data_7HHE
# 
_entry.id   7HHE 
# 
_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   7HHE         pdb_00007hhe 10.2210/pdb7hhe/pdb 
WWPDB D_1001407476 ?            ?                   
# 
_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                        7HHE 
_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    1   ? ?    ? ? 
4 non-polymer syn 'N-methyl-N-(pyridin-3-yl)acetamide'               150.178   3   ? ?    ? ? 
5 water       nat water                                              18.015    252 ? ?    ? ? 
# 
_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 'N-methyl-N-(pyridin-3-yl)acetamide' A1A38 
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 
A1A38 non-polymer         . 'N-methyl-N-(pyridin-3-yl)acetamide' ?                 'C8 H10 N2 O'    150.178 
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 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 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 29 ALA ALA 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        A1A38 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A38 
_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 4 A1A38 1   104 101 A1A38 LIG A . 
H 2 SO4   1   105 4   SO4   SO4 A . 
I 2 SO4   1   101 1   SO4   SO4 B . 
J 2 SO4   1   102 3   SO4   SO4 B . 
K 4 A1A38 1   103 102 A1A38 LIG B . 
L 2 SO4   1   101 5   SO4   SO4 C . 
M 4 A1A38 1   102 101 A1A38 LIG C . 
N 5 HOH   1   201 339 HOH   HOH A . 
N 5 HOH   2   202 84  HOH   HOH A . 
N 5 HOH   3   203 202 HOH   HOH A . 
N 5 HOH   4   204 307 HOH   HOH A . 
N 5 HOH   5   205 334 HOH   HOH A . 
N 5 HOH   6   206 139 HOH   HOH A . 
N 5 HOH   7   207 338 HOH   HOH A . 
N 5 HOH   8   208 71  HOH   HOH A . 
N 5 HOH   9   209 336 HOH   HOH A . 
N 5 HOH   10  210 167 HOH   HOH A . 
N 5 HOH   11  211 12  HOH   HOH A . 
N 5 HOH   12  212 38  HOH   HOH A . 
N 5 HOH   13  213 188 HOH   HOH A . 
N 5 HOH   14  214 66  HOH   HOH A . 
N 5 HOH   15  215 32  HOH   HOH A . 
N 5 HOH   16  216 35  HOH   HOH A . 
N 5 HOH   17  217 287 HOH   HOH A . 
N 5 HOH   18  218 27  HOH   HOH A . 
N 5 HOH   19  219 94  HOH   HOH A . 
N 5 HOH   20  220 86  HOH   HOH A . 
N 5 HOH   21  221 87  HOH   HOH A . 
N 5 HOH   22  222 42  HOH   HOH A . 
N 5 HOH   23  223 292 HOH   HOH A . 
N 5 HOH   24  224 346 HOH   HOH A . 
N 5 HOH   25  225 95  HOH   HOH A . 
N 5 HOH   26  226 78  HOH   HOH A . 
N 5 HOH   27  227 97  HOH   HOH A . 
N 5 HOH   28  228 289 HOH   HOH A . 
N 5 HOH   29  229 91  HOH   HOH A . 
N 5 HOH   30  230 85  HOH   HOH A . 
N 5 HOH   31  231 93  HOH   HOH A . 
N 5 HOH   32  232 288 HOH   HOH A . 
N 5 HOH   33  233 1   HOH   HOH A . 
N 5 HOH   34  234 293 HOH   HOH A . 
N 5 HOH   35  235 26  HOH   HOH A . 
N 5 HOH   36  236 60  HOH   HOH A . 
N 5 HOH   37  237 8   HOH   HOH A . 
N 5 HOH   38  238 199 HOH   HOH A . 
N 5 HOH   39  239 55  HOH   HOH A . 
N 5 HOH   40  240 2   HOH   HOH A . 
N 5 HOH   41  241 299 HOH   HOH A . 
N 5 HOH   42  242 290 HOH   HOH A . 
N 5 HOH   43  243 23  HOH   HOH A . 
N 5 HOH   44  244 165 HOH   HOH A . 
N 5 HOH   45  245 20  HOH   HOH A . 
N 5 HOH   46  246 34  HOH   HOH A . 
N 5 HOH   47  247 274 HOH   HOH A . 
N 5 HOH   48  248 109 HOH   HOH A . 
N 5 HOH   49  249 333 HOH   HOH A . 
N 5 HOH   50  250 37  HOH   HOH A . 
N 5 HOH   51  251 28  HOH   HOH A . 
N 5 HOH   52  252 18  HOH   HOH A . 
N 5 HOH   53  253 7   HOH   HOH A . 
N 5 HOH   54  254 152 HOH   HOH A . 
N 5 HOH   55  255 203 HOH   HOH A . 
N 5 HOH   56  256 222 HOH   HOH A . 
N 5 HOH   57  257 164 HOH   HOH A . 
N 5 HOH   58  258 58  HOH   HOH A . 
N 5 HOH   59  259 267 HOH   HOH A . 
N 5 HOH   60  260 145 HOH   HOH A . 
N 5 HOH   61  261 300 HOH   HOH A . 
N 5 HOH   62  262 143 HOH   HOH A . 
N 5 HOH   63  263 297 HOH   HOH A . 
N 5 HOH   64  264 111 HOH   HOH A . 
N 5 HOH   65  265 318 HOH   HOH A . 
N 5 HOH   66  266 115 HOH   HOH A . 
N 5 HOH   67  267 281 HOH   HOH A . 
N 5 HOH   68  268 116 HOH   HOH A . 
N 5 HOH   69  269 21  HOH   HOH A . 
N 5 HOH   70  270 260 HOH   HOH A . 
N 5 HOH   71  271 99  HOH   HOH A . 
N 5 HOH   72  272 47  HOH   HOH A . 
N 5 HOH   73  273 14  HOH   HOH A . 
N 5 HOH   74  274 218 HOH   HOH A . 
N 5 HOH   75  275 350 HOH   HOH A . 
N 5 HOH   76  276 9   HOH   HOH A . 
N 5 HOH   77  277 296 HOH   HOH A . 
N 5 HOH   78  278 301 HOH   HOH A . 
N 5 HOH   79  279 83  HOH   HOH A . 
N 5 HOH   80  280 16  HOH   HOH A . 
N 5 HOH   81  281 190 HOH   HOH A . 
N 5 HOH   82  282 77  HOH   HOH A . 
N 5 HOH   83  283 19  HOH   HOH A . 
N 5 HOH   84  284 64  HOH   HOH A . 
N 5 HOH   85  285 327 HOH   HOH A . 
N 5 HOH   86  286 171 HOH   HOH A . 
N 5 HOH   87  287 131 HOH   HOH A . 
N 5 HOH   88  288 22  HOH   HOH A . 
N 5 HOH   89  289 31  HOH   HOH A . 
N 5 HOH   90  290 210 HOH   HOH A . 
N 5 HOH   91  291 113 HOH   HOH A . 
N 5 HOH   92  292 208 HOH   HOH A . 
N 5 HOH   93  293 219 HOH   HOH A . 
N 5 HOH   94  294 270 HOH   HOH A . 
N 5 HOH   95  295 283 HOH   HOH A . 
N 5 HOH   96  296 353 HOH   HOH A . 
N 5 HOH   97  297 75  HOH   HOH A . 
N 5 HOH   98  298 73  HOH   HOH A . 
N 5 HOH   99  299 108 HOH   HOH A . 
N 5 HOH   100 300 324 HOH   HOH A . 
N 5 HOH   101 301 63  HOH   HOH A . 
N 5 HOH   102 302 179 HOH   HOH A . 
N 5 HOH   103 303 304 HOH   HOH A . 
N 5 HOH   104 304 205 HOH   HOH A . 
N 5 HOH   105 305 211 HOH   HOH A . 
N 5 HOH   106 306 156 HOH   HOH A . 
N 5 HOH   107 307 185 HOH   HOH A . 
N 5 HOH   108 308 125 HOH   HOH A . 
N 5 HOH   109 309 57  HOH   HOH A . 
N 5 HOH   110 310 347 HOH   HOH A . 
N 5 HOH   111 311 206 HOH   HOH A . 
N 5 HOH   112 312 313 HOH   HOH A . 
N 5 HOH   113 313 259 HOH   HOH A . 
N 5 HOH   114 314 332 HOH   HOH A . 
O 5 HOH   1   201 258 HOH   HOH B . 
O 5 HOH   2   202 331 HOH   HOH B . 
O 5 HOH   3   203 123 HOH   HOH B . 
O 5 HOH   4   204 335 HOH   HOH B . 
O 5 HOH   5   205 247 HOH   HOH B . 
O 5 HOH   6   206 184 HOH   HOH B . 
O 5 HOH   7   207 117 HOH   HOH B . 
O 5 HOH   8   208 215 HOH   HOH B . 
O 5 HOH   9   209 89  HOH   HOH B . 
O 5 HOH   10  210 329 HOH   HOH B . 
O 5 HOH   11  211 17  HOH   HOH B . 
O 5 HOH   12  212 59  HOH   HOH B . 
O 5 HOH   13  213 69  HOH   HOH B . 
O 5 HOH   14  214 170 HOH   HOH B . 
O 5 HOH   15  215 272 HOH   HOH B . 
O 5 HOH   16  216 249 HOH   HOH B . 
O 5 HOH   17  217 25  HOH   HOH B . 
O 5 HOH   18  218 6   HOH   HOH B . 
O 5 HOH   19  219 279 HOH   HOH B . 
O 5 HOH   20  220 5   HOH   HOH B . 
O 5 HOH   21  221 74  HOH   HOH B . 
O 5 HOH   22  222 68  HOH   HOH B . 
O 5 HOH   23  223 96  HOH   HOH B . 
O 5 HOH   24  224 120 HOH   HOH B . 
O 5 HOH   25  225 10  HOH   HOH B . 
O 5 HOH   26  226 169 HOH   HOH B . 
O 5 HOH   27  227 172 HOH   HOH B . 
O 5 HOH   28  228 315 HOH   HOH B . 
O 5 HOH   29  229 119 HOH   HOH B . 
O 5 HOH   30  230 217 HOH   HOH B . 
O 5 HOH   31  231 342 HOH   HOH B . 
O 5 HOH   32  232 320 HOH   HOH B . 
O 5 HOH   33  233 98  HOH   HOH B . 
O 5 HOH   34  234 54  HOH   HOH B . 
O 5 HOH   35  235 197 HOH   HOH B . 
O 5 HOH   36  236 224 HOH   HOH B . 
O 5 HOH   37  237 24  HOH   HOH B . 
O 5 HOH   38  238 150 HOH   HOH B . 
O 5 HOH   39  239 303 HOH   HOH B . 
O 5 HOH   40  240 137 HOH   HOH B . 
O 5 HOH   41  241 214 HOH   HOH B . 
O 5 HOH   42  242 46  HOH   HOH B . 
O 5 HOH   43  243 101 HOH   HOH B . 
O 5 HOH   44  244 261 HOH   HOH B . 
O 5 HOH   45  245 61  HOH   HOH B . 
O 5 HOH   46  246 343 HOH   HOH B . 
O 5 HOH   47  247 280 HOH   HOH B . 
O 5 HOH   48  248 153 HOH   HOH B . 
O 5 HOH   49  249 345 HOH   HOH B . 
O 5 HOH   50  250 36  HOH   HOH B . 
O 5 HOH   51  251 13  HOH   HOH B . 
O 5 HOH   52  252 72  HOH   HOH B . 
O 5 HOH   53  253 104 HOH   HOH B . 
O 5 HOH   54  254 76  HOH   HOH B . 
O 5 HOH   55  255 182 HOH   HOH B . 
O 5 HOH   56  256 175 HOH   HOH B . 
O 5 HOH   57  257 242 HOH   HOH B . 
O 5 HOH   58  258 157 HOH   HOH B . 
O 5 HOH   59  259 223 HOH   HOH B . 
O 5 HOH   60  260 316 HOH   HOH B . 
O 5 HOH   61  261 79  HOH   HOH B . 
O 5 HOH   62  262 44  HOH   HOH B . 
O 5 HOH   63  263 160 HOH   HOH B . 
O 5 HOH   64  264 201 HOH   HOH B . 
O 5 HOH   65  265 163 HOH   HOH B . 
O 5 HOH   66  266 309 HOH   HOH B . 
O 5 HOH   67  267 177 HOH   HOH B . 
O 5 HOH   68  268 291 HOH   HOH B . 
O 5 HOH   69  269 319 HOH   HOH B . 
O 5 HOH   70  270 322 HOH   HOH B . 
O 5 HOH   71  271 314 HOH   HOH B . 
O 5 HOH   72  272 107 HOH   HOH B . 
O 5 HOH   73  273 348 HOH   HOH B . 
O 5 HOH   74  274 92  HOH   HOH B . 
O 5 HOH   75  275 312 HOH   HOH B . 
O 5 HOH   76  276 352 HOH   HOH B . 
P 5 HOH   1   201 161 HOH   HOH C . 
P 5 HOH   2   202 340 HOH   HOH C . 
P 5 HOH   3   203 269 HOH   HOH C . 
P 5 HOH   4   204 323 HOH   HOH C . 
P 5 HOH   5   205 341 HOH   HOH C . 
P 5 HOH   6   206 275 HOH   HOH C . 
P 5 HOH   7   207 173 HOH   HOH C . 
P 5 HOH   8   208 344 HOH   HOH C . 
P 5 HOH   9   209 321 HOH   HOH C . 
P 5 HOH   10  210 226 HOH   HOH C . 
P 5 HOH   11  211 102 HOH   HOH C . 
P 5 HOH   12  212 254 HOH   HOH C . 
P 5 HOH   13  213 49  HOH   HOH C . 
P 5 HOH   14  214 142 HOH   HOH C . 
P 5 HOH   15  215 271 HOH   HOH C . 
P 5 HOH   16  216 118 HOH   HOH C . 
P 5 HOH   17  217 15  HOH   HOH C . 
P 5 HOH   18  218 90  HOH   HOH C . 
P 5 HOH   19  219 4   HOH   HOH C . 
P 5 HOH   20  220 45  HOH   HOH C . 
P 5 HOH   21  221 48  HOH   HOH C . 
P 5 HOH   22  222 209 HOH   HOH C . 
P 5 HOH   23  223 134 HOH   HOH C . 
P 5 HOH   24  224 56  HOH   HOH C . 
P 5 HOH   25  225 122 HOH   HOH C . 
P 5 HOH   26  226 41  HOH   HOH C . 
P 5 HOH   27  227 302 HOH   HOH C . 
P 5 HOH   28  228 43  HOH   HOH C . 
P 5 HOH   29  229 53  HOH   HOH C . 
P 5 HOH   30  230 284 HOH   HOH C . 
P 5 HOH   31  231 298 HOH   HOH C . 
P 5 HOH   32  232 349 HOH   HOH C . 
P 5 HOH   33  233 317 HOH   HOH C . 
P 5 HOH   34  234 295 HOH   HOH C . 
P 5 HOH   35  235 67  HOH   HOH C . 
P 5 HOH   36  236 337 HOH   HOH C . 
P 5 HOH   37  237 148 HOH   HOH C . 
P 5 HOH   38  238 294 HOH   HOH C . 
P 5 HOH   39  239 132 HOH   HOH C . 
P 5 HOH   40  240 135 HOH   HOH C . 
P 5 HOH   41  241 126 HOH   HOH C . 
P 5 HOH   42  242 65  HOH   HOH C . 
P 5 HOH   43  243 40  HOH   HOH C . 
P 5 HOH   44  244 130 HOH   HOH C . 
P 5 HOH   45  245 62  HOH   HOH C . 
P 5 HOH   46  246 246 HOH   HOH C . 
P 5 HOH   47  247 149 HOH   HOH C . 
P 5 HOH   48  248 82  HOH   HOH C . 
P 5 HOH   49  249 328 HOH   HOH C . 
P 5 HOH   50  250 198 HOH   HOH C . 
P 5 HOH   51  251 189 HOH   HOH C . 
P 5 HOH   52  252 168 HOH   HOH C . 
P 5 HOH   53  253 151 HOH   HOH C . 
P 5 HOH   54  254 305 HOH   HOH C . 
P 5 HOH   55  255 325 HOH   HOH C . 
P 5 HOH   56  256 330 HOH   HOH C . 
P 5 HOH   57  257 241 HOH   HOH C . 
P 5 HOH   58  258 146 HOH   HOH C . 
P 5 HOH   59  259 70  HOH   HOH C . 
P 5 HOH   60  260 103 HOH   HOH C . 
P 5 HOH   61  261 351 HOH   HOH C . 
P 5 HOH   62  262 310 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 ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
17 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
18 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
19 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
20 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
21 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
22 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
23 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
24 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
25 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
26 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
27 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
28 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
29 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
30 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
31 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
32 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
33 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
34 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
35 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
36 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
37 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
38 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
39 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
40 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
41 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
42 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
43 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
44 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
45 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
46 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
47 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 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' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHE 
_cell.length_a           41.483 
_cell.length_b           41.981 
_cell.length_c           157.989 
_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                         7HHE 
_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          7HHE 
_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                     7HHE 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             78.99 
_reflns.d_resolution_high            2.04 
_reflns.number_obs                   18462 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.187 
_reflns.pdbx_netI_over_sigmaI        6.9 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.203 
_reflns.pdbx_Rpim_I_all              0.080 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     117733 
_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                  2.04 
_reflns_shell.d_res_low                   2.15 
_reflns_shell.number_measured_all         16792 
_reflns_shell.number_unique_obs           2601 
_reflns_shell.Rmerge_I_obs                1.910 
_reflns_shell.pdbx_chi_squared            0.89 
_reflns_shell.pdbx_redundancy             6.5 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             2.077 
_reflns_shell.pdbx_Rpim_I_all             0.809 
_reflns_shell.pdbx_CC_half                0.417 
_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                                 7HHE 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17404 
_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                             78.99 
_refine.ls_d_res_high                            2.04 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_R_factor_obs                          0.19065 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18646 
_refine.ls_R_factor_R_free                       0.26462 
_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                  974 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.B_iso_mean                               44.387 
_refine.aniso_B[1][1]                            0.99 
_refine.aniso_B[2][2]                            -0.44 
_refine.aniso_B[3][3]                            -0.55 
_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                       0.223 
_refine.pdbx_overall_ESU_R_Free                  0.207 
_refine.overall_SU_ML                            0.190 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             7.575 
_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        2153 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             252 
_refine_hist.number_atoms_total               2472 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        78.99 
# 
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             0.008  0.012  ? 2315 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.778  1.834  ? 3146 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.565  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.648  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.130 10.000 ? 310  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.143  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1976 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.365  4.238  ? 1075 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.228  7.559  ? 1336 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.152  4.497  ? 1240 '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       12.004 64.84  ? 3692 '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                       2.038 
_refine_ls_shell.d_res_low                        2.090 
_refine_ls_shell.number_reflns_R_work             1230 
_refine_ls_shell.R_factor_R_work                  0.339 
_refine_ls_shell.percent_reflns_obs               97.97 
_refine_ls_shell.R_factor_R_free                  0.414 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             71 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHE 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1203252645' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHE 
_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 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 4 ? 
L N N 2 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P 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 7HHE A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHE B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHE 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 7HHE GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHE SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHE GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHE SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHE GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHE 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,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHE 
_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 241 ? ? O C HOH 202 ? ? 1.67 
2 1 OD1 A ASP 27  ? ? O A HOH 201 ? ? 2.00 
3 1 O   B HOH 227 ? ? O B HOH 237 ? ? 2.02 
4 1 O   A PRO 37  ? ? O A HOH 202 ? ? 2.10 
5 1 O4  A SO4 105 ? ? O A HOH 203 ? ? 2.13 
6 1 OD2 B ASP 26  ? ? O B HOH 201 ? ? 2.14 
7 1 O   B HOH 247 ? ? O B HOH 270 ? ? 2.17 
8 1 O   B LYS 16  ? ? O B HOH 202 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 269 ? ? 1_555 O C HOH 238 ? ? 4_435 1.98 
2 1 O A HOH 223 ? ? 1_555 O A HOH 256 ? ? 4_545 2.16 
# 
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 PRO A 71 ? ? -43.66  150.12 
2 1 ASN A 87 ? ? -157.39 67.68  
3 1 ASN B 38 ? ? 90.40   -20.15 
4 1 PRO B 60 ? ? -39.21  123.88 
5 1 ASN B 87 ? ? -159.45 60.16  
6 1 ASN C 87 ? ? -171.89 53.01  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.15 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       314 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.93 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ASP 30 ? C ASP 31 
11 1 Y 1 C GLY 31 ? C GLY 32 
12 1 Y 1 C ALA 32 ? C ALA 33 
13 1 Y 1 C VAL 33 ? C VAL 34 
14 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 
A1A38 N1   N Y N 1   
A1A38 C4   C Y N 2   
A1A38 C5   C Y N 3   
A1A38 C6   C Y N 4   
A1A38 C7   C Y N 5   
A1A38 O    O N N 6   
A1A38 C1   C N N 7   
A1A38 C2   C N N 8   
A1A38 N    N N N 9   
A1A38 C    C N N 10  
A1A38 C3   C Y N 11  
A1A38 H6   H N N 12  
A1A38 H7   H N N 13  
A1A38 H8   H N N 14  
A1A38 H9   H N N 15  
A1A38 H4   H N N 16  
A1A38 H3   H N N 17  
A1A38 H5   H N N 18  
A1A38 H1   H N N 19  
A1A38 H2   H N N 20  
A1A38 H    H N N 21  
ALA   N    N N N 22  
ALA   CA   C N S 23  
ALA   C    C N N 24  
ALA   O    O N N 25  
ALA   CB   C N N 26  
ALA   OXT  O N N 27  
ALA   H    H N N 28  
ALA   H2   H N N 29  
ALA   HA   H N N 30  
ALA   HB1  H N N 31  
ALA   HB2  H N N 32  
ALA   HB3  H N N 33  
ALA   HXT  H N N 34  
ARG   N    N N N 35  
ARG   CA   C N S 36  
ARG   C    C N N 37  
ARG   O    O N N 38  
ARG   CB   C N N 39  
ARG   CG   C N N 40  
ARG   CD   C N N 41  
ARG   NE   N N N 42  
ARG   CZ   C N N 43  
ARG   NH1  N N N 44  
ARG   NH2  N N N 45  
ARG   OXT  O N N 46  
ARG   H    H N N 47  
ARG   H2   H N N 48  
ARG   HA   H N N 49  
ARG   HB2  H N N 50  
ARG   HB3  H N N 51  
ARG   HG2  H N N 52  
ARG   HG3  H N N 53  
ARG   HD2  H N N 54  
ARG   HD3  H N N 55  
ARG   HE   H N N 56  
ARG   HH11 H N N 57  
ARG   HH12 H N N 58  
ARG   HH21 H N N 59  
ARG   HH22 H N N 60  
ARG   HXT  H N N 61  
ASN   N    N N N 62  
ASN   CA   C N S 63  
ASN   C    C N N 64  
ASN   O    O N N 65  
ASN   CB   C N N 66  
ASN   CG   C N N 67  
ASN   OD1  O N N 68  
ASN   ND2  N N N 69  
ASN   OXT  O N N 70  
ASN   H    H N N 71  
ASN   H2   H N N 72  
ASN   HA   H N N 73  
ASN   HB2  H N N 74  
ASN   HB3  H N N 75  
ASN   HD21 H N N 76  
ASN   HD22 H N N 77  
ASN   HXT  H N N 78  
ASP   N    N N N 79  
ASP   CA   C N S 80  
ASP   C    C N N 81  
ASP   O    O N N 82  
ASP   CB   C N N 83  
ASP   CG   C N N 84  
ASP   OD1  O N N 85  
ASP   OD2  O N N 86  
ASP   OXT  O N N 87  
ASP   H    H N N 88  
ASP   H2   H N N 89  
ASP   HA   H N N 90  
ASP   HB2  H N N 91  
ASP   HB3  H N N 92  
ASP   HD2  H N N 93  
ASP   HXT  H N N 94  
CYS   N    N N N 95  
CYS   CA   C N R 96  
CYS   C    C N N 97  
CYS   O    O N N 98  
CYS   CB   C N N 99  
CYS   SG   S N N 100 
CYS   OXT  O N N 101 
CYS   H    H N N 102 
CYS   H2   H N N 103 
CYS   HA   H N N 104 
CYS   HB2  H N N 105 
CYS   HB3  H N N 106 
CYS   HG   H N N 107 
CYS   HXT  H N N 108 
EDO   C1   C N N 109 
EDO   O1   O N N 110 
EDO   C2   C N N 111 
EDO   O2   O N N 112 
EDO   H11  H N N 113 
EDO   H12  H N N 114 
EDO   HO1  H N N 115 
EDO   H21  H N N 116 
EDO   H22  H N N 117 
EDO   HO2  H N N 118 
GLN   N    N N N 119 
GLN   CA   C N S 120 
GLN   C    C N N 121 
GLN   O    O N N 122 
GLN   CB   C N N 123 
GLN   CG   C N N 124 
GLN   CD   C N N 125 
GLN   OE1  O N N 126 
GLN   NE2  N N N 127 
GLN   OXT  O N N 128 
GLN   H    H N N 129 
GLN   H2   H N N 130 
GLN   HA   H N N 131 
GLN   HB2  H N N 132 
GLN   HB3  H N N 133 
GLN   HG2  H N N 134 
GLN   HG3  H N N 135 
GLN   HE21 H N N 136 
GLN   HE22 H N N 137 
GLN   HXT  H N N 138 
GLU   N    N N N 139 
GLU   CA   C N S 140 
GLU   C    C N N 141 
GLU   O    O N N 142 
GLU   CB   C N N 143 
GLU   CG   C N N 144 
GLU   CD   C N N 145 
GLU   OE1  O N N 146 
GLU   OE2  O N N 147 
GLU   OXT  O N N 148 
GLU   H    H N N 149 
GLU   H2   H N N 150 
GLU   HA   H N N 151 
GLU   HB2  H N N 152 
GLU   HB3  H N N 153 
GLU   HG2  H N N 154 
GLU   HG3  H N N 155 
GLU   HE2  H N N 156 
GLU   HXT  H N N 157 
GLY   N    N N N 158 
GLY   CA   C N N 159 
GLY   C    C N N 160 
GLY   O    O N N 161 
GLY   OXT  O N N 162 
GLY   H    H N N 163 
GLY   H2   H N N 164 
GLY   HA2  H N N 165 
GLY   HA3  H N N 166 
GLY   HXT  H N N 167 
HIS   N    N N N 168 
HIS   CA   C N S 169 
HIS   C    C N N 170 
HIS   O    O N N 171 
HIS   CB   C N N 172 
HIS   CG   C Y N 173 
HIS   ND1  N Y N 174 
HIS   CD2  C Y N 175 
HIS   CE1  C Y N 176 
HIS   NE2  N Y N 177 
HIS   OXT  O N N 178 
HIS   H    H N N 179 
HIS   H2   H N N 180 
HIS   HA   H N N 181 
HIS   HB2  H N N 182 
HIS   HB3  H N N 183 
HIS   HD1  H N N 184 
HIS   HD2  H N N 185 
HIS   HE1  H N N 186 
HIS   HE2  H N N 187 
HIS   HXT  H N N 188 
HOH   O    O N N 189 
HOH   H1   H N N 190 
HOH   H2   H N N 191 
ILE   N    N N N 192 
ILE   CA   C N S 193 
ILE   C    C N N 194 
ILE   O    O N N 195 
ILE   CB   C N S 196 
ILE   CG1  C N N 197 
ILE   CG2  C N N 198 
ILE   CD1  C N N 199 
ILE   OXT  O N N 200 
ILE   H    H N N 201 
ILE   H2   H N N 202 
ILE   HA   H N N 203 
ILE   HB   H N N 204 
ILE   HG12 H N N 205 
ILE   HG13 H N N 206 
ILE   HG21 H N N 207 
ILE   HG22 H N N 208 
ILE   HG23 H N N 209 
ILE   HD11 H N N 210 
ILE   HD12 H N N 211 
ILE   HD13 H N N 212 
ILE   HXT  H N N 213 
LEU   N    N N N 214 
LEU   CA   C N S 215 
LEU   C    C N N 216 
LEU   O    O N N 217 
LEU   CB   C N N 218 
LEU   CG   C N N 219 
LEU   CD1  C N N 220 
LEU   CD2  C N N 221 
LEU   OXT  O N N 222 
LEU   H    H N N 223 
LEU   H2   H N N 224 
LEU   HA   H N N 225 
LEU   HB2  H N N 226 
LEU   HB3  H N N 227 
LEU   HG   H N N 228 
LEU   HD11 H N N 229 
LEU   HD12 H N N 230 
LEU   HD13 H N N 231 
LEU   HD21 H N N 232 
LEU   HD22 H N N 233 
LEU   HD23 H N N 234 
LEU   HXT  H N N 235 
LYS   N    N N N 236 
LYS   CA   C N S 237 
LYS   C    C N N 238 
LYS   O    O N N 239 
LYS   CB   C N N 240 
LYS   CG   C N N 241 
LYS   CD   C N N 242 
LYS   CE   C N N 243 
LYS   NZ   N N N 244 
LYS   OXT  O N N 245 
LYS   H    H N N 246 
LYS   H2   H N N 247 
LYS   HA   H N N 248 
LYS   HB2  H N N 249 
LYS   HB3  H N N 250 
LYS   HG2  H N N 251 
LYS   HG3  H N N 252 
LYS   HD2  H N N 253 
LYS   HD3  H N N 254 
LYS   HE2  H N N 255 
LYS   HE3  H N N 256 
LYS   HZ1  H N N 257 
LYS   HZ2  H N N 258 
LYS   HZ3  H N N 259 
LYS   HXT  H N N 260 
MET   N    N N N 261 
MET   CA   C N S 262 
MET   C    C N N 263 
MET   O    O N N 264 
MET   CB   C N N 265 
MET   CG   C N N 266 
MET   SD   S N N 267 
MET   CE   C N N 268 
MET   OXT  O N N 269 
MET   H    H N N 270 
MET   H2   H N N 271 
MET   HA   H N N 272 
MET   HB2  H N N 273 
MET   HB3  H N N 274 
MET   HG2  H N N 275 
MET   HG3  H N N 276 
MET   HE1  H N N 277 
MET   HE2  H N N 278 
MET   HE3  H N N 279 
MET   HXT  H N N 280 
PHE   N    N N N 281 
PHE   CA   C N S 282 
PHE   C    C N N 283 
PHE   O    O N N 284 
PHE   CB   C N N 285 
PHE   CG   C Y N 286 
PHE   CD1  C Y N 287 
PHE   CD2  C Y N 288 
PHE   CE1  C Y N 289 
PHE   CE2  C Y N 290 
PHE   CZ   C Y N 291 
PHE   OXT  O N N 292 
PHE   H    H N N 293 
PHE   H2   H N N 294 
PHE   HA   H N N 295 
PHE   HB2  H N N 296 
PHE   HB3  H N N 297 
PHE   HD1  H N N 298 
PHE   HD2  H N N 299 
PHE   HE1  H N N 300 
PHE   HE2  H N N 301 
PHE   HZ   H N N 302 
PHE   HXT  H N N 303 
PRO   N    N N N 304 
PRO   CA   C N S 305 
PRO   C    C N N 306 
PRO   O    O N N 307 
PRO   CB   C N N 308 
PRO   CG   C N N 309 
PRO   CD   C N N 310 
PRO   OXT  O N N 311 
PRO   H    H N N 312 
PRO   HA   H N N 313 
PRO   HB2  H N N 314 
PRO   HB3  H N N 315 
PRO   HG2  H N N 316 
PRO   HG3  H N N 317 
PRO   HD2  H N N 318 
PRO   HD3  H N N 319 
PRO   HXT  H N N 320 
SER   N    N N N 321 
SER   CA   C N S 322 
SER   C    C N N 323 
SER   O    O N N 324 
SER   CB   C N N 325 
SER   OG   O N N 326 
SER   OXT  O N N 327 
SER   H    H N N 328 
SER   H2   H N N 329 
SER   HA   H N N 330 
SER   HB2  H N N 331 
SER   HB3  H N N 332 
SER   HG   H N N 333 
SER   HXT  H N N 334 
SO4   S    S N N 335 
SO4   O1   O N N 336 
SO4   O2   O N N 337 
SO4   O3   O N N 338 
SO4   O4   O N N 339 
THR   N    N N N 340 
THR   CA   C N S 341 
THR   C    C N N 342 
THR   O    O N N 343 
THR   CB   C N R 344 
THR   OG1  O N N 345 
THR   CG2  C N N 346 
THR   OXT  O N N 347 
THR   H    H N N 348 
THR   H2   H N N 349 
THR   HA   H N N 350 
THR   HB   H N N 351 
THR   HG1  H N N 352 
THR   HG21 H N N 353 
THR   HG22 H N N 354 
THR   HG23 H N N 355 
THR   HXT  H N N 356 
TRP   N    N N N 357 
TRP   CA   C N S 358 
TRP   C    C N N 359 
TRP   O    O N N 360 
TRP   CB   C N N 361 
TRP   CG   C Y N 362 
TRP   CD1  C Y N 363 
TRP   CD2  C Y N 364 
TRP   NE1  N Y N 365 
TRP   CE2  C Y N 366 
TRP   CE3  C Y N 367 
TRP   CZ2  C Y N 368 
TRP   CZ3  C Y N 369 
TRP   CH2  C Y N 370 
TRP   OXT  O N N 371 
TRP   H    H N N 372 
TRP   H2   H N N 373 
TRP   HA   H N N 374 
TRP   HB2  H N N 375 
TRP   HB3  H N N 376 
TRP   HD1  H N N 377 
TRP   HE1  H N N 378 
TRP   HE3  H N N 379 
TRP   HZ2  H N N 380 
TRP   HZ3  H N N 381 
TRP   HH2  H N N 382 
TRP   HXT  H N N 383 
TYR   N    N N N 384 
TYR   CA   C N S 385 
TYR   C    C N N 386 
TYR   O    O N N 387 
TYR   CB   C N N 388 
TYR   CG   C Y N 389 
TYR   CD1  C Y N 390 
TYR   CD2  C Y N 391 
TYR   CE1  C Y N 392 
TYR   CE2  C Y N 393 
TYR   CZ   C Y N 394 
TYR   OH   O N N 395 
TYR   OXT  O N N 396 
TYR   H    H N N 397 
TYR   H2   H N N 398 
TYR   HA   H N N 399 
TYR   HB2  H N N 400 
TYR   HB3  H N N 401 
TYR   HD1  H N N 402 
TYR   HD2  H N N 403 
TYR   HE1  H N N 404 
TYR   HE2  H N N 405 
TYR   HH   H N N 406 
TYR   HXT  H N N 407 
VAL   N    N N N 408 
VAL   CA   C N S 409 
VAL   C    C N N 410 
VAL   O    O N N 411 
VAL   CB   C N N 412 
VAL   CG1  C N N 413 
VAL   CG2  C N N 414 
VAL   OXT  O N N 415 
VAL   H    H N N 416 
VAL   H2   H N N 417 
VAL   HA   H N N 418 
VAL   HB   H N N 419 
VAL   HG11 H N N 420 
VAL   HG12 H N N 421 
VAL   HG13 H N N 422 
VAL   HG21 H N N 423 
VAL   HG22 H N N 424 
VAL   HG23 H N N 425 
VAL   HXT  H N N 426 
# 
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 
A1A38 C   N    sing N N 1   
A1A38 N   C1   sing N N 2   
A1A38 C1  O    doub N N 3   
A1A38 C2  C1   sing N N 4   
A1A38 C3  N    sing N N 5   
A1A38 C3  C4   sing Y N 6   
A1A38 C4  C5   doub Y N 7   
A1A38 C5  C6   sing Y N 8   
A1A38 C6  N1   doub Y N 9   
A1A38 N1  C7   sing Y N 10  
A1A38 C7  C3   doub Y N 11  
A1A38 C4  H6   sing N N 12  
A1A38 C5  H7   sing N N 13  
A1A38 C6  H8   sing N N 14  
A1A38 C7  H9   sing N N 15  
A1A38 C2  H4   sing N N 16  
A1A38 C2  H3   sing N N 17  
A1A38 C2  H5   sing N N 18  
A1A38 C   H1   sing N N 19  
A1A38 C   H2   sing N N 20  
A1A38 C   H    sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
CYS   N   CA   sing N N 91  
CYS   N   H    sing N N 92  
CYS   N   H2   sing N N 93  
CYS   CA  C    sing N N 94  
CYS   CA  CB   sing N N 95  
CYS   CA  HA   sing N N 96  
CYS   C   O    doub N N 97  
CYS   C   OXT  sing N N 98  
CYS   CB  SG   sing N N 99  
CYS   CB  HB2  sing N N 100 
CYS   CB  HB3  sing N N 101 
CYS   SG  HG   sing N N 102 
CYS   OXT HXT  sing N N 103 
EDO   C1  O1   sing N N 104 
EDO   C1  C2   sing N N 105 
EDO   C1  H11  sing N N 106 
EDO   C1  H12  sing N N 107 
EDO   O1  HO1  sing N N 108 
EDO   C2  O2   sing N N 109 
EDO   C2  H21  sing N N 110 
EDO   C2  H22  sing N N 111 
EDO   O2  HO2  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
HIS   N   CA   sing N N 159 
HIS   N   H    sing N N 160 
HIS   N   H2   sing N N 161 
HIS   CA  C    sing N N 162 
HIS   CA  CB   sing N N 163 
HIS   CA  HA   sing N N 164 
HIS   C   O    doub N N 165 
HIS   C   OXT  sing N N 166 
HIS   CB  CG   sing N N 167 
HIS   CB  HB2  sing N N 168 
HIS   CB  HB3  sing N N 169 
HIS   CG  ND1  sing Y N 170 
HIS   CG  CD2  doub Y N 171 
HIS   ND1 CE1  doub Y N 172 
HIS   ND1 HD1  sing N N 173 
HIS   CD2 NE2  sing Y N 174 
HIS   CD2 HD2  sing N N 175 
HIS   CE1 NE2  sing Y N 176 
HIS   CE1 HE1  sing N N 177 
HIS   NE2 HE2  sing N N 178 
HIS   OXT HXT  sing N N 179 
HOH   O   H1   sing N N 180 
HOH   O   H2   sing N N 181 
ILE   N   CA   sing N N 182 
ILE   N   H    sing N N 183 
ILE   N   H2   sing N N 184 
ILE   CA  C    sing N N 185 
ILE   CA  CB   sing N N 186 
ILE   CA  HA   sing N N 187 
ILE   C   O    doub N N 188 
ILE   C   OXT  sing N N 189 
ILE   CB  CG1  sing N N 190 
ILE   CB  CG2  sing N N 191 
ILE   CB  HB   sing N N 192 
ILE   CG1 CD1  sing N N 193 
ILE   CG1 HG12 sing N N 194 
ILE   CG1 HG13 sing N N 195 
ILE   CG2 HG21 sing N N 196 
ILE   CG2 HG22 sing N N 197 
ILE   CG2 HG23 sing N N 198 
ILE   CD1 HD11 sing N N 199 
ILE   CD1 HD12 sing N N 200 
ILE   CD1 HD13 sing N N 201 
ILE   OXT HXT  sing N N 202 
LEU   N   CA   sing N N 203 
LEU   N   H    sing N N 204 
LEU   N   H2   sing N N 205 
LEU   CA  C    sing N N 206 
LEU   CA  CB   sing N N 207 
LEU   CA  HA   sing N N 208 
LEU   C   O    doub N N 209 
LEU   C   OXT  sing N N 210 
LEU   CB  CG   sing N N 211 
LEU   CB  HB2  sing N N 212 
LEU   CB  HB3  sing N N 213 
LEU   CG  CD1  sing N N 214 
LEU   CG  CD2  sing N N 215 
LEU   CG  HG   sing N N 216 
LEU   CD1 HD11 sing N N 217 
LEU   CD1 HD12 sing N N 218 
LEU   CD1 HD13 sing N N 219 
LEU   CD2 HD21 sing N N 220 
LEU   CD2 HD22 sing N N 221 
LEU   CD2 HD23 sing N N 222 
LEU   OXT HXT  sing N N 223 
LYS   N   CA   sing N N 224 
LYS   N   H    sing N N 225 
LYS   N   H2   sing N N 226 
LYS   CA  C    sing N N 227 
LYS   CA  CB   sing N N 228 
LYS   CA  HA   sing N N 229 
LYS   C   O    doub N N 230 
LYS   C   OXT  sing N N 231 
LYS   CB  CG   sing N N 232 
LYS   CB  HB2  sing N N 233 
LYS   CB  HB3  sing N N 234 
LYS   CG  CD   sing N N 235 
LYS   CG  HG2  sing N N 236 
LYS   CG  HG3  sing N N 237 
LYS   CD  CE   sing N N 238 
LYS   CD  HD2  sing N N 239 
LYS   CD  HD3  sing N N 240 
LYS   CE  NZ   sing N N 241 
LYS   CE  HE2  sing N N 242 
LYS   CE  HE3  sing N N 243 
LYS   NZ  HZ1  sing N N 244 
LYS   NZ  HZ2  sing N N 245 
LYS   NZ  HZ3  sing N N 246 
LYS   OXT HXT  sing N N 247 
MET   N   CA   sing N N 248 
MET   N   H    sing N N 249 
MET   N   H2   sing N N 250 
MET   CA  C    sing N N 251 
MET   CA  CB   sing N N 252 
MET   CA  HA   sing N N 253 
MET   C   O    doub N N 254 
MET   C   OXT  sing N N 255 
MET   CB  CG   sing N N 256 
MET   CB  HB2  sing N N 257 
MET   CB  HB3  sing N N 258 
MET   CG  SD   sing N N 259 
MET   CG  HG2  sing N N 260 
MET   CG  HG3  sing N N 261 
MET   SD  CE   sing N N 262 
MET   CE  HE1  sing N N 263 
MET   CE  HE2  sing N N 264 
MET   CE  HE3  sing N N 265 
MET   OXT HXT  sing N N 266 
PHE   N   CA   sing N N 267 
PHE   N   H    sing N N 268 
PHE   N   H2   sing N N 269 
PHE   CA  C    sing N N 270 
PHE   CA  CB   sing N N 271 
PHE   CA  HA   sing N N 272 
PHE   C   O    doub N N 273 
