data_7HHP
# 
_entry.id   7HHP 
# 
_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   7HHP         pdb_00007hhp 10.2210/pdb7hhp/pdb 
WWPDB D_1001407487 ?            ?                   
# 
_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                        7HHP 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn N,N-diethyl-2-methylbenzamide                      191.269   1   ? ?    ? ? 
5 water       nat water                                              18.015    254 ? ?    ? ? 
# 
_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,N-diethyl-2-methylbenzamide A1A3Z 
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 
A1A3Z non-polymer         . N,N-diethyl-2-methylbenzamide ?                 'C12 H17 N O'    191.269 
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 ?  ?   ?   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        A1A3Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3Z 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 2 SO4   1   104 4   SO4   SO4 A . 
H 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1A3Z 1   103 101 A1A3Z LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 338 HOH   HOH A . 
M 5 HOH   2   202 354 HOH   HOH A . 
M 5 HOH   3   203 66  HOH   HOH A . 
M 5 HOH   4   204 307 HOH   HOH A . 
M 5 HOH   5   205 341 HOH   HOH A . 
M 5 HOH   6   206 84  HOH   HOH A . 
M 5 HOH   7   207 35  HOH   HOH A . 
M 5 HOH   8   208 339 HOH   HOH A . 
M 5 HOH   9   209 26  HOH   HOH A . 
M 5 HOH   10  210 208 HOH   HOH A . 
M 5 HOH   11  211 340 HOH   HOH A . 
M 5 HOH   12  212 347 HOH   HOH A . 
M 5 HOH   13  213 139 HOH   HOH A . 
M 5 HOH   14  214 87  HOH   HOH A . 
M 5 HOH   15  215 97  HOH   HOH A . 
M 5 HOH   16  216 91  HOH   HOH A . 
M 5 HOH   17  217 111 HOH   HOH A . 
M 5 HOH   18  218 290 HOH   HOH A . 
M 5 HOH   19  219 167 HOH   HOH A . 
M 5 HOH   20  220 38  HOH   HOH A . 
M 5 HOH   21  221 179 HOH   HOH A . 
M 5 HOH   22  222 41  HOH   HOH A . 
M 5 HOH   23  223 202 HOH   HOH A . 
M 5 HOH   24  224 289 HOH   HOH A . 
M 5 HOH   25  225 27  HOH   HOH A . 
M 5 HOH   26  226 333 HOH   HOH A . 
M 5 HOH   27  227 288 HOH   HOH A . 
M 5 HOH   28  228 32  HOH   HOH A . 
M 5 HOH   29  229 165 HOH   HOH A . 
M 5 HOH   30  230 278 HOH   HOH A . 
M 5 HOH   31  231 55  HOH   HOH A . 
M 5 HOH   32  232 292 HOH   HOH A . 
M 5 HOH   33  233 23  HOH   HOH A . 
M 5 HOH   34  234 86  HOH   HOH A . 
M 5 HOH   35  235 152 HOH   HOH A . 
M 5 HOH   36  236 188 HOH   HOH A . 
M 5 HOH   37  237 304 HOH   HOH A . 
M 5 HOH   38  238 109 HOH   HOH A . 
M 5 HOH   39  239 2   HOH   HOH A . 
M 5 HOH   40  240 71  HOH   HOH A . 
M 5 HOH   41  241 336 HOH   HOH A . 
M 5 HOH   42  242 190 HOH   HOH A . 
M 5 HOH   43  243 37  HOH   HOH A . 
M 5 HOH   44  244 8   HOH   HOH A . 
M 5 HOH   45  245 28  HOH   HOH A . 
M 5 HOH   46  246 99  HOH   HOH A . 
M 5 HOH   47  247 94  HOH   HOH A . 
M 5 HOH   48  248 301 HOH   HOH A . 
M 5 HOH   49  249 18  HOH   HOH A . 
M 5 HOH   50  250 7   HOH   HOH A . 
M 5 HOH   51  251 267 HOH   HOH A . 
M 5 HOH   52  252 293 HOH   HOH A . 
M 5 HOH   53  253 60  HOH   HOH A . 
M 5 HOH   54  254 1   HOH   HOH A . 
M 5 HOH   55  255 47  HOH   HOH A . 
M 5 HOH   56  256 34  HOH   HOH A . 
M 5 HOH   57  257 274 HOH   HOH A . 
M 5 HOH   58  258 12  HOH   HOH A . 
M 5 HOH   59  259 42  HOH   HOH A . 
M 5 HOH   60  260 203 HOH   HOH A . 
M 5 HOH   61  261 116 HOH   HOH A . 
M 5 HOH   62  262 78  HOH   HOH A . 
M 5 HOH   63  263 93  HOH   HOH A . 
M 5 HOH   64  264 300 HOH   HOH A . 
M 5 HOH   65  265 260 HOH   HOH A . 
M 5 HOH   66  266 145 HOH   HOH A . 
M 5 HOH   67  267 143 HOH   HOH A . 
M 5 HOH   68  268 222 HOH   HOH A . 
M 5 HOH   69  269 20  HOH   HOH A . 
M 5 HOH   70  270 95  HOH   HOH A . 
M 5 HOH   71  271 299 HOH   HOH A . 
M 5 HOH   72  272 327 HOH   HOH A . 
M 5 HOH   73  273 199 HOH   HOH A . 
M 5 HOH   74  274 21  HOH   HOH A . 
M 5 HOH   75  275 259 HOH   HOH A . 
M 5 HOH   76  276 164 HOH   HOH A . 
M 5 HOH   77  277 58  HOH   HOH A . 
M 5 HOH   78  278 14  HOH   HOH A . 
M 5 HOH   79  279 281 HOH   HOH A . 
M 5 HOH   80  280 9   HOH   HOH A . 
M 5 HOH   81  281 211 HOH   HOH A . 
M 5 HOH   82  282 19  HOH   HOH A . 
M 5 HOH   83  283 115 HOH   HOH A . 
M 5 HOH   84  284 31  HOH   HOH A . 
M 5 HOH   85  285 218 HOH   HOH A . 
M 5 HOH   86  286 16  HOH   HOH A . 
M 5 HOH   87  287 296 HOH   HOH A . 
M 5 HOH   88  288 64  HOH   HOH A . 
M 5 HOH   89  289 131 HOH   HOH A . 
M 5 HOH   90  290 77  HOH   HOH A . 
M 5 HOH   91  291 73  HOH   HOH A . 
M 5 HOH   92  292 318 HOH   HOH A . 
M 5 HOH   93  293 22  HOH   HOH A . 
M 5 HOH   94  294 83  HOH   HOH A . 
M 5 HOH   95  295 353 HOH   HOH A . 
M 5 HOH   96  296 113 HOH   HOH A . 
M 5 HOH   97  297 270 HOH   HOH A . 
M 5 HOH   98  298 210 HOH   HOH A . 
M 5 HOH   99  299 63  HOH   HOH A . 
M 5 HOH   100 300 344 HOH   HOH A . 
M 5 HOH   101 301 343 HOH   HOH A . 
M 5 HOH   102 302 205 HOH   HOH A . 
M 5 HOH   103 303 75  HOH   HOH A . 
M 5 HOH   104 304 219 HOH   HOH A . 
M 5 HOH   105 305 352 HOH   HOH A . 
M 5 HOH   106 306 156 HOH   HOH A . 
M 5 HOH   107 307 185 HOH   HOH A . 
M 5 HOH   108 308 57  HOH   HOH A . 
M 5 HOH   109 309 313 HOH   HOH A . 
M 5 HOH   110 310 283 HOH   HOH A . 
M 5 HOH   111 311 332 HOH   HOH A . 
N 5 HOH   1   201 247 HOH   HOH B . 
N 5 HOH   2   202 258 HOH   HOH B . 
N 5 HOH   3   203 331 HOH   HOH B . 
N 5 HOH   4   204 89  HOH   HOH B . 
N 5 HOH   5   205 117 HOH   HOH B . 
N 5 HOH   6   206 215 HOH   HOH B . 
N 5 HOH   7   207 123 HOH   HOH B . 
N 5 HOH   8   208 329 HOH   HOH B . 
N 5 HOH   9   209 272 HOH   HOH B . 
N 5 HOH   10  210 157 HOH   HOH B . 
N 5 HOH   11  211 98  HOH   HOH B . 
N 5 HOH   12  212 69  HOH   HOH B . 
N 5 HOH   13  213 119 HOH   HOH B . 
N 5 HOH   14  214 249 HOH   HOH B . 
N 5 HOH   15  215 59  HOH   HOH B . 
N 5 HOH   16  216 172 HOH   HOH B . 
N 5 HOH   17  217 242 HOH   HOH B . 
N 5 HOH   18  218 54  HOH   HOH B . 
N 5 HOH   19  219 337 HOH   HOH B . 
N 5 HOH   20  220 150 HOH   HOH B . 
N 5 HOH   21  221 17  HOH   HOH B . 
N 5 HOH   22  222 168 HOH   HOH B . 
N 5 HOH   23  223 349 HOH   HOH B . 
N 5 HOH   24  224 6   HOH   HOH B . 
N 5 HOH   25  225 153 HOH   HOH B . 
N 5 HOH   26  226 5   HOH   HOH B . 
N 5 HOH   27  227 320 HOH   HOH B . 
N 5 HOH   28  228 261 HOH   HOH B . 
N 5 HOH   29  229 10  HOH   HOH B . 
N 5 HOH   30  230 101 HOH   HOH B . 
N 5 HOH   31  231 68  HOH   HOH B . 
N 5 HOH   32  232 25  HOH   HOH B . 
N 5 HOH   33  233 96  HOH   HOH B . 
N 5 HOH   34  234 137 HOH   HOH B . 
N 5 HOH   35  235 224 HOH   HOH B . 
N 5 HOH   36  236 24  HOH   HOH B . 
N 5 HOH   37  237 315 HOH   HOH B . 
N 5 HOH   38  238 280 HOH   HOH B . 
N 5 HOH   39  239 303 HOH   HOH B . 
N 5 HOH   40  240 61  HOH   HOH B . 
N 5 HOH   41  241 36  HOH   HOH B . 
N 5 HOH   42  242 169 HOH   HOH B . 
N 5 HOH   43  243 170 HOH   HOH B . 
N 5 HOH   44  244 13  HOH   HOH B . 
N 5 HOH   45  245 197 HOH   HOH B . 
N 5 HOH   46  246 72  HOH   HOH B . 
N 5 HOH   47  247 342 HOH   HOH B . 
N 5 HOH   48  248 76  HOH   HOH B . 
N 5 HOH   49  249 175 HOH   HOH B . 
N 5 HOH   50  250 214 HOH   HOH B . 
N 5 HOH   51  251 217 HOH   HOH B . 
N 5 HOH   52  252 104 HOH   HOH B . 
N 5 HOH   53  253 120 HOH   HOH B . 
N 5 HOH   54  254 279 HOH   HOH B . 
N 5 HOH   55  255 223 HOH   HOH B . 
N 5 HOH   56  256 79  HOH   HOH B . 
N 5 HOH   57  257 44  HOH   HOH B . 
N 5 HOH   58  258 160 HOH   HOH B . 
N 5 HOH   59  259 74  HOH   HOH B . 
N 5 HOH   60  260 182 HOH   HOH B . 
N 5 HOH   61  261 163 HOH   HOH B . 
N 5 HOH   62  262 316 HOH   HOH B . 
N 5 HOH   63  263 46  HOH   HOH B . 
N 5 HOH   64  264 319 HOH   HOH B . 
N 5 HOH   65  265 350 HOH   HOH B . 
N 5 HOH   66  266 291 HOH   HOH B . 
N 5 HOH   67  267 322 HOH   HOH B . 
N 5 HOH   68  268 177 HOH   HOH B . 
N 5 HOH   69  269 314 HOH   HOH B . 
N 5 HOH   70  270 107 HOH   HOH B . 
N 5 HOH   71  271 201 HOH   HOH B . 
N 5 HOH   72  272 312 HOH   HOH B . 
O 5 HOH   1   201 161 HOH   HOH C . 
O 5 HOH   2   202 323 HOH   HOH C . 
O 5 HOH   3   203 334 HOH   HOH C . 
O 5 HOH   4   204 226 HOH   HOH C . 
O 5 HOH   5   205 321 HOH   HOH C . 
O 5 HOH   6   206 335 HOH   HOH C . 
O 5 HOH   7   207 317 HOH   HOH C . 
O 5 HOH   8   208 134 HOH   HOH C . 
O 5 HOH   9   209 254 HOH   HOH C . 
O 5 HOH   10  210 118 HOH   HOH C . 
O 5 HOH   11  211 15  HOH   HOH C . 
O 5 HOH   12  212 309 HOH   HOH C . 
O 5 HOH   13  213 325 HOH   HOH C . 
O 5 HOH   14  214 90  HOH   HOH C . 
O 5 HOH   15  215 126 HOH   HOH C . 
O 5 HOH   16  216 142 HOH   HOH C . 
O 5 HOH   17  217 45  HOH   HOH C . 
O 5 HOH   18  218 49  HOH   HOH C . 
O 5 HOH   19  219 326 HOH   HOH C . 
O 5 HOH   20  220 85  HOH   HOH C . 
O 5 HOH   21  221 284 HOH   HOH C . 
O 5 HOH   22  222 149 HOH   HOH C . 
O 5 HOH   23  223 189 HOH   HOH C . 
O 5 HOH   24  224 269 HOH   HOH C . 
O 5 HOH   25  225 130 HOH   HOH C . 
O 5 HOH   26  226 271 HOH   HOH C . 
O 5 HOH   27  227 82  HOH   HOH C . 
O 5 HOH   28  228 173 HOH   HOH C . 
O 5 HOH   29  229 135 HOH   HOH C . 
O 5 HOH   30  230 102 HOH   HOH C . 
O 5 HOH   31  231 209 HOH   HOH C . 
O 5 HOH   32  232 40  HOH   HOH C . 
O 5 HOH   33  233 4   HOH   HOH C . 
O 5 HOH   34  234 56  HOH   HOH C . 
O 5 HOH   35  235 346 HOH   HOH C . 
O 5 HOH   36  236 48  HOH   HOH C . 
O 5 HOH   37  237 53  HOH   HOH C . 
O 5 HOH   38  238 184 HOH   HOH C . 
O 5 HOH   39  239 295 HOH   HOH C . 
O 5 HOH   40  240 122 HOH   HOH C . 
O 5 HOH   41  241 132 HOH   HOH C . 
O 5 HOH   42  242 275 HOH   HOH C . 
O 5 HOH   43  243 294 HOH   HOH C . 
O 5 HOH   44  244 171 HOH   HOH C . 
O 5 HOH   45  245 302 HOH   HOH C . 
O 5 HOH   46  246 62  HOH   HOH C . 
O 5 HOH   47  247 43  HOH   HOH C . 
O 5 HOH   48  248 67  HOH   HOH C . 
O 5 HOH   49  249 198 HOH   HOH C . 
O 5 HOH   50  250 287 HOH   HOH C . 
O 5 HOH   51  251 305 HOH   HOH C . 
O 5 HOH   52  252 348 HOH   HOH C . 
O 5 HOH   53  253 328 HOH   HOH C . 
O 5 HOH   54  254 148 HOH   HOH C . 
O 5 HOH   55  255 65  HOH   HOH C . 
O 5 HOH   56  256 246 HOH   HOH C . 
O 5 HOH   57  257 151 HOH   HOH C . 
O 5 HOH   58  258 298 HOH   HOH C . 
O 5 HOH   59  259 146 HOH   HOH C . 
O 5 HOH   60  260 241 HOH   HOH C . 
O 5 HOH   61  261 345 HOH   HOH C . 
O 5 HOH   62  262 70  HOH   HOH C . 
O 5 HOH   63  263 108 HOH   HOH C . 
O 5 HOH   64  264 103 HOH   HOH C . 
O 5 HOH   65  265 330 HOH   HOH C . 
O 5 HOH   66  266 324 HOH   HOH C . 
O 5 HOH   67  267 351 HOH   HOH C . 
O 5 HOH   68  268 206 HOH   HOH C . 
O 5 HOH   69  269 92  HOH   HOH C . 
O 5 HOH   70  270 125 HOH   HOH C . 
O 5 HOH   71  271 310 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 LYS 73 ? CG  ? B LYS 74 CG  
20 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
21 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
22 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
23 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
24 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
25 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
26 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
27 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
28 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
29 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
30 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
31 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
32 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
33 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
34 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
35 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
36 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
37 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
38 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
39 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
40 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
41 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
42 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
43 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
44 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
45 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
46 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
47 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
48 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
49 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
50 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
51 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
52 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' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHP 
_cell.length_a           41.420 
_cell.length_b           42.010 
_cell.length_c           159.030 
_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                         7HHP 
_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          7HHP 
_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                     7HHP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.01 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   27274 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            0.093 
_reflns.pdbx_netI_over_sigmaI        10.3 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.102 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     171489 
_reflns.pdbx_chi_squared             0.99 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.78 
_reflns_shell.d_res_low                   1.83 
_reflns_shell.number_measured_all         13466 
_reflns_shell.number_unique_obs           1978 
_reflns_shell.Rmerge_I_obs                2.083 
_reflns_shell.pdbx_chi_squared            0.80 
_reflns_shell.pdbx_redundancy             6.8 
_reflns_shell.percent_possible_obs        98.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             2.255 
_reflns_shell.pdbx_Rpim_I_all             0.854 
_reflns_shell.pdbx_CC_half                0.334 
_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                                 7HHP 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25818 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.65 
_refine.ls_d_res_high                            1.78 
_refine.ls_percent_reflns_obs                    98.83 
_refine.ls_R_factor_obs                          0.20111 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19856 
_refine.ls_R_factor_R_free                       0.24632 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1396 
_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          0.951 
_refine.B_iso_mean                               43.627 
_refine.aniso_B[1][1]                            0.75 
_refine.aniso_B[2][2]                            -1.22 
_refine.aniso_B[3][3]                            0.47 
_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                       0.142 
_refine.pdbx_overall_ESU_R_Free                  0.138 
_refine.overall_SU_ML                            0.136 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.748 
_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        2143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             254 
_refine_hist.number_atoms_total               2449 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        40.65 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.012  ? 2298 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.647  1.833  ? 3126 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.231  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.328  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.568 10.000 ? 308  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.127  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1920 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.698  4.153  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.189  7.420  ? 1338 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.663  4.435  ? 1225 '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       9.936  62.44  ? 3663 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.780 
_refine_ls_shell.d_res_low                        1.826 
_refine_ls_shell.number_reflns_R_work             1882 
_refine_ls_shell.R_factor_R_work                  0.367 
_refine_ls_shell.percent_reflns_obs               97.77 
_refine_ls_shell.R_factor_R_free                  0.361 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             90 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHP 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z31723394' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHP 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHP A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHP B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHP 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 7HHP GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHP SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHP GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHP SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHP GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHP SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O 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                   7HHP 
_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 271 ? ? O C HOH 206 ? ? 1.63 
2  1 O   A LYS 14  ? ? O A HOH 201 ? ? 1.80 
3  1 O   A HOH 226 ? ? O A HOH 293 ? ? 1.93 
4  1 O   B HOH 238 ? ? O B HOH 267 ? ? 1.99 
5  1 O   B HOH 247 ? ? O B HOH 268 ? ? 2.04 
6  1 OD1 A ASP 66  ? B O A HOH 202 ? ? 2.06 
7  1 O   B HOH 240 ? ? O B HOH 272 ? ? 2.08 
8  1 O   C THR 47  ? ? O C HOH 201 ? ? 2.12 
9  1 OD1 C ASP 9   ? ? O C HOH 202 ? ? 2.15 
10 1 O1  A SO4 104 ? ? O A HOH 203 ? ? 2.15 
11 1 CG  A ASP 57  ? ? O A HOH 201 ? ? 2.15 
12 1 O   C HOH 259 ? ? O C HOH 266 ? ? 2.15 
13 1 OD1 C ASP 26  ? ? O C HOH 203 ? ? 2.15 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 232 ? ? 1_555 O A HOH 268 ? ? 4_545 2.09 
2 1 O A HOH 207 ? ? 1_555 O A HOH 310 ? ? 4_545 2.11 
3 1 O A HOH 270 ? ? 1_555 O A HOH 286 ? ? 4_545 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -153.89 64.93  
2 1 HIS B 20 ? ? -35.07  126.16 
3 1 ASN B 38 ? ? 81.73   -8.16  
4 1 ASN B 87 ? ? -158.36 60.46  
5 1 ASN C 87 ? ? -158.32 51.21  
# 
_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            147.53 
# 
_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                       311 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.89 
_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 ALA 29 ? C ALA 30 
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A3Z C4   C N N 1   
A1A3Z C5   C Y N 2   
A1A3Z C6   C Y N 3   
A1A3Z C7   C Y N 4   
A1A3Z C8   C Y N 5   
A1A3Z C10  C Y N 6   
A1A3Z O    O N N 7   
A1A3Z N    N N N 8   
A1A3Z C2   C N N 9   
A1A3Z C3   C N N 10  
A1A3Z C1   C N N 11  
A1A3Z C    C N N 12  
A1A3Z C11  C N N 13  
A1A3Z C9   C Y N 14  
A1A3Z H10  H N N 15  
A1A3Z H11  H N N 16  
A1A3Z H12  H N N 17  
A1A3Z H5   H N N 18  
A1A3Z H6   H N N 19  
A1A3Z H7   H N N 20  
A1A3Z H9   H N N 21  
A1A3Z H8   H N N 22  
A1A3Z H3   H N N 23  
A1A3Z H4   H N N 24  
A1A3Z H    H N N 25  
A1A3Z H2   H N N 26  
A1A3Z H1   H N N 27  
A1A3Z H15  H N N 28  
A1A3Z H16  H N N 29  
A1A3Z H14  H N N 30  
A1A3Z H13  H N N 31  
ALA   N    N N N 32  
ALA   CA   C N S 33  
ALA   C    C N N 34  
ALA   O    O N N 35  
ALA   CB   C N N 36  
ALA   OXT  O N N 37  
ALA   H    H N N 38  
ALA   H2   H N N 39  
ALA   HA   H N N 40  
ALA   HB1  H N N 41  
ALA   HB2  H N N 42  
ALA   HB3  H N N 43  
ALA   HXT  H N N 44  
ARG   N    N N N 45  
ARG   CA   C N S 46  
ARG   C    C N N 47  
ARG   O    O N N 48  
ARG   CB   C N N 49  
ARG   CG   C N N 50  
ARG   CD   C N N 51  
ARG   NE   N N N 52  
ARG   CZ   C N N 53  
ARG   NH1  N N N 54  
ARG   NH2  N N N 55  
ARG   OXT  O N N 56  
ARG   H    H N N 57  
ARG   H2   H N N 58  
ARG   HA   H N N 59  
ARG   HB2  H N N 60  
ARG   HB3  H N N 61  
ARG   HG2  H N N 62  
ARG   HG3  H N N 63  
ARG   HD2  H N N 64  
ARG   HD3  H N N 65  
ARG   HE   H N N 66  
ARG   HH11 H N N 67  
ARG   HH12 H N N 68  
ARG   HH21 H N N 69  
ARG   HH22 H N N 70  
ARG   HXT  H N N 71  
ASN   N    N N N 72  
ASN   CA   C N S 73  
ASN   C    C N N 74  
ASN   O    O N N 75  
ASN   CB   C N N 76  
ASN   CG   C N N 77  
ASN   OD1  O N N 78  
ASN   ND2  N N N 79  
ASN   OXT  O N N 80  
ASN   H    H N N 81  
ASN   H2   H N N 82  
ASN   HA   H N N 83  
ASN   HB2  H N N 84  
ASN   HB3  H N N 85  
ASN   HD21 H N N 86  
ASN   HD22 H N N 87  
ASN   HXT  H N N 88  
ASP   N    N N N 89  
ASP   CA   C N S 90  
ASP   C    C N N 91  
ASP   O    O N N 92  
ASP   CB   C N N 93  
ASP   CG   C N N 94  
ASP   OD1  O N N 95  
ASP   OD2  O N N 96  
ASP   OXT  O N N 97  
ASP   H    H N N 98  
ASP   H2   H N N 99  
ASP   HA   H N N 100 
ASP   HB2  H N N 101 
ASP   HB3  H N N 102 
ASP   HD2  H N N 103 
ASP   HXT  H N N 104 
CYS   N    N N N 105 
CYS   CA   C N R 106 
CYS   C    C N N 107 
CYS   O    O N N 108 
CYS   CB   C N N 109 
CYS   SG   S N N 110 
CYS   OXT  O N N 111 
CYS   H    H N N 112 
CYS   H2   H N N 113 
CYS   HA   H N N 114 
CYS   HB2  H N N 115 
CYS   HB3  H N N 116 
CYS   HG   H N N 117 
CYS   HXT  H N N 118 
EDO   C1   C N N 119 
EDO   O1   O N N 120 
EDO   C2   C N N 121 
EDO   O2   O N N 122 
EDO   H11  H N N 123 
EDO   H12  H N N 124 
EDO   HO1  H N N 125 
EDO   H21  H N N 126 
EDO   H22  H N N 127 
EDO   HO2  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
HIS   N    N N N 178 
HIS   CA   C N S 179 
HIS   C    C N N 180 
HIS   O    O N N 181 
HIS   CB   C N N 182 
HIS   CG   C Y N 183 
HIS   ND1  N Y N 184 
HIS   CD2  C Y N 185 
HIS   CE1  C Y N 186 
HIS   NE2  N Y N 187 
HIS   OXT  O N N 188 
HIS   H    H N N 189 
HIS   H2   H N N 190 
HIS   HA   H N N 191 
HIS   HB2  H N N 192 
HIS   HB3  H N N 193 
HIS   HD1  H N N 194 
HIS   HD2  H N N 195 
HIS   HE1  H N N 196 
HIS   HE2  H N N 197 
HIS   HXT  H N N 198 
HOH   O    O N N 199 
HOH   H1   H N N 200 
HOH   H2   H N N 201 
ILE   N    N N N 202 
ILE   CA   C N S 203 
ILE   C    C N N 204 
ILE   O    O N N 205 
ILE   CB   C N S 206 
ILE   CG1  C N N 207 
ILE   CG2  C N N 208 
ILE   CD1  C N N 209 
ILE   OXT  O N N 210 
ILE   H    H N N 211 
ILE   H2   H N N 212 
ILE   HA   H N N 213 
ILE   HB   H N N 214 
ILE   HG12 H N N 215 
ILE   HG13 H N N 216 
ILE   HG21 H N N 217 
ILE   HG22 H N N 218 
ILE   HG23 H N N 219 
ILE   HD11 H N N 220 
ILE   HD12 H N N 221 
ILE   HD13 H N N 222 
ILE   HXT  H N N 223 
LEU   N    N N N 224 
LEU   CA   C N S 225 
LEU   C    C N N 226 
LEU   O    O N N 227 
LEU   CB   C N N 228 
LEU   CG   C N N 229 
LEU   CD1  C N N 230 
LEU   CD2  C N N 231 
LEU   OXT  O N N 232 
LEU   H    H N N 233 
LEU   H2   H N N 234 
LEU   HA   H N N 235 
LEU   HB2  H N N 236 
LEU   HB3  H N N 237 
LEU   HG   H N N 238 
LEU   HD11 H N N 239 
LEU   HD12 H N N 240 
LEU   HD13 H N N 241 
LEU   HD21 H N N 242 
LEU   HD22 H N N 243 
LEU   HD23 H N N 244 
LEU   HXT  H N N 245 
LYS   N    N N N 246 
LYS   CA   C N S 247 
LYS   C    C N N 248 
LYS   O    O N N 249 
LYS   CB   C N N 250 
LYS   CG   C N N 251 
LYS   CD   C N N 252 
LYS   CE   C N N 253 
LYS   NZ   N N N 254 
LYS   OXT  O N N 255 
LYS   H    H N N 256 
LYS   H2   H N N 257 
LYS   HA   H N N 258 
LYS   HB2  H N N 259 
LYS   HB3  H N N 260 
LYS   HG2  H N N 261 
LYS   HG3  H N N 262 
LYS   HD2  H N N 263 
LYS   HD3  H N N 264 
LYS   HE2  H N N 265 
LYS   HE3  H N N 266 
LYS   HZ1  H N N 267 
LYS   HZ2  H N N 268 
LYS   HZ3  H N N 269 
LYS   HXT  H N N 270 
MET   N    N N N 271 
MET   CA   C N S 272 
MET   C    C N N 273 
MET   O    O N N 274 
MET   CB   C N N 275 
MET   CG   C N N 276 
MET   SD   S N N 277 
MET   CE   C N N 278 
MET   OXT  O N N 279 
MET   H    H N N 280 
MET   H2   H N N 281 
MET   HA   H N N 282 
MET   HB2  H N N 283 
MET   HB3  H N N 284 
MET   HG2  H N N 285 
MET   HG3  H N N 286 
MET   HE1  H N N 287 
MET   HE2  H N N 288 
MET   HE3  H N N 289 
MET   HXT  H N N 290 
PHE   N    N N N 291 
PHE   CA   C N S 292 
PHE   C    C N N 293 
PHE   O    O N N 294 
PHE   CB   C N N 295 
PHE   CG   C Y N 296 
PHE   CD1  C Y N 297 
PHE   CD2  C Y N 298 
PHE   CE1  C Y N 299 
PHE   CE2  C Y N 300 
PHE   CZ   C Y N 301 
PHE   OXT  O N N 302 
PHE   H    H N N 303 
PHE   H2   H N N 304 
PHE   HA   H N N 305 
PHE   HB2  H N N 306 
PHE   HB3  H N N 307 
PHE   HD1  H N N 308 
PHE   HD2  H N N 309 
PHE   HE1  H N N 310 
PHE   HE2  H N N 311 
PHE   HZ   H N N 312 
PHE   HXT  H N N 313 
PRO   N    N N N 314 
PRO   CA   C N S 315 
PRO   C    C N N 316 
PRO   O    O N N 317 
PRO   CB   C N N 318 
PRO   CG   C N N 319 
PRO   CD   C N N 320 
PRO   OXT  O N N 321 
PRO   H    H N N 322 
PRO   HA   H N N 323 
PRO   HB2  H N N 324 
PRO   HB3  H N N 325 
PRO   HG2  H N N 326 
PRO   HG3  H N N 327 
PRO   HD2  H N N 328 
PRO   HD3  H N N 329 
PRO   HXT  H N N 330 
SER   N    N N N 331 
SER   CA   C N S 332 
SER   C    C N N 333 
SER   O    O N N 334 
SER   CB   C N N 335 
SER   OG   O N N 336 
SER   OXT  O N N 337 
SER   H    H N N 338 
SER   H2   H N N 339 
SER   HA   H N N 340 
SER   HB2  H N N 341 
SER   HB3  H N N 342 
SER   HG   H N N 343 
SER   HXT  H N N 344 
SO4   S    S N N 345 
SO4   O1   O N N 346 
SO4   O2   O N N 347 
SO4   O3   O N N 348 
SO4   O4   O N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
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 
A1A3Z C   C1   sing N N 1   
A1A3Z C1  N    sing N N 2   
A1A3Z C2  N    sing N N 3   
A1A3Z C3  C2   sing N N 4   
A1A3Z N   C4   sing N N 5   
A1A3Z C4  O    doub N N 6   
A1A3Z C5  C4   sing N N 7   
A1A3Z C5  C6   sing Y N 8   
A1A3Z C6  C7   doub Y N 9   
A1A3Z C7  C8   sing Y N 10  
A1A3Z C8  C9   doub Y N 11  
A1A3Z C9  C10  sing Y N 12  
A1A3Z C10 C5   doub Y N 13  
A1A3Z C11 C10  sing N N 14  
A1A3Z C6  H10  sing N N 15  
A1A3Z C7  H11  sing N N 16  
A1A3Z C8  H12  sing N N 17  
A1A3Z C2  H5   sing N N 18  
A1A3Z C2  H6   sing N N 19  
A1A3Z C3  H7   sing N N 20  
A1A3Z C3  H9   sing N N 21  
A1A3Z C3  H8   sing N N 22  
A1A3Z C1  H3   sing N N 23  
A1A3Z C1  H4   sing N N 24  
A1A3Z C   H    sing N N 25  
A1A3Z C   H2   sing N N 26  
A1A3Z C   H1   sing N N 27  
A1A3Z C11 H15  sing N N 28  
A1A3Z C11 H16  sing N N 29  
A1A3Z C11 H14  sing N N 30  
A1A3Z C9  H13  sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
EDO   C1  O1   sing N N 114 
EDO   C1  C2   sing N N 115 
EDO   C1  H11  sing N N 116 
EDO   C1  H12  sing N N 117 
EDO   O1  HO1  sing N N 118 
EDO   C2  O2   sing N N 119 
EDO   C2  H21  sing N N 120 
EDO   C2  H22  sing N N 121 
EDO   O2  HO2  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
SO4   S   O1   doub N N 330 
SO4   S   O2   doub N N 331 
SO4   S   O3   sing N N 332 
SO4   S   O4   sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
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                    7HHP 
_atom_sites.fract_transf_matrix[1][1]   0.024143 
_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]   0.023804 
_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]   0.006288 
