 1 13 ? 21.184  -25.474 14.553  1.00 43.79  ? 12  PHE   C CE1 1 
ATOM   1541 C CE2 . PHE   C 1 13 ? 22.486  -23.687 15.472  1.00 45.62  ? 12  PHE   C CE2 1 
ATOM   1542 C CZ  . PHE   C 1 13 ? 21.485  -24.128 14.625  1.00 45.67  ? 12  PHE   C CZ  1 
ATOM   1543 N N   . ALA   C 1 14 ? 22.954  -29.527 19.016  1.00 38.21  ? 13  ALA   C N   1 
ATOM   1544 C CA  . ALA   C 1 14 ? 23.432  -30.684 19.759  1.00 34.99  ? 13  ALA   C CA  1 
ATOM   1545 C C   . ALA   C 1 14 ? 23.771  -31.785 18.759  1.00 39.80  ? 13  ALA   C C   1 
ATOM   1546 O O   . ALA   C 1 14 ? 22.919  -32.099 17.931  1.00 35.92  ? 13  ALA   C O   1 
ATOM   1547 C CB  . ALA   C 1 14 ? 22.355  -31.133 20.722  1.00 35.78  ? 13  ALA   C CB  1 
ATOM   1548 N N   . LYS   C 1 15 ? 24.977  -32.370 18.876  1.00 35.25  ? 14  LYS   C N   1 
ATOM   1549 C CA  . LYS   C 1 15 ? 25.425  -33.380 17.916  1.00 37.60  ? 14  LYS   C CA  1 
ATOM   1550 C C   . LYS   C 1 15 ? 25.409  -34.771 18.535  1.00 36.59  ? 14  LYS   C C   1 
ATOM   1551 O O   . LYS   C 1 15 ? 26.151  -35.043 19.479  1.00 41.38  ? 14  LYS   C O   1 
ATOM   1552 C CB  . LYS   C 1 15 ? 26.852  -33.089 17.432  1.00 39.43  ? 14  LYS   C CB  1 
ATOM   1553 C CG  . LYS   C 1 15 ? 27.350  -34.064 16.350  1.00 41.66  ? 14  LYS   C CG  1 
ATOM   1554 C CD  . LYS   C 1 15 ? 26.508  -33.939 15.077  1.00 42.66  ? 14  LYS   C CD  1 
ATOM   1555 C CE  . LYS   C 1 15 ? 26.937  -34.741 13.868  1.00 45.28  ? 14  LYS   C CE  1 
ATOM   1556 N NZ  . LYS   C 1 15 ? 26.865  -36.183 14.097  1.00 38.74  ? 14  LYS   C NZ  1 
ATOM   1557 N N   . MET   C 1 16 ? 24.607  -35.689 17.962  1.00 34.26  ? 15  MET   C N   1 
ATOM   1558 C CA  . MET   C 1 16 ? 24.653  -37.112 18.308  1.00 35.90  ? 15  MET   C CA  1 
ATOM   1559 C C   . MET   C 1 16 ? 25.134  -37.898 17.091  1.00 43.40  ? 15  MET   C C   1 
ATOM   1560 O O   . MET   C 1 16 ? 24.879  -37.505 15.955  1.00 37.05  ? 15  MET   C O   1 
ATOM   1561 C CB  . MET   C 1 16 ? 23.248  -37.638 18.622  1.00 38.72  ? 15  MET   C CB  1 
ATOM   1562 C CG  . MET   C 1 16 ? 22.520  -36.923 19.778  1.00 38.85  ? 15  MET   C CG  1 
ATOM   1563 S SD  . MET   C 1 16 ? 20.945  -37.664 20.238  1.00 46.07  ? 15  MET   C SD  1 
ATOM   1564 C CE  . MET   C 1 16 ? 19.960  -37.076 18.846  1.00 44.79  ? 15  MET   C CE  1 
ATOM   1565 N N   . LYS   C 1 17 ? 25.754  -39.061 17.331  1.00 40.63  ? 16  LYS   C N   1 
ATOM   1566 C CA  . LYS   C 1 17 ? 26.162  -39.915 16.220  1.00 45.35  ? 16  LYS   C CA  1 
ATOM   1567 C C   . LYS   C 1 17 ? 24.922  -40.308 15.414  1.00 36.70  ? 16  LYS   C C   1 
ATOM   1568 O O   . LYS   C 1 17 ? 23.937  -40.788 15.982  1.00 40.53  ? 16  LYS   C O   1 
ATOM   1569 C CB  . LYS   C 1 17 ? 26.791  -41.192 16.793  1.00 41.04  ? 16  LYS   C CB  1 
ATOM   1570 C CG  . LYS   C 1 17 ? 27.359  -42.208 15.788  1.00 45.08  ? 16  LYS   C CG  1 
ATOM   1571 C CD  . LYS   C 1 17 ? 28.591  -41.550 15.173  1.00 50.01  ? 16  LYS   C CD  1 
ATOM   1572 C CE  . LYS   C 1 17 ? 29.359  -42.405 14.211  1.00 62.91  ? 16  LYS   C CE  1 
ATOM   1573 N NZ  . LYS   C 1 17 ? 30.540  -41.676 13.743  1.00 53.11  ? 16  LYS   C NZ  1 
ATOM   1574 N N   . GLY   C 1 18 ? 25.012  -40.088 14.092  1.00 43.51  ? 17  GLY   C N   1 
ATOM   1575 C CA  . GLY   C 1 18 ? 24.003  -40.574 13.158  1.00 40.27  ? 17  GLY   C CA  1 
ATOM   1576 C C   . GLY   C 1 18 ? 22.944  -39.517 12.869  1.00 39.79  ? 17  GLY   C C   1 
ATOM   1577 O O   . GLY   C 1 18 ? 21.917  -39.837 12.272  1.00 39.56  ? 17  GLY   C O   1 
ATOM   1578 N N   . TYR   C 1 19 ? 23.161  -38.308 13.407  1.00 37.83  ? 18  TYR   C N   1 
ATOM   1579 C CA  . TYR   C 1 19 ? 22.233  -37.190 13.208  1.00 38.46  ? 18  TYR   C CA  1 
ATOM   1580 C C   . TYR   C 1 19 ? 23.017  -35.920 12.917  1.00 37.29  ? 18  TYR   C C   1 
ATOM   1581 O O   . TYR   C 1 19 ? 24.125  -35.732 13.419  1.00 36.47  ? 18  TYR   C O   1 
ATOM   1582 C CB  . TYR   C 1 19 ? 21.374  -36.942 14.453  1.00 35.30  ? 18  TYR   C CB  1 
ATOM   1583 C CG  . TYR   C 1 19 ? 20.553  -38.152 14.832  1.00 38.34  ? 18  TYR   C CG  1 
ATOM   1584 C CD1 . TYR   C 1 19 ? 21.090  -39.182 15.596  1.00 40.19  ? 18  TYR   C CD1 1 
ATOM   1585 C CD2 . TYR   C 1 19 ? 19.229  -38.234 14.425  1.00 37.97  ? 18  TYR   C CD2 1 
ATOM   1586 C CE1 . TYR   C 1 19 ? 20.314  -40.280 15.939  1.00 37.52  ? 18  TYR   C CE1 1 
ATOM   1587 C CE2 . TYR   C 1 19 ? 18.446  -39.320 14.778  1.00 46.88  ? 18  TYR   C CE2 1 
ATOM   1588 C CZ  . TYR   C 1 19 ? 18.986  -40.334 15.544  1.00 41.74  ? 18  TYR   C CZ  1 
ATOM   1589 O OH  . TYR   C 1 19 ? 18.186  -41.409 15.849  1.00 52.46  ? 18  TYR   C OH  1 
ATOM   1590 N N   . PRO   C 1 20 ? 22.439  -34.984 12.125  1.00 36.78  ? 19  PRO   C N   1 
ATOM   1591 C CA  . PRO   C 1 20 ? 23.055  -33.691 11.877  1.00 36.18  ? 19  PRO   C CA  1 
ATOM   1592 C C   . PRO   C 1 20 ? 22.995  -32.883 13.175  1.00 35.74  ? 19  PRO   C C   1 
ATOM   1593 O O   . PRO   C 1 20 ? 22.212  -33.169 14.105  1.00 34.68  ? 19  PRO   C O   1 
ATOM   1594 C CB  . PRO   C 1 20 ? 22.142  -33.074 10.788  1.00 38.16  ? 19  PRO   C CB  1 
ATOM   1595 C CG  . PRO   C 1 20 ? 20.796  -33.712 11.040  1.00 37.55  ? 19  PRO   C CG  1 
ATOM   1596 C CD  . PRO   C 1 20 ? 21.107  -35.122 11.498  1.00 36.59  ? 19  PRO   C CD  1 
ATOM   1597 N N   . HIS   C 1 21 ? 23.850  -31.870 13.253  1.00 38.16  ? 20  HIS   C N   1 
ATOM   1598 C CA  . HIS   C 1 21 ? 23.762  -30.936 14.378  1.00 36.35  ? 20  HIS   C CA  1 
ATOM   1599 C C   . HIS   C 1 21 ? 22.333  -30.431 14.522  1.00 37.71  ? 20  HIS   C C   1 
ATOM   1600 O O   . HIS   C 1 21 ? 21.783  -29.886 13.585  1.00 36.48  ? 20  HIS   C O   1 
ATOM   1601 C CB  . HIS   C 1 21 ? 24.738  -29.779 14.157  1.00 42.44  ? 20  HIS   C CB  1 
ATOM   1602 C CG  . HIS   C 1 21 ? 26.179  -30.181 14.237  1.00 41.97  ? 20  HIS   C CG  1 
ATOM   1603 N ND1 . HIS   C 1 21 ? 26.929  -30.784 13.246  1.00 42.92  ? 20  HIS   C ND1 1 
ATOM   1604 C CD2 . HIS   C 1 21 ? 26.997  -30.041 15.290  1.00 44.90  ? 20  HIS   C CD2 1 
ATOM   1605 C CE1 . HIS   C 1 21 ? 28.160  -30.993 13.695  1.00 49.18  ? 20  HIS   C CE1 1 
ATOM   1606 N NE2 . HIS   C 1 21 ? 28.233  -30.511 14.923  1.00 42.19  ? 20  HIS   C NE2 1 
ATOM   1607 N N   . TRP   C 1 22 ? 21.744  -30.552 15.724  1.00 34.03  ? 21  TRP   C N   1 
ATOM   1608 C CA  . TRP   C 1 22 ? 20.296  -30.463 15.829  1.00 34.19  ? 21  TRP   C CA  1 
ATOM   1609 C C   . TRP   C 1 22 ? 19.899  -29.276 16.720  1.00 35.40  ? 21  TRP   C C   1 
ATOM   1610 O O   . TRP   C 1 22 ? 20.431  -29.122 17.840  1.00 35.36  ? 21  TRP   C O   1 
ATOM   1611 C CB  . TRP   C 1 22 ? 19.740  -31.777 16.403  1.00 34.80  ? 21  TRP   C CB  1 
ATOM   1612 C CG  . TRP   C 1 22 ? 18.289  -31.962 16.046  1.00 35.02  ? 21  TRP   C CG  1 
ATOM   1613 C CD1 . TRP   C 1 22 ? 17.202  -31.372 16.617  1.00 38.31  ? 21  TRP   C CD1 1 
ATOM   1614 C CD2 . TRP   C 1 22 ? 17.795  -32.858 15.022  1.00 34.65  ? 21  TRP   C CD2 1 
ATOM   1615 N NE1 . TRP   C 1 22 ? 16.062  -31.819 15.987  1.00 36.52  ? 21  TRP   C NE1 1 
ATOM   1616 C CE2 . TRP   C 1 22 ? 16.389  -32.721 15.011  1.00 36.40  ? 21  TRP   C CE2 1 
ATOM   1617 C CE3 . TRP   C 1 22 ? 18.405  -33.747 14.131  1.00 35.36  ? 21  TRP   C CE3 1 
ATOM   1618 C CZ2 . TRP   C 1 22 ? 15.585  -33.469 14.134  1.00 35.01  ? 21  TRP   C CZ2 1 
ATOM   1619 C CZ3 . TRP   C 1 22 ? 17.619  -34.449 13.231  1.00 35.60  ? 21  TRP   C CZ3 1 
ATOM   1620 C CH2 . TRP   C 1 22 ? 16.223  -34.323 13.267  1.00 35.52  ? 21  TRP   C CH2 1 
ATOM   1621 N N   . PRO   C 1 23 ? 18.919  -28.415 16.340  1.00 39.97  ? 22  PRO   C N   1 
ATOM   1622 C CA  . PRO   C 1 23 ? 18.490  -27.354 17.266  1.00 35.54  ? 22  PRO   C CA  1 
ATOM   1623 C C   . PRO   C 1 23 ? 17.939  -27.877 18.588  1.00 34.23  ? 22  PRO   C C   1 
ATOM   1624 O O   . PRO   C 1 23 ? 17.087  -28.759 18.601  1.00 35.28  ? 22  PRO   C O   1 
ATOM   1625 C CB  . PRO   C 1 23 ? 17.436  -26.585 16.441  1.00 38.97  ? 22  PRO   C CB  1 
ATOM   1626 C CG  . PRO   C 1 23 ? 16.890  -27.623 15.475  1.00 35.23  ? 22  PRO   C CG  1 
ATOM   1627 C CD  . PRO   C 1 23 ? 18.141  -28.417 15.077  1.00 35.31  ? 22  PRO   C CD  1 
ATOM   1628 N N   . ALA   C 1 24 ? 18.461  -27.335 19.711  1.00 36.51  ? 23  ALA   C N   1 
ATOM   1629 C CA  . ALA   C 1 24 ? 18.164  -27.915 21.012  1.00 42.53  ? 23  ALA   C CA  1 
ATOM   1630 C C   . ALA   C 1 24 ? 18.302  -26.860 22.110  1.00 43.63  ? 23  ALA   C C   1 
ATOM   1631 O O   . ALA   C 1 24 ? 18.788  -25.749 21.853  1.00 44.42  ? 23  ALA   C O   1 
ATOM   1632 C CB  . ALA   C 1 24 ? 19.110  -29.102 21.261  1.00 38.27  ? 23  ALA   C CB  1 
ATOM   1633 N N   . ARG   C 1 25 ? 17.863  -27.227 23.325  1.00 45.64  ? 24  ARG   C N   1 
ATOM   1634 C CA  . ARG   C 1 25 ? 18.186  -26.443 24.505  1.00 41.35  ? 24  ARG   C CA  1 
ATOM   1635 C C   . ARG   C 1 25 ? 18.705  -27.338 25.638  1.00 44.19  ? 24  ARG   C C   1 
ATOM   1636 O O   . ARG   C 1 25 ? 18.439  -28.538 25.666  1.00 42.00  ? 24  ARG   C O   1 
ATOM   1637 C CB  . ARG   C 1 25 ? 16.952  -25.673 24.975  1.00 41.25  ? 24  ARG   C CB  1 
ATOM   1638 C CG  . ARG   C 1 25 ? 15.685  -26.440 25.318  1.00 54.35  ? 24  ARG   C CG  1 
ATOM   1639 C CD  . ARG   C 1 25 ? 14.650  -25.523 25.964  1.00 53.21  ? 24  ARG   C CD  1 
ATOM   1640 N NE  . ARG   C 1 25 ? 13.492  -26.350 26.323  1.00 61.42  ? 24  ARG   C NE  1 
ATOM   1641 C CZ  . ARG   C 1 25 ? 12.216  -26.111 26.075  1.00 60.27  ? 24  ARG   C CZ  1 
ATOM   1642 N NH1 . ARG   C 1 25 ? 11.839  -24.963 25.535  1.00 55.88  ? 24  ARG   C NH1 1 
ATOM   1643 N NH2 . ARG   C 1 25 ? 11.311  -27.020 26.405  1.00 61.33  ? 24  ARG   C NH2 1 
ATOM   1644 N N   . ILE   C 1 26 ? 19.382  -26.706 26.591  1.00 46.16  ? 25  ILE   C N   1 
ATOM   1645 C CA  . ILE   C 1 26 ? 19.746  -27.336 27.853  1.00 48.95  ? 25  ILE   C CA  1 
ATOM   1646 C C   . ILE   C 1 26 ? 18.508  -27.352 28.741  1.00 52.15  ? 25  ILE   C C   1 
ATOM   1647 O O   . ILE   C 1 26 ? 17.951  -26.291 29.003  1.00 57.25  ? 25  ILE   C O   1 
ATOM   1648 C CB  . ILE   C 1 26 ? 20.885  -26.563 28.538  1.00 46.23  ? 25  ILE   C CB  1 
ATOM   1649 C CG1 . ILE   C 1 26 ? 22.086  -26.290 27.614  1.00 50.70  ? 25  ILE   C CG1 1 
ATOM   1650 C CG2 . ILE   C 1 26 ? 21.314  -27.296 29.823  1.00 48.46  ? 25  ILE   C CG2 1 
ATOM   1651 C CD1 . ILE   C 1 26 ? 22.817  -27.525 27.108  1.00 49.69  ? 25  ILE   C CD1 1 
ATOM   1652 N N   . ASP   C 1 27 ? 18.070  -28.540 29.170  1.00 51.57  ? 26  ASP   C N   1 
ATOM   1653 C CA  . ASP   C 1 27 ? 16.992  -28.654 30.138  1.00 61.53  ? 26  ASP   C CA  1 
ATOM   1654 C C   . ASP   C 1 27 ? 17.551  -28.500 31.548  1.00 72.30  ? 26  ASP   C C   1 
ATOM   1655 O O   . ASP   C 1 27 ? 18.756  -28.330 31.736  1.00 71.73  ? 26  ASP   C O   1 
ATOM   1656 C CB  . ASP   C 1 27 ? 16.273  -29.992 30.059  1.00 58.11  ? 26  ASP   C CB  1 
ATOM   1657 C CG  . ASP   C 1 27 ? 15.008  -30.037 29.215  1.00 64.59  ? 26  ASP   C CG  1 
ATOM   1658 O OD1 . ASP   C 1 27 ? 14.705  -29.013 28.565  1.00 59.65  ? 26  ASP   C OD1 1 