PHE   C   OXT  sing N N 274 
PHE   CB  CG   sing N N 275 
PHE   CB  HB2  sing N N 276 
PHE   CB  HB3  sing N N 277 
PHE   CG  CD1  doub Y N 278 
PHE   CG  CD2  sing Y N 279 
PHE   CD1 CE1  sing Y N 280 
PHE   CD1 HD1  sing N N 281 
PHE   CD2 CE2  doub Y N 282 
PHE   CD2 HD2  sing N N 283 
PHE   CE1 CZ   doub Y N 284 
PHE   CE1 HE1  sing N N 285 
PHE   CE2 CZ   sing Y N 286 
PHE   CE2 HE2  sing N N 287 
PHE   CZ  HZ   sing N N 288 
PHE   OXT HXT  sing N N 289 
PRO   N   CA   sing N N 290 
PRO   N   CD   sing N N 291 
PRO   N   H    sing N N 292 
PRO   CA  C    sing N N 293 
PRO   CA  CB   sing N N 294 
PRO   CA  HA   sing N N 295 
PRO   C   O    doub N N 296 
PRO   C   OXT  sing N N 297 
PRO   CB  CG   sing N N 298 
PRO   CB  HB2  sing N N 299 
PRO   CB  HB3  sing N N 300 
PRO   CG  CD   sing N N 301 
PRO   CG  HG2  sing N N 302 
PRO   CG  HG3  sing N N 303 
PRO   CD  HD2  sing N N 304 
PRO   CD  HD3  sing N N 305 
PRO   OXT HXT  sing N N 306 
SER   N   CA   sing N N 307 
SER   N   H    sing N N 308 
SER   N   H2   sing N N 309 
SER   CA  C    sing N N 310 
SER   CA  CB   sing N N 311 
SER   CA  HA   sing N N 312 
SER   C   O    doub N N 313 
SER   C   OXT  sing N N 314 
SER   CB  OG   sing N N 315 
SER   CB  HB2  sing N N 316 
SER   CB  HB3  sing N N 317 
SER   OG  HG   sing N N 318 
SER   OXT HXT  sing N N 319 
SO4   S   O1   doub N N 320 
SO4   S   O2   doub N N 321 
SO4   S   O3   sing N N 322 
SO4   S   O4   sing N N 323 
THR   N   CA   sing N N 324 
THR   N   H    sing N N 325 
THR   N   H2   sing N N 326 
THR   CA  C    sing N N 327 
THR   CA  CB   sing N N 328 
THR   CA  HA   sing N N 329 
THR   C   O    doub N N 330 
THR   C   OXT  sing N N 331 
THR   CB  OG1  sing N N 332 
THR   CB  CG2  sing N N 333 
THR   CB  HB   sing N N 334 
THR   OG1 HG1  sing N N 335 
THR   CG2 HG21 sing N N 336 
THR   CG2 HG22 sing N N 337 
THR   CG2 HG23 sing N N 338 
THR   OXT HXT  sing N N 339 
TRP   N   CA   sing N N 340 
TRP   N   H    sing N N 341 
TRP   N   H2   sing N N 342 
TRP   CA  C    sing N N 343 
TRP   CA  CB   sing N N 344 
TRP   CA  HA   sing N N 345 
TRP   C   O    doub N N 346 
TRP   C   OXT  sing N N 347 
TRP   CB  CG   sing N N 348 
TRP   CB  HB2  sing N N 349 
TRP   CB  HB3  sing N N 350 
TRP   CG  CD1  doub Y N 351 
TRP   CG  CD2  sing Y N 352 
TRP   CD1 NE1  sing Y N 353 
TRP   CD1 HD1  sing N N 354 
TRP   CD2 CE2  doub Y N 355 
TRP   CD2 CE3  sing Y N 356 
TRP   NE1 CE2  sing Y N 357 
TRP   NE1 HE1  sing N N 358 
TRP   CE2 CZ2  sing Y N 359 
TRP   CE3 CZ3  doub Y N 360 
TRP   CE3 HE3  sing N N 361 
TRP   CZ2 CH2  doub Y N 362 
TRP   CZ2 HZ2  sing N N 363 
TRP   CZ3 CH2  sing Y N 364 
TRP   CZ3 HZ3  sing N N 365 
TRP   CH2 HH2  sing N N 366 
TRP   OXT HXT  sing N N 367 
TYR   N   CA   sing N N 368 
TYR   N   H    sing N N 369 
TYR   N   H2   sing N N 370 
TYR   CA  C    sing N N 371 
TYR   CA  CB   sing N N 372 
TYR   CA  HA   sing N N 373 
TYR   C   O    doub N N 374 
TYR   C   OXT  sing N N 375 
TYR   CB  CG   sing N N 376 
TYR   CB  HB2  sing N N 377 
TYR   CB  HB3  sing N N 378 
TYR   CG  CD1  doub Y N 379 
TYR   CG  CD2  sing Y N 380 
TYR   CD1 CE1  sing Y N 381 
TYR   CD1 HD1  sing N N 382 
TYR   CD2 CE2  doub Y N 383 
TYR   CD2 HD2  sing N N 384 
TYR   CE1 CZ   doub Y N 385 
TYR   CE1 HE1  sing N N 386 
TYR   CE2 CZ   sing Y N 387 
TYR   CE2 HE2  sing N N 388 
TYR   CZ  OH   sing N N 389 
TYR   OH  HH   sing N N 390 
TYR   OXT HXT  sing N N 391 
VAL   N   CA   sing N N 392 
VAL   N   H    sing N N 393 
VAL   N   H2   sing N N 394 
VAL   CA  C    sing N N 395 
VAL   CA  CB   sing N N 396 
VAL   CA  HA   sing N N 397 
VAL   C   O    doub N N 398 
VAL   C   OXT  sing N N 399 
VAL   CB  CG1  sing N N 400 
VAL   CB  CG2  sing N N 401 
VAL   CB  HB   sing N N 402 
VAL   CG1 HG11 sing N N 403 
VAL   CG1 HG12 sing N N 404 
VAL   CG1 HG13 sing N N 405 
VAL   CG2 HG21 sing N N 406 
VAL   CG2 HG22 sing N N 407 
VAL   CG2 HG23 sing N N 408 
VAL   OXT HXT  sing N N 409 
# 
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                    7HHE 
_atom_sites.fract_transf_matrix[1][1]   0.024106 
_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]   0.023820 
_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]   0.006330 
_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  ? -0.053  4.602   2.257   1.00 67.14  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -1.059  3.742   1.575   1.00 75.20  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? -0.357  2.672   0.731   1.00 63.15  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 0.761   2.887   0.284   1.00 54.89  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -2.019  4.579   0.719   1.00 82.01  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -3.063  5.387   1.493   1.00 91.00  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -4.194  4.552   2.632   1.00 86.67  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.099  4.457   4.059   1.00 80.23  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.952  1.460   0.568   1.00 60.46  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.425  0.414   -0.325  1.00 54.95  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? -0.132  0.771   -1.789  1.00 54.92  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.819  1.594   -2.398  1.00 45.72  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.556  -0.661  -0.227  1.00 55.20  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -2.073  -0.509  1.189   1.00 59.03  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -2.129  1.002   1.329   1.00 60.53  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 0.904   0.134   -2.343  1.00 47.11  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.139   0.156   -3.774  1.00 45.98  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.499   -1.110  -4.339  1.00 46.88  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? -0.032  -1.917  -3.567  1.00 41.20  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.644   0.244   -4.052  1.00 51.32  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.243   1.565   -3.661  1.00 76.74  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 2.881   2.269   -2.527  1.00 80.22  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.173   2.318   -4.274  1.00 79.60  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.571   3.398   -2.461  1.00 77.10  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.367   3.444   -3.508  1.00 87.42  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.535   -1.255  -5.679  1.00 35.88  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.285   -2.520  -6.352  1.00 34.56  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.409   -3.495  -6.006  1.00 34.61  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.462   -3.074  -5.521  1.00 33.17  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.174   -2.278  -7.832  1.00 33.88  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.150   -4.795  -6.172  1.00 29.04  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.143   -5.826  -5.896  1.00 33.91  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.333   -5.656  -6.850  1.00 38.89  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.165   -5.252  -8.010  1.00 35.86  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.559   -7.252  -5.933  1.00 28.39  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 0.826   -7.669  -4.649  1.00 31.22  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.509   -7.842  -3.435  1.00 26.16  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.561  -7.875  -4.653  1.00 27.13  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 0.832   -8.192  -2.265  1.00 27.59  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -1.239  -8.260  -3.499  1.00 23.93  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.548  -8.424  -2.305  1.00 30.82  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.538   -6.021  -6.383  1.00 34.87  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.703   -5.957  -7.248  1.00 33.31  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.626   -7.149  -6.976  1.00 33.83  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.617   -7.743  -5.907  1.00 31.42  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.421   -4.622  -7.027  1.00 32.69  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.021   -4.560  -5.616  1.00 34.17  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.677   -3.222  -5.304  1.00 39.25  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.414   -3.239  -3.991  1.00 37.99  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.484   -3.214  -2.869  1.00 48.58  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.460   -7.565  -7.951  1.00 31.06  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.366   -8.676  -7.709  1.00 29.47  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.229   -8.383  -6.474  1.00 26.22  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.669   -7.248  -6.232  1.00 27.17  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.164   -8.760  -9.029  1.00 28.54  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.279   -8.080  -10.064 1.00 34.92  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.552   -6.995  -9.306  1.00 31.98  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.436   -9.434  -5.682  1.00 25.13  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.145  -9.400  -4.417  1.00 22.09  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.200   -9.279  -3.219  1.00 29.53  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.608   -9.595  -2.096  1.00 30.45  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 7.963   -8.773  -3.412  1.00 28.22  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.019   -8.690  -2.290  1.00 26.57  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 6.789   -10.063 -1.654  1.00 26.08  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.681   -11.059 -2.360  1.00 26.51  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.687   -8.068  -2.695  1.00 26.25  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.719   -6.560  -2.927  1.00 29.12  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.688   -5.919  -2.463  1.00 27.24  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.806   -6.024  -3.601  1.00 31.51  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.609   -10.100 -0.319  1.00 24.29  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.498   -11.374 0.383   1.00 26.16  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.055   -11.506 0.851   1.00 25.56  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.466   -10.528 1.309   1.00 29.12  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.452   -11.455 1.581   1.00 24.23  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 8.941   -11.174 1.323   1.00 23.97  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 9.711   -11.243 2.642   1.00 23.06  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.456   -12.231 0.388   1.00 24.05  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.503   -12.716 0.776   1.00 23.27  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.065   -12.843 0.972   1.00 24.60  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 2.785   -14.193 1.601   1.00 25.17  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.662   -15.056 1.630   1.00 27.77  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.307   -12.733 -0.378  1.00 23.58  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.494   -11.368 -1.020  1.00 23.48  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.724   -13.838 -1.340  1.00 23.15  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.539   -14.367 2.042   1.00 24.24  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 0.937   -15.687 2.169   1.00 22.64  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.003   -15.803 0.983   1.00 24.67  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.778  -14.882 0.727   1.00 24.45  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.130   -15.923 3.467   1.00 22.88  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.073   -16.060 4.663   1.00 22.72  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.500   -14.942 5.367   1.00 25.17  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.573   -17.292 5.029   1.00 23.91  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.389   -15.058 6.411   1.00 28.13  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.462   -17.418 6.085   1.00 30.98  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 2.866   -16.309 6.777   1.00 32.26  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.106   -16.928 0.270   1.00 26.63  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.656  -17.109 -0.958  1.00 29.84  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.660  -18.231 -0.722  1.00 30.39  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -1.310  -19.280 -0.159  1.00 33.24  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.258   -17.389 -2.152  1.00 25.51  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.912  -17.979 -1.112  1.00 32.24  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.971  -18.930 -0.818  1.00 31.15  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -4.411  -19.603 -2.115  1.00 33.40  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.847  -18.923 -3.040  1.00 33.93  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -5.192  -18.278 -0.148  1.00 32.40  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -6.313  -19.259 0.186   1.00 36.01  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.954  -20.185 1.344   1.00 40.45  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -7.068  -21.069 1.787   1.00 36.57  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -7.401  -22.105 0.807   1.00 35.13  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -4.324  -20.944 -2.138  1.00 30.90  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.994  -21.736 -3.161  1.00 38.14  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -6.021  -22.683 -2.526  1.00 33.76  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.834  -23.116 -1.388  1.00 34.28  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.967  -22.511 -3.989  1.00 34.17  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -3.058  -21.542 -4.752  1.00 40.98  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.858  -22.276 -5.874  1.00 39.87  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -3.001  -22.874 -7.136  1.00 45.69  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -7.111  -22.935 -3.272  1.00 40.65  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -8.165  -23.899 -2.963  1.00 42.86  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -7.521  -25.187 -2.468  1.00 42.98  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -6.668  -25.761 -3.144  1.00 41.65  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.988  -24.275 -4.210  1.00 50.02  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -10.513 -24.160 -4.034  1.00 56.82  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -11.297 -23.330 -5.051  1.00 52.75  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.860  -25.576 -1.244  1.00 35.19  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -7.429  -26.875 -0.773  1.00 35.42  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -6.131  -26.792 0.014   1.00 38.21  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.702  -27.794 0.550   1.00 44.50  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -5.480  -25.621 0.076   1.00 37.96  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -4.217  -25.544 0.803   1.00 34.82  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -4.330  -24.405 1.792   1.00 34.37  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -5.086  -23.460 1.543   1.00 37.73  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.961  -25.369 -0.066  1.00 41.96  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.905  -26.425 -1.160  1.00 41.64  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -2.251  -27.639 -0.981  1.00 42.96  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -3.611  -26.230 -2.345  1.00 53.87  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -2.277  -28.608 -1.973  1.00 52.75  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -3.621  -27.177 -3.357  1.00 56.44  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -2.965  -28.381 -3.164  1.00 59.81  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -3.037  -29.288 -4.199  1.00 56.76  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -3.590  -24.462 2.920   1.00 30.87  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -3.525  -23.327 3.851   1.00 33.67  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.818  -22.125 3.198   1.00 37.58  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -2.074  -22.289 2.223   1.00 33.13  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.751  -23.903 5.073   1.00 33.00  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.912  -25.065 4.502   1.00 32.32  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.728  -25.588 3.312   1.00 35.24  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -3.069  -20.918 3.722   1.00 29.87  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -2.302  -19.734 3.352   1.00 32.89  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.803  -20.069 3.375   1.00 38.55  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? -0.284  -20.520 4.404   1.00 34.09  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.714  -18.537 4.227   1.00 29.21  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -4.189  -18.247 4.118   1.00 37.98  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -5.185  -18.904 4.835   1.00 32.80  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.824  -17.336 3.334   1.00 35.01  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -6.376  -18.419 4.467   1.00 35.92  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -6.190  -17.456 3.572   1.00 36.56  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? -0.085  -19.813 2.260   1.00 33.03  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.230   -20.438 2.133   1.00 31.26  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.320   -19.386 1.939   1.00 31.72  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.127   -18.482 1.134   1.00 27.84  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.228   -21.441 0.967   1.00 33.45  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.296   -22.494 1.070   1.00 34.86  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 3.634   -22.300 0.888   1.00 35.98  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.126   -23.900 1.376   1.00 34.39  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.310   -23.481 1.045   1.00 36.13  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.416   -24.481 1.356   1.00 38.16  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.033   -24.725 1.666   1.00 39.89  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 3.632   -25.844 1.611   1.00 38.23  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.250   -26.072 1.896   1.00 42.06  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.537   -26.631 1.881   1.00 35.21  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.486   -19.473 2.641   1.00 27.81  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.563   -18.501 2.456   1.00 27.87  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.088   -18.557 1.019   1.00 27.90  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.307   -19.646 0.466   1.00 26.71  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.648   -18.893 3.511   1.00 27.19  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.358   -20.369 3.783   1.00 28.76  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 3.837   -20.521 3.614   1.00 27.51  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.271   -17.366 0.446   1.00 25.21  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.461   -17.174 -0.990  1.00 25.02  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.005   -15.765 -1.316  1.00 27.42  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.059   -14.869 -0.468  1.00 25.50  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.150   -17.482 -1.686  1.00 21.77  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.537   -15.595 -2.540  1.00 27.80  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 6.969   -14.287 -2.987  1.00 28.08  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.387   -14.036 -4.380  1.00 27.33  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.074   -14.974 -5.107  1.00 28.79  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.498   -14.215 -2.892  1.00 25.48  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.174   -15.137 -3.900  1.00 23.65  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 10.684  -14.918 -3.842  1.00 25.52  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.408  -15.797 -4.773  1.00 23.92  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 12.684  -16.175 -4.688  1.00 26.02  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.416  -15.964 -3.614  1.00 24.26  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.223  -16.847 -5.674  1.00 28.03  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.192   -12.763 -4.730  1.00 28.76  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.002   -12.400 -6.128  1.00 28.97  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.352   -12.551 -6.829  1.00 31.61  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.331   -11.894 -6.444  1.00 29.30  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.525   -10.948 -6.277  1.00 27.95  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.368   -10.578 -5.330  1.00 30.01  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.215   -10.639 -7.737  1.00 24.91  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.051   -11.180 -5.680  1.00 30.50  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.400   -13.450 -7.813  1.00 29.37  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 8.608   -13.654 -8.601  1.00 32.45  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 8.751   -12.632 -9.729  1.00 35.90  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 7.770   -12.056 -10.189 1.00 27.83  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 8.693   -15.064 -9.155  1.00 29.26  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 9.718   -15.934 -8.449  1.00 33.87  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.343  -15.436 -7.489  1.00 35.96  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 9.898   -17.091 -8.870  1.00 35.69  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.004  -12.407 -10.169 1.00 37.87  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.266  -11.798 -11.466 1.00 41.40  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.014  -12.815 -12.574 1.00 36.73  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.095  -14.013 -12.351 1.00 36.81  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 11.740  -11.443 -11.619 1.00 53.52  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.244  -10.242 -10.816 1.00 65.59  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 11.941  -9.080  -11.212 1.00 60.67  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 12.951  -10.467 -9.799  1.00 67.60  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 9.763   -12.339 -13.791 1.00 37.45  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 9.870   -13.203 -14.961 1.00 37.22  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.255  -13.043 -15.589 1.00 39.24  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.644  -11.921 -15.918 1.00 38.28  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 8.781   -12.792 -15.953 1.00 39.66  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.414   -12.747 -15.219 1.00 38.58  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.794   -13.727 -17.173 1.00 32.21  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.601   -11.489 -15.504 1.00 40.39  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.012  -14.146 -15.715 1.00 38.78  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.293  -14.093 -16.413 1.00 38.53  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.097  -13.721 -17.889 1.00 41.38  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.095  -14.046 -18.533 1.00 37.52  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.046  -15.400 -16.269 1.00 37.63  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.055  -12.956 -18.406 1.00 45.45  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.137  -12.719 -19.838 1.00 39.74  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 13.983  -14.048 -20.558 1.00 31.38  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.671  -14.989 -20.221 1.00 33.23  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.493  -12.136 -20.175 1.00 40.35  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.588  -10.636 -19.968 1.00 42.57  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.531  -9.975  -19.887 1.00 44.48  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.719  -10.145 -19.915 1.00 49.39  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.005  -14.136 -21.461 1.00 34.49  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 12.840  -15.307 -22.310 1.00 36.86  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 11.943  -16.383 -21.712 1.00 37.10  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.686  -17.393 -22.367 1.00 39.23  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.457  -16.149 -20.488 1.00 36.45  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.614  -17.095 -19.755 1.00 37.86  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.135   -16.824 -20.023 1.00 36.05  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.744   -15.723 -20.420 1.00 35.58  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 10.921  -16.982 -18.274 1.00 40.17  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.300   -17.831 -19.751 1.00 42.16  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 6.861   -17.739 -19.959 1.00 37.54  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.259   -16.709 -19.007 1.00 35.60  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.476   -16.787 -17.799 1.00 36.72  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.265   -19.134 -19.699 1.00 42.40  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 4.749   -19.131 -19.838 1.00 42.53  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 6.874   -20.184 -20.617 1.00 44.58  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.498   -15.766 -19.571 1.00 33.72  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.820   -14.713 -18.834 1.00 37.83  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.508   -15.269 -18.292 1.00 45.99  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 2.985   -16.235 -18.837 1.00 45.15  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.413   -13.518 -19.709 1.00 34.76  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.561   -12.639 -20.174 1.00 39.29  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.139   -11.506 -21.097 1.00 41.55  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.159   -11.889 -22.545 1.00 43.36  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 4.770   -10.697 -23.285 1.00 41.30  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 2.945   -14.681 -17.210 1.00 45.50  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.652   -15.112 -16.698 1.00 41.83  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.553   -14.479 -17.545 1.00 41.72  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.842   -13.579 -18.327 1.00 37.72  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.668   -14.590 -15.247 1.00 46.29  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.588   -13.391 -15.248 1.00 50.36  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.552   -13.612 -16.400 1.00 49.08  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.722  -14.918 -17.400 1.00 38.48  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.875  -14.208 -17.945 1.00 39.57  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.982  -12.809 -17.379 1.00 43.02  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.428  -12.526 -16.313 1.00 43.09  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -3.057  -15.047 -17.458 1.00 39.18  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.482  -16.432 -17.334 1.00 38.97  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -1.129  -16.153 -16.714 1.00 42.65  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.755  -11.928 -18.054 1.00 45.93  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.975  -10.569 -17.567 1.00 48.28  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.725  -10.698 -16.245 1.00 42.81  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.436  -11.672 -15.985 1.00 47.97  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.851  -9.963  -18.672 1.00 53.50  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.609  -11.153 -19.224 1.00 47.20  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.520  -12.222 -19.280 1.00 53.00  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.469  -9.736  -15.379 1.00 41.99  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -4.058  -9.692  -14.056 1.00 49.27  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.477  -10.756 -13.127 1.00 42.19  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.927  -10.841 -11.992 1.00 44.49  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.568  -9.468  -14.126 1.00 53.49  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.861  -8.142  -14.798 1.00 61.95  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.772  -7.087  -14.154 1.00 54.38  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.160  -8.169  -16.091 1.00 57.36  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.472  -11.536 -13.563 1.00 35.53  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.937  -12.566 -12.674 1.00 35.30  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.450  -12.319 -12.411 1.00 36.00  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.231   -11.751 -13.268 1.00 35.52  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -2.219  -14.013 -13.106 1.00 33.20  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.692  -14.364 -13.359 1.00 37.18  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.565  -14.228 -12.110 1.00 41.83  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -6.041  -14.414 -12.373 1.00 40.79  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -6.065  -15.857 -12.629 1.00 43.63  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.029   -12.754 -11.230 1.00 28.75  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.434   -12.632 -10.867 1.00 29.23  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.060   -14.010 -10.767 1.00 29.04  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.387   -14.969 -10.378 1.00 29.49  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.610   -12.002 -9.486  1.00 32.42  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.100   -10.576 -9.459  1.00 32.78  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.263  -10.291 -9.342  1.00 34.27  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 1.984   -9.529  -9.655  1.00 32.50  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.718  -8.980  -9.371  1.00 32.34  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.540   -8.218  -9.679  1.00 37.67  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.191   -7.948  -9.536  1.00 37.95  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.162  -6.625  -9.556  1.00 43.62  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.370   -14.151 -11.084 1.00 25.89  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.084   -15.408 -10.836 1.00 25.07  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.353   -15.559 -9.334  1.00 24.86  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 4.978   -14.710 -8.699  1.00 30.18  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.370   -15.337 -11.679 1.00 23.64  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.541   -13.861 -11.943 1.00 24.27  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.233   -13.096 -11.624 1.00 29.76  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 3.818   -16.618 -8.741  1.00 23.15  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 3.971   -16.770 -7.313  1.00 23.84  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 4.903   -17.942 -7.053  1.00 25.85  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 4.618   -19.074 -7.430  1.00 27.91  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 2.624   -16.920 -6.582  1.00 24.60  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 1.618   -15.752 -6.894  1.00 22.69  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 2.837   -17.158 -5.076  1.00 22.34  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.084   -14.354 -6.504  1.00 22.16  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.005   -17.659 -6.366  1.00 24.67  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 6.883   -18.736 -5.931  1.00 25.61  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.546   -19.047 -4.475  1.00 24.89  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 6.605   -18.163 -3.622  1.00 26.19  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.352   -18.333 -6.133  1.00 25.03  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.363   -19.373 -5.664  1.00 26.51  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 9.758   -20.410 -6.509  1.00 26.75  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 9.916   -19.306 -4.390  1.00 26.49  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 10.701  -21.335 -6.089  1.00 28.57  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 10.842  -20.259 -3.962  1.00 30.26  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.246  -21.257 -4.829  1.00 29.42  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.217   -20.314 -4.218  1.00 27.11  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 5.829   -20.811 -2.911  1.00 26.62  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.088   -21.365 -2.260  1.00 27.26  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 7.732   -22.244 -2.832  1.00 28.39  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 4.810   -21.952 -3.114  1.00 28.61  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.427   -21.488 -3.574  1.00 34.16  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.143   -21.282 -4.929  1.00 34.59  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 2.416   -21.261 -2.641  1.00 31.92  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 1.902   -20.789 -5.342  1.00 34.58  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.163   -20.820 -3.060  1.00 33.66  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 0.918   -20.564 -4.395  1.00 32.90  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.423   -20.841 -1.081  1.00 27.15  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 8.540   -21.327 -0.290  1.00 30.99  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.267   -22.776 0.132   1.00 29.07  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.107   -23.236 0.174   1.00 25.93  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 8.880   -20.355 0.849   1.00 27.09  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.341   -18.983 0.373   1.00 27.96  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 10.579  -18.806 -0.250  1.00 29.11  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 8.571   -17.848 0.614   1.00 25.93  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 10.995  -17.536 -0.664  1.00 27.23  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.010   -16.579 0.213   1.00 27.24  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.225  -16.412 -0.432  1.00 25.14  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.361   -23.527 0.290   1.00 25.14  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.245   -24.889 0.797   1.00 33.04  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 8.985   -25.926 -0.292  1.00 35.88  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 9.772   -26.861 -0.434  1.00 35.19  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 7.906   -25.747 -1.071  1.00 34.94  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 7.626   -26.679 -2.153  1.00 32.89  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 8.430   -26.295 -3.394  1.00 33.53  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 8.710   -27.136 -4.255  1.00 38.83  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.129   -26.733 -2.442  1.00 33.78  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 5.825   -25.379 -2.763  1.00 32.95  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.347   -27.261 -1.259  1.00 36.98  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 8.748   -25.002 -3.496  1.00 30.74  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 9.428   -24.395 -4.631  1.00 29.64  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 8.615   -24.496 -5.911  1.00 30.37  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.203   -24.378 -6.984  1.00 34.87  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 10.882  -24.853 -4.818  1.00 27.34  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 11.646  -24.822 -3.546  1.00 27.82  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 12.287  -25.926 -3.044  1.00 29.48  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 11.738  -23.859 -2.601  1.00 27.92  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 12.809  -25.624 -1.857  1.00 30.87  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 12.505  -24.364 -1.586  1.00 33.82  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.283   -24.554 -5.808  1.00 33.28  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 6.442   -24.582 -7.005  1.00 31.60  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 5.946   -23.183 -7.349  1.00 31.29  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 5.989   -22.309 -6.490  1.00 31.36  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.236   -25.479 -6.743  1.00 33.21  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 5.689   -26.906 -6.470  1.00 38.34  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 4.553   -27.822 -6.108  1.00 46.62  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.361   -27.459 -6.286  1.00 50.78  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 4.914   -28.885 -5.576  1.00 46.59  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 5.541   -22.975 -8.615  1.00 29.28  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 4.997   -21.693 -9.060  1.00 35.79  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 3.516   -21.852 -9.397  1.00 37.81  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.110   -22.877 -9.920  1.00 37.88  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 5.774   -21.129 -10.255 1.00 36.56  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.068   -20.752 -9.774  1.00 34.90  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.169   -19.845 -10.810 1.00 33.72  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 2.711   -20.827 -9.107  1.00 33.66  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.417   -20.720 -9.762  1.00 30.38  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.192   -19.251 -10.088 1.00 32.10  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 1.977   -18.414 -9.653  1.00 27.79  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.299   -21.313 -8.922  1.00 27.43  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.189   -18.976 -10.934 1.00 28.49  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? -0.206  -17.613 -11.273 1.00 29.35  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.488  -17.278 -10.514 1.00 34.28  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.493  -17.956 -10.698 1.00 35.98  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.490  -17.626 -12.775 1.00 30.20  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 0.691   -17.998 -13.665 1.00 36.91  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 1.919   -17.347 -13.547 1.00 42.98  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 0.566   -18.993 -14.635 1.00 37.18  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 2.989   -17.685 -14.381 1.00 51.13  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 1.631   -19.313 -15.476 1.00 44.74  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 2.848   -18.673 -15.343 1.00 40.33  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -1.447  -16.238 -9.668  1.00 30.47  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.581  -15.843 -8.848  1.00 33.58  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.801  -14.334 -8.943  1.00 34.62  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.854  -13.582 -9.228  1.00 31.81  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -2.249  -16.223 -7.407  1.00 31.95  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.958  -17.698 -7.159  1.00 31.97  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.710  -17.795 -5.661  1.00 32.84  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.277  -18.349 -7.495  1.00 34.36  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -4.065  -13.926 -8.712  1.00 27.31  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -4.430  -12.522 -8.621  1.00 26.91  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -4.363  -12.034 -7.170  1.00 26.92  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -4.253  -12.826 -6.225  1.00 30.30  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.403  -10.712 -6.959  1.00 29.14  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.373  -10.135 -5.609  1.00 28.65  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.326  -10.689 -4.546  1.00 26.95  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.986  -10.717 -3.361  1.00 27.76  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.589  -8.662  -5.896  1.00 26.58  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.928  -8.492  -7.243  1.00 28.05  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.384  -9.701  -8.032  1.00 27.42  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.500  -11.168 -4.965  1.00 28.29  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.444  -11.689 -3.992  1.00 31.88  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.859  -12.858 -3.193  1.00 30.03  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.380  -13.197 -2.130  1.00 29.06  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.725  -12.207 -4.652  1.00 34.94  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.550  -13.474 -5.457  1.00 35.86  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.797  -13.678 -6.328  1.00 45.31  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.703  -14.915 -7.144  1.00 50.21  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.405  -16.086 -6.299  1.00 62.13  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.819  -13.504 -3.719  1.00 26.01  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -5.277  -14.686 -3.089  1.00 27.35  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.960  -14.383 -2.371  1.00 28.54  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -3.297  -15.310 -1.864  1.00 30.57  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -5.119  -15.807 -4.111  1.00 29.49  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.461  -16.407 -4.454  1.00 34.65  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.233  -16.570 -3.484  1.00 33.32  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.747  -16.579 -5.654  1.00 30.68  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.603  -13.098 -2.330  1.00 26.02  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -2.268  -12.660 -1.905  1.00 24.72  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.400  -11.791 -0.652  1.00 21.91  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.971  -10.724 -0.719  1.00 24.37  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.612  -11.876 -3.054  1.00 24.02  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.395  -12.631 -4.369  1.00 24.52  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.613  -11.871 -5.403  1.00 25.62  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.765  -14.015 -4.149  1.00 24.61  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.845  -12.241 0.475   1.00 25.20  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.906  -11.551 1.755   1.00 28.34  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.492  -11.137 2.156   1.00 27.04  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.400   -11.984 2.372   1.00 25.96  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.457  -12.539 2.790   1.00 26.66  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.881  -13.007 2.517   1.00 29.73  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -4.152  -13.932 1.506   1.00 27.33  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.951  -12.524 3.286   1.00 31.15  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.456  -14.388 1.297   1.00 36.31  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -6.258  -12.959 3.050   1.00 33.85  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.514  -13.900 2.061   1.00 29.68  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? -0.234  -9.819  2.217   1.00 28.86  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.095   -9.315  2.597   1.00 29.91  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.633   -9.912  3.897   1.00 28.40  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 0.912   -10.005 4.896   1.00 30.01  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 0.836   -7.795  2.760   1.00 29.92  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? -0.289  -7.531  1.768   1.00 32.32  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -1.206  -8.742  1.932   1.00 31.73  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 2.928   -10.252 3.873   1.00 29.30  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.526   -11.158 4.832   1.00 29.69  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.530   -10.528 6.224   1.00 32.79  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.136   -11.197 7.186   1.00 31.60  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 4.937   -11.553 4.392   1.00 30.32  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.676   -12.348 5.456   1.00 29.30  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.345   -13.684 5.704   1.00 29.95  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 6.735   -11.793 6.169   1.00 29.25  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.040   -14.454 6.626   1.00 30.37  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.412   -12.547 7.124   1.00 29.62  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.063   -13.871 7.360   1.00 33.47  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 7.714   -14.629 8.309   1.00 39.27  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 3.987   -9.265  6.293   1.00 31.30  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.166   -8.551  7.554   1.00 43.70  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 2.869   -8.553  8.361   1.00 40.28  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.813   -9.066  9.473   1.00 41.71  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 4.889   -7.229  7.340   1.00 42.32  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.413   -7.378  7.297   1.00 65.20  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 7.017   -7.960  8.257   1.00 69.41  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 7.013   -6.912  6.312   1.00 69.56  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 1.804   -8.078  7.722   1.00 41.97  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.461   -8.002  8.280   1.00 39.97  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? -0.104  -9.373  8.665   1.00 38.66  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.913  -9.449  9.582   1.00 40.13  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.430  -7.239  7.287   1.00 36.83  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.895  -7.204  7.651   1.00 44.71  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.678  -6.533  6.541   1.00 38.82  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.718  -5.689  7.178   1.00 47.45  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.756  -6.501  7.799   1.00 45.61  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.304   -10.459 7.989   1.00 36.72  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.443  -11.705 8.115   1.00 35.09  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.348   -12.763 8.870   1.00 38.90  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? -0.179  -13.851 9.106   1.00 35.15  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.829  -12.253 6.739   1.00 37.55  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.596  -11.287 6.035   1.00 44.15  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.612   -12.464 9.215   1.00 40.35  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.454   -13.516 9.768   1.00 40.57  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 1.876   -14.046 11.079  1.00 44.23  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 1.946   -15.253 11.336  1.00 47.15  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 3.961   -13.233 9.861   1.00 40.21  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.378   -12.004 10.617  1.00 48.83  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 5.870   -12.099 10.889  1.00 57.67  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.421   -10.758 11.260  1.00 68.64  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.524   -9.868  10.095  1.00 70.24  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.288   -13.162 11.895  0.50 44.25  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.322   -13.140 11.893  0.50 45.29  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 0.776   -13.578 13.197  0.50 42.53  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 0.746   -13.528 13.171  0.50 44.75  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? -0.407  -14.537 13.042  0.50 41.40  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? -0.324  -14.595 12.957  0.50 42.80  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.570  -15.459 13.828  0.50 39.91  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? -0.325  -15.627 13.615  0.50 41.11  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.573   -12.398 14.135  0.50 45.77  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.151   -12.346 13.912  0.50 49.81  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 1.843   -11.815 14.743  0.50 47.99  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? -0.520  -12.730 15.220  0.50 53.27  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 2.945   -12.344 14.457  0.50 40.14  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.223   -13.020 16.184  0.50 50.83  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.722   -10.826 15.498  0.50 55.23  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.770  -12.795 15.236  0.50 55.26  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -1.225  -14.348 12.006  1.00 42.86  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -2.286  -15.293 11.730  1.00 42.07  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.730  -16.574 11.098  1.00 41.19  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -2.177  -17.661 11.432  1.00 37.02  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -3.308  -14.574 10.852  1.00 44.04  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.567  -15.397 10.622  1.00 49.14  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.718  -14.464 10.250  1.00 49.40  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -7.004  -15.170 10.019  1.00 50.90  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.969  -14.254 9.404   1.00 62.35  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.782  -16.466 10.156  1.00 38.59  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.653  -17.549 9.178   1.00 37.78  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 0.681   -18.277 9.330   1.00 37.23  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 0.819   -19.400 8.834   1.00 37.27  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.844  -17.121 7.715   1.00 38.06  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -2.256  -16.677 7.362   1.00 41.81  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -3.376  -17.417 7.766   1.00 39.38  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -2.473  -15.531 6.585   1.00 43.72  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.664  -17.017 7.418   1.00 40.40  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.758  -15.127 6.230   1.00 39.99  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.852  -15.870 6.655   1.00 40.83  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -6.101  -15.470 6.302   1.00 40.85  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 1.624   -17.632 10.026  1.00 33.83  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 2.992   -18.115 10.106  1.00 36.53  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.171   -19.088 11.273  1.00 43.32  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 3.951   -18.849 12.175  1.00 45.69  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.436   -20.197 11.247  1.00 44.35  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 2.516   -21.151 12.332  1.00 47.61  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 2.774   -22.505 11.693  1.00 45.49  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 2.301   -22.750 10.594  1.00 42.87  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.228   -21.126 13.167  1.00 47.52  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.014   -19.830 13.956  1.00 48.85  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? -0.017  -19.917 15.079  1.00 54.05  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 3.559   -23.397 12.330  1.00 43.65  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 3.817   -24.728 11.779  1.00 42.36  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 2.559   -25.375 11.233  1.00 39.50  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 1.473   -25.111 11.719  1.00 45.53  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 4.368   -25.478 12.986  1.00 44.68  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.123   -24.411 13.741  1.00 47.00  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.289   -23.134 13.578  1.00 44.32  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 2.744   -26.218 10.220  1.00 42.02  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 1.662   -26.888 9.526   1.00 46.56  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.169   -28.250 9.057   1.00 51.88  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 3.339   -28.396 8.687   1.00 53.87  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.145   -26.009 8.395   1.00 48.80  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? -0.102  -26.557 7.751   1.00 51.13  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? -0.034  -27.486 6.938   1.00 51.61  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -1.244  -25.971 8.074   1.00 56.68  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 1.255   -29.226 9.031   1.00 49.30  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 1.592   -30.619 8.784   1.00 54.10  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.031   -30.796 7.331   1.00 50.63  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 2.833   -31.673 7.028   1.00 52.09  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 0.477   -31.571 9.259   1.00 56.62  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? -0.832  -31.590 8.443   1.00 62.01  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 1.544   -29.929 6.442   1.00 45.07  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 1.684   -30.147 5.004   1.00 46.37  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.149   -30.136 4.541   1.00 43.46  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 3.969   -29.363 5.040   1.00 37.21  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 0.761   -29.202 4.221   1.00 44.65  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? -0.720  -29.332 4.544   1.00 46.93  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -1.255  -30.514 3.786   1.00 46.88  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -2.111  -30.051 2.695   1.00 66.58  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -3.235  -29.352 2.869   1.00 70.60  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -4.009  -29.097 1.825   1.00 63.19  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.596  -28.942 4.082   1.00 72.90  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 3.441   -30.980 3.538   1.00 40.66  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 4.780   -31.167 3.000   1.00 44.03  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 5.345   -29.827 2.535   1.00 39.89  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 4.759   -29.150 1.693   1.00 35.14  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 4.767   -32.150 1.826   1.00 42.93  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.078   -32.396 1.062   1.00 47.96  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 5.861   -33.547 0.080   1.00 53.45  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 7.024   -33.876 -0.812  1.00 61.02  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 6.508   -29.468 3.081   1.00 38.29  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.243   -28.310 2.603   1.00 36.58  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 6.844   -27.025 3.341   1.00 36.00  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 7.549   -26.030 3.259   1.00 37.79  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 5.757   -27.060 4.119   1.00 33.08  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 5.274   -25.843 4.744   1.00 33.93  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 6.315   -25.240 5.690   1.00 34.35  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 6.545   -24.018 5.716   1.00 31.30  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 3.997   -26.128 5.526   1.00 32.83  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.263   -24.840 5.862   1.00 34.06  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 3.569   -24.138 7.022   1.00 32.97  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 2.281   -24.337 5.009   1.00 29.19  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 2.936   -22.936 7.314   1.00 33.03  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 1.644   -23.145 5.315   1.00 27.50  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 1.958   -22.462 6.466   1.00 28.02  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 6.904   -26.089 6.523   1.00 31.36  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 7.744   -25.558 7.595   1.00 30.47  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.101   -25.097 7.037   1.00 31.42  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 9.704   -24.111 7.501   1.00 29.41  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 7.872   -26.560 8.736   1.00 36.18  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 6.559   -26.848 9.451   1.00 42.54  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 5.638   -26.018 9.463   1.00 35.54  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 6.467   -28.013 10.087  1.00 35.31  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 9.590   -25.831 6.037   1.00 29.38  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 10.712  -25.341 5.250   1.00 31.79  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 10.403  -23.946 4.711   1.00 31.26  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.244  -23.033 4.748   1.00 28.72  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.013  -26.257 4.068   1.00 33.62  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 12.356  -25.911 3.432   1.00 40.85  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 12.980  -26.901 2.482   1.00 47.61  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 12.518  -28.051 2.434   1.00 48.27  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 13.947  -26.508 1.813   1.00 45.98  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.190   -23.819 4.173   1.00 32.83  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 8.702   -22.574 3.611   1.00 32.23  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 8.782   -21.442 4.628   1.00 30.13  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.179   -20.332 4.286   1.00 27.79  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 8.467   -21.739 5.892   1.00 31.19  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 8.475   -20.688 6.906   1.00 30.08  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 9.898   -20.235 7.179   1.00 29.44  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.129  -19.041 7.418   1.00 25.66  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 7.766   -20.983 8.231   1.00 28.78  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.292   -21.367 8.095   1.00 33.18  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 5.867   -22.016 9.428   1.00 36.98  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 5.435   -20.160 7.792   1.00 31.95  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 10.819  -21.204 7.216   1.00 29.07  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.216  -20.864 7.427   1.00 32.12  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 12.692  -19.952 6.281   1.00 30.81  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 13.309  -18.897 6.509   1.00 29.82  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.079  -22.128 7.631   1.00 31.24  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 14.538  -21.800 7.812   1.00 31.55  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.196  -21.639 8.999   1.00 33.44  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 15.493  -21.498 6.774   1.00 30.61  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 16.496  -21.282 8.782   1.00 31.21  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 16.705  -21.186 7.428   1.00 29.89  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 15.443  -21.480 5.371   1.00 27.85  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 17.857  -20.853 6.724   1.00 28.06  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 16.583  -21.164 4.671   1.00 32.64  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 17.772  -20.833 5.352   1.00 29.97  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 12.290  -20.276 5.045   1.00 28.56  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 12.818  -19.551 3.887   1.00 24.97  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 12.292  -18.116 3.863   1.00 27.36  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.055  -17.160 3.636   1.00 24.28  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 12.478  -20.254 2.584   1.00 24.25  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.240  -21.554 2.345   1.00 26.08  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 12.739  -22.354 1.139   1.00 29.93  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 11.719  -21.963 0.498   1.00 25.64  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 13.361  -23.422 0.847   1.00 33.21  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 10.985  -17.944 4.111   1.00 29.60  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 10.422  -16.609 4.001   1.00 25.90  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.020  -15.742 5.117   1.00 31.90  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.249  -14.538 4.932   1.00 29.01  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 8.882   -16.622 3.998   1.00 26.28  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.296   -15.254 3.552   1.00 24.08  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 8.363   -17.037 5.388   1.00 25.62  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 6.836   -15.258 3.095   1.00 24.52  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.329  -16.365 6.267   1.00 30.59  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 11.837  -15.604 7.400   1.00 30.66  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 13.340  -15.378 7.277   1.00 29.39  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 13.792  -14.339 7.710   1.00 36.60  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 11.422  -16.211 8.743   1.00 29.66  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 11.869  -15.428 9.978   1.00 41.68  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.353  -15.975 11.306  1.00 50.26  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 11.177  -17.190 11.492  1.00 50.16  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.085  -15.079 12.251  1.00 44.73  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.096  -16.328 6.706   1.00 28.03  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 