_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  ? 0.761   4.379   2.338   1.00 49.26  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.305  3.599   1.656   1.00 57.52  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.304   2.506   0.776   1.00 56.47  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.409   2.648   0.264   1.00 56.99  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.252  4.498   0.846   1.00 64.81  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.321  5.197   1.684   1.00 78.25  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.446  4.171   2.663   1.00 86.96  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.320  5.395   3.649   1.00 79.74  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.396  1.361   0.603   1.00 51.79  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.068   0.271   -0.266  1.00 50.48  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.241   0.604   -1.752  1.00 50.13  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.527  1.365   -2.346  1.00 50.99  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.029  -0.832  -0.070  1.00 52.25  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.769  -0.448  1.193   1.00 52.61  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.670  1.053   1.283   1.00 51.64  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.236   -0.024  -2.373  1.00 42.02  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.369   0.107   -3.808  1.00 40.41  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.811   -1.174  -4.420  1.00 35.20  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.326   -2.025  -3.681  1.00 39.03  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.846   0.307   -4.177  1.00 46.97  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.472   1.583   -3.705  1.00 61.99  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.293   2.124   -2.448  1.00 66.95  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.322   2.405   -4.342  1.00 65.04  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.997   3.242   -2.344  1.00 68.11  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.633   3.429   -3.481  1.00 72.96  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.883   -1.296  -5.752  1.00 30.38  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.663   -2.579  -6.407  1.00 29.88  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.772   -3.570  -6.019  1.00 32.51  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.836   -3.187  -5.530  1.00 32.24  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.561   -2.369  -7.906  1.00 35.46  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.496   -4.856  -6.195  1.00 31.22  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.490   -5.887  -5.958  1.00 31.99  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.674   -5.685  -6.909  1.00 36.11  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.492   -5.254  -8.050  1.00 33.41  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.851   -7.275  -6.057  1.00 28.22  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.119   -7.665  -4.780  1.00 31.82  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.833   -7.865  -3.590  1.00 29.88  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.269  -7.878  -4.779  1.00 27.29  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.172   -8.218  -2.418  1.00 29.00  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.916  -8.304  -3.613  1.00 26.92  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.204  -8.430  -2.437  1.00 29.63  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.893   -5.965  -6.429  1.00 31.47  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.057   -5.853  -7.291  1.00 32.14  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.949   -7.058  -7.011  1.00 29.07  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.884   -7.629  -5.938  1.00 26.02  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.757   -4.504  -7.061  1.00 35.09  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.344   -4.402  -5.686  1.00 39.55  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.863   -3.019  -5.325  1.00 44.94  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.567   -3.143  -4.015  1.00 45.70  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.617   -3.232  -2.909  1.00 39.61  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.783   -7.508  -7.967  1.00 30.62  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.728   -8.595  -7.688  1.00 30.46  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.566   -8.339  -6.431  1.00 27.79  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.006  -7.218  -6.201  1.00 28.60  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.592   -8.582  -8.959  1.00 30.29  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.676   -8.059  -10.062 1.00 32.22  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.880   -6.966  -9.340  1.00 33.53  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.776   -9.393  -5.619  1.00 26.36  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.467  -9.264  -4.351  1.00 23.29  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.507   -9.212  -3.161  1.00 27.38  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.886   -9.565  -2.031  1.00 28.96  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.251   -8.790  -3.389  1.00 23.86  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.309   -8.725  -2.272  1.00 23.03  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.040   -10.101 -1.672  1.00 23.00  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.924   -11.081 -2.421  1.00 25.59  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.972   -8.106  -2.665  1.00 25.13  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.961   -6.604  -2.888  1.00 27.83  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.920   -5.915  -2.466  1.00 28.12  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.013   -6.125  -3.525  1.00 26.65  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.971   -10.162 -0.323  1.00 23.24  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.799   -11.429 0.387   1.00 24.03  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.331   -11.521 0.802   1.00 26.22  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.771   -10.528 1.298   1.00 27.99  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.737   -11.479 1.596   1.00 23.45  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.229   -11.265 1.273   1.00 22.02  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.090  -11.292 2.545   1.00 24.67  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.666   -12.286 0.217   1.00 24.43  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.752   -12.727 0.710   1.00 25.42  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.316   -12.836 0.932   1.00 25.75  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.061   -14.200 1.558   1.00 28.78  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.961   -15.043 1.614   1.00 26.15  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.519   -12.704 -0.383  1.00 21.70  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.724   -11.331 -1.006  1.00 22.23  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.809   -13.817 -1.402  1.00 23.40  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.831   -14.388 2.027   1.00 24.94  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.251   -15.714 2.087   1.00 26.63  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.299   -15.811 0.904   1.00 30.26  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.494  -14.900 0.716   1.00 27.02  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.470   -16.031 3.373   1.00 27.24  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.404   -16.168 4.570   1.00 27.79  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.799   -15.048 5.312   1.00 29.93  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.877   -17.411 4.947   1.00 28.10  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.696   -15.177 6.360   1.00 34.63  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.772   -17.547 6.001   1.00 30.49  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.175   -16.443 6.710   1.00 30.52  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.406   -16.906 0.121   1.00 27.64  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.370  -17.080 -1.099  1.00 24.82  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.363  -18.231 -0.893  1.00 29.51  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.991  -19.299 -0.394  1.00 29.12  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.547   -17.387 -2.270  1.00 22.89  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.622  -18.007 -1.283  1.00 29.52  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.652  -18.997 -1.012  1.00 31.28  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.975  -19.718 -2.317  1.00 34.16  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.251  -19.070 -3.328  1.00 37.41  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.907  -18.366 -0.408  1.00 30.45  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.985  -19.398 -0.022  1.00 36.27  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.527  -20.316 1.115   1.00 39.93  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.630  -21.177 1.683   1.00 40.39  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -7.020  -22.166 0.674   1.00 39.10  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.892  -21.048 -2.282  1.00 32.43  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.490  -21.865 -3.328  1.00 32.04  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.549  -22.801 -2.743  1.00 33.45  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.441  -23.205 -1.595  1.00 34.72  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.382  -22.585 -4.082  1.00 40.06  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.567  -21.527 -4.822  1.00 41.42  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.668  -22.259 -6.175  1.00 50.77  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -2.912  -22.841 -7.334  1.00 63.15  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.586  -23.087 -3.536  1.00 39.29  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.630  -24.041 -3.190  1.00 39.41  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -7.005  -25.284 -2.578  1.00 43.19  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -6.100  -25.875 -3.164  1.00 45.76  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.301  -24.502 -4.491  1.00 44.32  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.621  -25.235 -4.312  1.00 46.60  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.663 -24.382 -3.583  1.00 55.95  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.494  -25.677 -1.393  1.00 41.90  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -7.087  -26.949 -0.828  1.00 41.53  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.717  -26.894 -0.155  1.00 45.72  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.224  -27.914 0.310   1.00 48.19  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -5.102  -25.709 -0.060  1.00 39.23  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.837  -25.657 0.641   1.00 37.56  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.906  -24.562 1.680   1.00 37.15  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.631  -23.597 1.469   1.00 34.58  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.749  -25.216 -0.332  1.00 43.67  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.211  -26.281 -1.272  1.00 45.70  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -1.129  -27.067 -0.901  1.00 53.46  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.744  -26.451 -2.543  1.00 51.49  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.595  -28.006 -1.765  1.00 61.09  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.225  -27.392 -3.418  1.00 61.74  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.148  -28.173 -3.023  1.00 70.20  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.624  -29.119 -3.863  1.00 85.44  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -3.128  -24.642 2.789   1.00 33.89  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -3.102  -23.539 3.758   1.00 34.63  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.446  -22.329 3.075   1.00 31.11  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.756  -22.510 2.070   1.00 30.81  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.254  -24.144 4.904   1.00 35.31  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.320  -25.106 4.194   1.00 35.73  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.171  -25.725 3.100   1.00 37.02  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.724  -21.111 3.567   1.00 29.75  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.992  -19.922 3.156   1.00 27.16  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.489  -20.221 3.249   1.00 28.64  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? -0.014  -20.703 4.289   1.00 29.87  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.408  -18.705 3.999   1.00 27.34  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.863  -18.356 3.851   1.00 31.24  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.866  -19.050 4.528   1.00 32.41  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.486  -17.395 3.121   1.00 29.40  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -6.052  -18.532 4.214   1.00 32.89  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.851  -17.523 3.357   1.00 35.26  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.260   -19.939 2.170   1.00 28.56  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.588   -20.543 2.031   1.00 29.19  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.668   -19.480 1.852   1.00 28.28  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.510   -18.581 1.034   1.00 30.80  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.618   -21.494 0.835   1.00 28.41  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.701   -22.536 0.900   1.00 32.19  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.037   -22.390 0.642   1.00 33.98  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.501   -23.926 1.213   1.00 31.13  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.690   -23.594 0.792   1.00 32.00  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.764   -24.560 1.116   1.00 32.67  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.376   -24.701 1.523   1.00 34.56  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 3.944   -25.926 1.362   1.00 34.59  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.556   -26.058 1.742   1.00 34.34  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.820   -26.657 1.685   1.00 38.14  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.801   -19.572 2.586   1.00 26.92  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.878   -18.577 2.446   1.00 25.34  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.360   -18.543 0.994   1.00 24.78  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.616   -19.599 0.380   1.00 25.05  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.955   -19.043 3.451   1.00 27.29  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.668   -20.544 3.632   1.00 25.24  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.108   -20.606 3.591   1.00 27.85  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.409   -17.328 0.442   1.00 23.46  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.723   -17.116 -0.962  1.00 25.53  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.261   -15.722 -1.273  1.00 21.02  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.362   -14.810 -0.419  1.00 21.81  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.534   -17.480 -1.853  1.00 24.95  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.736   -15.593 -2.515  1.00 24.84  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.167   -14.281 -2.962  1.00 25.90  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.647   -14.037 -4.372  1.00 24.79  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.367   -14.992 -5.100  1.00 26.32  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.694   -14.195 -2.887  1.00 21.72  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.380   -15.115 -3.892  1.00 22.17  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 10.909  -14.877 -3.874  1.00 22.46  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.625  -15.703 -4.872  1.00 25.91  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 12.891  -16.132 -4.753  1.00 25.33  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.615  -15.935 -3.649  1.00 25.27  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.419  -16.783 -5.762  1.00 27.70  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.547   -12.759 -4.763  1.00 24.99  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.339   -12.386 -6.158  1.00 27.28  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.685   -12.512 -6.861  1.00 27.37  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.658   -11.921 -6.402  1.00 26.80  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.810   -10.943 -6.299  1.00 32.82  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.610   -10.643 -5.361  1.00 36.59  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.545   -10.594 -7.780  1.00 27.55  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.312   -11.292 -5.764  1.00 36.57  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.735   -13.295 -7.941  1.00 26.72  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 8.985   -13.483 -8.667  1.00 32.30  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.105   -12.494 -9.823  1.00 35.30  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.115   -11.943 -10.293 1.00 30.83  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.123   -14.886 -9.241  1.00 30.00  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.059  -15.827 -8.498  1.00 31.29  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.682  -15.404 -7.512  1.00 35.90  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.167  -16.978 -8.920  1.00 32.39  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.352  -12.291 -10.270 1.00 38.11  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.634  -11.680 -11.552 1.00 42.25  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.347  -12.709 -12.645 1.00 41.75  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.410  -13.911 -12.396 1.00 36.69  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.106  -11.295 -11.635 1.00 43.24  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.527  -10.067 -10.841 1.00 50.73  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.211  -8.932  -11.301 1.00 55.72  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.166  -10.259 -9.772  1.00 49.36  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 9.990   -12.232 -13.843 1.00 45.02  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 9.970   -13.078 -15.027 1.00 41.17  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.352  -12.959 -15.665 1.00 42.30  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.783  -11.849 -15.975 1.00 38.28  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 8.868   -12.601 -15.990 1.00 44.52  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.502   -12.500 -15.271 1.00 44.81  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.808   -13.488 -17.240 1.00 37.35  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.564   -11.457 -15.853 1.00 45.19  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.056  -14.084 -15.836 1.00 42.13  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.360  -14.046 -16.491 1.00 41.83  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.192  -13.716 -17.982 1.00 40.05  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.185  -14.058 -18.602 1.00 39.70  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.097  -15.351 -16.274 1.00 41.34  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.163  -12.979 -18.529 1.00 42.89  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.279  -12.802 -19.969 1.00 40.84  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.066  -14.148 -20.652 1.00 35.16  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.726  -15.127 -20.310 1.00 35.54  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.651  -12.269 -20.358 1.00 42.13  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.828  -10.770 -20.176 1.00 44.82  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.826  -10.087 -19.939 1.00 52.48  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.964  -10.292 -20.304 1.00 49.19  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.106  -14.177 -21.583 1.00 33.30  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 12.868  -15.328 -22.438 1.00 36.40  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 11.964  -16.373 -21.792 1.00 44.96  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.764  -17.441 -22.370 1.00 42.20  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.443  -16.054 -20.599 1.00 42.88  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.606  -16.983 -19.850 1.00 47.53  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.134   -16.657 -20.094 1.00 41.76  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.790   -15.518 -20.397 1.00 39.60  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 10.943  -16.917 -18.364 1.00 45.70  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.275   -17.678 -19.937 1.00 46.10  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 6.837   -17.573 -20.152 1.00 40.29  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.252   -16.541 -19.188 1.00 37.51  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.497   -16.613 -17.992 1.00 41.56  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.230   -18.963 -19.895 1.00 47.49  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 4.704   -18.933 -19.977 1.00 41.46  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 6.824   -20.016 -20.834 1.00 47.77  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.523   -15.565 -19.734 1.00 40.91  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.872   -14.514 -18.963 1.00 40.77  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.618   -15.096 -18.307 1.00 45.43  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.091   -16.101 -18.783 1.00 41.02  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.530   -13.292 -19.829 1.00 43.97  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.737   -12.438 -20.259 1.00 48.11  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.517   -11.285 -21.241 1.00 51.60  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.154   -11.739 -22.625 1.00 45.82  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 4.765   -10.605 -23.462 1.00 47.27  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.118   -14.498 -17.198 1.00 45.92  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.852   -14.918 -16.593 1.00 46.06  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.693   -14.348 -17.403 1.00 45.76  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.871   -13.355 -18.095 1.00 43.70  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.896   -14.301 -15.189 1.00 43.87  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.820   -13.110 -15.307 1.00 49.50  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.760   -13.403 -16.458 1.00 48.78  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.538  -14.900 -17.290 1.00 45.14  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.707  -14.296 -17.941 1.00 49.21  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.889  -12.889 -17.394 1.00 49.49  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.281  -12.566 -16.374 1.00 46.08  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.875  -15.189 -17.532 1.00 42.88  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.210  -16.489 -17.115 1.00 40.63  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.864  -16.110 -16.515 1.00 42.21  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.698  -12.029 -18.064 1.00 47.18  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -3.045  -10.704 -17.545 1.00 48.61  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.654  -10.708 -16.145 1.00 45.17  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.432  -11.584 -15.795 1.00 47.70  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -4.015  -10.092 -18.588 1.00 48.96  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.356  -11.230 -19.531 1.00 43.25  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.259  -12.267 -19.409 1.00 51.05  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.258  -9.718  -15.346 1.00 47.78  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.717  -9.558  -13.976 1.00 48.49  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.214  -10.678 -13.058 1.00 41.97  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.635  -10.715 -11.909 1.00 40.36  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.229  -9.341  -13.913 1.00 56.25  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.663  -8.170  -14.763 1.00 62.86  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.615  -7.018  -14.319 1.00 61.34  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.088  -8.446  -15.986 1.00 65.25  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.339  -11.587 -13.539 1.00 36.98  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.744  -12.599 -12.663 1.00 31.08  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.269  -12.272 -12.381 1.00 29.21  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.398   -11.553 -13.138 1.00 34.74  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.951  -14.044 -13.135 1.00 33.87  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.378  -14.538 -13.359 1.00 39.86  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.407  -13.925 -12.410 1.00 43.46  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.861  -14.319 -12.567 1.00 44.37  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.989  -15.779 -12.572 1.00 45.69  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.224   -12.752 -11.244 1.00 25.09  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.629   -12.545 -10.895 1.00 26.52  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.296   -13.904 -10.810 1.00 28.05  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.653   -14.871 -10.418 1.00 29.83  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.726   -11.874 -9.527  1.00 26.61  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.239   -10.438 -9.523  1.00 30.95  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.118  -10.140 -9.425  1.00 39.01  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.126   -9.385  -9.675  1.00 34.48  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.564  -8.825  -9.484  1.00 37.68  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.703   -8.062  -9.697  1.00 33.92  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.350   -7.789  -9.601  1.00 35.79  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.092  -6.489  -9.648  1.00 40.64  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.614   -14.037 -11.067 1.00 28.25  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.266   -15.335 -10.865 1.00 27.71  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.578   -15.465 -9.380  1.00 26.65  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.237   -14.593 -8.807  1.00 30.22  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.538   -15.262 -11.709 1.00 28.17  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.743   -13.809 -12.026 1.00 26.47  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.537   -12.975 -11.508 1.00 28.93  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.045   -16.517 -8.761  1.00 27.22  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.221   -16.732 -7.347  1.00 25.14  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.193   -17.883 -7.139  1.00 26.16  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 4.917   -19.019 -7.539  1.00 30.53  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 2.884   -16.978 -6.634  1.00 27.40  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 1.896   -15.789 -6.911  1.00 23.28  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.127   -17.215 -5.131  1.00 27.36  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.412   -14.390 -6.569  1.00 22.15  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.300   -17.588 -6.452  1.00 24.78  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.189   -18.663 -6.034  1.00 27.26  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.891   -19.073 -4.592  1.00 25.26  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.022   -18.263 -3.659  1.00 27.92  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.633   -18.170 -6.200  1.00 26.85  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.663   -19.171 -5.694  1.00 26.75  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.121  -20.197 -6.537  1.00 28.62  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.180  -19.081 -4.402  1.00 26.33  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.066  -21.099 -6.098  1.00 30.45  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.105  -20.023 -3.952  1.00 30.85  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.553  -21.013 -4.813  1.00 31.55  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.604   -20.367 -4.406  1.00 26.77  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.229   -20.929 -3.113  1.00 23.10  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.504   -21.411 -2.417  1.00 29.56  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.225   -22.279 -2.952  1.00 27.01  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.228   -22.078 -3.354  1.00 27.89  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.863   -21.544 -3.762  1.00 27.61  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.520   -21.356 -5.107  1.00 30.14  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 2.917   -21.254 -2.789  1.00 29.67  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.268   -20.840 -5.454  1.00 30.96  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.688   -20.710 -3.136  1.00 29.61  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.364   -20.524 -4.469  1.00 29.84  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.782   -20.848 -1.235  1.00 29.61  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 8.909   -21.325 -0.443  1.00 30.34  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.681   -22.780 -0.018  1.00 29.48  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.536   -23.239 0.112   1.00 28.25  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.208   -20.387 0.742   1.00 27.80  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.648   -18.975 0.356   1.00 26.74  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 10.884  -18.732 -0.242  1.00 27.49  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 8.854   -17.868 0.668   1.00 25.48  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.281  -17.434 -0.585  1.00 27.16  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.254   -16.566 0.327   1.00 24.57  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.484  -16.349 -0.288  1.00 29.20  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.790   -23.499 0.203   1.00 28.09  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.723   -24.873 0.678   1.00 31.14  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.507   -25.846 -0.482  1.00 38.17  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.380  -26.673 -0.764  1.00 34.77  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.376   -25.719 -1.190  1.00 35.90  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.100   -26.601 -2.317  1.00 37.42  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 