ATOM   1659 O OD2 . ASP   C 1 27 ? 14.329  -31.092 29.241  1.00 63.10  ? 26  ASP   C OD2 1 
ATOM   1660 N N   . ASP   C 1 28 ? 16.642  -28.551 32.526  1.00 79.07  ? 27  ASP   C N   1 
ATOM   1661 C CA  . ASP   C 1 28 ? 17.007  -28.744 33.918  1.00 82.05  ? 27  ASP   C CA  1 
ATOM   1662 C C   . ASP   C 1 28 ? 16.721  -30.199 34.264  1.00 77.20  ? 27  ASP   C C   1 
ATOM   1663 O O   . ASP   C 1 28 ? 16.197  -30.943 33.439  1.00 69.59  ? 27  ASP   C O   1 
ATOM   1664 C CB  . ASP   C 1 28 ? 16.259  -27.789 34.837  1.00 93.73  ? 27  ASP   C CB  1 
ATOM   1665 C CG  . ASP   C 1 28 ? 16.715  -27.742 36.293  1.00 106.84 ? 27  ASP   C CG  1 
ATOM   1666 O OD1 . ASP   C 1 28 ? 17.786  -28.310 36.610  1.00 106.68 ? 27  ASP   C OD1 1 
ATOM   1667 O OD2 . ASP   C 1 28 ? 15.991  -27.137 37.110  1.00 119.07 ? 27  ASP   C OD2 1 
ATOM   1668 N N   . ILE   C 1 29 ? 17.127  -30.588 35.476  1.00 78.79  ? 28  ILE   C N   1 
ATOM   1669 C CA  . ILE   C 1 29 ? 16.698  -31.813 36.124  1.00 74.55  ? 28  ILE   C CA  1 
ATOM   1670 C C   . ILE   C 1 29 ? 16.070  -31.393 37.459  1.00 74.23  ? 28  ILE   C C   1 
ATOM   1671 O O   . ILE   C 1 29 ? 16.654  -30.463 38.076  1.00 68.41  ? 28  ILE   C O   1 
ATOM   1672 C CB  . ILE   C 1 29 ? 17.895  -32.755 36.349  1.00 69.34  ? 28  ILE   C CB  1 
ATOM   1673 N N   . LYS   C 1 35 ? 19.950  -38.876 37.854  1.00 62.75  ? 34  LYS   C N   1 
ATOM   1674 C CA  . LYS   C 1 35 ? 21.021  -37.891 37.556  1.00 63.68  ? 34  LYS   C CA  1 
ATOM   1675 C C   . LYS   C 1 35 ? 21.629  -38.203 36.192  1.00 54.72  ? 34  LYS   C C   1 
ATOM   1676 O O   . LYS   C 1 35 ? 21.621  -39.347 35.749  1.00 54.12  ? 34  LYS   C O   1 
ATOM   1677 C CB  . LYS   C 1 35 ? 22.083  -37.948 38.660  1.00 66.13  ? 34  LYS   C CB  1 
ATOM   1678 N N   . PRO   C 1 36 ? 22.170  -37.186 35.489  1.00 55.45  ? 35  PRO   C N   1 
ATOM   1679 C CA  . PRO   C 1 36 ? 22.944  -37.410 34.275  1.00 57.34  ? 35  PRO   C CA  1 
ATOM   1680 C C   . PRO   C 1 36 ? 24.057  -38.422 34.536  1.00 59.92  ? 35  PRO   C C   1 
ATOM   1681 O O   . PRO   C 1 36 ? 24.415  -38.693 35.691  1.00 55.74  ? 35  PRO   C O   1 
ATOM   1682 C CB  . PRO   C 1 36 ? 23.516  -36.009 33.967  1.00 64.32  ? 35  PRO   C CB  1 
ATOM   1683 C CG  . PRO   C 1 36 ? 22.529  -35.047 34.592  1.00 60.19  ? 35  PRO   C CG  1 
ATOM   1684 C CD  . PRO   C 1 36 ? 22.048  -35.761 35.842  1.00 57.54  ? 35  PRO   C CD  1 
ATOM   1685 N N   . PRO   C 1 37 ? 24.621  -39.036 33.477  1.00 58.25  ? 36  PRO   C N   1 
ATOM   1686 C CA  . PRO   C 1 37 ? 25.900  -39.721 33.607  1.00 56.01  ? 36  PRO   C CA  1 
ATOM   1687 C C   . PRO   C 1 37 ? 26.833  -38.572 33.968  1.00 54.67  ? 36  PRO   C C   1 
ATOM   1688 O O   . PRO   C 1 37 ? 26.521  -37.400 33.720  1.00 49.00  ? 36  PRO   C O   1 
ATOM   1689 C CB  . PRO   C 1 37 ? 26.132  -40.262 32.186  1.00 54.77  ? 36  PRO   C CB  1 
ATOM   1690 C CG  . PRO   C 1 37 ? 24.734  -40.373 31.630  1.00 54.31  ? 36  PRO   C CG  1 
ATOM   1691 C CD  . PRO   C 1 37 ? 24.066  -39.110 32.112  1.00 51.75  ? 36  PRO   C CD  1 
ATOM   1692 N N   . PRO   C 1 38 ? 27.995  -38.858 34.593  1.00 45.40  ? 37  PRO   C N   1 
ATOM   1693 C CA  . PRO   C 1 38 ? 28.972  -37.808 34.883  1.00 47.85  ? 37  PRO   C CA  1 
ATOM   1694 C C   . PRO   C 1 38 ? 29.291  -36.920 33.687  1.00 42.76  ? 37  PRO   C C   1 
ATOM   1695 O O   . PRO   C 1 38 ? 29.599  -37.414 32.599  1.00 49.11  ? 37  PRO   C O   1 
ATOM   1696 C CB  . PRO   C 1 38 ? 30.191  -38.646 35.340  1.00 49.87  ? 37  PRO   C CB  1 
ATOM   1697 C CG  . PRO   C 1 38 ? 29.528  -39.829 36.011  1.00 49.62  ? 37  PRO   C CG  1 
ATOM   1698 C CD  . PRO   C 1 38 ? 28.420  -40.195 35.044  1.00 46.87  ? 37  PRO   C CD  1 
ATOM   1699 N N   . ASN   C 1 39 ? 29.179  -35.599 33.924  1.00 46.49  ? 38  ASN   C N   1 
ATOM   1700 C CA  . ASN   C 1 39 ? 29.637  -34.539 33.047  1.00 45.63  ? 38  ASN   C CA  1 
ATOM   1701 C C   . ASN   C 1 39 ? 28.755  -34.457 31.807  1.00 48.21  ? 38  ASN   C C   1 
ATOM   1702 O O   . ASN   C 1 39 ? 29.244  -34.015 30.760  1.00 51.38  ? 38  ASN   C O   1 
ATOM   1703 C CB  . ASN   C 1 39 ? 31.096  -34.704 32.642  1.00 47.35  ? 38  ASN   C CB  1 
ATOM   1704 C CG  . ASN   C 1 39 ? 31.734  -33.485 32.011  1.00 56.93  ? 38  ASN   C CG  1 
ATOM   1705 O OD1 . ASN   C 1 39 ? 31.515  -32.357 32.461  1.00 61.97  ? 38  ASN   C OD1 1 
ATOM   1706 N ND2 . ASN   C 1 39 ? 32.544  -33.681 30.977  1.00 53.13  ? 38  ASN   C ND2 1 
ATOM   1707 N N   . LYS   C 1 40 ? 27.497  -34.914 31.935  1.00 43.36  ? 39  LYS   C N   1 
ATOM   1708 C CA  . LYS   C 1 40 ? 26.547  -34.814 30.832  1.00 38.98  ? 39  LYS   C CA  1 
ATOM   1709 C C   . LYS   C 1 40 ? 25.430  -33.834 31.169  1.00 42.01  ? 39  LYS   C C   1 
ATOM   1710 O O   . LYS   C 1 40 ? 25.034  -33.687 32.314  1.00 45.55  ? 39  LYS   C O   1 
ATOM   1711 C CB  . LYS   C 1 40 ? 25.848  -36.143 30.510  1.00 40.47  ? 39  LYS   C CB  1 
ATOM   1712 C CG  . LYS   C 1 40 ? 26.744  -37.280 30.093  1.00 45.55  ? 39  LYS   C CG  1 
ATOM   1713 C CD  . LYS   C 1 40 ? 27.591  -37.092 28.846  1.00 55.55  ? 39  LYS   C CD  1 
ATOM   1714 C CE  . LYS   C 1 40 ? 28.407  -38.332 28.556  1.00 61.51  ? 39  LYS   C CE  1 
ATOM   1715 N NZ  . LYS   C 1 40 ? 29.555  -38.083 27.678  1.00 67.00  ? 39  LYS   C NZ  1 
ATOM   1716 N N   . TYR   C 1 41 ? 24.892  -33.182 30.130  1.00 40.85  ? 40  TYR   C N   1 
ATOM   1717 C CA  . TYR   C 1 41 ? 23.785  -32.242 30.262  1.00 43.71  ? 40  TYR   C CA  1 
ATOM   1718 C C   . TYR   C 1 41 ? 22.514  -32.892 29.738  1.00 41.95  ? 40  TYR   C C   1 
ATOM   1719 O O   . TYR   C 1 41 ? 22.586  -33.616 28.750  1.00 39.39  ? 40  TYR   C O   1 
ATOM   1720 C CB  . TYR   C 1 41 ? 23.945  -31.023 29.348  1.00 36.68  ? 40  TYR   C CB  1 
ATOM   1721 C CG  . TYR   C 1 41 ? 25.107  -30.124 29.742  1.00 36.37  ? 40  TYR   C CG  1 
ATOM   1722 C CD1 . TYR   C 1 41 ? 26.403  -30.363 29.278  1.00 37.99  ? 40  TYR   C CD1 1 
ATOM   1723 C CD2 . TYR   C 1 41 ? 24.920  -29.090 30.654  1.00 43.84  ? 40  TYR   C CD2 1 
ATOM   1724 C CE1 . TYR   C 1 41 ? 27.481  -29.583 29.654  1.00 50.26  ? 40  TYR   C CE1 1 
ATOM   1725 C CE2 . TYR   C 1 41 ? 25.999  -28.308 31.038  1.00 41.95  ? 40  TYR   C CE2 1 
ATOM   1726 C CZ  . TYR   C 1 41 ? 27.265  -28.547 30.546  1.00 48.50  ? 40  TYR   C CZ  1 
ATOM   1727 O OH  . TYR   C 1 41 ? 28.301  -27.770 30.962  1.00 56.43  ? 40  TYR   C OH  1 
ATOM   1728 N N   . PRO   C 1 42 ? 21.331  -32.581 30.329  1.00 45.29  ? 41  PRO   C N   1 
ATOM   1729 C CA  . PRO   C 1 42 ? 20.040  -33.005 29.793  1.00 43.33  ? 41  PRO   C CA  1 
ATOM   1730 C C   . PRO   C 1 42 ? 19.707  -32.084 28.630  1.00 43.91  ? 41  PRO   C C   1 
ATOM   1731 O O   . PRO   C 1 42 ? 19.716  -30.866 28.781  1.00 44.15  ? 41  PRO   C O   1 
ATOM   1732 C CB  . PRO   C 1 42 ? 19.032  -32.824 30.949  1.00 47.36  ? 41  PRO   C CB  1 
ATOM   1733 C CG  . PRO   C 1 42 ? 19.769  -32.006 31.978  1.00 48.69  ? 41  PRO   C CG  1 
ATOM   1734 C CD  . PRO   C 1 42 ? 21.188  -31.729 31.525  1.00 49.27  ? 41  PRO   C CD  1 
ATOM   1735 N N   . ILE   C 1 43 ? 19.432  -32.695 27.474  1.00 41.69  ? 42  ILE   C N   1 
ATOM   1736 C CA  . ILE   C 1 43 ? 19.203  -31.892 26.280  1.00 41.75  ? 42  ILE   C CA  1 
ATOM   1737 C C   . ILE   C 1 43 ? 17.756  -32.105 25.876  1.00 37.01  ? 42  ILE   C C   1 
ATOM   1738 O O   . ILE   C 1 43 ? 17.250  -33.215 25.955  1.00 42.98  ? 42  ILE   C O   1 
ATOM   1739 C CB  . ILE   C 1 43 ? 20.154  -32.331 25.153  1.00 37.80  ? 42  ILE   C CB  1 
ATOM   1740 C CG1 . ILE   C 1 43 ? 21.622  -32.157 25.554  1.00 37.44  ? 42  ILE   C CG1 1 
ATOM   1741 C CG2 . ILE   C 1 43 ? 19.819  -31.605 23.834  1.00 43.52  ? 42  ILE   C CG2 1 
ATOM   1742 C CD1 . ILE   C 1 43 ? 22.001  -30.727 25.913  1.00 37.68  ? 42  ILE   C CD1 1 
ATOM   1743 N N   . PHE   C 1 44 ? 17.086  -31.050 25.381  1.00 40.73  ? 43  PHE   C N   1 
ATOM   1744 C CA  . PHE   C 1 44 ? 15.801  -31.273 24.731  1.00 40.90  ? 43  PHE   C CA  1 
ATOM   1745 C C   . PHE   C 1 44 ? 15.948  -30.821 23.280  1.00 39.53  ? 43  PHE   C C   1 
ATOM   1746 O O   . PHE   C 1 44 ? 16.535  -29.754 23.042  1.00 39.71  ? 43  PHE   C O   1 
ATOM   1747 C CB  . PHE   C 1 44 ? 14.755  -30.349 25.360  1.00 45.10  ? 43  PHE   C CB  1 
ATOM   1748 C CG  . PHE   C 1 44 ? 13.372  -30.305 24.711  1.00 45.99  ? 43  PHE   C CG  1 
ATOM   1749 C CD1 . PHE   C 1 44 ? 12.423  -31.280 24.997  1.00 47.11  ? 43  PHE   C CD1 1 
ATOM   1750 C CD2 . PHE   C 1 44 ? 13.031  -29.278 23.825  1.00 47.94  ? 43  PHE   C CD2 1 
ATOM   1751 C CE1 . PHE   C 1 44 ? 11.155  -31.235 24.416  1.00 51.34  ? 43  PHE   C CE1 1 
ATOM   1752 C CE2 . PHE   C 1 44 ? 11.760  -29.228 23.242  1.00 43.81  ? 43  PHE   C CE2 1 
ATOM   1753 C CZ  . PHE   C 1 44 ? 10.827  -30.201 23.547  1.00 52.00  ? 43  PHE   C CZ  1 
ATOM   1754 N N   . PHE   C 1 45 ? 15.474  -31.677 22.365  1.00 39.21  ? 44  PHE   C N   1 
ATOM   1755 C CA  . PHE   C 1 45 ? 15.635  -31.453 20.934  1.00 41.51  ? 44  PHE   C CA  1 
ATOM   1756 C C   . PHE   C 1 45 ? 14.366  -30.817 20.381  1.00 36.51  ? 44  PHE   C C   1 
ATOM   1757 O O   . PHE   C 1 45 ? 13.268  -31.366 20.502  1.00 44.18  ? 44  PHE   C O   1 
ATOM   1758 C CB  . PHE   C 1 45 ? 15.926  -32.766 20.216  1.00 39.32  ? 44  PHE   C CB  1 
ATOM   1759 C CG  . PHE   C 1 45 ? 17.293  -33.345 20.535  1.00 37.29  ? 44  PHE   C CG  1 
ATOM   1760 C CD1 . PHE   C 1 45 ? 18.410  -32.966 19.799  1.00 35.20  ? 44  PHE   C CD1 1 
ATOM   1761 C CD2 . PHE   C 1 45 ? 17.440  -34.286 21.558  1.00 38.90  ? 44  PHE   C CD2 1 
ATOM   1762 C CE1 . PHE   C 1 45 ? 19.676  -33.512 20.070  1.00 41.32  ? 44  PHE   C CE1 1 
ATOM   1763 C CE2 . PHE   C 1 45 ? 18.691  -34.824 21.830  1.00 42.73  ? 44  PHE   C CE2 1 
ATOM   1764 C CZ  . PHE   C 1 45 ? 19.801  -34.429 21.099  1.00 37.62  ? 44  PHE   C CZ  1 
ATOM   1765 N N   . PHE   C 1 46 ? 14.519  -29.638 19.751  1.00 40.85  ? 45  PHE   C N   1 
ATOM   1766 C CA  . PHE   C 1 46 ? 13.356  -29.067 19.080  1.00 37.64  ? 45  PHE   C CA  1 
ATOM   1767 C C   . PHE   C 1 46 ? 12.912  -29.927 17.903  1.00 40.66  ? 45  PHE   C C   1 
ATOM   1768 O O   . PHE   C 1 46 ? 13.706  -30.671 17.308  1.00 38.48  ? 45  PHE   C O   1 
ATOM   1769 C CB  . PHE   C 1 46 ? 13.635  -27.629 18.637  1.00 36.30  ? 45  PHE   C CB  1 
ATOM   1770 C CG  . PHE   C 1 46 ? 13.868  -26.642 19.761  1.00 40.33  ? 45  PHE   C CG  1 
ATOM   1771 C CD1 . PHE   C 1 46 ? 12.812  -26.184 20.549  1.00 40.43  ? 45  PHE   C CD1 1 
ATOM   1772 C CD2 . PHE   C 1 46 ? 15.155  -26.167 19.994  1.00 41.34  ? 45  PHE   C CD2 1 
ATOM   1773 C CE1 . PHE   C 1 46 ? 13.067  -25.274 21.565  1.00 44.78  ? 45  PHE   C CE1 1 
ATOM   1774 C CE2 . PHE   C 1 46 ? 15.403  -25.270 21.020  1.00 46.73  ? 45  PHE   C CE2 1 
ATOM   1775 C CZ  . PHE   C 1 46 ? 14.356  -24.830 21.791  1.00 40.95  ? 45  PHE   C CZ  1 
ATOM   1776 N N   . GLY   C 1 47 ? 11.628  -29.778 17.522  1.00 36.01  ? 46  GLY   C N   1 