15.552  -16.368 6.815   1.00 27.93  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.262  -15.972 5.516   1.00 31.22  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 17.334  -15.347 5.558   1.00 31.55  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.007  -17.656 7.498   1.00 29.82  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 15.485  -17.673 8.927   1.00 34.38  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 15.845  -16.794 9.707   1.00 34.75  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 14.553  -18.542 9.282   1.00 31.59  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 15.690  -16.286 4.338   1.00 27.38  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 16.387  -15.866 3.120   1.00 29.36  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 15.381  -15.792 1.982   1.00 28.97  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 15.404  -16.617 1.061   1.00 26.92  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 17.571  -16.771 2.771   1.00 31.55  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 18.586  -16.157 1.832   1.00 34.11  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 18.374  -15.095 1.228   1.00 28.73  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 19.736  -16.811 1.717   1.00 39.12  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 14.431  -14.829 2.048   1.00 29.14  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.300  -14.852 1.126   1.00 28.08  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 13.642  -14.426 -0.303  1.00 27.37  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 12.815  -14.609 -1.168  1.00 31.03  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.288  -13.933 1.805   1.00 22.79  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.151  -12.943 2.553   1.00 27.64  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.379  -13.717 3.017   1.00 27.16  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 14.826  -13.852 -0.538  1.00 25.66  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.180  -13.316 -1.843  1.00 29.86  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.238  -14.163 -2.559  1.00 31.26  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 16.788  -13.741 -3.584  1.00 28.64  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 15.545  -11.837 -1.703  1.00 28.89  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 14.441  -11.019 -1.077  1.00 28.96  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.172  -10.895 -1.611  1.00 26.54  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 14.464  -10.222 0.013   1.00 26.29  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 12.449  -10.063 -0.855  1.00 25.27  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.220  -9.621  0.131   1.00 27.31  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 16.535  -15.360 -2.026  1.00 33.07  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 17.589  -16.195 -2.586  1.00 28.92  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.085  -16.920 -3.823  1.00 28.10  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 15.879  -16.970 -4.106  1.00 31.27  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.110  -17.186 -1.547  1.00 27.31  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.051  -17.467 -4.563  1.00 30.32  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 17.777  -18.412 -5.634  1.00 35.35  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 17.472  -19.782 -5.038  1.00 35.97  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 18.287  -20.359 -4.303  1.00 41.10  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 18.959  -18.446 -6.589  1.00 37.83  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 18.920  -19.608 -7.401  1.00 51.08  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 16.273  -20.289 -5.315  1.00 36.11  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 15.928  -21.655 -4.936  1.00 40.44  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 15.868  -22.568 -6.162  1.00 48.99  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 15.184  -23.589 -6.132  1.00 54.65  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 14.649  -21.795 -4.098  1.00 34.37  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 14.774  -21.122 -2.742  1.00 29.15  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.291  -21.816 -1.653  1.00 31.33  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 14.398  -19.791 -2.557  1.00 27.93  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 15.459  -21.196 -0.421  1.00 34.46  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 14.513  -19.171 -1.324  1.00 29.87  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.053  -19.881 -0.250  1.00 32.14  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.235  -19.340 0.987   1.00 33.18  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 16.612  -22.210 -7.212  1.00 60.67  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 16.970  -23.117 -8.297  1.00 75.09  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 17.307  -24.522 -7.763  1.00 82.61  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 18.227  -24.627 -6.916  1.00 93.20  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 18.120  -22.561 -9.105  1.00 71.12  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 17.696  -21.416 -9.828  1.00 70.94  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 16.653  -25.474 -8.231  1.00 88.92  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 39.173  -11.173 -41.676 1.00 97.69  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.768  -12.231 -42.641 1.00 107.99 ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 37.239  -12.328 -42.690 1.00 99.58  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.599  -12.471 -41.647 1.00 90.31  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.408  -13.572 -42.250 1.00 115.53 ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.654  -14.536 -43.408 1.00 117.39 ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.510  -13.843 -44.841 1.00 104.09 ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.874  -12.954 -44.081 1.00 96.39  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.598  -12.223 -43.885 1.00 89.32  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 35.161  -12.487 -44.015 1.00 82.61  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.770  -13.914 -43.624 1.00 82.82  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.580  -14.843 -43.711 1.00 71.23  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.847  -12.164 -45.494 1.00 74.71  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.993  -11.272 -45.923 1.00 71.25  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 37.203  -11.794 -45.160 1.00 76.36  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.513  -14.060 -43.179 1.00 86.93  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.967  -15.319 -42.682 1.00 87.28  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.548  -15.532 -43.212 1.00 79.04  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 30.961  -14.607 -43.778 1.00 77.14  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 33.030  -15.349 -41.153 1.00 84.99  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.411  -15.557 -40.628 1.00 96.68  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.353  -16.312 -41.299 1.00 95.74  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 34.999  -15.124 -39.500 1.00 80.67  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.470  -16.330 -40.589 1.00 92.36  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.273  -15.616 -39.494 1.00 88.11  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 31.003  -16.750 -43.030 1.00 58.33  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.694  -17.072 -43.577 1.00 56.86  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.685  -16.076 -43.033 1.00 54.67  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.865  -15.557 -43.788 1.00 57.96  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.286  -18.476 -43.222 1.00 62.47  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.788  -15.825 -41.722 1.00 49.35  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.994  -14.809 -41.051 1.00 57.42  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.859  -13.571 -40.800 1.00 53.32  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.960  -13.679 -40.274 1.00 48.70  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.436  -15.391 -39.745 1.00 53.08  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.302  -16.388 -39.938 1.00 45.15  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 25.011  -15.948 -40.245 1.00 40.13  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.528  -17.754 -39.797 1.00 44.94  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.972  -16.851 -40.425 1.00 39.93  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.489  -18.661 -39.989 1.00 42.07  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.217  -18.212 -40.298 1.00 36.94  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.357  -12.396 -41.195 1.00 56.43  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 29.058  -11.133 -40.996 1.00 56.14  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.293  -10.248 -40.000 1.00 61.76  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 27.053  -10.312 -39.905 1.00 49.79  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 29.249  -10.453 -42.353 1.00 53.06  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.960  -10.186 -43.134 1.00 55.49  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 28.179  -9.623  -44.536 1.00 59.84  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 26.930  -9.158  -45.226 1.00 67.39  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 25.956  -10.236 -45.428 1.00 63.57  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 29.011  -9.367  -39.253 1.00 59.90  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.381  -8.467  -38.286 1.00 49.15  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.222  -7.729  -38.932 1.00 47.72  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.334  -7.241  -40.052 1.00 47.60  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.572  -7.570  -37.969 1.00 51.48  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.731  -8.549  -37.928 1.00 52.29  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.476  -9.185  -39.292 1.00 59.28  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 26.069  -7.729  -38.250 1.00 40.83  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.925  -7.037  -38.800 1.00 32.50  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.932  -7.990  -39.455 1.00 35.81  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.828  -7.568  -39.788 1.00 37.34  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.335  -9.260  -39.648 1.00 39.93  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.464  -10.284 -40.225 1.00 36.00  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.318  -10.583 -39.259 1.00 38.49  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.543  -10.681 -38.049 1.00 39.10  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.261  -11.547 -40.507 1.00 38.40  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 25.032  -11.571 -41.823 1.00 46.55  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.827  -10.648 -42.641 1.00 45.98  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.825  -12.521 -42.023 1.00 45.09  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.103  -10.740 -39.796 1.00 31.15  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.959  -11.022 -38.948 1.00 33.74  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.682  -12.525 -38.940 1.00 34.91  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.771  -13.180 -39.981 1.00 40.51  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.772  -10.200 -39.463 1.00 30.07  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 19.031  -8.697  -39.593 1.00 29.47  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.826  -7.857  -40.012 1.00 27.64  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.608  -8.210  -38.277 1.00 30.66  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.332  -13.081 -37.767 1.00 34.34  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 19.017  -14.507 -37.680 1.00 28.96  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.860  -14.725 -36.697 1.00 34.45  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.433  -13.812 -35.987 1.00 31.33  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.273  -15.311 -37.260 1.00 33.12  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.406  -15.226 -38.299 1.00 30.87  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.802  -14.877 -35.885 1.00 30.23  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.312  -15.941 -36.689 1.00 30.51  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.797  -16.453 -35.439 1.00 31.69  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 17.893  -17.332 -34.866 1.00 34.99  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.501  -18.085 -35.651 1.00 29.51  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.575  -17.336 -35.638 1.00 31.16  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.416  -16.487 -36.110 1.00 33.06  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.180  -16.308 -37.467 1.00 33.03  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.552  -15.894 -35.194 1.00 31.70  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.103  -15.553 -37.903 1.00 35.28  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.485  -15.115 -35.633 1.00 35.24  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.263  -14.949 -36.983 1.00 37.71  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.129  -17.177 -33.538 1.00 29.97  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.143  -17.921 -32.800 1.00 30.29  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.462  -18.856 -31.791 1.00 32.20  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.541  -18.444 -31.085 1.00 33.71  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.078  -16.948 -32.118 1.00 29.47  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 18.929  -20.109 -31.731 1.00 34.09  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.312  -21.178 -30.953 1.00 33.28  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.214  -21.500 -29.766 1.00 35.05  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.387  -21.819 -29.944 1.00 38.80  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.158  -22.470 -31.771 1.00 31.83  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.338  -23.581 -31.095 1.00 31.75  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 15.952  -23.074 -30.695 1.00 34.26  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.013  -24.071 -30.046 1.00 35.28  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.573  -24.553 -28.783 1.00 31.61  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.675  -21.353 -28.554 1.00 37.37  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.314  -21.893 -27.369 1.00 39.18  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.345  -22.882 -26.723 1.00 39.06  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.128  -22.749 -26.880 1.00 38.55  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.649  -20.786 -26.367 1.00 40.63  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.516  -19.693 -26.949 1.00 50.01  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.434  -18.718 -25.740 1.00 56.73  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 20.799  -19.295 -24.159 1.00 68.82  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 18.902  -23.874 -26.020 1.00 37.71  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.112  -24.846 -25.272 1.00 43.79  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.259  -24.108 -24.238 1.00 38.60  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 17.756  -23.222 -23.534 1.00 41.54  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.108  -25.834 -24.654 1.00 49.92  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 18.579  -27.164 -24.116 1.00 65.63  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 19.741  -28.122 -23.850 1.00 76.52  ? 16  LYS   B CD  1 
ATOM   881  C CE  . LYS   B 1 17 ? 19.389  -29.455 -23.248 1.00 84.55  ? 16  LYS   B CE  1 
ATOM   882  N NZ  . LYS   B 1 17 ? 20.590  -30.278 -23.049 1.00 78.82  ? 16  LYS   B NZ  1 
ATOM   883  N N   . GLY   B 1 18 ? 15.967  -24.429 -24.195 1.00 34.00  ? 17  GLY   B N   1 
ATOM   884  C CA  . GLY   B 1 18 ? 15.076  -23.814 -23.220 1.00 35.42  ? 17  GLY   B CA  1 
ATOM   885  C C   . GLY   B 1 18 ? 14.193  -22.732 -23.846 1.00 36.35  ? 17  GLY   B C   1 
ATOM   886  O O   . GLY   B 1 18 ? 13.241  -22.254 -23.213 1.00 43.14  ? 17  GLY   B O   1 
ATOM   887  N N   . TYR   B 1 19 ? 14.477  -22.377 -25.109 1.00 33.90  ? 18  TYR   B N   1 
ATOM   888  C CA  . TYR   B 1 19 ? 13.876  -21.190 -25.691 1.00 31.27  ? 18  TYR   B CA  1 
ATOM   889  C C   . TYR   B 1 19 ? 13.529  -21.435 -27.148 1.00 32.55  ? 18  TYR   B C   1 
ATOM   890  O O   . TYR   B 1 19 ? 14.195  -22.188 -27.846 1.00 38.17  ? 18  TYR   B O   1 
ATOM   891  C CB  . TYR   B 1 19 ? 14.837  -20.005 -25.621 1.00 31.32  ? 18  TYR   B CB  1 
ATOM   892  C CG  . TYR   B 1 19 ? 15.286  -19.720 -24.197 1.00 34.06  ? 18  TYR   B CG  1 
ATOM   893  C CD1 . TYR   B 1 19 ? 14.611  -18.794 -23.399 1.00 37.15  ? 18  TYR   B CD1 1 
ATOM   894  C CD2 . TYR   B 1 19 ? 16.368  -20.398 -23.642 1.00 37.65  ? 18  TYR   B CD2 1 
ATOM   895  C CE1 . TYR   B 1 19 ? 14.988  -18.560 -22.088 1.00 38.85  ? 18  TYR   B CE1 1 
ATOM   896  C CE2 . TYR   B 1 19 ? 16.755  -20.178 -22.326 1.00 42.35  ? 18  TYR   B CE2 1 
ATOM   897  C CZ  . TYR   B 1 19 ? 16.064  -19.252 -21.559 1.00 41.70  ? 18  TYR   B CZ  1 
ATOM   898  O OH  . TYR   B 1 19 ? 16.464  -19.042 -20.286 1.00 52.08  ? 18  TYR   B OH  1 
ATOM   899  N N   . PRO   B 1 20 ? 12.507  -20.732 -27.662 1.00 30.38  ? 19  PRO   B N   1 
ATOM   900  C CA  . PRO   B 1 20 ? 12.201  -20.785 -29.092 1.00 27.87  ? 19  PRO   B CA  1 
ATOM   901  C C   . PRO   B 1 20 ? 13.276  -20.056 -29.911 1.00 29.21  ? 19  PRO   B C   1 
ATOM   902  O O   . PRO   B 1 20 ? 14.008  -19.211 -29.378 1.00 29.08  ? 19  PRO   B O   1 
ATOM   903  C CB  . PRO   B 1 20 ? 10.834  -20.105 -29.128 1.00 25.08  ? 19  PRO   B CB  1 
ATOM   904  C CG  . PRO   B 1 20 ? 10.921  -19.063 -27.985 1.00 27.76  ? 19  PRO   B CG  1 
ATOM   905  C CD  . PRO   B 1 20 ? 11.653  -19.812 -26.884 1.00 26.38  ? 19  PRO   B CD  1 
ATOM   906  N N   . HIS   B 1 21 ? 13.421  -20.456 -31.178 1.00 27.80  ? 20  HIS   B N   1 
ATOM   907  C CA  . HIS   B 1 21 ? 14.270  -19.740 -32.134 1.00 29.03  ? 20  HIS   B CA  1 
ATOM   908  C C   . HIS   B 1 21 ? 13.990  -18.246 -32.025 1.00 29.31  ? 20  HIS   B C   1 
ATOM   909  O O   . HIS   B 1 21 ? 12.852  -17.801 -32.223 1.00 32.50  ? 20  HIS   B O   1 
ATOM   910  C CB  . HIS   B 1 21 ? 13.966  -20.183 -33.575 1.00 30.71  ? 20  HIS   B CB  1 
ATOM   911  C CG  . HIS   B 1 21 ? 14.143  -21.647 -33.753 1.00 35.23  ? 20  HIS   B CG  1 
ATOM   912  N ND1 . HIS   B 1 21 ? 13.154  -22.552 -33.434 1.00 34.91  ? 20  HIS   B ND1 1 
ATOM   913  C CD2 . HIS   B 1 21 ? 15.214  -22.368 -34.122 1.00 37.61  ? 20  HIS   B CD2 1 
ATOM   914  C CE1 . HIS   B 1 21 ? 13.602  -23.776 -33.667 1.00 39.11  ? 20  HIS   B CE1 1 
ATOM   915  N NE2 . HIS   B 1 21 ? 14.853  -23.698 -34.071 1.00 40.14  ? 20  HIS   B NE2 1 
ATOM   916  N N   . TRP   B 1 22 ? 15.037  -17.489 -31.702 1.00 27.76  ? 21  TRP   B N   1 
ATOM   917  C CA  . TRP   B 1 22 ? 14.860  -16.153 -31.168 1.00 31.00  ? 21  TRP   B CA  1 
ATOM   918  C C   . TRP   B 1 22 ? 15.407  -15.097 -32.133 1.00 30.20  ? 21  TRP   B C   1 
ATOM   919  O O   . TRP   B 1 22 ? 16.562  -15.207 -32.562 1.00 34.69  ? 21  TRP   B O   1 
ATOM   920  C CB  . TRP   B 1 22 ? 15.558  -16.043 -29.803 1.00 29.71  ? 21  TRP   B CB  1 
ATOM   921  C CG  . TRP   B 1 22 ? 15.041  -14.882 -28.996 1.00 31.80  ? 21  TRP   B CG  1 
ATOM   922  C CD1 . TRP   B 1 22 ? 15.338  -13.559 -29.167 1.00 32.86  ? 21  TRP   B CD1 1 
ATOM   923  C CD2 . TRP   B 1 22 ? 14.072  -14.941 -27.919 1.00 34.58  ? 21  TRP   B CD2 1 
ATOM   924  N NE1 . TRP   B 1 22 ? 14.641  -12.794 -28.260 1.00 33.36  ? 21  TRP   B NE1 1 
ATOM   925  C CE2 . TRP   B 1 22 ? 13.855  -13.615 -27.480 1.00 32.95  ? 21  TRP   B CE2 1 
ATOM   926  C CE3 . TRP   B 1 22 ? 13.382  -15.977 -27.281 1.00 35.60  ? 21  TRP   B CE3 1 
ATOM   927  C CZ2 . TRP   B 1 22 ? 12.974  -13.307 -26.436 1.00 35.21  ? 21  TRP   B CZ2 1 
ATOM   928  C CZ3 . TRP   B 1 22 ? 12.507  -15.675 -26.256 1.00 35.20  ? 21  TRP   B CZ3 1 
ATOM   929  C CH2 . TRP   B 1 22 ? 12.286  -14.350 -25.852 1.00 35.83  ? 21  TRP   B CH2 1 
ATOM   930  N N   . PRO   B 1 23 ? 14.642  -14.016 -32.438 1.00 29.50  ? 22  PRO   B N   1 
ATOM   931  C CA  . PRO   B 1 23 ? 15.127  -12.932 -33.308 1.00 31.55  ? 22  PRO   B CA  1 
ATOM   932  C C   . PRO   B 1 23 ? 16.408  -12.360 -32.714 1.00 33.15  ? 22  PRO   B C   1 
ATOM   933  O O   . PRO   B 1 23 ? 16.430  -11.990 -31.549 1.00 35.38  ? 22  PRO   B O   1 
ATOM   934  C CB  . PRO   B 1 23 ? 14.004  -11.899 -33.292 1.00 29.35  ? 22  PRO   B CB  1 
ATOM   935  C CG  . PRO   B 1 23 ? 13.268  -12.229 -32.011 1.00 27.46  ? 22  PRO   B CG  1 
ATOM   936  C CD  . PRO   B 1 23 ? 13.271  -13.760 -31.964 1.00 27.14  ? 22  PRO   B CD  1 
ATOM   937  N N   . ALA   B 1 24 ? 17.466  -12.277 -33.535 1.00 33.96  ? 23  ALA   B N   1 
ATOM   938  C CA  . ALA   B 1 24 ? 18.798  -11.957 -33.054 1.00 27.95  ? 23  ALA   B CA  1 
ATOM   939  C C   . ALA   B 1 24 ? 19.627  -11.349 -34.192 1.00 32.85  ? 23  ALA   B C   1 
ATOM   940  O O   . ALA   B 1 24 ? 19.173  -11.256 -35.343 1.00 32.45  ? 23  ALA   B O   1 
ATOM   941  C CB  . ALA   B 1 24 ? 19.448  -13.204 -32.462 1.00 31.25  ? 23  ALA   B CB  1 
ATOM   942  N N   . ARG   B 1 25 ? 20.856  -10.927 -33.846 1.00 31.50  ? 24  ARG   B N   1 
ATOM   943  C CA  . ARG   B 1 25 ? 21.746  -10.378 -34.852 1.00 32.90  ? 24  ARG   B CA  1 
ATOM   944  C C   . ARG   B 1 25 ? 23.153  -10.853 -34.545 1.00 30.25  ? 24  ARG   B C   1 
ATOM   945  O O   . ARG   B 1 25 ? 23.442  -11.197 -33.392 1.00 31.10  ? 24  ARG   B O   1 
ATOM   946  C CB  . ARG   B 1 25 ? 21.646  -8.846  -34.939 1.00 31.68  ? 24  ARG   B CB  1 
ATOM   947  C CG  . ARG   B 1 25 ? 22.463  -8.072  -33.923 1.00 34.35  ? 24  ARG   B CG  1 
ATOM   948  C CD  . ARG   B 1 25 ? 22.118  -6.581  -33.990 1.00 33.74  ? 24  ARG   B CD  1 
ATOM   949  N NE  . ARG   B 1 25 ? 22.773  -5.836  -32.907 1.00 33.83  ? 24  ARG   B NE  1 
ATOM   950  C CZ  . ARG   B 1 25 ? 22.383  -4.614  -32.544 1.00 31.57  ? 24  ARG   B CZ  1 
ATOM   951  N NH1 . ARG   B 1 25 ? 21.496  -3.966  -33.295 1.00 26.50  ? 24  ARG   B NH1 1 
ATOM   952  N NH2 . ARG   B 1 25 ? 22.909  -4.055  -31.470 1.00 29.69  ? 24  ARG   B NH2 1 
ATOM   953  N N   . ILE   B 1 26 ? 24.013  -10.841 -35.579 1.00 32.44  ? 25  ILE   B N   1 
ATOM   954  C CA  . ILE   B 1 26 ? 25.435  -11.089 -35.346 1.00 33.85  ? 25  ILE   B CA  1 
ATOM   955  C C   . ILE   B 1 26 ? 26.058  -9.736  -35.020 1.00 38.70  ? 25  ILE   B C   1 
ATOM   956  O O   . ILE   B 1 26 ? 25.849  -8.760  -35.742 1.00 39.47  ? 25  ILE   B O   1 
ATOM   957  C CB  . ILE   B 1 26 ? 26.130  -11.713 -36.574 1.00 35.11  ? 25  ILE   B CB  1 
ATOM   958  C CG1 . ILE   B 1 26 ? 25.334  -12.862 -37.205 1.00 31.62  ? 25  ILE   B CG1 1 
ATOM   959  C CG2 . ILE   B 1 26 ? 27.585  -12.103 -36.255 1.00 38.48  ? 25  ILE   B CG2 1 
ATOM   960  C CD1 . ILE   B 1 26 ? 25.262  -14.144 -36.399 1.00 34.23  ? 25  ILE   B CD1 1 
ATOM   961  N N   . ASP   B 1 27 ? 26.796  -9.682  -33.917 1.00 46.73  ? 26  ASP   B N   1 
ATOM   962  C CA  . ASP   B 1 27 ? 27.470  -8.464  -33.488 1.00 52.11  ? 26  ASP   B CA  1 
ATOM   963  C C   . ASP   B 1 27 ? 28.972  -8.562  -33.804 1.00 63.62  ? 26  ASP   B C   1 
ATOM   964  O O   . ASP   B 1 27 ? 29.512  -9.664  -33.966 1.00 58.85  ? 26  ASP   B O   1 
ATOM   965  C CB  . ASP   B 1 27 ? 27.268  -8.280  -31.990 1.00 42.40  ? 26  ASP   B CB  1 
ATOM   966  C CG  . ASP   B 1 27 ? 26.008  -7.538  -31.564 1.00 53.09  ? 26  ASP   B CG  1 
ATOM   967  O OD1 . ASP   B 1 27 ? 25.219  -7.132  -32.453 1.00 51.42  ? 26  ASP   B OD1 1 
ATOM   968  O OD2 . ASP   B 1 27 ? 25.837  -7.338  -30.334 1.00 49.68  ? 26  ASP   B OD2 1 
ATOM   969  N N   . ASP   B 1 28 ? 29.658  -7.406  -33.817 1.00 67.22  ? 27  ASP   B N   1 
ATOM   970  C CA  . ASP   B 1 28 ? 31.106  -7.325  -33.989 1.00 70.59  ? 27  ASP   B CA  1 
ATOM   971  C C   . ASP   B 1 28 ? 31.808  -7.735  -32.697 1.00 77.28  ? 27  ASP   B C   1 
ATOM   972  O O   . ASP   B 1 28 ? 31.179  -7.750  -31.638 1.00 67.58  ? 27  ASP   B O   1 
ATOM   973  C CB  . ASP   B 1 28 ? 31.545  -5.920  -34.363 1.00 70.76  ? 27  ASP   B CB  1 
ATOM   974  C CG  . ASP   B 1 28 ? 30.630  -5.199  -35.342 1.00 84.08  ? 27  ASP   B CG  1 
ATOM   975  O OD1 . ASP   B 1 28 ? 31.085  -4.951  -36.477 1.00 84.79  ? 27  ASP   B OD1 1 
ATOM   976  O OD2 . ASP   B 1 28 ? 29.472  -4.893  -34.963 1.00 86.37  ? 27  ASP   B OD2 1 
ATOM   977  N N   . ILE   B 1 29 ? 33.112  -8.057  -32.803 1.00 77.47  ? 28  ILE   B N   1 
ATOM   978  C CA  . ILE   B 1 29 ? 33.907  -8.518  -31.673 1.00 69.15  ? 28  ILE   B CA  1 
ATOM   979  C C   . ILE   B 1 29 ? 34.532  -7.307  -30.949 1.00 72.56  ? 28  ILE   B C   1 
ATOM   980  O O   . ILE   B 1 29 ? 34.903  -6.320  -31.640 1.00 76.30  ? 28  ILE   B O   1 
ATOM   981  C CB  . ILE   B 1 29 ? 34.962  -9.548  -32.117 1.00 59.89  ? 28  ILE   B CB  1 
ATOM   982  N N   . VAL   B 1 34 ? 36.715  -10.159 -24.653 1.00 78.47  ? 33  VAL   B N   1 
ATOM   983  C CA  . VAL   B 1 34 ? 36.655  -11.647 -24.760 1.00 77.12  ? 33  VAL   B CA  1 
ATOM   984  C C   . VAL   B 1 34 ? 36.188  -11.971 -26.169 1.00 82.35  ? 33  VAL   B C   1 
ATOM   985  O O   . VAL   B 1 34 ? 35.006  -11.809 -26.451 1.00 97.76  ? 33  VAL   B O   1 
ATOM   986  C CB  . VAL   B 1 34 ? 35.699  -12.222 -23.692 1.00 75.52  ? 33  VAL   B CB  1 
ATOM   987  C CG1 . VAL   B 1 34 ? 34.660  -11.193 -23.255 1.00 79.82  ? 33  VAL   B CG1 1 
ATOM   988  C CG2 . VAL   B 1 34 ? 35.040  -13.538 -24.116 1.00 57.42  ? 33  VAL   B CG2 1 
ATOM   989  N N   . LYS   B 1 35 ? 37.125  -12.402 -27.032 1.00 87.08  ? 34  LYS   B N   1 
ATOM   990  C CA  . LYS   B 1 35 ? 36.850  -12.769 -28.422 1.00 86.13  ? 34  LYS   B CA  1 
ATOM   991  C C   . LYS   B 1 35 ? 36.188  -14.154 -28.493 1.00 85.03  ? 34  LYS   B C   1 
ATOM   992  O O   . LYS   B 1 35 ? 36.606  -15.071 -27.785 1.00 97.31  ? 34  LYS   B O   1 
ATOM   993  C CB  . LYS   B 1 35 ? 38.142  -12.707 -29.251 1.00 69.57  ? 34  LYS   B CB  1 
ATOM   994  N N   . PRO   B 1 36 ? 35.173  -14.380 -29.370 1.00 80.08  ? 35  PRO   B N   1 
ATOM   995  C CA  . PRO   B 1 36 ? 34.370  -15.616 -29.340 1.00 67.32  ? 35  PRO   B CA  1 
ATOM   996  C C   . PRO   B 1 36 ? 35.175  -16.911 -29.373 1.00 57.33  ? 35  PRO   B C   1 
ATOM   997  O O   . PRO   B 1 36 ? 36.182  -16.957 -30.068 1.00 62.89  ? 35  PRO   B O   1 
ATOM   998  C CB  . PRO   B 1 36 ? 33.442  -15.498 -30.570 1.00 65.94  ? 35  PRO   B CB  1 
ATOM   999  C CG  . PRO   B 1 36 ? 34.098  -14.437 -31.441 1.00 77.46  ? 35  PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 1 36 ? 34.774  -13.475 -30.466 1.00 81.57  ? 35  PRO   B CD  1 
ATOM   1001 N N   . PRO   B 1 37 ? 34.743  -18.000 -28.678 1.00 56.82  ? 36  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 37 ? 35.406  -19.305 -28.771 1.00 58.21  ? 36  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 37 ? 35.401  -19.653 -30.257 1.00 74.60  ? 36  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 37 ? 34.512  -19.203 -30.977 1.00 77.60  ? 36  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 37 ? 34.529  -20.309 -27.989 1.00 52.20  ? 36  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 37 ? 33.439  -19.493 -27.330 1.00 46.89  ? 36  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 37 ? 33.531  -18.055 -27.842 1.00 52.68  ? 36  PRO   B CD  1 
ATOM   1008 N N   . PRO   B 1 38 ? 36.358  -20.460 -30.777 1.00 84.49  ? 37  PRO   B N   1 
ATOM   1009 C CA  . PRO   B 1 38 ? 36.372  -20.781 -32.212 1.00 83.10  ? 37  PRO   B CA  1 
ATOM   1010 C C   . PRO   B 1 38 ? 35.089  -21.432 -32.747 1.00 76.95  ? 37  PRO   B C   1 
ATOM   1011 O O   . PRO   B 1 38 ? 34.428  -22.204 -32.045 1.00 64.60  ? 37  PRO   B O   1 
ATOM   1012 C CB  . PRO   B 1 38 ? 37.641  -21.654 -32.402 1.00 75.20  ? 37  PRO   B CB  1 
ATOM   1013 C CG  . PRO   B 1 38 ? 38.476  -21.362 -31.165 1.00 78.07  ? 37  PRO   B CG  1 
ATOM   1014 C CD  . PRO   B 1 38 ? 37.476  -21.079 -30.039 1.00 83.71  ? 37  PRO   B CD  1 
ATOM   1015 N N   . ASN   B 1 39 ? 34.719  -21.067 -33.985 1.00 65.54  ? 38  ASN   B N   1 
ATOM   1016 C CA  . ASN   B 1 39 ? 33.542  -21.608 -34.650 1.00 63.19  ? 38  ASN   B CA  1 
ATOM   1017 C C   . ASN   B 1 39 ? 32.289  -20.777 -34.382 1.00 56.97  ? 38  ASN   B C   1 
ATOM   1018 O O   . ASN   B 1 39 ? 31.345  -20.845 -35.160 1.00 56.98  ? 38  ASN   B O   1 
ATOM   1019 C CB  . ASN   B 1 39 ? 33.224  -23.033 -34.212 1.00 66.92  ? 38  ASN   B CB  1 
ATOM   1020 C CG  . ASN   B 1 39 ? 34.116  -24.053 -34.873 1.00 70.58  ? 38  ASN   B CG  1 
ATOM   1021 O OD1 . ASN   B 1 39 ? 33.760  -25.235 -34.920 1.00 80.61  ? 38  ASN   B OD1 1 
ATOM   1022 N ND2 . ASN   B 1 39 ? 35.246  -23.622 -35.414 1.00 67.60  ? 38  ASN   B ND2 1 
ATOM   1023 N N   . LYS   B 1 40 ? 32.293  -19.971 -33.316 1.00 54.36  ? 39  LYS   B N   1 
ATOM   1024 C CA  . LYS   B 1 40 ? 31.078  -19.358 -32.810 1.00 47.53  ? 39  LYS   B CA  1 
ATOM   1025 C C   . LYS   B 1 40 ? 31.093  -17.851 -33.033 1.00 46.68  ? 39  LYS   B C   1 
ATOM   1026 O O   . LYS   B 1 40 ? 32.141  -17.253 -33.251 1.00 48.42  ? 39  LYS   B O   1 
ATOM   1027 C CB  . LYS   B 1 40 ? 31.023  -19.679 -31.318 1.00 47.43  ? 39  LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 1 40 ? 31.266  -21.128 -30.970 1.00 43.69  ? 39  LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 1 40 ? 31.056  -21.298 -29.471 1.00 50.90  ? 39  LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 1 40 ? 29.679  -21.689 -29.022 1.00 57.93  ? 39  LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 1 40 ? 29.488  -23.143 -28.987 1.00 62.18  ? 39  LYS   B NZ  1 
ATOM   1032 N N   . TYR   B 1 41 ? 29.916  -17.226 -32.963 1.00 44.22  ? 40  TYR   B N   1 
ATOM   1033 C CA  . TYR   B 1 41 ? 29.881  -15.784 -33.109 1.00 44.29  ? 40  TYR   B CA  1 
ATOM   1034 C C   . TYR   B 1 41 ? 29.221  -15.115 -31.898 1.00 44.37  ? 40  TYR   B C   1 
ATOM   1035 O O   . TYR   B 1 41 ? 28.403  -15.724 -31.201 1.00 41.84  ? 40  TYR   B O   1 
ATOM   1036 C CB  . TYR   B 1 41 ? 29.013  -15.517 -34.336 1.00 43.23  ? 40  TYR   B CB  1 
ATOM   1037 C CG  . TYR   B 1 41 ? 29.476  -16.046 -35.684 1.00 45.24  ? 40  TYR   B CG  1 
ATOM   1038 C CD1 . TYR   B 1 41 ? 30.006  -15.176 -36.636 1.00 47.92  ? 40  TYR   B CD1 1 
ATOM   1039 C CD2 . TYR   B 1 41 ? 29.320  -17.385 -36.038 1.00 46.82  ? 40  TYR   B CD2 1 
ATOM   1040 C CE1 . TYR   B 1 41 ? 30.411  -15.629 -37.883 1.00 49.99  ? 40  TYR   B CE1 1 
ATOM   1041 C CE2 . TYR   B 1 41 ? 29.724  -17.850 -37.285 1.00 45.78  ? 40  TYR   B CE2 1 
ATOM   1042 C CZ  . TYR   B 1 41 ? 30.264  -16.968 -38.209 1.00 50.18  ? 40  TYR   B CZ  1 
ATOM   1043 O OH  . TYR   B 1 41 ? 30.638  -17.371 -39.460 1.00 58.42  ? 40  TYR   B OH  1 
ATOM   1044 N N   . PRO   B 1 42 ? 29.457  -13.794 -31.686 1.00 43.67  ? 41  PRO   B N   1 
ATOM   1045 C CA  . PRO   B 1 42 ? 28.711  -13.041 -30.684 1.00 41.07  ? 41  PRO   B CA  1 
ATOM   1046 C C   . PRO   B 1 42 ? 27.314  -12.798 -31.248 1.00 40.07  ? 41  PRO   B C   1 
ATOM   1047 O O   . PRO   B 1 42 ? 27.177  -12.099 -32.263 1.00 37.90  ? 41  PRO   B O   1 
ATOM   1048 C CB  . PRO   B 1 42 ? 29.521  -11.707 -30.574 1.00 41.76  ? 41  PRO   B CB  1 
ATOM   1049 C CG  . PRO   B 1 42 ? 30.195  -11.515 -31.935 1.00 41.84  ? 41  PRO   B CG  1 
ATOM   1050 C CD  . PRO   B 1 42 ? 30.379  -12.936 -32.461 1.00 42.14  ? 41  PRO   B CD  1 
ATOM   1051 N N   . ILE   B 1 43 ? 26.298  -13.304 -30.524 1.00 38.09  ? 42  ILE   B N   1 
ATOM   1052 C CA  . ILE   B 1 43 ? 24.882  -13.080 -30.826 1.00 39.98  ? 42  ILE   B CA  1 
ATOM   1053 C C   . ILE   B 1 43 ? 24.248  -12.004 -29.925 1.00 39.89  ? 42  ILE   B C   1 
ATOM   1054 O O   . ILE   B 1 43 ? 24.427  -12.014 -28.717 1.00 44.95  ? 42  ILE   B O   1 
ATOM   1055 C CB  . ILE   B 1 43 ? 24.123  -14.411 -30.686 1.00 35.83  ? 42  ILE   B CB  1 
ATOM   1056 C CG1 . ILE   B 1 43 ? 24.815  -15.517 -31.535 1.00 35.79  ? 42  ILE   B CG1 1 
ATOM   1057 C CG2 . ILE   B 1 43 ? 22.646  -14.215 -31.042 1.00 37.65  ? 42  ILE   B CG2 1 
ATOM   1058 C CD1 . ILE   B 1 43 ? 25.373  -15.023 -32.873 1.00 31.55  ? 42  ILE   B CD1 1 