8.884   -26.157 -3.546  1.00 39.70  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.163   -26.956 -4.445  1.00 35.91  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.605   -26.668 -2.637  1.00 37.62  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.213   -25.355 -3.031  1.00 41.92  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.780   -27.209 -1.493  1.00 36.89  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.160   -24.852 -3.607  1.00 31.40  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 9.857   -24.217 -4.713  1.00 33.76  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.042   -24.313 -5.997  1.00 34.12  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.623   -24.273 -7.083  1.00 34.14  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.294  -24.751 -4.859  1.00 32.01  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.013  -24.809 -3.563  1.00 37.92  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 12.866  -25.843 -3.267  1.00 39.04  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.042  -23.979 -2.497  1.00 36.62  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.373  -25.659 -2.049  1.00 47.07  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 12.896  -24.529 -1.567  1.00 44.66  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.710   -24.421 -5.864  1.00 35.52  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 6.781   -24.406 -6.990  1.00 36.41  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.392   -22.970 -7.350  1.00 36.97  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.492   -22.059 -6.502  1.00 33.89  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.534   -25.230 -6.666  1.00 40.96  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 5.862   -26.721 -6.569  1.00 49.43  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 4.801   -27.658 -6.019  1.00 55.97  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.616   -27.277 -5.850  1.00 54.37  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.211   -28.798 -5.714  1.00 60.34  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.051   -22.787 -8.635  1.00 29.91  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.513   -21.539 -9.157  1.00 34.27  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.063   -21.764 -9.582  1.00 33.93  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.718   -22.779 -10.195 1.00 35.40  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.339   -21.020 -10.335 1.00 35.07  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.610   -20.629 -9.832  1.00 30.48  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.725   -19.787 -10.983 1.00 39.08  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.204   -20.812 -9.238  1.00 30.76  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.905   -20.684 -9.868  1.00 31.27  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.622   -19.216 -10.158 1.00 33.53  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.326   -18.305 -9.690  1.00 28.80  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.830   -21.332 -9.000  1.00 32.42  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.548   -19.009 -10.927 1.00 29.39  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.096   -17.690 -11.314 1.00 32.11  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.146  -17.352 -10.506 1.00 33.32  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.137  -18.080 -10.575 1.00 36.77  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.198  -17.687 -12.812 1.00 29.43  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.029   -17.957 -13.668 1.00 36.42  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.160   -17.153 -13.564 1.00 39.64  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.042   -19.013 -14.575 1.00 39.20  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.276   -17.390 -14.360 1.00 52.47  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.161   -19.244 -15.371 1.00 47.28  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.272   -18.434 -15.269 1.00 43.90  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -1.066  -16.251 -9.745  1.00 28.36  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.163  -15.835 -8.887  1.00 28.89  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.416  -14.329 -9.021  1.00 28.72  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.519  -13.534 -9.338  1.00 29.56  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.781  -16.163 -7.448  1.00 32.07  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.788  -17.633 -7.039  1.00 30.63  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.332  -17.666 -5.591  1.00 30.06  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.197  -18.206 -7.170  1.00 38.09  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.684  -13.951 -8.821  1.00 27.98  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -4.084  -12.557 -8.768  1.00 27.95  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -4.110  -12.089 -7.318  1.00 28.07  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.991  -12.907 -6.385  1.00 26.68  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.228  -10.765 -7.107  1.00 27.91  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.164  -10.171 -5.767  1.00 26.94  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.125  -10.690 -4.701  1.00 27.05  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.806  -10.644 -3.522  1.00 25.23  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.298  -8.676  -6.061  1.00 28.04  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.612  -8.578  -7.394  1.00 30.75  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.254  -9.743  -8.171  1.00 28.29  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.267  -11.260 -5.108  1.00 26.78  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.211  -11.727 -4.103  1.00 26.94  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.629  -12.875 -3.276  1.00 28.06  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.120  -13.143 -2.175  1.00 27.34  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.510  -12.224 -4.756  1.00 30.64  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.385  -13.535 -5.511  1.00 36.11  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.687  -13.810 -6.269  1.00 47.35  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.601  -15.001 -7.170  1.00 51.81  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.405  -16.249 -6.423  1.00 49.24  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.613  -13.569 -3.829  1.00 25.91  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -5.018  -14.732 -3.206  1.00 28.68  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.690  -14.386 -2.527  1.00 26.47  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -3.031  -15.291 -2.011  1.00 25.40  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.992  -15.873 -4.217  1.00 27.03  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.381  -16.434 -4.470  1.00 31.45  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.192  -16.320 -3.535  1.00 33.05  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.660  -16.891 -5.600  1.00 31.48  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.318  -13.087 -2.491  1.00 25.20  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.984  -12.696 -2.031  1.00 24.37  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.097  -11.838 -0.757  1.00 23.67  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.769  -10.811 -0.769  1.00 26.74  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.258  -11.966 -3.171  1.00 23.65  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.141  -12.729 -4.497  1.00 24.69  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.298  -11.867 -5.422  1.00 26.81  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.404  -14.044 -4.327  1.00 25.71  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.520  -12.321 0.358   1.00 24.48  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.618  -11.637 1.652   1.00 24.35  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.241  -11.144 2.055   1.00 24.62  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.638   -11.983 2.312   1.00 26.54  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.034  -12.652 2.717   1.00 23.96  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.484  -13.052 2.484   1.00 25.55  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.807  -13.968 1.483   1.00 25.54  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.496  -12.548 3.303   1.00 27.25  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.130  -14.330 1.259   1.00 30.19  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.830  -12.893 3.057   1.00 28.01  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.135  -13.806 2.055   1.00 28.24  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? -0.015  -9.816  2.140   1.00 30.03  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.298   -9.294  2.555   1.00 28.26  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.842   -9.967  3.817   1.00 29.99  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.153   -10.082 4.814   1.00 27.64  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.012   -7.787  2.737   1.00 33.62  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? -0.065  -7.524  1.682   1.00 36.62  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.968  -8.761  1.758   1.00 29.68  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.101   -10.427 3.751   1.00 28.76  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.701   -11.248 4.792   1.00 29.55  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.697   -10.564 6.171   1.00 27.95  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.339   -11.207 7.144   1.00 35.64  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.122   -11.615 4.331   1.00 28.57  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.899   -12.383 5.386   1.00 29.87  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.622   -13.720 5.654   1.00 29.83  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 6.929   -11.763 6.104   1.00 35.04  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.322   -14.424 6.627   1.00 33.44  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.655   -12.466 7.057   1.00 32.85  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.334   -13.782 7.331   1.00 36.91  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.049   -14.440 8.292   1.00 38.60  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.161   -9.311  6.261   1.00 31.09  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.279   -8.649  7.562   1.00 39.32  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 2.931   -8.600  8.284   1.00 39.95  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.807   -9.096  9.400   1.00 42.62  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.045   -7.337  7.487   1.00 43.05  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.558   -7.505  7.486   1.00 65.67  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 7.056   -8.195  6.583   1.00 73.60  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 7.227   -6.977  8.407   1.00 81.95  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 1.900   -8.078  7.610   1.00 40.67  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.560   -8.052  8.188   1.00 39.70  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? 0.047   -9.440  8.601   1.00 37.42  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.743  -9.514  9.544   1.00 38.18  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.418  -7.354  7.228   1.00 38.65  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.861  -7.202  7.717   1.00 45.25  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.756  -6.660  6.611   1.00 42.62  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.847  -5.784  7.154   1.00 48.38  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.905  -6.583  7.753   1.00 47.17  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.424   -10.532 7.893   1.00 33.83  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.316  -11.791 8.004   1.00 33.43  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.473   -12.864 8.746   1.00 31.89  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? -0.059  -13.944 8.940   1.00 29.26  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.710  -12.392 6.654   1.00 35.02  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.242  -11.386 5.810   1.00 46.54  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.749   -12.605 9.043   1.00 34.32  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.621   -13.641 9.607   1.00 37.06  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 2.145   -14.191 10.957  1.00 36.98  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 2.300   -15.389 11.226  1.00 34.34  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 4.113   -13.274 9.572   1.00 40.61  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.562   -12.062 10.370  1.00 43.60  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 6.085   -12.040 10.346  1.00 53.79  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.680   -10.845 11.052  1.00 60.11  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.537   -9.580  10.313  1.00 68.53  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.542   -13.329 11.788  0.50 38.58  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.571   -13.327 11.804  0.50 37.84  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 0.995   -13.733 13.081  0.50 41.35  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 1.000   -13.772 13.072  0.50 39.89  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? -0.118  -14.775 12.911  0.50 41.70  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? -0.037  -14.871 12.825  0.50 40.88  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.228  -15.725 13.682  0.50 42.30  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? -0.018  -15.933 13.450  0.50 38.65  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.633   -12.522 13.933  0.50 41.99  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.400   -12.612 13.855  0.50 40.15  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 1.823   -11.723 14.446  0.50 46.34  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? 0.012   -12.940 15.290  0.50 42.85  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 2.964   -12.213 14.286  0.50 44.20  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.923   -12.999 16.138  0.50 44.95  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.609   -10.615 14.994  0.50 46.93  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.189  -13.163 15.539  0.50 42.37  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -0.923  -14.634 11.861  1.00 39.01  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -1.991  -15.577 11.629  1.00 37.83  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.502  -16.819 10.888  1.00 37.49  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -1.965  -17.922 11.180  1.00 39.62  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -3.043  -14.847 10.803  1.00 38.21  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.278  -15.677 10.570  1.00 41.14  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.323  -14.744 9.964   1.00 45.52  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.635  -15.405 9.639   1.00 52.72  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.633  -14.454 9.127   1.00 46.82  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.647  -16.637 9.867   1.00 34.19  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.444  -17.734 8.928   1.00 31.78  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 0.931   -18.381 9.101   1.00 31.66  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 1.169   -19.443 8.528   1.00 36.90  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.614  -17.267 7.474   1.00 30.00  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -2.017  -16.823 7.081   1.00 33.94  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -3.158  -17.522 7.499   1.00 33.52  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -2.197  -15.690 6.282   1.00 32.74  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.432  -17.103 7.130   1.00 36.53  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.469  -15.257 5.930   1.00 38.27  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.585  -15.962 6.349   1.00 32.24  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -5.828  -15.516 5.967   1.00 36.49  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 1.828   -17.719 9.849   1.00 34.48  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 3.208   -18.170 9.963   1.00 35.39  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.385   -19.152 11.125  1.00 38.54  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.108   -18.873 12.058  1.00 42.09  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.688   -20.287 11.068  1.00 43.76  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 2.760   -21.278 12.131  1.00 46.84  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 3.007   -22.632 11.480  1.00 42.74  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 2.655   -22.829 10.318  1.00 36.83  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.537   -21.172 13.052  1.00 47.91  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.435   -19.828 13.789  1.00 49.75  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.193   -19.689 14.663  1.00 59.92  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 3.685   -23.586 12.156  1.00 41.98  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 4.027   -24.855 11.511  1.00 39.50  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 2.804   -25.610 11.008  1.00 39.83  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 1.724   -25.482 11.571  1.00 45.40  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 4.760   -25.623 12.617  1.00 46.29  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.283   -24.528 13.523  1.00 48.95  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.170   -23.486 13.541  1.00 46.80  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 3.000   -26.391 9.945   1.00 44.73  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 1.917   -27.065 9.256   1.00 47.10  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.460   -28.399 8.773   1.00 50.34  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 3.633   -28.515 8.438   1.00 52.54  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.337   -26.190 8.145   1.00 52.17  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? 0.039   -26.716 7.576   1.00 54.34  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? 0.046   -27.637 6.752   1.00 52.04  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -1.086  -26.133 7.968   1.00 54.77  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 1.586   -29.406 8.758   1.00 57.14  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 1.979   -30.774 8.481   1.00 56.39  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.400   -30.918 7.017   1.00 58.05  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 3.187   -31.805 6.697   1.00 57.47  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 0.863   -31.723 8.948   1.00 59.04  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? -0.331  -31.875 8.010   1.00 60.68  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 1.905   -30.032 6.138   1.00 53.03  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 2.013   -30.230 4.696   1.00 51.85  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.469   -30.211 4.216   1.00 45.10  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 4.308   -29.491 4.760   1.00 46.73  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 1.112   -29.241 3.945   1.00 52.66  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? -0.357  -29.382 4.320   1.00 55.19  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -0.998  -30.590 3.654   1.00 53.87  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -1.859  -30.163 2.546   1.00 72.39  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -3.007  -29.499 2.720   1.00 74.85  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -3.688  -29.079 1.669   1.00 69.70  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.462  -29.252 3.943   1.00 76.14  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 3.740   -30.992 3.162   1.00 41.38  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 5.086   -31.189 2.643   1.00 40.97  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 5.661   -29.847 2.216   1.00 38.45  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 5.079   -29.144 1.381   1.00 36.37  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 5.071   -32.058 1.382   1.00 39.46  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.403   -32.366 0.738   1.00 44.55  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.376   -33.486 -0.299  1.00 48.06  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 7.739   -33.955 -0.713  1.00 48.77  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 6.800   -29.501 2.816   1.00 38.54  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.560   -28.345 2.380   1.00 38.50  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 7.186   -27.056 3.112   1.00 38.16  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 7.864   -26.052 2.936   1.00 32.89  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 6.145   -27.081 3.942   1.00 34.94  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 5.656   -25.850 4.539   1.00 35.23  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 6.644   -25.254 5.548   1.00 38.62  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 6.850   -24.042 5.607   1.00 34.00  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 4.331   -26.125 5.244   1.00 34.52  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.571   -24.856 5.601   1.00 35.24  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 3.764   -24.207 6.816   1.00 35.63  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 2.662   -24.306 4.701   1.00 35.19  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 3.065   -23.036 7.113   1.00 39.07  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 1.961   -23.147 5.004   1.00 29.14  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 2.153   -22.523 6.223   1.00 29.51  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 7.179   -26.092 6.435   1.00 35.51  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 8.069   -25.626 7.490   1.00 33.23  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.413   -25.154 6.910   1.00 31.59  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 10.015  -24.195 7.411   1.00 32.80  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 8.173   -26.703 8.562   1.00 38.04  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 6.853   -26.887 9.278   1.00 44.60  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 6.004   -25.987 9.266   1.00 36.41  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 6.676   -28.023 9.943   1.00 41.57  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 9.880   -25.849 5.870   1.00 31.22  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 11.032  -25.390 5.124   1.00 35.27  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 10.697  -24.005 4.587   1.00 30.55  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.498  -23.078 4.712   1.00 29.90  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.448  -26.309 3.976   1.00 36.02  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 12.787  -25.922 3.350   1.00 37.81  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 13.274  -26.925 2.312   1.00 48.41  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 12.569  -27.922 2.051   1.00 50.04  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 14.346  -26.704 1.732   1.00 47.46  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.486   -23.882 4.047   1.00 28.86  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 9.070   -22.612 3.474   1.00 32.70  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 9.074   -21.489 4.511   1.00 31.21  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.414   -20.335 4.192   1.00 28.48  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 8.645   -21.808 5.736   1.00 27.28  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 8.653   -20.798 6.785   1.00 29.51  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 10.084  -20.327 7.075   1.00 31.59  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.286  -19.134 7.327   1.00 26.50  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 7.928   -21.124 8.089   1.00 29.44  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.444   -21.495 7.957   1.00 32.93  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 6.015   -22.096 9.271   1.00 34.85  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 5.554   -20.315 7.636   1.00 30.15  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 11.063  -21.257 7.035   1.00 29.40  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.440  -20.882 7.337   1.00 31.19  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 12.899  -19.928 6.240   1.00 29.52  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 13.520  -18.899 6.503   1.00 31.38  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.366  -22.120 7.469   1.00 29.94  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 14.814  -21.764 7.726   1.00 31.48  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.451  -21.616 8.928   1.00 30.67  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 15.786  -21.429 6.720   1.00 30.16  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 16.758  -21.250 8.735   1.00 31.78  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 16.980  -21.102 7.395   1.00 32.40  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 15.745  -21.371 5.320   1.00 30.87  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 18.132  -20.729 6.715   1.00 30.94  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 16.881  -20.979 4.646   1.00 37.80  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 18.050  -20.649 5.346   1.00 34.37  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 12.557  -20.272 5.000   1.00 27.26  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 13.065  -19.556 3.845   1.00 25.16  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 12.568  -18.110 3.863   1.00 29.10  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.337  -17.168 3.649   1.00 26.77  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 12.643  -20.234 2.544   1.00 25.18  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.429  -21.521 2.293   1.00 29.59  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 12.977  -22.307 1.071   1.00 33.74  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 12.006  -21.878 0.420   1.00 33.08  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 13.607  -23.349 0.744   1.00 34.42  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 11.264  -17.945 4.079   1.00 29.40  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 10.701  -16.610 3.975   1.00 26.76  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.281  -15.728 5.084   1.00 26.70  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.425  -14.516 4.909   1.00 26.40  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 9.161   -16.613 3.991   1.00 24.37  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.605   -15.229 3.513   1.00 24.80  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 8.609   -17.005 5.369   1.00 24.86  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 7.149   -15.249 3.016   1.00 23.36  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.591  -16.337 6.241   1.00 24.86  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 12.082  -15.562 7.378   1.00 28.37  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 13.593  -15.325 7.242   1.00 30.04  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 14.050  -14.243 7.598   1.00 34.95  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 11.694  -16.237 8.704   1.00 28.22  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 11.987  -15.407 9.951   1.00 37.59  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.463  -15.997 11.250  1.00 43.07  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 11.171  -17.200 11.371  1.00 47.66  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.369  -15.136 12.258  1.00 39.51  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.349  -16.311 6.713   1.00 27.49  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 15.810  -16.301 6.787   1.00 27.13  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.520  -15.908 5.484   1.00 30.13  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 17.626  -15.342 5.546   1.00 27.40  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.351  -17.522 7.535   1.00 26.95  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 15.777  -17.589 8.931   1.00 27.14  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 16.089  -16.753 9.790   1.00 31.97  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 14.825  -18.477 9.154   1.00 31.16  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 15.980  -16.269 4.303   1.00 27.34  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 16.634  -15.886 3.050   1.00 29.75  