ATOM   1777 C CA  . GLY   C 1 47 ? 11.144  -30.507 16.365  1.00 39.27  ? 46  GLY   C CA  1 
ATOM   1778 C C   . GLY   C 1 47 ? 10.658  -31.905 16.754  1.00 47.33  ? 46  GLY   C C   1 
ATOM   1779 O O   . GLY   C 1 47 ? 9.470   -32.198 16.668  1.00 48.36  ? 46  GLY   C O   1 
ATOM   1780 N N   . THR   C 1 48 ? 11.589  -32.768 17.195  1.00 40.19  ? 47  THR   C N   1 
ATOM   1781 C CA  . THR   C 1 48 ? 11.241  -34.130 17.591  1.00 41.81  ? 47  THR   C CA  1 
ATOM   1782 C C   . THR   C 1 48 ? 10.696  -34.132 19.011  1.00 43.90  ? 47  THR   C C   1 
ATOM   1783 O O   . THR   C 1 48 ? 9.930   -35.028 19.352  1.00 47.89  ? 47  THR   C O   1 
ATOM   1784 C CB  . THR   C 1 48 ? 12.480  -35.017 17.538  1.00 39.34  ? 47  THR   C CB  1 
ATOM   1785 O OG1 . THR   C 1 48 ? 13.327  -34.454 18.548  1.00 41.36  ? 47  THR   C OG1 1 
ATOM   1786 C CG2 . THR   C 1 48 ? 13.040  -35.171 16.139  1.00 41.30  ? 47  THR   C CG2 1 
ATOM   1787 N N   . HIS   C 1 49 ? 11.160  -33.183 19.830  1.00 43.55  ? 48  HIS   C N   1 
ATOM   1788 C CA  . HIS   C 1 49 ? 10.756  -33.023 21.221  1.00 49.46  ? 48  HIS   C CA  1 
ATOM   1789 C C   . HIS   C 1 49 ? 11.211  -34.205 22.086  1.00 45.14  ? 48  HIS   C C   1 
ATOM   1790 O O   . HIS   C 1 49 ? 10.584  -34.505 23.109  1.00 53.06  ? 48  HIS   C O   1 
ATOM   1791 C CB  . HIS   C 1 49 ? 9.242   -32.811 21.340  1.00 45.81  ? 48  HIS   C CB  1 
ATOM   1792 C CG  . HIS   C 1 49 ? 8.678   -31.692 20.524  1.00 50.52  ? 48  HIS   C CG  1 
ATOM   1793 N ND1 . HIS   C 1 49 ? 7.514   -31.864 19.805  1.00 57.01  ? 48  HIS   C ND1 1 
ATOM   1794 C CD2 . HIS   C 1 49 ? 9.059   -30.428 20.317  1.00 52.06  ? 48  HIS   C CD2 1 
ATOM   1795 C CE1 . HIS   C 1 49 ? 7.218   -30.738 19.174  1.00 56.56  ? 48  HIS   C CE1 1 
ATOM   1796 N NE2 . HIS   C 1 49 ? 8.147   -29.854 19.458  1.00 53.52  ? 48  HIS   C NE2 1 
ATOM   1797 N N   . GLU   C 1 50 ? 12.320  -34.837 21.693  1.00 43.10  ? 49  GLU   C N   1 
ATOM   1798 C CA  . GLU   C 1 50 ? 12.916  -35.943 22.424  1.00 44.72  ? 49  GLU   C CA  1 
ATOM   1799 C C   . GLU   C 1 50 ? 14.009  -35.428 23.366  1.00 42.46  ? 49  GLU   C C   1 
ATOM   1800 O O   . GLU   C 1 50 ? 14.357  -34.251 23.374  1.00 45.28  ? 49  GLU   C O   1 
ATOM   1801 C CB  . GLU   C 1 50 ? 13.397  -36.971 21.400  1.00 46.38  ? 49  GLU   C CB  1 
ATOM   1802 C CG  . GLU   C 1 50 ? 12.276  -37.557 20.544  1.00 50.35  ? 49  GLU   C CG  1 
ATOM   1803 C CD  . GLU   C 1 50 ? 12.771  -38.521 19.487  1.00 54.67  ? 49  GLU   C CD  1 
ATOM   1804 O OE1 . GLU   C 1 50 ? 13.986  -38.792 19.484  1.00 64.96  ? 49  GLU   C OE1 1 
ATOM   1805 O OE2 . GLU   C 1 50 ? 11.964  -38.991 18.662  1.00 63.84  ? 49  GLU   C OE2 1 
ATOM   1806 N N   . THR   C 1 51 ? 14.510  -36.311 24.246  1.00 47.58  ? 50  THR   C N   1 
ATOM   1807 C CA  . THR   C 1 51 ? 15.517  -35.929 25.235  1.00 45.99  ? 50  THR   C CA  1 
ATOM   1808 C C   . THR   C 1 51 ? 16.664  -36.927 25.147  1.00 40.44  ? 50  THR   C C   1 
ATOM   1809 O O   . THR   C 1 51 ? 16.448  -38.077 24.770  1.00 45.98  ? 50  THR   C O   1 
ATOM   1810 C CB  . THR   C 1 51 ? 14.958  -35.917 26.663  1.00 48.68  ? 50  THR   C CB  1 
ATOM   1811 O OG1 . THR   C 1 51 ? 14.447  -37.238 26.854  1.00 44.58  ? 50  THR   C OG1 1 
ATOM   1812 C CG2 . THR   C 1 51 ? 13.960  -34.799 26.900  1.00 52.79  ? 50  THR   C CG2 1 
ATOM   1813 N N   . ALA   C 1 52 ? 17.866  -36.454 25.478  1.00 40.72  ? 51  ALA   C N   1 
ATOM   1814 C CA  . ALA   C 1 52 ? 19.072  -37.264 25.596  1.00 42.01  ? 51  ALA   C CA  1 
ATOM   1815 C C   . ALA   C 1 52 ? 20.039  -36.565 26.551  1.00 48.85  ? 51  ALA   C C   1 
ATOM   1816 O O   . ALA   C 1 52 ? 19.813  -35.424 26.949  1.00 45.97  ? 51  ALA   C O   1 
ATOM   1817 C CB  . ALA   C 1 52 ? 19.728  -37.464 24.250  1.00 45.29  ? 51  ALA   C CB  1 
ATOM   1818 N N   . PHE   C 1 53 ? 21.118  -37.266 26.920  1.00 44.07  ? 52  PHE   C N   1 
ATOM   1819 C CA  . PHE   C 1 53 ? 22.181  -36.695 27.738  1.00 46.07  ? 52  PHE   C CA  1 
ATOM   1820 C C   . PHE   C 1 53 ? 23.412  -36.547 26.864  1.00 41.68  ? 52  PHE   C C   1 
ATOM   1821 O O   . PHE   C 1 53 ? 23.839  -37.510 26.238  1.00 42.95  ? 52  PHE   C O   1 
ATOM   1822 C CB  . PHE   C 1 53 ? 22.585  -37.565 28.941  1.00 45.78  ? 52  PHE   C CB  1 
ATOM   1823 C CG  . PHE   C 1 53 ? 21.549  -37.588 30.053  1.00 49.16  ? 52  PHE   C CG  1 
ATOM   1824 C CD1 . PHE   C 1 53 ? 21.283  -36.449 30.802  1.00 47.43  ? 52  PHE   C CD1 1 
ATOM   1825 C CD2 . PHE   C 1 53 ? 20.820  -38.741 30.335  1.00 62.49  ? 52  PHE   C CD2 1 
ATOM   1826 C CE1 . PHE   C 1 53 ? 20.338  -36.468 31.820  1.00 52.31  ? 52  PHE   C CE1 1 
ATOM   1827 C CE2 . PHE   C 1 53 ? 19.867  -38.747 31.349  1.00 60.33  ? 52  PHE   C CE2 1 
ATOM   1828 C CZ  . PHE   C 1 53 ? 19.621  -37.608 32.081  1.00 55.97  ? 52  PHE   C CZ  1 
ATOM   1829 N N   . LEU   C 1 54 ? 24.026  -35.359 26.869  1.00 37.29  ? 53  LEU   C N   1 
ATOM   1830 C CA  . LEU   C 1 54 ? 25.187  -35.148 26.013  1.00 38.19  ? 53  LEU   C CA  1 
ATOM   1831 C C   . LEU   C 1 54 ? 26.273  -34.374 26.763  1.00 36.83  ? 53  LEU   C C   1 
ATOM   1832 O O   . LEU   C 1 54 ? 25.965  -33.575 27.634  1.00 42.86  ? 53  LEU   C O   1 
ATOM   1833 C CB  . LEU   C 1 54 ? 24.777  -34.387 24.750  1.00 40.23  ? 53  LEU   C CB  1 
ATOM   1834 C CG  . LEU   C 1 54 ? 23.973  -35.171 23.711  1.00 45.31  ? 53  LEU   C CG  1 
ATOM   1835 C CD1 . LEU   C 1 54 ? 23.692  -34.180 22.603  1.00 45.90  ? 53  LEU   C CD1 1 
ATOM   1836 C CD2 . LEU   C 1 54 ? 24.783  -36.349 23.156  1.00 50.65  ? 53  LEU   C CD2 1 
ATOM   1837 N N   . GLY   C 1 55 ? 27.533  -34.591 26.383  1.00 41.78  ? 54  GLY   C N   1 
ATOM   1838 C CA  . GLY   C 1 55 ? 28.649  -33.868 26.976  1.00 43.04  ? 54  GLY   C CA  1 
ATOM   1839 C C   . GLY   C 1 55 ? 28.979  -32.580 26.222  1.00 49.90  ? 54  GLY   C C   1 
ATOM   1840 O O   . GLY   C 1 55 ? 28.459  -32.322 25.126  1.00 45.98  ? 54  GLY   C O   1 
ATOM   1841 N N   . PRO   C 1 56 ? 29.855  -31.715 26.787  1.00 49.59  ? 55  PRO   C N   1 
ATOM   1842 C CA  . PRO   C 1 56 ? 30.094  -30.386 26.230  1.00 49.88  ? 55  PRO   C CA  1 
ATOM   1843 C C   . PRO   C 1 56 ? 30.677  -30.383 24.825  1.00 47.40  ? 55  PRO   C C   1 
ATOM   1844 O O   . PRO   C 1 56 ? 30.403  -29.460 24.061  1.00 63.63  ? 55  PRO   C O   1 
ATOM   1845 C CB  . PRO   C 1 56 ? 31.006  -29.653 27.259  1.00 48.09  ? 55  PRO   C CB  1 
ATOM   1846 C CG  . PRO   C 1 56 ? 31.574  -30.766 28.105  1.00 44.79  ? 55  PRO   C CG  1 
ATOM   1847 C CD  . PRO   C 1 56 ? 30.620  -31.946 28.027  1.00 51.43  ? 55  PRO   C CD  1 
ATOM   1848 N N   . LYS   C 1 57 ? 31.442  -31.429 24.482  1.00 50.18  ? 56  LYS   C N   1 
ATOM   1849 C CA  . LYS   C 1 57 ? 32.065  -31.509 23.170  1.00 49.75  ? 56  LYS   C CA  1 
ATOM   1850 C C   . LYS   C 1 57 ? 30.979  -31.567 22.095  1.00 54.40  ? 56  LYS   C C   1 
ATOM   1851 O O   . LYS   C 1 57 ? 31.242  -31.267 20.928  1.00 48.67  ? 56  LYS   C O   1 
ATOM   1852 C CB  . LYS   C 1 57 ? 32.920  -32.768 22.981  1.00 52.95  ? 56  LYS   C CB  1 
ATOM   1853 N N   . ASP   C 1 58 ? 29.763  -31.951 22.510  1.00 49.37  ? 57  ASP   C N   1 
ATOM   1854 C CA  . ASP   C 1 58 ? 28.702  -32.262 21.557  1.00 50.90  ? 57  ASP   C CA  1 
ATOM   1855 C C   . ASP   C 1 58 ? 27.753  -31.082 21.394  1.00 46.45  ? 57  ASP   C C   1 
ATOM   1856 O O   . ASP   C 1 58 ? 26.755  -31.190 20.688  1.00 44.48  ? 57  ASP   C O   1 
ATOM   1857 C CB  . ASP   C 1 58 ? 27.917  -33.497 21.976  1.00 48.35  ? 57  ASP   C CB  1 
ATOM   1858 C CG  . ASP   C 1 58 ? 28.715  -34.792 21.957  1.00 52.43  ? 57  ASP   C CG  1 
ATOM   1859 O OD1 . ASP   C 1 58 ? 29.711  -34.845 21.229  1.00 53.62  ? 57  ASP   C OD1 1 
ATOM   1860 O OD2 . ASP   C 1 58 ? 28.339  -35.721 22.683  1.00 58.16  ? 57  ASP   C OD2 1 
ATOM   1861 N N   . LEU   C 1 59 ? 28.054  -29.961 22.059  1.00 42.28  ? 58  LEU   C N   1 
ATOM   1862 C CA  . LEU   C 1 59 ? 27.127  -28.848 22.150  1.00 43.18  ? 58  LEU   C CA  1 
ATOM   1863 C C   . LEU   C 1 59 ? 27.769  -27.589 21.581  1.00 49.99  ? 58  LEU   C C   1 
ATOM   1864 O O   . LEU   C 1 59 ? 28.971  -27.381 21.757  1.00 57.59  ? 58  LEU   C O   1 
ATOM   1865 C CB  . LEU   C 1 59 ? 26.726  -28.664 23.614  1.00 41.55  ? 58  LEU   C CB  1 
ATOM   1866 C CG  . LEU   C 1 59 ? 26.126  -29.907 24.287  1.00 40.67  ? 58  LEU   C CG  1 
ATOM   1867 C CD1 . LEU   C 1 59 ? 25.995  -29.729 25.775  1.00 41.44  ? 58  LEU   C CD1 1 
ATOM   1868 C CD2 . LEU   C 1 59 ? 24.758  -30.321 23.704  1.00 37.46  ? 58  LEU   C CD2 1 
ATOM   1869 N N   . PHE   C 1 60 ? 26.960  -26.773 20.888  1.00 48.57  ? 59  PHE   C N   1 
ATOM   1870 C CA  . PHE   C 1 60 ? 27.453  -25.563 20.232  1.00 45.25  ? 59  PHE   C CA  1 
ATOM   1871 C C   . PHE   C 1 60 ? 26.455  -24.437 20.509  1.00 49.06  ? 59  PHE   C C   1 
ATOM   1872 O O   . PHE   C 1 60 ? 25.256  -24.585 20.260  1.00 45.20  ? 59  PHE   C O   1 
ATOM   1873 C CB  . PHE   C 1 60 ? 27.636  -25.861 18.733  1.00 46.63  ? 59  PHE   C CB  1 
ATOM   1874 C CG  . PHE   C 1 60 ? 28.608  -26.996 18.430  1.00 46.23  ? 59  PHE   C CG  1 
ATOM   1875 C CD1 . PHE   C 1 60 ? 28.207  -28.331 18.466  1.00 45.36  ? 59  PHE   C CD1 1 
ATOM   1876 C CD2 . PHE   C 1 60 ? 29.955  -26.737 18.161  1.00 52.03  ? 59  PHE   C CD2 1 
ATOM   1877 C CE1 . PHE   C 1 60 ? 29.107  -29.360 18.237  1.00 48.17  ? 59  PHE   C CE1 1 
ATOM   1878 C CE2 . PHE   C 1 60 ? 30.852  -27.771 17.906  1.00 47.60  ? 59  PHE   C CE2 1 
ATOM   1879 C CZ  . PHE   C 1 60 ? 30.433  -29.083 17.944  1.00 50.21  ? 59  PHE   C CZ  1 
ATOM   1880 N N   . PRO   C 1 61 ? 26.858  -23.272 21.082  1.00 51.05  ? 60  PRO   C N   1 
ATOM   1881 C CA  . PRO   C 1 61 ? 25.878  -22.235 21.417  1.00 48.34  ? 60  PRO   C CA  1 
ATOM   1882 C C   . PRO   C 1 61 ? 25.173  -21.753 20.151  1.00 46.13  ? 60  PRO   C C   1 
ATOM   1883 O O   . PRO   C 1 61 ? 25.792  -21.686 19.087  1.00 48.05  ? 60  PRO   C O   1 
ATOM   1884 C CB  . PRO   C 1 61 ? 26.655  -21.116 22.155  1.00 50.02  ? 60  PRO   C CB  1 
ATOM   1885 C CG  . PRO   C 1 61 ? 28.038  -21.711 22.374  1.00 47.56  ? 60  PRO   C CG  1 
ATOM   1886 C CD  . PRO   C 1 61 ? 28.240  -22.880 21.414  1.00 54.15  ? 60  PRO   C CD  1 
ATOM   1887 N N   . TYR   C 1 62 ? 23.857  -21.512 20.284  1.00 50.01  ? 61  TYR   C N   1 
ATOM   1888 C CA  . TYR   C 1 62 ? 22.950  -21.267 19.174  1.00 48.67  ? 61  TYR   C CA  1 
ATOM   1889 C C   . TYR   C 1 62 ? 23.410  -20.046 18.383  1.00 60.39  ? 61  TYR   C C   1 
ATOM   1890 O O   . TYR   C 1 62 ? 23.686  -20.145 17.182  1.00 61.43  ? 61  TYR   C O   1 
ATOM   1891 C CB  . TYR   C 1 62 ? 21.498  -21.041 19.600  1.00 46.90  ? 61  TYR   C CB  1 
ATOM   1892 C CG  . TYR   C 1 62 ? 20.567  -20.712 18.435  1.00 50.09  ? 61  TYR   C CG  1 
ATOM   1893 C CD1 . TYR   C 1 62 ? 20.409  -21.590 17.359  1.00 52.94  ? 61  TYR   C CD1 1 
ATOM   1894 C CD2 . TYR   C 1 62 ? 19.872  -19.507 18.393  1.00 51.64  ? 61  TYR   C CD2 1 
ATOM   1895 C CE1 . TYR   C 1 62 ? 19.560  -21.297 16.296  1.00 50.94  ? 61  TYR   C CE1 1 