ATOM   1059 N N   . PHE   B 1 44 ? 23.448  -11.101 -30.512 1.00 36.88  ? 43  PHE   B N   1 
ATOM   1060 C CA  . PHE   B 1 44 ? 22.635  -10.176 -29.737 1.00 34.49  ? 43  PHE   B CA  1 
ATOM   1061 C C   . PHE   B 1 44 ? 21.167  -10.534 -29.958 1.00 33.54  ? 43  PHE   B C   1 
ATOM   1062 O O   . PHE   B 1 44 ? 20.716  -10.605 -31.111 1.00 34.23  ? 43  PHE   B O   1 
ATOM   1063 C CB  . PHE   B 1 44 ? 22.938  -8.699  -30.044 1.00 31.29  ? 43  PHE   B CB  1 
ATOM   1064 C CG  . PHE   B 1 44 ? 21.998  -7.678  -29.408 1.00 33.66  ? 43  PHE   B CG  1 
ATOM   1065 C CD1 . PHE   B 1 44 ? 20.835  -7.263  -30.065 1.00 32.27  ? 43  PHE   B CD1 1 
ATOM   1066 C CD2 . PHE   B 1 44 ? 22.269  -7.139  -28.148 1.00 35.51  ? 43  PHE   B CD2 1 
ATOM   1067 C CE1 . PHE   B 1 44 ? 19.975  -6.328  -29.479 1.00 34.47  ? 43  PHE   B CE1 1 
ATOM   1068 C CE2 . PHE   B 1 44 ? 21.425  -6.187  -27.571 1.00 33.47  ? 43  PHE   B CE2 1 
ATOM   1069 C CZ  . PHE   B 1 44 ? 20.265  -5.803  -28.227 1.00 37.92  ? 43  PHE   B CZ  1 
ATOM   1070 N N   . PHE   B 1 45 ? 20.458  -10.776 -28.835 1.00 33.00  ? 44  PHE   B N   1 
ATOM   1071 C CA  . PHE   B 1 45 ? 19.064  -11.200 -28.786 1.00 28.63  ? 44  PHE   B CA  1 
ATOM   1072 C C   . PHE   B 1 45 ? 18.164  -9.965  -28.726 1.00 30.29  ? 44  PHE   B C   1 
ATOM   1073 O O   . PHE   B 1 45 ? 18.186  -9.213  -27.756 1.00 34.86  ? 44  PHE   B O   1 
ATOM   1074 C CB  . PHE   B 1 45 ? 18.857  -12.175 -27.612 1.00 28.24  ? 44  PHE   B CB  1 
ATOM   1075 C CG  . PHE   B 1 45 ? 19.509  -13.547 -27.771 1.00 30.72  ? 44  PHE   B CG  1 
ATOM   1076 C CD1 . PHE   B 1 45 ? 20.857  -13.740 -27.519 1.00 32.90  ? 44  PHE   B CD1 1 
ATOM   1077 C CD2 . PHE   B 1 45 ? 18.784  -14.633 -28.240 1.00 33.09  ? 44  PHE   B CD2 1 
ATOM   1078 C CE1 . PHE   B 1 45 ? 21.433  -14.985 -27.683 1.00 40.28  ? 44  PHE   B CE1 1 
ATOM   1079 C CE2 . PHE   B 1 45 ? 19.359  -15.886 -28.388 1.00 36.72  ? 44  PHE   B CE2 1 
ATOM   1080 C CZ  . PHE   B 1 45 ? 20.686  -16.061 -28.133 1.00 36.45  ? 44  PHE   B CZ  1 
ATOM   1081 N N   . PHE   B 1 46 ? 17.362  -9.721  -29.769 1.00 31.26  ? 45  PHE   B N   1 
ATOM   1082 C CA  . PHE   B 1 46 ? 16.454  -8.586  -29.692 1.00 31.04  ? 45  PHE   B CA  1 
ATOM   1083 C C   . PHE   B 1 46 ? 15.443  -8.812  -28.561 1.00 34.64  ? 45  PHE   B C   1 
ATOM   1084 O O   . PHE   B 1 46 ? 15.187  -9.948  -28.175 1.00 34.18  ? 45  PHE   B O   1 
ATOM   1085 C CB  . PHE   B 1 46 ? 15.750  -8.362  -31.023 1.00 29.63  ? 45  PHE   B CB  1 
ATOM   1086 C CG  . PHE   B 1 46 ? 16.714  -7.911  -32.113 1.00 38.94  ? 45  PHE   B CG  1 
ATOM   1087 C CD1 . PHE   B 1 46 ? 17.199  -6.598  -32.142 1.00 41.97  ? 45  PHE   B CD1 1 
ATOM   1088 C CD2 . PHE   B 1 46 ? 17.100  -8.775  -33.132 1.00 32.39  ? 45  PHE   B CD2 1 
ATOM   1089 C CE1 . PHE   B 1 46 ? 18.055  -6.172  -33.155 1.00 37.98  ? 45  PHE   B CE1 1 
ATOM   1090 C CE2 . PHE   B 1 46 ? 17.959  -8.343  -34.137 1.00 37.58  ? 45  PHE   B CE2 1 
ATOM   1091 C CZ  . PHE   B 1 46 ? 18.418  -7.040  -34.155 1.00 32.03  ? 45  PHE   B CZ  1 
ATOM   1092 N N   . GLY   B 1 47 ? 14.847  -7.731  -28.044 1.00 37.37  ? 46  GLY   B N   1 
ATOM   1093 C CA  . GLY   B 1 47 ? 13.809  -7.857  -27.020 1.00 33.99  ? 46  GLY   B CA  1 
ATOM   1094 C C   . GLY   B 1 47 ? 14.450  -7.977  -25.642 1.00 34.48  ? 46  GLY   B C   1 
ATOM   1095 O O   . GLY   B 1 47 ? 14.239  -7.157  -24.779 1.00 37.18  ? 46  GLY   B O   1 
ATOM   1096 N N   . THR   B 1 48 ? 15.267  -8.999  -25.448 1.00 36.03  ? 47  THR   B N   1 
ATOM   1097 C CA  . THR   B 1 48 ? 15.840  -9.196  -24.144 1.00 36.29  ? 47  THR   B CA  1 
ATOM   1098 C C   . THR   B 1 48 ? 17.131  -8.400  -24.074 1.00 36.69  ? 47  THR   B C   1 
ATOM   1099 O O   . THR   B 1 48 ? 17.618  -8.155  -22.976 1.00 36.16  ? 47  THR   B O   1 
ATOM   1100 C CB  . THR   B 1 48 ? 16.110  -10.682 -23.911 1.00 36.10  ? 47  THR   B CB  1 
ATOM   1101 O OG1 . THR   B 1 48 ? 17.103  -11.085 -24.857 1.00 32.69  ? 47  THR   B OG1 1 
ATOM   1102 C CG2 . THR   B 1 48 ? 14.831  -11.496 -23.912 1.00 35.45  ? 47  THR   B CG2 1 
ATOM   1103 N N   . HIS   B 1 49 ? 17.750  -8.158  -25.235 1.00 34.12  ? 48  HIS   B N   1 
ATOM   1104 C CA  . HIS   B 1 49 ? 19.007  -7.423  -25.311 1.00 34.82  ? 48  HIS   B CA  1 
ATOM   1105 C C   . HIS   B 1 49 ? 20.127  -8.147  -24.576 1.00 37.88  ? 48  HIS   B C   1 
ATOM   1106 O O   . HIS   B 1 49 ? 21.062  -7.482  -24.125 1.00 42.27  ? 48  HIS   B O   1 
ATOM   1107 C CB  . HIS   B 1 49 ? 18.873  -5.966  -24.831 1.00 34.22  ? 48  HIS   B CB  1 
ATOM   1108 C CG  . HIS   B 1 49 ? 17.710  -5.287  -25.462 1.00 35.42  ? 48  HIS   B CG  1 
ATOM   1109 N ND1 . HIS   B 1 49 ? 16.815  -4.548  -24.730 1.00 38.27  ? 48  HIS   B ND1 1 
ATOM   1110 C CD2 . HIS   B 1 49 ? 17.212  -5.317  -26.718 1.00 37.06  ? 48  HIS   B CD2 1 
ATOM   1111 C CE1 . HIS   B 1 49 ? 15.846  -4.093  -25.534 1.00 39.12  ? 48  HIS   B CE1 1 
ATOM   1112 N NE2 . HIS   B 1 49 ? 16.057  -4.550  -26.747 1.00 39.30  ? 48  HIS   B NE2 1 
ATOM   1113 N N   . GLU   B 1 50 ? 20.051  -9.484  -24.481 1.00 36.47  ? 49  GLU   B N   1 
ATOM   1114 C CA  . GLU   B 1 50 ? 21.163  -10.262 -23.936 1.00 40.48  ? 49  GLU   B CA  1 
ATOM   1115 C C   . GLU   B 1 50 ? 22.068  -10.766 -25.057 1.00 37.64  ? 49  GLU   B C   1 
ATOM   1116 O O   . GLU   B 1 50 ? 21.714  -10.655 -26.223 1.00 42.13  ? 49  GLU   B O   1 
ATOM   1117 C CB  . GLU   B 1 50 ? 20.658  -11.489 -23.190 1.00 46.30  ? 49  GLU   B CB  1 
ATOM   1118 C CG  . GLU   B 1 50 ? 20.326  -11.183 -21.734 1.00 50.16  ? 49  GLU   B CG  1 
ATOM   1119 C CD  . GLU   B 1 50 ? 19.567  -12.327 -21.085 1.00 54.22  ? 49  GLU   B CD  1 
ATOM   1120 O OE1 . GLU   B 1 50 ? 18.545  -12.038 -20.439 1.00 56.29  ? 49  GLU   B OE1 1 
ATOM   1121 O OE2 . GLU   B 1 50 ? 19.971  -13.502 -21.225 1.00 56.46  ? 49  GLU   B OE2 1 
ATOM   1122 N N   . THR   B 1 51 ? 23.241  -11.304 -24.691 1.00 36.02  ? 50  THR   B N   1 
ATOM   1123 C CA  . THR   B 1 51 ? 24.225  -11.797 -25.651 1.00 39.38  ? 50  THR   B CA  1 
ATOM   1124 C C   . THR   B 1 51 ? 24.608  -13.228 -25.275 1.00 43.43  ? 50  THR   B C   1 
ATOM   1125 O O   . THR   B 1 51 ? 24.506  -13.632 -24.130 1.00 47.12  ? 50  THR   B O   1 
ATOM   1126 C CB  . THR   B 1 51 ? 25.483  -10.915 -25.762 1.00 39.64  ? 50  THR   B CB  1 
ATOM   1127 O OG1 . THR   B 1 51 ? 26.120  -10.909 -24.493 1.00 47.36  ? 50  THR   B OG1 1 
ATOM   1128 C CG2 . THR   B 1 51 ? 25.233  -9.448  -26.061 1.00 40.54  ? 50  THR   B CG2 1 
ATOM   1129 N N   . ALA   B 1 52 ? 25.082  -13.990 -26.260 1.00 44.90  ? 51  ALA   B N   1 
ATOM   1130 C CA  . ALA   B 1 52 ? 25.630  -15.315 -26.041 1.00 37.71  ? 51  ALA   B CA  1 
ATOM   1131 C C   . ALA   B 1 52 ? 26.513  -15.653 -27.236 1.00 38.37  ? 51  ALA   B C   1 
ATOM   1132 O O   . ALA   B 1 52 ? 26.517  -14.936 -28.244 1.00 42.88  ? 51  ALA   B O   1 
ATOM   1133 C CB  . ALA   B 1 52 ? 24.528  -16.342 -25.847 1.00 34.09  ? 51  ALA   B CB  1 
ATOM   1134 N N   . PHE   B 1 53 ? 27.271  -16.734 -27.089 1.00 36.16  ? 52  PHE   B N   1 
ATOM   1135 C CA  . PHE   B 1 53 ? 28.066  -17.272 -28.179 1.00 45.23  ? 52  PHE   B CA  1 
ATOM   1136 C C   . PHE   B 1 53 ? 27.340  -18.499 -28.722 1.00 49.39  ? 52  PHE   B C   1 
ATOM   1137 O O   . PHE   B 1 53 ? 27.009  -19.403 -27.958 1.00 49.84  ? 52  PHE   B O   1 
ATOM   1138 C CB  . PHE   B 1 53 ? 29.494  -17.600 -27.718 1.00 50.54  ? 52  PHE   B CB  1 
ATOM   1139 C CG  . PHE   B 1 53 ? 30.341  -16.395 -27.333 1.00 45.38  ? 52  PHE   B CG  1 
ATOM   1140 C CD1 . PHE   B 1 53 ? 30.459  -15.308 -28.191 1.00 48.54  ? 52  PHE   B CD1 1 
ATOM   1141 C CD2 . PHE   B 1 53 ? 30.985  -16.337 -26.102 1.00 46.03  ? 52  PHE   B CD2 1 
ATOM   1142 C CE1 . PHE   B 1 53 ? 31.222  -14.211 -27.833 1.00 47.37  ? 52  PHE   B CE1 1 
ATOM   1143 C CE2 . PHE   B 1 53 ? 31.743  -15.228 -25.746 1.00 47.24  ? 52  PHE   B CE2 1 
ATOM   1144 C CZ  . PHE   B 1 53 ? 31.845  -14.163 -26.604 1.00 45.61  ? 52  PHE   B CZ  1 
ATOM   1145 N N   . LEU   B 1 54 ? 27.098  -18.501 -30.042 1.00 41.39  ? 53  LEU   B N   1 
ATOM   1146 C CA  . LEU   B 1 54 ? 26.408  -19.597 -30.701 1.00 39.08  ? 53  LEU   B CA  1 
ATOM   1147 C C   . LEU   B 1 54 ? 27.155  -19.974 -31.967 1.00 41.27  ? 53  LEU   B C   1 
ATOM   1148 O O   . LEU   B 1 54 ? 27.767  -19.107 -32.603 1.00 40.12  ? 53  LEU   B O   1 
ATOM   1149 C CB  . LEU   B 1 54 ? 24.985  -19.186 -31.061 1.00 38.07  ? 53  LEU   B CB  1 
ATOM   1150 C CG  . LEU   B 1 54 ? 24.016  -19.131 -29.878 1.00 36.42  ? 53  LEU   B CG  1 
ATOM   1151 C CD1 . LEU   B 1 54 ? 22.645  -18.955 -30.519 1.00 33.94  ? 53  LEU   B CD1 1 
ATOM   1152 C CD2 . LEU   B 1 54 ? 24.100  -20.440 -29.086 1.00 30.67  ? 53  LEU   B CD2 1 
ATOM   1153 N N   . GLY   B 1 55 ? 27.068  -21.268 -32.307 1.00 36.27  ? 54  GLY   B N   1 
ATOM   1154 C CA  . GLY   B 1 55 ? 27.625  -21.768 -33.544 1.00 37.03  ? 54  GLY   B CA  1 
ATOM   1155 C C   . GLY   B 1 55 ? 26.575  -21.777 -34.651 1.00 38.11  ? 54  GLY   B C   1 
ATOM   1156 O O   . GLY   B 1 55 ? 25.376  -21.709 -34.394 1.00 40.46  ? 54  GLY   B O   1 
ATOM   1157 N N   . PRO   B 1 56 ? 27.000  -21.932 -35.923 1.00 35.54  ? 55  PRO   B N   1 
ATOM   1158 C CA  . PRO   B 1 56 ? 26.090  -21.842 -37.053 1.00 29.39  ? 55  PRO   B CA  1 
ATOM   1159 C C   . PRO   B 1 56 ? 24.938  -22.838 -36.990 1.00 32.44  ? 55  PRO   B C   1 
ATOM   1160 O O   . PRO   B 1 56 ? 23.893  -22.585 -37.580 1.00 35.07  ? 55  PRO   B O   1 
ATOM   1161 C CB  . PRO   B 1 56 ? 26.983  -22.082 -38.269 1.00 31.43  ? 55  PRO   B CB  1 
ATOM   1162 C CG  . PRO   B 1 56 ? 28.385  -21.895 -37.761 1.00 33.87  ? 55  PRO   B CG  1 
ATOM   1163 C CD  . PRO   B 1 56 ? 28.380  -22.258 -36.304 1.00 36.12  ? 55  PRO   B CD  1 
ATOM   1164 N N   . LYS   B 1 57 ? 25.109  -23.959 -36.271 1.00 35.21  ? 56  LYS   B N   1 
ATOM   1165 C CA  . LYS   B 1 57 ? 24.064  -24.980 -36.233 1.00 35.56  ? 56  LYS   B CA  1 
ATOM   1166 C C   . LYS   B 1 57 ? 22.813  -24.398 -35.580 1.00 35.21  ? 56  LYS   B C   1 
ATOM   1167 O O   . LYS   B 1 57 ? 21.704  -24.893 -35.817 1.00 33.00  ? 56  LYS   B O   1 
ATOM   1168 C CB  . LYS   B 1 57 ? 24.502  -26.296 -35.572 1.00 38.60  ? 56  LYS   B CB  1 
ATOM   1169 C CG  . LYS   B 1 57 ? 24.651  -26.261 -34.057 1.00 43.43  ? 56  LYS   B CG  1 
ATOM   1170 C CD  . LYS   B 1 57 ? 24.727  -27.663 -33.453 1.00 55.69  ? 56  LYS   B CD  1 
ATOM   1171 C CE  . LYS   B 1 57 ? 25.037  -27.723 -31.967 1.00 62.02  ? 56  LYS   B CE  1 
ATOM   1172 N NZ  . LYS   B 1 57 ? 23.961  -27.199 -31.112 1.00 60.20  ? 56  LYS   B NZ  1 
ATOM   1173 N N   . ASP   B 1 58 ? 23.007  -23.309 -34.821 1.00 32.55  ? 57  ASP   B N   1 
ATOM   1174 C CA  . ASP   B 1 58 ? 21.926  -22.697 -34.065 1.00 37.05  ? 57  ASP   B CA  1 
ATOM   1175 C C   . ASP   B 1 58 ? 21.578  -21.309 -34.604 1.00 37.72  ? 57  ASP   B C   1 
ATOM   1176 O O   . ASP   B 1 58 ? 20.833  -20.587 -33.923 1.00 32.88  ? 57  ASP   B O   1 
ATOM   1177 C CB  . ASP   B 1 58 ? 22.216  -22.593 -32.568 1.00 36.24  ? 57  ASP   B CB  1 
ATOM   1178 C CG  . ASP   B 1 58 ? 22.472  -23.895 -31.818 1.00 41.98  ? 57  ASP   B CG  1 
ATOM   1179 O OD1 . ASP   B 1 58 ? 21.622  -24.805 -31.874 1.00 36.78  ? 57  ASP   B OD1 1 
ATOM   1180 O OD2 . ASP   B 1 58 ? 23.550  -24.008 -31.203 1.00 46.20  ? 57  ASP   B OD2 1 
ATOM   1181 N N   . LEU   B 1 59 ? 22.085  -20.956 -35.807 1.00 32.48  ? 58  LEU   B N   1 
ATOM   1182 C CA  . LEU   B 1 59 ? 21.812  -19.651 -36.397 1.00 32.76  ? 58  LEU   B CA  1 
ATOM   1183 C C   . LEU   B 1 59 ? 21.086  -19.841 -37.718 1.00 33.70  ? 58  LEU   B C   1 
ATOM   1184 O O   . LEU   B 1 59 ? 21.570  -20.549 -38.575 1.00 36.79  ? 58  LEU   B O   1 
ATOM   1185 C CB  . LEU   B 1 59 ? 23.082  -18.826 -36.582 1.00 33.61  ? 58  LEU   B CB  1 
ATOM   1186 C CG  . LEU   B 1 59 ? 23.952  -18.671 -35.329 1.00 33.59  ? 58  LEU   B CG  1 
ATOM   1187 C CD1 . LEU   B 1 59 ? 25.322  -18.085 -35.652 1.00 30.96  ? 58  LEU   B CD1 1 
ATOM   1188 C CD2 . LEU   B 1 59 ? 23.241  -17.820 -34.281 1.00 31.71  ? 58  LEU   B CD2 1 
ATOM   1189 N N   . PHE   B 1 60 ? 19.923  -19.208 -37.845 1.00 31.84  ? 59  PHE   B N   1 
ATOM   1190 C CA  . PHE   B 1 60 ? 19.007  -19.414 -38.947 1.00 33.26  ? 59  PHE   B CA  1 
ATOM   1191 C C   . PHE   B 1 60 ? 18.820  -18.073 -39.668 1.00 39.31  ? 59  PHE   B C   1 
ATOM   1192 O O   . PHE   B 1 60 ? 18.154  -17.179 -39.160 1.00 33.91  ? 59  PHE   B O   1 
ATOM   1193 C CB  . PHE   B 1 60 ? 17.677  -20.008 -38.477 1.00 26.42  ? 59  PHE   B CB  1 
ATOM   1194 C CG  . PHE   B 1 60 ? 17.762  -21.402 -37.867 1.00 30.38  ? 59  PHE   B CG  1 
ATOM   1195 C CD1 . PHE   B 1 60 ? 18.121  -21.584 -36.533 1.00 28.61  ? 59  PHE   B CD1 1 
ATOM   1196 C CD2 . PHE   B 1 60 ? 17.459  -22.533 -38.625 1.00 29.79  ? 59  PHE   B CD2 1 
ATOM   1197 C CE1 . PHE   B 1 60 ? 18.215  -22.857 -35.981 1.00 32.83  ? 59  PHE   B CE1 1 
ATOM   1198 C CE2 . PHE   B 1 60 ? 17.494  -23.799 -38.058 1.00 34.59  ? 59  PHE   B CE2 1 
ATOM   1199 C CZ  . PHE   B 1 60 ? 17.892  -23.965 -36.738 1.00 35.71  ? 59  PHE   B CZ  1 
ATOM   1200 N N   . PRO   B 1 61 ? 19.406  -17.891 -40.878 1.00 43.82  ? 60  PRO   B N   1 
ATOM   1201 C CA  . PRO   B 1 61 ? 19.152  -16.692 -41.682 1.00 42.39  ? 60  PRO   B CA  1 
ATOM   1202 C C   . PRO   B 1 61 ? 17.696  -16.228 -41.635 1.00 40.17  ? 60  PRO   B C   1 
ATOM   1203 O O   . PRO   B 1 61 ? 16.781  -16.990 -41.932 1.00 39.73  ? 60  PRO   B O   1 
ATOM   1204 C CB  . PRO   B 1 61 ? 19.625  -17.131 -43.079 1.00 42.88  ? 60  PRO   B CB  1 
ATOM   1205 C CG  . PRO   B 1 61 ? 20.817  -18.028 -42.760 1.00 52.44  ? 60  PRO   B CG  1 
ATOM   1206 C CD  . PRO   B 1 61 ? 20.381  -18.805 -41.507 1.00 45.88  ? 60  PRO   B CD  1 
ATOM   1207 N N   . TYR   B 1 62 ? 17.499  -14.963 -41.235 1.00 37.55  ? 61  TYR   B N   1 
ATOM   1208 C CA  . TYR   B 1 62 ? 16.199  -14.439 -40.864 1.00 37.09  ? 61  TYR   B CA  1 
ATOM   1209 C C   . TYR   B 1 62 ? 15.196  -14.450 -42.007 1.00 47.15  ? 61  TYR   B C   1 
ATOM   1210 O O   . TYR   B 1 62 ? 14.009  -14.726 -41.776 1.00 46.91  ? 61  TYR   B O   1 
ATOM   1211 C CB  . TYR   B 1 62 ? 16.406  -12.983 -40.460 1.00 45.11  ? 61  TYR   B CB  1 
ATOM   1212 C CG  . TYR   B 1 62 ? 15.114  -12.231 -40.201 1.00 41.21  ? 61  TYR   B CG  1 
ATOM   1213 C CD1 . TYR   B 1 62 ? 14.336  -12.511 -39.085 1.00 41.71  ? 61  TYR   B CD1 1 
ATOM   1214 C CD2 . TYR   B 1 62 ? 14.698  -11.217 -41.056 1.00 47.75  ? 61  TYR   B CD2 1 
ATOM   1215 C CE1 . TYR   B 1 62 ? 13.170  -11.813 -38.832 1.00 37.80  ? 61  TYR   B CE1 1 
ATOM   1216 C CE2 . TYR   B 1 62 ? 13.542  -10.497 -40.810 1.00 44.61  ? 61  TYR   B CE2 1 
ATOM   1217 C CZ  . TYR   B 1 62 ? 12.793  -10.797 -39.687 1.00 41.20  ? 61  TYR   B CZ  1 
ATOM   1218 O OH  . TYR   B 1 62 ? 11.644  -10.132 -39.477 1.00 45.26  ? 61  TYR   B OH  1 
ATOM   1219 N N   . ASP   B 1 63 ? 15.656  -14.120 -43.228 1.00 57.30  ? 62  ASP   B N   1 
ATOM   1220 C CA  . ASP   B 1 63 ? 14.725  -13.980 -44.345 1.00 53.01  ? 62  ASP   B CA  1 
ATOM   1221 C C   . ASP   B 1 63 ? 14.142  -15.337 -44.724 1.00 48.19  ? 62  ASP   B C   1 
ATOM   1222 O O   . ASP   B 1 63 ? 12.935  -15.460 -44.850 1.00 52.09  ? 62  ASP   B O   1 
ATOM   1223 C CB  . ASP   B 1 63 ? 15.282  -13.163 -45.494 1.00 57.08  ? 62  ASP   B CB  1 
ATOM   1224 C CG  . ASP   B 1 63 ? 15.099  -11.661 -45.338 1.00 76.49  ? 62  ASP   B CG  1 
ATOM   1225 O OD1 . ASP   B 1 63 ? 14.046  -11.249 -44.777 1.00 76.63  ? 62  ASP   B OD1 1 
ATOM   1226 O OD2 . ASP   B 1 63 ? 16.000  -10.915 -45.793 1.00 87.39  ? 62  ASP   B OD2 1 
ATOM   1227 N N   . LYS   B 1 64 ? 15.006  -16.353 -44.804 1.00 48.51  ? 63  LYS   B N   1 
ATOM   1228 C CA  . LYS   B 1 64 ? 14.609  -17.721 -45.088 1.00 49.25  ? 63  LYS   B CA  1 
ATOM   1229 C C   . LYS   B 1 64 ? 13.631  -18.245 -44.033 1.00 49.16  ? 63  LYS   B C   1 
ATOM   1230 O O   . LYS   B 1 64 ? 12.702  -18.992 -44.344 1.00 48.86  ? 63  LYS   B O   1 
ATOM   1231 C CB  . LYS   B 1 64 ? 15.871  -18.592 -45.127 1.00 51.19  ? 63  LYS   B CB  1 
ATOM   1232 C CG  . LYS   B 1 64 ? 15.639  -20.007 -45.658 1.00 52.86  ? 63  LYS   B CG  1 
ATOM   1233 C CD  . LYS   B 1 64 ? 16.899  -20.863 -45.680 1.00 53.29  ? 63  LYS   B CD  1 
ATOM   1234 C CE  . LYS   B 1 64 ? 16.722  -22.179 -46.377 1.00 50.83  ? 63  LYS   B CE  1 
ATOM   1235 N NZ  . LYS   B 1 64 ? 15.472  -22.813 -45.993 1.00 47.62  ? 63  LYS   B NZ  1 
ATOM   1236 N N   . SER   B 1 65 ? 13.849  -17.876 -42.771 1.00 44.46  ? 64  SER   B N   1 
ATOM   1237 C CA  . SER   B 1 65 ? 13.215  -18.610 -41.687 1.00 41.82  ? 64  SER   B CA  1 
ATOM   1238 C C   . SER   B 1 65 ? 12.115  -17.800 -40.986 1.00 42.81  ? 64  SER   B C   1 
ATOM   1239 O O   . SER   B 1 65 ? 11.468  -18.341 -40.105 1.00 38.97  ? 64  SER   B O   1 
ATOM   1240 C CB  . SER   B 1 65 ? 14.265  -19.082 -40.726 1.00 46.23  ? 64  SER   B CB  1 
ATOM   1241 O OG  . SER   B 1 65 ? 15.101  -17.994 -40.336 1.00 54.66  ? 64  SER   B OG  1 
ATOM   1242 N N   . LYS   B 1 66 ? 11.850  -16.547 -41.420 1.00 43.82  ? 65  LYS   B N   1 
ATOM   1243 C CA  . LYS   B 1 66 ? 10.967  -15.636 -40.698 1.00 42.91  ? 65  LYS   B CA  1 
ATOM   1244 C C   . LYS   B 1 66 ? 9.514   -16.110 -40.670 1.00 52.75  ? 65  LYS   B C   1 
ATOM   1245 O O   . LYS   B 1 66 ? 8.790   -15.791 -39.732 1.00 63.30  ? 65  LYS   B O   1 
ATOM   1246 C CB  . LYS   B 1 66 ? 11.096  -14.156 -41.086 1.00 40.05  ? 65  LYS   B CB  1 
ATOM   1247 C CG  . LYS   B 1 66 ? 10.462  -13.728 -42.399 1.00 41.36  ? 65  LYS   B CG  1 
ATOM   1248 N N   . ASP   B 1 67 ? 9.045   -16.866 -41.667 1.00 53.24  ? 66  ASP   B N   1 
ATOM   1249 C CA  . ASP   B 1 67 ? 7.630   -17.195 -41.587 1.00 59.16  ? 66  ASP   B CA  1 
ATOM   1250 C C   . ASP   B 1 67 ? 7.432   -18.415 -40.683 1.00 58.58  ? 66  ASP   B C   1 
ATOM   1251 O O   . ASP   B 1 67 ? 6.398   -18.538 -40.027 1.00 57.06  ? 66  ASP   B O   1 
ATOM   1252 C CB  . ASP   B 1 67 ? 6.914   -17.046 -42.923 1.00 81.47  ? 66  ASP   B CB  1 
ATOM   1253 C CG  . ASP   B 1 67 ? 7.213   -18.073 -44.006 1.00 90.74  ? 66  ASP   B CG  1 
ATOM   1254 O OD1 . ASP   B 1 67 ? 6.980   -17.746 -45.197 1.00 92.26  ? 66  ASP   B OD1 1 
ATOM   1255 O OD2 . ASP   B 1 67 ? 7.641   -19.194 -43.651 1.00 86.80  ? 66  ASP   B OD2 1 
ATOM   1256 N N   . LYS   B 1 68 ? 8.476   -19.254 -40.592 1.00 51.48  ? 67  LYS   B N   1 
ATOM   1257 C CA  . LYS   B 1 68 ? 8.529   -20.411 -39.711 1.00 47.06  ? 67  LYS   B CA  1 
ATOM   1258 C C   . LYS   B 1 68 ? 8.728   -20.001 -38.247 1.00 47.13  ? 67  LYS   B C   1 
ATOM   1259 O O   . LYS   B 1 68 ? 8.089   -20.576 -37.371 1.00 44.31  ? 67  LYS   B O   1 
ATOM   1260 C CB  . LYS   B 1 68 ? 9.646   -21.331 -40.213 1.00 50.24  ? 67  LYS   B CB  1 
ATOM   1261 C CG  . LYS   B 1 68 ? 9.754   -22.699 -39.542 1.00 64.79  ? 67  LYS   B CG  1 
ATOM   1262 C CD  . LYS   B 1 68 ? 10.394  -23.712 -40.493 1.00 77.38  ? 67  LYS   B CD  1 
ATOM   1263 C CE  . LYS   B 1 68 ? 11.034  -24.918 -39.847 1.00 88.17  ? 67  LYS   B CE  1 
ATOM   1264 N NZ  . LYS   B 1 68 ? 10.185  -25.709 -38.947 1.00 92.25  ? 67  LYS   B NZ  1 
ATOM   1265 N N   . TYR   B 1 69 ? 9.621   -19.031 -37.970 1.00 45.13  ? 68  TYR   B N   1 
ATOM   1266 C CA  . TYR   B 1 69 ? 10.054  -18.795 -36.594 1.00 39.33  ? 68  TYR   B CA  1 
ATOM   1267 C C   . TYR   B 1 69 ? 9.501   -17.494 -36.021 1.00 44.85  ? 68  TYR   B C   1 
ATOM   1268 O O   . TYR   B 1 69 ? 9.493   -17.328 -34.801 1.00 41.90  ? 68  TYR   B O   1 
ATOM   1269 C CB  . TYR   B 1 69 ? 11.566  -18.876 -36.375 1.00 39.18  ? 68  TYR   B CB  1 
ATOM   1270 C CG  . TYR   B 1 69 ? 12.155  -20.248 -36.697 1.00 40.99  ? 68  TYR   B CG  1 
ATOM   1271 C CD1 . TYR   B 1 69 ? 11.648  -21.408 -36.122 1.00 45.85  ? 68  TYR   B CD1 1 
ATOM   1272 C CD2 . TYR   B 1 69 ? 13.212  -20.377 -37.587 1.00 40.12  ? 68  TYR   B CD2 1 
ATOM   1273 C CE1 . TYR   B 1 69 ? 12.186  -22.655 -36.401 1.00 44.49  ? 68  TYR   B CE1 1 
ATOM   1274 C CE2 . TYR   B 1 69 ? 13.739  -21.616 -37.899 1.00 43.65  ? 68  TYR   B CE2 1 
ATOM   1275 C CZ  . TYR   B 1 69 ? 13.224  -22.758 -37.307 1.00 40.28  ? 68  TYR   B CZ  1 
ATOM   1276 O OH  . TYR   B 1 69 ? 13.776  -23.971 -37.604 1.00 39.07  ? 68  TYR   B OH  1 
ATOM   1277 N N   . GLY   B 1 70 ? 8.993   -16.610 -36.886 1.00 38.67  ? 69  GLY   B N   1 
ATOM   1278 C CA  . GLY   B 1 70 ? 8.724   -15.242 -36.478 1.00 45.35  ? 69  GLY   B CA  1 
ATOM   1279 C C   . GLY   B 1 70 ? 7.309   -15.030 -35.942 1.00 47.65  ? 69  GLY   B C   1 
ATOM   1280 O O   . GLY   B 1 70 ? 6.728   -13.974 -36.194 1.00 54.06  ? 69  GLY   B O   1 
ATOM   1281 N N   . LYS   B 1 71 ? 6.763   -16.020 -35.224 1.00 42.95  ? 70  LYS   B N   1 
ATOM   1282 C CA  . LYS   B 1 71 ? 5.394   -15.916 -34.754 1.00 49.22  ? 70  LYS   B CA  1 
ATOM   1283 C C   . LYS   B 1 71 ? 5.368   -15.569 -33.275 1.00 55.25  ? 70  LYS   B C   1 
ATOM   1284 O O   . LYS   B 1 71 ? 6.075   -16.205 -32.491 1.00 56.87  ? 70  LYS   B O   1 
ATOM   1285 C CB  . LYS   B 1 71 ? 4.564   -17.195 -34.847 1.00 45.70  ? 70  LYS   B CB  1 
ATOM   1286 C CG  . LYS   B 1 71 ? 3.735   -17.274 -36.108 1.00 59.73  ? 70  LYS   B CG  1 
ATOM   1287 C CD  . LYS   B 1 71 ? 4.365   -18.169 -37.163 1.00 62.66  ? 70  LYS   B CD  1 
ATOM   1288 C CE  . LYS   B 1 71 ? 3.328   -18.587 -38.146 1.00 67.47  ? 70  LYS   B CE  1 
ATOM   1289 N NZ  . LYS   B 1 71 ? 3.832   -19.618 -39.057 1.00 70.62  ? 70  LYS   B NZ  1 
ATOM   1290 N N   . PRO   B 1 72 ? 4.515   -14.595 -32.860 1.00 59.56  ? 71  PRO   B N   1 
ATOM   1291 C CA  . PRO   B 1 72 ? 4.383   -14.231 -31.448 1.00 57.19  ? 71  PRO   B CA  1 
ATOM   1292 C C   . PRO   B 1 72 ? 4.075   -15.415 -30.533 1.00 55.16  ? 71  PRO   B C   1 
ATOM   1293 O O   . PRO   B 1 72 ? 3.345   -16.331 -30.910 1.00 50.59  ? 71  PRO   B O   1 
ATOM   1294 C CB  . PRO   B 1 72 ? 3.316   -13.099 -31.414 1.00 54.37  ? 71  PRO   B CB  1 
ATOM   1295 C CG  . PRO   B 1 72 ? 3.335   -12.563 -32.829 1.00 60.75  ? 71  PRO   B CG  1 
ATOM   1296 C CD  . PRO   B 1 72 ? 3.675   -13.753 -33.732 1.00 56.30  ? 71  PRO   B CD  1 
ATOM   1297 N N   . ASN   B 1 73 ? 4.723   -15.399 -29.359 1.00 54.27  ? 72  ASN   B N   1 
ATOM   1298 C CA  . ASN   B 1 73 ? 4.504   -16.353 -28.281 1.00 49.01  ? 72  ASN   B CA  1 
ATOM   1299 C C   . ASN   B 1 73 ? 4.474   -15.577 -26.959 1.00 55.22  ? 72  ASN   B C   1 
ATOM   1300 O O   . ASN   B 1 73 ? 4.490   -14.341 -26.947 1.00 56.62  ? 72  ASN   B O   1 
ATOM   1301 C CB  . ASN   B 1 73 ? 5.530   -17.477 -28.335 1.00 43.70  ? 72  ASN   B CB  1 
ATOM   1302 C CG  . ASN   B 1 73 ? 6.929   -16.944 -28.176 1.00 45.03  ? 72  ASN   B CG  1 
ATOM   1303 O OD1 . ASN   B 1 73 ? 7.160   -16.160 -27.248 1.00 38.57  ? 72  ASN   B OD1 1 
ATOM   1304 N ND2 . ASN   B 1 73 ? 7.854   -17.330 -29.051 1.00 41.99  ? 72  ASN   B ND2 1 
ATOM   1305 N N   . LYS   B 1 74 ? 4.465   -16.305 -25.841 1.00 48.88  ? 73  LYS   B N   1 
ATOM   1306 C CA  . LYS   B 1 74 ? 4.262   -15.675 -24.544 1.00 52.29  ? 73  LYS   B CA  1 
ATOM   1307 C C   . LYS   B 1 74 ? 5.572   -15.611 -23.741 1.00 46.47  ? 73  LYS   B C   1 
ATOM   1308 O O   . LYS   B 1 74 ? 5.552   -15.394 -22.537 1.00 49.19  ? 73  LYS   B O   1 
ATOM   1309 C CB  . LYS   B 1 74 ? 3.070   -16.389 -23.889 1.00 50.62  ? 73  LYS   B CB  1 
ATOM   1310 C CG  . LYS   B 1 74 ? 3.384   -17.836 -23.510 1.00 54.46  ? 73  LYS   B CG  1 
ATOM   1311 C CD  . LYS   B 1 74 ? 2.261   -18.869 -23.595 1.00 60.36  ? 73  LYS   B CD  1 
ATOM   1312 C CE  . LYS   B 1 74 ? 1.038   -18.576 -22.768 1.00 72.93  ? 73  LYS   B CE  1 
ATOM   1313 N NZ  . LYS   B 1 74 ? 0.185   -19.758 -22.605 1.00 74.06  ? 73  LYS   B NZ  1 
ATOM   1314 N N   . ARG   B 1 75 ? 6.723   -15.776 -24.403 1.00 36.53  ? 74  ARG   B N   1 
ATOM   1315 C CA  . ARG   B 1 75 ? 7.996   -15.628 -23.733 1.00 34.01  ? 74  ARG   B CA  1 
ATOM   1316 C C   . ARG   B 1 75 ? 8.339   -14.141 -23.614 1.00 40.77  ? 74  ARG   B C   1 
ATOM   1317 O O   . ARG   B 1 75 ? 8.163   -13.361 -24.551 1.00 39.52  ? 74  ARG   B O   1 
ATOM   1318 C CB  . ARG   B 1 75 ? 9.097   -16.441 -24.426 1.00 37.04  ? 74  ARG   B CB  1 
ATOM   1319 C CG  . ARG   B 1 75 ? 8.895   -17.942 -24.587 1.00 33.66  ? 74  ARG   B CG  1 
ATOM   1320 C CD  . ARG   B 1 75 ? 8.736   -18.736 -23.288 1.00 39.64  ? 74  ARG   B CD  1 
ATOM   1321 N NE  . ARG   B 1 75 ? 8.994   -20.164 -23.513 1.00 35.45  ? 74  ARG   B NE  1 
ATOM   1322 C CZ  . ARG   B 1 75 ? 10.191  -20.718 -23.376 1.00 35.56  ? 74  ARG   B CZ  1 
ATOM   1323 N NH1 . ARG   B 1 75 ? 11.256  -20.000 -23.035 1.00 40.83  ? 74  ARG   B NH1 1 
ATOM   1324 N NH2 . ARG   B 1 75 ? 10.339  -22.008 -23.609 1.00 34.14  ? 74  ARG   B NH2 1 
ATOM   1325 N N   . LYS   B 1 76 ? 8.815   -13.749 -22.419 1.00 40.02  ? 75  LYS   B N   1 
ATOM   1326 C CA  . LYS   B 1 76 ? 9.099   -12.364 -22.107 1.00 35.43  ? 75  LYS   B CA  1 
ATOM   1327 C C   . LYS   B 1 76 ? 10.184  -11.831 -23.049 1.00 32.36  ? 75  LYS   B C   1 
ATOM   1328 O O   . LYS   B 1 76 ? 11.287  -12.395 -23.101 1.00 30.79  ? 75  LYS   B O   1 
ATOM   1329 C CB  . LYS   B 1 76 ? 9.644   -12.317 -20.673 1.00 35.44  ? 75  LYS   B CB  1 
ATOM   1330 C CG  . LYS   B 1 76 ? 9.933   -10.888 -20.212 1.00 39.22  ? 75  LYS   B CG  1 
ATOM   1331 C CD  . LYS   B 1 76 ? 10.530  -10.830 -18.812 1.00 44.08  ? 75  LYS   B CD  1 
ATOM   1332 C CE  . LYS   B 1 76 ? 10.924  -9.436  -18.430 1.00 51.69  ? 75  LYS   B CE  1 
ATOM   1333 N NZ  . LYS   B 1 76 ? 10.821  -9.259  -16.974 1.00 56.50  ? 75  LYS   B NZ  1 
ATOM   1334 N N   . GLY   B 1 77 ? 9.875   -10.717 -23.718 1.00 28.93  ? 76  GLY   B N   1 
ATOM   1335 C CA  . GLY   B 1 77 ? 10.808  -10.003 -24.586 1.00 31.01  ? 76  GLY   B CA  1 
ATOM   1336 C C   . GLY   B 1 77 ? 10.715  -10.436 -26.058 1.00 36.01  ? 76  GLY   B C   1 
ATOM   1337 O O   . GLY   B 1 77 ? 11.325  -9.826  -26.921 1.00 34.29  ? 76  GLY   B O   1 
ATOM   1338 N N   . PHE   B 1 78 ? 9.902   -11.457 -26.373 1.00 38.46  ? 77  PHE   B N   1 
ATOM   1339 C CA  . PHE   B 1 78 ? 9.893   -12.044 -27.703 1.00 32.29  ? 77  PHE   B CA  1 
ATOM   1340 C C   . PHE   B 1 78 ? 9.170   -11.125 -28.661 1.00 33.73  ? 77  PHE   B C   1 
ATOM   1341 O O   . PHE   B 1 78 ? 9.654   -10.884 -29.761 1.00 31.33  ? 77  PHE   B O   1 
ATOM   1342 C CB  . PHE   B 1 78 ? 9.059   -13.315 -27.789 1.00 29.64  ? 77  PHE   B CB  1 
ATOM   1343 C CG  . PHE   B 1 78 ? 9.384   -14.117 -29.030 1.00 33.07  ? 77  PHE   B CG  1 
ATOM   1344 C CD1 . PHE   B 1 78 ? 10.519  -14.928 -29.066 1.00 34.31  ? 77  PHE   B CD1 1 
ATOM   1345 C CD2 . PHE   B 1 78 ? 8.550   -14.067 -30.137 1.00 39.33  ? 77  PHE   B CD2 1 
ATOM   1346 C CE1 . PHE   B 1 78 ? 10.815  -15.663 -30.194 1.00 33.93  ? 77  PHE   B CE1 1 
ATOM   1347 C CE2 . PHE   B 1 78 ? 8.862   -14.798 -31.273 1.00 42.49  ? 77  PHE   B CE2 1 
ATOM   1348 C CZ  . PHE   B 1 78 ? 9.988   -15.599 -31.291 1.00 38.10  ? 77  PHE   B CZ  1 
ATOM   1349 N N   . ASN   B 1 79 ? 8.003   -10.631 -28.248 1.00 31.96  ? 78  ASN   B N   1 
ATOM   1350 C CA  . ASN   B 1 79 ? 7.317   -9.769  -29.192 1.00 35.49  ? 78  ASN   B CA  1 
ATOM   1351 C C   . ASN   B 1 79 ? 8.107   -8.477  -29.371 1.00 37.93  ? 78  ASN   B C   1 
ATOM   1352 O O   . ASN   B 1 79 ? 8.084   -7.882  -30.443 1.00 42.52  ? 78  ASN   B O   1 
ATOM   1353 C CB  . ASN   B 1 79 ? 5.847   -9.573  -28.848 1.00 42.16  ? 78  ASN   B CB  1 
ATOM   1354 C CG  . ASN   B 1 79 ? 5.071   -10.866 -28.954 1.00 45.56  ? 78  ASN   B CG  1 
ATOM   1355 O OD1 . ASN   B 1 79 ? 5.620   -11.922 -29.282 1.00 49.98  ? 78  ASN   B OD1 1 
ATOM   1356 N ND2 . ASN   B 1 79 ? 3.795   -10.824 -28.639 1.00 48.25  ? 78  ASN   B ND2 1 
ATOM   1357 N N   . GLU   B 1 80 ? 8.816   -8.043  -28.329 1.00 36.19  ? 79  GLU   B N   1 
ATOM   1358 C CA  . GLU   B 1 80 ? 9.602   -6.835  -28.508 1.00 38.99  ? 79  GLU   B CA  1 
ATOM   1359 C C   . GLU   B 1 80 ? 10.766  -7.102  -29.465 1.00 35.44  ? 79  GLU   B C   1 
ATOM   1360 O O   . GLU   B 1 80 ? 11.153  -6.197  -30.189 1.00 40.58  ? 79  GLU   B O   1 
ATOM   1361 C CB  . GLU   B 1 80 ? 10.068  -6.197  -27.200 1.00 32.08  ? 79  GLU   B CB  1 
ATOM   1362 C CG  . GLU   B 1 80 ? 8.927   -5.500  -26.465 1.00 46.65  ? 79  GLU   B CG  1 
ATOM   1363 N N   . GLY   B 1 81 ? 11.330  -8.322  -29.409 1.00 33.99  ? 80  GLY   B N   1 
ATOM   1364 C CA  . GLY   B 1 81 ? 12.398  -8.803  -30.266 1.00 32.11  ? 80  GLY   B CA  1 
ATOM   1365 C C   . GLY   B 1 81 ? 11.926  -8.783  -31.721 1.00 35.32  ? 80  GLY   B C   1 
ATOM   1366 O O   . GLY   B 1 81 ? 12.651  -8.355  -32.602 1.00 33.58  ? 80  GLY   B O   1 
ATOM   1367 N N   . LEU   B 1 82 ? 10.675  -9.194  -31.940 1.00 30.66  ? 81  LEU   B N   1 
ATOM   1368 C CA  . LEU   B 1 82 ? 10.098  -9.188  -33.265 1.00 36.71  ? 81  LEU   B CA  1 
ATOM   1369 C C   . LEU   B 1 82 ? 9.976   -7.751  -33.736 1.00 37.76  ? 81  LEU   B C   1 
ATOM   1370 O O   . LEU   B 1 82 ? 10.337  -7.457  -34.877 1.00 43.97  ? 81  LEU   B O   1 
ATOM   1371 C CB  . LEU   B 1 82 ? 8.776   -9.947  -33.366 1.00 30.81  ? 81  LEU   B CB  1 
ATOM   1372 C CG  . LEU   B 1 82 ? 8.901   -11.446 -33.081 1.00 31.84  ? 81  LEU   B CG  1 
ATOM   1373 C CD1 . LEU   B 1 82 ? 7.547   -12.117 -33.101 1.00 33.53  ? 81  LEU   B CD1 1 
ATOM   1374 C CD2 . LEU   B 1 82 ? 9.844   -12.098 -34.057 1.00 27.22  ? 81  LEU   B CD2 1 
ATOM   1375 N N   . TRP   B 1 83 ? 9.498   -6.870  -32.856 1.00 30.10  ? 82  TRP   B N   1 
ATOM   1376 C CA  . TRP   B 1 83 ? 9.418   -5.482  -33.258 1.00 34.54  ? 82  TRP   B CA  1 
ATOM   1377 C C   . TRP   B 1 83 ? 10.794  -4.963  -33.694 1.00 36.84  ? 82  TRP   B C   1 
ATOM   1378 O O   . TRP   B 1 83 ? 10.886  -4.318  -34.743 1.00 38.39  ? 82  TRP   B O   1 
ATOM   1379 C CB  . TRP   B 1 83 ? 8.792   -4.585  -32.185 1.00 35.76  ? 82  TRP   B CB  1 
ATOM   1380 C CG  . TRP   B 1 83 ? 8.559   -3.199  -32.721 1.00 40.39  ? 82  TRP   B CG  1 
ATOM   1381 C CD1 . TRP   B 1 83 ? 7.434   -2.769  -33.355 1.00 40.39  ? 82  TRP   B CD1 1 
ATOM   1382 C CD2 . TRP   B 1 83 ? 9.491   -2.091  -32.748 1.00 40.80  ? 82  TRP   B CD2 1 
ATOM   1383 N NE1 . TRP   B 1 83 ? 7.590   -1.468  -33.743 1.00 39.97  ? 82  TRP   B NE1 1 
ATOM   1384 C CE2 . TRP   B 1 83 ? 8.833   -1.024  -33.392 1.00 37.55  ? 82  TRP   B CE2 1 
ATOM   1385 C CE3 . TRP   B 1 83 ? 10.800  -1.888  -32.281 1.00 45.62  ? 82  TRP   B CE3 1 
ATOM   1386 C CZ2 . TRP   B 1 83 ? 9.435   0.222   -33.588 1.00 42.34  ? 82  TRP   B CZ2 1 
ATOM   1387 C CZ3 . TRP   B 1 83 ? 11.400  -0.655  -32.470 1.00 50.87  ? 82  TRP   B CZ3 1 
ATOM   1388 C CH2 . TRP   B 1 83 ? 10.726  0.387   -33.121 1.00 44.30  ? 82  TRP   B CH2 1 
ATOM   1389 N N   . GLU   B 1 84 ? 11.848  -5.276  -32.912 1.00 34.14  ? 83  GLU   B N   1 
ATOM   1390 C CA  . GLU   B 1 84 ? 13.178  -4.698  -33.096 1.00 33.72  ? 83  GLU   B CA  1 
ATOM   1391 C C   . GLU   B 1 84 ? 13.833  -5.126  -34.417 1.00 34.69  ? 83  GLU   B C   1 
ATOM   1392 O O   . GLU   B 1 84 ? 14.422  -4.299  -35.150 1.00 29.55  ? 83  GLU   B O   1 
ATOM   1393 C CB  . GLU   B 1 84 ? 14.123  -5.024  -31.945 1.00 32.55  ? 83  GLU   B CB  1 
ATOM   1394 C CG  . GLU   B 1 84 ? 13.729  -4.330  -30.647 1.00 35.14  ? 83  GLU   B CG  1 
ATOM   1395 C CD  . GLU   B 1 84 ? 14.554  -4.657  -29.416 1.00 34.65  ? 83  GLU   B CD  1 
ATOM   1396 O OE1 . GLU   B 1 84 ? 15.541  -5.426  -29.475 1.00 35.82  ? 83  GLU   B OE1 1 
ATOM   1397 O OE2 . GLU   B 1 84 ? 14.192  -4.105  -28.354 1.00 37.80  ? 83  GLU   B OE2 1 
ATOM   1398 N N   . ILE   B 1 85 ? 13.743  -6.431  -34.705 1.00 34.54  ? 84  ILE   B N   1 
ATOM   1399 C CA  . ILE   B 1 85 ? 14.448  -6.995  -35.841 1.00 34.18  ? 84  ILE   B CA  1 
ATOM   1400 C C   . ILE   B 1 85 ? 13.759  -6.481  -37.105 1.00 37.51  ? 84  ILE   B C   1 
ATOM   1401 O O   . ILE   B 1 85 ? 14.377  -6.367  -38.169 1.00 34.57  ? 84  ILE   B O   1 
ATOM   1402 C CB  . ILE   B 1 85 ? 14.451  -8.532  -35.777 1.00 33.40  ? 84  ILE   B CB  1 
ATOM   1403 C CG1 . ILE   B 1 85 ? 15.467  -9.114  -36.756 1.00 31.86  ? 84  ILE   B CG1 1 
ATOM   1404 C CG2 . ILE   B 1 85 ? 13.055  -9.123  -36.008 1.00 31.04  ? 84  ILE   B CG2 1 
ATOM   1405 C CD1 . ILE   B 1 85 ? 15.671  -10.614 -36.599 1.00 26.87  ? 84  ILE   B CD1 1 
ATOM   1406 N N   . GLN   B 1 86 ? 12.470  -6.149  -36.970 1.00 36.44  ? 85  GLN   B N   1 
ATOM   1407 C CA  . GLN   B 1 86 ? 11.668  -5.732  -38.110 1.00 34.41  ? 85  GLN   B CA  1 
ATOM   1408 C C   . GLN   B 1 86 ? 11.827  -4.229  -38.345 1.00 40.71  ? 85  GLN   B C   1 
ATOM   1409 O O   . GLN   B 1 86 ? 11.875  -3.797  -39.491 1.00 47.36  ? 85  GLN   B O   1 
ATOM   1410 C CB  . GLN   B 1 86 ? 10.217  -6.183  -37.940 1.00 36.25  ? 85  GLN   B CB  1 
ATOM   1411 N N   . ASN   B 1 87 ? 11.972  -3.431  -37.277 1.00 37.07  ? 86  ASN   B N   1 
ATOM   1412 C CA  . ASN   B 1 87 ? 11.820  -1.987  -37.403 1.00 34.20  ? 86  ASN   B CA  1 
ATOM   1413 C C   . ASN   B 1 87 ? 13.138  -1.227  -37.244 1.00 32.57  ? 86  ASN   B C   1 
ATOM   1414 O O   . ASN   B 1 87 ? 13.251  -0.101  -37.744 1.00 34.32  ? 86  ASN   B O   1 
ATOM   1415 C CB  . ASN   B 1 87 ? 10.764  -1.466  -36.428 1.00 36.14  ? 86  ASN   B CB  1 