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 15.579  -15.813 1.933   1.00 26.64  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 15.604  -16.566 0.957   1.00 26.98  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 17.848  -16.775 2.747   1.00 29.74  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 18.903  -16.138 1.869   1.00 33.71  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 18.625  -15.170 1.153   1.00 30.25  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 20.111  -16.710 1.839   1.00 30.83  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 14.631  -14.866 2.060   1.00 24.85  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.471  -14.768 1.167   1.00 26.63  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 13.832  -14.385 -0.264  1.00 29.23  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 13.036  -14.614 -1.153  1.00 24.97  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.595  -13.706 1.825   1.00 22.24  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.568  -12.879 2.617   1.00 23.24  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.617  -13.854 3.140   1.00 20.50  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 15.029  -13.818 -0.480  1.00 25.07  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.376  -13.271 -1.788  1.00 27.06  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.492  -14.071 -2.480  1.00 28.06  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 17.011  -13.635 -3.509  1.00 28.31  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 15.789  -11.801 -1.627  1.00 24.39  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 14.697  -10.958 -1.047  1.00 24.75  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.460  -10.868 -1.666  1.00 23.55  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 14.635  -10.141 0.042   1.00 23.06  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 12.681  -10.031 -0.975  1.00 23.16  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.379  -9.586  0.055   1.00 26.78  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 16.812  -15.256 -1.945  1.00 29.57  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 17.908  -16.073 -2.452  1.00 26.69  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.462  -16.807 -3.708  1.00 31.12  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 16.261  -16.967 -3.946  1.00 28.97  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.300  -17.063 -1.378  1.00 28.26  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.444  -17.296 -4.487  1.00 29.64  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 18.142  -18.199 -5.588  1.00 32.87  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 17.849  -19.592 -5.038  1.00 35.82  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 18.638  -20.120 -4.264  1.00 39.14  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.288  -18.236 -6.557  1.00 38.15  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 19.119  -19.310 -7.465  1.00 46.89  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 16.698  -20.166 -5.405  1.00 32.38  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 16.342  -21.493 -4.947  1.00 37.28  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 16.292  -22.430 -6.152  1.00 42.60  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 15.730  -23.516 -6.061  1.00 49.75  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 14.995  -21.463 -4.217  1.00 34.60  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 15.089  -20.897 -2.810  1.00 32.94  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.440  -21.707 -1.730  1.00 33.94  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 14.815  -19.558 -2.560  1.00 34.06  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 15.560  -21.182 -0.450  1.00 38.45  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 14.919  -19.033 -1.285  1.00 36.58  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.293  -19.844 -0.227  1.00 34.31  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.419  -19.336 1.028   1.00 34.62  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 16.887  -21.985 -7.266  1.00 55.86  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 17.020  -22.764 -8.490  1.00 71.18  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 17.643  -24.130 -8.160  1.00 82.77  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 18.766  -24.132 -7.596  1.00 84.22  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.862  -22.029 -9.517  1.00 69.15  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 17.505  -20.656 -9.599  1.00 79.80  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 16.984  -25.144 -8.469  1.00 99.97  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 38.470  -10.725 -42.307 1.00 69.64  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.251  -11.782 -43.330 1.00 75.49  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 36.757  -12.113 -43.388 1.00 70.15  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.196  -12.584 -42.398 1.00 70.33  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.102  -13.022 -43.018 1.00 81.24  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.109  -14.086 -44.110 1.00 99.89  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.056  -13.690 -45.596 1.00 107.49 ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.717  -13.471 -44.942 1.00 100.76 ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.069  -11.890 -44.539 1.00 61.79  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 34.621  -12.101 -44.619 1.00 61.76  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.305  -13.537 -44.208 1.00 62.22  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.126  -14.440 -44.405 1.00 60.48  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.237  -11.785 -46.078 1.00 60.76  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.422  -10.998 -46.608 1.00 61.65  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 36.645  -11.478 -45.833 1.00 56.75  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.145  -13.718 -43.566 1.00 57.29  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.735  -15.040 -43.113 1.00 62.75  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.363  -15.391 -43.688 1.00 60.93  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 30.684  -14.531 -44.259 1.00 58.90  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 32.881  -15.166 -41.593 1.00 68.29  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.288  -15.381 -41.113 1.00 80.01  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.187  -16.226 -41.733 1.00 79.61  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 34.931  -14.877 -40.039 1.00 70.96  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.329  -16.219 -41.056 1.00 74.02  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.194  -15.405 -40.028 1.00 70.57  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 30.971  -16.671 -43.562 1.00 50.98  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.646  -17.082 -43.997 1.00 50.09  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.654  -16.030 -43.525 1.00 46.28  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.870  -15.512 -44.318 1.00 48.71  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.304  -18.444 -43.438 1.00 53.58  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.733  -15.716 -42.227 1.00 44.18  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.921  -14.676 -41.602 1.00 53.17  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.786  -13.438 -41.362 1.00 48.70  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.918  -13.556 -40.886 1.00 47.81  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.316  -15.112 -40.260 1.00 45.76  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.249  -16.190 -40.373 1.00 42.69  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 24.922  -15.857 -40.606 1.00 39.23  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.577  -17.529 -40.220 1.00 42.04  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.949  -16.836 -40.719 1.00 41.49  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.606  -18.511 -40.340 1.00 39.39  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.294  -18.163 -40.568 1.00 43.19  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.222  -12.262 -41.668 1.00 48.89  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 28.910  -10.994 -41.489 1.00 46.47  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.142  -10.129 -40.482 1.00 50.82  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 26.910  -10.198 -40.405 1.00 42.43  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 28.994  -10.323 -42.861 1.00 48.88  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.665  -10.044 -43.548 1.00 50.38  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 27.884  -9.311  -44.869 1.00 59.17  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 26.625  -8.945  -45.589 1.00 62.92  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 25.840  -10.115 -46.005 1.00 66.04  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.832  -9.233  -39.729 1.00 50.56  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.171  -8.402  -38.717 1.00 42.13  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.040  -7.632  -39.383 1.00 41.83  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.218  -7.133  -40.494 1.00 43.50  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.339  -7.497  -38.297 1.00 47.33  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.564  -8.386  -38.456 1.00 47.13  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.276  -8.947  -39.835 1.00 49.94  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 25.856  -7.624  -38.744 1.00 37.22  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.678  -6.949  -39.265 1.00 35.23  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.684  -7.909  -39.916 1.00 37.24  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.553  -7.528  -40.233 1.00 35.49  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.139  -9.147  -40.176 1.00 38.13  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.265  -10.175 -40.707 1.00 37.62  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.170  -10.466 -39.673 1.00 29.46  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.448  -10.539 -38.482 1.00 33.60  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.038  -11.453 -40.983 1.00 36.81  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.756  -11.568 -42.319 1.00 45.71  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.443  -10.776 -43.224 1.00 39.63  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.623  -12.471 -42.434 1.00 44.87  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 20.930  -10.562 -40.138 1.00 32.09  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.829  -10.801 -39.223 1.00 34.70  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.529  -12.290 -39.218 1.00 34.27  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.523  -12.901 -40.282 1.00 34.04  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.640  -9.993  -39.723 1.00 33.02  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 18.918  -8.494  -39.884 1.00 29.73  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.605  -7.809  -40.233 1.00 31.27  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.500  -8.000  -38.568 1.00 29.94  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.260  -12.838 -38.028 1.00 31.05  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 19.022  -14.274 -37.932 1.00 31.27  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.881  -14.541 -36.956 1.00 34.75  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.468  -13.653 -36.208 1.00 29.33  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.294  -15.037 -37.495 1.00 35.45  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.417  -14.973 -38.541 1.00 37.35  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.795  -14.594 -36.123 1.00 32.51  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.407  -15.800 -36.930 1.00 33.28  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.896  -16.366 -35.693 1.00 29.17  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 17.989  -17.245 -35.103 1.00 32.45  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.617  -18.011 -35.861 1.00 31.81  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.651  -17.214 -35.959 1.00 27.59  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.430  -16.369 -36.272 1.00 33.39  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.115  -16.027 -37.581 1.00 34.24  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.604  -15.914 -35.253 1.00 35.08  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 12.994  -15.254 -37.863 1.00 42.24  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.484  -15.139 -35.538 1.00 37.99  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.176  -14.822 -36.840 1.00 41.18  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.191  -17.131 -33.767 1.00 27.98  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.251  -17.847 -33.076 1.00 28.86  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.639  -18.803 -32.054 1.00 27.91  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.696  -18.451 -31.359 1.00 31.92  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.217  -16.891 -32.402 1.00 28.05  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.196  -20.004 -31.962 1.00 30.16  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.563  -21.053 -31.169 1.00 33.64  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.434  -21.349 -29.954 1.00 36.98  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.633  -21.608 -30.091 1.00 36.95  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.352  -22.354 -31.961 1.00 34.53  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.620  -23.453 -31.158 1.00 29.08  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 16.154  -23.068 -30.964 1.00 35.34  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.248  -24.173 -30.404 1.00 35.49  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.698  -24.434 -29.035 1.00 35.07  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.813  -21.260 -28.771 1.00 41.64  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.444  -21.664 -27.526 1.00 42.84  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.590  -22.768 -26.912 1.00 38.75  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.364  -22.733 -26.999 1.00 34.49  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.497  -20.508 -26.517 1.00 41.17  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.110  -19.243 -27.060 1.00 48.60  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.858  -19.010 -26.693 1.00 53.37  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 21.666  -18.217 -25.089 1.00 53.54  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.251  -23.718 -26.252 1.00 37.91  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.534  -24.745 -25.516 1.00 41.93  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.601  -24.068 -24.507 1.00 38.84  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 18.019  -23.162 -23.791 1.00 43.98  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.552  -25.698 -24.878 1.00 48.09  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 18.935  -26.924 -24.200 1.00 56.58  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 19.966  -27.830 -23.535 1.00 59.15  ? 16  LYS   B CD  1 
ATOM   881  C CE  . LYS   B 1 17 ? 19.453  -29.219 -23.301 1.00 65.46  ? 16  LYS   B CE  1 
ATOM   882  N NZ  . LYS   B 1 17 ? 18.341  -29.273 -22.345 1.00 64.58  ? 16  LYS   B NZ  1 
ATOM   883  N N   . GLY   B 1 18 ? 16.327  -24.481 -24.510 1.00 39.44  ? 17  GLY   B N   1 
ATOM   884  C CA  . GLY   B 1 18 ? 15.305  -23.997 -23.596 1.00 39.76  ? 17  GLY   B CA  1 
ATOM   885  C C   . GLY   B 1 18 ? 14.437  -22.866 -24.155 1.00 42.34  ? 17  GLY   B C   1 
ATOM   886  O O   . GLY   B 1 18 ? 13.551  -22.384 -23.458 1.00 40.88  ? 17  GLY   B O   1 
ATOM   887  N N   . TYR   B 1 19 ? 14.695  -22.404 -25.386 1.00 37.39  ? 18  TYR   B N   1 
ATOM   888  C CA  . TYR   B 1 19 ? 13.977  -21.230 -25.872 1.00 35.76  ? 18  TYR   B CA  1 
ATOM   889  C C   . TYR   B 1 19 ? 13.667  -21.380 -27.359 1.00 33.71  ? 18  TYR   B C   1 
ATOM   890  O O   . TYR   B 1 19 ? 14.345  -22.123 -28.054 1.00 40.34  ? 18  TYR   B O   1 
ATOM   891  C CB  . TYR   B 1 19 ? 14.829  -19.974 -25.690 1.00 33.35  ? 18  TYR   B CB  1 
ATOM   892  C CG  . TYR   B 1 19 ? 15.342  -19.714 -24.284 1.00 43.08  ? 18  TYR   B CG  1 
ATOM   893  C CD1 . TYR   B 1 19 ? 14.622  -18.927 -23.384 1.00 45.39  ? 18  TYR   B CD1 1 
ATOM   894  C CD2 . TYR   B 1 19 ? 16.539  -20.276 -23.851 1.00 42.53  ? 18  TYR   B CD2 1 
ATOM   895  C CE1 . TYR   B 1 19 ? 15.094  -18.698 -22.098 1.00 50.06  ? 18  TYR   B CE1 1 
ATOM   896  C CE2 . TYR   B 1 19 ? 17.010  -20.062 -22.564 1.00 53.21  ? 18  TYR   B CE2 1 
ATOM   897  C CZ  . TYR   B 1 19 ? 16.288  -19.268 -21.686 1.00 50.08  ? 18  TYR   B CZ  1 
ATOM   898  O OH  . TYR   B 1 19 ? 16.786  -19.070 -20.428 1.00 54.21  ? 18  TYR   B OH  1 
ATOM   899  N N   . PRO   B 1 20 ? 12.617  -20.716 -27.889 1.00 32.79  ? 19  PRO   B N   1 
ATOM   900  C CA  . PRO   B 1 20 ? 12.299  -20.798 -29.318 1.00 31.81  ? 19  PRO   B CA  1 
ATOM   901  C C   . PRO   B 1 20 ? 13.385  -20.030 -30.078 1.00 30.11  ? 19  PRO   B C   1 
ATOM   902  O O   . PRO   B 1 20 ? 13.995  -19.138 -29.499 1.00 29.59  ? 19  PRO   B O   1 
ATOM   903  C CB  . PRO   B 1 20 ? 10.937  -20.087 -29.403 1.00 27.38  ? 19  PRO   B CB  1 
ATOM   904  C CG  . PRO   B 1 20 ? 10.976  -19.088 -28.249 1.00 30.63  ? 19  PRO   B CG  1 
ATOM   905  C CD  . PRO   B 1 20 ? 11.684  -19.859 -27.141 1.00 32.15  ? 19  PRO   B CD  1 
ATOM   906  N N   . HIS   B 1 21 ? 13.666  -20.437 -31.322 1.00 30.86  ? 20  HIS   B N   1 
ATOM   907  C CA  . HIS   B 1 21 ? 14.456  -19.624 -32.259 1.00 33.96  ? 20  HIS   B CA  1 
ATOM   908  C C   . HIS   B 1 21 ? 14.158  -18.144 -32.051 1.00 31.12  ? 20  HIS   B C   1 
ATOM   909  O O   . HIS   B 1 21 ? 13.002  -17.725 -32.116 1.00 30.64  ? 20  HIS   B O   1 
ATOM   910  C CB  . HIS   B 1 21 ? 14.127  -20.002 -33.709 1.00 31.71  ? 20  HIS   B CB  1 
ATOM   911  C CG  . HIS   B 1 21 ? 14.340  -21.472 -33.911 1.00 33.18  ? 20  HIS   B CG  1 
ATOM   912  N ND1 . HIS   B 1 21 ? 13.410  -22.411 -33.502 1.00 35.91  ? 20  HIS   B ND1 1 
ATOM   913  C CD2 . HIS   B 1 21 ? 15.390  -22.172 -34.385 1.00 35.29  ? 20  HIS   B CD2 1 
ATOM   914  C CE1 . HIS   B 1 21 ? 13.859  -23.632 -33.796 1.00 36.34  ? 20  HIS   B CE1 1 
ATOM   915  N NE2 . HIS   B 1 21 ? 15.078  -23.520 -34.298 1.00 32.98  ? 20  HIS   B NE2 1 
ATOM   916  N N   . TRP   B 1 22 ? 15.211  -17.354 -31.837 1.00 32.21  ? 21  TRP   B N   1 
ATOM   917  C CA  . TRP   B 1 22 ? 15.008  -16.035 -31.250 1.00 29.37  ? 21  TRP   B CA  1 
ATOM   918  C C   . TRP   B 1 22 ? 15.513  -14.958 -32.211 1.00 31.61  ? 21  TRP   B C   1 
ATOM   919  O O   . TRP   B 1 22 ? 16.627  -15.071 -32.677 1.00 33.20  ? 21  TRP   B O   1 
ATOM   920  C CB  . TRP   B 1 22 ? 15.728  -15.966 -29.901 1.00 28.81  ? 21  TRP   B CB  1 
ATOM   921  C CG  . TRP   B 1 22 ? 15.230  -14.812 -29.062 1.00 32.76  ? 21  TRP   B CG  1 
ATOM   922  C CD1 . TRP   B 1 22 ? 15.573  -13.492 -29.194 1.00 31.11  ? 21  TRP   B CD1 1 
ATOM   923  C CD2 . TRP   B 1 22 ? 14.257  -14.870 -27.989 1.00 33.65  ? 21  TRP   B CD2 1 
ATOM   924  N NE1 . TRP   B 1 22 ? 14.864  -12.722 -28.295 1.00 31.25  ? 21  TRP   B NE1 1 
ATOM   925  C CE2 . TRP   B 1 22 ? 14.056  -13.541 -27.536 1.00 34.42  ? 21  TRP   B CE2 1 
ATOM   926  C CE3 . TRP   B 1 22 ? 13.543  -15.907 -27.370 1.00 33.40  ? 21  TRP   B CE3 1 
ATOM   927  C CZ2 . TRP   B 1 22 ? 13.172  -13.234 -26.496 1.00 33.62  ? 21  TRP   B CZ2 1 
ATOM   928  C CZ3 . TRP   B 1 22 ? 12.681  -15.604 -26.332 1.00 36.75  ? 21  TRP   B CZ3 1 
ATOM   929  C CH2 . TRP   B 1 22 ? 12.479  -14.281 -25.921 1.00 32.28  ? 21  TRP   B CH2 1 
ATOM   930  N N   . PRO   B 1 23 ? 14.727  -13.910 -32.559 1.00 33.27  ? 22  PRO   B N   1 
ATOM   931  C CA  . PRO   B 1 23 ? 15.193  -12.860 -33.474 1.00 30.68  ? 22  PRO   B CA  1 
ATOM   932  C C   . PRO   B 1 23 ? 16.486  -12.265 -32.925 1.00 31.18  ? 22  PRO   B C   1 
ATOM   933  O O   . PRO   B 1 23 ? 16.565  -11.918 -31.752 1.00 30.35  ? 22  PRO   B O   1 
ATOM   934  C CB  . PRO   B 1 23 ? 14.022  -11.856 -33.493 1.00 30.00  ? 22  PRO   B CB  1 
ATOM   935  C CG  . PRO   B 1 23 ? 13.256  -12.162 -32.235 1.00 31.50  ? 22  PRO   B CG  1 
ATOM   936  C CD  . PRO   B 1 23 ? 13.349  -13.676 -32.112 1.00 31.34  ? 22  PRO   B CD  1 
ATOM   937  N N   . ALA   B 1 24 ? 17.523  -12.237 -33.768 1.00 31.52  ? 23  ALA   B N   1 
ATOM   938  C CA  . ALA   B 1 24 ? 18.826  -11.771 -33.358 1.00 28.78  ? 23  ALA   B CA  1 
ATOM   939  C C   . ALA   B 1 24 ? 19.600  -11.205 -34.549 1.00 28.35  ? 23  ALA   B C   1 
ATOM   940  O O   . ALA   B 1 24 ? 19.160  -11.271 -35.704 1.00 28.69  ? 23  ALA   B O   1 
ATOM   941  C CB  . ALA   B 1 24 ? 19.583  -12.895 -32.693 1.00 29.05  ? 23  ALA   B CB  1 
ATOM   942  N N   . ARG   B 1 25 ? 20.815  -10.735 -34.239 1.00 31.72  ? 24  ARG   B N   1 
ATOM   943  C CA  . ARG   B 1 25 ? 21.724  -10.238 -35.258 1.00 34.68  ? 24  ARG   B CA  1 
ATOM   944  C C   . ARG   B 1 25 ? 23.124  -10.701 -34.899 1.00 33.70  ? 24  ARG   B C   1 
ATOM   945  O O   . ARG   B 1 25 ? 23.375  -11.030 -33.745 1.00 34.49  ? 24  ARG   B O   1 
ATOM   946  C CB  . ARG   B 1 25 ? 21.724  -8.715  -35.361 1.00 33.15  ? 24  ARG   B CB  1 
ATOM   947  C CG  . ARG   B 1 25 ? 22.483  -8.002  -34.255 1.00 33.70  ? 24  ARG   B CG  1 
ATOM   948  C CD  . ARG   B 1 25 ? 22.171  -6.502  -34.369 1.00 34.65  ? 24  ARG   B CD  1 
ATOM   949  N NE  . ARG   B 1 25 ? 22.793  -5.749  -33.280 1.00 35.12  ? 24  ARG   B NE  1 
ATOM   950  C CZ  . ARG   B 1 25 ? 22.479  -4.509  -32.876 1.00 35.70  ? 24  ARG   B CZ  1 
ATOM   951  N NH1 . ARG   B 1 25 ? 21.482  -3.838  -33.445 1.00 32.75  ? 24  ARG   B NH1 1 
ATOM   952  N NH2 . ARG   B 1 25 ? 23.201  -3.961  -31.920 1.00 32.95  ? 24  ARG   B NH2 1 
ATOM   953  N N   . ILE   B 1 26 ? 23.991  -10.778 -35.924 1.00 35.43  ? 25  ILE   B N   1 
ATOM   954  C CA  . ILE   B 1 26 ? 25.421  -10.957 -35.732 1.00 35.26  ? 25  ILE   B CA  1 
ATOM   955  C C   . ILE   B 1 26 ? 25.970  -9.573  -35.406 1.00 39.70  ? 25  ILE   B C   1 
ATOM   956  O O   . ILE   B 1 26 ? 25.760  -8.644  -36.186 1.00 37.00  ? 25  ILE   B O   1 
ATOM   957  C CB  . ILE   B 1 26 ? 26.086  -11.477 -37.027 1.00 39.10  ? 25  ILE   B CB  1 
ATOM   958  C CG1 . ILE   B 1 26 ? 25.363  -12.692 -37.607 1.00 40.50  ? 25  ILE   B CG1 1 
ATOM   959  C CG2 . ILE   B 1 26 ? 27.594  -11.712 -36.854 1.00 40.65  ? 25  ILE   B CG2 1 
ATOM   960  C CD1 . ILE   B 1 26 ? 25.291  -13.888 -36.676 1.00 36.72  ? 25  ILE   B CD1 1 
ATOM   961  N N   . ASP   B 1 27 ? 26.713  -9.490  -34.307 1.00 37.12  ? 26  ASP   B N   1 
ATOM   962  C CA  . ASP   B 1 27 ? 27.428  -8.285  -33.908 1.00 50.30  ? 26  ASP   B CA  1 
ATOM   963  C C   . ASP   B 1 27 ? 28.908  -8.307  -34.322 1.00 53.95  ? 26  ASP   B C   1 
ATOM   964  O O   . ASP   B 1 27 ? 29.484  -9.377  -34.530 1.00 50.14  ? 26  ASP   B O   1 
ATOM   965  C CB  . ASP   B 1 27 ? 27.364  -8.152  -32.398 1.00 45.20  ? 26  ASP   B CB  1 
ATOM   966  C CG  . ASP   B 1 27 ? 26.183  -7.355  -31.870 1.00 47.63  ? 26  ASP   B CG  1 
ATOM   967  O OD1 . ASP   B 1 27 ? 25.420  -6.790  -32.703 1.00 44.16  ? 26  ASP   B OD1 1 
ATOM   968  O OD2 . ASP   B 1 27 ? 26.078  -7.270  -30.628 1.00 43.14  ? 26  ASP   B OD2 1 
ATOM   969  N N   A ASP   B 1 28 ? 29.503  -7.105  -34.381 0.50 56.27  ? 27  ASP   B N   1 
ATOM   970  N N   B ASP   B 1 28 ? 29.516  -7.112  -34.430 0.50 55.12  ? 27  ASP   B N   1 
ATOM   971  C CA  A ASP   B 1 28 ? 30.937  -6.881  -34.513 0.50 60.29  ? 27  ASP   B CA  1 
ATOM   972  C CA  B ASP   B 1 28 ? 30.962  -6.948  -34.562 0.50 58.48  ? 27  ASP   B CA  1 
ATOM   973  C C   A ASP   B 1 28 ? 31.632  -7.386  -33.248 0.50 62.41  ? 27  ASP   B C   1 
ATOM   974  C C   B ASP   B 1 28 ? 31.644  -7.271  -33.233 0.50 60.81  ? 27  ASP   B C   1 
ATOM   975  O O   A ASP   B 1 28 ? 30.965  -7.705  -32.268 0.50 68.27  ? 27  ASP   B O   1 
ATOM   976  O O   B ASP   B 1 28 ? 30.985  -7.336  -32.198 0.50 66.74  ? 27  ASP   B O   1 
ATOM   977  C CB  A ASP   B 1 28 ? 31.214  -5.398  -34.721 0.50 56.00  ? 27  ASP   B CB  1 
ATOM   978  C CB  B ASP   B 1 28 ? 31.339  -5.560  -35.065 0.50 53.46  ? 27  ASP   B CB  1 
ATOM   979  C CG  A ASP   B 1 28 ? 30.102  -4.622  -35.413 0.50 52.99  ? 27  ASP   B CG  1 
ATOM   980  C CG  B ASP   B 1 28 ? 31.763  -5.470  -36.524 0.50 51.57  ? 27  ASP   B CG  1 
ATOM   981  O OD1 A ASP   B 1 28 ? 30.383  -3.979  -36.442 0.50 54.47  ? 27  ASP   B OD1 1 
ATOM   982  O OD1 B ASP   B 1 28 ? 32.789  -6.085  -36.878 0.50 48.79  ? 27  ASP   B OD1 1 
ATOM   983  O OD2 A ASP   B 1 28 ? 28.953  -4.669  -34.921 0.50 53.00  ? 27  ASP   B OD2 1 
ATOM   984  O OD2 B ASP   B 1 28 ? 31.077  -4.771  -37.296 0.50 53.75  ? 27  ASP   B OD2 1 
ATOM   985  N N   . ILE   B 1 29 ? 32.971  -7.457  -33.269 1.00 70.65  ? 28  ILE   B N   1 
ATOM   986  C CA  . ILE   B 1 29 ? 33.728  -7.967  -32.127 1.00 74.03  ? 28  ILE   B CA  1 
ATOM   987  C C   . ILE   B 1 29 ? 34.024  -6.838  -31.119 1.00 82.31  ? 28  ILE   B C   1 
ATOM   988  O O   . ILE   B 1 29 ? 34.569  -5.790  -31.543 1.00 86.08  ? 28  ILE   B O   1 
ATOM   989  C CB  . ILE   B 1 29 ? 35.005  -8.705  -32.569 1.00 69.35  ? 28  ILE   B CB  1 
ATOM   990  N N   . VAL   B 1 34 ? 36.674  -10.004 -24.773 1.00 82.41  ? 33  VAL   B N   1 
ATOM   991  C CA  . VAL   B 1 34 ? 36.525  -11.413 -25.243 1.00 76.25  ? 33  VAL   B CA  1 
ATOM   992  C C   . VAL   B 1 34 ? 36.382  -11.382 -26.761 1.00 83.35  ? 33  VAL   B C   1 
ATOM   993  O O   . VAL   B 1 34 ? 35.790  -10.451 -27.304 1.00 96.98  ? 33  VAL   B O   1 
ATOM   994  C CB  . VAL   B 1 34 ? 35.275  -11.999 -24.554 1.00 76.35  ? 33  VAL   B CB  1 
ATOM   995  C CG1 . VAL   B 1 34 ? 34.001  -11.249 -24.934 1.00 77.24  ? 33  VAL   B CG1 1 
ATOM   996  C CG2 . VAL   B 1 34 ? 35.115  -13.502 -24.773 1.00 66.16  ? 33  VAL   B CG2 1 
ATOM   997  N N   . LYS   B 1 35 ? 36.971  -12.377 -27.436 1.00 84.12  ? 34  LYS   B N   1 
ATOM   998  C CA  . LYS   B 1 35 ? 36.644  -12.685 -28.822 1.00 76.13  ? 34  LYS   B CA  1 
ATOM   999  C C   . LYS   B 1 35 ? 35.887  -14.016 -28.837 1.00 80.01  ? 34  LYS   B C   1 
ATOM   1000 O O   . LYS   B 1 35 ? 36.079  -14.837 -27.937 1.00 81.50  ? 34  LYS   B O   1 
ATOM   1001 C CB  . LYS   B 1 35 ? 37.914  -12.699 -29.682 1.00 71.22  ? 34  LYS   B CB  1 
ATOM   1002 N N   . PRO   B 1 36 ? 34.992  -14.285 -29.824 1.00 73.14  ? 35  PRO   B N   1 
ATOM   1003 C CA  . PRO   B 1 36 ? 34.257  -15.557 -29.860 1.00 62.97  ? 35  PRO   B CA  1 
ATOM   1004 C C   . PRO   B 1 36 ? 35.171  -16.780 -29.830 1.00 56.55  ? 35  PRO   B C   1 
ATOM   1005 O O   . PRO   B 1 36 ? 36.295  -16.730 -30.317 1.00 64.77  ? 35  PRO   B O   1 
ATOM   1006 C CB  . PRO   B 1 36 ? 33.444  -15.467 -31.165 1.00 60.07  ? 35  PRO   B CB  1 
ATOM   1007 C CG  . PRO   B 1 36 ? 34.164  -14.407 -31.985 1.00 65.40  ? 35  PRO   B CG  1 
ATOM   1008 C CD  . PRO   B 1 36 ? 34.647  -13.399 -30.952 1.00 68.03  ? 35  PRO   B CD  1 
ATOM   1009 N N   . PRO   B 1 37 ? 34.749  -17.914 -29.232 1.00 55.50  ? 36  PRO   B N   1 
ATOM   1010 C CA  . PRO   B 1 37 ? 35.491  -19.161 -29.392 1.00 59.84  ? 36  PRO   B CA  1 
ATOM   1011 C C   . PRO   B 1 37 ? 35.620  -19.430 -30.893 1.00 70.53  ? 36  PRO   B C   1 
ATOM   1012 O O   . PRO   B 1 37 ? 34.896  -18.836 -31.697 1.00 69.01  ? 36  PRO   B O   1 
ATOM   1013 C CB  . PRO   B 1 37 ? 34.617  -20.216 -28.676 1.00 62.56  ? 36  PRO   B CB  1 
ATOM   1014 C CG  . PRO   B 1 37 ? 33.715  -19.423 -27.743 1.00 56.99  ? 36  PRO   B CG  1 
ATOM   1015 C CD  . PRO   B 1 37 ? 33.561  -18.044 -28.371 1.00 57.96  ? 36  PRO   B CD  1 
ATOM   1016 N N   . PRO   B 1 38 ? 36.534  -20.328 -31.335 1.00 75.76  ? 37  PRO   B N   1 
ATOM   1017 C CA  . PRO   B 1 38 ? 36.624  -20.679 -32.761 1.00 73.69  ? 37  PRO   B CA  1 
ATOM   1018 C C   . PRO   B 1 38 ? 35.304  -21.240 -33.306 1.00 65.53  ? 37  PRO   B C   1 
ATOM   1019 O O   . PRO   B 1 38 ? 34.625  -21.999 -32.616 1.00 65.12  ? 37  PRO   B O   1 
ATOM   1020 C CB  . PRO   B 1 38 ? 37.775  -21.710 -32.839 1.00 74.73  ? 37  PRO   B CB  1 
ATOM   1021 C CG  . PRO   B 1 38 ? 38.467  -21.658 -31.484 1.00 70.64  ? 37  PRO   B CG  1 
ATOM   1022 C CD  . PRO   B 1 38 ? 37.495  -21.055 -30.486 1.00 74.94  ? 37  PRO   B CD  1 
ATOM   1023 N N   . ASN   B 1 39 ? 34.929  -20.841 -34.533 1.00 61.33  ? 38  ASN   B N   1 
ATOM   1024 C CA  . ASN   B 1 39 ? 33.725  -21.331 -35.208 1.00 67.13  ? 38  ASN   B CA  1 
ATOM   1025 C C   . ASN   B 1 39 ? 32.446  -20.612 -34.764 1.00 58.48  ? 38  ASN   B C   1 
ATOM   1026 O O   . ASN   B 1 39 ? 31.385  -20.849 -35.332 1.00 56.17  ? 38  ASN   B O   1 
ATOM   1027 C CB  . ASN   B 1 39 ? 33.450  -22.815 -34.963 1.00 61.61  ? 38  ASN   B CB  1 
ATOM   1028 C CG  . ASN   B 1 39 ? 34.632  -23.695 -35.288 1.00 76.71  ? 38  ASN   B CG  1 
ATOM   1029 O OD1 . ASN   B 1 39 ? 34.842  -24.716 -34.621 1.00 81.11  ? 38  ASN   B OD1 1 
ATOM   1030 N ND2 . ASN   B 1 39 ? 35.398  -23.332 -36.309 1.00 73.24  ? 38  ASN   B ND2 1 
ATOM   1031 N N   . LYS   B 1 40 ? 32.527  -19.768 -33.727 1.00 58.38  ? 39  LYS   B N   1 
ATOM   1032 C CA  . LYS   B 1 40 ? 31.343  -19.174 -33.135 1.00 50.44  ? 39  LYS   B CA  1 
ATOM   1033 C C   . LYS   B 1 40 ? 31.286  -17.681 -33.449 1.00 47.98  ? 39  LYS   B C   1 