ATOM   1896 C CE2 . TYR   C 1 62 ? 19.039  -19.193 17.326  1.00 53.69  ? 61  TYR   C CE2 1 
ATOM   1897 C CZ  . TYR   C 1 62 ? 18.875  -20.088 16.280  1.00 52.55  ? 61  TYR   C CZ  1 
ATOM   1898 O OH  . TYR   C 1 62 ? 18.045  -19.737 15.246  1.00 52.87  ? 61  TYR   C OH  1 
ATOM   1899 N N   . ASP   C 1 63 ? 23.515  -18.902 19.074  1.00 56.64  ? 62  ASP   C N   1 
ATOM   1900 C CA  . ASP   C 1 63 ? 23.809  -17.654 18.379  1.00 57.36  ? 62  ASP   C CA  1 
ATOM   1901 C C   . ASP   C 1 63 ? 25.155  -17.713 17.660  1.00 56.19  ? 62  ASP   C C   1 
ATOM   1902 O O   . ASP   C 1 63 ? 25.275  -17.185 16.552  1.00 62.01  ? 62  ASP   C O   1 
ATOM   1903 C CB  . ASP   C 1 63 ? 23.516  -16.430 19.233  1.00 62.73  ? 62  ASP   C CB  1 
ATOM   1904 C CG  . ASP   C 1 63 ? 22.032  -16.121 19.385  1.00 75.49  ? 62  ASP   C CG  1 
ATOM   1905 O OD1 . ASP   C 1 63 ? 21.571  -15.982 20.539  1.00 68.98  ? 62  ASP   C OD1 1 
ATOM   1906 O OD2 . ASP   C 1 63 ? 21.340  -16.033 18.339  1.00 80.05  ? 62  ASP   C OD2 1 
ATOM   1907 N N   . LYS   C 1 64 ? 26.140  -18.396 18.250  1.00 50.31  ? 63  LYS   C N   1 
ATOM   1908 C CA  . LYS   C 1 64 ? 27.478  -18.434 17.681  1.00 56.04  ? 63  LYS   C CA  1 
ATOM   1909 C C   . LYS   C 1 64 ? 27.519  -19.326 16.445  1.00 53.81  ? 63  LYS   C C   1 
ATOM   1910 O O   . LYS   C 1 64 ? 28.324  -19.081 15.550  1.00 47.34  ? 63  LYS   C O   1 
ATOM   1911 C CB  . LYS   C 1 64 ? 28.563  -18.857 18.684  1.00 62.92  ? 63  LYS   C CB  1 
ATOM   1912 N N   . SER   C 1 65 ? 26.631  -20.344 16.373  1.00 51.73  ? 64  SER   C N   1 
ATOM   1913 C CA  . SER   C 1 65 ? 26.844  -21.375 15.366  1.00 43.89  ? 64  SER   C CA  1 
ATOM   1914 C C   . SER   C 1 65 ? 25.686  -21.517 14.372  1.00 42.09  ? 64  SER   C C   1 
ATOM   1915 O O   . SER   C 1 65 ? 25.805  -22.302 13.439  1.00 44.94  ? 64  SER   C O   1 
ATOM   1916 C CB  . SER   C 1 65 ? 27.209  -22.711 15.980  1.00 50.87  ? 64  SER   C CB  1 
ATOM   1917 O OG  . SER   C 1 65 ? 26.091  -23.233 16.682  1.00 49.20  ? 64  SER   C OG  1 
ATOM   1918 N N   . LYS   C 1 66 ? 24.627  -20.721 14.514  1.00 43.01  ? 65  LYS   C N   1 
ATOM   1919 C CA  . LYS   C 1 66 ? 23.503  -20.853 13.587  1.00 46.20  ? 65  LYS   C CA  1 
ATOM   1920 C C   . LYS   C 1 66 ? 23.869  -20.573 12.126  1.00 50.73  ? 65  LYS   C C   1 
ATOM   1921 O O   . LYS   C 1 66 ? 23.309  -21.199 11.227  1.00 47.46  ? 65  LYS   C O   1 
ATOM   1922 C CB  . LYS   C 1 66 ? 22.325  -19.992 14.037  1.00 47.71  ? 65  LYS   C CB  1 
ATOM   1923 C CG  . LYS   C 1 66 ? 22.619  -18.513 14.211  1.00 39.90  ? 65  LYS   C CG  1 
ATOM   1924 C CD  . LYS   C 1 66 ? 21.341  -17.885 14.752  1.00 53.48  ? 65  LYS   C CD  1 
ATOM   1925 C CE  . LYS   C 1 66 ? 21.416  -16.411 14.978  1.00 56.31  ? 65  LYS   C CE  1 
ATOM   1926 N NZ  . LYS   C 1 66 ? 20.062  -15.929 15.251  1.00 56.11  ? 65  LYS   C NZ  1 
ATOM   1927 N N   . ASP   C 1 67 ? 24.797  -19.637 11.870  1.00 48.58  ? 66  ASP   C N   1 
ATOM   1928 C CA  . ASP   C 1 67 ? 25.222  -19.365 10.501  1.00 50.83  ? 66  ASP   C CA  1 
ATOM   1929 C C   . ASP   C 1 67 ? 25.594  -20.679 9.809   1.00 51.39  ? 66  ASP   C C   1 
ATOM   1930 O O   . ASP   C 1 67 ? 25.252  -20.896 8.654   1.00 48.57  ? 66  ASP   C O   1 
ATOM   1931 C CB  . ASP   C 1 67 ? 26.153  -18.150 10.411  1.00 51.13  ? 66  ASP   C CB  1 
ATOM   1932 C CG  . ASP   C 1 67 ? 27.668  -18.334 10.504  1.00 69.54  ? 66  ASP   C CG  1 
ATOM   1933 O OD1 . ASP   C 1 67 ? 28.177  -19.446 10.216  1.00 64.74  ? 66  ASP   C OD1 1 
ATOM   1934 O OD2 . ASP   C 1 67 ? 28.351  -17.337 10.864  1.00 63.96  ? 66  ASP   C OD2 1 
ATOM   1935 N N   . LYS   C 1 68 ? 26.237  -21.589 10.554  1.00 47.11  ? 67  LYS   C N   1 
ATOM   1936 C CA  . LYS   C 1 68 ? 26.733  -22.843 10.018  1.00 45.07  ? 67  LYS   C CA  1 
ATOM   1937 C C   . LYS   C 1 68 ? 25.693  -23.979 10.118  1.00 45.40  ? 67  LYS   C C   1 
ATOM   1938 O O   . LYS   C 1 68 ? 25.529  -24.752 9.176   1.00 46.66  ? 67  LYS   C O   1 
ATOM   1939 C CB  . LYS   C 1 68 ? 27.984  -23.152 10.846  1.00 41.58  ? 67  LYS   C CB  1 
ATOM   1940 C CG  . LYS   C 1 68 ? 28.803  -24.320 10.385  1.00 44.23  ? 67  LYS   C CG  1 
ATOM   1941 C CD  . LYS   C 1 68 ? 29.978  -24.535 11.337  1.00 51.45  ? 67  LYS   C CD  1 
ATOM   1942 C CE  . LYS   C 1 68 ? 30.845  -25.695 10.955  1.00 54.78  ? 67  LYS   C CE  1 
ATOM   1943 N NZ  . LYS   C 1 68 ? 30.961  -25.883 9.504   1.00 65.37  ? 67  LYS   C NZ  1 
ATOM   1944 N N   . TYR   C 1 69 ? 25.009  -24.121 11.265  1.00 44.55  ? 68  TYR   C N   1 
ATOM   1945 C CA  . TYR   C 1 69 ? 24.158  -25.295 11.458  1.00 40.52  ? 68  TYR   C CA  1 
ATOM   1946 C C   . TYR   C 1 69 ? 22.674  -24.990 11.249  1.00 38.44  ? 68  TYR   C C   1 
ATOM   1947 O O   . TYR   C 1 69 ? 21.888  -25.912 11.051  1.00 38.21  ? 68  TYR   C O   1 
ATOM   1948 C CB  . TYR   C 1 69 ? 24.315  -25.890 12.868  1.00 39.68  ? 68  TYR   C CB  1 
ATOM   1949 C CG  . TYR   C 1 69 ? 25.739  -26.323 13.190  1.00 36.91  ? 68  TYR   C CG  1 
ATOM   1950 C CD1 . TYR   C 1 69 ? 26.470  -27.115 12.311  1.00 43.59  ? 68  TYR   C CD1 1 
ATOM   1951 C CD2 . TYR   C 1 69 ? 26.331  -25.946 14.393  1.00 43.31  ? 68  TYR   C CD2 1 
ATOM   1952 C CE1 . TYR   C 1 69 ? 27.763  -27.532 12.623  1.00 45.15  ? 68  TYR   C CE1 1 
ATOM   1953 C CE2 . TYR   C 1 69 ? 27.612  -26.364 14.713  1.00 45.13  ? 68  TYR   C CE2 1 
ATOM   1954 C CZ  . TYR   C 1 69 ? 28.329  -27.143 13.825  1.00 46.97  ? 68  TYR   C CZ  1 
ATOM   1955 O OH  . TYR   C 1 69 ? 29.610  -27.487 14.176  1.00 49.24  ? 68  TYR   C OH  1 
ATOM   1956 N N   . GLY   C 1 70 ? 22.283  -23.708 11.286  1.00 39.98  ? 69  GLY   C N   1 
ATOM   1957 C CA  . GLY   C 1 70 ? 20.863  -23.392 11.224  1.00 37.19  ? 69  GLY   C CA  1 
ATOM   1958 C C   . GLY   C 1 70 ? 20.457  -23.268 9.762   1.00 40.47  ? 69  GLY   C C   1 
ATOM   1959 O O   . GLY   C 1 70 ? 20.337  -22.162 9.231   1.00 42.69  ? 69  GLY   C O   1 
ATOM   1960 N N   . LYS   C 1 71 ? 20.375  -24.427 9.109   1.00 39.05  ? 70  LYS   C N   1 
ATOM   1961 C CA  . LYS   C 1 71 ? 19.978  -24.500 7.711   1.00 41.27  ? 70  LYS   C CA  1 
ATOM   1962 C C   . LYS   C 1 71 ? 19.083  -25.725 7.568   1.00 41.39  ? 70  LYS   C C   1 
ATOM   1963 O O   . LYS   C 1 71 ? 19.201  -26.693 8.328   1.00 44.21  ? 70  LYS   C O   1 
ATOM   1964 C CB  . LYS   C 1 71 ? 21.210  -24.612 6.802   1.00 43.88  ? 70  LYS   C CB  1 
ATOM   1965 C CG  . LYS   C 1 71 ? 22.100  -25.724 7.235   1.00 45.38  ? 70  LYS   C CG  1 
ATOM   1966 C CD  . LYS   C 1 71 ? 23.373  -25.995 6.447   1.00 54.20  ? 70  LYS   C CD  1 
ATOM   1967 C CE  . LYS   C 1 71 ? 24.127  -27.053 7.184   1.00 58.12  ? 70  LYS   C CE  1 
ATOM   1968 N N   . PRO   C 1 72 ? 18.109  -25.712 6.634   1.00 39.48  ? 71  PRO   C N   1 
ATOM   1969 C CA  . PRO   C 1 72 ? 17.173  -26.828 6.542   1.00 36.31  ? 71  PRO   C CA  1 
ATOM   1970 C C   . PRO   C 1 72 ? 17.863  -28.146 6.211   1.00 36.41  ? 71  PRO   C C   1 
ATOM   1971 O O   . PRO   C 1 72 ? 18.916  -28.204 5.565   1.00 43.36  ? 71  PRO   C O   1 
ATOM   1972 C CB  . PRO   C 1 72 ? 16.239  -26.402 5.401   1.00 38.48  ? 71  PRO   C CB  1 
ATOM   1973 C CG  . PRO   C 1 72 ? 16.310  -24.888 5.481   1.00 37.71  ? 71  PRO   C CG  1 
ATOM   1974 C CD  . PRO   C 1 72 ? 17.793  -24.587 5.729   1.00 36.53  ? 71  PRO   C CD  1 
ATOM   1975 N N   . ASN   C 1 73 ? 17.190  -29.196 6.621   1.00 37.57  ? 72  ASN   C N   1 
ATOM   1976 C CA  . ASN   C 1 73 ? 17.473  -30.484 6.020   1.00 46.07  ? 72  ASN   C CA  1 
ATOM   1977 C C   . ASN   C 1 73 ? 16.242  -31.361 6.183   1.00 41.64  ? 72  ASN   C C   1 
ATOM   1978 O O   . ASN   C 1 73 ? 15.294  -31.023 6.886   1.00 41.80  ? 72  ASN   C O   1 
ATOM   1979 C CB  . ASN   C 1 73 ? 18.824  -31.073 6.424   1.00 53.20  ? 72  ASN   C CB  1 
ATOM   1980 C CG  . ASN   C 1 73 ? 18.814  -31.742 7.778   1.00 52.04  ? 72  ASN   C CG  1 
ATOM   1981 O OD1 . ASN   C 1 73 ? 18.378  -32.894 7.913   1.00 48.39  ? 72  ASN   C OD1 1 
ATOM   1982 N ND2 . ASN   C 1 73 ? 19.361  -31.065 8.766   1.00 60.52  ? 72  ASN   C ND2 1 
ATOM   1983 N N   . LYS   C 1 74 ? 16.309  -32.534 5.561   1.00 42.73  ? 73  LYS   C N   1 
ATOM   1984 C CA  . LYS   C 1 74 ? 15.115  -33.328 5.308   1.00 41.74  ? 73  LYS   C CA  1 
ATOM   1985 C C   . LYS   C 1 74 ? 14.850  -34.288 6.459   1.00 40.37  ? 73  LYS   C C   1 
ATOM   1986 O O   . LYS   C 1 74 ? 13.785  -34.897 6.522   1.00 44.47  ? 73  LYS   C O   1 
ATOM   1987 C CB  . LYS   C 1 74 ? 15.216  -34.043 3.957   1.00 48.29  ? 73  LYS   C CB  1 
ATOM   1988 C CG  . LYS   C 1 74 ? 15.461  -33.102 2.756   1.00 51.64  ? 73  LYS   C CG  1 
ATOM   1989 N N   . ARG   C 1 75 ? 15.768  -34.353 7.433   1.00 37.20  ? 74  ARG   C N   1 
ATOM   1990 C CA  . ARG   C 1 75 ? 15.567  -35.289 8.533   1.00 34.47  ? 74  ARG   C CA  1 
ATOM   1991 C C   . ARG   C 1 75 ? 14.286  -34.987 9.312   1.00 34.99  ? 74  ARG   C C   1 
ATOM   1992 O O   . ARG   C 1 75 ? 13.876  -33.826 9.503   1.00 38.76  ? 74  ARG   C O   1 
ATOM   1993 C CB  . ARG   C 1 75 ? 16.812  -35.337 9.441   1.00 38.62  ? 74  ARG   C CB  1 
ATOM   1994 C CG  . ARG   C 1 75 ? 18.105  -35.673 8.705   1.00 46.48  ? 74  ARG   C CG  1 
ATOM   1995 C CD  . ARG   C 1 75 ? 18.326  -37.137 8.303   1.00 47.52  ? 74  ARG   C CD  1 
ATOM   1996 N NE  . ARG   C 1 75 ? 18.237  -37.972 9.496   1.00 44.23  ? 74  ARG   C NE  1 
ATOM   1997 C CZ  . ARG   C 1 75 ? 19.352  -38.421 10.097  1.00 41.52  ? 74  ARG   C CZ  1 
ATOM   1998 N NH1 . ARG   C 1 75 ? 19.270  -38.969 11.288  1.00 44.60  ? 74  ARG   C NH1 1 
ATOM   1999 N NH2 . ARG   C 1 75 ? 20.506  -38.184 9.515   1.00 42.11  ? 74  ARG   C NH2 1 
ATOM   2000 N N   . LYS   C 1 76 ? 13.636  -36.061 9.779   1.00 39.25  ? 75  LYS   C N   1 
ATOM   2001 C CA  . LYS   C 1 76 ? 12.362  -35.953 10.467  1.00 44.01  ? 75  LYS   C CA  1 
ATOM   2002 C C   . LYS   C 1 76 ? 12.430  -34.969 11.633  1.00 42.52  ? 75  LYS   C C   1 
ATOM   2003 O O   . LYS   C 1 76 ? 13.214  -35.118 12.577  1.00 39.15  ? 75  LYS   C O   1 
ATOM   2004 C CB  . LYS   C 1 76 ? 11.726  -37.302 10.839  1.00 42.94  ? 75  LYS   C CB  1 
ATOM   2005 C CG  . LYS   C 1 76 ? 10.233  -37.197 11.043  1.00 49.08  ? 75  LYS   C CG  1 
ATOM   2006 C CD  . LYS   C 1 76 ? 9.604   -38.331 11.847  1.00 61.66  ? 75  LYS   C CD  1 
ATOM   2007 N N   . GLY   C 1 77 ? 11.623  -33.905 11.509  1.00 44.30  ? 76  GLY   C N   1 
ATOM   2008 C CA  . GLY   C 1 77 ? 11.314  -33.016 12.619  1.00 38.41  ? 76  GLY   C CA  1 
ATOM   2009 C C   . GLY   C 1 77 ? 12.265  -31.818 12.678  1.00 37.45  ? 76  GLY   C C   1 
ATOM   2010 O O   . GLY   C 1 77 ? 12.086  -30.927 13.505  1.00 44.67  ? 76  GLY   C O   1 
ATOM   2011 N N   . PHE   C 1 78 ? 13.237  -31.797 11.764  1.00 36.28  ? 77  PHE   C N   1 
ATOM   2012 C CA  . PHE   C 1 78 ? 14.357  -30.870 11.822  1.00 37.10  ? 77  PHE   C CA  1 
ATOM   2013 C C   . PHE   C 1 78 ? 13.895  -29.431 11.529  1.00 37.89  ? 77  PHE   C C   1 