ATOM   1416 C CG  . ASN   B 1 87 ? 9.384   -1.824  -36.920 1.00 39.54  ? 86  ASN   B CG  1 
ATOM   1417 O OD1 . ASN   B 1 87 ? 8.838   -1.085  -37.735 1.00 47.06  ? 86  ASN   B OD1 1 
ATOM   1418 N ND2 . ASN   B 1 87 ? 8.825   -2.950  -36.494 1.00 35.48  ? 86  ASN   B ND2 1 
ATOM   1419 N N   . ASN   B 1 88 ? 14.105  -1.798  -36.515 1.00 32.13  ? 87  ASN   B N   1 
ATOM   1420 C CA  . ASN   B 1 88 ? 15.385  -1.122  -36.317 1.00 34.78  ? 87  ASN   B CA  1 
ATOM   1421 C C   . ASN   B 1 88 ? 16.477  -2.123  -35.915 1.00 34.26  ? 87  ASN   B C   1 
ATOM   1422 O O   . ASN   B 1 88 ? 17.090  -2.023  -34.844 1.00 33.02  ? 87  ASN   B O   1 
ATOM   1423 C CB  . ASN   B 1 88 ? 15.254  0.082   -35.384 1.00 36.54  ? 87  ASN   B CB  1 
ATOM   1424 C CG  . ASN   B 1 88 ? 16.387  1.072   -35.564 1.00 41.23  ? 87  ASN   B CG  1 
ATOM   1425 O OD1 . ASN   B 1 88 ? 17.457  0.762   -36.112 1.00 37.44  ? 87  ASN   B OD1 1 
ATOM   1426 N ND2 . ASN   B 1 88 ? 16.184  2.282   -35.084 1.00 38.54  ? 87  ASN   B ND2 1 
ATOM   1427 N N   . PRO   B 1 89 ? 16.781  -3.135  -36.760 1.00 32.31  ? 88  PRO   B N   1 
ATOM   1428 C CA  . PRO   B 1 89 ? 17.751  -4.163  -36.374 1.00 29.71  ? 88  PRO   B CA  1 
ATOM   1429 C C   . PRO   B 1 89 ? 19.165  -3.680  -36.092 1.00 32.67  ? 88  PRO   B C   1 
ATOM   1430 O O   . PRO   B 1 89 ? 19.982  -4.440  -35.555 1.00 36.93  ? 88  PRO   B O   1 
ATOM   1431 C CB  . PRO   B 1 89 ? 17.732  -5.144  -37.557 1.00 26.67  ? 88  PRO   B CB  1 
ATOM   1432 C CG  . PRO   B 1 89 ? 17.288  -4.281  -38.738 1.00 28.22  ? 88  PRO   B CG  1 
ATOM   1433 C CD  . PRO   B 1 89 ? 16.207  -3.364  -38.104 1.00 31.44  ? 88  PRO   B CD  1 
ATOM   1434 N N   . HIS   B 1 90 ? 19.450  -2.434  -36.487 1.00 32.90  ? 89  HIS   B N   1 
ATOM   1435 C CA  . HIS   B 1 90 ? 20.826  -1.951  -36.479 1.00 36.55  ? 89  HIS   B CA  1 
ATOM   1436 C C   . HIS   B 1 90 ? 21.064  -0.940  -35.361 1.00 33.56  ? 89  HIS   B C   1 
ATOM   1437 O O   . HIS   B 1 90 ? 22.185  -0.471  -35.189 1.00 36.34  ? 89  HIS   B O   1 
ATOM   1438 C CB  . HIS   B 1 90 ? 21.285  -1.557  -37.895 1.00 32.99  ? 89  HIS   B CB  1 
ATOM   1439 C CG  . HIS   B 1 90 ? 21.240  -2.733  -38.831 1.00 36.21  ? 89  HIS   B CG  1 
ATOM   1440 N ND1 . HIS   B 1 90 ? 21.967  -3.896  -38.620 1.00 30.98  ? 89  HIS   B ND1 1 
ATOM   1441 C CD2 . HIS   B 1 90 ? 20.462  -2.956  -39.927 1.00 31.55  ? 89  HIS   B CD2 1 
ATOM   1442 C CE1 . HIS   B 1 90 ? 21.680  -4.763  -39.593 1.00 33.17  ? 89  HIS   B CE1 1 
ATOM   1443 N NE2 . HIS   B 1 90 ? 20.772  -4.205  -40.400 1.00 33.69  ? 89  HIS   B NE2 1 
ATOM   1444 N N   . ALA   B 1 91 ? 20.050  -0.703  -34.532 1.00 35.37  ? 90  ALA   B N   1 
ATOM   1445 C CA  . ALA   B 1 91 ? 20.155  0.316   -33.491 1.00 37.36  ? 90  ALA   B CA  1 
ATOM   1446 C C   . ALA   B 1 91 ? 21.116  -0.115  -32.389 1.00 36.12  ? 90  ALA   B C   1 
ATOM   1447 O O   . ALA   B 1 91 ? 21.409  -1.295  -32.228 1.00 35.21  ? 90  ALA   B O   1 
ATOM   1448 C CB  . ALA   B 1 91 ? 18.782  0.627   -32.921 1.00 34.17  ? 90  ALA   B CB  1 
ATOM   1449 N N   . SER   B 1 92 ? 21.617  0.870   -31.643 1.00 39.01  ? 91  SER   B N   1 
ATOM   1450 C CA  . SER   B 1 92 ? 22.264  0.653   -30.357 1.00 44.22  ? 91  SER   B CA  1 
ATOM   1451 C C   . SER   B 1 92 ? 21.181  0.429   -29.290 1.00 47.12  ? 91  SER   B C   1 
ATOM   1452 O O   . SER   B 1 92 ? 20.185  1.154   -29.277 1.00 48.41  ? 91  SER   B O   1 
ATOM   1453 C CB  . SER   B 1 92 ? 23.140  1.834   -30.029 1.00 49.50  ? 91  SER   B CB  1 
ATOM   1454 O OG  . SER   B 1 92 ? 23.542  1.774   -28.669 1.00 63.37  ? 91  SER   B OG  1 
ATOM   1455 N N   . TYR   B 1 93 ? 21.340  -0.620  -28.461 1.00 43.31  ? 92  TYR   B N   1 
ATOM   1456 C CA  . TYR   B 1 93 ? 20.367  -1.058  -27.457 1.00 45.30  ? 92  TYR   B CA  1 
ATOM   1457 C C   . TYR   B 1 93 ? 21.067  -1.142  -26.099 1.00 49.36  ? 92  TYR   B C   1 
ATOM   1458 O O   . TYR   B 1 93 ? 20.504  -1.660  -25.145 1.00 56.13  ? 92  TYR   B O   1 
ATOM   1459 C CB  . TYR   B 1 93 ? 19.703  -2.413  -27.785 1.00 34.74  ? 92  TYR   B CB  1 
ATOM   1460 C CG  . TYR   B 1 93 ? 18.707  -2.354  -28.929 1.00 32.47  ? 92  TYR   B CG  1 
ATOM   1461 C CD1 . TYR   B 1 93 ? 17.420  -1.879  -28.734 1.00 36.15  ? 92  TYR   B CD1 1 
ATOM   1462 C CD2 . TYR   B 1 93 ? 19.067  -2.735  -30.215 1.00 33.66  ? 92  TYR   B CD2 1 
ATOM   1463 C CE1 . TYR   B 1 93 ? 16.514  -1.786  -29.780 1.00 35.76  ? 92  TYR   B CE1 1 
ATOM   1464 C CE2 . TYR   B 1 93 ? 18.167  -2.670  -31.262 1.00 30.16  ? 92  TYR   B CE2 1 
ATOM   1465 C CZ  . TYR   B 1 93 ? 16.894  -2.181  -31.050 1.00 32.60  ? 92  TYR   B CZ  1 
ATOM   1466 O OH  . TYR   B 1 93 ? 16.014  -2.125  -32.090 1.00 28.10  ? 92  TYR   B OH  1 
ATOM   1467 N N   . SER   B 1 94 ? 22.305  -0.633  -26.050 1.00 66.93  ? 93  SER   B N   1 
ATOM   1468 C CA  . SER   B 1 94 ? 23.180  -0.524  -24.889 1.00 80.03  ? 93  SER   B CA  1 
ATOM   1469 C C   . SER   B 1 94 ? 22.465  0.160   -23.714 1.00 91.04  ? 93  SER   B C   1 
ATOM   1470 O O   . SER   B 1 94 ? 21.414  0.800   -23.966 1.00 97.61  ? 93  SER   B O   1 
ATOM   1471 C CB  . SER   B 1 94 ? 24.408  0.283   -25.228 1.00 80.64  ? 93  SER   B CB  1 
ATOM   1472 O OG  . SER   B 1 94 ? 24.994  -0.107  -26.461 1.00 88.49  ? 93  SER   B OG  1 
ATOM   1473 O OXT . SER   B 1 94 ? 23.020  0.074   -22.590 1.00 95.67  ? 93  SER   B OXT 1 
ATOM   1474 N N   . HIS   C 1 4  ? 33.003  -23.480 26.464  1.00 80.19  ? 3   HIS   C N   1 
ATOM   1475 C CA  . HIS   C 1 4  ? 31.904  -22.535 26.802  1.00 91.07  ? 3   HIS   C CA  1 
ATOM   1476 C C   . HIS   C 1 4  ? 31.372  -22.865 28.202  1.00 93.12  ? 3   HIS   C C   1 
ATOM   1477 O O   . HIS   C 1 4  ? 32.088  -23.457 29.014  1.00 91.36  ? 3   HIS   C O   1 
ATOM   1478 C CB  . HIS   C 1 4  ? 30.882  -22.513 25.651  1.00 96.77  ? 3   HIS   C CB  1 
ATOM   1479 C CG  . HIS   C 1 4  ? 29.925  -21.355 25.657  1.00 104.26 ? 3   HIS   C CG  1 
ATOM   1480 N ND1 . HIS   C 1 4  ? 28.583  -21.482 25.949  1.00 106.50 ? 3   HIS   C ND1 1 
ATOM   1481 C CD2 . HIS   C 1 4  ? 30.115  -20.054 25.379  1.00 102.90 ? 3   HIS   C CD2 1 
ATOM   1482 C CE1 . HIS   C 1 4  ? 27.997  -20.294 25.870  1.00 109.24 ? 3   HIS   C CE1 1 
ATOM   1483 N NE2 . HIS   C 1 4  ? 28.912  -19.410 25.530  1.00 104.30 ? 3   HIS   C NE2 1 
ATOM   1484 N N   . ALA   C 1 5  ? 30.119  -22.450 28.464  1.00 81.88  ? 4   ALA   C N   1 
ATOM   1485 C CA  . ALA   C 1 5  ? 29.334  -22.774 29.647  1.00 72.93  ? 4   ALA   C CA  1 
ATOM   1486 C C   . ALA   C 1 5  ? 27.841  -22.652 29.338  1.00 82.02  ? 4   ALA   C C   1 
ATOM   1487 O O   . ALA   C 1 5  ? 27.406  -21.713 28.659  1.00 81.86  ? 4   ALA   C O   1 
ATOM   1488 C CB  . ALA   C 1 5  ? 29.691  -21.802 30.724  1.00 82.40  ? 4   ALA   C CB  1 
ATOM   1489 N N   . PHE   C 1 6  ? 27.047  -23.584 29.878  1.00 71.95  ? 5   PHE   C N   1 
ATOM   1490 C CA  . PHE   C 1 6  ? 25.652  -23.671 29.476  1.00 70.20  ? 5   PHE   C CA  1 
ATOM   1491 C C   . PHE   C 1 6  ? 24.785  -23.724 30.722  1.00 79.55  ? 5   PHE   C C   1 
ATOM   1492 O O   . PHE   C 1 6  ? 25.084  -24.494 31.627  1.00 94.46  ? 5   PHE   C O   1 
ATOM   1493 C CB  . PHE   C 1 6  ? 25.429  -24.922 28.614  1.00 57.94  ? 5   PHE   C CB  1 
ATOM   1494 C CG  . PHE   C 1 6  ? 26.213  -24.996 27.305  1.00 51.69  ? 5   PHE   C CG  1 
ATOM   1495 C CD1 . PHE   C 1 6  ? 27.220  -25.938 27.127  1.00 47.59  ? 5   PHE   C CD1 1 
ATOM   1496 C CD2 . PHE   C 1 6  ? 25.943  -24.128 26.247  1.00 50.45  ? 5   PHE   C CD2 1 
ATOM   1497 C CE1 . PHE   C 1 6  ? 27.925  -26.019 25.924  1.00 53.43  ? 5   PHE   C CE1 1 
ATOM   1498 C CE2 . PHE   C 1 6  ? 26.650  -24.206 25.053  1.00 51.39  ? 5   PHE   C CE2 1 
ATOM   1499 C CZ  . PHE   C 1 6  ? 27.636  -25.156 24.893  1.00 51.54  ? 5   PHE   C CZ  1 
ATOM   1500 N N   . LYS   C 1 7  ? 23.725  -22.906 30.757  1.00 74.83  ? 6   LYS   C N   1 
ATOM   1501 C CA  . LYS   C 1 7  ? 22.767  -22.934 31.857  1.00 73.80  ? 6   LYS   C CA  1 
ATOM   1502 C C   . LYS   C 1 7  ? 21.388  -23.284 31.292  1.00 71.67  ? 6   LYS   C C   1 
ATOM   1503 O O   . LYS   C 1 7  ? 21.163  -23.136 30.094  1.00 80.17  ? 6   LYS   C O   1 
ATOM   1504 C CB  . LYS   C 1 7  ? 22.858  -21.644 32.690  1.00 71.77  ? 6   LYS   C CB  1 
ATOM   1505 C CG  . LYS   C 1 7  ? 21.708  -20.637 32.627  1.00 64.04  ? 6   LYS   C CG  1 
ATOM   1506 C CD  . LYS   C 1 7  ? 22.132  -19.227 32.232  1.00 59.46  ? 6   LYS   C CD  1 
ATOM   1507 N N   . PRO   C 1 8  ? 20.420  -23.777 32.100  1.00 68.09  ? 7   PRO   C N   1 
ATOM   1508 C CA  . PRO   C 1 8  ? 19.094  -24.117 31.564  1.00 68.99  ? 7   PRO   C CA  1 
ATOM   1509 C C   . PRO   C 1 8  ? 18.463  -22.976 30.761  1.00 73.05  ? 7   PRO   C C   1 
ATOM   1510 O O   . PRO   C 1 8  ? 18.820  -21.814 30.962  1.00 76.98  ? 7   PRO   C O   1 
ATOM   1511 C CB  . PRO   C 1 8  ? 18.274  -24.522 32.802  1.00 66.76  ? 7   PRO   C CB  1 
ATOM   1512 C CG  . PRO   C 1 8  ? 19.334  -24.955 33.795  1.00 61.86  ? 7   PRO   C CG  1 
ATOM   1513 C CD  . PRO   C 1 8  ? 20.555  -24.060 33.540  1.00 64.75  ? 7   PRO   C CD  1 
ATOM   1514 N N   . GLY   C 1 9  ? 17.578  -23.322 29.809  1.00 66.40  ? 8   GLY   C N   1 
ATOM   1515 C CA  . GLY   C 1 9  ? 16.938  -22.344 28.936  1.00 60.24  ? 8   GLY   C CA  1 
ATOM   1516 C C   . GLY   C 1 9  ? 17.783  -21.955 27.714  1.00 57.86  ? 8   GLY   C C   1 
ATOM   1517 O O   . GLY   C 1 9  ? 17.221  -21.561 26.693  1.00 70.35  ? 8   GLY   C O   1 
ATOM   1518 N N   . ASP   C 1 10 ? 19.120  -22.063 27.822  1.00 46.13  ? 9   ASP   C N   1 
ATOM   1519 C CA  . ASP   C 1 10 ? 20.072  -21.774 26.759  1.00 47.22  ? 9   ASP   C CA  1 
ATOM   1520 C C   . ASP   C 1 10 ? 19.756  -22.581 25.505  1.00 50.32  ? 9   ASP   C C   1 
ATOM   1521 O O   . ASP   C 1 10 ? 19.516  -23.787 25.562  1.00 51.57  ? 9   ASP   C O   1 
ATOM   1522 C CB  . ASP   C 1 10 ? 21.512  -22.040 27.172  1.00 46.97  ? 9   ASP   C CB  1 
ATOM   1523 C CG  . ASP   C 1 10 ? 22.163  -21.024 28.111  1.00 60.66  ? 9   ASP   C CG  1 
ATOM   1524 O OD1 . ASP   C 1 10 ? 21.429  -20.141 28.615  1.00 66.98  ? 9   ASP   C OD1 1 
ATOM   1525 O OD2 . ASP   C 1 10 ? 23.412  -21.108 28.334  1.00 63.56  ? 9   ASP   C OD2 1 
ATOM   1526 N N   . LEU   C 1 11 ? 19.815  -21.883 24.367  1.00 51.04  ? 10  LEU   C N   1 
ATOM   1527 C CA  . LEU   C 1 11 ? 19.473  -22.393 23.052  1.00 47.23  ? 10  LEU   C CA  1 
ATOM   1528 C C   . LEU   C 1 11 ? 20.748  -22.842 22.328  1.00 45.28  ? 10  LEU   C C   1 
ATOM   1529 O O   . LEU   C 1 11 ? 21.712  -22.089 22.263  1.00 39.32  ? 10  LEU   C O   1 
ATOM   1530 C CB  . LEU   C 1 11 ? 18.786  -21.244 22.309  1.00 43.51  ? 10  LEU   C CB  1 
ATOM   1531 C CG  . LEU   C 1 11 ? 17.476  -20.709 22.900  1.00 43.74  ? 10  LEU   C CG  1 
ATOM   1532 C CD1 . LEU   C 1 11 ? 16.796  -19.765 21.899  1.00 42.35  ? 10  LEU   C CD1 1 
ATOM   1533 C CD2 . LEU   C 1 11 ? 16.518  -21.835 23.321  1.00 39.69  ? 10  LEU   C CD2 1 
ATOM   1534 N N   . VAL   C 1 12 ? 20.724  -24.053 21.746  1.00 38.65  ? 11  VAL   C N   1 
ATOM   1535 C CA  . VAL   C 1 12 ? 21.895  -24.626 21.104  1.00 36.04  ? 11  VAL   C CA  1 
ATOM   1536 C C   . VAL   C 1 12 ? 21.465  -25.375 19.827  1.00 41.80  ? 11  VAL   C C   1 
ATOM   1537 O O   . VAL   C 1 12 ? 20.282  -25.593 19.565  1.00 38.96  ? 11  VAL   C O   1 
ATOM   1538 C CB  . VAL   C 1 12 ? 22.556  -25.615 22.094  1.00 37.86  ? 11  VAL   C CB  1 
ATOM   1539 C CG1 . VAL   C 1 12 ? 23.098  -24.978 23.374  1.00 34.30  ? 11  VAL   C CG1 1 
ATOM   1540 C CG2 . VAL   C 1 12 ? 21.616  -26.765 22.460  1.00 35.40  ? 11  VAL   C CG2 1 
ATOM   1541 N N   . PHE   C 1 13 ? 22.449  -25.797 19.028  1.00 37.60  ? 12  PHE   C N   1 
ATOM   1542 C CA  . PHE   C 1 13 ? 22.302  -26.972 18.196  1.00 36.02  ? 12  PHE   C CA  1 
ATOM   1543 C C   . PHE   C 1 13 ? 22.967  -28.124 18.936  1.00 36.93  ? 12  PHE   C C   1 
ATOM   1544 O O   . PHE   C 1 13 ? 24.069  -27.955 19.462  1.00 40.19  ? 12  PHE   C O   1 
ATOM   1545 C CB  . PHE   C 1 13 ? 22.896  -26.769 16.791  1.00 40.52  ? 12  PHE   C CB  1 
ATOM   1546 C CG  . PHE   C 1 13 ? 22.093  -25.783 15.958  1.00 43.07  ? 12  PHE   C CG  1 
ATOM   1547 C CD1 . PHE   C 1 13 ? 21.065  -26.221 15.127  1.00 40.00  ? 12  PHE   C CD1 1 
ATOM   1548 C CD2 . PHE   C 1 13 ? 22.313  -24.405 16.065  1.00 46.91  ? 12  PHE   C CD2 1 
ATOM   1549 C CE1 . PHE   C 1 13 ? 20.322  -25.304 14.395  1.00 40.30  ? 12  PHE   C CE1 1 
ATOM   1550 C CE2 . PHE   C 1 13 ? 21.552  -23.495 15.337  1.00 41.60  ? 12  PHE   C CE2 1 
ATOM   1551 C CZ  . PHE   C 1 13 ? 20.560  -23.952 14.506  1.00 44.38  ? 12  PHE   C CZ  1 
ATOM   1552 N N   . ALA   C 1 14 ? 22.315  -29.295 18.929  1.00 32.38  ? 13  ALA   C N   1 
ATOM   1553 C CA  . ALA   C 1 14 ? 22.820  -30.461 19.640  1.00 32.15  ? 13  ALA   C CA  1 
ATOM   1554 C C   . ALA   C 1 14 ? 23.049  -31.595 18.655  1.00 35.96  ? 13  ALA   C C   1 
ATOM   1555 O O   . ALA   C 1 14 ? 22.175  -31.903 17.843  1.00 35.46  ? 13  ALA   C O   1 
ATOM   1556 C CB  . ALA   C 1 14 ? 21.842  -30.898 20.716  1.00 33.92  ? 13  ALA   C CB  1 
ATOM   1557 N N   . LYS   C 1 15 ? 24.234  -32.207 18.748  1.00 35.44  ? 14  LYS   C N   1 
ATOM   1558 C CA  . LYS   C 1 15 ? 24.648  -33.200 17.774  1.00 38.26  ? 14  LYS   C CA  1 
ATOM   1559 C C   . LYS   C 1 15 ? 24.647  -34.548 18.468  1.00 35.71  ? 14  LYS   C C   1 
ATOM   1560 O O   . LYS   C 1 15 ? 25.364  -34.709 19.447  1.00 37.54  ? 14  LYS   C O   1 
ATOM   1561 C CB  . LYS   C 1 15 ? 26.089  -33.018 17.267  1.00 38.44  ? 14  LYS   C CB  1 
ATOM   1562 C CG  . LYS   C 1 15 ? 26.557  -34.080 16.240  1.00 34.63  ? 14  LYS   C CG  1 
ATOM   1563 C CD  . LYS   C 1 15 ? 25.766  -33.972 14.939  1.00 35.07  ? 14  LYS   C CD  1 
ATOM   1564 C CE  . LYS   C 1 15 ? 26.244  -34.846 13.805  1.00 33.37  ? 14  LYS   C CE  1 
ATOM   1565 N NZ  . LYS   C 1 15 ? 26.064  -36.254 14.189  1.00 28.38  ? 14  LYS   C NZ  1 
ATOM   1566 N N   . MET   C 1 16 ? 23.827  -35.472 17.971  1.00 36.10  ? 15  MET   C N   1 
ATOM   1567 C CA  . MET   C 1 16 ? 23.932  -36.875 18.340  1.00 37.19  ? 15  MET   C CA  1 
ATOM   1568 C C   . MET   C 1 16 ? 24.310  -37.667 17.090  1.00 41.96  ? 15  MET   C C   1 
ATOM   1569 O O   . MET   C 1 16 ? 24.038  -37.250 15.955  1.00 40.16  ? 15  MET   C O   1 
ATOM   1570 C CB  . MET   C 1 16 ? 22.603  -37.502 18.778  1.00 34.57  ? 15  MET   C CB  1 
ATOM   1571 C CG  . MET   C 1 16 ? 21.723  -36.646 19.643  1.00 41.08  ? 15  MET   C CG  1 
ATOM   1572 S SD  . MET   C 1 16 ? 20.575  -37.455 20.781  1.00 44.58  ? 15  MET   C SD  1 
ATOM   1573 C CE  . MET   C 1 16 ? 20.303  -39.109 20.121  1.00 50.92  ? 15  MET   C CE  1 
ATOM   1574 N N   . LYS   C 1 17 ? 24.845  -38.865 17.341  1.00 42.39  ? 16  LYS   C N   1 
ATOM   1575 C CA  . LYS   C 1 17 ? 25.269  -39.765 16.289  1.00 44.96  ? 16  LYS   C CA  1 
ATOM   1576 C C   . LYS   C 1 17 ? 24.045  -40.151 15.458  1.00 40.51  ? 16  LYS   C C   1 
ATOM   1577 O O   . LYS   C 1 17 ? 23.038  -40.610 15.994  1.00 36.62  ? 16  LYS   C O   1 
ATOM   1578 C CB  . LYS   C 1 17 ? 25.845  -41.011 16.974  1.00 42.74  ? 16  LYS   C CB  1 
ATOM   1579 C CG  . LYS   C 1 17 ? 26.593  -41.967 16.054  1.00 47.69  ? 16  LYS   C CG  1 
ATOM   1580 C CD  . LYS   C 1 17 ? 27.770  -41.342 15.313  1.00 51.94  ? 16  LYS   C CD  1 
ATOM   1581 C CE  . LYS   C 1 17 ? 28.360  -42.296 14.317  1.00 66.60  ? 16  LYS   C CE  1 
ATOM   1582 N NZ  . LYS   C 1 17 ? 29.542  -41.724 13.665  1.00 59.84  ? 16  LYS   C NZ  1 
ATOM   1583 N N   . GLY   C 1 18 ? 24.161  -39.997 14.140  1.00 37.83  ? 17  GLY   C N   1 
ATOM   1584 C CA  . GLY   C 1 18 ? 23.107  -40.459 13.251  1.00 39.93  ? 17  GLY   C CA  1 
ATOM   1585 C C   . GLY   C 1 18 ? 22.062  -39.373 12.983  1.00 35.93  ? 17  GLY   C C   1 
ATOM   1586 O O   . GLY   C 1 18 ? 21.014  -39.654 12.419  1.00 35.38  ? 17  GLY   C O   1 
ATOM   1587 N N   . TYR   C 1 19 ? 22.370  -38.133 13.377  1.00 36.43  ? 18  TYR   C N   1 
ATOM   1588 C CA  . TYR   C 1 19 ? 21.459  -37.007 13.274  1.00 34.22  ? 18  TYR   C CA  1 
ATOM   1589 C C   . TYR   C 1 19 ? 22.276  -35.769 12.928  1.00 34.50  ? 18  TYR   C C   1 
ATOM   1590 O O   . TYR   C 1 19 ? 23.417  -35.620 13.358  1.00 34.42  ? 18  TYR   C O   1 
ATOM   1591 C CB  . TYR   C 1 19 ? 20.703  -36.754 14.583  1.00 32.65  ? 18  TYR   C CB  1 
ATOM   1592 C CG  . TYR   C 1 19 ? 19.845  -37.941 14.966  1.00 33.16  ? 18  TYR   C CG  1 
ATOM   1593 C CD1 . TYR   C 1 19 ? 20.385  -39.031 15.641  1.00 32.08  ? 18  TYR   C CD1 1 
ATOM   1594 C CD2 . TYR   C 1 19 ? 18.496  -37.964 14.642  1.00 38.88  ? 18  TYR   C CD2 1 
ATOM   1595 C CE1 . TYR   C 1 19 ? 19.613  -40.133 15.947  1.00 36.68  ? 18  TYR   C CE1 1 
ATOM   1596 C CE2 . TYR   C 1 19 ? 17.709  -39.054 14.961  1.00 41.28  ? 18  TYR   C CE2 1 
ATOM   1597 C CZ  . TYR   C 1 19 ? 18.274  -40.143 15.595  1.00 45.05  ? 18  TYR   C CZ  1 
ATOM   1598 O OH  . TYR   C 1 19 ? 17.465  -41.198 15.888  1.00 44.17  ? 18  TYR   C OH  1 
ATOM   1599 N N   . PRO   C 1 20 ? 21.708  -34.848 12.131  1.00 33.51  ? 19  PRO   C N   1 
ATOM   1600 C CA  . PRO   C 1 20 ? 22.343  -33.541 11.933  1.00 31.74  ? 19  PRO   C CA  1 
ATOM   1601 C C   . PRO   C 1 20 ? 22.303  -32.733 13.234  1.00 29.85  ? 19  PRO   C C   1 
ATOM   1602 O O   . PRO   C 1 20 ? 21.541  -33.062 14.167  1.00 25.37  ? 19  PRO   C O   1 
ATOM   1603 C CB  . PRO   C 1 20 ? 21.481  -32.898 10.806  1.00 33.54  ? 19  PRO   C CB  1 
ATOM   1604 C CG  . PRO   C 1 20 ? 20.131  -33.593 10.914  1.00 31.66  ? 19  PRO   C CG  1 
ATOM   1605 C CD  . PRO   C 1 20 ? 20.410  -35.006 11.440  1.00 33.50  ? 19  PRO   C CD  1 
ATOM   1606 N N   . HIS   C 1 21 ? 23.154  -31.694 13.287  1.00 29.70  ? 20  HIS   C N   1 
ATOM   1607 C CA  . HIS   C 1 21 ? 23.089  -30.694 14.353  1.00 35.11  ? 20  HIS   C CA  1 
ATOM   1608 C C   . HIS   C 1 21 ? 21.650  -30.180 14.467  1.00 35.81  ? 20  HIS   C C   1 
ATOM   1609 O O   . HIS   C 1 21 ? 21.089  -29.690 13.467  1.00 31.47  ? 20  HIS   C O   1 
ATOM   1610 C CB  . HIS   C 1 21 ? 24.098  -29.563 14.116  1.00 33.49  ? 20  HIS   C CB  1 
ATOM   1611 C CG  . HIS   C 1 21 ? 25.513  -30.048 14.081  1.00 34.68  ? 20  HIS   C CG  1 
ATOM   1612 N ND1 . HIS   C 1 21 ? 26.087  -30.662 12.989  1.00 41.08  ? 20  HIS   C ND1 1 
ATOM   1613 C CD2 . HIS   C 1 21 ? 26.471  -30.018 15.028  1.00 43.40  ? 20  HIS   C CD2 1 
ATOM   1614 C CE1 . HIS   C 1 21 ? 27.334  -31.006 13.283  1.00 45.40  ? 20  HIS   C CE1 1 
ATOM   1615 N NE2 . HIS   C 1 21 ? 27.592  -30.599 14.510  1.00 43.12  ? 20  HIS   C NE2 1 
ATOM   1616 N N   . TRP   C 1 22 ? 21.053  -30.368 15.669  1.00 34.23  ? 21  TRP   C N   1 
ATOM   1617 C CA  . TRP   C 1 22 ? 19.610  -30.252 15.868  1.00 34.23  ? 21  TRP   C CA  1 
ATOM   1618 C C   . TRP   C 1 22 ? 19.308  -29.044 16.757  1.00 33.49  ? 21  TRP   C C   1 
ATOM   1619 O O   . TRP   C 1 22 ? 19.981  -28.846 17.770  1.00 31.84  ? 21  TRP   C O   1 
ATOM   1620 C CB  . TRP   C 1 22 ? 19.003  -31.533 16.475  1.00 35.47  ? 21  TRP   C CB  1 
ATOM   1621 C CG  . TRP   C 1 22 ? 17.538  -31.739 16.137  1.00 37.58  ? 21  TRP   C CG  1 
ATOM   1622 C CD1 . TRP   C 1 22 ? 16.444  -31.119 16.693  1.00 30.66  ? 21  TRP   C CD1 1 
ATOM   1623 C CD2 . TRP   C 1 22 ? 17.015  -32.647 15.129  1.00 33.40  ? 21  TRP   C CD2 1 
ATOM   1624 N NE1 . TRP   C 1 22 ? 15.286  -31.549 16.080  1.00 32.15  ? 21  TRP   C NE1 1 
ATOM   1625 C CE2 . TRP   C 1 22 ? 15.603  -32.489 15.127  1.00 32.99  ? 21  TRP   C CE2 1 
ATOM   1626 C CE3 . TRP   C 1 22 ? 17.586  -33.573 14.236  1.00 32.15  ? 21  TRP   C CE3 1 
ATOM   1627 C CZ2 . TRP   C 1 22 ? 14.788  -33.249 14.280  1.00 32.12  ? 21  TRP   C CZ2 1 
ATOM   1628 C CZ3 . TRP   C 1 22 ? 16.776  -34.303 13.378  1.00 29.15  ? 21  TRP   C CZ3 1 
ATOM   1629 C CH2 . TRP   C 1 22 ? 15.384  -34.159 13.425  1.00 28.80  ? 21  TRP   C CH2 1 
ATOM   1630 N N   . PRO   C 1 23 ? 18.304  -28.206 16.408  1.00 29.48  ? 22  PRO   C N   1 
ATOM   1631 C CA  . PRO   C 1 23 ? 17.911  -27.081 17.265  1.00 31.83  ? 22  PRO   C CA  1 
ATOM   1632 C C   . PRO   C 1 23 ? 17.321  -27.616 18.573  1.00 31.95  ? 22  PRO   C C   1 
ATOM   1633 O O   . PRO   C 1 23 ? 16.502  -28.537 18.560  1.00 30.88  ? 22  PRO   C O   1 
ATOM   1634 C CB  . PRO   C 1 23 ? 16.870  -26.346 16.356  1.00 33.34  ? 22  PRO   C CB  1 
ATOM   1635 C CG  . PRO   C 1 23 ? 16.243  -27.487 15.531  1.00 30.63  ? 22  PRO   C CG  1 
ATOM   1636 C CD  . PRO   C 1 23 ? 17.520  -28.259 15.153  1.00 31.59  ? 22  PRO   C CD  1 
ATOM   1637 N N   . ALA   C 1 24 ? 17.766  -27.053 19.704  1.00 32.95  ? 23  ALA   C N   1 
ATOM   1638 C CA  . ALA   C 1 24 ? 17.486  -27.640 21.009  1.00 33.85  ? 23  ALA   C CA  1 
ATOM   1639 C C   . ALA   C 1 24 ? 17.722  -26.600 22.109  1.00 38.74  ? 23  ALA   C C   1 
ATOM   1640 O O   . ALA   C 1 24 ? 18.244  -25.503 21.848  1.00 41.50  ? 23  ALA   C O   1 
ATOM   1641 C CB  . ALA   C 1 24 ? 18.386  -28.872 21.198  1.00 28.93  ? 23  ALA   C CB  1 
ATOM   1642 N N   . ARG   C 1 25 ? 17.361  -26.952 23.354  1.00 41.28  ? 24  ARG   C N   1 
ATOM   1643 C CA  . ARG   C 1 25 ? 17.724  -26.090 24.471  1.00 40.24  ? 24  ARG   C CA  1 
ATOM   1644 C C   . ARG   C 1 25 ? 18.229  -26.914 25.654  1.00 40.42  ? 24  ARG   C C   1 
ATOM   1645 O O   . ARG   C 1 25 ? 17.852  -28.080 25.802  1.00 37.57  ? 24  ARG   C O   1 
ATOM   1646 C CB  . ARG   C 1 25 ? 16.526  -25.243 24.913  1.00 39.61  ? 24  ARG   C CB  1 
ATOM   1647 C CG  . ARG   C 1 25 ? 15.282  -26.023 25.302  1.00 43.44  ? 24  ARG   C CG  1 
ATOM   1648 C CD  . ARG   C 1 25 ? 14.269  -25.087 25.999  1.00 43.70  ? 24  ARG   C CD  1 
ATOM   1649 N NE  . ARG   C 1 25 ? 13.106  -25.847 26.486  1.00 50.80  ? 24  ARG   C NE  1 
ATOM   1650 C CZ  . ARG   C 1 25 ? 11.809  -25.674 26.212  1.00 55.51  ? 24  ARG   C CZ  1 
ATOM   1651 N NH1 . ARG   C 1 25 ? 11.400  -24.633 25.502  1.00 47.67  ? 24  ARG   C NH1 1 
ATOM   1652 N NH2 . ARG   C 1 25 ? 10.911  -26.546 26.659  1.00 52.63  ? 24  ARG   C NH2 1 
ATOM   1653 N N   . ILE   C 1 26 ? 19.023  -26.272 26.530  1.00 46.00  ? 25  ILE   C N   1 
ATOM   1654 C CA  . ILE   C 1 26 ? 19.402  -26.869 27.809  1.00 47.63  ? 25  ILE   C CA  1 
ATOM   1655 C C   . ILE   C 1 26 ? 18.175  -26.908 28.719  1.00 51.18  ? 25  ILE   C C   1 
ATOM   1656 O O   . ILE   C 1 26 ? 17.584  -25.872 29.032  1.00 54.91  ? 25  ILE   C O   1 
ATOM   1657 C CB  . ILE   C 1 26 ? 20.552  -26.138 28.528  1.00 45.05  ? 25  ILE   C CB  1 
ATOM   1658 C CG1 . ILE   C 1 26 ? 21.688  -25.695 27.619  1.00 47.74  ? 25  ILE   C CG1 1 
ATOM   1659 C CG2 . ILE   C 1 26 ? 21.062  -26.957 29.719  1.00 43.50  ? 25  ILE   C CG2 1 
ATOM   1660 C CD1 . ILE   C 1 26 ? 22.498  -26.817 27.022  1.00 42.19  ? 25  ILE   C CD1 1 
ATOM   1661 N N   . ASP   C 1 27 ? 17.812  -28.115 29.153  1.00 52.35  ? 26  ASP   C N   1 
ATOM   1662 C CA  . ASP   C 1 27 ? 16.737  -28.276 30.118  1.00 62.05  ? 26  ASP   C CA  1 
ATOM   1663 C C   . ASP   C 1 27 ? 17.246  -28.127 31.554  1.00 69.94  ? 26  ASP   C C   1 
ATOM   1664 O O   . ASP   C 1 27 ? 18.383  -27.716 31.777  1.00 64.90  ? 26  ASP   C O   1 
ATOM   1665 C CB  . ASP   C 1 27 ? 15.965  -29.556 29.857  1.00 61.63  ? 26  ASP   C CB  1 
ATOM   1666 C CG  . ASP   C 1 27 ? 14.581  -29.330 29.279  1.00 67.63  ? 26  ASP   C CG  1 
ATOM   1667 O OD1 . ASP   C 1 27 ? 14.335  -28.190 28.789  1.00 59.86  ? 26  ASP   C OD1 1 
ATOM   1668 O OD2 . ASP   C 1 27 ? 13.752  -30.267 29.399  1.00 70.08  ? 26  ASP   C OD2 1 
ATOM   1669 N N   . ASP   C 1 28 ? 16.381  -28.440 32.529  1.00 79.97  ? 27  ASP   C N   1 
ATOM   1670 C CA  . ASP   C 1 28 ? 16.802  -28.418 33.921  1.00 89.50  ? 27  ASP   C CA  1 
ATOM   1671 C C   . ASP   C 1 28 ? 16.506  -29.776 34.553  1.00 87.71  ? 27  ASP   C C   1 
ATOM   1672 O O   . ASP   C 1 28 ? 15.446  -30.340 34.312  1.00 92.90  ? 27  ASP   C O   1 
ATOM   1673 C CB  . ASP   C 1 28 ? 16.279  -27.186 34.652  1.00 97.97  ? 27  ASP   C CB  1 
ATOM   1674 C CG  . ASP   C 1 28 ? 17.066  -26.758 35.889  1.00 100.55 ? 27  ASP   C CG  1 
ATOM   1675 O OD1 . ASP   C 1 28 ? 17.983  -27.503 36.302  1.00 101.66 ? 27  ASP   C OD1 1 
ATOM   1676 O OD2 . ASP   C 1 28 ? 16.776  -25.667 36.428  1.00 93.61  ? 27  ASP   C OD2 1 
ATOM   1677 N N   . ILE   C 1 29 ? 17.473  -30.292 35.330  1.00 89.84  ? 28  ILE   C N   1 
ATOM   1678 C CA  . ILE   C 1 29 ? 17.366  -31.540 36.075  1.00 89.72  ? 28  ILE   C CA  1 
ATOM   1679 C C   . ILE   C 1 29 ? 16.562  -31.249 37.336  1.00 93.25  ? 28  ILE   C C   1 
ATOM   1680 O O   . ILE   C 1 29 ? 16.732  -30.181 37.918  1.00 99.55  ? 28  ILE   C O   1 
ATOM   1681 C CB  . ILE   C 1 29 ? 18.764  -32.096 36.414  1.00 74.51  ? 28  ILE   C CB  1 
ATOM   1682 N N   . ALA   C 1 30 ? 15.700  -32.192 37.750  1.00 87.25  ? 29  ALA   C N   1 
ATOM   1683 C CA  . ALA   C 1 30 ? 14.800  -31.968 38.876  1.00 81.88  ? 29  ALA   C CA  1 
ATOM   1684 C C   . ALA   C 1 30 ? 15.518  -32.210 40.213  1.00 82.16  ? 29  ALA   C C   1 
ATOM   1685 O O   . ALA   C 1 30 ? 15.096  -33.077 41.030  1.00 100.71 ? 29  ALA   C O   1 
ATOM   1686 C CB  . ALA   C 1 30 ? 13.527  -32.773 38.709  1.00 75.54  ? 29  ALA   C CB  1 
ATOM   1687 N N   . LYS   C 1 35 ? 19.475  -37.854 37.939  1.00 91.05  ? 34  LYS   C N   1 
ATOM   1688 C CA  . LYS   C 1 35 ? 20.829  -37.254 37.801  1.00 77.30  ? 34  LYS   C CA  1 
ATOM   1689 C C   . LYS   C 1 35 ? 21.389  -37.625 36.427  1.00 80.41  ? 34  LYS   C C   1 
ATOM   1690 O O   . LYS   C 1 35 ? 21.392  -38.804 36.044  1.00 76.73  ? 34  LYS   C O   1 
ATOM   1691 C CB  . LYS   C 1 35 ? 21.756  -37.628 38.969  1.00 65.20  ? 34  LYS   C CB  1 
ATOM   1692 N N   . PRO   C 1 36 ? 21.852  -36.616 35.645  1.00 77.01  ? 35  PRO   C N   1 
ATOM   1693 C CA  . PRO   C 1 36 ? 22.581  -36.862 34.397  1.00 74.03  ? 35  PRO   C CA  1 
ATOM   1694 C C   . PRO   C 1 36 ? 23.796  -37.765 34.631  1.00 81.05  ? 35  PRO   C C   1 
ATOM   1695 O O   . PRO   C 1 36 ? 24.368  -37.774 35.724  1.00 81.63  ? 35  PRO   C O   1 
ATOM   1696 C CB  . PRO   C 1 36 ? 23.021  -35.446 33.931  1.00 75.56  ? 35  PRO   C CB  1 
ATOM   1697 C CG  . PRO   C 1 36 ? 22.140  -34.464 34.681  1.00 75.21  ? 35  PRO   C CG  1 
ATOM   1698 C CD  . PRO   C 1 36 ? 21.700  -35.179 35.949  1.00 81.46  ? 35  PRO   C CD  1 
ATOM   1699 N N   . PRO   C 1 37 ? 24.251  -38.557 33.632  1.00 67.49  ? 36  PRO   C N   1 
ATOM   1700 C CA  . PRO   C 1 37 ? 25.593  -39.140 33.703  1.00 63.20  ? 36  PRO   C CA  1 
ATOM   1701 C C   . PRO   C 1 37 ? 26.585  -37.991 33.901  1.00 63.65  ? 36  PRO   C C   1 
ATOM   1702 O O   . PRO   C 1 37 ? 26.279  -36.838 33.589  1.00 57.92  ? 36  PRO   C O   1 
ATOM   1703 C CB  . PRO   C 1 37 ? 25.723  -39.847 32.344  1.00 54.38  ? 36  PRO   C CB  1 
ATOM   1704 C CG  . PRO   C 1 37 ? 24.291  -40.213 32.024  1.00 54.02  ? 36  PRO   C CG  1 
ATOM   1705 C CD  . PRO   C 1 37 ? 23.499  -38.980 32.442  1.00 59.05  ? 36  PRO   C CD  1 
ATOM   1706 N N   . PRO   C 1 38 ? 27.778  -38.250 34.485  1.00 62.78  ? 37  PRO   C N   1 
ATOM   1707 C CA  . PRO   C 1 38 ? 28.758  -37.189 34.724  1.00 62.48  ? 37  PRO   C CA  1 
ATOM   1708 C C   . PRO   C 1 38 ? 29.002  -36.320 33.493  1.00 57.99  ? 37  PRO   C C   1 
ATOM   1709 O O   . PRO   C 1 38 ? 29.174  -36.831 32.382  1.00 55.47  ? 37  PRO   C O   1 
ATOM   1710 C CB  . PRO   C 1 38 ? 30.053  -37.903 35.186  1.00 67.22  ? 37  PRO   C CB  1 
ATOM   1711 C CG  . PRO   C 1 38 ? 29.640  -39.335 35.485  1.00 57.25  ? 37  PRO   C CG  1 
ATOM   1712 C CD  . PRO   C 1 38 ? 28.237  -39.568 34.949  1.00 61.87  ? 37  PRO   C CD  1 
ATOM   1713 N N   . ASN   C 1 39 ? 28.953  -35.003 33.723  1.00 52.37  ? 38  ASN   C N   1 
ATOM   1714 C CA  . ASN   C 1 39 ? 29.338  -33.985 32.761  1.00 52.08  ? 38  ASN   C CA  1 
ATOM   1715 C C   . ASN   C 1 39 ? 28.351  -33.908 31.587  1.00 48.35  ? 38  ASN   C C   1 
ATOM   1716 O O   . ASN   C 1 39 ? 28.703  -33.371 30.540  1.00 47.23  ? 38  ASN   C O   1 
ATOM   1717 C CB  . ASN   C 1 39 ? 30.786  -34.175 32.324  1.00 56.58  ? 38  ASN   C CB  1 
ATOM   1718 C CG  . ASN   C 1 39 ? 31.384  -32.917 31.737  1.00 74.81  ? 38  ASN   C CG  1 
ATOM   1719 O OD1 . ASN   C 1 39 ? 30.787  -31.831 31.805  1.00 77.53  ? 38  ASN   C OD1 1 
ATOM   1720 N ND2 . ASN   C 1 39 ? 32.574  -33.046 31.168  1.00 76.65  ? 38  ASN   C ND2 1 
ATOM   1721 N N   . LYS   C 1 40 ? 27.128  -34.435 31.758  1.00 47.18  ? 39  LYS   C N   1 
ATOM   1722 C CA  . LYS   C 1 40 ? 26.125  -34.439 30.694  1.00 54.02  ? 39  LYS   C CA  1 
ATOM   1723 C C   . LYS   C 1 40 ? 24.976  -33.501 31.052  1.00 49.68  ? 39  LYS   C C   1 
ATOM   1724 O O   . LYS   C 1 40 ? 24.508  -33.494 32.187  1.00 61.73  ? 39  LYS   C O   1 
ATOM   1725 C CB  . LYS   C 1 40 ? 25.528  -35.827 30.431  1.00 53.21  ? 39  LYS   C CB  1 
ATOM   1726 C CG  . LYS   C 1 40 ? 26.566  -36.917 30.198  1.00 49.89  ? 39  LYS   C CG  1 
ATOM   1727 C CD  . LYS   C 1 40 ? 27.368  -36.741 28.921  1.00 49.23  ? 39  LYS   C CD  1 
ATOM   1728 C CE  . LYS   C 1 40 ? 28.219  -37.954 28.688  1.00 49.29  ? 39  LYS   C CE  1 
ATOM   1729 N NZ  . LYS   C 1 40 ? 29.028  -37.760 27.482  1.00 50.76  ? 39  LYS   C NZ  1 
ATOM   1730 N N   . TYR   C 1 41 ? 24.544  -32.699 30.076  1.00 42.96  ? 40  TYR   C N   1 
ATOM   1731 C CA  . TYR   C 1 41 ? 23.433  -31.773 30.268  1.00 40.79  ? 40  TYR   C CA  1 
ATOM   1732 C C   . TYR   C 1 41 ? 22.174  -32.429 29.711  1.00 48.11  ? 40  TYR   C C   1 
ATOM   1733 O O   . TYR   C 1 41 ? 22.261  -33.202 28.750  1.00 51.04  ? 40  TYR   C O   1 
ATOM   1734 C CB  . TYR   C 1 41 ? 23.652  -30.516 29.422  1.00 39.86  ? 40  TYR   C CB  1 
ATOM   1735 C CG  . TYR   C 1 41 ? 24.863  -29.656 29.774  1.00 44.44  ? 40  TYR   C CG  1 
ATOM   1736 C CD1 . TYR   C 1 41 ? 26.143  -29.998 29.346  1.00 45.71  ? 40  TYR   C CD1 1 
ATOM   1737 C CD2 . TYR   C 1 41 ? 24.717  -28.468 30.487  1.00 43.10  ? 40  TYR   C CD2 1 
ATOM   1738 C CE1 . TYR   C 1 41 ? 27.244  -29.222 29.676  1.00 54.89  ? 40  TYR   C CE1 1 
ATOM   1739 C CE2 . TYR   C 1 41 ? 25.805  -27.657 30.778  1.00 50.89  ? 40  TYR   C CE2 1 
ATOM   1740 C CZ  . TYR   C 1 41 ? 27.069  -28.040 30.379  1.00 57.61  ? 40  TYR   C CZ  1 
ATOM   1741 O OH  . TYR   C 1 41 ? 28.141  -27.254 30.682  1.00 71.17  ? 40  TYR   C OH  1 
ATOM   1742 N N   . PRO   C 1 42 ? 20.969  -32.134 30.262  1.00 45.80  ? 41  PRO   C N   1 
ATOM   1743 C CA  . PRO   C 1 42 ? 19.725  -32.704 29.732  1.00 37.15  ? 41  PRO   C CA  1 
ATOM   1744 C C   . PRO   C 1 42 ? 19.363  -31.758 28.587  1.00 41.82  ? 41  PRO   C C   1 
ATOM   1745 O O   . PRO   C 1 42 ? 19.476  -30.539 28.717  1.00 43.79  ? 41  PRO   C O   1 
ATOM   1746 C CB  . PRO   C 1 42 ? 18.759  -32.575 30.934  1.00 41.79  ? 41  PRO   C CB  1 
ATOM   1747 C CG  . PRO   C 1 42 ? 19.229  -31.310 31.644  1.00 42.65  ? 41  PRO   C CG  1 
ATOM   1748 C CD  . PRO   C 1 42 ? 20.740  -31.177 31.364  1.00 42.27  ? 41  PRO   C CD  1 
ATOM   1749 N N   . ILE   C 1 43 ? 19.006  -32.318 27.438  1.00 42.72  ? 42  ILE   C N   1 
ATOM   1750 C CA  . ILE   C 1 43 ? 18.726  -31.511 26.265  1.00 40.23  ? 42  ILE   C CA  1 
ATOM   1751 C C   . ILE   C 1 43 ? 17.323  -31.884 25.826  1.00 43.10  ? 42  ILE   C C   1 
ATOM   1752 O O   . ILE   C 1 43 ? 17.004  -33.076 25.796  1.00 45.59  ? 42  ILE   C O   1 
ATOM   1753 C CB  . ILE   C 1 43 ? 19.748  -31.813 25.146  1.00 41.25  ? 42  ILE   C CB  1 
ATOM   1754 C CG1 . ILE   C 1 43 ? 21.205  -31.487 25.577  1.00 35.24  ? 42  ILE   C CG1 1 
ATOM   1755 C CG2 . ILE   C 1 43 ? 19.363  -31.161 23.815  1.00 36.63  ? 42  ILE   C CG2 1 
ATOM   1756 C CD1 . ILE   C 1 43 ? 21.415  -30.087 26.098  1.00 34.17  ? 42  ILE   C CD1 1 
ATOM   1757 N N   . PHE   C 1 44 ? 16.518  -30.854 25.515  1.00 42.73  ? 43  PHE   C N   1 
ATOM   1758 C CA  . PHE   C 1 44 ? 15.242  -30.999 24.820  1.00 37.19  ? 43  PHE   C CA  1 
ATOM   1759 C C   . PHE   C 1 44 ? 15.412  -30.588 23.351  1.00 34.71  ? 43  PHE   C C   1 
ATOM   1760 O O   . PHE   C 1 44 ? 15.946  -29.513 23.052  1.00 39.97  ? 43  PHE   C O   1 
ATOM   1761 C CB  . PHE   C 1 44 ? 14.288  -30.030 25.531  1.00 34.18  ? 43  PHE   C CB  1 
ATOM   1762 C CG  . PHE   C 1 44 ? 12.912  -29.948 24.889  1.00 41.63  ? 43  PHE   C CG  1 
ATOM   1763 C CD1 . PHE   C 1 44 ? 11.970  -30.966 25.076  1.00 41.93  ? 43  PHE   C CD1 1 
ATOM   1764 C CD2 . PHE   C 1 44 ? 12.557  -28.845 24.103  1.00 48.30  ? 43  PHE   C CD2 1 
ATOM   1765 C CE1 . PHE   C 1 44 ? 10.703  -30.888 24.500  1.00 50.64  ? 43  PHE   C CE1 1 
ATOM   1766 C CE2 . PHE   C 1 44 ? 11.298  -28.783 23.499  1.00 47.85  ? 43  PHE   C CE2 1 
ATOM   1767 C CZ  . PHE   C 1 44 ? 10.373  -29.799 23.706  1.00 48.24  ? 43  PHE   C CZ  1 
ATOM   1768 N N   . PHE   C 1 45 ? 14.946  -31.441 22.435  1.00 35.01  ? 44  PHE   C N   1 
ATOM   1769 C CA  . PHE   C 1 45 ? 15.039  -31.211 21.001  1.00 34.26  ? 44  PHE   C CA  1 
ATOM   1770 C C   . PHE   C 1 45 ? 13.752  -30.546 20.518  1.00 39.28  ? 44  PHE   C C   1 
ATOM   1771 O O   . PHE   C 1 45 ? 12.656  -31.056 20.742  1.00 42.55  ? 44  PHE   C O   1 
ATOM   1772 C CB  . PHE   C 1 45 ? 15.328  -32.530 20.270  1.00 31.85  ? 44  PHE   C CB  1 