ATOM   1034 O O   . LYS   B 1 40 ? 32.285  -17.089 -33.835 1.00 50.88  ? 39  LYS   B O   1 
ATOM   1035 C CB  . LYS   B 1 40 ? 31.388  -19.550 -31.656 1.00 47.68  ? 39  LYS   B CB  1 
ATOM   1036 C CG  . LYS   B 1 40 ? 30.941  -20.975 -31.347 1.00 51.41  ? 39  LYS   B CG  1 
ATOM   1037 C CD  . LYS   B 1 40 ? 31.149  -21.285 -29.868 1.00 62.32  ? 39  LYS   B CD  1 
ATOM   1038 C CE  . LYS   B 1 40 ? 30.035  -21.975 -29.119 1.00 68.93  ? 39  LYS   B CE  1 
ATOM   1039 N NZ  . LYS   B 1 40 ? 29.739  -23.336 -29.571 1.00 69.73  ? 39  LYS   B NZ  1 
ATOM   1040 N N   . TYR   B 1 41 ? 30.100  -17.086 -33.297 1.00 49.95  ? 40  TYR   B N   1 
ATOM   1041 C CA  . TYR   B 1 41 ? 29.893  -15.682 -33.624 1.00 46.34  ? 40  TYR   B CA  1 
ATOM   1042 C C   . TYR   B 1 41 ? 29.283  -14.930 -32.439 1.00 44.37  ? 40  TYR   B C   1 
ATOM   1043 O O   . TYR   B 1 41 ? 28.499  -15.500 -31.679 1.00 43.16  ? 40  TYR   B O   1 
ATOM   1044 C CB  . TYR   B 1 41 ? 28.905  -15.558 -34.786 1.00 45.54  ? 40  TYR   B CB  1 
ATOM   1045 C CG  . TYR   B 1 41 ? 29.377  -15.981 -36.169 1.00 43.98  ? 40  TYR   B CG  1 
ATOM   1046 C CD1 . TYR   B 1 41 ? 30.042  -15.092 -37.007 1.00 42.34  ? 40  TYR   B CD1 1 
ATOM   1047 C CD2 . TYR   B 1 41 ? 29.105  -17.252 -36.656 1.00 45.87  ? 40  TYR   B CD2 1 
ATOM   1048 C CE1 . TYR   B 1 41 ? 30.457  -15.465 -38.278 1.00 48.14  ? 40  TYR   B CE1 1 
ATOM   1049 C CE2 . TYR   B 1 41 ? 29.513  -17.637 -37.925 1.00 49.95  ? 40  TYR   B CE2 1 
ATOM   1050 C CZ  . TYR   B 1 41 ? 30.205  -16.747 -38.735 1.00 50.53  ? 40  TYR   B CZ  1 
ATOM   1051 O OH  . TYR   B 1 41 ? 30.603  -17.125 -39.991 1.00 47.32  ? 40  TYR   B OH  1 
ATOM   1052 N N   . PRO   B 1 42 ? 29.563  -13.606 -32.289 1.00 46.56  ? 41  PRO   B N   1 
ATOM   1053 C CA  . PRO   B 1 42 ? 28.861  -12.777 -31.312 1.00 37.10  ? 41  PRO   B CA  1 
ATOM   1054 C C   . PRO   B 1 42 ? 27.413  -12.582 -31.737 1.00 36.62  ? 41  PRO   B C   1 
ATOM   1055 O O   . PRO   B 1 42 ? 27.156  -11.942 -32.768 1.00 39.08  ? 41  PRO   B O   1 
ATOM   1056 C CB  . PRO   B 1 42 ? 29.629  -11.411 -31.276 1.00 42.84  ? 41  PRO   B CB  1 
ATOM   1057 C CG  . PRO   B 1 42 ? 30.688  -11.484 -32.381 1.00 42.96  ? 41  PRO   B CG  1 
ATOM   1058 C CD  . PRO   B 1 42 ? 30.551  -12.836 -33.073 1.00 44.09  ? 41  PRO   B CD  1 
ATOM   1059 N N   . ILE   B 1 43 ? 26.475  -13.115 -30.925 1.00 32.50  ? 42  ILE   B N   1 
ATOM   1060 C CA  . ILE   B 1 43 ? 25.051  -12.906 -31.181 1.00 35.59  ? 42  ILE   B CA  1 
ATOM   1061 C C   . ILE   B 1 43 ? 24.439  -11.849 -30.256 1.00 34.65  ? 42  ILE   B C   1 
ATOM   1062 O O   . ILE   B 1 43 ? 24.637  -11.893 -29.054 1.00 36.34  ? 42  ILE   B O   1 
ATOM   1063 C CB  . ILE   B 1 43 ? 24.281  -14.235 -31.084 1.00 32.43  ? 42  ILE   B CB  1 
ATOM   1064 C CG1 . ILE   B 1 43 ? 25.045  -15.344 -31.838 1.00 32.56  ? 42  ILE   B CG1 1 
ATOM   1065 C CG2 . ILE   B 1 43 ? 22.848  -14.072 -31.593 1.00 34.09  ? 42  ILE   B CG2 1 
ATOM   1066 C CD1 . ILE   B 1 43 ? 25.292  -15.033 -33.300 1.00 34.62  ? 42  ILE   B CD1 1 
ATOM   1067 N N   . PHE   B 1 44 ? 23.599  -10.970 -30.826 1.00 33.78  ? 43  PHE   B N   1 
ATOM   1068 C CA  . PHE   B 1 44 ? 22.800  -10.044 -30.042 1.00 37.93  ? 43  PHE   B CA  1 
ATOM   1069 C C   . PHE   B 1 44 ? 21.326  -10.405 -30.200 1.00 32.52  ? 43  PHE   B C   1 
ATOM   1070 O O   . PHE   B 1 44 ? 20.798  -10.414 -31.310 1.00 32.43  ? 43  PHE   B O   1 
ATOM   1071 C CB  . PHE   B 1 44 ? 23.072  -8.591  -30.456 1.00 33.08  ? 43  PHE   B CB  1 
ATOM   1072 C CG  . PHE   B 1 44 ? 22.148  -7.575  -29.801 1.00 35.21  ? 43  PHE   B CG  1 
ATOM   1073 C CD1 . PHE   B 1 44 ? 20.930  -7.219  -30.392 1.00 36.59  ? 43  PHE   B CD1 1 
ATOM   1074 C CD2 . PHE   B 1 44 ? 22.501  -6.966  -28.598 1.00 41.03  ? 43  PHE   B CD2 1 
ATOM   1075 C CE1 . PHE   B 1 44 ? 20.104  -6.265  -29.807 1.00 38.42  ? 43  PHE   B CE1 1 
ATOM   1076 C CE2 . PHE   B 1 44 ? 21.666  -6.005  -28.012 1.00 37.86  ? 43  PHE   B CE2 1 
ATOM   1077 C CZ  . PHE   B 1 44 ? 20.473  -5.667  -28.611 1.00 39.16  ? 43  PHE   B CZ  1 
ATOM   1078 N N   . PHE   B 1 45 ? 20.661  -10.703 -29.074 1.00 34.34  ? 44  PHE   B N   1 
ATOM   1079 C CA  . PHE   B 1 45 ? 19.251  -11.060 -29.089 1.00 30.35  ? 44  PHE   B CA  1 
ATOM   1080 C C   . PHE   B 1 45 ? 18.388  -9.823  -28.935 1.00 30.88  ? 44  PHE   B C   1 
ATOM   1081 O O   . PHE   B 1 45 ? 18.443  -9.127  -27.913 1.00 32.47  ? 44  PHE   B O   1 
ATOM   1082 C CB  . PHE   B 1 45 ? 18.945  -12.069 -27.971 1.00 32.97  ? 44  PHE   B CB  1 
ATOM   1083 C CG  . PHE   B 1 45 ? 19.682  -13.387 -28.163 1.00 33.85  ? 44  PHE   B CG  1 
ATOM   1084 C CD1 . PHE   B 1 45 ? 21.020  -13.506 -27.801 1.00 33.31  ? 44  PHE   B CD1 1 
ATOM   1085 C CD2 . PHE   B 1 45 ? 19.054  -14.494 -28.726 1.00 32.62  ? 44  PHE   B CD2 1 
ATOM   1086 C CE1 . PHE   B 1 45 ? 21.710  -14.692 -27.986 1.00 41.29  ? 44  PHE   B CE1 1 
ATOM   1087 C CE2 . PHE   B 1 45 ? 19.758  -15.684 -28.911 1.00 34.38  ? 44  PHE   B CE2 1 
ATOM   1088 C CZ  . PHE   B 1 45 ? 21.079  -15.778 -28.549 1.00 31.94  ? 44  PHE   B CZ  1 
ATOM   1089 N N   . PHE   B 1 46 ? 17.544  -9.576  -29.937 1.00 31.61  ? 45  PHE   B N   1 
ATOM   1090 C CA  . PHE   B 1 46 ? 16.592  -8.483  -29.835 1.00 32.59  ? 45  PHE   B CA  1 
ATOM   1091 C C   . PHE   B 1 46 ? 15.565  -8.737  -28.721 1.00 38.00  ? 45  PHE   B C   1 
ATOM   1092 O O   . PHE   B 1 46 ? 15.267  -9.882  -28.362 1.00 32.53  ? 45  PHE   B O   1 
ATOM   1093 C CB  . PHE   B 1 46 ? 15.881  -8.344  -31.172 1.00 30.41  ? 45  PHE   B CB  1 
ATOM   1094 C CG  . PHE   B 1 46 ? 16.793  -7.872  -32.300 1.00 35.85  ? 45  PHE   B CG  1 
ATOM   1095 C CD1 . PHE   B 1 46 ? 17.237  -6.550  -32.377 1.00 40.18  ? 45  PHE   B CD1 1 
ATOM   1096 C CD2 . PHE   B 1 46 ? 17.167  -8.747  -33.321 1.00 34.85  ? 45  PHE   B CD2 1 
ATOM   1097 C CE1 . PHE   B 1 46 ? 18.051  -6.138  -33.432 1.00 35.73  ? 45  PHE   B CE1 1 
ATOM   1098 C CE2 . PHE   B 1 46 ? 17.965  -8.321  -34.379 1.00 38.45  ? 45  PHE   B CE2 1 
ATOM   1099 C CZ  . PHE   B 1 46 ? 18.391  -7.012  -34.437 1.00 35.91  ? 45  PHE   B CZ  1 
ATOM   1100 N N   . GLY   B 1 47 ? 15.013  -7.639  -28.187 1.00 39.27  ? 46  GLY   B N   1 
ATOM   1101 C CA  . GLY   B 1 47 ? 14.014  -7.732  -27.136 1.00 39.54  ? 46  GLY   B CA  1 
ATOM   1102 C C   . GLY   B 1 47 ? 14.702  -7.815  -25.781 1.00 37.23  ? 46  GLY   B C   1 
ATOM   1103 O O   . GLY   B 1 47 ? 14.575  -6.907  -24.968 1.00 37.85  ? 46  GLY   B O   1 
ATOM   1104 N N   . THR   B 1 48 ? 15.472  -8.878  -25.557 1.00 37.27  ? 47  THR   B N   1 
ATOM   1105 C CA  . THR   B 1 48 ? 16.157  -9.038  -24.292 1.00 38.77  ? 47  THR   B CA  1 
ATOM   1106 C C   . THR   B 1 48 ? 17.438  -8.207  -24.290 1.00 41.76  ? 47  THR   B C   1 
ATOM   1107 O O   . THR   B 1 48 ? 17.945  -7.866  -23.227 1.00 42.05  ? 47  THR   B O   1 
ATOM   1108 C CB  . THR   B 1 48 ? 16.422  -10.509 -23.955 1.00 38.03  ? 47  THR   B CB  1 
ATOM   1109 O OG1 . THR   B 1 48 ? 17.384  -11.003 -24.879 1.00 34.14  ? 47  THR   B OG1 1 
ATOM   1110 C CG2 . THR   B 1 48 ? 15.173  -11.372 -24.009 1.00 38.80  ? 47  THR   B CG2 1 
ATOM   1111 N N   . HIS   B 1 49 ? 17.986  -7.938  -25.478 1.00 35.90  ? 48  HIS   B N   1 
ATOM   1112 C CA  . HIS   B 1 49 ? 19.243  -7.211  -25.622 1.00 43.54  ? 48  HIS   B CA  1 
ATOM   1113 C C   . HIS   B 1 49 ? 20.389  -7.914  -24.907 1.00 40.72  ? 48  HIS   B C   1 
ATOM   1114 O O   . HIS   B 1 49 ? 21.301  -7.230  -24.455 1.00 46.37  ? 48  HIS   B O   1 
ATOM   1115 C CB  . HIS   B 1 49 ? 19.131  -5.739  -25.175 1.00 39.22  ? 48  HIS   B CB  1 
ATOM   1116 C CG  . HIS   B 1 49 ? 17.930  -5.073  -25.745 1.00 40.33  ? 48  HIS   B CG  1 
ATOM   1117 N ND1 . HIS   B 1 49 ? 17.112  -4.260  -24.992 1.00 45.53  ? 48  HIS   B ND1 1 
ATOM   1118 C CD2 . HIS   B 1 49 ? 17.356  -5.156  -26.960 1.00 40.62  ? 48  HIS   B CD2 1 
ATOM   1119 C CE1 . HIS   B 1 49 ? 16.092  -3.855  -25.740 1.00 49.50  ? 48  HIS   B CE1 1 
ATOM   1120 N NE2 . HIS   B 1 49 ? 16.220  -4.388  -26.943 1.00 46.40  ? 48  HIS   B NE2 1 
ATOM   1121 N N   . GLU   B 1 50 ? 20.346  -9.251  -24.803 1.00 40.08  ? 49  GLU   B N   1 
ATOM   1122 C CA  . GLU   B 1 50 ? 21.449  -10.022 -24.236 1.00 42.70  ? 49  GLU   B CA  1 
ATOM   1123 C C   . GLU   B 1 50 ? 22.328  -10.527 -25.380 1.00 40.55  ? 49  GLU   B C   1 
ATOM   1124 O O   . GLU   B 1 50 ? 21.961  -10.386 -26.544 1.00 39.01  ? 49  GLU   B O   1 
ATOM   1125 C CB  . GLU   B 1 50 ? 21.002  -11.283 -23.503 1.00 47.55  ? 49  GLU   B CB  1 
ATOM   1126 C CG  . GLU   B 1 50 ? 20.017  -11.050 -22.358 1.00 53.06  ? 49  GLU   B CG  1 
ATOM   1127 C CD  . GLU   B 1 50 ? 19.926  -12.245 -21.407 1.00 65.76  ? 49  GLU   B CD  1 
ATOM   1128 O OE1 . GLU   B 1 50 ? 18.881  -12.930 -21.303 1.00 60.01  ? 49  GLU   B OE1 1 
ATOM   1129 O OE2 . GLU   B 1 50 ? 20.949  -12.503 -20.743 1.00 79.44  ? 49  GLU   B OE2 1 
ATOM   1130 N N   . THR   B 1 51 ? 23.487  -11.096 -25.043 1.00 37.45  ? 50  THR   B N   1 
ATOM   1131 C CA  . THR   B 1 51 ? 24.419  -11.594 -26.043 1.00 39.93  ? 50  THR   B CA  1 
ATOM   1132 C C   . THR   B 1 51 ? 24.818  -13.018 -25.669 1.00 46.95  ? 50  THR   B C   1 
ATOM   1133 O O   . THR   B 1 51 ? 24.725  -13.405 -24.508 1.00 46.31  ? 50  THR   B O   1 
ATOM   1134 C CB  . THR   B 1 51 ? 25.641  -10.681 -26.218 1.00 43.38  ? 50  THR   B CB  1 
ATOM   1135 O OG1 . THR   B 1 51 ? 26.327  -10.676 -24.973 1.00 48.33  ? 50  THR   B OG1 1 
ATOM   1136 C CG2 . THR   B 1 51 ? 25.305  -9.248  -26.600 1.00 41.51  ? 50  THR   B CG2 1 
ATOM   1137 N N   . ALA   B 1 52 ? 25.239  -13.795 -26.676 1.00 46.00  ? 51  ALA   B N   1 
ATOM   1138 C CA  . ALA   B 1 52 ? 25.855  -15.094 -26.459 1.00 45.60  ? 51  ALA   B CA  1 
ATOM   1139 C C   . ALA   B 1 52 ? 26.738  -15.412 -27.661 1.00 44.68  ? 51  ALA   B C   1 
ATOM   1140 O O   . ALA   B 1 52 ? 26.651  -14.730 -28.682 1.00 44.22  ? 51  ALA   B O   1 
ATOM   1141 C CB  . ALA   B 1 52 ? 24.808  -16.155 -26.225 1.00 40.31  ? 51  ALA   B CB  1 
ATOM   1142 N N   . PHE   B 1 53 ? 27.598  -16.429 -27.522 1.00 42.78  ? 52  PHE   B N   1 
ATOM   1143 C CA  . PHE   B 1 53 ? 28.342  -16.941 -28.666 1.00 47.76  ? 52  PHE   B CA  1 
ATOM   1144 C C   . PHE   B 1 53 ? 27.653  -18.217 -29.164 1.00 48.09  ? 52  PHE   B C   1 
ATOM   1145 O O   . PHE   B 1 53 ? 27.438  -19.150 -28.381 1.00 45.10  ? 52  PHE   B O   1 
ATOM   1146 C CB  . PHE   B 1 53 ? 29.838  -17.182 -28.400 1.00 45.41  ? 52  PHE   B CB  1 
ATOM   1147 C CG  . PHE   B 1 53 ? 30.623  -15.978 -27.886 1.00 46.43  ? 52  PHE   B CG  1 
ATOM   1148 C CD1 . PHE   B 1 53 ? 30.931  -14.915 -28.729 1.00 49.05  ? 52  PHE   B CD1 1 
ATOM   1149 C CD2 . PHE   B 1 53 ? 31.038  -15.908 -26.559 1.00 52.24  ? 52  PHE   B CD2 1 
ATOM   1150 C CE1 . PHE   B 1 53 ? 31.632  -13.811 -28.263 1.00 51.11  ? 52  PHE   B CE1 1 
ATOM   1151 C CE2 . PHE   B 1 53 ? 31.735  -14.801 -26.089 1.00 52.46  ? 52  PHE   B CE2 1 
ATOM   1152 C CZ  . PHE   B 1 53 ? 32.033  -13.757 -26.942 1.00 51.78  ? 52  PHE   B CZ  1 
ATOM   1153 N N   . LEU   B 1 54 ? 27.327  -18.237 -30.469 1.00 44.97  ? 53  LEU   B N   1 
ATOM   1154 C CA  . LEU   B 1 54 ? 26.742  -19.388 -31.154 1.00 42.49  ? 53  LEU   B CA  1 
ATOM   1155 C C   . LEU   B 1 54 ? 27.488  -19.676 -32.459 1.00 41.62  ? 53  LEU   B C   1 
ATOM   1156 O O   . LEU   B 1 54 ? 28.007  -18.765 -33.127 1.00 40.17  ? 53  LEU   B O   1 
ATOM   1157 C CB  . LEU   B 1 54 ? 25.257  -19.185 -31.462 1.00 39.21  ? 53  LEU   B CB  1 
ATOM   1158 C CG  . LEU   B 1 54 ? 24.291  -19.071 -30.284 1.00 40.66  ? 53  LEU   B CG  1 
ATOM   1159 C CD1 . LEU   B 1 54 ? 22.981  -18.652 -30.915 1.00 35.85  ? 53  LEU   B CD1 1 
ATOM   1160 C CD2 . LEU   B 1 54 ? 24.157  -20.427 -29.575 1.00 38.63  ? 53  LEU   B CD2 1 
ATOM   1161 N N   . GLY   B 1 55 ? 27.456  -20.962 -32.836 1.00 43.09  ? 54  GLY   B N   1 
ATOM   1162 C CA  . GLY   B 1 55 ? 27.976  -21.462 -34.095 1.00 39.34  ? 54  GLY   B CA  1 
ATOM   1163 C C   . GLY   B 1 55 ? 26.853  -21.531 -35.130 1.00 39.26  ? 54  GLY   B C   1 
ATOM   1164 O O   . GLY   B 1 55 ? 25.673  -21.475 -34.785 1.00 38.54  ? 54  GLY   B O   1 
ATOM   1165 N N   . PRO   B 1 56 ? 27.185  -21.654 -36.431 1.00 37.72  ? 55  PRO   B N   1 
ATOM   1166 C CA  . PRO   B 1 56 ? 26.173  -21.719 -37.492 1.00 36.78  ? 55  PRO   B CA  1 
ATOM   1167 C C   . PRO   B 1 56 ? 25.009  -22.707 -37.389 1.00 33.61  ? 55  PRO   B C   1 
ATOM   1168 O O   . PRO   B 1 56 ? 23.941  -22.447 -37.939 1.00 35.71  ? 55  PRO   B O   1 
ATOM   1169 C CB  . PRO   B 1 56 ? 27.006  -21.951 -38.740 1.00 37.01  ? 55  PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 1 56 ? 28.336  -22.433 -38.219 1.00 39.35  ? 55  PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 1 56 ? 28.568  -21.719 -36.930 1.00 37.71  ? 55  PRO   B CD  1 
ATOM   1172 N N   . LYS   B 1 57 ? 25.191  -23.819 -36.664 1.00 35.28  ? 56  LYS   B N   1 
ATOM   1173 C CA  . LYS   B 1 57 ? 24.142  -24.831 -36.602 1.00 36.35  ? 56  LYS   B CA  1 
ATOM   1174 C C   . LYS   B 1 57 ? 22.914  -24.227 -35.919 1.00 35.66  ? 56  LYS   B C   1 
ATOM   1175 O O   . LYS   B 1 57 ? 21.800  -24.718 -36.074 1.00 34.60  ? 56  LYS   B O   1 
ATOM   1176 C CB  . LYS   B 1 57 ? 24.576  -26.098 -35.853 1.00 38.38  ? 56  LYS   B CB  1 
ATOM   1177 C CG  . LYS   B 1 57 ? 24.571  -25.973 -34.340 1.00 39.34  ? 56  LYS   B CG  1 
ATOM   1178 C CD  . LYS   B 1 57 ? 24.780  -27.337 -33.695 1.00 45.39  ? 56  LYS   B CD  1 
ATOM   1179 C CE  . LYS   B 1 57 ? 25.165  -27.264 -32.237 1.00 45.87  ? 56  LYS   B CE  1 
ATOM   1180 N NZ  . LYS   B 1 57 ? 24.102  -26.719 -31.389 1.00 49.08  ? 56  LYS   B NZ  1 
ATOM   1181 N N   . ASP   B 1 58 ? 23.150  -23.138 -35.180 1.00 34.03  ? 57  ASP   B N   1 
ATOM   1182 C CA  . ASP   B 1 58 ? 22.134  -22.540 -34.336 1.00 36.13  ? 57  ASP   B CA  1 
ATOM   1183 C C   . ASP   B 1 58 ? 21.689  -21.198 -34.914 1.00 35.11  ? 57  ASP   B C   1 
ATOM   1184 O O   . ASP   B 1 58 ? 20.921  -20.482 -34.255 1.00 35.59  ? 57  ASP   B O   1 
ATOM   1185 C CB  . ASP   B 1 58 ? 22.584  -22.506 -32.882 1.00 38.03  ? 57  ASP   B CB  1 
ATOM   1186 C CG  . ASP   B 1 58 ? 22.576  -23.850 -32.162 1.00 39.93  ? 57  ASP   B CG  1 
ATOM   1187 O OD1 . ASP   B 1 58 ? 21.607  -24.622 -32.368 1.00 37.06  ? 57  ASP   B OD1 1 
ATOM   1188 O OD2 . ASP   B 1 58 ? 23.510  -24.086 -31.366 1.00 41.88  ? 57  ASP   B OD2 1 
ATOM   1189 N N   . LEU   B 1 59 ? 22.113  -20.910 -36.159 1.00 34.32  ? 58  LEU   B N   1 
ATOM   1190 C CA  . LEU   B 1 59 ? 21.872  -19.612 -36.787 1.00 31.40  ? 58  LEU   B CA  1 
ATOM   1191 C C   . LEU   B 1 59 ? 21.093  -19.749 -38.086 1.00 31.34  ? 58  LEU   B C   1 
ATOM   1192 O O   . LEU   B 1 59 ? 21.557  -20.361 -39.053 1.00 31.92  ? 58  LEU   B O   1 
ATOM   1193 C CB  . LEU   B 1 59 ? 23.190  -18.875 -37.010 1.00 34.10  ? 58  LEU   B CB  1 
ATOM   1194 C CG  . LEU   B 1 59 ? 24.027  -18.637 -35.754 1.00 33.89  ? 58  LEU   B CG  1 
ATOM   1195 C CD1 . LEU   B 1 59 ? 25.343  -17.918 -36.045 1.00 38.43  ? 58  LEU   B CD1 1 
ATOM   1196 C CD2 . LEU   B 1 59 ? 23.229  -17.893 -34.674 1.00 34.20  ? 58  LEU   B CD2 1 
ATOM   1197 N N   . PHE   B 1 60 ? 19.892  -19.184 -38.094 1.00 28.28  ? 59  PHE   B N   1 
ATOM   1198 C CA  . PHE   B 1 60 ? 18.990  -19.341 -39.210 1.00 29.08  ? 59  PHE   B CA  1 
ATOM   1199 C C   . PHE   B 1 60 ? 18.828  -17.968 -39.869 1.00 31.77  ? 59  PHE   B C   1 
ATOM   1200 O O   . PHE   B 1 60 ? 18.252  -17.079 -39.254 1.00 30.87  ? 59  PHE   B O   1 
ATOM   1201 C CB  . PHE   B 1 60 ? 17.632  -19.883 -38.755 1.00 26.90  ? 59  PHE   B CB  1 
ATOM   1202 C CG  . PHE   B 1 60 ? 17.727  -21.281 -38.143 1.00 28.86  ? 59  PHE   B CG  1 
ATOM   1203 C CD1 . PHE   B 1 60 ? 18.332  -21.469 -36.906 1.00 33.15  ? 59  PHE   B CD1 1 
ATOM   1204 C CD2 . PHE   B 1 60 ? 17.236  -22.397 -38.830 1.00 32.24  ? 59  PHE   B CD2 1 
ATOM   1205 C CE1 . PHE   B 1 60 ? 18.450  -22.750 -36.361 1.00 34.96  ? 59  PHE   B CE1 1 
ATOM   1206 C CE2 . PHE   B 1 60 ? 17.329  -23.679 -38.277 1.00 32.76  ? 59  PHE   B CE2 1 
ATOM   1207 C CZ  . PHE   B 1 60 ? 17.951  -23.857 -37.058 1.00 34.23  ? 59  PHE   B CZ  1 
ATOM   1208 N N   . PRO   B 1 61 ? 19.313  -17.749 -41.116 1.00 36.34  ? 60  PRO   B N   1 
ATOM   1209 C CA  . PRO   B 1 61 ? 19.017  -16.497 -41.841 1.00 36.53  ? 60  PRO   B CA  1 
ATOM   1210 C C   . PRO   B 1 61 ? 17.568  -16.001 -41.764 1.00 34.90  ? 60  PRO   B C   1 
ATOM   1211 O O   . PRO   B 1 61 ? 16.608  -16.762 -41.969 1.00 34.63  ? 60  PRO   B O   1 
ATOM   1212 C CB  . PRO   B 1 61 ? 19.475  -16.847 -43.268 1.00 37.12  ? 60  PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 1 61 ? 20.665  -17.738 -43.015 1.00 44.42  ? 60  PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 1 61 ? 20.156  -18.675 -41.900 1.00 40.39  ? 60  PRO   B CD  1 
ATOM   1215 N N   . TYR   B 1 62 ? 17.409  -14.690 -41.479 1.00 32.71  ? 61  TYR   B N   1 
ATOM   1216 C CA  . TYR   B 1 62 ? 16.133  -14.154 -41.058 1.00 34.93  ? 61  TYR   B CA  1 
ATOM   1217 C C   . TYR   B 1 62 ? 15.133  -14.215 -42.201 1.00 37.50  ? 61  TYR   B C   1 
ATOM   1218 O O   . TYR   B 1 62 ? 13.990  -14.631 -42.006 1.00 37.32  ? 61  TYR   B O   1 
ATOM   1219 C CB  . TYR   B 1 62 ? 16.316  -12.723 -40.543 1.00 38.26  ? 61  TYR   B CB  1 
ATOM   1220 C CG  . TYR   B 1 62 ? 15.009  -11.976 -40.321 1.00 39.03  ? 61  TYR   B CG  1 
ATOM   1221 C CD1 . TYR   B 1 62 ? 14.250  -12.201 -39.181 1.00 38.38  ? 61  TYR   B CD1 1 
ATOM   1222 C CD2 . TYR   B 1 62 ? 14.563  -11.014 -41.225 1.00 42.74  ? 61  TYR   B CD2 1 
ATOM   1223 C CE1 . TYR   B 1 62 ? 13.079  -11.503 -38.945 1.00 41.02  ? 61  TYR   B CE1 1 
ATOM   1224 C CE2 . TYR   B 1 62 ? 13.388  -10.313 -41.007 1.00 43.70  ? 61  TYR   B CE2 1 
ATOM   1225 C CZ  . TYR   B 1 62 ? 12.648  -10.559 -39.859 1.00 43.91  ? 61  TYR   B CZ  1 
ATOM   1226 O OH  . TYR   B 1 62 ? 11.478  -9.903  -39.620 1.00 47.68  ? 61  TYR   B OH  1 
ATOM   1227 N N   . ASP   B 1 63 ? 15.600  -13.818 -43.398 1.00 50.17  ? 62  ASP   B N   1 
ATOM   1228 C CA  . ASP   B 1 63 ? 14.779  -13.791 -44.601 1.00 49.65  ? 62  ASP   B CA  1 
ATOM   1229 C C   . ASP   B 1 63 ? 14.141  -15.149 -44.838 1.00 45.44  ? 62  ASP   B C   1 
ATOM   1230 O O   . ASP   B 1 63 ? 12.915  -15.270 -44.854 1.00 52.57  ? 62  ASP   B O   1 
ATOM   1231 C CB  . ASP   B 1 63 ? 15.570  -13.359 -45.821 1.00 55.49  ? 62  ASP   B CB  1 
ATOM   1232 C CG  . ASP   B 1 63 ? 15.054  -12.070 -46.430 1.00 66.16  ? 62  ASP   B CG  1 
ATOM   1233 O OD1 . ASP   B 1 63 ? 14.760  -11.147 -45.639 1.00 75.03  ? 62  ASP   B OD1 1 
ATOM   1234 O OD2 . ASP   B 1 63 ? 14.914  -12.021 -47.674 1.00 73.52  ? 62  ASP   B OD2 1 
ATOM   1235 N N   . LYS   B 1 64 ? 15.006  -16.155 -44.973 1.00 46.57  ? 63  LYS   B N   1 
ATOM   1236 C CA  . LYS   B 1 64 ? 14.587  -17.516 -45.237 1.00 46.41  ? 63  LYS   B CA  1 
ATOM   1237 C C   . LYS   B 1 64 ? 13.610  -18.016 -44.173 1.00 43.23  ? 63  LYS   B C   1 
ATOM   1238 O O   . LYS   B 1 64 ? 12.701  -18.765 -44.488 1.00 45.36  ? 63  LYS   B O   1 
ATOM   1239 C CB  . LYS   B 1 64 ? 15.800  -18.449 -45.221 1.00 50.53  ? 63  LYS   B CB  1 
ATOM   1240 C CG  . LYS   B 1 64 ? 15.483  -19.871 -45.662 1.00 46.11  ? 63  LYS   B CG  1 
ATOM   1241 C CD  . LYS   B 1 64 ? 16.689  -20.792 -45.560 1.00 47.06  ? 63  LYS   B CD  1 
ATOM   1242 C CE  . LYS   B 1 64 ? 16.577  -22.059 -46.370 1.00 48.87  ? 63  LYS   B CE  1 
ATOM   1243 N NZ  . LYS   B 1 64 ? 15.286  -22.748 -46.320 1.00 49.03  ? 63  LYS   B NZ  1 
ATOM   1244 N N   . SER   B 1 65 ? 13.810  -17.637 -42.908 1.00 46.88  ? 64  SER   B N   1 
ATOM   1245 C CA  . SER   B 1 65 ? 13.146  -18.380 -41.843 1.00 43.96  ? 64  SER   B CA  1 
ATOM   1246 C C   . SER   B 1 65 ? 12.058  -17.573 -41.127 1.00 41.86  ? 64  SER   B C   1 
ATOM   1247 O O   . SER   B 1 65 ? 11.397  -18.092 -40.231 1.00 41.97  ? 64  SER   B O   1 
ATOM   1248 C CB  . SER   B 1 65 ? 14.147  -19.017 -40.913 1.00 40.96  ? 64  SER   B CB  1 
ATOM   1249 O OG  . SER   B 1 65 ? 15.125  -18.078 -40.499 1.00 51.30  ? 64  SER   B OG  1 
ATOM   1250 N N   . LYS   B 1 66 ? 11.795  -16.341 -41.576 1.00 41.54  ? 65  LYS   B N   1 
ATOM   1251 C CA  . LYS   B 1 66 ? 10.937  -15.463 -40.788 1.00 44.72  ? 65  LYS   B CA  1 
ATOM   1252 C C   . LYS   B 1 66 ? 9.487   -15.957 -40.719 1.00 48.66  ? 65  LYS   B C   1 
ATOM   1253 O O   . LYS   B 1 66 ? 8.767   -15.663 -39.763 1.00 51.65  ? 65  LYS   B O   1 
ATOM   1254 C CB  . LYS   B 1 66 ? 11.018  -13.990 -41.209 1.00 44.46  ? 65  LYS   B CB  1 
ATOM   1255 C CG  . LYS   B 1 66 ? 10.531  -13.677 -42.609 1.00 38.32  ? 65  LYS   B CG  1 
ATOM   1256 N N   . ASP   B 1 67 ? 9.023   -16.695 -41.724 1.00 48.20  ? 66  ASP   B N   1 
ATOM   1257 C CA  . ASP   B 1 67 ? 7.608   -17.026 -41.673 1.00 53.46  ? 66  ASP   B CA  1 
ATOM   1258 C C   . ASP   B 1 67 ? 7.438   -18.269 -40.805 1.00 53.46  ? 66  ASP   B C   1 
ATOM   1259 O O   . ASP   B 1 67 ? 6.369   -18.509 -40.241 1.00 51.88  ? 66  ASP   B O   1 
ATOM   1260 C CB  . ASP   B 1 67 ? 6.950   -16.918 -43.040 1.00 63.66  ? 66  ASP   B CB  1 
ATOM   1261 C CG  . ASP   B 1 67 ? 7.357   -17.962 -44.068 1.00 77.30  ? 66  ASP   B CG  1 
ATOM   1262 O OD1 . ASP   B 1 67 ? 7.222   -17.669 -45.283 1.00 83.52  ? 66  ASP   B OD1 1 
ATOM   1263 O OD2 . ASP   B 1 67 ? 7.762   -19.068 -43.646 1.00 76.45  ? 66  ASP   B OD2 1 
ATOM   1264 N N   . LYS   B 1 68 ? 8.540   -19.015 -40.650 1.00 49.59  ? 67  LYS   B N   1 
ATOM   1265 C CA  . LYS   B 1 68 ? 8.545   -20.191 -39.797 1.00 44.37  ? 67  LYS   B CA  1 
ATOM   1266 C C   . LYS   B 1 68 ? 8.732   -19.794 -38.332 1.00 43.91  ? 67  LYS   B C   1 
ATOM   1267 O O   . LYS   B 1 68 ? 7.989   -20.291 -37.486 1.00 46.62  ? 67  LYS   B O   1 
ATOM   1268 C CB  . LYS   B 1 68 ? 9.522   -21.227 -40.355 1.00 48.79  ? 67  LYS   B CB  1 
ATOM   1269 C CG  . LYS   B 1 68 ? 9.665   -22.525 -39.563 1.00 60.12  ? 67  LYS   B CG  1 
ATOM   1270 C CD  . LYS   B 1 68 ? 10.679  -23.425 -40.265 1.00 63.81  ? 67  LYS   B CD  1 
ATOM   1271 C CE  . LYS   B 1 68 ? 11.149  -24.595 -39.448 1.00 72.74  ? 67  LYS   B CE  1 
ATOM   1272 N NZ  . LYS   B 1 68 ? 10.179  -25.690 -39.356 1.00 64.84  ? 67  LYS   B NZ  1 
ATOM   1273 N N   . TYR   B 1 69 ? 9.689   -18.891 -38.032 1.00 36.48  ? 68  TYR   B N   1 
ATOM   1274 C CA  . TYR   B 1 69 ? 10.073  -18.656 -36.642 1.00 34.60  ? 68  TYR   B CA  1 
ATOM   1275 C C   . TYR   B 1 69 ? 9.549   -17.334 -36.094 1.00 38.02  ? 68  TYR   B C   1 
ATOM   1276 O O   . TYR   B 1 69 ? 9.718   -17.069 -34.906 1.00 36.17  ? 68  TYR   B O   1 
ATOM   1277 C CB  . TYR   B 1 69 ? 11.578  -18.722 -36.382 1.00 33.91  ? 68  TYR   B CB  1 
ATOM   1278 C CG  . TYR   B 1 69 ? 12.158  -20.101 -36.674 1.00 37.92  ? 68  TYR   B CG  1 
ATOM   1279 C CD1 . TYR   B 1 69 ? 11.577  -21.259 -36.148 1.00 42.07  ? 68  TYR   B CD1 1 
ATOM   1280 C CD2 . TYR   B 1 69 ? 13.268  -20.248 -37.503 1.00 41.22  ? 68  TYR   B CD2 1 
ATOM   1281 C CE1 . TYR   B 1 69 ? 12.100  -22.519 -36.420 1.00 39.14  ? 68  TYR   B CE1 1 
ATOM   1282 C CE2 . TYR   B 1 69 ? 13.797  -21.499 -37.780 1.00 41.94  ? 68  TYR   B CE2 1 
ATOM   1283 C CZ  . TYR   B 1 69 ? 13.216  -22.631 -37.229 1.00 41.40  ? 68  TYR   B CZ  1 
ATOM   1284 O OH  . TYR   B 1 69 ? 13.721  -23.862 -37.511 1.00 40.08  ? 68  TYR   B OH  1 
ATOM   1285 N N   . GLY   B 1 70 ? 8.922   -16.514 -36.945 1.00 38.47  ? 69  GLY   B N   1 
ATOM   1286 C CA  . GLY   B 1 70 ? 8.683   -15.135 -36.555 1.00 44.47  ? 69  GLY   B CA  1 
ATOM   1287 C C   . GLY   B 1 70 ? 7.247   -14.890 -36.107 1.00 49.82  ? 69  GLY   B C   1 
ATOM   1288 O O   . GLY   B 1 70 ? 6.688   -13.849 -36.430 1.00 49.91  ? 69  GLY   B O   1 
ATOM   1289 N N   . LYS   B 1 71 ? 6.663   -15.867 -35.405 1.00 53.60  ? 70  LYS   B N   1 
ATOM   1290 C CA  . LYS   B 1 71 ? 5.326   -15.737 -34.864 1.00 51.45  ? 70  LYS   B CA  1 
ATOM   1291 C C   . LYS   B 1 71 ? 5.455   -15.221 -33.445 1.00 52.35  ? 70  LYS   B C   1 
ATOM   1292 O O   . LYS   B 1 71 ? 6.365   -15.638 -32.732 1.00 55.44  ? 70  LYS   B O   1 
ATOM   1293 C CB  . LYS   B 1 71 ? 4.611   -17.088 -34.736 1.00 51.11  ? 70  LYS   B CB  1 
ATOM   1294 C CG  . LYS   B 1 71 ? 3.761   -17.514 -35.926 1.00 61.86  ? 70  LYS   B CG  1 
ATOM   1295 C CD  . LYS   B 1 71 ? 4.534   -17.915 -37.175 1.00 58.59  ? 70  LYS   B CD  1 
ATOM   1296 C CE  . LYS   B 1 71 ? 3.641   -18.356 -38.288 1.00 59.55  ? 70  LYS   B CE  1 
ATOM   1297 N NZ  . LYS   B 1 71 ? 4.259   -17.996 -39.569 1.00 60.62  ? 70  LYS   B NZ  1 
ATOM   1298 N N   . PRO   B 1 72 ? 4.563   -14.314 -32.986 1.00 51.38  ? 71  PRO   B N   1 
ATOM   1299 C CA  . PRO   B 1 72 ? 4.517   -13.966 -31.563 1.00 50.37  ? 71  PRO   B CA  1 
ATOM   1300 C C   . PRO   B 1 72 ? 4.247   -15.177 -30.667 1.00 52.84  ? 71  PRO   B C   1 
ATOM   1301 O O   . PRO   B 1 72 ? 3.608   -16.146 -31.094 1.00 50.26  ? 71  PRO   B O   1 
ATOM   1302 C CB  . PRO   B 1 72 ? 3.471   -12.848 -31.415 1.00 44.65  ? 71  PRO   B CB  1 
ATOM   1303 C CG  . PRO   B 1 72 ? 3.135   -12.452 -32.838 1.00 53.86  ? 71  PRO   B CG  1 
ATOM   1304 C CD  . PRO   B 1 72 ? 3.605   -13.548 -33.798 1.00 52.00  ? 71  PRO   B CD  1 
ATOM   1305 N N   . ASN   B 1 73 ? 4.803   -15.117 -29.445 1.00 44.32  ? 72  ASN   B N   1 
ATOM   1306 C CA  . ASN   B 1 73 ? 4.521   -16.051 -28.368 1.00 45.05  ? 72  ASN   B CA  1 
ATOM   1307 C C   . ASN   B 1 73 ? 4.500   -15.276 -27.042 1.00 49.34  ? 72  ASN   B C   1 
ATOM   1308 O O   . ASN   B 1 73 ? 4.567   -14.044 -27.031 1.00 53.02  ? 72  ASN   B O   1 
ATOM   1309 C CB  . ASN   B 1 73 ? 5.510   -17.217 -28.362 1.00 42.48  ? 72  ASN   B CB  1 
ATOM   1310 C CG  . ASN   B 1 73 ? 6.935   -16.743 -28.207 1.00 43.21  ? 72  ASN   B CG  1 
ATOM   1311 O OD1 . ASN   B 1 73 ? 7.235   -15.983 -27.284 1.00 40.90  ? 72  ASN   B OD1 1 
ATOM   1312 N ND2 . ASN   B 1 73 ? 7.816   -17.128 -29.119 1.00 41.47  ? 72  ASN   B ND2 1 
ATOM   1313 N N   . LYS   B 1 74 ? 4.480   -16.015 -25.925 1.00 45.54  ? 73  LYS   B N   1 
ATOM   1314 C CA  . LYS   B 1 74 ? 4.358   -15.447 -24.587 1.00 50.38  ? 73  LYS   B CA  1 
ATOM   1315 C C   . LYS   B 1 74 ? 5.702   -15.477 -23.841 1.00 50.19  ? 73  LYS   B C   1 
ATOM   1316 O O   . LYS   B 1 74 ? 5.733   -15.421 -22.615 1.00 48.25  ? 73  LYS   B O   1 
ATOM   1317 C CB  . LYS   B 1 74 ? 3.286   -16.259 -23.835 1.00 48.22  ? 73  LYS   B CB  1 
ATOM   1318 N N   . ARG   B 1 75 ? 6.823   -15.595 -24.561 1.00 40.52  ? 74  ARG   B N   1 
ATOM   1319 C CA  . ARG   B 1 75 ? 8.109   -15.516 -23.896 1.00 40.07  ? 74  ARG   B CA  1 
ATOM   1320 C C   . ARG   B 1 75 ? 8.475   -14.039 -23.738 1.00 41.12  ? 74  ARG   B C   1 
ATOM   1321 O O   . ARG   B 1 75 ? 8.286   -13.246 -24.661 1.00 45.15  ? 74  ARG   B O   1 
ATOM   1322 C CB  . ARG   B 1 75 ? 9.178   -16.347 -24.614 1.00 44.51  ? 74  ARG   B CB  1 
ATOM   1323 C CG  . ARG   B 1 75 ? 8.882   -17.824 -24.825 1.00 38.70  ? 74  ARG   B CG  1 
ATOM   1324 C CD  . ARG   B 1 75 ? 8.954   -18.615 -23.521 1.00 42.11  ? 74  ARG   B CD  1 
ATOM   1325 N NE  . ARG   B 1 75 ? 9.157   -20.048 -23.758 1.00 41.06  ? 74  ARG   B NE  1 
ATOM   1326 C CZ  . ARG   B 1 75 ? 10.291  -20.664 -23.510 1.00 38.87  ? 74  ARG   B CZ  1 
ATOM   1327 N NH1 . ARG   B 1 75 ? 11.283  -20.009 -22.928 1.00 45.47  ? 74  ARG   B NH1 1 
ATOM   1328 N NH2 . ARG   B 1 75 ? 10.461  -21.922 -23.884 1.00 42.70  ? 74  ARG   B NH2 1 
ATOM   1329 N N   . LYS   B 1 76 ? 8.958   -13.673 -22.546 1.00 38.80  ? 75  LYS   B N   1 
ATOM   1330 C CA  . LYS   B 1 76 ? 9.247   -12.284 -22.233 1.00 34.76  ? 75  LYS   B CA  1 
ATOM   1331 C C   . LYS   B 1 76 ? 10.379  -11.764 -23.121 1.00 35.87  ? 75  LYS   B C   1 
ATOM   1332 O O   . LYS   B 1 76 ? 11.467  -12.361 -23.178 1.00 34.59  ? 75  LYS   B O   1 
ATOM   1333 C CB  . LYS   B 1 76 ? 9.667   -12.160 -20.768 1.00 37.50  ? 75  LYS   B CB  1 
ATOM   1334 C CG  . LYS   B 1 76 ? 10.104  -10.756 -20.359 1.00 37.46  ? 75  LYS   B CG  1 
ATOM   1335 C CD  . LYS   B 1 76 ? 10.748  -10.754 -18.977 1.00 37.60  ? 75  LYS   B CD  1 
ATOM   1336 C CE  . LYS   B 1 76 ? 10.935  -9.340  -18.501 1.00 46.60  ? 75  LYS   B CE  1 
ATOM   1337 N NZ  . LYS   B 1 76 ? 11.163  -9.311  -17.054 1.00 53.77  ? 75  LYS   B NZ  1 
ATOM   1338 N N   . GLY   B 1 77 ? 10.095  -10.645 -23.792 1.00 32.92  ? 76  GLY   B N   1 
ATOM   1339 C CA  . GLY   B 1 77 ? 11.059  -9.958  -24.643 1.00 38.59  ? 76  GLY   B CA  1 
ATOM   1340 C C   . GLY   B 1 77 ? 10.939  -10.356 -26.119 1.00 36.17  ? 76  GLY   B C   1 
ATOM   1341 O O   . GLY   B 1 77 ? 11.541  -9.716  -26.975 1.00 37.65  ? 76  GLY   B O   1 
ATOM   1342 N N   . PHE   B 1 78 ? 10.149  -11.401 -26.424 1.00 36.97  ? 77  PHE   B N   1 
ATOM   1343 C CA  . PHE   B 1 78 ? 10.075  -11.972 -27.768 1.00 31.65  ? 77  PHE   B CA  1 
ATOM   1344 C C   . PHE   B 1 78 ? 9.339   -11.040 -28.717 1.00 32.89  ? 77  PHE   B C   1 
ATOM   1345 O O   . PHE   B 1 78 ? 9.831   -10.752 -29.812 1.00 31.16  ? 77  PHE   B O   1 
ATOM   1346 C CB  . PHE   B 1 78 ? 9.338   -13.312 -27.798 1.00 32.33  ? 77  PHE   B CB  1 
ATOM   1347 C CG  . PHE   B 1 78 ? 9.612   -14.087 -29.075 1.00 31.98  ? 77  PHE   B CG  1 
ATOM   1348 C CD1 . PHE   B 1 78 ? 10.739  -14.896 -29.172 1.00 30.80  ? 77  PHE   B CD1 1 
ATOM   1349 C CD2 . PHE   B 1 78 ? 8.754   -14.009 -30.160 1.00 33.18  ? 77  PHE   B CD2 1 
ATOM   1350 C CE1 . PHE   B 1 78 ? 11.012  -15.627 -30.321 1.00 31.68  ? 77  PHE   B CE1 1 
ATOM   1351 C CE2 . PHE   B 1 78 ? 9.029   -14.738 -31.318 1.00 36.98  ? 77  PHE   B CE2 1 
ATOM   1352 C CZ  . PHE   B 1 78 ? 10.156  -15.546 -31.388 1.00 34.91  ? 77  PHE   B CZ  1 
ATOM   1353 N N   . ASN   B 1 79 ? 8.140   -10.588 -28.331 1.00 33.82  ? 78  ASN   B N   1 
ATOM   1354 C CA  . ASN   B 1 79 ? 7.431   -9.691  -29.228 1.00 37.86  ? 78  ASN   B CA  1 