ATOM   2014 O O   . PHE   C 1 78 ? 14.254  -28.471 12.223  1.00 35.00  ? 77  PHE   C O   1 
ATOM   2015 C CB  . PHE   C 1 78 ? 15.433  -31.309 10.834  1.00 41.39  ? 77  PHE   C CB  1 
ATOM   2016 C CG  . PHE   C 1 78 ? 16.707  -30.528 11.088  1.00 36.80  ? 77  PHE   C CG  1 
ATOM   2017 C CD1 . PHE   C 1 78 ? 16.877  -29.247 10.572  1.00 40.39  ? 77  PHE   C CD1 1 
ATOM   2018 C CD2 . PHE   C 1 78 ? 17.732  -31.062 11.858  1.00 35.07  ? 77  PHE   C CD2 1 
ATOM   2019 C CE1 . PHE   C 1 78 ? 18.037  -28.538 10.820  1.00 38.58  ? 77  PHE   C CE1 1 
ATOM   2020 C CE2 . PHE   C 1 78 ? 18.902  -30.356 12.077  1.00 35.97  ? 77  PHE   C CE2 1 
ATOM   2021 C CZ  . PHE   C 1 78 ? 19.060  -29.096 11.565  1.00 39.42  ? 77  PHE   C CZ  1 
ATOM   2022 N N   . ASN   C 1 79 ? 13.107  -29.287 10.458  1.00 39.99  ? 78  ASN   C N   1 
ATOM   2023 C CA  . ASN   C 1 79 ? 12.730  -27.936 10.049  1.00 40.88  ? 78  ASN   C CA  1 
ATOM   2024 C C   . ASN   C 1 79 ? 11.721  -27.332 11.023  1.00 38.55  ? 78  ASN   C C   1 
ATOM   2025 O O   . ASN   C 1 79 ? 11.751  -26.120 11.305  1.00 37.31  ? 78  ASN   C O   1 
ATOM   2026 C CB  . ASN   C 1 79 ? 12.269  -27.885 8.599   1.00 38.97  ? 78  ASN   C CB  1 
ATOM   2027 C CG  . ASN   C 1 79 ? 13.362  -28.304 7.649   1.00 38.82  ? 78  ASN   C CG  1 
ATOM   2028 O OD1 . ASN   C 1 79 ? 14.532  -28.034 7.915   1.00 36.64  ? 78  ASN   C OD1 1 
ATOM   2029 N ND2 . ASN   C 1 79 ? 12.995  -28.966 6.553   1.00 38.90  ? 78  ASN   C ND2 1 
ATOM   2030 N N   . GLU   C 1 80 ? 10.831  -28.169 11.556  1.00 40.08  ? 79  GLU   C N   1 
ATOM   2031 C CA  . GLU   C 1 80 ? 9.983   -27.677 12.639  1.00 39.09  ? 79  GLU   C CA  1 
ATOM   2032 C C   . GLU   C 1 80 ? 10.871  -27.262 13.821  1.00 46.83  ? 79  GLU   C C   1 
ATOM   2033 O O   . GLU   C 1 80 ? 10.638  -26.237 14.462  1.00 41.62  ? 79  GLU   C O   1 
ATOM   2034 C CB  . GLU   C 1 80 ? 8.850   -28.679 12.902  1.00 44.39  ? 79  GLU   C CB  1 
ATOM   2035 C CG  . GLU   C 1 80 ? 7.863   -28.210 13.962  1.00 45.12  ? 79  GLU   C CG  1 
ATOM   2036 C CD  . GLU   C 1 80 ? 6.671   -29.107 14.191  1.00 50.69  ? 79  GLU   C CD  1 
ATOM   2037 O OE1 . GLU   C 1 80 ? 6.646   -30.294 13.791  1.00 58.48  ? 79  GLU   C OE1 1 
ATOM   2038 O OE2 . GLU   C 1 80 ? 5.736   -28.571 14.795  1.00 51.53  ? 79  GLU   C OE2 1 
ATOM   2039 N N   . GLY   C 1 81 ? 11.932  -28.043 14.092  1.00 39.80  ? 80  GLY   C N   1 
ATOM   2040 C CA  . GLY   C 1 81 ? 12.855  -27.643 15.149  1.00 37.43  ? 80  GLY   C CA  1 
ATOM   2041 C C   . GLY   C 1 81 ? 13.512  -26.284 14.899  1.00 39.27  ? 80  GLY   C C   1 
ATOM   2042 O O   . GLY   C 1 81 ? 13.695  -25.513 15.837  1.00 40.05  ? 80  GLY   C O   1 
ATOM   2043 N N   . LEU   C 1 82 ? 13.978  -26.033 13.654  1.00 39.80  ? 81  LEU   C N   1 
ATOM   2044 C CA  . LEU   C 1 82 ? 14.526  -24.725 13.303  1.00 41.10  ? 81  LEU   C CA  1 
ATOM   2045 C C   . LEU   C 1 82 ? 13.508  -23.619 13.579  1.00 38.57  ? 81  LEU   C C   1 
ATOM   2046 O O   . LEU   C 1 82 ? 13.873  -22.547 14.082  1.00 40.53  ? 81  LEU   C O   1 
ATOM   2047 C CB  . LEU   C 1 82 ? 14.949  -24.698 11.836  1.00 39.11  ? 81  LEU   C CB  1 
ATOM   2048 C CG  . LEU   C 1 82 ? 16.244  -25.442 11.482  1.00 34.83  ? 81  LEU   C CG  1 
ATOM   2049 C CD1 . LEU   C 1 82 ? 16.543  -25.302 10.001  1.00 36.31  ? 81  LEU   C CD1 1 
ATOM   2050 C CD2 . LEU   C 1 82 ? 17.468  -25.059 12.264  1.00 31.85  ? 81  LEU   C CD2 1 
ATOM   2051 N N   . TRP   C 1 83 ? 12.233  -23.869 13.269  1.00 37.36  ? 82  TRP   C N   1 
ATOM   2052 C CA  . TRP   C 1 83 ? 11.244  -22.830 13.503  1.00 44.59  ? 82  TRP   C CA  1 
ATOM   2053 C C   . TRP   C 1 83 ? 11.122  -22.555 15.009  1.00 47.18  ? 82  TRP   C C   1 
ATOM   2054 O O   . TRP   C 1 83 ? 11.130  -21.397 15.426  1.00 46.29  ? 82  TRP   C O   1 
ATOM   2055 C CB  . TRP   C 1 83 ? 9.889   -23.191 12.874  1.00 44.46  ? 82  TRP   C CB  1 
ATOM   2056 C CG  . TRP   C 1 83 ? 8.922   -22.042 12.988  1.00 48.80  ? 82  TRP   C CG  1 
ATOM   2057 C CD1 . TRP   C 1 83 ? 8.779   -21.003 12.111  1.00 45.45  ? 82  TRP   C CD1 1 
ATOM   2058 C CD2 . TRP   C 1 83 ? 8.017   -21.785 14.086  1.00 51.25  ? 82  TRP   C CD2 1 
ATOM   2059 N NE1 . TRP   C 1 83 ? 7.826   -20.132 12.575  1.00 47.51  ? 82  TRP   C NE1 1 
ATOM   2060 C CE2 . TRP   C 1 83 ? 7.336   -20.580 13.774  1.00 50.45  ? 82  TRP   C CE2 1 
ATOM   2061 C CE3 . TRP   C 1 83 ? 7.710   -22.456 15.283  1.00 46.97  ? 82  TRP   C CE3 1 
ATOM   2062 C CZ2 . TRP   C 1 83 ? 6.371   -20.035 14.620  1.00 54.23  ? 82  TRP   C CZ2 1 
ATOM   2063 C CZ3 . TRP   C 1 83 ? 6.744   -21.917 16.111  1.00 58.69  ? 82  TRP   C CZ3 1 
ATOM   2064 C CH2 . TRP   C 1 83 ? 6.103   -20.716 15.790  1.00 55.34  ? 82  TRP   C CH2 1 
ATOM   2065 N N   . GLU   C 1 84 ? 11.041  -23.627 15.822  1.00 42.32  ? 83  GLU   C N   1 
ATOM   2066 C CA  . GLU   C 1 84 ? 10.940  -23.497 17.276  1.00 48.15  ? 83  GLU   C CA  1 
ATOM   2067 C C   . GLU   C 1 84 ? 12.100  -22.716 17.910  1.00 42.71  ? 83  GLU   C C   1 
ATOM   2068 O O   . GLU   C 1 84 ? 11.866  -21.827 18.743  1.00 50.18  ? 83  GLU   C O   1 
ATOM   2069 C CB  . GLU   C 1 84 ? 10.757  -24.864 17.931  1.00 41.93  ? 83  GLU   C CB  1 
ATOM   2070 C CG  . GLU   C 1 84 ? 9.422   -25.513 17.583  1.00 44.53  ? 83  GLU   C CG  1 
ATOM   2071 C CD  . GLU   C 1 84 ? 9.329   -26.930 18.091  1.00 50.93  ? 83  GLU   C CD  1 
ATOM   2072 O OE1 . GLU   C 1 84 ? 10.354  -27.453 18.608  1.00 49.57  ? 83  GLU   C OE1 1 
ATOM   2073 O OE2 . GLU   C 1 84 ? 8.229   -27.489 17.968  1.00 52.67  ? 83  GLU   C OE2 1 
ATOM   2074 N N   . ILE   C 1 85 ? 13.351  -23.023 17.542  1.00 43.24  ? 84  ILE   C N   1 
ATOM   2075 C CA  . ILE   C 1 85 ? 14.506  -22.421 18.190  1.00 43.86  ? 84  ILE   C CA  1 
ATOM   2076 C C   . ILE   C 1 85 ? 14.595  -20.912 17.913  1.00 45.53  ? 84  ILE   C C   1 
ATOM   2077 O O   . ILE   C 1 85 ? 15.096  -20.165 18.750  1.00 44.39  ? 84  ILE   C O   1 
ATOM   2078 C CB  . ILE   C 1 85 ? 15.807  -23.159 17.828  1.00 43.12  ? 84  ILE   C CB  1 
ATOM   2079 C CG1 . ILE   C 1 85 ? 16.929  -22.826 18.827  1.00 42.43  ? 84  ILE   C CG1 1 
ATOM   2080 C CG2 . ILE   C 1 85 ? 16.211  -22.922 16.362  1.00 42.74  ? 84  ILE   C CG2 1 
ATOM   2081 C CD1 . ILE   C 1 85 ? 18.045  -23.852 18.883  1.00 41.85  ? 84  ILE   C CD1 1 
ATOM   2082 N N   . GLN   C 1 86 ? 14.131  -20.486 16.725  1.00 40.15  ? 85  GLN   C N   1 
ATOM   2083 C CA  . GLN   C 1 86 ? 14.158  -19.078 16.336  1.00 44.17  ? 85  GLN   C CA  1 
ATOM   2084 C C   . GLN   C 1 86 ? 12.923  -18.328 16.842  1.00 45.26  ? 85  GLN   C C   1 
ATOM   2085 O O   . GLN   C 1 86 ? 13.027  -17.153 17.176  1.00 51.22  ? 85  GLN   C O   1 
ATOM   2086 C CB  . GLN   C 1 86 ? 14.314  -18.980 14.814  1.00 44.35  ? 85  GLN   C CB  1 
ATOM   2087 C CG  . GLN   C 1 86 ? 14.432  -17.556 14.258  1.00 38.96  ? 85  GLN   C CG  1 
ATOM   2088 C CD  . GLN   C 1 86 ? 14.834  -17.515 12.792  1.00 45.72  ? 85  GLN   C CD  1 
ATOM   2089 O OE1 . GLN   C 1 86 ? 14.853  -18.528 12.078  1.00 43.60  ? 85  GLN   C OE1 1 
ATOM   2090 N NE2 . GLN   C 1 86 ? 15.219  -16.336 12.327  1.00 47.01  ? 85  GLN   C NE2 1 
ATOM   2091 N N   . ASN   C 1 87 ? 11.769  -18.987 16.912  1.00 47.48  ? 86  ASN   C N   1 
ATOM   2092 C CA  . ASN   C 1 87 ? 10.521  -18.266 17.135  1.00 51.48  ? 86  ASN   C CA  1 
ATOM   2093 C C   . ASN   C 1 87 ? 9.934   -18.506 18.528  1.00 55.45  ? 86  ASN   C C   1 
ATOM   2094 O O   . ASN   C 1 87 ? 9.432   -17.562 19.131  1.00 57.49  ? 86  ASN   C O   1 
ATOM   2095 C CB  . ASN   C 1 87 ? 9.494   -18.522 16.039  1.00 46.20  ? 86  ASN   C CB  1 
ATOM   2096 C CG  . ASN   C 1 87 ? 10.009  -18.012 14.719  1.00 52.97  ? 86  ASN   C CG  1 
ATOM   2097 O OD1 . ASN   C 1 87 ? 10.077  -16.798 14.508  1.00 51.65  ? 86  ASN   C OD1 1 
ATOM   2098 N ND2 . ASN   C 1 87 ? 10.401  -18.920 13.839  1.00 46.47  ? 86  ASN   C ND2 1 
ATOM   2099 N N   . ASN   C 1 88 ? 10.018  -19.745 19.037  1.00 52.91  ? 87  ASN   C N   1 
ATOM   2100 C CA  . ASN   C 1 88 ? 9.300   -20.139 20.246  1.00 48.26  ? 87  ASN   C CA  1 
ATOM   2101 C C   . ASN   C 1 88 ? 10.180  -21.021 21.143  1.00 49.84  ? 87  ASN   C C   1 
ATOM   2102 O O   . ASN   C 1 88 ? 9.727   -22.080 21.594  1.00 55.98  ? 87  ASN   C O   1 
ATOM   2103 C CB  . ASN   C 1 88 ? 7.992   -20.829 19.868  1.00 56.55  ? 87  ASN   C CB  1 
ATOM   2104 C CG  . ASN   C 1 88 ? 6.965   -20.838 20.978  1.00 61.76  ? 87  ASN   C CG  1 
ATOM   2105 O OD1 . ASN   C 1 88 ? 7.098   -20.113 21.971  1.00 64.20  ? 87  ASN   C OD1 1 
ATOM   2106 N ND2 . ASN   C 1 88 ? 5.913   -21.623 20.799  1.00 62.84  ? 87  ASN   C ND2 1 
ATOM   2107 N N   . PRO   C 1 89 ? 11.446  -20.630 21.429  1.00 47.42  ? 88  PRO   C N   1 
ATOM   2108 C CA  . PRO   C 1 89 ? 12.419  -21.531 22.068  1.00 47.65  ? 88  PRO   C CA  1 
ATOM   2109 C C   . PRO   C 1 89 ? 12.185  -21.937 23.522  1.00 55.13  ? 88  PRO   C C   1 
ATOM   2110 O O   . PRO   C 1 89 ? 12.860  -22.837 24.012  1.00 49.52  ? 88  PRO   C O   1 
ATOM   2111 C CB  . PRO   C 1 89 ? 13.769  -20.816 21.928  1.00 45.66  ? 88  PRO   C CB  1 
ATOM   2112 C CG  . PRO   C 1 89 ? 13.382  -19.351 21.820  1.00 56.03  ? 88  PRO   C CG  1 
ATOM   2113 C CD  . PRO   C 1 89 ? 12.063  -19.346 21.072  1.00 45.79  ? 88  PRO   C CD  1 
ATOM   2114 N N   . HIS   C 1 90 ? 11.247  -21.272 24.207  1.00 61.80  ? 89  HIS   C N   1 
ATOM   2115 C CA  . HIS   C 1 90 ? 11.042  -21.562 25.622  1.00 60.48  ? 89  HIS   C CA  1 
ATOM   2116 C C   . HIS   C 1 90 ? 9.583   -21.918 25.915  1.00 63.93  ? 89  HIS   C C   1 
ATOM   2117 O O   . HIS   C 1 90 ? 9.156   -21.859 27.065  1.00 72.06  ? 89  HIS   C O   1 
ATOM   2118 C CB  . HIS   C 1 90 ? 11.572  -20.438 26.522  1.00 47.58  ? 89  HIS   C CB  1 
ATOM   2119 C CG  . HIS   C 1 90 ? 12.975  -19.960 26.284  1.00 47.16  ? 89  HIS   C CG  1 
ATOM   2120 N ND1 . HIS   C 1 90 ? 14.119  -20.655 26.630  1.00 50.30  ? 89  HIS   C ND1 1 
ATOM   2121 C CD2 . HIS   C 1 90 ? 13.397  -18.816 25.743  1.00 49.74  ? 89  HIS   C CD2 1 
ATOM   2122 C CE1 . HIS   C 1 90 ? 15.193  -19.935 26.318  1.00 50.22  ? 89  HIS   C CE1 1 
ATOM   2123 N NE2 . HIS   C 1 90 ? 14.767  -18.811 25.764  1.00 50.61  ? 89  HIS   C NE2 1 
ATOM   2124 N N   . ALA   C 1 91 ? 8.824   -22.301 24.882  1.00 65.13  ? 90  ALA   C N   1 
ATOM   2125 C CA  . ALA   C 1 91 ? 7.511   -22.905 25.065  1.00 65.25  ? 90  ALA   C CA  1 
ATOM   2126 C C   . ALA   C 1 91 ? 7.652   -24.321 25.630  1.00 68.69  ? 90  ALA   C C   1 
ATOM   2127 O O   . ALA   C 1 91 ? 8.735   -24.908 25.603  1.00 68.23  ? 90  ALA   C O   1 
ATOM   2128 C CB  . ALA   C 1 91 ? 6.744   -22.911 23.759  1.00 64.11  ? 90  ALA   C CB  1 
ATOM   2129 N N   . SER   C 1 92 ? 6.522   -24.873 26.093  1.00 72.59  ? 91  SER   C N   1 
ATOM   2130 C CA  . SER   C 1 92 ? 6.464   -26.118 26.846  1.00 78.71  ? 91  SER   C CA  1 
ATOM   2131 C C   . SER   C 1 92 ? 6.774   -27.324 25.963  1.00 74.74  ? 91  SER   C C   1 
ATOM   2132 O O   . SER   C 1 92 ? 7.650   -28.116 26.290  1.00 81.93  ? 91  SER   C O   1 