ATOM   1773 C CG  . PHE   C 1 45 ? 16.702  -33.105 20.581  1.00 35.26  ? 44  PHE   C CG  1 
ATOM   1774 C CD1 . PHE   C 1 45 ? 17.805  -32.771 19.803  1.00 39.25  ? 44  PHE   C CD1 1 
ATOM   1775 C CD2 . PHE   C 1 45 ? 16.906  -33.912 21.701  1.00 36.40  ? 44  PHE   C CD2 1 
ATOM   1776 C CE1 . PHE   C 1 45 ? 19.076  -33.264 20.120  1.00 38.71  ? 44  PHE   C CE1 1 
ATOM   1777 C CE2 . PHE   C 1 45 ? 18.167  -34.412 22.005  1.00 39.43  ? 44  PHE   C CE2 1 
ATOM   1778 C CZ  . PHE   C 1 45 ? 19.247  -34.075 21.224  1.00 40.08  ? 44  PHE   C CZ  1 
ATOM   1779 N N   . PHE   C 1 46 ? 13.890  -29.403 19.833  1.00 38.96  ? 45  PHE   C N   1 
ATOM   1780 C CA  . PHE   C 1 46 ? 12.755  -28.791 19.156  1.00 36.63  ? 45  PHE   C CA  1 
ATOM   1781 C C   . PHE   C 1 46 ? 12.285  -29.673 17.996  1.00 34.19  ? 45  PHE   C C   1 
ATOM   1782 O O   . PHE   C 1 46 ? 13.046  -30.485 17.481  1.00 33.61  ? 45  PHE   C O   1 
ATOM   1783 C CB  . PHE   C 1 46 ? 13.107  -27.366 18.729  1.00 34.50  ? 45  PHE   C CB  1 
ATOM   1784 C CG  . PHE   C 1 46 ? 13.356  -26.388 19.863  1.00 41.14  ? 45  PHE   C CG  1 
ATOM   1785 C CD1 . PHE   C 1 46 ? 12.315  -26.012 20.720  1.00 39.86  ? 45  PHE   C CD1 1 
ATOM   1786 C CD2 . PHE   C 1 46 ? 14.626  -25.832 20.058  1.00 39.27  ? 45  PHE   C CD2 1 
ATOM   1787 C CE1 . PHE   C 1 46 ? 12.540  -25.087 21.747  1.00 39.61  ? 45  PHE   C CE1 1 
ATOM   1788 C CE2 . PHE   C 1 46 ? 14.839  -24.916 21.089  1.00 42.80  ? 45  PHE   C CE2 1 
ATOM   1789 C CZ  . PHE   C 1 46 ? 13.802  -24.543 21.930  1.00 38.30  ? 45  PHE   C CZ  1 
ATOM   1790 N N   . GLY   C 1 47 ? 11.014  -29.525 17.606  1.00 36.20  ? 46  GLY   C N   1 
ATOM   1791 C CA  . GLY   C 1 47 ? 10.436  -30.348 16.554  1.00 40.59  ? 46  GLY   C CA  1 
ATOM   1792 C C   . GLY   C 1 47 ? 9.953   -31.695 17.089  1.00 47.87  ? 46  GLY   C C   1 
ATOM   1793 O O   . GLY   C 1 47 ? 8.749   -31.974 17.113  1.00 43.00  ? 46  GLY   C O   1 
ATOM   1794 N N   . THR   C 1 48 ? 10.899  -32.535 17.519  1.00 47.35  ? 47  THR   C N   1 
ATOM   1795 C CA  . THR   C 1 48 ? 10.545  -33.874 17.973  1.00 44.31  ? 47  THR   C CA  1 
ATOM   1796 C C   . THR   C 1 48 ? 10.081  -33.800 19.426  1.00 43.99  ? 47  THR   C C   1 
ATOM   1797 O O   . THR   C 1 48 ? 9.284   -34.628 19.854  1.00 44.07  ? 47  THR   C O   1 
ATOM   1798 C CB  . THR   C 1 48 ? 11.723  -34.830 17.827  1.00 40.13  ? 47  THR   C CB  1 
ATOM   1799 O OG1 . THR   C 1 48 ? 12.693  -34.247 18.704  1.00 40.31  ? 47  THR   C OG1 1 
ATOM   1800 C CG2 . THR   C 1 48 ? 12.180  -34.987 16.384  1.00 35.07  ? 47  THR   C CG2 1 
ATOM   1801 N N   . HIS   C 1 49 ? 10.593  -32.820 20.183  1.00 38.12  ? 48  HIS   C N   1 
ATOM   1802 C CA  . HIS   C 1 49 ? 10.201  -32.667 21.587  1.00 47.88  ? 48  HIS   C CA  1 
ATOM   1803 C C   . HIS   C 1 49 ? 10.703  -33.825 22.459  1.00 47.29  ? 48  HIS   C C   1 
ATOM   1804 O O   . HIS   C 1 49 ? 10.265  -33.963 23.603  1.00 54.53  ? 48  HIS   C O   1 
ATOM   1805 C CB  . HIS   C 1 49 ? 8.697   -32.365 21.726  1.00 46.70  ? 48  HIS   C CB  1 
ATOM   1806 C CG  . HIS   C 1 49 ? 8.240   -31.287 20.786  1.00 48.36  ? 48  HIS   C CG  1 
ATOM   1807 N ND1 . HIS   C 1 49 ? 7.223   -31.496 19.880  1.00 51.69  ? 48  HIS   C ND1 1 
ATOM   1808 C CD2 . HIS   C 1 49 ? 8.712   -30.046 20.534  1.00 40.47  ? 48  HIS   C CD2 1 
ATOM   1809 C CE1 . HIS   C 1 49 ? 7.061   -30.397 19.137  1.00 52.01  ? 48  HIS   C CE1 1 
ATOM   1810 N NE2 . HIS   C 1 49 ? 7.954   -29.510 19.526  1.00 50.04  ? 48  HIS   C NE2 1 
ATOM   1811 N N   . GLU   C 1 50 ? 11.657  -34.613 21.942  1.00 38.96  ? 49  GLU   C N   1 
ATOM   1812 C CA  . GLU   C 1 50 ? 12.328  -35.670 22.703  1.00 38.88  ? 49  GLU   C CA  1 
ATOM   1813 C C   . GLU   C 1 50 ? 13.503  -35.114 23.520  1.00 38.84  ? 49  GLU   C C   1 
ATOM   1814 O O   . GLU   C 1 50 ? 13.886  -33.966 23.346  1.00 41.55  ? 49  GLU   C O   1 
ATOM   1815 C CB  . GLU   C 1 50 ? 12.728  -36.768 21.722  1.00 39.94  ? 49  GLU   C CB  1 
ATOM   1816 C CG  . GLU   C 1 50 ? 11.525  -37.570 21.224  1.00 46.15  ? 49  GLU   C CG  1 
ATOM   1817 C CD  . GLU   C 1 50 ? 11.925  -38.338 19.993  1.00 51.12  ? 49  GLU   C CD  1 
ATOM   1818 O OE1 . GLU   C 1 50 ? 13.081  -38.823 19.913  1.00 57.51  ? 49  GLU   C OE1 1 
ATOM   1819 O OE2 . GLU   C 1 50 ? 11.068  -38.430 19.102  1.00 65.38  ? 49  GLU   C OE2 1 
ATOM   1820 N N   . THR   C 1 51 ? 14.034  -35.901 24.472  1.00 41.30  ? 50  THR   C N   1 
ATOM   1821 C CA  . THR   C 1 51 ? 15.086  -35.438 25.387  1.00 42.27  ? 50  THR   C CA  1 
ATOM   1822 C C   . THR   C 1 51 ? 16.234  -36.459 25.425  1.00 33.84  ? 50  THR   C C   1 
ATOM   1823 O O   . THR   C 1 51 ? 16.064  -37.631 25.097  1.00 38.12  ? 50  THR   C O   1 
ATOM   1824 C CB  . THR   C 1 51 ? 14.580  -35.100 26.803  1.00 43.78  ? 50  THR   C CB  1 
ATOM   1825 O OG1 . THR   C 1 51 ? 13.972  -36.299 27.274  1.00 51.64  ? 50  THR   C OG1 1 
ATOM   1826 C CG2 . THR   C 1 51 ? 13.593  -33.946 26.899  1.00 38.56  ? 50  THR   C CG2 1 
ATOM   1827 N N   . ALA   C 1 52 ? 17.435  -35.982 25.757  1.00 36.02  ? 51  ALA   C N   1 
ATOM   1828 C CA  . ALA   C 1 52 ? 18.606  -36.833 25.892  1.00 35.43  ? 51  ALA   C CA  1 
ATOM   1829 C C   . ALA   C 1 52 ? 19.626  -36.139 26.781  1.00 42.74  ? 51  ALA   C C   1 
ATOM   1830 O O   . ALA   C 1 52 ? 19.474  -34.967 27.123  1.00 38.39  ? 51  ALA   C O   1 
ATOM   1831 C CB  . ALA   C 1 52 ? 19.197  -37.180 24.533  1.00 41.89  ? 51  ALA   C CB  1 
ATOM   1832 N N   . PHE   C 1 53 ? 20.665  -36.888 27.155  1.00 44.27  ? 52  PHE   C N   1 
ATOM   1833 C CA  . PHE   C 1 53 ? 21.784  -36.312 27.875  1.00 43.76  ? 52  PHE   C CA  1 
ATOM   1834 C C   . PHE   C 1 53 ? 22.952  -36.215 26.908  1.00 43.01  ? 52  PHE   C C   1 
ATOM   1835 O O   . PHE   C 1 53 ? 23.372  -37.230 26.359  1.00 41.25  ? 52  PHE   C O   1 
ATOM   1836 C CB  . PHE   C 1 53 ? 22.064  -37.361 28.950  1.00 41.41  ? 52  PHE   C CB  1 
ATOM   1837 C CG  . PHE   C 1 53 ? 21.151  -37.190 30.150  1.00 47.71  ? 52  PHE   C CG  1 
ATOM   1838 C CD1 . PHE   C 1 53 ? 21.020  -35.946 30.773  1.00 42.63  ? 52  PHE   C CD1 1 
ATOM   1839 C CD2 . PHE   C 1 53 ? 20.433  -38.273 30.661  1.00 49.47  ? 52  PHE   C CD2 1 
ATOM   1840 C CE1 . PHE   C 1 53 ? 20.200  -35.789 31.888  1.00 39.04  ? 52  PHE   C CE1 1 
ATOM   1841 C CE2 . PHE   C 1 53 ? 19.619  -38.111 31.774  1.00 44.39  ? 52  PHE   C CE2 1 
ATOM   1842 C CZ  . PHE   C 1 53 ? 19.494  -36.874 32.374  1.00 43.22  ? 52  PHE   C CZ  1 
ATOM   1843 N N   . LEU   C 1 54 ? 23.458  -34.995 26.702  1.00 41.06  ? 53  LEU   C N   1 
ATOM   1844 C CA  . LEU   C 1 54 ? 24.614  -34.818 25.841  1.00 43.22  ? 53  LEU   C CA  1 
ATOM   1845 C C   . LEU   C 1 54 ? 25.747  -34.157 26.621  1.00 42.41  ? 53  LEU   C C   1 
ATOM   1846 O O   . LEU   C 1 54 ? 25.517  -33.430 27.580  1.00 41.04  ? 53  LEU   C O   1 
ATOM   1847 C CB  . LEU   C 1 54 ? 24.247  -34.023 24.589  1.00 44.32  ? 53  LEU   C CB  1 
ATOM   1848 C CG  . LEU   C 1 54 ? 23.228  -34.672 23.648  1.00 44.45  ? 53  LEU   C CG  1 
ATOM   1849 C CD1 . LEU   C 1 54 ? 23.069  -33.829 22.380  1.00 42.28  ? 53  LEU   C CD1 1 
ATOM   1850 C CD2 . LEU   C 1 54 ? 23.660  -36.076 23.294  1.00 46.21  ? 53  LEU   C CD2 1 
ATOM   1851 N N   . GLY   C 1 55 ? 26.978  -34.477 26.217  1.00 45.33  ? 54  GLY   C N   1 
ATOM   1852 C CA  . GLY   C 1 55 ? 28.155  -33.820 26.754  1.00 39.57  ? 54  GLY   C CA  1 
ATOM   1853 C C   . GLY   C 1 55 ? 28.343  -32.488 26.038  1.00 44.95  ? 54  GLY   C C   1 
ATOM   1854 O O   . GLY   C 1 55 ? 27.789  -32.279 24.949  1.00 40.04  ? 54  GLY   C O   1 
ATOM   1855 N N   . PRO   C 1 56 ? 29.111  -31.538 26.619  1.00 47.73  ? 55  PRO   C N   1 
ATOM   1856 C CA  . PRO   C 1 56 ? 29.229  -30.203 26.023  1.00 49.17  ? 55  PRO   C CA  1 
ATOM   1857 C C   . PRO   C 1 56 ? 29.987  -30.261 24.701  1.00 38.12  ? 55  PRO   C C   1 
ATOM   1858 O O   . PRO   C 1 56 ? 29.942  -29.331 23.914  1.00 44.24  ? 55  PRO   C O   1 
ATOM   1859 C CB  . PRO   C 1 56 ? 29.964  -29.396 27.117  1.00 49.04  ? 55  PRO   C CB  1 
ATOM   1860 C CG  . PRO   C 1 56 ? 30.803  -30.449 27.790  1.00 46.77  ? 55  PRO   C CG  1 
ATOM   1861 C CD  . PRO   C 1 56 ? 29.889  -31.682 27.867  1.00 48.60  ? 55  PRO   C CD  1 
ATOM   1862 N N   . LYS   C 1 57 ? 30.643  -31.388 24.437  1.00 43.20  ? 56  LYS   C N   1 
ATOM   1863 C CA  . LYS   C 1 57 ? 31.273  -31.597 23.141  1.00 44.97  ? 56  LYS   C CA  1 
ATOM   1864 C C   . LYS   C 1 57 ? 30.226  -31.504 22.032  1.00 48.12  ? 56  LYS   C C   1 
ATOM   1865 O O   . LYS   C 1 57 ? 30.556  -31.190 20.892  1.00 46.34  ? 56  LYS   C O   1 
ATOM   1866 C CB  . LYS   C 1 57 ? 31.978  -32.959 23.086  1.00 47.49  ? 56  LYS   C CB  1 
ATOM   1867 N N   . ASP   C 1 58 ? 28.958  -31.758 22.385  1.00 44.65  ? 57  ASP   C N   1 
ATOM   1868 C CA  . ASP   C 1 58 ? 27.950  -32.039 21.381  1.00 44.12  ? 57  ASP   C CA  1 
ATOM   1869 C C   . ASP   C 1 58 ? 27.073  -30.818 21.178  1.00 40.50  ? 57  ASP   C C   1 
ATOM   1870 O O   . ASP   C 1 58 ? 26.055  -30.910 20.500  1.00 40.97  ? 57  ASP   C O   1 
ATOM   1871 C CB  . ASP   C 1 58 ? 27.144  -33.268 21.768  1.00 46.54  ? 57  ASP   C CB  1 
ATOM   1872 C CG  . ASP   C 1 58 ? 27.989  -34.527 21.877  1.00 45.22  ? 57  ASP   C CG  1 
ATOM   1873 O OD1 . ASP   C 1 58 ? 29.016  -34.576 21.188  1.00 50.30  ? 57  ASP   C OD1 1 
ATOM   1874 O OD2 . ASP   C 1 58 ? 27.635  -35.415 22.679  1.00 45.56  ? 57  ASP   C OD2 1 
ATOM   1875 N N   . LEU   C 1 59 ? 27.446  -29.702 21.813  1.00 39.74  ? 58  LEU   C N   1 
ATOM   1876 C CA  . LEU   C 1 59 ? 26.501  -28.607 21.988  1.00 42.53  ? 58  LEU   C CA  1 
ATOM   1877 C C   . LEU   C 1 59 ? 27.129  -27.344 21.435  1.00 44.47  ? 58  LEU   C C   1 
ATOM   1878 O O   . LEU   C 1 59 ? 28.321  -27.147 21.652  1.00 42.60  ? 58  LEU   C O   1 
ATOM   1879 C CB  . LEU   C 1 59 ? 26.198  -28.413 23.472  1.00 39.80  ? 58  LEU   C CB  1 
ATOM   1880 C CG  . LEU   C 1 59 ? 25.661  -29.628 24.233  1.00 36.10  ? 58  LEU   C CG  1 
ATOM   1881 C CD1 . LEU   C 1 59 ? 25.478  -29.175 25.675  1.00 36.23  ? 58  LEU   C CD1 1 
ATOM   1882 C CD2 . LEU   C 1 59 ? 24.336  -30.059 23.669  1.00 31.50  ? 58  LEU   C CD2 1 
ATOM   1883 N N   . PHE   C 1 60 ? 26.317  -26.526 20.742  1.00 44.92  ? 59  PHE   C N   1 
ATOM   1884 C CA  . PHE   C 1 60 ? 26.760  -25.301 20.084  1.00 42.62  ? 59  PHE   C CA  1 
ATOM   1885 C C   . PHE   C 1 60 ? 25.765  -24.172 20.343  1.00 48.69  ? 59  PHE   C C   1 
ATOM   1886 O O   . PHE   C 1 60 ? 24.570  -24.339 20.080  1.00 52.91  ? 59  PHE   C O   1 
ATOM   1887 C CB  . PHE   C 1 60 ? 26.937  -25.585 18.596  1.00 42.75  ? 59  PHE   C CB  1 
ATOM   1888 C CG  . PHE   C 1 60 ? 27.884  -26.744 18.313  1.00 40.34  ? 59  PHE   C CG  1 
ATOM   1889 C CD1 . PHE   C 1 60 ? 27.432  -28.060 18.361  1.00 38.59  ? 59  PHE   C CD1 1 
ATOM   1890 C CD2 . PHE   C 1 60 ? 29.213  -26.512 17.961  1.00 45.84  ? 59  PHE   C CD2 1 
ATOM   1891 C CE1 . PHE   C 1 60 ? 28.285  -29.124 18.089  1.00 38.39  ? 59  PHE   C CE1 1 
ATOM   1892 C CE2 . PHE   C 1 60 ? 30.071  -27.582 17.699  1.00 45.38  ? 59  PHE   C CE2 1 
ATOM   1893 C CZ  . PHE   C 1 60 ? 29.607  -28.881 17.775  1.00 42.62  ? 59  PHE   C CZ  1 
ATOM   1894 N N   . PRO   C 1 61 ? 26.201  -23.028 20.942  1.00 49.53  ? 60  PRO   C N   1 
ATOM   1895 C CA  . PRO   C 1 61 ? 25.316  -21.883 21.176  1.00 45.88  ? 60  PRO   C CA  1 
ATOM   1896 C C   . PRO   C 1 61 ? 24.606  -21.477 19.890  1.00 46.12  ? 60  PRO   C C   1 
ATOM   1897 O O   . PRO   C 1 61 ? 25.240  -21.377 18.831  1.00 44.70  ? 60  PRO   C O   1 
ATOM   1898 C CB  . PRO   C 1 61 ? 26.238  -20.773 21.728  1.00 47.29  ? 60  PRO   C CB  1 
ATOM   1899 C CG  . PRO   C 1 61 ? 27.438  -21.512 22.284  1.00 45.97  ? 60  PRO   C CG  1 
ATOM   1900 C CD  . PRO   C 1 61 ? 27.550  -22.812 21.500  1.00 51.77  ? 60  PRO   C CD  1 
ATOM   1901 N N   . TYR   C 1 62 ? 23.288  -21.263 20.034  1.00 44.85  ? 61  TYR   C N   1 
ATOM   1902 C CA  . TYR   C 1 62 ? 22.333  -21.074 18.953  1.00 48.38  ? 61  TYR   C CA  1 
ATOM   1903 C C   . TYR   C 1 62 ? 22.718  -19.855 18.124  1.00 59.27  ? 61  TYR   C C   1 
ATOM   1904 O O   . TYR   C 1 62 ? 22.781  -19.965 16.905  1.00 58.14  ? 61  TYR   C O   1 
ATOM   1905 C CB  . TYR   C 1 62 ? 20.880  -20.910 19.416  1.00 47.93  ? 61  TYR   C CB  1 
ATOM   1906 C CG  . TYR   C 1 62 ? 19.905  -20.503 18.317  1.00 47.13  ? 61  TYR   C CG  1 
ATOM   1907 C CD1 . TYR   C 1 62 ? 19.675  -21.335 17.217  1.00 50.07  ? 61  TYR   C CD1 1 
ATOM   1908 C CD2 . TYR   C 1 62 ? 19.200  -19.302 18.385  1.00 49.03  ? 61  TYR   C CD2 1 
ATOM   1909 C CE1 . TYR   C 1 62 ? 18.791  -20.972 16.208  1.00 46.04  ? 61  TYR   C CE1 1 
ATOM   1910 C CE2 . TYR   C 1 62 ? 18.320  -18.923 17.376  1.00 47.94  ? 61  TYR   C CE2 1 
ATOM   1911 C CZ  . TYR   C 1 62 ? 18.120  -19.758 16.284  1.00 45.98  ? 61  TYR   C CZ  1 
ATOM   1912 O OH  . TYR   C 1 62 ? 17.237  -19.405 15.302  1.00 46.89  ? 61  TYR   C OH  1 
ATOM   1913 N N   . ASP   C 1 63 ? 22.987  -18.723 18.796  1.00 62.63  ? 62  ASP   C N   1 
ATOM   1914 C CA  . ASP   C 1 63 ? 23.333  -17.480 18.117  1.00 67.70  ? 62  ASP   C CA  1 
ATOM   1915 C C   . ASP   C 1 63 ? 24.666  -17.583 17.392  1.00 58.81  ? 62  ASP   C C   1 
ATOM   1916 O O   . ASP   C 1 63 ? 24.791  -17.071 16.286  1.00 67.14  ? 62  ASP   C O   1 
ATOM   1917 C CB  . ASP   C 1 63 ? 23.284  -16.263 19.023  1.00 69.37  ? 62  ASP   C CB  1 
ATOM   1918 C CG  . ASP   C 1 63 ? 21.967  -15.511 18.927  1.00 88.04  ? 62  ASP   C CG  1 
ATOM   1919 O OD1 . ASP   C 1 63 ? 21.148  -15.649 19.861  1.00 80.11  ? 62  ASP   C OD1 1 
ATOM   1920 O OD2 . ASP   C 1 63 ? 21.765  -14.822 17.898  1.00 95.28  ? 62  ASP   C OD2 1 
ATOM   1921 N N   . LYS   C 1 64 ? 25.648  -18.237 18.019  1.00 50.38  ? 63  LYS   C N   1 
ATOM   1922 C CA  . LYS   C 1 64 ? 26.976  -18.320 17.433  1.00 48.93  ? 63  LYS   C CA  1 
ATOM   1923 C C   . LYS   C 1 64 ? 26.956  -19.173 16.165  1.00 47.55  ? 63  LYS   C C   1 
ATOM   1924 O O   . LYS   C 1 64 ? 27.667  -18.834 15.217  1.00 43.65  ? 63  LYS   C O   1 
ATOM   1925 C CB  . LYS   C 1 64 ? 28.070  -18.751 18.421  1.00 49.36  ? 63  LYS   C CB  1 
ATOM   1926 N N   . SER   C 1 65 ? 26.123  -20.240 16.127  1.00 42.85  ? 64  SER   C N   1 
ATOM   1927 C CA  . SER   C 1 65 ? 26.331  -21.303 15.147  1.00 41.17  ? 64  SER   C CA  1 
ATOM   1928 C C   . SER   C 1 65 ? 25.204  -21.409 14.099  1.00 44.10  ? 64  SER   C C   1 
ATOM   1929 O O   . SER   C 1 65 ? 25.267  -22.238 13.189  1.00 38.00  ? 64  SER   C O   1 
ATOM   1930 C CB  . SER   C 1 65 ? 26.583  -22.621 15.860  1.00 41.10  ? 64  SER   C CB  1 
ATOM   1931 O OG  . SER   C 1 65 ? 25.382  -23.115 16.458  1.00 39.94  ? 64  SER   C OG  1 
ATOM   1932 N N   . LYS   C 1 66 ? 24.144  -20.595 14.238  1.00 41.73  ? 65  LYS   C N   1 
ATOM   1933 C CA  . LYS   C 1 66 ? 22.922  -20.805 13.474  1.00 45.07  ? 65  LYS   C CA  1 
ATOM   1934 C C   . LYS   C 1 66 ? 23.126  -20.516 11.989  1.00 45.77  ? 65  LYS   C C   1 
ATOM   1935 O O   . LYS   C 1 66 ? 22.388  -21.057 11.175  1.00 48.77  ? 65  LYS   C O   1 
ATOM   1936 C CB  . LYS   C 1 66 ? 21.728  -20.006 14.007  1.00 41.79  ? 65  LYS   C CB  1 
ATOM   1937 C CG  . LYS   C 1 66 ? 21.902  -18.496 13.992  1.00 42.91  ? 65  LYS   C CG  1 
ATOM   1938 C CD  . LYS   C 1 66 ? 20.714  -17.843 14.691  1.00 48.99  ? 65  LYS   C CD  1 
ATOM   1939 C CE  . LYS   C 1 66 ? 20.655  -16.355 14.555  1.00 46.47  ? 65  LYS   C CE  1 
ATOM   1940 N NZ  . LYS   C 1 66 ? 19.459  -15.916 15.270  1.00 54.91  ? 65  LYS   C NZ  1 
ATOM   1941 N N   . ASP   C 1 67 ? 24.102  -19.657 11.650  1.00 45.47  ? 66  ASP   C N   1 
ATOM   1942 C CA  . ASP   C 1 67 ? 24.449  -19.379 10.257  1.00 52.11  ? 66  ASP   C CA  1 
ATOM   1943 C C   . ASP   C 1 67 ? 24.908  -20.688 9.617   1.00 46.06  ? 66  ASP   C C   1 
ATOM   1944 O O   . ASP   C 1 67 ? 24.656  -20.935 8.439   1.00 49.55  ? 66  ASP   C O   1 
ATOM   1945 C CB  . ASP   C 1 67 ? 25.359  -18.161 10.072  1.00 50.30  ? 66  ASP   C CB  1 
ATOM   1946 C CG  . ASP   C 1 67 ? 26.662  -18.148 10.872  1.00 64.67  ? 66  ASP   C CG  1 
ATOM   1947 O OD1 . ASP   C 1 67 ? 26.934  -19.133 11.603  1.00 62.42  ? 66  ASP   C OD1 1 
ATOM   1948 O OD2 . ASP   C 1 67 ? 27.398  -17.134 10.796  1.00 68.18  ? 66  ASP   C OD2 1 
ATOM   1949 N N   . LYS   C 1 68 ? 25.484  -21.561 10.444  1.00 35.90  ? 67  LYS   C N   1 
ATOM   1950 C CA  . LYS   C 1 68 ? 26.045  -22.816 9.963   1.00 42.99  ? 67  LYS   C CA  1 
ATOM   1951 C C   . LYS   C 1 68 ? 25.018  -23.961 10.009  1.00 41.84  ? 67  LYS   C C   1 
ATOM   1952 O O   . LYS   C 1 68 ? 24.904  -24.696 9.039   1.00 43.51  ? 67  LYS   C O   1 
ATOM   1953 C CB  . LYS   C 1 68 ? 27.399  -23.057 10.651  1.00 40.25  ? 67  LYS   C CB  1 
ATOM   1954 C CG  . LYS   C 1 68 ? 28.063  -24.403 10.407  1.00 44.81  ? 67  LYS   C CG  1 
ATOM   1955 C CD  . LYS   C 1 68 ? 29.422  -24.379 11.115  1.00 56.75  ? 67  LYS   C CD  1 
ATOM   1956 C CE  . LYS   C 1 68 ? 30.111  -25.703 11.283  1.00 67.30  ? 67  LYS   C CE  1 
ATOM   1957 N NZ  . LYS   C 1 68 ? 30.351  -26.384 10.007  1.00 79.15  ? 67  LYS   C NZ  1 
ATOM   1958 N N   . TYR   C 1 69 ? 24.297  -24.144 11.130  1.00 41.46  ? 68  TYR   C N   1 
ATOM   1959 C CA  . TYR   C 1 69 ? 23.429  -25.307 11.283  1.00 40.91  ? 68  TYR   C CA  1 
ATOM   1960 C C   . TYR   C 1 69 ? 21.950  -24.932 11.139  1.00 43.58  ? 68  TYR   C C   1 
ATOM   1961 O O   . TYR   C 1 69 ? 21.083  -25.809 11.075  1.00 38.60  ? 68  TYR   C O   1 
ATOM   1962 C CB  . TYR   C 1 69 ? 23.593  -25.822 12.712  1.00 38.13  ? 68  TYR   C CB  1 
ATOM   1963 C CG  . TYR   C 1 69 ? 25.004  -26.267 13.024  1.00 43.96  ? 68  TYR   C CG  1 
ATOM   1964 C CD1 . TYR   C 1 69 ? 25.704  -27.071 12.135  1.00 41.03  ? 68  TYR   C CD1 1 
ATOM   1965 C CD2 . TYR   C 1 69 ? 25.644  -25.848 14.181  1.00 51.00  ? 68  TYR   C CD2 1 
ATOM   1966 C CE1 . TYR   C 1 69 ? 26.989  -27.487 12.420  1.00 42.08  ? 68  TYR   C CE1 1 
ATOM   1967 C CE2 . TYR   C 1 69 ? 26.934  -26.263 14.476  1.00 50.36  ? 68  TYR   C CE2 1 
ATOM   1968 C CZ  . TYR   C 1 69 ? 27.613  -27.073 13.581  1.00 46.84  ? 68  TYR   C CZ  1 
ATOM   1969 O OH  . TYR   C 1 69 ? 28.902  -27.467 13.832  1.00 46.33  ? 68  TYR   C OH  1 
ATOM   1970 N N   . GLY   C 1 70 ? 21.640  -23.631 11.167  1.00 36.04  ? 69  GLY   C N   1 
ATOM   1971 C CA  . GLY   C 1 70 ? 20.234  -23.249 11.117  1.00 42.99  ? 69  GLY   C CA  1 
ATOM   1972 C C   . GLY   C 1 70 ? 19.795  -23.165 9.661   1.00 46.12  ? 69  GLY   C C   1 
ATOM   1973 O O   . GLY   C 1 70 ? 19.900  -22.111 9.039   1.00 42.43  ? 69  GLY   C O   1 
ATOM   1974 N N   . LYS   C 1 71 ? 19.390  -24.312 9.110   1.00 45.51  ? 70  LYS   C N   1 
ATOM   1975 C CA  . LYS   C 1 71 ? 19.140  -24.427 7.682   1.00 43.21  ? 70  LYS   C CA  1 
ATOM   1976 C C   . LYS   C 1 71 ? 18.346  -25.708 7.481   1.00 40.15  ? 70  LYS   C C   1 
ATOM   1977 O O   . LYS   C 1 71 ? 18.594  -26.710 8.143   1.00 36.40  ? 70  LYS   C O   1 
ATOM   1978 C CB  . LYS   C 1 71 ? 20.386  -24.434 6.787   1.00 38.42  ? 70  LYS   C CB  1 
ATOM   1979 C CG  . LYS   C 1 71 ? 21.391  -25.520 7.101   1.00 51.41  ? 70  LYS   C CG  1 
ATOM   1980 C CD  . LYS   C 1 71 ? 22.461  -25.815 6.060   1.00 57.26  ? 70  LYS   C CD  1 
ATOM   1981 C CE  . LYS   C 1 71 ? 23.438  -26.833 6.585   1.00 68.95  ? 70  LYS   C CE  1 
ATOM   1982 N N   . PRO   C 1 72 ? 17.312  -25.676 6.623   1.00 33.69  ? 71  PRO   C N   1 
ATOM   1983 C CA  . PRO   C 1 72 ? 16.370  -26.793 6.557   1.00 34.77  ? 71  PRO   C CA  1 
ATOM   1984 C C   . PRO   C 1 72 ? 16.997  -28.145 6.204   1.00 37.66  ? 71  PRO   C C   1 
ATOM   1985 O O   . PRO   C 1 72 ? 18.106  -28.252 5.673   1.00 36.65  ? 71  PRO   C O   1 
ATOM   1986 C CB  . PRO   C 1 72 ? 15.378  -26.273 5.510   1.00 34.81  ? 71  PRO   C CB  1 
ATOM   1987 C CG  . PRO   C 1 72 ? 15.428  -24.777 5.695   1.00 32.16  ? 71  PRO   C CG  1 
ATOM   1988 C CD  . PRO   C 1 72 ? 16.939  -24.528 5.778   1.00 33.34  ? 71  PRO   C CD  1 
ATOM   1989 N N   . ASN   C 1 73 ? 16.314  -29.210 6.591   1.00 35.92  ? 72  ASN   C N   1 
ATOM   1990 C CA  . ASN   C 1 73 ? 16.636  -30.514 6.041   1.00 42.30  ? 72  ASN   C CA  1 
ATOM   1991 C C   . ASN   C 1 73 ? 15.375  -31.319 6.247   1.00 34.47  ? 72  ASN   C C   1 
ATOM   1992 O O   . ASN   C 1 73 ? 14.469  -30.805 6.887   1.00 34.34  ? 72  ASN   C O   1 
ATOM   1993 C CB  . ASN   C 1 73 ? 17.941  -31.109 6.575   1.00 46.31  ? 72  ASN   C CB  1 
ATOM   1994 C CG  . ASN   C 1 73 ? 17.762  -31.588 7.993   1.00 39.81  ? 72  ASN   C CG  1 
ATOM   1995 O OD1 . ASN   C 1 73 ? 16.887  -32.425 8.261   1.00 38.19  ? 72  ASN   C OD1 1 
ATOM   1996 N ND2 . ASN   C 1 73 ? 18.543  -31.032 8.902   1.00 43.84  ? 72  ASN   C ND2 1 
ATOM   1997 N N   . LYS   C 1 74 ? 15.334  -32.527 5.679   1.00 39.76  ? 73  LYS   C N   1 
ATOM   1998 C CA  . LYS   C 1 74 ? 14.088  -33.264 5.526   1.00 38.31  ? 73  LYS   C CA  1 
ATOM   1999 C C   . LYS   C 1 74 ? 13.909  -34.238 6.685   1.00 39.82  ? 73  LYS   C C   1 
ATOM   2000 O O   . LYS   C 1 74 ? 12.889  -34.914 6.754   1.00 50.18  ? 73  LYS   C O   1 
ATOM   2001 C CB  . LYS   C 1 74 ? 14.011  -33.875 4.116   1.00 35.81  ? 73  LYS   C CB  1 
ATOM   2002 N N   . ARG   C 1 75 ? 14.891  -34.313 7.603   1.00 36.37  ? 74  ARG   C N   1 
ATOM   2003 C CA  . ARG   C 1 75 ? 14.736  -35.175 8.769   1.00 37.38  ? 74  ARG   C CA  1 
ATOM   2004 C C   . ARG   C 1 75 ? 13.445  -34.814 9.495   1.00 38.22  ? 74  ARG   C C   1 
ATOM   2005 O O   . ARG   C 1 75 ? 13.085  -33.640 9.567   1.00 34.85  ? 74  ARG   C O   1 
ATOM   2006 C CB  . ARG   C 1 75 ? 15.905  -35.165 9.764   1.00 32.80  ? 74  ARG   C CB  1 
ATOM   2007 C CG  . ARG   C 1 75 ? 17.183  -35.600 9.054   1.00 37.34  ? 74  ARG   C CG  1 
ATOM   2008 C CD  . ARG   C 1 75 ? 17.193  -37.012 8.490   1.00 40.81  ? 74  ARG   C CD  1 
ATOM   2009 N NE  . ARG   C 1 75 ? 17.228  -38.006 9.576   1.00 45.94  ? 74  ARG   C NE  1 
ATOM   2010 C CZ  . ARG   C 1 75 ? 18.293  -38.425 10.277  1.00 40.76  ? 74  ARG   C CZ  1 
ATOM   2011 N NH1 . ARG   C 1 75 ? 18.104  -39.141 11.375  1.00 44.95  ? 74  ARG   C NH1 1 
ATOM   2012 N NH2 . ARG   C 1 75 ? 19.521  -38.087 9.912   1.00 41.60  ? 74  ARG   C NH2 1 
ATOM   2013 N N   . LYS   C 1 76 ? 12.786  -35.830 10.062  1.00 39.92  ? 75  LYS   C N   1 
ATOM   2014 C CA  . LYS   C 1 76 ? 11.471  -35.637 10.655  1.00 41.53  ? 75  LYS   C CA  1 
ATOM   2015 C C   . LYS   C 1 76 ? 11.526  -34.639 11.817  1.00 37.04  ? 75  LYS   C C   1 
ATOM   2016 O O   . LYS   C 1 76 ? 12.256  -34.825 12.787  1.00 35.42  ? 75  LYS   C O   1 
ATOM   2017 C CB  . LYS   C 1 76 ? 10.829  -37.002 10.938  1.00 45.29  ? 75  LYS   C CB  1 
ATOM   2018 C CG  . LYS   C 1 76 ? 9.308   -36.950 10.998  1.00 60.49  ? 75  LYS   C CG  1 
ATOM   2019 C CD  . LYS   C 1 76 ? 8.704   -38.059 11.855  1.00 68.83  ? 75  LYS   C CD  1 
ATOM   2020 C CE  . LYS   C 1 76 ? 7.445   -37.657 12.556  1.00 66.06  ? 75  LYS   C CE  1 
ATOM   2021 N NZ  . LYS   C 1 76 ? 7.067   -38.693 13.524  1.00 71.83  ? 75  LYS   C NZ  1 
ATOM   2022 N N   . GLY   C 1 77 ? 10.724  -33.573 11.725  1.00 36.15  ? 76  GLY   C N   1 
ATOM   2023 C CA  . GLY   C 1 77 ? 10.556  -32.684 12.862  1.00 33.84  ? 76  GLY   C CA  1 
ATOM   2024 C C   . GLY   C 1 77 ? 11.558  -31.534 12.809  1.00 36.79  ? 76  GLY   C C   1 
ATOM   2025 O O   . GLY   C 1 77 ? 11.413  -30.527 13.508  1.00 36.35  ? 76  GLY   C O   1 
ATOM   2026 N N   . PHE   C 1 78 ? 12.549  -31.682 11.923  1.00 35.65  ? 77  PHE   C N   1 
ATOM   2027 C CA  . PHE   C 1 78 ? 13.641  -30.729 11.839  1.00 36.73  ? 77  PHE   C CA  1 
ATOM   2028 C C   . PHE   C 1 78 ? 13.089  -29.331 11.545  1.00 39.04  ? 77  PHE   C C   1 
ATOM   2029 O O   . PHE   C 1 78 ? 13.454  -28.369 12.233  1.00 37.46  ? 77  PHE   C O   1 
ATOM   2030 C CB  . PHE   C 1 78 ? 14.753  -31.118 10.854  1.00 31.97  ? 77  PHE   C CB  1 
ATOM   2031 C CG  . PHE   C 1 78 ? 16.038  -30.323 11.102  1.00 32.49  ? 77  PHE   C CG  1 
ATOM   2032 C CD1 . PHE   C 1 78 ? 16.217  -29.040 10.586  1.00 31.88  ? 77  PHE   C CD1 1 
ATOM   2033 C CD2 . PHE   C 1 78 ? 17.096  -30.870 11.822  1.00 30.03  ? 77  PHE   C CD2 1 
ATOM   2034 C CE1 . PHE   C 1 78 ? 17.399  -28.330 10.820  1.00 30.83  ? 77  PHE   C CE1 1 
ATOM   2035 C CE2 . PHE   C 1 78 ? 18.278  -30.151 12.066  1.00 29.84  ? 77  PHE   C CE2 1 
ATOM   2036 C CZ  . PHE   C 1 78 ? 18.432  -28.881 11.555  1.00 28.88  ? 77  PHE   C CZ  1 
ATOM   2037 N N   . ASN   C 1 79 ? 12.270  -29.197 10.491  1.00 31.99  ? 78  ASN   C N   1 
ATOM   2038 C CA  . ASN   C 1 79 ? 11.906  -27.841 10.119  1.00 35.24  ? 78  ASN   C CA  1 
ATOM   2039 C C   . ASN   C 1 79 ? 10.955  -27.213 11.138  1.00 33.12  ? 78  ASN   C C   1 
ATOM   2040 O O   . ASN   C 1 79 ? 11.087  -26.035 11.474  1.00 32.04  ? 78  ASN   C O   1 
ATOM   2041 C CB  . ASN   C 1 79 ? 11.549  -27.656 8.646   1.00 36.04  ? 78  ASN   C CB  1 
ATOM   2042 C CG  . ASN   C 1 79 ? 12.636  -28.157 7.713   1.00 40.68  ? 78  ASN   C CG  1 
ATOM   2043 O OD1 . ASN   C 1 79 ? 13.836  -27.954 7.946   1.00 37.01  ? 78  ASN   C OD1 1 
ATOM   2044 N ND2 . ASN   C 1 79 ? 12.232  -28.791 6.626   1.00 33.27  ? 78  ASN   C ND2 1 
ATOM   2045 N N   . GLU   C 1 80 ? 10.013  -27.970 11.690  1.00 40.19  ? 79  GLU   C N   1 
ATOM   2046 C CA  . GLU   C 1 80 ? 9.224   -27.383 12.774  1.00 38.62  ? 79  GLU   C CA  1 
ATOM   2047 C C   . GLU   C 1 80 ? 10.151  -26.980 13.921  1.00 39.55  ? 79  GLU   C C   1 
ATOM   2048 O O   . GLU   C 1 80 ? 9.945   -25.924 14.530  1.00 36.45  ? 79  GLU   C O   1 
ATOM   2049 C CB  . GLU   C 1 80 ? 8.069   -28.295 13.174  1.00 41.82  ? 79  GLU   C CB  1 
ATOM   2050 C CG  . GLU   C 1 80 ? 7.498   -28.003 14.557  1.00 44.46  ? 79  GLU   C CG  1 
ATOM   2051 C CD  . GLU   C 1 80 ? 6.263   -28.883 14.623  1.00 62.43  ? 79  GLU   C CD  1 
ATOM   2052 O OE1 . GLU   C 1 80 ? 6.358   -30.060 14.192  1.00 64.13  ? 79  GLU   C OE1 1 
ATOM   2053 O OE2 . GLU   C 1 80 ? 5.200   -28.393 15.061  1.00 62.70  ? 79  GLU   C OE2 1 
ATOM   2054 N N   . GLY   C 1 81 ? 11.215  -27.792 14.132  1.00 36.10  ? 80  GLY   C N   1 
ATOM   2055 C CA  . GLY   C 1 81 ? 12.281  -27.495 15.086  1.00 30.49  ? 80  GLY   C CA  1 
ATOM   2056 C C   . GLY   C 1 81 ? 12.883  -26.099 14.901  1.00 32.35  ? 80  GLY   C C   1 
ATOM   2057 O O   . GLY   C 1 81 ? 13.113  -25.386 15.870  1.00 35.69  ? 80  GLY   C O   1 
ATOM   2058 N N   . LEU   C 1 82 ? 13.224  -25.748 13.654  1.00 34.50  ? 81  LEU   C N   1 
ATOM   2059 C CA  . LEU   C 1 82 ? 13.838  -24.467 13.331  1.00 37.00  ? 81  LEU   C CA  1 
ATOM   2060 C C   . LEU   C 1 82 ? 12.828  -23.353 13.595  1.00 36.27  ? 81  LEU   C C   1 
ATOM   2061 O O   . LEU   C 1 82 ? 13.202  -22.266 14.046  1.00 36.64  ? 81  LEU   C O   1 
ATOM   2062 C CB  . LEU   C 1 82 ? 14.314  -24.401 11.874  1.00 34.66  ? 81  LEU   C CB  1 
ATOM   2063 C CG  . LEU   C 1 82 ? 15.400  -25.396 11.465  1.00 32.43  ? 81  LEU   C CG  1 
ATOM   2064 C CD1 . LEU   C 1 82 ? 15.615  -25.264 9.935   1.00 34.26  ? 81  LEU   C CD1 1 
ATOM   2065 C CD2 . LEU   C 1 82 ? 16.633  -24.979 12.241  1.00 27.90  ? 81  LEU   C CD2 1 
ATOM   2066 N N   . TRP   C 1 83 ? 11.549  -23.643 13.339  1.00 33.73  ? 82  TRP   C N   1 
ATOM   2067 C CA  . TRP   C 1 83 ? 10.528  -22.651 13.650  1.00 43.24  ? 82  TRP   C CA  1 
ATOM   2068 C C   . TRP   C 1 83 ? 10.449  -22.362 15.165  1.00 42.73  ? 82  TRP   C C   1 
ATOM   2069 O O   . TRP   C 1 83 ? 10.512  -21.210 15.598  1.00 38.92  ? 82  TRP   C O   1 
ATOM   2070 C CB  . TRP   C 1 83 ? 9.180   -23.009 12.999  1.00 41.46  ? 82  TRP   C CB  1 
ATOM   2071 C CG  . TRP   C 1 83 ? 8.167   -21.897 13.151  1.00 48.80  ? 82  TRP   C CG  1 
ATOM   2072 C CD1 . TRP   C 1 83 ? 7.934   -20.848 12.309  1.00 42.89  ? 82  TRP   C CD1 1 
ATOM   2073 C CD2 . TRP   C 1 83 ? 7.291   -21.700 14.285  1.00 51.73  ? 82  TRP   C CD2 1 
ATOM   2074 N NE1 . TRP   C 1 83 ? 6.965   -20.031 12.825  1.00 50.99  ? 82  TRP   C NE1 1 
ATOM   2075 C CE2 . TRP   C 1 83 ? 6.550   -20.529 14.029  1.00 48.92  ? 82  TRP   C CE2 1 
ATOM   2076 C CE3 . TRP   C 1 83 ? 7.055   -22.414 15.470  1.00 48.54  ? 82  TRP   C CE3 1 
ATOM   2077 C CZ2 . TRP   C 1 83 ? 5.599   -20.057 14.926  1.00 58.19  ? 82  TRP   C CZ2 1 
ATOM   2078 C CZ3 . TRP   C 1 83 ? 6.110   -21.948 16.357  1.00 50.52  ? 82  TRP   C CZ3 1 
ATOM   2079 C CH2 . TRP   C 1 83 ? 5.404   -20.776 16.087  1.00 52.92  ? 82  TRP   C CH2 1 
ATOM   2080 N N   . GLU   C 1 84 ? 10.334  -23.411 15.982  1.00 41.83  ? 83  GLU   C N   1 
ATOM   2081 C CA  . GLU   C 1 84 ? 10.274  -23.263 17.433  1.00 41.67  ? 83  GLU   C CA  1 
ATOM   2082 C C   . GLU   C 1 84 ? 11.459  -22.464 17.973  1.00 44.34  ? 83  GLU   C C   1 
ATOM   2083 O O   . GLU   C 1 84 ? 11.256  -21.537 18.765  1.00 43.21  ? 83  GLU   C O   1 
ATOM   2084 C CB  . GLU   C 1 84 ? 10.081  -24.604 18.140  1.00 39.09  ? 83  GLU   C CB  1 
ATOM   2085 C CG  . GLU   C 1 84 ? 8.782   -25.279 17.707  1.00 38.32  ? 83  GLU   C CG  1 
ATOM   2086 C CD  . GLU   C 1 84 ? 8.706   -26.708 18.165  1.00 43.26  ? 83  GLU   C CD  1 
ATOM   2087 O OE1 . GLU   C 1 84 ? 9.711   -27.165 18.740  1.00 46.36  ? 83  GLU   C OE1 1 
ATOM   2088 O OE2 . GLU   C 1 84 ? 7.666   -27.365 17.951  1.00 49.21  ? 83  GLU   C OE2 1 
ATOM   2089 N N   . ILE   C 1 85 ? 12.690  -22.763 17.522  1.00 42.52  ? 84  ILE   C N   1 
ATOM   2090 C CA  . ILE   C 1 85 ? 13.829  -22.200 18.245  1.00 39.40  ? 84  ILE   C CA  1 
ATOM   2091 C C   . ILE   C 1 85 ? 13.908  -20.687 18.016  1.00 43.19  ? 84  ILE   C C   1 
ATOM   2092 O O   . ILE   C 1 85 ? 14.350  -19.966 18.894  1.00 46.57  ? 84  ILE   C O   1 
ATOM   2093 C CB  . ILE   C 1 85 ? 15.151  -22.944 17.982  1.00 32.87  ? 84  ILE   C CB  1 
ATOM   2094 C CG1 . ILE   C 1 85 ? 16.266  -22.483 18.947  1.00 35.03  ? 84  ILE   C CG1 1 
ATOM   2095 C CG2 . ILE   C 1 85 ? 15.578  -22.836 16.515  1.00 36.43  ? 84  ILE   C CG2 1 
ATOM   2096 C CD1 . ILE   C 1 85 ? 17.536  -23.331 18.951  1.00 31.13  ? 84  ILE   C CD1 1 
ATOM   2097 N N   . GLN   C 1 86 ? 13.460  -20.236 16.839  1.00 45.43  ? 85  GLN   C N   1 
ATOM   2098 C CA  . GLN   C 1 86 ? 13.448  -18.847 16.387  1.00 49.05  ? 85  GLN   C CA  1 
ATOM   2099 C C   . GLN   C 1 86 ? 12.207  -18.145 16.933  1.00 42.60  ? 85  GLN   C C   1 
ATOM   2100 O O   . GLN   C 1 86 ? 12.303  -16.995 17.328  1.00 48.05  ? 85  GLN   C O   1 
ATOM   2101 C CB  . GLN   C 1 86 ? 13.407  -18.745 14.850  1.00 48.40  ? 85  GLN   C CB  1 
ATOM   2102 C CG  . GLN   C 1 86 ? 13.731  -17.370 14.258  1.00 43.11  ? 85  GLN   C CG  1 
ATOM   2103 C CD  . GLN   C 1 86 ? 14.157  -17.373 12.786  1.00 48.98  ? 85  GLN   C CD  1 
ATOM   2104 O OE1 . GLN   C 1 86 ? 13.950  -18.316 12.003  1.00 46.54  ? 85  GLN   C OE1 1 
ATOM   2105 N NE2 . GLN   C 1 86 ? 14.767  -16.278 12.363  1.00 42.58  ? 85  GLN   C NE2 1 
ATOM   2106 N N   . ASN   C 1 87 ? 11.072  -18.846 16.987  1.00 41.11  ? 86  ASN   C N   1 
ATOM   2107 C CA  . ASN   C 1 87 ? 9.770   -18.187 17.082  1.00 48.76  ? 86  ASN   C CA  1 
ATOM   2108 C C   . ASN   C 1 87 ? 9.017   -18.477 18.383  1.00 48.72  ? 86  ASN   C C   1 
ATOM   2109 O O   . ASN   C 1 87 ? 7.979   -17.872 18.600  1.00 52.78  ? 86  ASN   C O   1 
ATOM   2110 C CB  . ASN   C 1 87 ? 8.886   -18.459 15.864  1.00 45.50  ? 86  ASN   C CB  1 
ATOM   2111 C CG  . ASN   C 1 87 ? 9.557   -17.958 14.602  1.00 54.55  ? 86  ASN   C CG  1 
ATOM   2112 O OD1 . ASN   C 1 87 ? 9.817   -16.754 14.483  1.00 52.66  ? 86  ASN   C OD1 1 
ATOM   2113 N ND2 . ASN   C 1 87 ? 9.906   -18.851 13.682  1.00 43.99  ? 86  ASN   C ND2 1 
ATOM   2114 N N   . ASN   C 1 88 ? 9.501   -19.395 19.235  1.00 55.26  ? 87  ASN   C N   1 
ATOM   2115 C CA  . ASN   C 1 88 ? 8.767   -19.844 20.423  1.00 53.22  ? 87  ASN   C CA  1 
ATOM   2116 C C   . ASN   C 1 88 ? 9.675   -20.733 21.277  1.00 48.94  ? 87  ASN   C C   1 
ATOM   2117 O O   . ASN   C 1 88 ? 9.322   -21.874 21.604  1.00 50.13  ? 87  ASN   C O   1 
ATOM   2118 C CB  . ASN   C 1 88 ? 7.512   -20.650 20.065  1.00 56.85  ? 87  ASN   C CB  1 
ATOM   2119 C CG  . ASN   C 1 88 ? 6.506   -20.746 21.194  1.00 62.88  ? 87  ASN   C CG  1 
ATOM   2120 O OD1 . ASN   C 1 88 ? 6.560   -19.961 22.147  1.00 66.69  ? 87  ASN   C OD1 1 
ATOM   2121 N ND2 . ASN   C 1 88 ? 5.569   -21.680 21.104  1.00 58.49  ? 87  ASN   C ND2 1 
ATOM   2122 N N   . PRO   C 1 89 ? 10.890  -20.269 21.645  1.00 40.23  ? 88  PRO   C N   1 
ATOM   2123 C CA  . PRO   C 1 89 ? 11.866  -21.161 22.264  1.00 41.63  ? 88  PRO   C CA  1 
ATOM   2124 C C   . PRO   C 1 89 ? 11.627  -21.551 23.723  1.00 50.19  ? 88  PRO   C C   1 
ATOM   2125 O O   . PRO   C 1 89 ? 12.398  -22.353 24.243  1.00 53.74  ? 88  PRO   C O   1 
ATOM   2126 C CB  . PRO   C 1 89 ? 13.201  -20.406 22.054  1.00 45.83  ? 88  PRO   C CB  1 
ATOM   2127 C CG  . PRO   C 1 89 ? 12.793  -18.935 22.090  1.00 42.27  ? 88  PRO   C CG  1 
ATOM   2128 C CD  . PRO   C 1 89 ? 11.382  -18.891 21.487  1.00 38.85  ? 88  PRO   C CD  1 
ATOM   2129 N N   . HIS   C 1 90 ? 10.577  -21.010 24.375  1.00 53.19  ? 89  HIS   C N   1 