ATOM   1355 C C   . ASN   B 1 79 ? 8.211   -8.377  -29.378 1.00 34.21  ? 78  ASN   B C   1 
ATOM   1356 O O   . ASN   B 1 79 ? 8.229   -7.780  -30.448 1.00 39.28  ? 78  ASN   B O   1 
ATOM   1357 C CB  . ASN   B 1 79 ? 5.942   -9.582  -28.905 1.00 40.57  ? 78  ASN   B CB  1 
ATOM   1358 C CG  . ASN   B 1 79 ? 5.224   -10.915 -28.969 1.00 47.91  ? 78  ASN   B CG  1 
ATOM   1359 O OD1 . ASN   B 1 79 ? 5.797   -11.936 -29.376 1.00 47.52  ? 78  ASN   B OD1 1 
ATOM   1360 N ND2 . ASN   B 1 79 ? 3.972   -10.943 -28.538 1.00 51.20  ? 78  ASN   B ND2 1 
ATOM   1361 N N   . GLU   B 1 80 ? 8.890   -7.933  -28.329 1.00 37.79  ? 79  GLU   B N   1 
ATOM   1362 C CA  . GLU   B 1 80 ? 9.755   -6.770  -28.481 1.00 39.42  ? 79  GLU   B CA  1 
ATOM   1363 C C   . GLU   B 1 80 ? 10.874  -7.057  -29.481 1.00 38.02  ? 79  GLU   B C   1 
ATOM   1364 O O   . GLU   B 1 80 ? 11.204  -6.199  -30.294 1.00 38.56  ? 79  GLU   B O   1 
ATOM   1365 C CB  . GLU   B 1 80 ? 10.271  -6.188  -27.171 1.00 41.17  ? 79  GLU   B CB  1 
ATOM   1366 C CG  . GLU   B 1 80 ? 9.209   -5.344  -26.479 1.00 50.08  ? 79  GLU   B CG  1 
ATOM   1367 N N   . GLY   B 1 81 ? 11.450  -8.264  -29.414 1.00 37.12  ? 80  GLY   B N   1 
ATOM   1368 C CA  . GLY   B 1 81 ? 12.479  -8.724  -30.336 1.00 34.86  ? 80  GLY   B CA  1 
ATOM   1369 C C   . GLY   B 1 81 ? 12.012  -8.665  -31.784 1.00 37.55  ? 80  GLY   B C   1 
ATOM   1370 O O   . GLY   B 1 81 ? 12.770  -8.220  -32.646 1.00 36.40  ? 80  GLY   B O   1 
ATOM   1371 N N   . LEU   B 1 82 ? 10.757  -9.080  -32.029 1.00 31.15  ? 81  LEU   B N   1 
ATOM   1372 C CA  . LEU   B 1 82 ? 10.191  -9.101  -33.363 1.00 34.13  ? 81  LEU   B CA  1 
ATOM   1373 C C   . LEU   B 1 82 ? 10.010  -7.672  -33.856 1.00 33.54  ? 81  LEU   B C   1 
ATOM   1374 O O   . LEU   B 1 82 ? 10.250  -7.398  -35.022 1.00 34.61  ? 81  LEU   B O   1 
ATOM   1375 C CB  . LEU   B 1 82 ? 8.873   -9.882  -33.449 1.00 33.11  ? 81  LEU   B CB  1 
ATOM   1376 C CG  . LEU   B 1 82 ? 8.977   -11.398 -33.253 1.00 32.50  ? 81  LEU   B CG  1 
ATOM   1377 C CD1 . LEU   B 1 82 ? 7.587   -12.014 -33.266 1.00 35.21  ? 81  LEU   B CD1 1 
ATOM   1378 C CD2 . LEU   B 1 82 ? 9.924   -12.130 -34.222 1.00 29.64  ? 81  LEU   B CD2 1 
ATOM   1379 N N   . TRP   B 1 83 ? 9.560   -6.770  -32.977 1.00 31.52  ? 82  TRP   B N   1 
ATOM   1380 C CA  . TRP   B 1 83 ? 9.488   -5.363  -33.340 1.00 31.86  ? 82  TRP   B CA  1 
ATOM   1381 C C   . TRP   B 1 83 ? 10.866  -4.828  -33.744 1.00 31.09  ? 82  TRP   B C   1 
ATOM   1382 O O   . TRP   B 1 83 ? 10.961  -4.127  -34.757 1.00 34.04  ? 82  TRP   B O   1 
ATOM   1383 C CB  . TRP   B 1 83 ? 8.804   -4.499  -32.265 1.00 33.64  ? 82  TRP   B CB  1 
ATOM   1384 C CG  . TRP   B 1 83 ? 8.592   -3.086  -32.744 1.00 36.21  ? 82  TRP   B CG  1 
ATOM   1385 C CD1 . TRP   B 1 83 ? 7.476   -2.565  -33.327 1.00 42.25  ? 82  TRP   B CD1 1 
ATOM   1386 C CD2 . TRP   B 1 83 ? 9.582   -2.037  -32.768 1.00 39.31  ? 82  TRP   B CD2 1 
ATOM   1387 N NE1 . TRP   B 1 83 ? 7.696   -1.262  -33.701 1.00 38.46  ? 82  TRP   B NE1 1 
ATOM   1388 C CE2 . TRP   B 1 83 ? 8.976   -0.910  -33.371 1.00 41.12  ? 82  TRP   B CE2 1 
ATOM   1389 C CE3 . TRP   B 1 83 ? 10.912  -1.939  -32.329 1.00 39.00  ? 82  TRP   B CE3 1 
ATOM   1390 C CZ2 . TRP   B 1 83 ? 9.653   0.300   -33.531 1.00 44.57  ? 82  TRP   B CZ2 1 
ATOM   1391 C CZ3 . TRP   B 1 83 ? 11.586  -0.746  -32.502 1.00 42.99  ? 82  TRP   B CZ3 1 
ATOM   1392 C CH2 . TRP   B 1 83 ? 10.970  0.350   -33.111 1.00 43.65  ? 82  TRP   B CH2 1 
ATOM   1393 N N   . GLU   B 1 84 ? 11.924  -5.227  -33.019 1.00 30.77  ? 83  GLU   B N   1 
ATOM   1394 C CA  . GLU   B 1 84 ? 13.262  -4.668  -33.214 1.00 34.25  ? 83  GLU   B CA  1 
ATOM   1395 C C   . GLU   B 1 84 ? 13.906  -5.127  -34.526 1.00 38.47  ? 83  GLU   B C   1 
ATOM   1396 O O   . GLU   B 1 84 ? 14.510  -4.321  -35.257 1.00 37.11  ? 83  GLU   B O   1 
ATOM   1397 C CB  . GLU   B 1 84 ? 14.165  -4.966  -32.024 1.00 33.03  ? 83  GLU   B CB  1 
ATOM   1398 C CG  . GLU   B 1 84 ? 13.734  -4.185  -30.788 1.00 36.66  ? 83  GLU   B CG  1 
ATOM   1399 C CD  . GLU   B 1 84 ? 14.606  -4.531  -29.614 1.00 38.05  ? 83  GLU   B CD  1 
ATOM   1400 O OE1 . GLU   B 1 84 ? 15.476  -5.430  -29.762 1.00 36.23  ? 83  GLU   B OE1 1 
ATOM   1401 O OE2 . GLU   B 1 84 ? 14.456  -3.862  -28.555 1.00 40.38  ? 83  GLU   B OE2 1 
ATOM   1402 N N   . ILE   B 1 85 ? 13.784  -6.424  -34.822 1.00 34.10  ? 84  ILE   B N   1 
ATOM   1403 C CA  . ILE   B 1 85 ? 14.410  -6.981  -36.014 1.00 31.99  ? 84  ILE   B CA  1 
ATOM   1404 C C   . ILE   B 1 85 ? 13.707  -6.437  -37.255 1.00 36.90  ? 84  ILE   B C   1 
ATOM   1405 O O   . ILE   B 1 85 ? 14.338  -6.256  -38.302 1.00 35.04  ? 84  ILE   B O   1 
ATOM   1406 C CB  . ILE   B 1 85 ? 14.463  -8.520  -35.955 1.00 32.18  ? 84  ILE   B CB  1 
ATOM   1407 C CG1 . ILE   B 1 85 ? 15.415  -9.114  -36.990 1.00 32.45  ? 84  ILE   B CG1 1 
ATOM   1408 C CG2 . ILE   B 1 85 ? 13.059  -9.124  -36.058 1.00 27.41  ? 84  ILE   B CG2 1 
ATOM   1409 C CD1 . ILE   B 1 85 ? 15.987  -10.477 -36.609 1.00 34.63  ? 84  ILE   B CD1 1 
ATOM   1410 N N   . GLN   B 1 86 ? 12.409  -6.138  -37.108 1.00 33.76  ? 85  GLN   B N   1 
ATOM   1411 C CA  . GLN   B 1 86 ? 11.576  -5.636  -38.188 1.00 39.15  ? 85  GLN   B CA  1 
ATOM   1412 C C   . GLN   B 1 86 ? 11.765  -4.132  -38.401 1.00 37.78  ? 85  GLN   B C   1 
ATOM   1413 O O   . GLN   B 1 86 ? 11.744  -3.683  -39.536 1.00 37.84  ? 85  GLN   B O   1 
ATOM   1414 C CB  . GLN   B 1 86 ? 10.109  -6.012  -37.952 1.00 44.03  ? 85  GLN   B CB  1 
ATOM   1415 C CG  . GLN   B 1 86 ? 9.772   -7.468  -38.282 1.00 55.29  ? 85  GLN   B CG  1 
ATOM   1416 C CD  . GLN   B 1 86 ? 8.553   -8.033  -37.567 1.00 66.07  ? 85  GLN   B CD  1 
ATOM   1417 O OE1 . GLN   B 1 86 ? 7.454   -7.452  -37.558 1.00 60.77  ? 85  GLN   B OE1 1 
ATOM   1418 N NE2 . GLN   B 1 86 ? 8.744   -9.199  -36.956 1.00 50.40  ? 85  GLN   B NE2 1 
ATOM   1419 N N   . ASN   B 1 87 ? 11.927  -3.328  -37.343 1.00 36.00  ? 86  ASN   B N   1 
ATOM   1420 C CA  . ASN   B 1 87 ? 11.768  -1.889  -37.555 1.00 37.96  ? 86  ASN   B CA  1 
ATOM   1421 C C   . ASN   B 1 87 ? 13.066  -1.101  -37.392 1.00 37.23  ? 86  ASN   B C   1 
ATOM   1422 O O   . ASN   B 1 87 ? 13.165  0.021   -37.900 1.00 40.56  ? 86  ASN   B O   1 
ATOM   1423 C CB  . ASN   B 1 87 ? 10.690  -1.291  -36.650 1.00 40.56  ? 86  ASN   B CB  1 
ATOM   1424 C CG  . ASN   B 1 87 ? 9.343   -1.924  -36.911 1.00 45.69  ? 86  ASN   B CG  1 
ATOM   1425 O OD1 . ASN   B 1 87 ? 8.734   -1.689  -37.956 1.00 44.01  ? 86  ASN   B OD1 1 
ATOM   1426 N ND2 . ASN   B 1 87 ? 8.881   -2.771  -36.005 1.00 45.93  ? 86  ASN   B ND2 1 
ATOM   1427 N N   . ASN   B 1 88 ? 14.037  -1.650  -36.652 1.00 33.08  ? 87  ASN   B N   1 
ATOM   1428 C CA  . ASN   B 1 88 ? 15.310  -0.989  -36.420 1.00 37.64  ? 87  ASN   B CA  1 
ATOM   1429 C C   . ASN   B 1 88 ? 16.378  -2.005  -36.030 1.00 32.87  ? 87  ASN   B C   1 
ATOM   1430 O O   . ASN   B 1 88 ? 16.977  -1.927  -34.964 1.00 33.75  ? 87  ASN   B O   1 
ATOM   1431 C CB  . ASN   B 1 88 ? 15.208  0.155   -35.416 1.00 41.18  ? 87  ASN   B CB  1 
ATOM   1432 C CG  . ASN   B 1 88 ? 16.264  1.207   -35.668 1.00 42.71  ? 87  ASN   B CG  1 
ATOM   1433 O OD1 . ASN   B 1 88 ? 17.309  0.950   -36.276 1.00 37.05  ? 87  ASN   B OD1 1 
ATOM   1434 N ND2 . ASN   B 1 88 ? 16.024  2.411   -35.182 1.00 40.40  ? 87  ASN   B ND2 1 
ATOM   1435 N N   . PRO   B 1 89 ? 16.682  -2.991  -36.906 1.00 34.08  ? 88  PRO   B N   1 
ATOM   1436 C CA  . PRO   B 1 89 ? 17.633  -4.048  -36.555 1.00 28.12  ? 88  PRO   B CA  1 
ATOM   1437 C C   . PRO   B 1 89 ? 19.072  -3.609  -36.297 1.00 31.11  ? 88  PRO   B C   1 
ATOM   1438 O O   . PRO   B 1 89 ? 19.846  -4.342  -35.695 1.00 29.78  ? 88  PRO   B O   1 
ATOM   1439 C CB  . PRO   B 1 89 ? 17.556  -4.988  -37.778 1.00 26.96  ? 88  PRO   B CB  1 
ATOM   1440 C CG  . PRO   B 1 89 ? 17.121  -4.101  -38.938 1.00 31.17  ? 88  PRO   B CG  1 
ATOM   1441 C CD  . PRO   B 1 89 ? 16.170  -3.084  -38.280 1.00 30.46  ? 88  PRO   B CD  1 
ATOM   1442 N N   . HIS   B 1 90 ? 19.440  -2.404  -36.761 1.00 30.87  ? 89  HIS   B N   1 
ATOM   1443 C CA  . HIS   B 1 90 ? 20.841  -2.002  -36.727 1.00 31.87  ? 89  HIS   B CA  1 
ATOM   1444 C C   . HIS   B 1 90 ? 21.093  -0.941  -35.655 1.00 33.60  ? 89  HIS   B C   1 
ATOM   1445 O O   . HIS   B 1 90 ? 22.227  -0.464  -35.541 1.00 34.20  ? 89  HIS   B O   1 
ATOM   1446 C CB  . HIS   B 1 90 ? 21.350  -1.601  -38.126 1.00 29.34  ? 89  HIS   B CB  1 
ATOM   1447 C CG  . HIS   B 1 90 ? 21.180  -2.700  -39.142 1.00 35.43  ? 89  HIS   B CG  1 
ATOM   1448 N ND1 . HIS   B 1 90 ? 21.792  -3.922  -38.986 1.00 36.03  ? 89  HIS   B ND1 1 
ATOM   1449 C CD2 . HIS   B 1 90 ? 20.435  -2.800  -40.266 1.00 34.23  ? 89  HIS   B CD2 1 
ATOM   1450 C CE1 . HIS   B 1 90 ? 21.451  -4.711  -40.004 1.00 33.55  ? 89  HIS   B CE1 1 
ATOM   1451 N NE2 . HIS   B 1 90 ? 20.647  -4.039  -40.792 1.00 35.72  ? 89  HIS   B NE2 1 
ATOM   1452 N N   . ALA   B 1 91 ? 20.081  -0.661  -34.816 1.00 33.08  ? 90  ALA   B N   1 
ATOM   1453 C CA  . ALA   B 1 91 ? 20.203  0.379   -33.799 1.00 34.14  ? 90  ALA   B CA  1 
ATOM   1454 C C   . ALA   B 1 91 ? 21.205  -0.007  -32.718 1.00 40.93  ? 90  ALA   B C   1 
ATOM   1455 O O   . ALA   B 1 91 ? 21.532  -1.176  -32.534 1.00 36.21  ? 90  ALA   B O   1 
ATOM   1456 C CB  . ALA   B 1 91 ? 18.843  0.743   -33.200 1.00 32.32  ? 90  ALA   B CB  1 
ATOM   1457 N N   . SER   B 1 92 ? 21.669  1.008   -31.981 1.00 39.01  ? 91  SER   B N   1 
ATOM   1458 C CA  . SER   B 1 92 ? 22.325  0.791   -30.702 1.00 43.28  ? 91  SER   B CA  1 
ATOM   1459 C C   . SER   B 1 92 ? 21.275  0.473   -29.641 1.00 44.48  ? 91  SER   B C   1 
ATOM   1460 O O   . SER   B 1 92 ? 20.323  1.232   -29.469 1.00 45.18  ? 91  SER   B O   1 
ATOM   1461 C CB  . SER   B 1 92 ? 23.100  2.018   -30.299 1.00 44.23  ? 91  SER   B CB  1 
ATOM   1462 O OG  . SER   B 1 92 ? 23.612  1.803   -28.996 1.00 56.79  ? 91  SER   B OG  1 
ATOM   1463 N N   . TYR   B 1 93 ? 21.458  -0.653  -28.939 1.00 44.70  ? 92  TYR   B N   1 
ATOM   1464 C CA  . TYR   B 1 93 ? 20.564  -1.051  -27.861 1.00 44.39  ? 92  TYR   B CA  1 
ATOM   1465 C C   . TYR   B 1 93 ? 21.337  -1.019  -26.545 1.00 49.89  ? 92  TYR   B C   1 
ATOM   1466 O O   . TYR   B 1 93 ? 20.961  -1.675  -25.581 1.00 49.27  ? 92  TYR   B O   1 
ATOM   1467 C CB  . TYR   B 1 93 ? 19.872  -2.385  -28.165 1.00 38.40  ? 92  TYR   B CB  1 
ATOM   1468 C CG  . TYR   B 1 93 ? 18.837  -2.249  -29.267 1.00 33.80  ? 92  TYR   B CG  1 
ATOM   1469 C CD1 . TYR   B 1 93 ? 17.560  -1.786  -28.989 1.00 35.62  ? 92  TYR   B CD1 1 
ATOM   1470 C CD2 . TYR   B 1 93 ? 19.121  -2.623  -30.581 1.00 36.05  ? 92  TYR   B CD2 1 
ATOM   1471 C CE1 . TYR   B 1 93 ? 16.617  -1.620  -29.987 1.00 32.65  ? 92  TYR   B CE1 1 
ATOM   1472 C CE2 . TYR   B 1 93 ? 18.180  -2.483  -31.591 1.00 32.63  ? 92  TYR   B CE2 1 
ATOM   1473 C CZ  . TYR   B 1 93 ? 16.917  -2.004  -31.285 1.00 34.98  ? 92  TYR   B CZ  1 
ATOM   1474 O OH  . TYR   B 1 93 ? 15.954  -1.892  -32.250 1.00 34.43  ? 92  TYR   B OH  1 
ATOM   1475 N N   . SER   B 1 94 ? 22.407  -0.215  -26.534 1.00 64.93  ? 93  SER   B N   1 
ATOM   1476 C CA  . SER   B 1 94 ? 23.224  0.074   -25.367 1.00 74.18  ? 93  SER   B CA  1 
ATOM   1477 C C   . SER   B 1 94 ? 22.343  0.589   -24.221 1.00 86.97  ? 93  SER   B C   1 
ATOM   1478 O O   . SER   B 1 94 ? 21.326  1.262   -24.527 1.00 86.45  ? 93  SER   B O   1 
ATOM   1479 C CB  . SER   B 1 94 ? 24.270  1.099   -25.709 1.00 72.67  ? 93  SER   B CB  1 
ATOM   1480 O OG  . SER   B 1 94 ? 25.163  0.599   -26.693 1.00 78.77  ? 93  SER   B OG  1 
ATOM   1481 O OXT . SER   B 1 94 ? 22.720  0.323   -23.059 1.00 101.80 ? 93  SER   B OXT 1 
ATOM   1482 N N   . HIS   C 1 4  ? 32.643  -23.899 27.197  1.00 78.58  ? 3   HIS   C N   1 
ATOM   1483 C CA  . HIS   C 1 4  ? 31.543  -22.906 27.360  1.00 87.53  ? 3   HIS   C CA  1 
ATOM   1484 C C   . HIS   C 1 4  ? 30.860  -23.164 28.708  1.00 87.47  ? 3   HIS   C C   1 
ATOM   1485 O O   . HIS   C 1 4  ? 31.445  -23.806 29.579  1.00 89.00  ? 3   HIS   C O   1 
ATOM   1486 C CB  . HIS   C 1 4  ? 30.658  -22.935 26.103  1.00 89.68  ? 3   HIS   C CB  1 
ATOM   1487 C CG  . HIS   C 1 4  ? 29.921  -21.667 25.803  1.00 103.45 ? 3   HIS   C CG  1 
ATOM   1488 N ND1 . HIS   C 1 4  ? 28.655  -21.390 26.277  1.00 106.93 ? 3   HIS   C ND1 1 
ATOM   1489 C CD2 . HIS   C 1 4  ? 30.276  -20.607 25.062  1.00 103.07 ? 3   HIS   C CD2 1 
ATOM   1490 C CE1 . HIS   C 1 4  ? 28.271  -20.198 25.841  1.00 104.53 ? 3   HIS   C CE1 1 
ATOM   1491 N NE2 . HIS   C 1 4  ? 29.242  -19.704 25.102  1.00 105.12 ? 3   HIS   C NE2 1 
ATOM   1492 N N   . ALA   C 1 5  ? 29.630  -22.655 28.883  1.00 87.42  ? 4   ALA   C N   1 
ATOM   1493 C CA  . ALA   C 1 5  ? 28.788  -22.991 30.024  1.00 78.70  ? 4   ALA   C CA  1 
ATOM   1494 C C   . ALA   C 1 5  ? 27.308  -22.909 29.653  1.00 74.07  ? 4   ALA   C C   1 
ATOM   1495 O O   . ALA   C 1 5  ? 26.900  -22.037 28.885  1.00 71.95  ? 4   ALA   C O   1 
ATOM   1496 C CB  . ALA   C 1 5  ? 29.092  -22.062 31.158  1.00 84.96  ? 4   ALA   C CB  1 
ATOM   1497 N N   . PHE   C 1 6  ? 26.501  -23.797 30.248  1.00 61.72  ? 5   PHE   C N   1 
ATOM   1498 C CA  . PHE   C 1 6  ? 25.140  -23.990 29.771  1.00 60.19  ? 5   PHE   C CA  1 
ATOM   1499 C C   . PHE   C 1 6  ? 24.181  -24.090 30.959  1.00 65.09  ? 5   PHE   C C   1 
ATOM   1500 O O   . PHE   C 1 6  ? 24.180  -25.096 31.665  1.00 75.75  ? 5   PHE   C O   1 
ATOM   1501 C CB  . PHE   C 1 6  ? 25.054  -25.198 28.819  1.00 47.75  ? 5   PHE   C CB  1 
ATOM   1502 C CG  . PHE   C 1 6  ? 25.846  -25.150 27.511  1.00 49.25  ? 5   PHE   C CG  1 
ATOM   1503 C CD1 . PHE   C 1 6  ? 26.987  -25.927 27.332  1.00 45.95  ? 5   PHE   C CD1 1 
ATOM   1504 C CD2 . PHE   C 1 6  ? 25.464  -24.316 26.459  1.00 46.80  ? 5   PHE   C CD2 1 
ATOM   1505 C CE1 . PHE   C 1 6  ? 27.706  -25.886 26.138  1.00 52.83  ? 5   PHE   C CE1 1 
ATOM   1506 C CE2 . PHE   C 1 6  ? 26.187  -24.283 25.265  1.00 42.94  ? 5   PHE   C CE2 1 
ATOM   1507 C CZ  . PHE   C 1 6  ? 27.304  -25.067 25.102  1.00 47.57  ? 5   PHE   C CZ  1 
ATOM   1508 N N   . LYS   C 1 7  ? 23.368  -23.048 31.181  1.00 66.45  ? 6   LYS   C N   1 
ATOM   1509 C CA  . LYS   C 1 7  ? 22.327  -23.102 32.203  1.00 70.21  ? 6   LYS   C CA  1 
ATOM   1510 C C   . LYS   C 1 7  ? 21.038  -23.566 31.532  1.00 68.13  ? 6   LYS   C C   1 
ATOM   1511 O O   . LYS   C 1 7  ? 20.931  -23.497 30.310  1.00 72.98  ? 6   LYS   C O   1 
ATOM   1512 C CB  . LYS   C 1 7  ? 22.150  -21.772 32.950  1.00 68.10  ? 6   LYS   C CB  1 
ATOM   1513 N N   . PRO   C 1 8  ? 20.035  -24.104 32.265  1.00 71.92  ? 7   PRO   C N   1 
ATOM   1514 C CA  . PRO   C 1 8  ? 18.763  -24.468 31.637  1.00 71.61  ? 7   PRO   C CA  1 
ATOM   1515 C C   . PRO   C 1 8  ? 18.229  -23.293 30.820  1.00 75.44  ? 7   PRO   C C   1 
ATOM   1516 O O   . PRO   C 1 8  ? 18.517  -22.136 31.135  1.00 79.05  ? 7   PRO   C O   1 
ATOM   1517 C CB  . PRO   C 1 8  ? 17.862  -24.850 32.823  1.00 72.97  ? 7   PRO   C CB  1 
ATOM   1518 C CG  . PRO   C 1 8  ? 18.844  -25.329 33.877  1.00 70.35  ? 7   PRO   C CG  1 
ATOM   1519 C CD  . PRO   C 1 8  ? 20.086  -24.459 33.695  1.00 74.44  ? 7   PRO   C CD  1 
ATOM   1520 N N   . GLY   C 1 9  ? 17.504  -23.605 29.737  1.00 70.21  ? 8   GLY   C N   1 
ATOM   1521 C CA  . GLY   C 1 9  ? 16.891  -22.585 28.900  1.00 64.50  ? 8   GLY   C CA  1 
ATOM   1522 C C   . GLY   C 1 9  ? 17.799  -22.085 27.771  1.00 62.69  ? 8   GLY   C C   1 
ATOM   1523 O O   . GLY   C 1 9  ? 17.282  -21.554 26.788  1.00 67.63  ? 8   GLY   C O   1 
ATOM   1524 N N   . ASP   C 1 10 ? 19.130  -22.243 27.915  1.00 52.42  ? 9   ASP   C N   1 
ATOM   1525 C CA  . ASP   C 1 10 ? 20.098  -21.899 26.882  1.00 47.72  ? 9   ASP   C CA  1 
ATOM   1526 C C   . ASP   C 1 10 ? 19.757  -22.613 25.577  1.00 51.92  ? 9   ASP   C C   1 
ATOM   1527 O O   . ASP   C 1 10 ? 19.410  -23.791 25.580  1.00 50.14  ? 9   ASP   C O   1 
ATOM   1528 C CB  . ASP   C 1 10 ? 21.533  -22.209 27.282  1.00 50.63  ? 9   ASP   C CB  1 
ATOM   1529 C CG  . ASP   C 1 10 ? 22.175  -21.279 28.306  1.00 61.91  ? 9   ASP   C CG  1 
ATOM   1530 O OD1 . ASP   C 1 10 ? 21.574  -20.227 28.602  1.00 73.52  ? 9   ASP   C OD1 1 
ATOM   1531 O OD2 . ASP   C 1 10 ? 23.265  -21.617 28.824  1.00 63.38  ? 9   ASP   C OD2 1 
ATOM   1532 N N   . LEU   C 1 11 ? 19.856  -21.875 24.463  1.00 52.39  ? 10  LEU   C N   1 
ATOM   1533 C CA  . LEU   C 1 11 ? 19.475  -22.378 23.155  1.00 50.40  ? 10  LEU   C CA  1 
ATOM   1534 C C   . LEU   C 1 11 ? 20.730  -22.833 22.410  1.00 42.29  ? 10  LEU   C C   1 
ATOM   1535 O O   . LEU   C 1 11 ? 21.730  -22.118 22.370  1.00 43.92  ? 10  LEU   C O   1 
ATOM   1536 C CB  . LEU   C 1 11 ? 18.673  -21.331 22.374  1.00 47.90  ? 10  LEU   C CB  1 
ATOM   1537 C CG  . LEU   C 1 11 ? 17.325  -20.883 22.954  1.00 42.93  ? 10  LEU   C CG  1 
ATOM   1538 C CD1 . LEU   C 1 11 ? 16.723  -19.824 22.010  1.00 47.50  ? 10  LEU   C CD1 1 
ATOM   1539 C CD2 . LEU   C 1 11 ? 16.323  -22.014 23.157  1.00 47.82  ? 10  LEU   C CD2 1 
ATOM   1540 N N   . VAL   C 1 12 ? 20.666  -24.035 21.814  1.00 41.97  ? 11  VAL   C N   1 
ATOM   1541 C CA  . VAL   C 1 12 ? 21.837  -24.680 21.241  1.00 37.94  ? 11  VAL   C CA  1 
ATOM   1542 C C   . VAL   C 1 12 ? 21.465  -25.430 19.949  1.00 34.43  ? 11  VAL   C C   1 
ATOM   1543 O O   . VAL   C 1 12 ? 20.293  -25.547 19.617  1.00 32.08  ? 11  VAL   C O   1 
ATOM   1544 C CB  . VAL   C 1 12 ? 22.394  -25.658 22.299  1.00 37.05  ? 11  VAL   C CB  1 
ATOM   1545 C CG1 . VAL   C 1 12 ? 22.655  -24.967 23.636  1.00 39.24  ? 11  VAL   C CG1 1 
ATOM   1546 C CG2 . VAL   C 1 12 ? 21.508  -26.886 22.485  1.00 35.79  ? 11  VAL   C CG2 1 
ATOM   1547 N N   . PHE   C 1 13 ? 22.490  -25.857 19.193  1.00 34.08  ? 12  PHE   C N   1 
ATOM   1548 C CA  . PHE   C 1 13 ? 22.423  -27.003 18.290  1.00 29.56  ? 12  PHE   C CA  1 
ATOM   1549 C C   . PHE   C 1 13 ? 23.136  -28.145 18.998  1.00 33.26  ? 12  PHE   C C   1 
ATOM   1550 O O   . PHE   C 1 13 ? 24.201  -27.944 19.569  1.00 36.66  ? 12  PHE   C O   1 
ATOM   1551 C CB  . PHE   C 1 13 ? 23.091  -26.752 16.928  1.00 35.88  ? 12  PHE   C CB  1 
ATOM   1552 C CG  . PHE   C 1 13 ? 22.324  -25.773 16.046  1.00 39.84  ? 12  PHE   C CG  1 
ATOM   1553 C CD1 . PHE   C 1 13 ? 21.242  -26.197 15.271  1.00 39.16  ? 12  PHE   C CD1 1 
ATOM   1554 C CD2 . PHE   C 1 13 ? 22.652  -24.417 16.032  1.00 42.06  ? 12  PHE   C CD2 1 
ATOM   1555 C CE1 . PHE   C 1 13 ? 20.515  -25.286 14.505  1.00 43.28  ? 12  PHE   C CE1 1 
ATOM   1556 C CE2 . PHE   C 1 13 ? 21.930  -23.516 15.259  1.00 43.49  ? 12  PHE   C CE2 1 
ATOM   1557 C CZ  . PHE   C 1 13 ? 20.867  -23.949 14.500  1.00 41.24  ? 12  PHE   C CZ  1 
ATOM   1558 N N   . ALA   C 1 14 ? 22.517  -29.327 18.966  1.00 31.32  ? 13  ALA   C N   1 
ATOM   1559 C CA  . ALA   C 1 14 ? 23.017  -30.475 19.702  1.00 29.27  ? 13  ALA   C CA  1 
ATOM   1560 C C   . ALA   C 1 14 ? 23.248  -31.623 18.722  1.00 34.05  ? 13  ALA   C C   1 
ATOM   1561 O O   . ALA   C 1 14 ? 22.358  -31.945 17.936  1.00 31.49  ? 13  ALA   C O   1 
ATOM   1562 C CB  . ALA   C 1 14 ? 21.999  -30.872 20.730  1.00 31.92  ? 13  ALA   C CB  1 
ATOM   1563 N N   . LYS   C 1 15 ? 24.431  -32.241 18.800  1.00 34.58  ? 14  LYS   C N   1 
ATOM   1564 C CA  . LYS   C 1 15 ? 24.856  -33.230 17.820  1.00 38.61  ? 14  LYS   C CA  1 
ATOM   1565 C C   . LYS   C 1 15 ? 24.876  -34.600 18.479  1.00 37.90  ? 14  LYS   C C   1 
ATOM   1566 O O   . LYS   C 1 15 ? 25.554  -34.783 19.476  1.00 36.94  ? 14  LYS   C O   1 
ATOM   1567 C CB  . LYS   C 1 15 ? 26.277  -32.969 17.293  1.00 43.26  ? 14  LYS   C CB  1 
ATOM   1568 C CG  . LYS   C 1 15 ? 26.744  -33.902 16.158  1.00 40.80  ? 14  LYS   C CG  1 
ATOM   1569 C CD  . LYS   C 1 15 ? 25.892  -33.746 14.893  1.00 42.12  ? 14  LYS   C CD  1 
ATOM   1570 C CE  . LYS   C 1 15 ? 26.337  -34.654 13.755  1.00 38.78  ? 14  LYS   C CE  1 
ATOM   1571 N NZ  . LYS   C 1 15 ? 26.250  -36.058 14.177  1.00 33.81  ? 14  LYS   C NZ  1 
ATOM   1572 N N   . MET   C 1 16 ? 24.095  -35.528 17.913  1.00 35.24  ? 15  MET   C N   1 
ATOM   1573 C CA  . MET   C 1 16 ? 24.069  -36.931 18.278  1.00 34.22  ? 15  MET   C CA  1 
ATOM   1574 C C   . MET   C 1 16 ? 24.594  -37.719 17.083  1.00 39.74  ? 15  MET   C C   1 
ATOM   1575 O O   . MET   C 1 16 ? 24.443  -37.304 15.925  1.00 32.68  ? 15  MET   C O   1 
ATOM   1576 C CB  . MET   C 1 16 ? 22.633  -37.379 18.569  1.00 33.47  ? 15  MET   C CB  1 
ATOM   1577 C CG  . MET   C 1 16 ? 22.052  -36.852 19.889  1.00 40.92  ? 15  MET   C CG  1 
ATOM   1578 S SD  . MET   C 1 16 ? 20.434  -37.569 20.254  1.00 47.70  ? 15  MET   C SD  1 
ATOM   1579 C CE  . MET   C 1 16 ? 19.456  -36.930 18.881  1.00 40.40  ? 15  MET   C CE  1 
ATOM   1580 N N   . LYS   C 1 17 ? 25.217  -38.867 17.360  1.00 40.54  ? 16  LYS   C N   1 
ATOM   1581 C CA  . LYS   C 1 17 ? 25.619  -39.730 16.255  1.00 41.01  ? 16  LYS   C CA  1 
ATOM   1582 C C   . LYS   C 1 17 ? 24.350  -40.168 15.519  1.00 38.82  ? 16  LYS   C C   1 
ATOM   1583 O O   . LYS   C 1 17 ? 23.385  -40.631 16.138  1.00 37.98  ? 16  LYS   C O   1 
ATOM   1584 C CB  . LYS   C 1 17 ? 26.408  -40.943 16.781  1.00 41.68  ? 16  LYS   C CB  1 
ATOM   1585 C CG  . LYS   C 1 17 ? 27.022  -41.857 15.720  1.00 44.09  ? 16  LYS   C CG  1 
ATOM   1586 C CD  . LYS   C 1 17 ? 28.269  -41.236 15.102  1.00 51.12  ? 16  LYS   C CD  1 
ATOM   1587 C CE  . LYS   C 1 17 ? 28.944  -42.207 14.180  1.00 61.99  ? 16  LYS   C CE  1 
ATOM   1588 N NZ  . LYS   C 1 17 ? 30.249  -41.727 13.715  1.00 66.02  ? 16  LYS   C NZ  1 
ATOM   1589 N N   . GLY   C 1 18 ? 24.368  -40.025 14.192  1.00 41.12  ? 17  GLY   C N   1 
ATOM   1590 C CA  . GLY   C 1 18 ? 23.272  -40.521 13.371  1.00 39.81  ? 17  GLY   C CA  1 
ATOM   1591 C C   . GLY   C 1 18 ? 22.327  -39.395 12.924  1.00 42.17  ? 17  GLY   C C   1 
ATOM   1592 O O   . GLY   C 1 18 ? 21.359  -39.666 12.224  1.00 38.03  ? 17  GLY   C O   1 
ATOM   1593 N N   . TYR   C 1 19 ? 22.622  -38.145 13.321  1.00 39.66  ? 18  TYR   C N   1 
ATOM   1594 C CA  . TYR   C 1 19 ? 21.701  -37.016 13.181  1.00 37.33  ? 18  TYR   C CA  1 
ATOM   1595 C C   . TYR   C 1 19 ? 22.472  -35.732 12.914  1.00 33.85  ? 18  TYR   C C   1 
ATOM   1596 O O   . TYR   C 1 19 ? 23.554  -35.528 13.431  1.00 32.53  ? 18  TYR   C O   1 
ATOM   1597 C CB  . TYR   C 1 19 ? 20.949  -36.744 14.483  1.00 33.23  ? 18  TYR   C CB  1 
ATOM   1598 C CG  . TYR   C 1 19 ? 20.084  -37.928 14.878  1.00 35.84  ? 18  TYR   C CG  1 
ATOM   1599 C CD1 . TYR   C 1 19 ? 20.597  -38.982 15.633  1.00 36.92  ? 18  TYR   C CD1 1 
ATOM   1600 C CD2 . TYR   C 1 19 ? 18.756  -37.988 14.488  1.00 41.05  ? 18  TYR   C CD2 1 
ATOM   1601 C CE1 . TYR   C 1 19 ? 19.805  -40.062 15.977  1.00 38.53  ? 18  TYR   C CE1 1 
ATOM   1602 C CE2 . TYR   C 1 19 ? 17.958  -39.066 14.828  1.00 45.95  ? 18  TYR   C CE2 1 
ATOM   1603 C CZ  . TYR   C 1 19 ? 18.486  -40.103 15.571  1.00 42.89  ? 18  TYR   C CZ  1 
ATOM   1604 O OH  . TYR   C 1 19 ? 17.668  -41.143 15.905  1.00 47.49  ? 18  TYR   C OH  1 
ATOM   1605 N N   . PRO   C 1 20 ? 21.926  -34.823 12.087  1.00 31.43  ? 19  PRO   C N   1 
ATOM   1606 C CA  . PRO   C 1 20 ? 22.562  -33.525 11.855  1.00 31.20  ? 19  PRO   C CA  1 
ATOM   1607 C C   . PRO   C 1 20 ? 22.527  -32.708 13.159  1.00 31.08  ? 19  PRO   C C   1 
ATOM   1608 O O   . PRO   C 1 20 ? 21.802  -33.038 14.101  1.00 29.75  ? 19  PRO   C O   1 
ATOM   1609 C CB  . PRO   C 1 20 ? 21.633  -32.950 10.753  1.00 35.07  ? 19  PRO   C CB  1 
ATOM   1610 C CG  . PRO   C 1 20 ? 20.276  -33.521 11.057  1.00 33.89  ? 19  PRO   C CG  1 
ATOM   1611 C CD  . PRO   C 1 20 ? 20.609  -34.979 11.434  1.00 32.23  ? 19  PRO   C CD  1 
ATOM   1612 N N   . HIS   C 1 21 ? 23.351  -31.661 13.243  1.00 36.43  ? 20  HIS   C N   1 
ATOM   1613 C CA  . HIS   C 1 21 ? 23.288  -30.758 14.387  1.00 31.68  ? 20  HIS   C CA  1 
ATOM   1614 C C   . HIS   C 1 21 ? 21.849  -30.252 14.511  1.00 34.25  ? 20  HIS   C C   1 
ATOM   1615 O O   . HIS   C 1 21 ? 21.320  -29.703 13.542  1.00 31.57  ? 20  HIS   C O   1 
ATOM   1616 C CB  . HIS   C 1 21 ? 24.246  -29.581 14.195  1.00 38.06  ? 20  HIS   C CB  1 
ATOM   1617 C CG  . HIS   C 1 21 ? 25.675  -30.007 14.214  1.00 41.67  ? 20  HIS   C CG  1 
ATOM   1618 N ND1 . HIS   C 1 21 ? 26.288  -30.617 13.142  1.00 43.88  ? 20  HIS   C ND1 1 
ATOM   1619 C CD2 . HIS   C 1 21 ? 26.597  -29.943 15.192  1.00 46.07  ? 20  HIS   C CD2 1 
ATOM   1620 C CE1 . HIS   C 1 21 ? 27.544  -30.914 13.470  1.00 46.38  ? 20  HIS   C CE1 1 
ATOM   1621 N NE2 . HIS   C 1 21 ? 27.759  -30.493 14.708  1.00 46.44  ? 20  HIS   C NE2 1 
ATOM   1622 N N   . TRP   C 1 22 ? 21.224  -30.469 15.687  1.00 29.64  ? 21  TRP   C N   1 
ATOM   1623 C CA  . TRP   C 1 22 ? 19.774  -30.328 15.802  1.00 29.52  ? 21  TRP   C CA  1 
ATOM   1624 C C   . TRP   C 1 22 ? 19.448  -29.141 16.703  1.00 29.62  ? 21  TRP   C C   1 
ATOM   1625 O O   . TRP   C 1 22 ? 20.073  -28.978 17.753  1.00 32.94  ? 21  TRP   C O   1 
ATOM   1626 C CB  . TRP   C 1 22 ? 19.152  -31.592 16.418  1.00 33.03  ? 21  TRP   C CB  1 
ATOM   1627 C CG  . TRP   C 1 22 ? 17.705  -31.808 16.048  1.00 34.35  ? 21  TRP   C CG  1 
ATOM   1628 C CD1 . TRP   C 1 22 ? 16.580  -31.251 16.598  1.00 36.64  ? 21  TRP   C CD1 1 
ATOM   1629 C CD2 . TRP   C 1 22 ? 17.247  -32.708 15.016  1.00 33.16  ? 21  TRP   C CD2 1 
ATOM   1630 N NE1 . TRP   C 1 22 ? 15.457  -31.718 15.960  1.00 33.97  ? 21  TRP   C NE1 1 
ATOM   1631 C CE2 . TRP   C 1 22 ? 15.838  -32.631 15.004  1.00 34.55  ? 21  TRP   C CE2 1 
ATOM   1632 C CE3 . TRP   C 1 22 ? 17.893  -33.565 14.112  1.00 31.85  ? 21  TRP   C CE3 1 
ATOM   1633 C CZ2 . TRP   C 1 22 ? 15.076  -33.385 14.113  1.00 32.27  ? 21  TRP   C CZ2 1 
ATOM   1634 C CZ3 . TRP   C 1 22 ? 17.135  -34.294 13.219  1.00 31.81  ? 21  TRP   C CZ3 1 
ATOM   1635 C CH2 . TRP   C 1 22 ? 15.744  -34.214 13.240  1.00 30.60  ? 21  TRP   C CH2 1 
ATOM   1636 N N   . PRO   C 1 23 ? 18.427  -28.318 16.359  1.00 32.51  ? 22  PRO   C N   1 
ATOM   1637 C CA  . PRO   C 1 23 ? 18.021  -27.234 17.253  1.00 30.02  ? 22  PRO   C CA  1 
ATOM   1638 C C   . PRO   C 1 23 ? 17.427  -27.743 18.572  1.00 27.34  ? 22  PRO   C C   1 
ATOM   1639 O O   . PRO   C 1 23 ? 16.562  -28.610 18.600  1.00 30.19  ? 22  PRO   C O   1 
ATOM   1640 C CB  . PRO   C 1 23 ? 17.042  -26.442 16.365  1.00 32.40  ? 22  PRO   C CB  1 
ATOM   1641 C CG  . PRO   C 1 23 ? 16.461  -27.466 15.412  1.00 28.78  ? 22  PRO   C CG  1 
ATOM   1642 C CD  . PRO   C 1 23 ? 17.703  -28.304 15.070  1.00 28.31  ? 22  PRO   C CD  1 
ATOM   1643 N N   . ALA   C 1 24 ? 17.900  -27.188 19.688  1.00 31.13  ? 23  ALA   C N   1 
ATOM   1644 C CA  . ALA   C 1 24 ? 17.554  -27.742 20.990  1.00 37.38  ? 23  ALA   C CA  1 
ATOM   1645 C C   . ALA   C 1 24 ? 17.747  -26.670 22.061  1.00 38.02  ? 23  ALA   C C   1 
ATOM   1646 O O   . ALA   C 1 24 ? 18.211  -25.569 21.750  1.00 36.65  ? 23  ALA   C O   1 
ATOM   1647 C CB  . ALA   C 1 24 ? 18.437  -28.963 21.254  1.00 34.18  ? 23  ALA   C CB  1 
ATOM   1648 N N   . ARG   C 1 25 ? 17.400  -27.008 23.314  1.00 38.66  ? 24  ARG   C N   1 
ATOM   1649 C CA  . ARG   C 1 25 ? 17.766  -26.210 24.478  1.00 40.69  ? 24  ARG   C CA  1 
ATOM   1650 C C   . ARG   C 1 25 ? 18.168  -27.127 25.638  1.00 41.64  ? 24  ARG   C C   1 
ATOM   1651 O O   . ARG   C 1 25 ? 17.758  -28.291 25.687  1.00 39.82  ? 24  ARG   C O   1 
ATOM   1652 C CB  . ARG   C 1 25 ? 16.599  -25.326 24.938  1.00 43.99  ? 24  ARG   C CB  1 
ATOM   1653 C CG  . ARG   C 1 25 ? 15.328  -26.080 25.304  1.00 47.27  ? 24  ARG   C CG  1 
ATOM   1654 C CD  . ARG   C 1 25 ? 14.240  -25.200 25.936  1.00 54.21  ? 24  ARG   C CD  1 
ATOM   1655 N NE  . ARG   C 1 25 ? 13.099  -26.071 26.250  1.00 59.90  ? 24  ARG   C NE  1 
ATOM   1656 C CZ  . ARG   C 1 25 ? 11.824  -25.924 25.902  1.00 63.24  ? 24  ARG   C CZ  1 
ATOM   1657 N NH1 . ARG   C 1 25 ? 11.413  -24.839 25.264  1.00 59.83  ? 24  ARG   C NH1 1 
ATOM   1658 N NH2 . ARG   C 1 25 ? 10.953  -26.868 26.219  1.00 62.28  ? 24  ARG   C NH2 1 
ATOM   1659 N N   . ILE   C 1 26 ? 18.923  -26.556 26.585  1.00 43.66  ? 25  ILE   C N   1 
ATOM   1660 C CA  . ILE   C 1 26 ? 19.267  -27.171 27.864  1.00 47.88  ? 25  ILE   C CA  1 
ATOM   1661 C C   . ILE   C 1 26 ? 18.024  -27.199 28.749  1.00 53.53  ? 25  ILE   C C   1 
ATOM   1662 O O   . ILE   C 1 26 ? 17.406  -26.160 28.971  1.00 62.96  ? 25  ILE   C O   1 
ATOM   1663 C CB  . ILE   C 1 26 ? 20.384  -26.385 28.585  1.00 49.48  ? 25  ILE   C CB  1 
ATOM   1664 C CG1 . ILE   C 1 26 ? 21.510  -25.886 27.674  1.00 49.64  ? 25  ILE   C CG1 1 
ATOM   1665 C CG2 . ILE   C 1 26 ? 20.917  -27.143 29.805  1.00 48.39  ? 25  ILE   C CG2 1 
ATOM   1666 C CD1 . ILE   C 1 26 ? 22.464  -26.946 27.154  1.00 46.54  ? 25  ILE   C CD1 1 
ATOM   1667 N N   . ASP   C 1 27 ? 17.704  -28.378 29.293  1.00 56.68  ? 26  ASP   C N   1 
ATOM   1668 C CA  . ASP   C 1 27 ? 16.594  -28.567 30.220  1.00 65.90  ? 26  ASP   C CA  1 
ATOM   1669 C C   . ASP   C 1 27 ? 17.008  -28.321 31.670  1.00 72.98  ? 26  ASP   C C   1 
ATOM   1670 O O   . ASP   C 1 27 ? 18.194  -28.182 31.970  1.00 76.76  ? 26  ASP   C O   1 
ATOM   1671 C CB  . ASP   C 1 27 ? 15.968  -29.950 30.098  1.00 64.72  ? 26  ASP   C CB  1 
ATOM   1672 C CG  . ASP   C 1 27 ? 14.587  -29.976 29.462  1.00 71.37  ? 26  ASP   C CG  1 
ATOM   1673 O OD1 . ASP   C 1 27 ? 14.240  -28.970 28.806  1.00 67.94  ? 26  ASP   C OD1 1 
ATOM   1674 O OD2 . ASP   C 1 27 ? 13.849  -30.973 29.678  1.00 63.42  ? 26  ASP   C OD2 1 
ATOM   1675 N N   . ASP   C 1 28 ? 15.991  -28.276 32.551  1.00 82.67  ? 27  ASP   C N   1 
ATOM   1676 C CA  . ASP   C 1 28 ? 16.133  -28.313 34.000  1.00 76.80  ? 27  ASP   C CA  1 
ATOM   1677 C C   . ASP   C 1 28 ? 16.440  -29.752 34.401  1.00 80.63  ? 27  ASP   C C   1 