ATOM   2133 C CB  . SER   C 1 92 ? 5.116   -26.281 27.513  1.00 75.04  ? 91  SER   C CB  1 
ATOM   2134 O OG  . SER   C 1 92 ? 4.848   -25.182 28.368  1.00 84.38  ? 91  SER   C OG  1 
ATOM   2135 N N   . TYR   C 1 93 ? 6.014   -27.471 24.872  1.00 76.23  ? 92  TYR   C N   1 
ATOM   2136 C CA  . TYR   C 1 93 ? 6.062   -28.630 23.992  1.00 78.42  ? 92  TYR   C CA  1 
ATOM   2137 C C   . TYR   C 1 93 ? 5.756   -29.902 24.794  1.00 79.43  ? 92  TYR   C C   1 
ATOM   2138 O O   . TYR   C 1 93 ? 6.133   -30.996 24.315  1.00 81.69  ? 92  TYR   C O   1 
ATOM   2139 C CB  . TYR   C 1 93 ? 7.389   -28.697 23.226  1.00 74.62  ? 92  TYR   C CB  1 
ATOM   2140 C CG  . TYR   C 1 93 ? 7.721   -27.418 22.465  1.00 68.17  ? 92  TYR   C CG  1 
ATOM   2141 C CD1 . TYR   C 1 93 ? 7.003   -27.052 21.331  1.00 60.39  ? 92  TYR   C CD1 1 
ATOM   2142 C CD2 . TYR   C 1 93 ? 8.758   -26.589 22.879  1.00 62.58  ? 92  TYR   C CD2 1 
ATOM   2143 C CE1 . TYR   C 1 93 ? 7.295   -25.893 20.636  1.00 64.83  ? 92  TYR   C CE1 1 
ATOM   2144 C CE2 . TYR   C 1 93 ? 9.060   -25.426 22.190  1.00 67.14  ? 92  TYR   C CE2 1 
ATOM   2145 C CZ  . TYR   C 1 93 ? 8.332   -25.081 21.066  1.00 67.36  ? 92  TYR   C CZ  1 
ATOM   2146 O OH  . TYR   C 1 93 ? 8.640   -23.933 20.391  1.00 70.25  ? 92  TYR   C OH  1 
HETATM 2147 S S   . SO4   D 2 .  ? 1.771   -33.903 1.993   1.00 84.03  ? 101 SO4   A S   1 
HETATM 2148 O O1  . SO4   D 2 .  ? 2.380   -34.586 0.886   1.00 67.15  ? 101 SO4   A O1  1 
HETATM 2149 O O2  . SO4   D 2 .  ? 1.749   -32.486 1.736   1.00 64.06  ? 101 SO4   A O2  1 
HETATM 2150 O O3  . SO4   D 2 .  ? 0.420   -34.369 2.161   1.00 83.13  ? 101 SO4   A O3  1 
HETATM 2151 O O4  . SO4   D 2 .  ? 2.522   -34.177 3.196   1.00 81.01  ? 101 SO4   A O4  1 
HETATM 2152 S S   . SO4   E 2 .  ? -8.719  -25.072 1.692   1.00 88.14  ? 102 SO4   A S   1 
HETATM 2153 O O1  . SO4   E 2 .  ? -9.157  -24.652 0.378   1.00 61.97  ? 102 SO4   A O1  1 
HETATM 2154 O O2  . SO4   E 2 .  ? -8.805  -23.959 2.608   1.00 72.22  ? 102 SO4   A O2  1 
HETATM 2155 O O3  . SO4   E 2 .  ? -9.542  -26.163 2.149   1.00 76.72  ? 102 SO4   A O3  1 
HETATM 2156 O O4  . SO4   E 2 .  ? -7.359  -25.526 1.644   1.00 85.76  ? 102 SO4   A O4  1 
HETATM 2157 C C1  . EDO   F 3 .  ? 14.267  -19.551 -7.376  1.00 45.84  ? 103 EDO   A C1  1 
HETATM 2158 O O1  . EDO   F 3 .  ? 15.442  -18.789 -7.237  1.00 41.10  ? 103 EDO   A O1  1 
HETATM 2159 C C2  . EDO   F 3 .  ? 13.366  -19.017 -8.455  1.00 43.28  ? 103 EDO   A C2  1 
HETATM 2160 O O2  . EDO   F 3 .  ? 12.804  -17.742 -8.220  1.00 41.63  ? 103 EDO   A O2  1 
HETATM 2161 S S   . SO4   G 2 .  ? 9.309   -29.618 5.744   1.00 63.41  ? 104 SO4   A S   1 
HETATM 2162 O O1  . SO4   G 2 .  ? 10.066  -28.832 4.859   1.00 53.21  ? 104 SO4   A O1  1 
HETATM 2163 O O2  . SO4   G 2 .  ? 8.784   -30.784 5.035   1.00 54.53  ? 104 SO4   A O2  1 
HETATM 2164 O O3  . SO4   G 2 .  ? 10.153  -30.046 6.832   1.00 68.37  ? 104 SO4   A O3  1 
HETATM 2165 O O4  . SO4   G 2 .  ? 8.179   -28.863 6.232   1.00 64.27  ? 104 SO4   A O4  1 
HETATM 2166 S S   . SO4   H 2 .  ? 7.454   -8.704  -25.010 1.00 75.68  ? 101 SO4   B S   1 
HETATM 2167 O O1  . SO4   H 2 .  ? 8.594   -8.588  -25.903 1.00 52.99  ? 101 SO4   B O1  1 
HETATM 2168 O O2  . SO4   H 2 .  ? 6.393   -9.458  -25.642 1.00 56.51  ? 101 SO4   B O2  1 
HETATM 2169 O O3  . SO4   H 2 .  ? 7.841   -9.368  -23.782 1.00 57.07  ? 101 SO4   B O3  1 
HETATM 2170 O O4  . SO4   H 2 .  ? 7.010   -7.371  -24.709 1.00 74.06  ? 101 SO4   B O4  1 
HETATM 2171 S S   . SO4   I 2 .  ? 14.888  -27.057 -26.592 1.00 58.91  ? 102 SO4   B S   1 
HETATM 2172 O O1  . SO4   I 2 .  ? 16.181  -26.558 -26.199 1.00 60.29  ? 102 SO4   B O1  1 
HETATM 2173 O O2  . SO4   I 2 .  ? 15.069  -28.322 -27.260 1.00 70.70  ? 102 SO4   B O2  1 
HETATM 2174 O O3  . SO4   I 2 .  ? 14.071  -27.243 -25.426 1.00 67.33  ? 102 SO4   B O3  1 
HETATM 2175 O O4  . SO4   I 2 .  ? 14.213  -26.141 -27.482 1.00 61.61  ? 102 SO4   B O4  1 
HETATM 2176 C C4  . A1A3V J 4 .  ? 18.810  -16.720 -24.428 0.82 54.30  ? 103 A1A3V B C4  1 
HETATM 2177 C C5  . A1A3V J 4 .  ? 18.730  -16.105 -25.820 0.82 42.99  ? 103 A1A3V B C5  1 
HETATM 2178 C C6  . A1A3V J 4 .  ? 17.300  -15.789 -26.203 0.82 45.55  ? 103 A1A3V B C6  1 
HETATM 2179 C C7  . A1A3V J 4 .  ? 16.613  -14.911 -25.157 0.82 51.42  ? 103 A1A3V B C7  1 
HETATM 2180 C C8  . A1A3V J 4 .  ? 16.755  -15.462 -23.736 0.82 41.38  ? 103 A1A3V B C8  1 
HETATM 2181 O O   . A1A3V J 4 .  ? 18.496  -14.179 -19.661 0.82 53.11  ? 103 A1A3V B O   1 
HETATM 2182 C C1  . A1A3V J 4 .  ? 18.582  -15.605 -19.588 0.82 54.71  ? 103 A1A3V B C1  1 
HETATM 2183 C C   . A1A3V J 4 .  ? 17.806  -16.084 -18.374 0.82 46.89  ? 103 A1A3V B C   1 
HETATM 2184 C C2  . A1A3V J 4 .  ? 17.900  -16.085 -20.899 0.82 43.99  ? 103 A1A3V B C2  1 
HETATM 2185 N N   . A1A3V J 4 .  ? 18.802  -15.979 -22.051 0.82 49.46  ? 103 A1A3V B N   1 
HETATM 2186 C C3  . A1A3V J 4 .  ? 18.213  -15.782 -23.394 0.82 46.50  ? 103 A1A3V B C3  1 
HETATM 2187 C C1  . EDO   K 3 .  ? 16.935  -36.303 16.368  1.00 44.63  ? 101 EDO   C C1  1 
HETATM 2188 O O1  . EDO   K 3 .  ? 15.818  -37.041 15.835  1.00 49.18  ? 101 EDO   C O1  1 
HETATM 2189 C C2  . EDO   K 3 .  ? 16.563  -35.364 17.500  1.00 38.07  ? 101 EDO   C C2  1 
HETATM 2190 O O2  . EDO   K 3 .  ? 15.659  -35.925 18.414  1.00 42.73  ? 101 EDO   C O2  1 
HETATM 2191 S S   . SO4   L 2 .  ? 29.562  -38.462 12.116  1.00 104.75 ? 102 SO4   C S   1 
HETATM 2192 O O1  . SO4   L 2 .  ? 30.250  -37.692 11.110  1.00 96.03  ? 102 SO4   C O1  1 
HETATM 2193 O O2  . SO4   L 2 .  ? 28.147  -38.226 12.010  1.00 70.26  ? 102 SO4   C O2  1 
HETATM 2194 O O3  . SO4   L 2 .  ? 29.826  -39.865 11.923  1.00 91.50  ? 102 SO4   C O3  1 
HETATM 2195 O O4  . SO4   L 2 .  ? 30.020  -38.064 13.425  1.00 101.11 ? 102 SO4   C O4  1 
HETATM 2196 O O   . HOH   M 5 .  ? 9.787   -32.009 3.889   1.00 60.18  ? 201 HOH   A O   1 
HETATM 2197 O O   . HOH   M 5 .  ? 6.221   -29.018 7.050   1.00 59.58  ? 202 HOH   A O   1 
HETATM 2198 O O   . HOH   M 5 .  ? -8.145  -22.839 4.543   1.00 68.98  ? 203 HOH   A O   1 
HETATM 2199 O O   . HOH   M 5 .  ? 6.480   -7.888  9.889   1.00 71.85  ? 204 HOH   A O   1 
HETATM 2200 O O   . HOH   M 5 .  ? 4.326   -10.532 13.677  1.00 56.82  ? 205 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 1.277   -25.002 13.764  1.00 60.01  ? 206 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? 11.413  -29.821 3.001   1.00 52.23  ? 207 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? -1.899  -31.011 -3.911  1.00 53.94  ? 208 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? -5.695  -13.497 -16.535 1.00 54.58  ? 209 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? 13.113  -12.140 8.080   1.00 59.84  ? 210 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? 9.491   -18.222 -10.899 1.00 41.21  ? 211 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 16.252  -24.621 1.780   1.00 47.24  ? 212 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? 0.533   -33.886 4.742   1.00 62.58  ? 213 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? -3.582  -10.962 6.761   1.00 49.14  ? 214 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 0.788   -10.506 -15.530 1.00 52.11  ? 215 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 14.186  -15.726 -9.181  1.00 44.21  ? 216 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 4.860   -7.914  1.188   1.00 39.76  ? 217 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 2.650   -25.408 -6.558  1.00 59.49  ? 218 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 0.631   -23.198 9.273   1.00 59.40  ? 219 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 2.835   -25.231 -9.999  1.00 43.57  ? 220 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 9.794   -22.987 -9.391  1.00 54.56  ? 221 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 4.800   -34.632 4.493   1.00 74.20  ? 222 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? -7.667  -17.113 6.626   1.00 49.49  ? 223 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 4.683   -3.586  -3.231  1.00 40.59  ? 224 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 7.196   -10.434 -12.037 1.00 45.17  ? 225 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 9.171   -16.202 -13.097 1.00 49.32  ? 226 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 11.511  -23.787 9.836   1.00 45.38  ? 227 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -5.947  -11.508 -11.389 1.00 47.87  ? 228 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 20.133  -15.503 7.312   1.00 37.46  ? 229 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 1.732   -18.522 -18.761 1.00 60.53  ? 230 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? -8.189  -17.305 3.265   1.00 62.13  ? 231 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 13.523  -28.106 -4.701  1.00 59.36  ? 232 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 11.203  -5.204  -7.723  1.00 41.35  ? 233 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 3.512   -29.626 -0.474  1.00 48.88  ? 234 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -0.422  -21.039 6.909   1.00 42.08  ? 235 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 11.778  -11.963 5.914   1.00 42.24  ? 236 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 14.635  -17.599 -19.244 1.00 45.43  ? 237 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? -5.468  -15.999 -8.010  1.00 35.93  ? 238 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? -7.903  -15.745 -1.082  1.00 43.14  ? 239 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -2.378  -11.673 13.745  1.00 58.65  ? 240 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -4.210  -25.949 -5.636  1.00 53.10  ? 241 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? -2.102  3.362   -2.200  1.00 51.05  ? 242 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 8.357   -17.486 8.540   1.00 49.06  ? 243 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 9.936   -6.005  -1.611  1.00 40.14  ? 244 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? -4.040  -21.378 6.026   1.00 48.35  ? 245 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -5.516  -26.892 3.242   1.00 56.97  ? 246 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 15.925  -12.040 -5.225  1.00 40.46  ? 247 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 13.587  -12.014 -4.218  1.00 30.04  ? 248 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 11.734  -12.401 -6.103  1.00 34.65  ? 249 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? -5.520  -19.833 -5.654  1.00 42.63  ? 250 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -0.392  -20.653 11.301  1.00 63.20  ? 251 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 17.460  -12.876 1.393   1.00 28.68  ? 252 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 11.774  -16.465 -14.832 1.00 56.92  ? 