ATOM   2130 C CA  . HIS   C 1 90 ? 10.371  -21.276 25.798  1.00 49.67  ? 89  HIS   C CA  1 
ATOM   2131 C C   . HIS   C 1 90 ? 8.938   -21.724 26.117  1.00 52.84  ? 89  HIS   C C   1 
ATOM   2132 O O   . HIS   C 1 90 ? 8.514   -21.637 27.257  1.00 58.61  ? 89  HIS   C O   1 
ATOM   2133 C CB  . HIS   C 1 90 ? 10.995  -20.196 26.703  1.00 42.93  ? 89  HIS   C CB  1 
ATOM   2134 C CG  . HIS   C 1 90 ? 12.415  -19.770 26.383  1.00 47.54  ? 89  HIS   C CG  1 
ATOM   2135 N ND1 . HIS   C 1 90 ? 12.726  -18.576 25.759  1.00 54.65  ? 89  HIS   C ND1 1 
ATOM   2136 C CD2 . HIS   C 1 90 ? 13.614  -20.344 26.627  1.00 50.69  ? 89  HIS   C CD2 1 
ATOM   2137 C CE1 . HIS   C 1 90 ? 14.053  -18.444 25.618  1.00 44.87  ? 89  HIS   C CE1 1 
ATOM   2138 N NE2 . HIS   C 1 90 ? 14.613  -19.508 26.145  1.00 46.91  ? 89  HIS   C NE2 1 
ATOM   2139 N N   . ALA   C 1 91 ? 8.197   -22.245 25.133  1.00 62.96  ? 90  ALA   C N   1 
ATOM   2140 C CA  . ALA   C 1 91 ? 6.921   -22.920 25.382  1.00 77.03  ? 90  ALA   C CA  1 
ATOM   2141 C C   . ALA   C 1 91 ? 7.124   -24.286 26.062  1.00 78.45  ? 90  ALA   C C   1 
ATOM   2142 O O   . ALA   C 1 91 ? 8.253   -24.667 26.352  1.00 87.26  ? 90  ALA   C O   1 
ATOM   2143 C CB  . ALA   C 1 91 ? 6.135   -23.033 24.086  1.00 64.93  ? 90  ALA   C CB  1 
ATOM   2144 N N   . SER   C 1 92 ? 6.034   -25.041 26.291  1.00 78.60  ? 91  SER   C N   1 
ATOM   2145 C CA  . SER   C 1 92 ? 6.035   -26.195 27.193  1.00 79.80  ? 91  SER   C CA  1 
ATOM   2146 C C   . SER   C 1 92 ? 6.058   -27.549 26.475  1.00 81.56  ? 91  SER   C C   1 
ATOM   2147 O O   . SER   C 1 92 ? 6.824   -28.434 26.855  1.00 77.41  ? 91  SER   C O   1 
ATOM   2148 C CB  . SER   C 1 92 ? 4.894   -26.130 28.200  1.00 76.09  ? 91  SER   C CB  1 
ATOM   2149 O OG  . SER   C 1 92 ? 5.231   -25.316 29.318  1.00 74.98  ? 91  SER   C OG  1 
ATOM   2150 N N   . TYR   C 1 93 ? 5.164   -27.746 25.496  1.00 90.58  ? 92  TYR   C N   1 
ATOM   2151 C CA  . TYR   C 1 93 ? 5.094   -28.985 24.725  1.00 96.11  ? 92  TYR   C CA  1 
ATOM   2152 C C   . TYR   C 1 93 ? 4.829   -30.199 25.661  1.00 95.17  ? 92  TYR   C C   1 
ATOM   2153 O O   . TYR   C 1 93 ? 3.688   -30.746 25.779  1.00 81.21  ? 92  TYR   C O   1 
ATOM   2154 C CB  . TYR   C 1 93 ? 6.370   -29.148 23.888  1.00 94.48  ? 92  TYR   C CB  1 
ATOM   2155 C CG  . TYR   C 1 93 ? 6.831   -27.923 23.098  1.00 93.26  ? 92  TYR   C CG  1 
ATOM   2156 C CD1 . TYR   C 1 93 ? 6.363   -27.676 21.807  1.00 92.89  ? 92  TYR   C CD1 1 
ATOM   2157 C CD2 . TYR   C 1 93 ? 7.752   -27.021 23.630  1.00 81.96  ? 92  TYR   C CD2 1 
ATOM   2158 C CE1 . TYR   C 1 93 ? 6.786   -26.574 21.076  1.00 82.31  ? 92  TYR   C CE1 1 
ATOM   2159 C CE2 . TYR   C 1 93 ? 8.183   -25.917 22.907  1.00 81.98  ? 92  TYR   C CE2 1 
ATOM   2160 C CZ  . TYR   C 1 93 ? 7.703   -25.692 21.626  1.00 82.83  ? 92  TYR   C CZ  1 
ATOM   2161 O OH  . TYR   C 1 93 ? 8.118   -24.595 20.918  1.00 79.76  ? 92  TYR   C OH  1 
HETATM 2162 S S   . SO4   D 2 .  ? 0.775   -33.549 2.330   1.00 95.74  ? 101 SO4   A S   1 
HETATM 2163 O O1  . SO4   D 2 .  ? 1.309   -34.217 1.159   1.00 77.94  ? 101 SO4   A O1  1 
HETATM 2164 O O2  . SO4   D 2 .  ? 0.712   -32.125 2.113   1.00 105.54 ? 101 SO4   A O2  1 
HETATM 2165 O O3  . SO4   D 2 .  ? -0.555  -34.049 2.598   1.00 107.31 ? 101 SO4   A O3  1 
HETATM 2166 O O4  . SO4   D 2 .  ? 1.631   -33.801 3.458   1.00 89.87  ? 101 SO4   A O4  1 
HETATM 2167 S S   . SO4   E 2 .  ? -9.953  -24.417 1.293   1.00 99.85  ? 102 SO4   A S   1 
HETATM 2168 O O1  . SO4   E 2 .  ? -9.713  -24.201 -0.108  1.00 102.21 ? 102 SO4   A O1  1 
HETATM 2169 O O2  . SO4   E 2 .  ? -10.014 -23.149 1.968   1.00 105.76 ? 102 SO4   A O2  1 
HETATM 2170 O O3  . SO4   E 2 .  ? -11.201 -25.116 1.454   1.00 108.63 ? 102 SO4   A O3  1 
HETATM 2171 O O4  . SO4   E 2 .  ? -8.884  -25.200 1.856   1.00 99.47  ? 102 SO4   A O4  1 
HETATM 2172 C C1  . EDO   F 3 .  ? 13.557  -19.591 -7.394  1.00 44.59  ? 103 EDO   A C1  1 
HETATM 2173 O O1  . EDO   F 3 .  ? 14.776  -18.813 -7.306  1.00 39.20  ? 103 EDO   A O1  1 
HETATM 2174 C C2  . EDO   F 3 .  ? 12.556  -19.127 -8.430  1.00 42.18  ? 103 EDO   A C2  1 
HETATM 2175 O O2  . EDO   F 3 .  ? 12.199  -17.752 -8.266  1.00 36.34  ? 103 EDO   A O2  1 
HETATM 2176 N N1  . A1A38 G 4 .  ? -0.411  -26.117 -6.586  0.88 48.36  ? 104 A1A38 A N1  1 
HETATM 2177 C C4  . A1A38 G 4 .  ? 1.529   -24.382 -5.695  0.88 48.53  ? 104 A1A38 A C4  1 
HETATM 2178 C C5  . A1A38 G 4 .  ? 1.291   -24.527 -7.040  0.88 42.62  ? 104 A1A38 A C5  1 
HETATM 2179 C C6  . A1A38 G 4 .  ? 0.314   -25.397 -7.436  0.88 43.28  ? 104 A1A38 A C6  1 
HETATM 2180 C C7  . A1A38 G 4 .  ? -0.181  -25.961 -5.284  0.88 45.54  ? 104 A1A38 A C7  1 
HETATM 2181 O O   . A1A38 G 4 .  ? 3.088   -25.434 -3.566  0.88 43.05  ? 104 A1A38 A O   1 
HETATM 2182 C C1  . A1A38 G 4 .  ? 2.186   -25.073 -2.857  0.88 42.60  ? 104 A1A38 A C1  1 
HETATM 2183 C C2  . A1A38 G 4 .  ? 2.334   -24.730 -1.432  0.88 43.35  ? 104 A1A38 A C2  1 
HETATM 2184 N N   . A1A38 G 4 .  ? 0.970   -24.935 -3.378  0.88 49.82  ? 104 A1A38 A N   1 
HETATM 2185 C C   . A1A38 G 4 .  ? -0.110  -24.484 -2.509  0.88 42.21  ? 104 A1A38 A C   1 
HETATM 2186 C C3  . A1A38 G 4 .  ? 0.772   -25.110 -4.790  0.88 45.43  ? 104 A1A38 A C3  1 
HETATM 2187 S S   . SO4   H 2 .  ? 8.490   -29.265 6.000   1.00 72.31  ? 105 SO4   A S   1 
HETATM 2188 O O1  . SO4   H 2 .  ? 9.347   -28.398 5.243   1.00 77.33  ? 105 SO4   A O1  1 
HETATM 2189 O O2  . SO4   H 2 .  ? 7.989   -30.317 5.149   1.00 74.74  ? 105 SO4   A O2  1 
HETATM 2190 O O3  . SO4   H 2 .  ? 9.246   -29.831 7.094   1.00 74.24  ? 105 SO4   A O3  1 
HETATM 2191 O O4  . SO4   H 2 .  ? 7.368   -28.514 6.507   1.00 89.13  ? 105 SO4   A O4  1 
HETATM 2192 S S   . SO4   I 2 .  ? 7.307   -8.599  -24.861 1.00 80.56  ? 101 SO4   B S   1 
HETATM 2193 O O1  . SO4   I 2 .  ? 8.451   -8.876  -25.691 1.00 63.81  ? 101 SO4   B O1  1 
HETATM 2194 O O2  . SO4   I 2 .  ? 6.108   -9.027  -25.537 1.00 69.95  ? 101 SO4   B O2  1 
HETATM 2195 O O3  . SO4   I 2 .  ? 7.375   -9.321  -23.590 1.00 55.49  ? 101 SO4   B O3  1 
HETATM 2196 O O4  . SO4   I 2 .  ? 7.289   -7.170  -24.632 1.00 66.43  ? 101 SO4   B O4  1 
HETATM 2197 S S   . SO4   J 2 .  ? 14.169  -27.147 -26.544 1.00 72.02  ? 102 SO4   B S   1 
HETATM 2198 O O1  . SO4   J 2 .  ? 15.022  -26.388 -25.666 1.00 57.11  ? 102 SO4   B O1  1 
HETATM 2199 O O2  . SO4   J 2 .  ? 14.996  -28.044 -27.313 1.00 83.34  ? 102 SO4   B O2  1 
HETATM 2200 O O3  . SO4   J 2 .  ? 13.208  -27.909 -25.787 1.00 84.76  ? 102 SO4   B O3  1 
HETATM 2201 O O4  . SO4   J 2 .  ? 13.449  -26.261 -27.432 1.00 77.82  ? 102 SO4   B O4  1 
HETATM 2202 N N1  . A1A38 K 4 .  ? 20.284  -16.740 -21.562 0.94 71.44  ? 103 A1A38 B N1  1 
HETATM 2203 C C4  . A1A38 K 4 .  ? 20.461  -15.712 -24.138 0.94 65.19  ? 103 A1A38 B C4  1 
HETATM 2204 C C5  . A1A38 K 4 .  ? 21.602  -15.925 -23.389 0.94 58.59  ? 103 A1A38 B C5  1 
HETATM 2205 C C6  . A1A38 K 4 .  ? 21.465  -16.436 -22.112 0.94 66.57  ? 103 A1A38 B C6  1 
HETATM 2206 C C7  . A1A38 K 4 .  ? 19.188  -16.546 -22.304 0.94 61.24  ? 103 A1A38 B C7  1 
HETATM 2207 O O   . A1A38 K 4 .  ? 17.891  -13.602 -23.974 0.94 52.54  ? 103 A1A38 B O   1 
HETATM 2208 C C1  . A1A38 K 4 .  ? 17.444  -14.568 -24.544 0.94 42.52  ? 103 A1A38 B C1  1 
HETATM 2209 C C2  . A1A38 K 4 .  ? 16.308  -14.448 -25.499 0.94 37.43  ? 103 A1A38 B C2  1 
HETATM 2210 N N   . A1A38 K 4 .  ? 18.022  -15.807 -24.337 0.94 46.60  ? 103 A1A38 B N   1 
HETATM 2211 C C   . A1A38 K 4 .  ? 17.434  -16.970 -24.975 0.94 42.02  ? 103 A1A38 B C   1 
HETATM 2212 C C3  . A1A38 K 4 .  ? 19.223  -16.030 -23.589 0.94 56.42  ? 103 A1A38 B C3  1 
HETATM 2213 S S   . SO4   L 2 .  ? 28.942  -38.227 12.663  1.00 120.37 ? 101 SO4   C S   1 
HETATM 2214 O O1  . SO4   L 2 .  ? 30.109  -37.387 12.763  1.00 111.77 ? 101 SO4   C O1  1 
HETATM 2215 O O2  . SO4   L 2 .  ? 28.008  -37.660 11.721  1.00 110.64 ? 101 SO4   C O2  1 
HETATM 2216 O O3  . SO4   L 2 .  ? 29.325  -39.540 12.221  1.00 103.10 ? 101 SO4   C O3  1 
HETATM 2217 O O4  . SO4   L 2 .  ? 28.322  -38.327 13.957  1.00 139.66 ? 101 SO4   C O4  1 
HETATM 2218 N N1  . A1A38 M 4 .  ? 16.936  -40.020 20.209  0.64 45.16  ? 102 A1A38 C N1  1 
HETATM 2219 C C4  . A1A38 M 4 .  ? 16.701  -37.328 20.842  0.64 41.43  ? 102 A1A38 C C4  1 
HETATM 2220 C C5  . A1A38 M 4 .  ? 16.631  -38.293 21.831  0.64 42.83  ? 102 A1A38 C C5  1 
HETATM 2221 C C6  . A1A38 M 4 .  ? 16.756  -39.619 21.471  0.64 36.78  ? 102 A1A38 C C6  1 
HETATM 2222 C C7  . A1A38 M 4 .  ? 16.997  -39.078 19.259  0.64 41.44  ? 102 A1A38 C C7  1 
HETATM 2223 O O   . A1A38 M 4 .  ? 14.898  -35.974 18.589  0.64 30.73  ? 102 A1A38 C O   1 
HETATM 2224 C C1  . A1A38 M 4 .  ? 15.999  -35.855 18.127  0.64 32.37  ? 102 A1A38 C C1  1 
HETATM 2225 C C2  . A1A38 M 4 .  ? 16.320  -34.718 17.242  0.64 29.84  ? 102 A1A38 C C2  1 
HETATM 2226 N N   . A1A38 M 4 .  ? 17.024  -36.738 18.483  0.64 36.94  ? 102 A1A38 C N   1 
HETATM 2227 C C   . A1A38 M 4 .  ? 18.350  -36.620 17.884  0.64 29.12  ? 102 A1A38 C C   1 
HETATM 2228 C C3  . A1A38 M 4 .  ? 16.888  -37.722 19.524  0.64 41.14  ? 102 A1A38 C C3  1 
HETATM 2229 O O   . HOH   N 5 .  ? 10.613  -9.195  -12.705 1.00 53.65  ? 201 HOH   A O   1 
HETATM 2230 O O   . HOH   N 5 .  ? -5.709  -13.216 -16.630 1.00 67.20  ? 202 HOH   A O   1 
HETATM 2231 O O   . HOH   N 5 .  ? 5.378   -29.119 6.969   1.00 45.50  ? 203 HOH   A O   1 
HETATM 2232 O O   . HOH   N 5 .  ? 8.516   -32.254 4.228   1.00 58.65  ? 204 HOH   A O   1 
HETATM 2233 O O   . HOH   N 5 .  ? 9.880   -18.656 10.417  1.00 62.40  ? 205 HOH   A O   1 
HETATM 2234 O O   . HOH   N 5 .  ? 0.077   -11.068 -15.413 1.00 100.19 ? 206 HOH   A O   1 
HETATM 2235 O O   . HOH   N 5 .  ? -9.438  -15.241 10.907  1.00 62.27  ? 207 HOH   A O   1 
HETATM 2236 O O   . HOH   N 5 .  ? -0.070  -33.651 5.130   1.00 46.11  ? 208 HOH   A O   1 
HETATM 2237 O O   . HOH   N 5 .  ? 3.807   -10.264 13.631  1.00 56.51  ? 209 HOH   A O   1 
HETATM 2238 O O   . HOH   N 5 .  ? -1.020  -28.802 9.949   1.00 57.44  ? 210 HOH   A O   1 
HETATM 2239 O O   . HOH   N 5 .  ? -6.015  -15.761 -7.912  1.00 32.78  ? 211 HOH   A O   1 
HETATM 2240 O O   . HOH   N 5 .  ? -8.691  -20.967 -1.050  1.00 56.62  ? 212 HOH   A O   1 
HETATM 2241 O O   . HOH   N 5 .  ? -4.816  -21.057 6.128   1.00 38.04  ? 213 HOH   A O   1 
HETATM 2242 O O   . HOH   N 5 .  ? 10.648  -29.586 3.208   1.00 46.19  ? 214 HOH   A O   1 
HETATM 2243 O O   . HOH   N 5 .  ? -8.083  -15.845 -1.180  1.00 42.73  ? 215 HOH   A O   1 
HETATM 2244 O O   . HOH   N 5 .  ? 8.025   -8.467  4.541   1.00 53.76  ? 216 HOH   A O   1 
HETATM 2245 O O   . HOH   N 5 .  ? 13.861  -29.164 4.338   1.00 76.00  ? 217 HOH   A O   1 
HETATM 2246 O O   . HOH   N 5 .  ? 1.533   -4.792  -10.271 1.00 48.88  ? 218 HOH   A O   1 
HETATM 2247 O O   . HOH   N 5 .  ? -7.700  -21.430 -5.306  1.00 74.15  ? 219 HOH   A O   1 
HETATM 2248 O O   . HOH   N 5 .  ? 15.394  -24.308 2.209   1.00 47.91  ? 220 HOH   A O   1 
HETATM 2249 O O   . HOH   N 5 .  ? 6.645   -10.640 -12.061 1.00 38.93  ? 221 HOH   A O   1 
HETATM 2250 O O   . HOH   N 5 .  ? -6.285  -11.473 -11.084 1.00 45.02  ? 222 HOH   A O   1 
HETATM 2251 O O   . HOH   N 5 .  ? 12.581  -9.457  -7.396  1.00 46.74  ? 223 HOH   A O   1 
HETATM 2252 O O   . HOH   N 5 .  ? 9.064   -6.504  9.076   1.00 69.04  ? 224 HOH   A O   1 
HETATM 2253 O O   . HOH   N 5 .  ? 12.408  -12.088 7.894   1.00 82.55  ? 225 HOH   A O   1 
HETATM 2254 O O   . HOH   N 5 .  ? -8.367  -16.528 2.370   1.00 44.24  ? 226 HOH   A O   1 
HETATM 2255 O O   . HOH   N 5 .  ? 10.349  -5.124  -7.679  1.00 36.85  ? 227 HOH   A O   1 
HETATM 2256 O O   . HOH   N 5 .  ? 13.666  -15.736 -9.207  1.00 31.89  ? 228 HOH   A O   1 
HETATM 2257 O O   . HOH   N 5 .  ? -2.819  3.305   -1.970  1.00 44.62  ? 229 HOH   A O   1 
HETATM 2258 O O   . HOH   N 5 .  ? 8.613   -22.907 -9.445  1.00 44.86  ? 230 HOH   A O   1 
HETATM 2259 O O   . HOH   N 5 .  ? -5.781  -25.574 -5.658  1.00 52.38  ? 231 HOH   A O   1 
HETATM 2260 O O   . HOH   N 5 .  ? 15.390  -12.083 -5.149  1.00 40.51  ? 232 HOH   A O   1 
HETATM 2261 O O   . HOH   N 5 .  ? 16.860  -12.891 1.406   1.00 22.06  ? 233 HOH   A O   1 
HETATM 2262 O O   . HOH   N 5 .  ? -4.035  -10.428 6.819   1.00 59.10  ? 234 HOH   A O   1 
HETATM 2263 O O   . HOH   N 5 .  ? 10.661  -23.522 9.974   1.00 46.90  ? 235 HOH   A O   1 
HETATM 2264 O O   . HOH   N 5 .  ? -5.918  -19.242 -5.516  1.00 44.51  ? 236 HOH   A O   1 
HETATM 2265 O O   . HOH   N 5 .  ? 19.422  -15.469 7.297   1.00 34.17  ? 237 HOH   A O   1 
HETATM 2266 O O   . HOH   N 5 .  ? 8.329   -17.863 -16.118 1.00 44.33  ? 238 HOH   A O   1 
HETATM 2267 O O   . HOH   N 5 .  ? 8.628   -18.326 -10.940 1.00 34.66  ? 239 HOH   A O   1 
HETATM 2268 O O   . HOH   N 5 .  ? -2.289  -22.027 -0.481  1.00 29.92  ? 240 HOH   A O   1 
HETATM 2269 O O   . HOH   N 5 .  ? 8.876   -30.403 9.733   1.00 36.88  ? 241 HOH   A O   1 
HETATM 2270 O O   . HOH   N 5 .  ? 1.759   -25.222 -10.323 1.00 40.42  ? 242 HOH   A O   1 
HETATM 2271 O O   . HOH   N 5 .  ? 11.109  -11.991 5.933   1.00 44.13  ? 243 HOH   A O   1 
HETATM 2272 O O   . HOH   N 5 .  ? 12.270  -15.642 -11.988 1.00 50.90  ? 244 HOH   A O   1 
HETATM 2273 O O   . HOH   N 5 .  ? 7.593   -7.971  1.133   1.00 35.63  ? 245 HOH   A O   1 
HETATM 2274 O O   . HOH   N 5 .  ? 9.292   -6.385  -1.654  1.00 55.56  ? 246 HOH   A O   1 
HETATM 2275 O O   . HOH   N 5 .  ? 11.031  -12.426 -6.104  1.00 31.29  ? 247 HOH   A O   1 
HETATM 2276 O O   . HOH   N 5 .  ? 10.751  -6.227  -3.889  1.00 42.36  ? 248 HOH   A O   1 
HETATM 2277 O O   . HOH   N 5 .  ? 10.885  -16.544 -14.879 1.00 40.74  ? 249 HOH   A O   1 
HETATM 2278 O O   . HOH   N 5 .  ? 4.174   -7.796  0.814   1.00 36.88  ? 250 HOH   A O   1 
HETATM 2279 O O   . HOH   N 5 .  ? 4.043   -3.360  -3.202  1.00 35.12  ? 251 HOH   A O   1 
HETATM 2280 O O   . HOH   N 5 .  ? 1.522   -10.294 11.637  1.00 43.81  ? 252 HOH   A O   1 
HETATM 2281 O O   . HOH   N 5 .  ? -1.060  -20.705 7.100   1.00 39.18  ? 253 HOH   A O   1 
HETATM 2282 O O   . HOH   N 5 .  ? 7.542   -2.408  -0.175  1.00 61.66  ? 254 HOH   A O   1 
HETATM 2283 O O   . HOH   N 5 .  ? -0.286  -23.277 9.591   1.00 43.30  ? 255 HOH   A O   1 
HETATM 2284 O O   . HOH   N 5 .  ? -6.528  -12.666 6.537   1.00 44.45  ? 256 HOH   A O   1 
HETATM 2285 O O   . HOH   N 5 .  ? 12.307  -13.162 -8.654  1.00 40.56  ? 257 HOH   A O   1 
HETATM 2286 O O   . HOH   N 5 .  ? 7.993   -17.670 8.765   1.00 57.75  ? 258 HOH   A O   1 
HETATM 2287 O O   . HOH   N 5 .  ? 12.946  -11.986 -4.269  1.00 23.82  ? 259 HOH   A O   1 
HETATM 2288 O O   . HOH   N 5 .  ? -1.672  -7.463  11.528  1.00 55.81  ? 260 HOH   A O   1 
HETATM 2289 O O   . HOH   N 5 .  ? -1.907  -11.636 11.181  1.00 53.10  ? 261 HOH   A O   1 
HETATM 2290 O O   . HOH   N 5 .  ? 5.998   -5.914  0.357   1.00 51.70  ? 262 HOH   A O   1 
HETATM 2291 O O   . HOH   N 5 .  ? 2.558   -6.316  5.521   1.00 44.79  ? 263 HOH   A O   1 
HETATM 2292 O O   . HOH   N 5 .  ? 2.622   -29.792 -0.228  1.00 46.89  ? 264 HOH   A O   1 
HETATM 2293 O O   . HOH   N 5 .  ? -4.254  -8.045  10.257  1.00 51.16  ? 265 HOH   A O   1 
HETATM 2294 O O   . HOH   N 5 .  ? 6.452   -16.596 -14.819 1.00 61.47  ? 266 HOH   A O   1 
HETATM 2295 O O   . HOH   N 5 .  ? 22.098  -16.829 -0.128  1.00 50.52  ? 267 HOH   A O   1 
HETATM 2296 O O   . HOH   N 5 .  ? 2.724   -10.095 -13.458 1.00 63.71  ? 268 HOH   A O   1 
HETATM 2297 O O   . HOH   N 5 .  ? 8.372   -16.367 -13.062 1.00 40.15  ? 269 HOH   A O   1 
HETATM 2298 O O   . HOH   N 5 .  ? -8.217  -17.505 6.954   1.00 50.49  ? 270 HOH   A O   1 
HETATM 2299 O O   . HOH   N 5 .  ? 0.519   -17.927 -19.196 1.00 47.45  ? 271 HOH   A O   1 
HETATM 2300 O O   . HOH   N 5 .  ? 9.242   -20.378 -18.445 1.00 48.46  ? 272 HOH   A O   1 
HETATM 2301 O O   . HOH   N 5 .  ? 4.708   -7.590  3.892   1.00 39.00  ? 273 HOH   A O   1 
HETATM 2302 O O   . HOH   N 5 .  ? -0.803  -20.449 11.162  1.00 71.31  ? 274 HOH   A O   1 
HETATM 2303 O O   . HOH   N 5 .  ? 13.723  -12.938 10.400  1.00 51.82  ? 275 HOH   A O   1 
HETATM 2304 O O   . HOH   N 5 .  ? 10.722  -7.858  0.204   1.00 27.03  ? 276 HOH   A O   1 
HETATM 2305 O O   . HOH   N 5 .  ? 0.534   -29.036 -6.646  1.00 63.65  ? 277 HOH   A O   1 
HETATM 2306 O O   . HOH   N 5 .  ? 16.698  -18.399 -9.687  1.00 54.18  ? 278 HOH   A O   1 
HETATM 2307 O O   . HOH   N 5 .  ? -7.110  -14.257 -9.173  1.00 57.91  ? 279 HOH   A O   1 
HETATM 2308 O O   . HOH   N 5 .  ? -7.558  -11.426 -7.867  1.00 40.63  ? 280 HOH   A O   1 
HETATM 2309 O O   . HOH   N 5 .  ? 9.892   -12.998 9.925   1.00 51.38  ? 281 HOH   A O   1 
HETATM 2310 O O   . HOH   N 5 .  ? 16.805  -12.587 -16.877 1.00 46.66  ? 282 HOH   A O   1 
HETATM 2311 O O   . HOH   N 5 .  ? 20.944  -16.612 -3.542  1.00 30.62  ? 283 HOH   A O   1 
HETATM 2312 O O   . HOH   N 5 .  ? 10.067  -27.574 -7.113  1.00 57.28  ? 284 HOH   A O   1 
HETATM 2313 O O   . HOH   N 5 .  ? -4.718  -27.021 6.418   1.00 61.82  ? 285 HOH   A O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 0.895   -29.190 12.241  1.00 78.99  ? 286 HOH   A O   1 
HETATM 2315 O O   . HOH   N 5 .  ? -4.345  -7.497  -11.225 1.00 58.12  ? 287 HOH   A O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 8.497   -9.301  -13.638 1.00 34.28  ? 288 HOH   A O   1 
HETATM 2317 O O   . HOH   N 5 .  ? -6.368  -26.505 3.592   1.00 41.46  ? 289 HOH   A O   1 
HETATM 2318 O O   . HOH   N 5 .  ? -4.006  -10.831 9.868   1.00 52.35  ? 290 HOH   A O   1 
HETATM 2319 O O   . HOH   N 5 .  ? -8.538  -19.734 -3.327  1.00 41.51  ? 291 HOH   A O   1 
HETATM 2320 O O   . HOH   N 5 .  ? -1.635  -26.554 11.520  1.00 56.15  ? 292 HOH   A O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 10.598  -2.204  -1.526  1.00 68.32  ? 293 HOH   A O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 11.622  -20.786 10.684  1.00 40.65  ? 294 HOH   A O   1 
HETATM 2323 O O   . HOH   N 5 .  ? -11.016 -13.091 -2.271  1.00 80.42  ? 295 HOH   A O   1 
HETATM 2324 O O   . HOH   N 5 .  ? -0.478  -3.323  -11.137 1.00 53.66  ? 296 HOH   A O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 6.231   -30.675 -2.647  1.00 70.91  ? 297 HOH   A O   1 
HETATM 2326 O O   . HOH   N 5 .  ? -11.791 -16.966 -3.637  1.00 58.67  ? 298 HOH   A O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 4.694   -7.025  -10.862 1.00 55.87  ? 299 HOH   A O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 1.476   -7.095  -12.920 1.00 56.50  ? 300 HOH   A O   1 
HETATM 2329 O O   . HOH   N 5 .  ? -6.587  -23.006 -7.028  1.00 54.18  ? 301 HOH   A O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 11.576  -29.696 -3.389  1.00 65.01  ? 302 HOH   A O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 13.079  -32.027 2.145   1.00 59.53  ? 303 HOH   A O   1 
HETATM 2332 O O   . HOH   N 5 .  ? -6.499  -22.526 6.055   1.00 52.62  ? 304 HOH   A O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 15.188  -28.477 -1.734  1.00 62.71  ? 305 HOH   A O   1 
HETATM 2334 O O   . HOH   N 5 .  ? -7.440  -19.116 8.369   1.00 61.08  ? 306 HOH   A O   1 
HETATM 2335 O O   . HOH   N 5 .  ? -11.043 -28.535 -1.149  1.00 70.68  ? 307 HOH   A O   1 
HETATM 2336 O O   . HOH   N 5 .  ? -5.800  -20.335 -7.867  1.00 62.54  ? 308 HOH   A O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 4.291   -9.608  -11.603 1.00 52.43  ? 309 HOH   A O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 14.732  -29.503 -7.168  1.00 53.31  ? 310 HOH   A O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 12.527  -18.703 -15.127 1.00 48.89  ? 311 HOH   A O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 8.227   -22.393 -18.917 1.00 82.21  ? 312 HOH   A O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 4.629   3.283   3.029   1.00 84.79  ? 313 HOH   A O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 4.157   -3.170  2.147   1.00 63.70  ? 314 HOH   A O   1 
HETATM 2343 O O   . HOH   O 5 .  ? 27.309  -7.972  -28.911 1.00 54.55  ? 201 HOH   B O   1 
HETATM 2344 O O   . HOH   O 5 .  ? 19.720  -22.259 -23.406 1.00 62.69  ? 202 HOH   B O   1 
HETATM 2345 O O   . HOH   O 5 .  ? 25.840  -5.257  -33.438 1.00 55.64  ? 203 HOH   B O   1 
HETATM 2346 O O   . HOH   O 5 .  ? 35.189  -15.819 -26.245 1.00 56.34  ? 204 HOH   B O   1 
HETATM 2347 O O   . HOH   O 5 .  ? 31.457  -8.796  -29.619 1.00 58.35  ? 205 HOH   B O   1 
HETATM 2348 O O   . HOH   O 5 .  ? 30.144  -12.793 -45.058 1.00 56.45  ? 206 HOH   B O   1 
HETATM 2349 O O   . HOH   O 5 .  ? 27.500  -17.640 -24.875 1.00 63.64  ? 207 HOH   B O   1 
HETATM 2350 O O   . HOH   O 5 .  ? 34.881  -23.154 -29.882 1.00 51.54  ? 208 HOH   B O   1 
HETATM 2351 O O   . HOH   O 5 .  ? 6.452   -12.193 -25.852 1.00 45.82  ? 209 HOH   B O   1 
HETATM 2352 O O   . HOH   O 5 .  ? 9.936   -19.482 -42.842 1.00 123.35 ? 210 HOH   B O   1 
HETATM 2353 O O   . HOH   O 5 .  ? 25.896  -22.984 -30.915 1.00 35.86  ? 211 HOH   B O   1 
HETATM 2354 O O   . HOH   O 5 .  ? 8.367   -8.853  -16.480 1.00 44.30  ? 212 HOH   B O   1 
HETATM 2355 O O   . HOH   O 5 .  ? 11.384  1.219   -38.864 1.00 47.19  ? 213 HOH   B O   1 
HETATM 2356 O O   . HOH   O 5 .  ? 31.001  -12.181 -38.490 1.00 62.61  ? 214 HOH   B O   1 
HETATM 2357 O O   . HOH   O 5 .  ? 10.000  -11.821 -38.469 1.00 85.29  ? 215 HOH   B O   1 
HETATM 2358 O O   . HOH   O 5 .  ? 24.262  -1.848  -35.797 1.00 82.28  ? 216 HOH   B O   1 
HETATM 2359 O O   . HOH   O 5 .  ? 23.666  -4.399  -36.761 1.00 35.01  ? 217 HOH   B O   1 
HETATM 2360 O O   . HOH   O 5 .  ? 10.421  -18.887 -32.976 1.00 35.26  ? 218 HOH   B O   1 
HETATM 2361 O O   . HOH   O 5 .  ? 25.775  -0.371  -28.923 1.00 41.03  ? 219 HOH   B O   1 
HETATM 2362 O O   . HOH   O 5 .  ? 18.122  -0.726  -38.141 1.00 36.08  ? 220 HOH   B O   1 
HETATM 2363 O O   . HOH   O 5 .  ? 14.275  -24.517 -40.130 1.00 54.58  ? 221 HOH   B O   1 
HETATM 2364 O O   . HOH   O 5 .  ? 9.885   -17.187 -44.142 1.00 83.73  ? 222 HOH   B O   1 
HETATM 2365 O O   . HOH   O 5 .  ? 19.867  -25.780 -34.083 1.00 53.97  ? 223 HOH   B O   1 
HETATM 2366 O O   . HOH   O 5 .  ? 17.780  -26.077 -28.783 1.00 54.11  ? 224 HOH   B O   1 
HETATM 2367 O O   . HOH   O 5 .  ? 16.603  -19.267 -28.684 1.00 23.94  ? 225 HOH   B O   1 
HETATM 2368 O O   . HOH   O 5 .  ? 12.890  -22.499 -20.557 1.00 55.29  ? 226 HOH   B O   1 
HETATM 2369 O O   . HOH   O 5 .  ? 13.669  -4.842  -41.284 1.00 69.34  ? 227 HOH   B O   1 
HETATM 2370 O O   . HOH   O 5 .  ? 7.250   -18.941 -34.679 1.00 50.73  ? 228 HOH   B O   1 
HETATM 2371 O O   . HOH   O 5 .  ? 32.601  -18.485 -41.575 1.00 64.02  ? 229 HOH   B O   1 
HETATM 2372 O O   . HOH   O 5 .  ? 31.920  -21.601 -37.775 1.00 51.34  ? 230 HOH   B O   1 
HETATM 2373 O O   . HOH   O 5 .  ? 16.100  -26.178 -34.548 1.00 54.35  ? 231 HOH   B O   1 
HETATM 2374 O O   . HOH   O 5 .  ? 17.423  -19.742 -41.803 1.00 76.91  ? 232 HOH   B O   1 
HETATM 2375 O O   . HOH   O 5 .  ? 24.634  -4.953  -29.394 1.00 45.68  ? 233 HOH   B O   1 
HETATM 2376 O O   . HOH   O 5 .  ? 25.525  -5.946  -35.628 1.00 51.44  ? 234 HOH   B O   1 
HETATM 2377 O O   . HOH   O 5 .  ? 1.822   -12.804 -28.149 1.00 45.51  ? 235 HOH   B O   1 
HETATM 2378 O O   . HOH   O 5 .  ? 21.537  -4.061  -24.009 1.00 75.14  ? 236 HOH   B O   1 
HETATM 2379 O O   . HOH   O 5 .  ? 14.708  -6.552  -41.017 1.00 47.05  ? 237 HOH   B O   1 
HETATM 2380 O O   . HOH   O 5 .  ? 23.545  -2.465  -28.709 1.00 45.46  ? 238 HOH   B O   1 
HETATM 2381 O O   . HOH   O 5 .  ? 17.819  4.585   -34.462 1.00 55.34  ? 239 HOH   B O   1 
HETATM 2382 O O   . HOH   O 5 .  ? 21.504  -13.544 -42.297 1.00 44.62  ? 240 HOH   B O   1 
HETATM 2383 O O   . HOH   O 5 .  ? 17.761  -15.620 -45.421 1.00 46.48  ? 241 HOH   B O   1 
HETATM 2384 O O   . HOH   O 5 .  ? 17.361  -9.463  -43.651 1.00 50.98  ? 242 HOH   B O   1 
HETATM 2385 O O   . HOH   O 5 .  ? 7.474   -18.649 -31.661 1.00 63.12  ? 243 HOH   B O   1 
HETATM 2386 O O   . HOH   O 5 .  ? 22.454  -23.343 -28.507 1.00 72.53  ? 244 HOH   B O   1 
HETATM 2387 O O   . HOH   O 5 .  ? 20.601  -10.156 -42.653 1.00 34.89  ? 245 HOH   B O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 4.515   -19.288 -25.906 1.00 59.90  ? 246 HOH   B O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 21.732  3.699   -32.614 1.00 43.08  ? 247 HOH   B O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 20.409  -25.193 -29.116 1.00 59.76  ? 248 HOH   B O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 24.978  -27.421 -28.234 1.00 51.38  ? 249 HOH   B O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 21.345  -6.484  -42.419 1.00 43.36  ? 250 HOH   B O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 10.162  -21.839 -32.716 1.00 40.02  ? 251 HOH   B O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 23.402  -11.355 -21.529 1.00 64.60  ? 252 HOH   B O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 27.874  -24.782 -34.811 1.00 48.88  ? 253 HOH   B O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 7.346   -8.286  -20.575 1.00 55.90  ? 254 HOH   B O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 6.240   -20.557 -25.131 1.00 41.53  ? 255 HOH   B O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 27.218  -10.382 -28.673 1.00 61.47  ? 256 HOH   B O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 6.337   -7.558  -33.248 1.00 97.72  ? 257 HOH   B O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 7.472   -12.819 -39.390 1.00 54.23  ? 258 HOH   B O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 2.740   -7.654  -28.155 1.00 73.27  ? 259 HOH   B O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 39.313  -13.139 -38.918 1.00 79.86  ? 260 HOH   B O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 17.924  -3.716  -21.634 1.00 49.80  ? 261 HOH   B O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 24.887  -7.017  -42.441 1.00 66.94  ? 262 HOH   B O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 16.928  -26.022 -21.310 1.00 79.95  ? 263 HOH   B O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 15.062  -8.336  -43.004 1.00 68.74  ? 264 HOH   B O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 12.721  -20.313 -19.803 1.00 52.73  ? 265 HOH   B O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 28.770  -17.371 -46.760 1.00 61.56  ? 266 HOH   B O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 17.022  -0.335  -25.286 1.00 52.59  ? 267 HOH   B O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 9.645   -6.688  -40.683 1.00 53.83  ? 268 HOH   B O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 6.710   -23.487 -24.223 1.00 56.68  ? 269 HOH   B O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 19.655  3.983   -33.185 1.00 38.96  ? 270 HOH   B O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 15.174  -21.799 -41.676 1.00 68.72  ? 271 HOH   B O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 7.093   -9.929  -18.569 1.00 42.64  ? 272 HOH   B O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 20.210  -20.974 -20.521 1.00 55.22  ? 273 HOH   B O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 6.840   -21.318 -30.227 1.00 54.80  ? 274 HOH   B O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 21.891  -29.250 -35.777 1.00 58.65  ? 275 HOH   B O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 39.645  -4.140  -33.854 1.00 60.36  ? 276 HOH   B O   1 
HETATM 2419 O O   . HOH   P 5 .  ? 8.653   -36.571 18.999  1.00 50.66  ? 201 HOH   C O   1 
HETATM 2420 O O   . HOH   P 5 .  ? 9.217   -30.062 11.335  1.00 62.89  ? 202 HOH   C O   1 
HETATM 2421 O O   . HOH   P 5 .  ? 14.202  -20.716 11.949  1.00 43.54  ? 203 HOH   C O   1 
HETATM 2422 O O   . HOH   P 5 .  ? 19.417  -19.450 29.907  1.00 67.80  ? 204 HOH   C O   1 
HETATM 2423 O O   . HOH   P 5 .  ? 30.138  -28.972 12.233  1.00 57.08  ? 205 HOH   C O   1 
HETATM 2424 O O   . HOH   P 5 .  ? 25.499  -17.764 13.963  1.00 47.30  ? 206 HOH   C O   1 
HETATM 2425 O O   . HOH   P 5 .  ? 5.587   -26.300 16.922  1.00 60.19  ? 207 HOH   C O   1 
HETATM 2426 O O   . HOH   P 5 .  ? 14.760  -34.146 36.389  1.00 60.77  ? 208 HOH   C O   1 
HETATM 2427 O O   . HOH   P 5 .  ? 26.249  -37.407 9.865   1.00 45.47  ? 209 HOH   C O   1 
HETATM 2428 O O   . HOH   P 5 .  ? 6.884   -31.620 12.215  1.00 49.24  ? 210 HOH   C O   1 
HETATM 2429 O O   . HOH   P 5 .  ? 24.871  -31.368 10.813  1.00 39.72  ? 211 HOH   C O   1 
HETATM 2430 O O   . HOH   P 5 .  ? 26.001  -39.115 12.490  1.00 49.51  ? 212 HOH   C O   1 
HETATM 2431 O O   . HOH   P 5 .  ? 27.824  -36.941 16.101  1.00 43.44  ? 213 HOH   C O   1 
HETATM 2432 O O   . HOH   P 5 .  ? 25.326  -19.793 6.196   1.00 44.14  ? 214 HOH   C O   1 
HETATM 2433 O O   . HOH   P 5 .  ? 18.720  -20.292 10.484  1.00 52.14  ? 215 HOH   C O   1 
HETATM 2434 O O   . HOH   P 5 .  ? 17.166  -16.838 14.422  1.00 68.52  ? 216 HOH   C O   1 
HETATM 2435 O O   . HOH   P 5 .  ? 19.524  -41.818 12.220  1.00 36.79  ? 217 HOH   C O   1 
HETATM 2436 O O   . HOH   P 5 .  ? 12.314  -31.243 8.342   1.00 32.33  ? 218 HOH   C O   1 
HETATM 2437 O O   . HOH   P 5 .  ? 21.619  -34.232 16.570  1.00 31.33  ? 219 HOH   C O   1 
HETATM 2438 O O   . HOH   P 5 .  ? 21.779  -28.402 11.105  1.00 34.45  ? 220 HOH   C O   1 
HETATM 2439 O O   . HOH   P 5 .  ? 29.318  -39.370 31.494  1.00 50.28  ? 221 HOH   C O   1 
HETATM 2440 O O   . HOH   P 5 .  ? 27.525  -15.184 12.662  1.00 53.15  ? 222 HOH   C O   1 
HETATM 2441 O O   . HOH   P 5 .  ? 22.766  -41.105 18.638  1.00 50.04  ? 223 HOH   C O   1 
HETATM 2442 O O   . HOH   P 5 .  ? 30.951  -39.657 27.235  1.00 43.71  ? 224 HOH   C O   1 
HETATM 2443 O O   . HOH   P 5 .  ? 20.324  -28.797 8.459   1.00 38.09  ? 225 HOH   C O   1 
HETATM 2444 O O   . HOH   P 5 .  ? 22.406  -21.921 7.232   1.00 46.03  ? 226 HOH   C O   1 
HETATM 2445 O O   . HOH   P 5 .  ? 31.617  -33.578 25.768  1.00 66.54  ? 227 HOH   C O   1 
HETATM 2446 O O   . HOH   P 5 .  ? 20.447  -39.611 26.869  1.00 52.50  ? 228 HOH   C O   1 
HETATM 2447 O O   . HOH   P 5 .  ? 23.075  -18.016 21.456  1.00 52.80  ? 229 HOH   C O   1 
HETATM 2448 O O   . HOH   P 5 .  ? 29.833  -31.825 15.627  1.00 50.86  ? 230 HOH   C O   1 
HETATM 2449 O O   . HOH   P 5 .  ? 30.348  -35.856 29.080  1.00 73.83  ? 231 HOH   C O   1 
HETATM 2450 O O   . HOH   P 5 .  ? 25.427  -19.490 29.469  1.00 60.58  ? 232 HOH   C O   1 
HETATM 2451 O O   . HOH   P 5 .  ? 11.560  -29.545 27.771  1.00 60.03  ? 233 HOH   C O   1 
HETATM 2452 O O   . HOH   P 5 .  ? 20.148  -40.534 38.535  1.00 88.95  ? 234 HOH   C O   1 
HETATM 2453 O O   . HOH   P 5 .  ? 25.504  -17.706 20.795  1.00 56.02  ? 235 HOH   C O   1 
HETATM 2454 O O   . HOH   P 5 .  ? 32.060  -26.136 28.060  1.00 53.51  ? 236 HOH   C O   1 
HETATM 2455 O O   . HOH   P 5 .  ? 8.899   -18.787 23.754  1.00 55.29  ? 237 HOH   C O   1 
HETATM 2456 O O   . HOH   P 5 .  ? 27.433  -37.547 24.624  1.00 50.96  ? 238 HOH   C O   1 
HETATM 2457 O O   . HOH   P 5 .  ? 18.827  -26.888 3.178   1.00 52.50  ? 239 HOH   C O   1 
HETATM 2458 O O   . HOH   P 5 .  ? 30.903  -43.401 15.657  1.00 56.81  ? 240 HOH   C O   1 
HETATM 2459 O O   . HOH   P 5 .  ? 15.892  -17.487 19.235  1.00 57.41  ? 241 HOH   C O   1 
HETATM 2460 O O   . HOH   P 5 .  ? 29.611  -32.207 18.289  1.00 64.56  ? 242 HOH   C O   1 
HETATM 2461 O O   . HOH   P 5 .  ? 6.654   -17.691 11.013  1.00 40.73  ? 243 HOH   C O   1 
HETATM 2462 O O   . HOH   P 5 .  ? 20.800  -29.343 4.966   1.00 59.67  ? 244 HOH   C O   1 
HETATM 2463 O O   . HOH   P 5 .  ? 24.967  -39.739 20.223  1.00 36.80  ? 245 HOH   C O   1 
HETATM 2464 O O   . HOH   P 5 .  ? 5.456   -24.561 19.441  1.00 88.23  ? 246 HOH   C O   1 
HETATM 2465 O O   . HOH   P 5 .  ? 31.575  -43.170 11.873  1.00 62.43  ? 247 HOH   C O   1 
HETATM 2466 O O   . HOH   P 5 .  ? 25.957  -33.791 34.945  1.00 60.95  ? 248 HOH   C O   1 
HETATM 2467 O O   . HOH   P 5 .  ? 13.919  -38.737 9.704   1.00 51.83  ? 249 HOH   C O   1 
HETATM 2468 O O   . HOH   P 5 .  ? 19.527  -18.684 24.835  1.00 49.20  ? 250 HOH   C O   1 
HETATM 2469 O O   . HOH   P 5 .  ? 13.751  -37.191 14.447  1.00 63.53  ? 251 HOH   C O   1 
HETATM 2470 O O   . HOH   P 5 .  ? 29.268  -34.843 36.999  1.00 72.49  ? 252 HOH   C O   1 
HETATM 2471 O O   . HOH   P 5 .  ? 30.642  -17.099 10.036  1.00 62.67  ? 253 HOH   C O   1 
HETATM 2472 O O   . HOH   P 5 .  ? 30.403  -25.061 31.872  1.00 64.68  ? 254 HOH   C O   1 
HETATM 2473 O O   . HOH   P 5 .  ? 13.929  -39.377 16.700  1.00 55.18  ? 255 HOH   C O   1 
HETATM 2474 O O   . HOH   P 5 .  ? 16.082  -19.057 29.260  1.00 53.03  ? 256 HOH   C O   1 
HETATM 2475 O O   . HOH   P 5 .  ? 16.080  -38.477 29.191  1.00 56.49  ? 257 HOH   C O   1 
HETATM 2476 O O   . HOH   P 5 .  ? 20.098  -12.963 13.302  1.00 45.83  ? 258 HOH   C O   1 
HETATM 2477 O O   . HOH   P 5 .  ? 28.824  -41.493 27.080  1.00 43.87  ? 259 HOH   C O   1 
HETATM 2478 O O   . HOH   P 5 .  ? 31.604  -39.262 30.096  1.00 69.74  ? 260 HOH   C O   1 
HETATM 2479 O O   . HOH   P 5 .  ? 28.645  -21.006 7.573   1.00 58.74  ? 261 HOH   C O   1 
HETATM 2480 O O   . HOH   P 5 .  ? 37.616  -25.292 25.609  1.00 61.96  ? 262 HOH   C O   1 
# 