ATOM   1678 O O   . ASP   C 1 28 ? 16.187  -30.666 33.620  1.00 81.52  ? 27  ASP   C O   1 
ATOM   1679 C CB  . ASP   C 1 28 ? 14.854  -27.848 34.679  1.00 77.28  ? 27  ASP   C CB  1 
ATOM   1680 N N   . ILE   C 1 29 ? 16.987  -29.945 35.611  1.00 85.37  ? 28  ILE   C N   1 
ATOM   1681 C CA  . ILE   C 1 29 ? 17.324  -31.276 36.097  1.00 86.87  ? 28  ILE   C CA  1 
ATOM   1682 C C   . ILE   C 1 29 ? 16.039  -31.988 36.564  1.00 87.34  ? 28  ILE   C C   1 
ATOM   1683 O O   . ILE   C 1 29 ? 15.639  -31.770 37.732  1.00 94.48  ? 28  ILE   C O   1 
ATOM   1684 C CB  . ILE   C 1 29 ? 18.397  -31.204 37.201  1.00 87.52  ? 28  ILE   C CB  1 
ATOM   1685 N N   . LYS   C 1 35 ? 19.332  -38.531 37.929  1.00 82.00  ? 34  LYS   C N   1 
ATOM   1686 C CA  . LYS   C 1 35 ? 20.335  -37.455 37.702  1.00 77.93  ? 34  LYS   C CA  1 
ATOM   1687 C C   . LYS   C 1 35 ? 21.146  -37.822 36.460  1.00 77.57  ? 34  LYS   C C   1 
ATOM   1688 O O   . LYS   C 1 35 ? 21.180  -38.994 36.081  1.00 75.15  ? 34  LYS   C O   1 
ATOM   1689 C CB  . LYS   C 1 35 ? 21.159  -37.210 38.974  1.00 69.99  ? 34  LYS   C CB  1 
ATOM   1690 N N   . PRO   C 1 36 ? 21.806  -36.850 35.778  1.00 80.70  ? 35  PRO   C N   1 
ATOM   1691 C CA  . PRO   C 1 36 ? 22.521  -37.140 34.528  1.00 77.23  ? 35  PRO   C CA  1 
ATOM   1692 C C   . PRO   C 1 36 ? 23.641  -38.174 34.670  1.00 78.73  ? 35  PRO   C C   1 
ATOM   1693 O O   . PRO   C 1 36 ? 24.104  -38.460 35.776  1.00 82.19  ? 35  PRO   C O   1 
ATOM   1694 C CB  . PRO   C 1 36 ? 23.067  -35.760 34.094  1.00 79.40  ? 35  PRO   C CB  1 
ATOM   1695 C CG  . PRO   C 1 36 ? 22.251  -34.739 34.868  1.00 72.47  ? 35  PRO   C CG  1 
ATOM   1696 C CD  . PRO   C 1 36 ? 21.904  -35.432 36.177  1.00 75.50  ? 35  PRO   C CD  1 
ATOM   1697 N N   . PRO   C 1 37 ? 24.116  -38.803 33.573  1.00 69.86  ? 36  PRO   C N   1 
ATOM   1698 C CA  . PRO   C 1 37 ? 25.458  -39.387 33.589  1.00 66.26  ? 36  PRO   C CA  1 
ATOM   1699 C C   . PRO   C 1 37 ? 26.461  -38.268 33.879  1.00 64.92  ? 36  PRO   C C   1 
ATOM   1700 O O   . PRO   C 1 37 ? 26.192  -37.097 33.597  1.00 51.27  ? 36  PRO   C O   1 
ATOM   1701 C CB  . PRO   C 1 37 ? 25.613  -40.016 32.193  1.00 62.11  ? 36  PRO   C CB  1 
ATOM   1702 C CG  . PRO   C 1 37 ? 24.186  -40.253 31.752  1.00 64.25  ? 36  PRO   C CG  1 
ATOM   1703 C CD  . PRO   C 1 37 ? 23.381  -39.089 32.331  1.00 69.04  ? 36  PRO   C CD  1 
ATOM   1704 N N   . PRO   C 1 38 ? 27.612  -38.576 34.523  1.00 59.91  ? 37  PRO   C N   1 
ATOM   1705 C CA  . PRO   C 1 38 ? 28.617  -37.558 34.834  1.00 59.75  ? 37  PRO   C CA  1 
ATOM   1706 C C   . PRO   C 1 38 ? 28.892  -36.626 33.661  1.00 51.48  ? 37  PRO   C C   1 
ATOM   1707 O O   . PRO   C 1 38 ? 29.187  -37.092 32.561  1.00 48.29  ? 37  PRO   C O   1 
ATOM   1708 C CB  . PRO   C 1 38 ? 29.839  -38.428 35.176  1.00 57.83  ? 37  PRO   C CB  1 
ATOM   1709 C CG  . PRO   C 1 38 ? 29.226  -39.643 35.834  1.00 63.09  ? 37  PRO   C CG  1 
ATOM   1710 C CD  . PRO   C 1 38 ? 27.985  -39.916 35.010  1.00 59.95  ? 37  PRO   C CD  1 
ATOM   1711 N N   . ASN   C 1 39 ? 28.770  -35.316 33.926  1.00 50.04  ? 38  ASN   C N   1 
ATOM   1712 C CA  . ASN   C 1 39 ? 29.203  -34.256 33.025  1.00 50.74  ? 38  ASN   C CA  1 
ATOM   1713 C C   . ASN   C 1 39 ? 28.333  -34.204 31.763  1.00 52.71  ? 38  ASN   C C   1 
ATOM   1714 O O   . ASN   C 1 39 ? 28.811  -33.784 30.702  1.00 51.45  ? 38  ASN   C O   1 
ATOM   1715 C CB  . ASN   C 1 39 ? 30.682  -34.396 32.667  1.00 49.04  ? 38  ASN   C CB  1 
ATOM   1716 C CG  . ASN   C 1 39 ? 31.255  -33.158 32.012  1.00 66.29  ? 38  ASN   C CG  1 
ATOM   1717 O OD1 . ASN   C 1 39 ? 30.719  -32.052 32.165  1.00 80.08  ? 38  ASN   C OD1 1 
ATOM   1718 N ND2 . ASN   C 1 39 ? 32.349  -33.316 31.283  1.00 68.46  ? 38  ASN   C ND2 1 
ATOM   1719 N N   . LYS   C 1 40 ? 27.064  -34.631 31.869  1.00 45.09  ? 39  LYS   C N   1 
ATOM   1720 C CA  . LYS   C 1 40 ? 26.155  -34.552 30.732  1.00 42.11  ? 39  LYS   C CA  1 
ATOM   1721 C C   . LYS   C 1 40 ? 25.012  -33.596 31.050  1.00 45.78  ? 39  LYS   C C   1 
ATOM   1722 O O   . LYS   C 1 40 ? 24.580  -33.517 32.196  1.00 48.94  ? 39  LYS   C O   1 
ATOM   1723 C CB  . LYS   C 1 40 ? 25.480  -35.890 30.421  1.00 38.24  ? 39  LYS   C CB  1 
ATOM   1724 C CG  . LYS   C 1 40 ? 26.409  -37.032 30.119  1.00 41.78  ? 39  LYS   C CG  1 
ATOM   1725 C CD  . LYS   C 1 40 ? 27.423  -36.777 29.023  1.00 43.50  ? 39  LYS   C CD  1 
ATOM   1726 C CE  . LYS   C 1 40 ? 27.795  -38.098 28.417  1.00 52.05  ? 39  LYS   C CE  1 
ATOM   1727 N NZ  . LYS   C 1 40 ? 28.930  -37.887 27.513  1.00 56.44  ? 39  LYS   C NZ  1 
ATOM   1728 N N   . TYR   C 1 41 ? 24.518  -32.891 30.020  1.00 42.89  ? 40  TYR   C N   1 
ATOM   1729 C CA  . TYR   C 1 41 ? 23.348  -32.035 30.175  1.00 39.21  ? 40  TYR   C CA  1 
ATOM   1730 C C   . TYR   C 1 41 ? 22.105  -32.724 29.620  1.00 43.01  ? 40  TYR   C C   1 
ATOM   1731 O O   . TYR   C 1 41 ? 22.193  -33.513 28.666  1.00 39.49  ? 40  TYR   C O   1 
ATOM   1732 C CB  . TYR   C 1 41 ? 23.439  -30.773 29.314  1.00 40.61  ? 40  TYR   C CB  1 
ATOM   1733 C CG  . TYR   C 1 41 ? 24.593  -29.877 29.716  1.00 42.59  ? 40  TYR   C CG  1 
ATOM   1734 C CD1 . TYR   C 1 41 ? 25.886  -30.105 29.228  1.00 40.40  ? 40  TYR   C CD1 1 
ATOM   1735 C CD2 . TYR   C 1 41 ? 24.378  -28.805 30.580  1.00 42.94  ? 40  TYR   C CD2 1 
ATOM   1736 C CE1 . TYR   C 1 41 ? 26.939  -29.288 29.601  1.00 45.91  ? 40  TYR   C CE1 1 
ATOM   1737 C CE2 . TYR   C 1 41 ? 25.422  -27.958 30.920  1.00 44.91  ? 40  TYR   C CE2 1 
ATOM   1738 C CZ  . TYR   C 1 41 ? 26.698  -28.211 30.444  1.00 44.69  ? 40  TYR   C CZ  1 
ATOM   1739 O OH  . TYR   C 1 41 ? 27.718  -27.380 30.819  1.00 61.44  ? 40  TYR   C OH  1 
ATOM   1740 N N   . PRO   C 1 42 ? 20.922  -32.404 30.205  1.00 43.04  ? 41  PRO   C N   1 
ATOM   1741 C CA  . PRO   C 1 42 ? 19.640  -32.875 29.683  1.00 42.22  ? 41  PRO   C CA  1 
ATOM   1742 C C   . PRO   C 1 42 ? 19.285  -31.906 28.562  1.00 42.73  ? 41  PRO   C C   1 
ATOM   1743 O O   . PRO   C 1 42 ? 19.291  -30.687 28.766  1.00 40.13  ? 41  PRO   C O   1 
ATOM   1744 C CB  . PRO   C 1 42 ? 18.689  -32.798 30.882  1.00 37.41  ? 41  PRO   C CB  1 
ATOM   1745 C CG  . PRO   C 1 42 ? 19.303  -31.734 31.766  1.00 39.74  ? 41  PRO   C CG  1 
ATOM   1746 C CD  . PRO   C 1 42 ? 20.768  -31.562 31.411  1.00 40.16  ? 41  PRO   C CD  1 
ATOM   1747 N N   . ILE   C 1 43 ? 19.059  -32.490 27.375  1.00 42.60  ? 42  ILE   C N   1 
ATOM   1748 C CA  . ILE   C 1 43 ? 18.749  -31.760 26.160  1.00 38.56  ? 42  ILE   C CA  1 
ATOM   1749 C C   . ILE   C 1 43 ? 17.302  -32.058 25.773  1.00 41.74  ? 42  ILE   C C   1 
ATOM   1750 O O   . ILE   C 1 43 ? 16.849  -33.208 25.799  1.00 39.02  ? 42  ILE   C O   1 
ATOM   1751 C CB  . ILE   C 1 43 ? 19.747  -32.131 25.042  1.00 40.86  ? 42  ILE   C CB  1 
ATOM   1752 C CG1 . ILE   C 1 43 ? 21.233  -31.797 25.420  1.00 38.06  ? 42  ILE   C CG1 1 
ATOM   1753 C CG2 . ILE   C 1 43 ? 19.341  -31.524 23.694  1.00 35.97  ? 42  ILE   C CG2 1 
ATOM   1754 C CD1 . ILE   C 1 43 ? 21.456  -30.365 25.890  1.00 36.34  ? 42  ILE   C CD1 1 
ATOM   1755 N N   . PHE   C 1 44 ? 16.588  -31.000 25.370  1.00 41.60  ? 43  PHE   C N   1 
ATOM   1756 C CA  . PHE   C 1 44 ? 15.290  -31.142 24.737  1.00 38.58  ? 43  PHE   C CA  1 
ATOM   1757 C C   . PHE   C 1 44 ? 15.450  -30.720 23.279  1.00 36.77  ? 43  PHE   C C   1 
ATOM   1758 O O   . PHE   C 1 44 ? 16.022  -29.668 23.008  1.00 35.97  ? 43  PHE   C O   1 
ATOM   1759 C CB  . PHE   C 1 44 ? 14.300  -30.198 25.427  1.00 39.97  ? 43  PHE   C CB  1 
ATOM   1760 C CG  . PHE   C 1 44 ? 12.942  -30.102 24.747  1.00 40.37  ? 43  PHE   C CG  1 
ATOM   1761 C CD1 . PHE   C 1 44 ? 11.934  -31.044 25.003  1.00 44.96  ? 43  PHE   C CD1 1 
ATOM   1762 C CD2 . PHE   C 1 44 ? 12.656  -29.043 23.882  1.00 42.37  ? 43  PHE   C CD2 1 
ATOM   1763 C CE1 . PHE   C 1 44 ? 10.688  -30.951 24.381  1.00 46.39  ? 43  PHE   C CE1 1 
ATOM   1764 C CE2 . PHE   C 1 44 ? 11.417  -28.954 23.250  1.00 42.50  ? 43  PHE   C CE2 1 
ATOM   1765 C CZ  . PHE   C 1 44 ? 10.434  -29.901 23.507  1.00 51.57  ? 43  PHE   C CZ  1 
ATOM   1766 N N   . PHE   C 1 45 ? 14.950  -31.550 22.362  1.00 35.77  ? 44  PHE   C N   1 
ATOM   1767 C CA  . PHE   C 1 45 ? 15.142  -31.301 20.950  1.00 36.14  ? 44  PHE   C CA  1 
ATOM   1768 C C   . PHE   C 1 45 ? 13.894  -30.629 20.399  1.00 40.24  ? 44  PHE   C C   1 
ATOM   1769 O O   . PHE   C 1 45 ? 12.792  -31.162 20.543  1.00 36.37  ? 44  PHE   C O   1 
ATOM   1770 C CB  . PHE   C 1 45 ? 15.452  -32.585 20.187  1.00 35.28  ? 44  PHE   C CB  1 
ATOM   1771 C CG  . PHE   C 1 45 ? 16.824  -33.139 20.528  1.00 34.55  ? 44  PHE   C CG  1 
ATOM   1772 C CD1 . PHE   C 1 45 ? 17.947  -32.761 19.798  1.00 33.35  ? 44  PHE   C CD1 1 
ATOM   1773 C CD2 . PHE   C 1 45 ? 16.985  -34.000 21.609  1.00 34.15  ? 44  PHE   C CD2 1 
ATOM   1774 C CE1 . PHE   C 1 45 ? 19.202  -33.284 20.120  1.00 38.51  ? 44  PHE   C CE1 1 
ATOM   1775 C CE2 . PHE   C 1 45 ? 18.231  -34.541 21.916  1.00 37.32  ? 44  PHE   C CE2 1 
ATOM   1776 C CZ  . PHE   C 1 45 ? 19.336  -34.173 21.178  1.00 38.64  ? 44  PHE   C CZ  1 
ATOM   1777 N N   . PHE   C 1 46 ? 14.082  -29.473 19.742  1.00 36.46  ? 45  PHE   C N   1 
ATOM   1778 C CA  . PHE   C 1 46 ? 12.932  -28.852 19.104  1.00 35.59  ? 45  PHE   C CA  1 
ATOM   1779 C C   . PHE   C 1 46 ? 12.431  -29.709 17.947  1.00 36.26  ? 45  PHE   C C   1 
ATOM   1780 O O   . PHE   C 1 46 ? 13.192  -30.456 17.321  1.00 38.55  ? 45  PHE   C O   1 
ATOM   1781 C CB  . PHE   C 1 46 ? 13.129  -27.413 18.625  1.00 34.32  ? 45  PHE   C CB  1 
ATOM   1782 C CG  . PHE   C 1 46 ? 13.446  -26.438 19.745  1.00 32.50  ? 45  PHE   C CG  1 
ATOM   1783 C CD1 . PHE   C 1 46 ? 12.444  -25.998 20.608  1.00 34.13  ? 45  PHE   C CD1 1 
ATOM   1784 C CD2 . PHE   C 1 46 ? 14.745  -25.973 19.935  1.00 33.65  ? 45  PHE   C CD2 1 
ATOM   1785 C CE1 . PHE   C 1 46 ? 12.743  -25.122 21.644  1.00 37.43  ? 45  PHE   C CE1 1 
ATOM   1786 C CE2 . PHE   C 1 46 ? 15.030  -25.087 20.965  1.00 34.43  ? 45  PHE   C CE2 1 
ATOM   1787 C CZ  . PHE   C 1 46 ? 14.033  -24.650 21.813  1.00 35.27  ? 45  PHE   C CZ  1 
ATOM   1788 N N   . GLY   C 1 47 ? 11.146  -29.535 17.634  1.00 31.96  ? 46  GLY   C N   1 
ATOM   1789 C CA  . GLY   C 1 47 ? 10.592  -30.223 16.484  1.00 39.45  ? 46  GLY   C CA  1 
ATOM   1790 C C   . GLY   C 1 47 ? 10.191  -31.653 16.835  1.00 44.45  ? 46  GLY   C C   1 
ATOM   1791 O O   . GLY   C 1 47 ? 9.026   -32.023 16.688  1.00 43.92  ? 46  GLY   C O   1 
ATOM   1792 N N   . THR   C 1 48 ? 11.157  -32.472 17.268  1.00 45.74  ? 47  THR   C N   1 
ATOM   1793 C CA  . THR   C 1 48 ? 10.769  -33.821 17.669  1.00 43.19  ? 47  THR   C CA  1 
ATOM   1794 C C   . THR   C 1 48 ? 10.250  -33.799 19.103  1.00 39.18  ? 47  THR   C C   1 
ATOM   1795 O O   . THR   C 1 48 ? 9.488   -34.686 19.487  1.00 47.16  ? 47  THR   C O   1 
ATOM   1796 C CB  . THR   C 1 48 ? 11.900  -34.835 17.538  1.00 39.58  ? 47  THR   C CB  1 
ATOM   1797 O OG1 . THR   C 1 48 ? 12.801  -34.329 18.519  1.00 42.01  ? 47  THR   C OG1 1 
ATOM   1798 C CG2 . THR   C 1 48 ? 12.451  -34.967 16.129  1.00 37.97  ? 47  THR   C CG2 1 
ATOM   1799 N N   . HIS   C 1 49 ? 10.691  -32.807 19.891  1.00 37.08  ? 48  HIS   C N   1 
ATOM   1800 C CA  . HIS   C 1 49 ? 10.372  -32.671 21.310  1.00 46.06  ? 48  HIS   C CA  1 
ATOM   1801 C C   . HIS   C 1 49 ? 10.774  -33.910 22.119  1.00 47.02  ? 48  HIS   C C   1 
ATOM   1802 O O   . HIS   C 1 49 ? 10.089  -34.248 23.080  1.00 47.22  ? 48  HIS   C O   1 
ATOM   1803 C CB  . HIS   C 1 49 ? 8.886   -32.362 21.549  1.00 44.46  ? 48  HIS   C CB  1 
ATOM   1804 C CG  . HIS   C 1 49 ? 8.317   -31.362 20.605  1.00 47.26  ? 48  HIS   C CG  1 
ATOM   1805 N ND1 . HIS   C 1 49 ? 7.168   -31.630 19.892  1.00 50.61  ? 48  HIS   C ND1 1 
ATOM   1806 C CD2 . HIS   C 1 49 ? 8.735   -30.155 20.215  1.00 45.65  ? 48  HIS   C CD2 1 
ATOM   1807 C CE1 . HIS   C 1 49 ? 6.899   -30.599 19.101  1.00 50.94  ? 48  HIS   C CE1 1 
ATOM   1808 N NE2 . HIS   C 1 49 ? 7.831   -29.692 19.290  1.00 52.30  ? 48  HIS   C NE2 1 
ATOM   1809 N N   . GLU   C 1 50 ? 11.886  -34.563 21.748  1.00 45.55  ? 49  GLU   C N   1 
ATOM   1810 C CA  . GLU   C 1 50 ? 12.419  -35.674 22.528  1.00 45.79  ? 49  GLU   C CA  1 
ATOM   1811 C C   . GLU   C 1 50 ? 13.554  -35.163 23.412  1.00 44.67  ? 49  GLU   C C   1 
ATOM   1812 O O   . GLU   C 1 50 ? 13.930  -33.999 23.305  1.00 42.94  ? 49  GLU   C O   1 
ATOM   1813 C CB  . GLU   C 1 50 ? 12.887  -36.779 21.588  1.00 48.41  ? 49  GLU   C CB  1 
ATOM   1814 C CG  . GLU   C 1 50 ? 11.769  -37.342 20.717  1.00 54.08  ? 49  GLU   C CG  1 
ATOM   1815 C CD  . GLU   C 1 50 ? 12.415  -38.178 19.629  1.00 66.41  ? 49  GLU   C CD  1 
ATOM   1816 O OE1 . GLU   C 1 50 ? 13.629  -38.463 19.761  1.00 66.43  ? 49  GLU   C OE1 1 
ATOM   1817 O OE2 . GLU   C 1 50 ? 11.728  -38.511 18.640  1.00 70.33  ? 49  GLU   C OE2 1 
ATOM   1818 N N   . THR   C 1 51 ? 14.062  -36.018 24.325  1.00 44.55  ? 50  THR   C N   1 
ATOM   1819 C CA  . THR   C 1 51 ? 15.109  -35.617 25.268  1.00 45.58  ? 50  THR   C CA  1 
ATOM   1820 C C   . THR   C 1 51 ? 16.286  -36.594 25.181  1.00 41.78  ? 50  THR   C C   1 
ATOM   1821 O O   . THR   C 1 51 ? 16.130  -37.704 24.689  1.00 43.91  ? 50  THR   C O   1 
ATOM   1822 C CB  . THR   C 1 51 ? 14.562  -35.548 26.698  1.00 46.85  ? 50  THR   C CB  1 
ATOM   1823 O OG1 . THR   C 1 51 ? 13.894  -36.796 26.882  1.00 46.78  ? 50  THR   C OG1 1 
ATOM   1824 C CG2 . THR   C 1 51 ? 13.650  -34.363 26.968  1.00 45.31  ? 50  THR   C CG2 1 
ATOM   1825 N N   . ALA   C 1 52 ? 17.473  -36.159 25.622  1.00 42.18  ? 51  ALA   C N   1 
ATOM   1826 C CA  . ALA   C 1 52 ? 18.656  -37.007 25.691  1.00 41.87  ? 51  ALA   C CA  1 
ATOM   1827 C C   . ALA   C 1 52 ? 19.690  -36.337 26.588  1.00 44.88  ? 51  ALA   C C   1 
ATOM   1828 O O   . ALA   C 1 52 ? 19.522  -35.184 26.958  1.00 49.58  ? 51  ALA   C O   1 
ATOM   1829 C CB  . ALA   C 1 52 ? 19.224  -37.279 24.309  1.00 38.03  ? 51  ALA   C CB  1 
ATOM   1830 N N   . PHE   C 1 53 ? 20.741  -37.081 26.960  1.00 47.85  ? 52  PHE   C N   1 
ATOM   1831 C CA  . PHE   C 1 53 ? 21.857  -36.544 27.725  1.00 47.95  ? 52  PHE   C CA  1 
ATOM   1832 C C   . PHE   C 1 53 ? 23.026  -36.391 26.766  1.00 44.63  ? 52  PHE   C C   1 
ATOM   1833 O O   . PHE   C 1 53 ? 23.333  -37.335 26.048  1.00 45.28  ? 52  PHE   C O   1 
ATOM   1834 C CB  . PHE   C 1 53 ? 22.204  -37.489 28.883  1.00 46.14  ? 52  PHE   C CB  1 
ATOM   1835 C CG  . PHE   C 1 53 ? 21.272  -37.305 30.066  1.00 48.80  ? 52  PHE   C CG  1 
ATOM   1836 C CD1 . PHE   C 1 53 ? 21.096  -36.052 30.650  1.00 50.18  ? 52  PHE   C CD1 1 
ATOM   1837 C CD2 . PHE   C 1 53 ? 20.507  -38.368 30.541  1.00 60.47  ? 52  PHE   C CD2 1 
ATOM   1838 C CE1 . PHE   C 1 53 ? 20.206  -35.881 31.707  1.00 56.36  ? 52  PHE   C CE1 1 
ATOM   1839 C CE2 . PHE   C 1 53 ? 19.618  -38.189 31.595  1.00 56.37  ? 52  PHE   C CE2 1 
ATOM   1840 C CZ  . PHE   C 1 53 ? 19.458  -36.945 32.169  1.00 52.68  ? 52  PHE   C CZ  1 
ATOM   1841 N N   . LEU   C 1 54 ? 23.643  -35.200 26.753  1.00 39.97  ? 53  LEU   C N   1 
ATOM   1842 C CA  . LEU   C 1 54 ? 24.761  -34.892 25.872  1.00 38.39  ? 53  LEU   C CA  1 
ATOM   1843 C C   . LEU   C 1 54 ? 25.835  -34.160 26.672  1.00 42.72  ? 53  LEU   C C   1 
ATOM   1844 O O   . LEU   C 1 54 ? 25.518  -33.395 27.583  1.00 40.96  ? 53  LEU   C O   1 
ATOM   1845 C CB  . LEU   C 1 54 ? 24.308  -34.064 24.665  1.00 39.33  ? 53  LEU   C CB  1 
ATOM   1846 C CG  . LEU   C 1 54 ? 23.516  -34.821 23.589  1.00 43.88  ? 53  LEU   C CG  1 
ATOM   1847 C CD1 . LEU   C 1 54 ? 23.123  -33.887 22.462  1.00 38.11  ? 53  LEU   C CD1 1 
ATOM   1848 C CD2 . LEU   C 1 54 ? 24.303  -35.999 23.013  1.00 44.38  ? 53  LEU   C CD2 1 
ATOM   1849 N N   . GLY   C 1 55 ? 27.101  -34.438 26.336  1.00 42.91  ? 54  GLY   C N   1 
ATOM   1850 C CA  . GLY   C 1 55 ? 28.233  -33.722 26.891  1.00 38.59  ? 54  GLY   C CA  1 
ATOM   1851 C C   . GLY   C 1 55 ? 28.456  -32.411 26.147  1.00 44.52  ? 54  GLY   C C   1 
ATOM   1852 O O   . GLY   C 1 55 ? 27.961  -32.236 25.021  1.00 40.37  ? 54  GLY   C O   1 
ATOM   1853 N N   . PRO   C 1 56 ? 29.215  -31.463 26.748  1.00 45.93  ? 55  PRO   C N   1 
ATOM   1854 C CA  . PRO   C 1 56 ? 29.251  -30.078 26.268  1.00 53.70  ? 55  PRO   C CA  1 
ATOM   1855 C C   . PRO   C 1 56 ? 29.850  -29.945 24.871  1.00 51.05  ? 55  PRO   C C   1 
ATOM   1856 O O   . PRO   C 1 56 ? 29.518  -29.018 24.136  1.00 55.13  ? 55  PRO   C O   1 
ATOM   1857 C CB  . PRO   C 1 56 ? 30.096  -29.348 27.353  1.00 57.24  ? 55  PRO   C CB  1 
ATOM   1858 C CG  . PRO   C 1 56 ? 31.012  -30.441 27.896  1.00 51.42  ? 55  PRO   C CG  1 
ATOM   1859 C CD  . PRO   C 1 56 ? 30.110  -31.678 27.906  1.00 48.53  ? 55  PRO   C CD  1 
ATOM   1860 N N   . LYS   C 1 57 ? 30.719  -30.894 24.519  1.00 45.51  ? 56  LYS   C N   1 
ATOM   1861 C CA  . LYS   C 1 57 ? 31.372  -30.937 23.220  1.00 50.62  ? 56  LYS   C CA  1 
ATOM   1862 C C   . LYS   C 1 57 ? 30.338  -31.112 22.109  1.00 50.78  ? 56  LYS   C C   1 
ATOM   1863 O O   . LYS   C 1 57 ? 30.594  -30.784 20.950  1.00 49.61  ? 56  LYS   C O   1 
ATOM   1864 C CB  . LYS   C 1 57 ? 32.273  -32.178 23.162  1.00 56.89  ? 56  LYS   C CB  1 
ATOM   1865 N N   . ASP   C 1 58 ? 29.182  -31.672 22.474  1.00 46.80  ? 57  ASP   C N   1 
ATOM   1866 C CA  . ASP   C 1 58 ? 28.148  -32.010 21.509  1.00 43.56  ? 57  ASP   C CA  1 
ATOM   1867 C C   . ASP   C 1 58 ? 27.198  -30.836 21.344  1.00 43.40  ? 57  ASP   C C   1 
ATOM   1868 O O   . ASP   C 1 58 ? 26.202  -30.952 20.638  1.00 42.44  ? 57  ASP   C O   1 
ATOM   1869 C CB  . ASP   C 1 58 ? 27.393  -33.247 21.951  1.00 42.34  ? 57  ASP   C CB  1 
ATOM   1870 C CG  . ASP   C 1 58 ? 28.201  -34.527 21.861  1.00 45.17  ? 57  ASP   C CG  1 
ATOM   1871 O OD1 . ASP   C 1 58 ? 29.156  -34.541 21.065  1.00 48.31  ? 57  ASP   C OD1 1 
ATOM   1872 O OD2 . ASP   C 1 58 ? 27.882  -35.478 22.604  1.00 49.97  ? 57  ASP   C OD2 1 
ATOM   1873 N N   . LEU   C 1 59 ? 27.535  -29.706 21.979  1.00 38.91  ? 58  LEU   C N   1 
ATOM   1874 C CA  . LEU   C 1 59 ? 26.615  -28.585 22.100  1.00 44.36  ? 58  LEU   C CA  1 
ATOM   1875 C C   . LEU   C 1 59 ? 27.258  -27.322 21.544  1.00 45.93  ? 58  LEU   C C   1 
ATOM   1876 O O   . LEU   C 1 59 ? 28.476  -27.182 21.627  1.00 48.81  ? 58  LEU   C O   1 
ATOM   1877 C CB  . LEU   C 1 59 ? 26.290  -28.434 23.579  1.00 41.71  ? 58  LEU   C CB  1 
ATOM   1878 C CG  . LEU   C 1 59 ? 25.634  -29.647 24.240  1.00 39.10  ? 58  LEU   C CG  1 
ATOM   1879 C CD1 . LEU   C 1 59 ? 25.297  -29.228 25.653  1.00 39.51  ? 58  LEU   C CD1 1 
ATOM   1880 C CD2 . LEU   C 1 59 ? 24.360  -30.081 23.505  1.00 32.26  ? 58  LEU   C CD2 1 
ATOM   1881 N N   . PHE   C 1 60 ? 26.420  -26.444 20.967  1.00 44.51  ? 59  PHE   C N   1 
ATOM   1882 C CA  . PHE   C 1 60 ? 26.831  -25.246 20.244  1.00 45.69  ? 59  PHE   C CA  1 
ATOM   1883 C C   . PHE   C 1 60 ? 25.813  -24.129 20.492  1.00 42.71  ? 59  PHE   C C   1 
ATOM   1884 O O   . PHE   C 1 60 ? 24.642  -24.267 20.134  1.00 41.32  ? 59  PHE   C O   1 
ATOM   1885 C CB  . PHE   C 1 60 ? 27.003  -25.540 18.751  1.00 43.64  ? 59  PHE   C CB  1 
ATOM   1886 C CG  . PHE   C 1 60 ? 27.985  -26.657 18.434  1.00 43.04  ? 59  PHE   C CG  1 
ATOM   1887 C CD1 . PHE   C 1 60 ? 27.564  -27.985 18.370  1.00 43.05  ? 59  PHE   C CD1 1 
ATOM   1888 C CD2 . PHE   C 1 60 ? 29.332  -26.382 18.193  1.00 50.41  ? 59  PHE   C CD2 1 
ATOM   1889 C CE1 . PHE   C 1 60 ? 28.461  -29.013 18.105  1.00 41.64  ? 59  PHE   C CE1 1 
ATOM   1890 C CE2 . PHE   C 1 60 ? 30.227  -27.411 17.909  1.00 48.48  ? 59  PHE   C CE2 1 
ATOM   1891 C CZ  . PHE   C 1 60 ? 29.787  -28.723 17.865  1.00 50.43  ? 59  PHE   C CZ  1 
ATOM   1892 N N   . PRO   C 1 61 ? 26.192  -22.990 21.132  1.00 44.70  ? 60  PRO   C N   1 
ATOM   1893 C CA  . PRO   C 1 61 ? 25.221  -21.930 21.403  1.00 43.20  ? 60  PRO   C CA  1 
ATOM   1894 C C   . PRO   C 1 61 ? 24.614  -21.484 20.077  1.00 43.87  ? 60  PRO   C C   1 
ATOM   1895 O O   . PRO   C 1 61 ? 25.303  -21.432 19.053  1.00 46.29  ? 60  PRO   C O   1 
ATOM   1896 C CB  . PRO   C 1 61 ? 25.964  -20.783 22.130  1.00 43.37  ? 60  PRO   C CB  1 
ATOM   1897 C CG  . PRO   C 1 61 ? 27.423  -21.240 22.188  1.00 42.14  ? 60  PRO   C CG  1 
ATOM   1898 C CD  . PRO   C 1 61 ? 27.558  -22.633 21.565  1.00 46.60  ? 60  PRO   C CD  1 
ATOM   1899 N N   . TYR   C 1 62 ? 23.304  -21.204 20.150  1.00 49.38  ? 61  TYR   C N   1 
ATOM   1900 C CA  . TYR   C 1 62 ? 22.406  -21.005 19.028  1.00 49.93  ? 61  TYR   C CA  1 
ATOM   1901 C C   . TYR   C 1 62 ? 22.768  -19.746 18.248  1.00 56.26  ? 61  TYR   C C   1 
ATOM   1902 O O   . TYR   C 1 62 ? 22.868  -19.805 17.028  1.00 55.72  ? 61  TYR   C O   1 
ATOM   1903 C CB  . TYR   C 1 62 ? 20.946  -20.976 19.485  1.00 53.17  ? 61  TYR   C CB  1 
ATOM   1904 C CG  . TYR   C 1 62 ? 19.983  -20.615 18.365  1.00 53.88  ? 61  TYR   C CG  1 
ATOM   1905 C CD1 . TYR   C 1 62 ? 19.852  -21.433 17.241  1.00 53.05  ? 61  TYR   C CD1 1 
ATOM   1906 C CD2 . TYR   C 1 62 ? 19.194  -19.466 18.445  1.00 53.13  ? 61  TYR   C CD2 1 
ATOM   1907 C CE1 . TYR   C 1 62 ? 18.967  -21.100 16.223  1.00 54.01  ? 61  TYR   C CE1 1 
ATOM   1908 C CE2 . TYR   C 1 62 ? 18.303  -19.130 17.439  1.00 50.46  ? 61  TYR   C CE2 1 
ATOM   1909 C CZ  . TYR   C 1 62 ? 18.195  -19.949 16.324  1.00 49.19  ? 61  TYR   C CZ  1 
ATOM   1910 O OH  . TYR   C 1 62 ? 17.330  -19.608 15.332  1.00 46.40  ? 61  TYR   C OH  1 
ATOM   1911 N N   . ASP   C 1 63 ? 22.972  -18.624 18.950  1.00 59.83  ? 62  ASP   C N   1 
ATOM   1912 C CA  . ASP   C 1 63 ? 23.306  -17.373 18.283  1.00 64.31  ? 62  ASP   C CA  1 
ATOM   1913 C C   . ASP   C 1 63 ? 24.660  -17.480 17.587  1.00 58.67  ? 62  ASP   C C   1 
ATOM   1914 O O   . ASP   C 1 63 ? 24.850  -16.921 16.504  1.00 59.72  ? 62  ASP   C O   1 
ATOM   1915 C CB  . ASP   C 1 63 ? 23.152  -16.177 19.207  1.00 72.06  ? 62  ASP   C CB  1 
ATOM   1916 C CG  . ASP   C 1 63 ? 21.771  -15.542 19.147  1.00 91.62  ? 62  ASP   C CG  1 
ATOM   1917 O OD1 . ASP   C 1 63 ? 20.944  -15.856 20.032  1.00 89.49  ? 62  ASP   C OD1 1 
ATOM   1918 O OD2 . ASP   C 1 63 ? 21.533  -14.750 18.201  1.00 94.01  ? 62  ASP   C OD2 1 
ATOM   1919 N N   . LYS   C 1 64 ? 25.577  -18.232 18.202  1.00 44.47  ? 63  LYS   C N   1 
ATOM   1920 C CA  . LYS   C 1 64 ? 26.944  -18.338 17.715  1.00 46.23  ? 63  LYS   C CA  1 
ATOM   1921 C C   . LYS   C 1 64 ? 27.021  -19.196 16.456  1.00 46.99  ? 63  LYS   C C   1 
ATOM   1922 O O   . LYS   C 1 64 ? 27.827  -18.905 15.578  1.00 47.26  ? 63  LYS   C O   1 
ATOM   1923 C CB  . LYS   C 1 64 ? 27.909  -18.891 18.774  1.00 48.07  ? 63  LYS   C CB  1 
ATOM   1924 N N   . SER   C 1 65 ? 26.187  -20.248 16.363  1.00 45.85  ? 64  SER   C N   1 
ATOM   1925 C CA  . SER   C 1 65 ? 26.404  -21.240 15.315  1.00 43.24  ? 64  SER   C CA  1 
ATOM   1926 C C   . SER   C 1 65 ? 25.226  -21.353 14.336  1.00 41.97  ? 64  SER   C C   1 
ATOM   1927 O O   . SER   C 1 65 ? 25.273  -22.176 13.417  1.00 39.84  ? 64  SER   C O   1 
ATOM   1928 C CB  . SER   C 1 65 ? 26.784  -22.590 15.910  1.00 45.55  ? 64  SER   C CB  1 
ATOM   1929 O OG  . SER   C 1 65 ? 25.644  -23.154 16.556  1.00 48.83  ? 64  SER   C OG  1 
ATOM   1930 N N   . LYS   C 1 66 ? 24.159  -20.559 14.536  1.00 36.72  ? 65  LYS   C N   1 
ATOM   1931 C CA  . LYS   C 1 66 ? 22.993  -20.682 13.667  1.00 41.76  ? 65  LYS   C CA  1 
ATOM   1932 C C   . LYS   C 1 66 ? 23.375  -20.450 12.207  1.00 41.38  ? 65  LYS   C C   1 
ATOM   1933 O O   . LYS   C 1 66 ? 22.873  -21.164 11.351  1.00 45.60  ? 65  LYS   C O   1 
ATOM   1934 C CB  . LYS   C 1 66 ? 21.741  -19.884 14.043  1.00 45.21  ? 65  LYS   C CB  1 
ATOM   1935 C CG  . LYS   C 1 66 ? 21.940  -18.386 14.066  1.00 44.21  ? 65  LYS   C CG  1 
ATOM   1936 C CD  . LYS   C 1 66 ? 20.706  -17.690 14.620  1.00 51.92  ? 65  LYS   C CD  1 
ATOM   1937 C CE  . LYS   C 1 66 ? 20.792  -16.206 14.491  1.00 48.08  ? 65  LYS   C CE  1 
ATOM   1938 N NZ  . LYS   C 1 66 ? 19.685  -15.654 15.265  1.00 57.24  ? 65  LYS   C NZ  1 
ATOM   1939 N N   . ASP   C 1 67 ? 24.294  -19.510 11.925  1.00 43.93  ? 66  ASP   C N   1 
ATOM   1940 C CA  . ASP   C 1 67 ? 24.711  -19.246 10.546  1.00 46.48  ? 66  ASP   C CA  1 
ATOM   1941 C C   . ASP   C 1 67 ? 25.160  -20.543 9.859   1.00 44.00  ? 66  ASP   C C   1 
ATOM   1942 O O   . ASP   C 1 67 ? 24.977  -20.702 8.658   1.00 42.45  ? 66  ASP   C O   1 
ATOM   1943 C CB  . ASP   C 1 67 ? 25.619  -18.022 10.402  1.00 46.82  ? 66  ASP   C CB  1 
ATOM   1944 C CG  . ASP   C 1 67 ? 27.034  -18.089 10.977  1.00 61.69  ? 66  ASP   C CG  1 
ATOM   1945 O OD1 . ASP   C 1 67 ? 27.468  -19.190 11.408  1.00 60.61  ? 66  ASP   C OD1 1 
ATOM   1946 O OD2 . ASP   C 1 67 ? 27.709  -17.023 11.009  1.00 61.45  ? 66  ASP   C OD2 1 
ATOM   1947 N N   . LYS   C 1 68 ? 25.699  -21.500 10.630  1.00 39.04  ? 67  LYS   C N   1 
ATOM   1948 C CA  . LYS   C 1 68 ? 26.235  -22.736 10.071  1.00 39.83  ? 67  LYS   C CA  1 
ATOM   1949 C C   . LYS   C 1 68 ? 25.226  -23.902 10.133  1.00 38.73  ? 67  LYS   C C   1 
ATOM   1950 O O   . LYS   C 1 68 ? 25.076  -24.623 9.147   1.00 41.72  ? 67  LYS   C O   1 
ATOM   1951 C CB  . LYS   C 1 68 ? 27.580  -23.010 10.756  1.00 39.07  ? 67  LYS   C CB  1 
ATOM   1952 C CG  . LYS   C 1 68 ? 28.204  -24.364 10.532  1.00 47.41  ? 67  LYS   C CG  1 
ATOM   1953 C CD  . LYS   C 1 68 ? 29.523  -24.520 11.288  1.00 55.79  ? 67  LYS   C CD  1 
ATOM   1954 C CE  . LYS   C 1 68 ? 30.205  -25.822 10.990  1.00 63.51  ? 67  LYS   C CE  1 
ATOM   1955 N NZ  . LYS   C 1 68 ? 30.358  -26.055 9.546   1.00 63.93  ? 67  LYS   C NZ  1 
ATOM   1956 N N   . TYR   C 1 69 ? 24.537  -24.103 11.274  1.00 34.52  ? 68  TYR   C N   1 
ATOM   1957 C CA  . TYR   C 1 69 ? 23.677  -25.277 11.424  1.00 37.90  ? 68  TYR   C CA  1 
ATOM   1958 C C   . TYR   C 1 69 ? 22.204  -24.943 11.181  1.00 39.08  ? 68  TYR   C C   1 
ATOM   1959 O O   . TYR   C 1 69 ? 21.388  -25.841 11.018  1.00 36.79  ? 68  TYR   C O   1 
ATOM   1960 C CB  . TYR   C 1 69 ? 23.807  -25.885 12.827  1.00 34.50  ? 68  TYR   C CB  1 
ATOM   1961 C CG  . TYR   C 1 69 ? 25.231  -26.305 13.160  1.00 36.52  ? 68  TYR   C CG  1 
ATOM   1962 C CD1 . TYR   C 1 69 ? 25.987  -27.060 12.267  1.00 39.50  ? 68  TYR   C CD1 1 
ATOM   1963 C CD2 . TYR   C 1 69 ? 25.821  -25.941 14.367  1.00 45.75  ? 68  TYR   C CD2 1 
ATOM   1964 C CE1 . TYR   C 1 69 ? 27.285  -27.462 12.567  1.00 38.09  ? 68  TYR   C CE1 1 
ATOM   1965 C CE2 . TYR   C 1 69 ? 27.115  -26.343 14.679  1.00 43.54  ? 68  TYR   C CE2 1 
ATOM   1966 C CZ  . TYR   C 1 69 ? 27.852  -27.088 13.772  1.00 42.37  ? 68  TYR   C CZ  1 
ATOM   1967 O OH  . TYR   C 1 69 ? 29.137  -27.443 14.091  1.00 47.27  ? 68  TYR   C OH  1 
ATOM   1968 N N   . GLY   C 1 70 ? 21.857  -23.658 11.248  1.00 36.33  ? 69  GLY   C N   1 
ATOM   1969 C CA  . GLY   C 1 70 ? 20.464  -23.270 11.129  1.00 39.66  ? 69  GLY   C CA  1 
ATOM   1970 C C   . GLY   C 1 70 ? 20.116  -23.117 9.660   1.00 43.61  ? 69  GLY   C C   1 
ATOM   1971 O O   . GLY   C 1 70 ? 20.015  -21.999 9.169   1.00 43.71  ? 69  GLY   C O   1 
ATOM   1972 N N   . LYS   C 1 71 ? 20.038  -24.259 8.966   1.00 41.42  ? 70  LYS   C N   1 
ATOM   1973 C CA  . LYS   C 1 71 ? 19.645  -24.332 7.566   1.00 41.89  ? 70  LYS   C CA  1 
ATOM   1974 C C   . LYS   C 1 71 ? 18.724  -25.536 7.449   1.00 41.23  ? 70  LYS   C C   1 
ATOM   1975 O O   . LYS   C 1 71 ? 18.886  -26.490 8.206   1.00 41.79  ? 70  LYS   C O   1 
ATOM   1976 C CB  . LYS   C 1 71 ? 20.841  -24.549 6.630   1.00 40.35  ? 70  LYS   C CB  1 
ATOM   1977 C CG  . LYS   C 1 71 ? 21.923  -25.444 7.235   1.00 46.14  ? 70  LYS   C CG  1 
ATOM   1978 C CD  . LYS   C 1 71 ? 23.042  -26.011 6.372   1.00 56.65  ? 70  LYS   C CD  1 
ATOM   1979 C CE  . LYS   C 1 71 ? 23.954  -26.909 7.169   1.00 56.55  ? 70  LYS   C CE  1 
ATOM   1980 N N   . PRO   C 1 72 ? 17.709  -25.520 6.553   1.00 36.67  ? 71  PRO   C N   1 
ATOM   1981 C CA  . PRO   C 1 72 ? 16.749  -26.619 6.508   1.00 33.30  ? 71  PRO   C CA  1 
ATOM   1982 C C   . PRO   C 1 72 ? 17.392  -27.967 6.195   1.00 39.63  ? 71  PRO   C C   1 
ATOM   1983 O O   . PRO   C 1 72 ? 18.414  -28.031 5.504   1.00 37.90  ? 71  PRO   C O   1 
ATOM   1984 C CB  . PRO   C 1 72 ? 15.807  -26.184 5.396   1.00 34.76  ? 71  PRO   C CB  1 
ATOM   1985 C CG  . PRO   C 1 72 ? 15.881  -24.674 5.512   1.00 34.06  ? 71  PRO   C CG  1 
ATOM   1986 C CD  . PRO   C 1 72 ? 17.380  -24.415 5.633   1.00 34.18  ? 71  PRO   C CD  1 
ATOM   1987 N N   . ASN   C 1 73 ? 16.759  -29.037 6.672   1.00 37.17  ? 72  ASN   C N   1 
ATOM   1988 C CA  . ASN   C 1 73 ? 16.998  -30.322 6.035   1.00 45.68  ? 72  ASN   C CA  1 
ATOM   1989 C C   . ASN   C 1 73 ? 15.768  -31.197 6.208   1.00 35.38  ? 72  ASN   C C   1 
ATOM   1990 O O   . ASN   C 1 73 ? 14.808  -30.794 6.857   1.00 36.11  ? 72  ASN   C O   1 
ATOM   1991 C CB  . ASN   C 1 73 ? 18.326  -30.992 6.386   1.00 48.45  ? 72  ASN   C CB  1 
ATOM   1992 C CG  . ASN   C 1 73 ? 18.322  -31.616 7.760   1.00 46.80  ? 72  ASN   C CG  1 
ATOM   1993 O OD1 . ASN   C 1 73 ? 17.498  -32.490 8.075   1.00 48.56  ? 72  ASN   C OD1 1 
ATOM   1994 N ND2 . ASN   C 1 73 ? 19.253  -31.174 8.581   1.00 47.71  ? 72  ASN   C ND2 1 
ATOM   1995 N N   . LYS   C 1 74 ? 15.843  -32.391 5.617   1.00 39.75  ? 73  LYS   C N   1 
ATOM   1996 C CA  . LYS   C 1 74 ? 14.647  -33.170 5.337   1.00 38.88  ? 73  LYS   C CA  1 
ATOM   1997 C C   . LYS   C 1 74 ? 14.377  -34.159 6.466   1.00 40.39  ? 73  LYS   C C   1 
ATOM   1998 O O   . LYS   C 1 74 ? 13.395  -34.905 6.399   1.00 45.91  ? 73  LYS   C O   1 
ATOM   1999 C CB  . LYS   C 1 74 ? 14.757  -33.840 3.956   1.00 35.68  ? 73  LYS   C CB  1 