253 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -8.088  -19.230 -3.236  1.00 54.41  ? 254 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 15.108  -13.382 10.339  1.00 54.49  ? 255 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 3.151   -2.184  -1.260  1.00 52.67  ? 256 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? -1.472  -22.124 -0.645  1.00 35.07  ? 257 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 11.637  -6.051  -3.868  1.00 54.34  ? 258 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 13.155  -9.544  -7.082  1.00 48.22  ? 259 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 2.737   -6.483  5.484   1.00 42.77  ? 260 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 2.154   -4.632  -10.357 1.00 46.08  ? 261 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 10.352  -13.119 9.562   1.00 47.81  ? 262 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? -7.648  -16.705 1.578   1.00 46.97  ? 263 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 16.924  -12.571 -17.168 1.00 51.64  ? 264 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? 6.074   -8.734  3.969   1.00 55.23  ? 265 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? -2.581  -5.917  10.616  1.00 91.02  ? 266 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? -0.238  -29.516 10.352  1.00 64.52  ? 267 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -1.375  -11.913 11.255  1.00 46.28  ? 268 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 1.915   -10.646 11.728  1.00 42.61  ? 269 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 15.890  -28.163 -0.570  1.00 56.37  ? 270 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 8.084   -7.851  1.259   1.00 42.12  ? 271 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? -1.168  -7.577  11.601  1.00 50.98  ? 272 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 8.382   -8.331  4.434   1.00 44.87  ? 273 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 10.338  -27.617 -7.271  1.00 56.82  ? 274 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 6.904   -5.803  0.570   1.00 63.07  ? 275 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 3.162   -9.913  -13.245 1.00 52.44  ? 276 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -8.476  -16.213 -12.694 1.00 62.30  ? 277 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 13.071  -13.495 -8.421  1.00 54.48  ? 278 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -5.941  -12.766 6.721   1.00 46.64  ? 279 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -10.974 -16.117 -3.942  1.00 63.90  ? 280 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 17.617  -13.992 10.472  1.00 57.59  ? 281 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 12.246  -16.367 -12.060 1.00 73.37  ? 282 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 6.551   -15.969 -15.034 1.00 53.22  ? 283 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 21.686  -16.799 -3.476  1.00 39.30  ? 284 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 9.760   -20.306 -18.462 1.00 62.19  ? 285 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 14.660  -29.645 4.016   1.00 46.80  ? 286 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 8.615   -17.991 -15.741 1.00 71.91  ? 287 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 11.339  -7.811  0.389   1.00 36.33  ? 288 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 17.517  -18.335 -9.542  1.00 67.60  ? 289 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 9.772   -3.380  -0.351  1.00 70.95  ? 290 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 5.274   -7.463  3.966   1.00 41.51  ? 291 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 7.935   -30.084 -3.726  1.00 59.84  ? 292 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -2.570  -21.163 -9.727  1.00 48.80  ? 293 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? -7.075  -11.555 -8.022  1.00 36.25  ? 294 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 22.666  -16.558 -0.445  1.00 47.65  ? 295 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -3.788  -7.900  10.630  1.00 53.18  ? 296 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -5.190  -23.688 -6.812  1.00 45.43  ? 297 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -3.770  -26.525 7.489   1.00 68.55  ? 298 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? -8.314  -21.224 -1.389  1.00 46.17  ? 299 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? -10.594 -27.087 -1.136  1.00 67.66  ? 300 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -6.978  -21.628 -6.180  1.00 58.35  ? 301 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 9.204   -9.145  -13.847 1.00 47.68  ? 302 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -3.620  -10.905 9.554   1.00 57.34  ? 303 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 1.426   -29.065 -7.210  1.00 61.09  ? 304 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 0.332   -8.129  -13.240 1.00 57.17  ? 305 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? -0.331  -3.477  -10.888 1.00 64.70  ? 306 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -7.034  -14.097 -9.322  1.00 43.96  ? 307 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 5.286   -7.135  -11.027 1.00 58.13  ? 308 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 11.759  -2.027  -1.751  1.00 53.05  ? 309 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? -5.652  -23.479 5.483   1.00 64.78  ? 310 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -7.946  -13.984 -14.928 1.00 75.57  ? 311 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? 9.691   -7.493  2.929   1.00 47.76  ? 312 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? -2.855  -21.521 7.966   1.00 53.58  ? 313 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? 4.850   -9.573  -11.378 1.00 47.00  ? 314 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? 13.335  -19.112 -12.658 1.00 58.17  ? 315 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -6.849  -19.443 8.428   1.00 56.46  ? 316 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? -4.878  -21.037 -8.359  1.00 59.44  ? 317 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -9.598  -21.689 -6.431  1.00 59.72  ? 318 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? 4.801   -3.454  1.881   1.00 65.51  ? 319 HOH   A O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 10.153  -11.244 -38.283 1.00 52.90  ? 201 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 28.042  -8.106  -29.240 1.00 52.06  ? 202 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 30.656  -7.928  -30.337 1.00 56.51  ? 203 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 6.748   -12.264 -26.335 1.00 46.19  ? 204 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 30.462  -19.821 -40.643 1.00 46.85  ? 205 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 25.257  -5.144  -30.096 1.00 51.48  ? 206 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 13.419  -1.183  -34.373 1.00 82.97  ? 207 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 7.179   -19.289 -35.415 1.00 60.78  ? 208 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 15.686  -25.534 -45.661 1.00 56.90  ? 209 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 8.694   -8.576  -16.703 1.00 54.07  ? 210 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 6.063   -7.435  -32.285 1.00 62.86  ? 211 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 21.157  -26.303 -30.611 1.00 67.08  ? 212 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 16.820  -19.240 -29.028 1.00 36.46  ? 213 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 26.439  -23.024 -31.561 1.00 45.72  ? 214 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 11.306  -8.102  -41.649 1.00 50.93  ? 215 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 22.633  -12.296 -20.574 1.00 57.82  ? 216 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 3.316   -8.765  -27.523 1.00 64.09  ? 217 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 23.553  -2.349  -29.379 1.00 52.93  ? 218 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 20.761  -13.446 -42.983 1.00 51.04  ? 219 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 13.052  -4.657  -42.175 1.00 72.76  ? 220 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 10.739  -18.945 -33.143 1.00 40.72  ? 221 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 8.375   -27.949 -38.633 1.00 63.10  ? 222 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 24.595  -1.643  -36.836 1.00 57.19  ? 223 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 7.485   -18.191 -31.833 1.00 57.28  ? 224 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 18.105  -0.552  -38.716 1.00 39.60  ? 225 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 17.627  -19.869 -42.255 1.00 56.25  ? 226 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 14.370  -6.224  -41.315 1.00 58.16  ? 227 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 25.462  -5.923  -36.124 1.00 52.29  ? 228 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 20.345  -2.442  -23.265 1.00 72.00  ? 229 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 18.550  -0.410  -25.735 1.00 65.84  ? 230 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 22.855  -23.159 -29.029 1.00 47.26  ? 231 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 17.749  -15.934 -46.001 1.00 54.47  ? 232 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 20.065  -25.690 -34.314 1.00 48.88  ? 233 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 18.996  -20.137 -19.423 1.00 62.99  ? 234 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 23.686  -4.172  -37.140 1.00 41.35  ? 235 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 18.669  -25.878 -28.925 1.00 49.60  ? 236 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 4.565   -18.984 -25.915 1.00 70.52  ? 237 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 10.398  -16.969 -44.513 1.00 51.04  ? 238 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 13.635  -22.237 -20.807 1.00 58.18  ? 239 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 10.364  -19.816 -43.321 1.00 63.56  ? 240 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 17.255  -25.801 -34.485 1.00 47.64  ? 241 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 22.468  3.615   -33.108 1.00 59.68  ? 242 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 28.460  -17.505 -25.266 1.00 52.08  ? 243 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 31.764  -12.395 -39.261 1.00 63.88  ? 244 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 20.391  -10.237 -43.268 1.00 48.47  ? 245 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 10.865  -21.959 -32.857 1.00 47.26  ? 246 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 32.050  -21.255 -38.501 1.00 51.92  ? 247 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 27.953  -24.818 -35.529 1.00 45.71  ? 248 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 14.764  -24.364 -40.569 1.00 47.85  ? 249 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 16.802  -9.545  -44.224 1.00 54.65  ? 250 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 18.371  -13.141 -44.682 1.00 56.37  ? 251 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 32.505  -19.269 -42.813 1.00 57.68  ? 252 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 20.912  -6.460  -42.902 1.00 44.18  ? 253 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 1.784   -13.174 -28.721 1.00 56.79  ? 254 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 18.333  -3.668  -22.248 1.00 65.69  ? 255 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 17.330  1.684   -29.639 1.00 66.25  ? 256 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 6.629   -20.796 -25.217 1.00 51.06  ? 257 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 24.027  -11.024 -22.181 1.00 50.21  ? 258 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 7.649   -7.936  -20.952 1.00 63.77  ? 259 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 34.517  -23.807 -30.321 1.00 63.74  ? 260 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 24.801  -6.424  -43.105 1.00 53.47  ? 261 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 18.516  4.536   -34.559 1.00 48.69  ? 262 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 7.558   -12.403 -39.416 1.00 57.34  ? 263 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 20.607  3.799   -33.226 1.00 47.48  ? 264 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 26.582  -0.509  -29.457 1.00 60.33  ? 265 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 20.880  -20.970 -23.370 1.00 56.47  ? 266 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 28.058  -10.856 -28.962 1.00 66.87  ? 267 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 17.178  -26.004 -21.408 1.00 72.54  ? 268 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 9.756   -6.250  -41.284 1.00 63.55  ? 269 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 13.071  -19.870 -19.553 1.00 57.65  ? 270 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 15.307  -8.082  -43.338 1.00 52.48  ? 271 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 15.229  -18.428 -16.761 1.00 49.15  ? 272 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 14.961  -21.790 -42.208 1.00 55.65  ? 273 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 36.045  -28.819 -35.546 1.00 76.31  ? 274 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 7.344   -9.841  -18.739 1.00 53.92  ? 275 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 24.812  -4.141  -27.999 1.00 66.87  ? 276 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 40.191  -13.844 -38.711 1.00 61.16  ? 277 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 22.830  -29.339 -35.917 1.00 53.56  ? 278 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 8.545   -22.670 -19.779 1.00 62.91  ? 279 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 17.199  -14.428 -15.142 1.00 56.09  ? 280 HOH   B O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 26.812  -39.415 12.731  1.00 53.76  ? 201 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 27.342  -37.895 10.228  1.00 50.50  ? 202 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 15.672  -17.213 24.773  1.00 69.84  ? 203 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 15.910  -27.133 28.516  1.00 61.39  ? 204 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 8.041   -31.682 12.559  1.00 55.66  ? 205 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 15.876  -41.177 15.450  1.00 66.21  ? 206 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 20.175  -19.870 29.873  1.00 68.01  ? 207 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 31.861  -33.351 25.903  1.00 56.77  ? 208 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 15.090  -39.243 16.628  1.00 66.17  ? 209 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 30.640  -28.316 30.457  1.00 65.11  ? 210 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 18.074  -21.124 13.221  1.00 59.07  ? 211 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 13.363  -20.055 10.856  1.00 59.63  ? 212 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 13.994  -22.780 27.861  1.00 78.89  ? 213 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 33.555  -24.464 31.697  1.00 57.96  ? 214 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 12.262  -28.676 28.024  1.00 64.09  ? 215 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 17.661  -17.262 15.151  1.00 52.76  ? 216 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 19.494  -20.220 10.596  1.00 50.26  ? 217 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 25.813  -19.600 6.484   1.00 47.66  ? 218 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 15.899  -17.767 19.319  1.00 58.68  ? 219 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 9.434   -37.320 18.243  1.00 64.31  ? 220 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 13.128  -31.558 8.210   1.00 40.81  ? 221 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 27.853  -19.240 12.822  1.00 64.47  ? 222 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 5.527   -26.829 16.761  1.00 60.36  ? 223 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 16.412  -37.859 20.057  1.00 64.10  ? 224 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 20.332  -41.983 12.172  1.00 37.34  ? 225 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 28.561  -37.246 15.870  1.00 49.96  ? 226 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 25.761  -33.833 34.892  1.00 61.17  ? 227 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 30.710  -17.602 9.612   1.00 51.52  ? 228 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 14.846  -37.311 13.338  1.00 50.96  ? 229 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 30.628  -35.862 28.811  1.00 66.09  ? 230 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 15.564  -21.135 12.364  1.00 48.26  ? 231 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 26.126  -17.546 13.991  1.00 59.21  ? 232 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 22.907  -21.641 7.453   1.00 45.60  ? 233 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 9.117   -18.964 23.436  1.00 59.13  ? 234 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 30.260  -39.801 31.407  1.00 48.04  ? 235 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 24.079  -18.465 21.735  1.00 63.50  ? 236 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 22.479  -28.626 11.042  1.00 40.51  ? 237 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 31.696  -39.787 27.120  1.00 53.42  ? 238 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 22.478  -34.498 16.564  1.00 35.46  ? 239 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 23.270  -41.780 18.516  1.00 48.89  ? 240 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 21.172  -29.638 4.710   1.00 68.57  ? 241 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 19.560  -26.877 3.175   1.00 52.54  ? 242 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 7.143   -18.021 10.823  1.00 47.69  ? 243 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 20.930  -40.085 26.496  1.00 48.17  ? 244 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 30.666  -31.695 15.884  1.00 55.96  ? 245 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 25.528  -31.455 10.807  1.00 43.41  ? 246 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 21.200  -28.796 8.525   1.00 43.55  ? 247 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 20.591  -19.198 24.777  1.00 69.03  ? 248 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 9.977   -30.470 9.983   1.00 42.58  ? 249 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 26.000  -39.825 20.145  1.00 47.92  ? 250 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 30.794  -29.244 12.097  1.00 53.53  ? 251 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 27.980  -37.652 25.135  1.00 61.50  ? 252 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 28.651  -15.210 13.004  1.00 67.13  ? 253 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 2.763   -28.347 14.131  1.00 60.39  ? 254 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 31.826  -29.308 32.621  1.00 66.06  ? 255 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 13.959  -39.047 9.134   1.00 77.93  ? 256 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 30.565  -32.737 18.291  1.00 54.83  ? 257 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 31.756  -43.498 16.017  1.00 65.16  ? 258 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 26.529  -17.841 21.334  1.00 79.04  ? 259 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 32.158  -43.314 11.572  1.00 58.57  ? 260 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 31.768  -34.467 35.363  1.00 69.66  ? 261 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 4.799   -23.788 18.763  1.00 75.88  ? 262 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 20.344  -36.971 40.549  1.00 62.00  ? 263 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 30.462  -25.640 32.447  1.00 67.76  ? 264 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 17.644  -36.496 29.317  1.00 60.90  ? 265 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 17.313  -38.483 28.590  1.00 61.18  ? 266 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 29.180  -34.230 11.073  1.00 72.97  ? 267 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 12.156  -21.338 10.614  1.00 48.54  ? 268 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 29.325  -41.750 27.277  1.00 52.44  ? 269 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 22.910  -14.339 13.485  1.00 57.00  ? 270 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 7.854   -18.554 25.967  1.00 64.89  ? 271 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 24.052  -15.902 12.139  1.00 54.42  ? 272 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 17.163  -39.726 21.400  1.00 62.39  ? 273 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 32.487  -39.214 30.021  1.00 55.11  ? 274 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 20.188  -33.426 35.058  1.00 72.10  ? 275 HOH   C O   1 
HETATM 2470 O O   . HOH   O 5 .  ? 37.572  -24.332 27.002  1.00 73.67  ? 276 HOH   C O   1 
HETATM 2471 O O   . HOH   O 5 .  ? 28.586  -41.746 29.933  1.00 50.44  ? 277 HOH   C O   1 
HETATM 2472 O O   . HOH   O 5 .  ? 27.267  -39.940 24.397  1.00 65.84  ? 278 HOH   C O   1 
HETATM 2473 O O   . HOH   O 5 .  ? 21.491  -42.074 40.864  1.00 67.52  ? 279 HOH   C O   1 
HETATM 2474 O O   . HOH   O 5 .  ? 33.702  -44.787 15.301  1.00 46.95  ? 280 HOH   C O   1 
HETATM 2475 O O   . HOH   O 5 .  ? 12.054  -41.241 13.346  1.00 58.02  ? 281 HOH   C O   1 
# 