ATOM   2000 N N   . ARG   C 1 75 ? 15.250  -34.176 7.489   1.00 38.61  ? 74  ARG   C N   1 
ATOM   2001 C CA  . ARG   C 1 75 ? 15.067  -35.114 8.592   1.00 36.59  ? 74  ARG   C CA  1 
ATOM   2002 C C   . ARG   C 1 75 ? 13.798  -34.748 9.354   1.00 43.41  ? 74  ARG   C C   1 
ATOM   2003 O O   . ARG   C 1 75 ? 13.520  -33.564 9.601   1.00 37.46  ? 74  ARG   C O   1 
ATOM   2004 C CB  . ARG   C 1 75 ? 16.239  -35.261 9.578   1.00 46.35  ? 74  ARG   C CB  1 
ATOM   2005 C CG  . ARG   C 1 75 ? 17.609  -35.453 8.939   1.00 51.88  ? 74  ARG   C CG  1 
ATOM   2006 C CD  . ARG   C 1 75 ? 17.853  -36.817 8.298   1.00 51.73  ? 74  ARG   C CD  1 
ATOM   2007 N NE  . ARG   C 1 75 ? 17.827  -37.821 9.366   1.00 54.19  ? 74  ARG   C NE  1 
ATOM   2008 C CZ  . ARG   C 1 75 ? 18.900  -38.312 9.986   1.00 47.35  ? 74  ARG   C CZ  1 
ATOM   2009 N NH1 . ARG   C 1 75 ? 18.729  -39.057 11.070  1.00 44.92  ? 74  ARG   C NH1 1 
ATOM   2010 N NH2 . ARG   C 1 75 ? 20.113  -37.999 9.554   1.00 42.06  ? 74  ARG   C NH2 1 
ATOM   2011 N N   . LYS   C 1 76 ? 13.090  -35.808 9.772   1.00 42.72  ? 75  LYS   C N   1 
ATOM   2012 C CA  . LYS   C 1 76 ? 11.791  -35.709 10.408  1.00 45.50  ? 75  LYS   C CA  1 
ATOM   2013 C C   . LYS   C 1 76 ? 11.852  -34.750 11.594  1.00 43.81  ? 75  LYS   C C   1 
ATOM   2014 O O   . LYS   C 1 76 ? 12.648  -34.946 12.518  1.00 35.93  ? 75  LYS   C O   1 
ATOM   2015 C CB  . LYS   C 1 76 ? 11.174  -37.076 10.739  1.00 47.93  ? 75  LYS   C CB  1 
ATOM   2016 C CG  . LYS   C 1 76 ? 9.670   -36.964 11.000  1.00 55.91  ? 75  LYS   C CG  1 
ATOM   2017 C CD  . LYS   C 1 76 ? 8.913   -38.266 11.245  1.00 65.76  ? 75  LYS   C CD  1 
ATOM   2018 C CE  . LYS   C 1 76 ? 7.768   -38.085 12.196  1.00 63.80  ? 75  LYS   C CE  1 
ATOM   2019 N NZ  . LYS   C 1 76 ? 7.227   -39.373 12.633  1.00 72.56  ? 75  LYS   C NZ  1 
ATOM   2020 N N   . GLY   C 1 77 ? 10.984  -33.723 11.556  1.00 44.17  ? 76  GLY   C N   1 
ATOM   2021 C CA  . GLY   C 1 77 ? 10.811  -32.820 12.685  1.00 38.22  ? 76  GLY   C CA  1 
ATOM   2022 C C   . GLY   C 1 77 ? 11.801  -31.649 12.662  1.00 35.72  ? 76  GLY   C C   1 
ATOM   2023 O O   . GLY   C 1 77 ? 11.652  -30.691 13.419  1.00 38.56  ? 76  GLY   C O   1 
ATOM   2024 N N   . PHE   C 1 78 ? 12.816  -31.710 11.800  1.00 36.33  ? 77  PHE   C N   1 
ATOM   2025 C CA  . PHE   C 1 78 ? 13.893  -30.728 11.868  1.00 33.58  ? 77  PHE   C CA  1 
ATOM   2026 C C   . PHE   C 1 78 ? 13.393  -29.299 11.588  1.00 36.81  ? 77  PHE   C C   1 
ATOM   2027 O O   . PHE   C 1 78 ? 13.734  -28.337 12.296  1.00 32.17  ? 77  PHE   C O   1 
ATOM   2028 C CB  . PHE   C 1 78 ? 14.934  -31.066 10.802  1.00 34.13  ? 77  PHE   C CB  1 
ATOM   2029 C CG  . PHE   C 1 78 ? 16.219  -30.292 11.040  1.00 33.86  ? 77  PHE   C CG  1 
ATOM   2030 C CD1 . PHE   C 1 78 ? 16.388  -29.010 10.532  1.00 37.54  ? 77  PHE   C CD1 1 
ATOM   2031 C CD2 . PHE   C 1 78 ? 17.259  -30.851 11.778  1.00 30.81  ? 77  PHE   C CD2 1 
ATOM   2032 C CE1 . PHE   C 1 78 ? 17.567  -28.309 10.757  1.00 31.58  ? 77  PHE   C CE1 1 
ATOM   2033 C CE2 . PHE   C 1 78 ? 18.438  -30.142 12.005  1.00 32.16  ? 77  PHE   C CE2 1 
ATOM   2034 C CZ  . PHE   C 1 78 ? 18.584  -28.872 11.498  1.00 34.02  ? 77  PHE   C CZ  1 
ATOM   2035 N N   . ASN   C 1 79 ? 12.644  -29.161 10.490  1.00 33.23  ? 78  ASN   C N   1 
ATOM   2036 C CA  . ASN   C 1 79 ? 12.266  -27.844 10.003  1.00 36.58  ? 78  ASN   C CA  1 
ATOM   2037 C C   . ASN   C 1 79 ? 11.301  -27.194 10.993  1.00 36.15  ? 78  ASN   C C   1 
ATOM   2038 O O   . ASN   C 1 79 ? 11.386  -25.989 11.273  1.00 34.56  ? 78  ASN   C O   1 
ATOM   2039 C CB  . ASN   C 1 79 ? 11.808  -27.916 8.552   1.00 35.76  ? 78  ASN   C CB  1 
ATOM   2040 C CG  . ASN   C 1 79 ? 12.968  -28.187 7.617   1.00 35.28  ? 78  ASN   C CG  1 
ATOM   2041 O OD1 . ASN   C 1 79 ? 14.116  -27.854 7.934   1.00 36.04  ? 78  ASN   C OD1 1 
ATOM   2042 N ND2 . ASN   C 1 79 ? 12.697  -28.785 6.464   1.00 34.70  ? 78  ASN   C ND2 1 
ATOM   2043 N N   . GLU   C 1 80 ? 10.417  -28.009 11.578  1.00 35.93  ? 79  GLU   C N   1 
ATOM   2044 C CA  . GLU   C 1 80 ? 9.534   -27.503 12.623  1.00 35.11  ? 79  GLU   C CA  1 
ATOM   2045 C C   . GLU   C 1 80 ? 10.367  -27.050 13.811  1.00 40.85  ? 79  GLU   C C   1 
ATOM   2046 O O   . GLU   C 1 80 ? 10.042  -26.031 14.423  1.00 42.22  ? 79  GLU   C O   1 
ATOM   2047 C CB  . GLU   C 1 80 ? 8.521   -28.568 13.054  1.00 38.66  ? 79  GLU   C CB  1 
ATOM   2048 C CG  . GLU   C 1 80 ? 7.580   -28.040 14.127  1.00 39.32  ? 79  GLU   C CG  1 
ATOM   2049 C CD  . GLU   C 1 80 ? 6.291   -28.819 14.298  1.00 54.89  ? 79  GLU   C CD  1 
ATOM   2050 O OE1 . GLU   C 1 80 ? 6.110   -29.878 13.650  1.00 56.53  ? 79  GLU   C OE1 1 
ATOM   2051 O OE2 . GLU   C 1 80 ? 5.452   -28.336 15.086  1.00 57.98  ? 79  GLU   C OE2 1 
ATOM   2052 N N   . GLY   C 1 81 ? 11.434  -27.829 14.121  1.00 40.48  ? 80  GLY   C N   1 
ATOM   2053 C CA  . GLY   C 1 81 ? 12.389  -27.483 15.166  1.00 34.39  ? 80  GLY   C CA  1 
ATOM   2054 C C   . GLY   C 1 81 ? 13.049  -26.131 14.899  1.00 35.06  ? 80  GLY   C C   1 
ATOM   2055 O O   . GLY   C 1 81 ? 13.268  -25.348 15.820  1.00 32.12  ? 80  GLY   C O   1 
ATOM   2056 N N   . LEU   C 1 82 ? 13.420  -25.878 13.637  1.00 33.93  ? 81  LEU   C N   1 
ATOM   2057 C CA  . LEU   C 1 82 ? 14.007  -24.594 13.271  1.00 37.43  ? 81  LEU   C CA  1 
ATOM   2058 C C   . LEU   C 1 82 ? 13.019  -23.456 13.549  1.00 36.86  ? 81  LEU   C C   1 
ATOM   2059 O O   . LEU   C 1 82 ? 13.419  -22.390 14.031  1.00 37.08  ? 81  LEU   C O   1 
ATOM   2060 C CB  . LEU   C 1 82 ? 14.466  -24.565 11.818  1.00 36.66  ? 81  LEU   C CB  1 
ATOM   2061 C CG  . LEU   C 1 82 ? 15.719  -25.372 11.467  1.00 36.68  ? 81  LEU   C CG  1 
ATOM   2062 C CD1 . LEU   C 1 82 ? 15.949  -25.197 9.976   1.00 36.92  ? 81  LEU   C CD1 1 
ATOM   2063 C CD2 . LEU   C 1 82 ? 16.960  -24.928 12.226  1.00 32.44  ? 81  LEU   C CD2 1 
ATOM   2064 N N   . TRP   C 1 83 ? 11.730  -23.685 13.253  1.00 36.01  ? 82  TRP   C N   1 
ATOM   2065 C CA  . TRP   C 1 83 ? 10.720  -22.661 13.531  1.00 45.01  ? 82  TRP   C CA  1 
ATOM   2066 C C   . TRP   C 1 83 ? 10.623  -22.374 15.041  1.00 43.64  ? 82  TRP   C C   1 
ATOM   2067 O O   . TRP   C 1 83 ? 10.744  -21.218 15.471  1.00 41.37  ? 82  TRP   C O   1 
ATOM   2068 C CB  . TRP   C 1 83 ? 9.355   -23.008 12.912  1.00 45.20  ? 82  TRP   C CB  1 
ATOM   2069 C CG  . TRP   C 1 83 ? 8.351   -21.887 13.035  1.00 51.38  ? 82  TRP   C CG  1 
ATOM   2070 C CD1 . TRP   C 1 83 ? 8.119   -20.877 12.145  1.00 49.51  ? 82  TRP   C CD1 1 
ATOM   2071 C CD2 . TRP   C 1 83 ? 7.463   -21.644 14.151  1.00 52.10  ? 82  TRP   C CD2 1 
ATOM   2072 N NE1 . TRP   C 1 83 ? 7.137   -20.045 12.611  1.00 45.46  ? 82  TRP   C NE1 1 
ATOM   2073 C CE2 . TRP   C 1 83 ? 6.716   -20.483 13.835  1.00 48.05  ? 82  TRP   C CE2 1 
ATOM   2074 C CE3 . TRP   C 1 83 ? 7.233   -22.291 15.375  1.00 48.14  ? 82  TRP   C CE3 1 
ATOM   2075 C CZ2 . TRP   C 1 83 ? 5.760   -19.965 14.704  1.00 53.98  ? 82  TRP   C CZ2 1 
ATOM   2076 C CZ3 . TRP   C 1 83 ? 6.303   -21.765 16.246  1.00 47.28  ? 82  TRP   C CZ3 1 
ATOM   2077 C CH2 . TRP   C 1 83 ? 5.574   -20.620 15.908  1.00 54.14  ? 82  TRP   C CH2 1 
ATOM   2078 N N   . GLU   C 1 84 ? 10.502  -23.446 15.840  1.00 42.80  ? 83  GLU   C N   1 
ATOM   2079 C CA  . GLU   C 1 84 ? 10.394  -23.363 17.292  1.00 44.58  ? 83  GLU   C CA  1 
ATOM   2080 C C   . GLU   C 1 84 ? 11.540  -22.564 17.905  1.00 43.48  ? 83  GLU   C C   1 
ATOM   2081 O O   . GLU   C 1 84 ? 11.298  -21.698 18.755  1.00 42.82  ? 83  GLU   C O   1 
ATOM   2082 C CB  . GLU   C 1 84 ? 10.253  -24.737 17.952  1.00 35.34  ? 83  GLU   C CB  1 
ATOM   2083 C CG  . GLU   C 1 84 ? 8.943   -25.411 17.560  1.00 37.92  ? 83  GLU   C CG  1 
ATOM   2084 C CD  . GLU   C 1 84 ? 8.866   -26.812 18.106  1.00 47.64  ? 83  GLU   C CD  1 
ATOM   2085 O OE1 . GLU   C 1 84 ? 9.875   -27.236 18.716  1.00 46.11  ? 83  GLU   C OE1 1 
ATOM   2086 O OE2 . GLU   C 1 84 ? 7.815   -27.463 17.906  1.00 51.71  ? 83  GLU   C OE2 1 
ATOM   2087 N N   . ILE   C 1 85 ? 12.781  -22.854 17.490  1.00 41.03  ? 84  ILE   C N   1 
ATOM   2088 C CA  . ILE   C 1 85 ? 13.949  -22.281 18.156  1.00 40.97  ? 84  ILE   C CA  1 
ATOM   2089 C C   . ILE   C 1 85 ? 14.121  -20.793 17.825  1.00 42.37  ? 84  ILE   C C   1 
ATOM   2090 O O   . ILE   C 1 85 ? 14.737  -20.056 18.592  1.00 37.29  ? 84  ILE   C O   1 
ATOM   2091 C CB  . ILE   C 1 85 ? 15.231  -23.093 17.882  1.00 38.65  ? 84  ILE   C CB  1 
ATOM   2092 C CG1 . ILE   C 1 85 ? 16.376  -22.636 18.807  1.00 41.35  ? 84  ILE   C CG1 1 
ATOM   2093 C CG2 . ILE   C 1 85 ? 15.621  -23.080 16.400  1.00 35.79  ? 84  ILE   C CG2 1 
ATOM   2094 C CD1 . ILE   C 1 85 ? 17.600  -23.541 18.820  1.00 42.38  ? 84  ILE   C CD1 1 
ATOM   2095 N N   . GLN   C 1 86 ? 13.589  -20.366 16.676  1.00 44.96  ? 85  GLN   C N   1 
ATOM   2096 C CA  . GLN   C 1 86 ? 13.580  -18.958 16.293  1.00 44.27  ? 85  GLN   C CA  1 
ATOM   2097 C C   . GLN   C 1 86 ? 12.333  -18.245 16.826  1.00 39.41  ? 85  GLN   C C   1 
ATOM   2098 O O   . GLN   C 1 86 ? 12.408  -17.074 17.170  1.00 43.22  ? 85  GLN   C O   1 
ATOM   2099 C CB  . GLN   C 1 86 ? 13.699  -18.844 14.772  1.00 42.28  ? 85  GLN   C CB  1 
ATOM   2100 C CG  . GLN   C 1 86 ? 13.889  -17.420 14.242  1.00 39.62  ? 85  GLN   C CG  1 
ATOM   2101 C CD  . GLN   C 1 86 ? 14.284  -17.402 12.776  1.00 41.23  ? 85  GLN   C CD  1 
ATOM   2102 O OE1 . GLN   C 1 86 ? 14.145  -18.392 12.044  1.00 45.03  ? 85  GLN   C OE1 1 
ATOM   2103 N NE2 . GLN   C 1 86 ? 14.836  -16.283 12.336  1.00 42.75  ? 85  GLN   C NE2 1 
ATOM   2104 N N   . ASN   C 1 87 ? 11.202  -18.949 16.943  1.00 46.07  ? 86  ASN   C N   1 
ATOM   2105 C CA  . ASN   C 1 87 ? 9.904   -18.281 17.043  1.00 53.37  ? 86  ASN   C CA  1 
ATOM   2106 C C   . ASN   C 1 87 ? 9.129   -18.624 18.318  1.00 53.39  ? 86  ASN   C C   1 
ATOM   2107 O O   . ASN   C 1 87 ? 8.133   -17.970 18.612  1.00 48.96  ? 86  ASN   C O   1 
ATOM   2108 C CB  . ASN   C 1 87 ? 9.011   -18.531 15.827  1.00 44.61  ? 86  ASN   C CB  1 
ATOM   2109 C CG  . ASN   C 1 87 ? 9.661   -17.976 14.585  1.00 47.88  ? 86  ASN   C CG  1 
ATOM   2110 O OD1 . ASN   C 1 87 ? 9.835   -16.754 14.490  1.00 45.23  ? 86  ASN   C OD1 1 
ATOM   2111 N ND2 . ASN   C 1 87 ? 10.080  -18.846 13.669  1.00 42.71  ? 86  ASN   C ND2 1 
ATOM   2112 N N   . ASN   C 1 88 ? 9.535   -19.666 19.053  1.00 51.96  ? 87  ASN   C N   1 
ATOM   2113 C CA  . ASN   C 1 88 ? 8.792   -20.033 20.256  1.00 47.95  ? 87  ASN   C CA  1 
ATOM   2114 C C   . ASN   C 1 88 ? 9.702   -20.841 21.172  1.00 45.86  ? 87  ASN   C C   1 
ATOM   2115 O O   . ASN   C 1 88 ? 9.337   -21.946 21.572  1.00 54.79  ? 87  ASN   C O   1 
ATOM   2116 C CB  . ASN   C 1 88 ? 7.574   -20.890 19.904  1.00 53.60  ? 87  ASN   C CB  1 
ATOM   2117 C CG  . ASN   C 1 88 ? 6.489   -20.905 20.961  1.00 54.30  ? 87  ASN   C CG  1 
ATOM   2118 O OD1 . ASN   C 1 88 ? 6.499   -20.086 21.887  1.00 55.56  ? 87  ASN   C OD1 1 
ATOM   2119 N ND2 . ASN   C 1 88 ? 5.531   -21.811 20.823  1.00 57.91  ? 87  ASN   C ND2 1 
ATOM   2120 N N   . PRO   C 1 89 ? 10.925  -20.357 21.489  1.00 47.97  ? 88  PRO   C N   1 
ATOM   2121 C CA  . PRO   C 1 89 ? 11.952  -21.221 22.079  1.00 50.80  ? 88  PRO   C CA  1 
ATOM   2122 C C   . PRO   C 1 89 ? 11.728  -21.711 23.508  1.00 59.30  ? 88  PRO   C C   1 
ATOM   2123 O O   . PRO   C 1 89 ? 12.405  -22.651 23.938  1.00 58.01  ? 88  PRO   C O   1 
ATOM   2124 C CB  . PRO   C 1 89 ? 13.246  -20.395 21.939  1.00 47.56  ? 88  PRO   C CB  1 
ATOM   2125 C CG  . PRO   C 1 89 ? 12.761  -18.951 21.988  1.00 46.26  ? 88  PRO   C CG  1 
ATOM   2126 C CD  . PRO   C 1 89 ? 11.412  -18.983 21.259  1.00 47.24  ? 88  PRO   C CD  1 
ATOM   2127 N N   . HIS   C 1 90 ? 10.783  -21.075 24.224  1.00 60.89  ? 89  HIS   C N   1 
ATOM   2128 C CA  . HIS   C 1 90 ? 10.561  -21.397 25.627  1.00 56.72  ? 89  HIS   C CA  1 
ATOM   2129 C C   . HIS   C 1 90 ? 9.118   -21.830 25.888  1.00 57.37  ? 89  HIS   C C   1 
ATOM   2130 O O   . HIS   C 1 90 ? 8.640   -21.729 27.009  1.00 63.39  ? 89  HIS   C O   1 
ATOM   2131 C CB  . HIS   C 1 90 ? 11.105  -20.309 26.559  1.00 46.77  ? 89  HIS   C CB  1 
ATOM   2132 C CG  . HIS   C 1 90 ? 12.522  -19.873 26.307  1.00 45.54  ? 89  HIS   C CG  1 
ATOM   2133 N ND1 . HIS   C 1 90 ? 12.818  -18.664 25.715  1.00 48.06  ? 89  HIS   C ND1 1 
ATOM   2134 C CD2 . HIS   C 1 90 ? 13.715  -20.419 26.606  1.00 48.97  ? 89  HIS   C CD2 1 
ATOM   2135 C CE1 . HIS   C 1 90 ? 14.141  -18.503 25.636  1.00 46.59  ? 89  HIS   C CE1 1 
ATOM   2136 N NE2 . HIS   C 1 90 ? 14.705  -19.551 26.181  1.00 49.80  ? 89  HIS   C NE2 1 
ATOM   2137 N N   . ALA   C 1 91 ? 8.439   -22.368 24.870  1.00 65.64  ? 90  ALA   C N   1 
ATOM   2138 C CA  . ALA   C 1 91 ? 7.126   -22.970 25.068  1.00 75.14  ? 90  ALA   C CA  1 
ATOM   2139 C C   . ALA   C 1 91 ? 7.260   -24.389 25.629  1.00 83.32  ? 90  ALA   C C   1 
ATOM   2140 O O   . ALA   C 1 91 ? 8.370   -24.900 25.775  1.00 85.49  ? 90  ALA   C O   1 
ATOM   2141 C CB  . ALA   C 1 91 ? 6.324   -22.942 23.781  1.00 70.11  ? 90  ALA   C CB  1 
ATOM   2142 N N   . SER   C 1 92 ? 6.106   -25.029 25.879  1.00 89.18  ? 91  SER   C N   1 
ATOM   2143 C CA  . SER   C 1 92 ? 5.976   -26.245 26.674  1.00 89.96  ? 91  SER   C CA  1 
ATOM   2144 C C   . SER   C 1 92 ? 6.238   -27.514 25.858  1.00 89.42  ? 91  SER   C C   1 
ATOM   2145 O O   . SER   C 1 92 ? 7.092   -28.321 26.226  1.00 83.07  ? 91  SER   C O   1 
ATOM   2146 C CB  . SER   C 1 92 ? 4.614   -26.306 27.331  1.00 87.20  ? 91  SER   C CB  1 
ATOM   2147 O OG  . SER   C 1 92 ? 4.427   -25.199 28.198  1.00 83.80  ? 91  SER   C OG  1 
ATOM   2148 N N   . TYR   C 1 93 ? 5.450   -27.701 24.789  1.00 90.46  ? 92  TYR   C N   1 
ATOM   2149 C CA  . TYR   C 1 93 ? 5.461   -28.891 23.947  1.00 87.10  ? 92  TYR   C CA  1 
ATOM   2150 C C   . TYR   C 1 93 ? 5.352   -30.149 24.826  1.00 90.67  ? 92  TYR   C C   1 
ATOM   2151 O O   . TYR   C 1 93 ? 4.232   -30.429 25.323  1.00 95.35  ? 92  TYR   C O   1 
ATOM   2152 C CB  . TYR   C 1 93 ? 6.656   -28.942 22.984  1.00 82.01  ? 92  TYR   C CB  1 
ATOM   2153 C CG  . TYR   C 1 93 ? 6.992   -27.636 22.267  1.00 70.37  ? 92  TYR   C CG  1 
ATOM   2154 C CD1 . TYR   C 1 93 ? 6.217   -27.178 21.205  1.00 62.53  ? 92  TYR   C CD1 1 
ATOM   2155 C CD2 . TYR   C 1 93 ? 8.097   -26.872 22.640  1.00 63.00  ? 92  TYR   C CD2 1 
ATOM   2156 C CE1 . TYR   C 1 93 ? 6.515   -25.992 20.556  1.00 60.98  ? 92  TYR   C CE1 1 
ATOM   2157 C CE2 . TYR   C 1 93 ? 8.419   -25.693 21.984  1.00 51.58  ? 92  TYR   C CE2 1 
ATOM   2158 C CZ  . TYR   C 1 93 ? 7.621   -25.249 20.943  1.00 59.94  ? 92  TYR   C CZ  1 
ATOM   2159 O OH  . TYR   C 1 93 ? 7.909   -24.072 20.300  1.00 55.99  ? 92  TYR   C OH  1 
HETATM 2160 S S   . SO4   D 2 .  ? 1.131   -33.600 1.729   1.00 103.38 ? 101 SO4   A S   1 
HETATM 2161 O O1  . SO4   D 2 .  ? 1.637   -34.198 0.514   1.00 83.17  ? 101 SO4   A O1  1 
HETATM 2162 O O2  . SO4   D 2 .  ? 1.088   -32.165 1.591   1.00 98.27  ? 101 SO4   A O2  1 
HETATM 2163 O O3  . SO4   D 2 .  ? -0.197  -34.097 1.989   1.00 107.13 ? 101 SO4   A O3  1 
HETATM 2164 O O4  . SO4   D 2 .  ? 1.994   -33.943 2.829   1.00 99.72  ? 101 SO4   A O4  1 
HETATM 2165 S S   . SO4   E 2 .  ? -9.827  -24.513 1.240   1.00 113.87 ? 102 SO4   A S   1 
HETATM 2166 O O1  . SO4   E 2 .  ? -9.800  -24.231 -0.170  1.00 109.56 ? 102 SO4   A O1  1 
HETATM 2167 O O2  . SO4   E 2 .  ? -9.875  -23.276 1.974   1.00 106.69 ? 102 SO4   A O2  1 
HETATM 2168 O O3  . SO4   E 2 .  ? -10.992 -25.307 1.543   1.00 122.67 ? 102 SO4   A O3  1 
HETATM 2169 O O4  . SO4   E 2 .  ? -8.643  -25.243 1.613   1.00 112.17 ? 102 SO4   A O4  1 
HETATM 2170 C C1  . EDO   F 3 .  ? 13.859  -19.518 -7.439  1.00 44.03  ? 103 EDO   A C1  1 
HETATM 2171 O O1  . EDO   F 3 .  ? 15.073  -18.863 -7.085  1.00 35.94  ? 103 EDO   A O1  1 
HETATM 2172 C C2  . EDO   F 3 .  ? 13.144  -18.886 -8.598  1.00 47.00  ? 103 EDO   A C2  1 
HETATM 2173 O O2  . EDO   F 3 .  ? 12.397  -17.721 -8.233  1.00 42.38  ? 103 EDO   A O2  1 
HETATM 2174 S S   . SO4   G 2 .  ? 9.035   -29.293 5.743   1.00 66.34  ? 104 SO4   A S   1 
HETATM 2175 O O1  . SO4   G 2 .  ? 9.924   -28.863 4.703   1.00 61.00  ? 104 SO4   A O1  1 
HETATM 2176 O O2  . SO4   G 2 .  ? 8.120   -30.277 5.212   1.00 77.02  ? 104 SO4   A O2  1 
HETATM 2177 O O3  . SO4   G 2 .  ? 9.790   -29.868 6.840   1.00 65.60  ? 104 SO4   A O3  1 
HETATM 2178 O O4  . SO4   G 2 .  ? 8.294   -28.156 6.211   1.00 78.59  ? 104 SO4   A O4  1 
HETATM 2179 S S   . SO4   H 2 .  ? 7.480   -8.497  -24.901 1.00 76.61  ? 101 SO4   B S   1 
HETATM 2180 O O1  . SO4   H 2 .  ? 8.583   -8.741  -25.783 1.00 58.52  ? 101 SO4   B O1  1 
HETATM 2181 O O2  . SO4   H 2 .  ? 6.247   -8.888  -25.537 1.00 65.31  ? 101 SO4   B O2  1 
HETATM 2182 O O3  . SO4   H 2 .  ? 7.625   -9.258  -23.673 1.00 58.10  ? 101 SO4   B O3  1 
HETATM 2183 O O4  . SO4   H 2 .  ? 7.466   -7.082  -24.616 1.00 75.25  ? 101 SO4   B O4  1 
HETATM 2184 S S   . SO4   I 2 .  ? 14.498  -27.075 -26.493 1.00 63.60  ? 102 SO4   B S   1 
HETATM 2185 O O1  . SO4   I 2 .  ? 15.839  -26.637 -26.209 1.00 62.47  ? 102 SO4   B O1  1 
HETATM 2186 O O2  . SO4   I 2 .  ? 14.556  -28.379 -27.111 1.00 73.71  ? 102 SO4   B O2  1 
HETATM 2187 O O3  . SO4   I 2 .  ? 13.749  -27.150 -25.273 1.00 71.81  ? 102 SO4   B O3  1 
HETATM 2188 O O4  . SO4   I 2 .  ? 13.852  -26.142 -27.379 1.00 61.56  ? 102 SO4   B O4  1 
HETATM 2189 C C4  . A1A3Z J 4 .  ? 18.635  -14.423 -24.085 0.68 43.43  ? 103 A1A3Z B C4  1 
HETATM 2190 C C5  . A1A3Z J 4 .  ? 19.872  -14.931 -23.406 0.68 46.39  ? 103 A1A3Z B C5  1 
HETATM 2191 C C6  . A1A3Z J 4 .  ? 21.122  -14.556 -23.899 0.68 44.05  ? 103 A1A3Z B C6  1 
HETATM 2192 C C7  . A1A3Z J 4 .  ? 22.279  -15.013 -23.287 0.68 45.17  ? 103 A1A3Z B C7  1 
HETATM 2193 C C8  . A1A3Z J 4 .  ? 22.201  -15.843 -22.191 0.68 47.47  ? 103 A1A3Z B C8  1 
HETATM 2194 C C10 . A1A3Z J 4 .  ? 19.778  -15.772 -22.275 0.68 51.35  ? 103 A1A3Z B C10 1 
HETATM 2195 O O   . A1A3Z J 4 .  ? 18.304  -13.266 -23.943 0.68 43.13  ? 103 A1A3Z B O   1 
HETATM 2196 N N   . A1A3Z J 4 .  ? 17.900  -15.283 -24.808 0.68 45.73  ? 103 A1A3Z B N   1 
HETATM 2197 C C2  . A1A3Z J 4 .  ? 18.178  -16.701 -25.082 0.68 42.88  ? 103 A1A3Z B C2  1 
HETATM 2198 C C3  . A1A3Z J 4 .  ? 17.689  -17.116 -26.438 0.68 43.05  ? 103 A1A3Z B C3  1 
HETATM 2199 C C1  . A1A3Z J 4 .  ? 16.606  -14.773 -25.263 0.68 43.89  ? 103 A1A3Z B C1  1 
HETATM 2200 C C   . A1A3Z J 4 .  ? 15.530  -15.188 -24.313 0.68 46.73  ? 103 A1A3Z B C   1 
HETATM 2201 C C11 . A1A3Z J 4 .  ? 18.458  -16.197 -21.686 0.68 48.90  ? 103 A1A3Z B C11 1 
HETATM 2202 C C9  . A1A3Z J 4 .  ? 20.966  -16.213 -21.687 0.68 49.96  ? 103 A1A3Z B C9  1 
HETATM 2203 C C1  . EDO   K 3 .  ? 16.645  -36.199 16.425  1.00 46.06  ? 101 EDO   C C1  1 
HETATM 2204 O O1  . EDO   K 3 .  ? 15.540  -36.874 15.842  1.00 44.61  ? 101 EDO   C O1  1 
HETATM 2205 C C2  . EDO   K 3 .  ? 16.247  -35.282 17.514  1.00 44.16  ? 101 EDO   C C2  1 
HETATM 2206 O O2  . EDO   K 3 .  ? 15.100  -35.745 18.176  1.00 35.75  ? 101 EDO   C O2  1 
HETATM 2207 S S   . SO4   L 2 .  ? 28.857  -38.257 12.139  1.00 101.61 ? 102 SO4   C S   1 
HETATM 2208 O O1  . SO4   L 2 .  ? 30.068  -37.725 11.569  1.00 104.12 ? 102 SO4   C O1  1 
HETATM 2209 O O2  . SO4   L 2 .  ? 27.779  -37.334 11.911  1.00 98.42  ? 102 SO4   C O2  1 
HETATM 2210 O O3  . SO4   L 2 .  ? 28.544  -39.518 11.526  1.00 105.06 ? 102 SO4   C O3  1 
HETATM 2211 O O4  . SO4   L 2 .  ? 29.035  -38.448 13.554  1.00 106.60 ? 102 SO4   C O4  1 
HETATM 2212 O O   . HOH   M 5 .  ? -5.870  -18.312 -3.549  1.00 68.76  ? 201 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 2.285   -14.020 17.307  1.00 61.90  ? 202 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 10.776  -29.570 2.862   1.00 47.67  ? 203 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 8.308   -32.381 4.361   1.00 53.04  ? 204 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? -9.235  -15.008 10.675  1.00 56.42  ? 205 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? -5.604  -13.437 -16.496 1.00 57.49  ? 206 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 7.903   -8.212  4.426   1.00 43.45  ? 207 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 4.297   -10.304 13.707  1.00 63.44  ? 208 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 10.847  -23.738 9.649   1.00 46.17  ? 209 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 0.362   -24.868 13.532  1.00 73.61  ? 210 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? -2.670  -11.729 14.111  1.00 55.99  ? 211 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 15.743  -17.138 -19.181 1.00 54.16  ? 212 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 0.516   -10.625 -15.488 1.00 54.60  ? 213 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 6.872   -10.451 -11.958 1.00 54.68  ? 214 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 10.747  -5.229  -7.650  1.00 39.53  ? 215 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? -2.457  3.024   -1.955  1.00 46.90  ? 216 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 3.181   -29.596 -0.308  1.00 48.15  ? 217 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 2.264   -24.909 -10.080 1.00 50.90  ? 218 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -0.705  -29.144 9.964   1.00 60.27  ? 219 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -8.623  -21.100 -1.089  1.00 48.08  ? 220 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 13.065  -28.039 -4.670  1.00 57.06  ? 221 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 1.612   0.768   -7.188  1.00 52.31  ? 222 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 5.898   -29.053 6.817   1.00 57.17  ? 223 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -6.787  -5.360  9.143   1.00 37.93  ? 224 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 1.752   -4.675  -10.230 1.00 47.35  ? 225 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 10.376  -9.694  -13.167 1.00 65.07  ? 226 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 15.811  -12.042 -5.262  1.00 47.11  ? 227 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? -8.111  -15.864 -1.082  1.00 37.57  ? 228 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 12.541  -15.432 -11.929 1.00 67.77  ? 229 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 2.322   -25.080 -6.614  1.00 62.16  ? 230 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 8.910   -18.120 -10.976 1.00 41.78  ? 231 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 12.812  -9.333  -7.295  1.00 44.88  ? 232 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 11.345  -12.011 5.827   1.00 50.56  ? 233 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 15.870  -24.322 1.789   1.00 52.97  ? 234 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 7.796   -1.609  -0.788  1.00 61.61  ? 235 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? -4.282  -21.150 6.087   1.00 45.07  ? 236 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -3.014  -30.325 -3.664  1.00 65.67  ? 237 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 10.960  -5.902  -4.055  1.00 59.43  ? 238 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? -1.939  -21.916 -0.616  1.00 30.50  ? 239 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 0.009   -33.655 4.655   1.00 50.95  ? 240 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 2.726   -6.552  5.524   1.00 42.04  ? 241 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 9.853   -12.984 9.705   1.00 45.04  ? 242 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 4.495   -7.833  1.074   1.00 35.72  ? 243 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? -0.955  -5.461  -7.281  1.00 34.62  ? 244 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 4.454   -3.365  -3.333  1.00 42.32  ? 245 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 1.361   -18.208 -18.527 1.00 61.20  ? 246 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? -7.703  -21.574 -5.536  1.00 73.61  ? 247 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 16.930  -17.938 -9.631  1.00 47.27  ? 248 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? 1.751   -10.255 11.694  1.00 44.47  ? 249 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? -0.721  -20.882 6.973   1.00 42.39  ? 250 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 13.187  -11.876 -4.247  1.00 25.41  ? 251 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -3.841  -11.160 6.786   1.00 47.80  ? 252 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -5.936  -19.583 -5.573  1.00 39.19  ? 253 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 17.084  -12.846 1.374   1.00 23.10  ? 254 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 9.027   -19.967 -18.483 1.00 52.43  ? 255 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 9.672   -6.062  -1.833  1.00 42.04  ? 256 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 11.452  -12.291 -6.140  1.00 29.37  ? 257 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? -5.779  -15.731 -8.036  1.00 32.19  ? 258 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -6.331  -11.399 -11.315 1.00 38.28  ? 259 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 0.001   -23.169 9.348   1.00 44.41  ? 260 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 2.748   -9.943  -13.116 1.00 62.06  ? 261 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -8.123  -16.599 1.903   1.00 46.12  ? 262 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -4.446  -25.794 -5.489  1.00 56.12  ? 263 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -1.457  -11.782 11.159  1.00 45.37  ? 264 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -7.972  -17.383 6.507   1.00 51.35  ? 265 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -1.514  -7.431  11.405  1.00 57.86  ? 266 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 6.348   -5.622  0.360   1.00 56.55  ? 267 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? -6.197  -12.739 6.733   1.00 45.26  ? 268 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 7.894   -7.840  1.165   1.00 34.62  ? 269 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 13.040  -11.517 7.958   1.00 59.60  ? 270 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 9.660   -30.547 9.692   1.00 37.56  ? 271 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? -3.943  -26.572 7.390   1.00 51.70  ? 272 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 8.029   -18.047 -15.920 1.00 60.07  ? 273 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 8.772   -16.289 -13.068 1.00 42.77  ? 274 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 4.500   -34.725 4.212   1.00 64.83  ? 275 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 12.659  -13.432 -8.575  1.00 43.75  ? 276 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 7.873   -17.395 8.795   1.00 56.74  ? 277 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 5.079   -7.609  3.946   1.00 36.71  ? 278 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 22.232  -16.746 -0.333  1.00 45.29  ? 279 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 10.900  -7.853  0.331   1.00 29.99  ? 280 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 15.437  -27.936 -0.858  1.00 53.85  ? 281 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 21.261  -16.497 -3.563  1.00 33.59  ? 282 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 6.441   -15.884 -14.984 1.00 50.46  ? 283 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? -6.352  -26.265 3.428   1.00 50.19  ? 284 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -0.566  -20.831 10.786  1.00 69.44  ? 285 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? -7.264  -11.558 -8.113  1.00 35.02  ? 286 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 1.161   -28.803 -7.239  1.00 56.82  ? 287 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 8.925   -27.639 -7.668  1.00 65.67  ? 288 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? -4.424  -7.640  -10.965 1.00 58.30  ? 289 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 17.040  -12.899 -16.838 1.00 48.37  ? 290 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -11.235 -15.938 -3.633  1.00 56.82  ? 291 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? -3.786  -8.218  10.465  1.00 55.25  ? 292 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 8.648   -9.116  -13.812 1.00 42.71  ? 293 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? -7.180  -13.981 -9.134  1.00 55.54  ? 294 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 12.054  -29.256 -2.862  1.00 67.42  ? 295 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -8.247  -19.936 -3.567  1.00 48.76  ? 296 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 11.675  -21.033 10.628  1.00 45.62  ? 297 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -3.913  -11.319 10.081  1.00 67.16  ? 298 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -5.830  -23.429 -7.164  1.00 56.70  ? 299 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -0.420  -3.070  -11.100 1.00 60.11  ? 300 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? -9.271  -20.514 4.516   1.00 66.71  ? 301 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -6.310  -22.434 5.730   1.00 57.68  ? 302 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? 7.129   -30.324 -2.691  1.00 61.73  ? 303 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? 11.119  -1.974  -1.737  1.00 61.59  ? 304 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? 17.928  -20.853 -13.520 1.00 53.78  ? 305 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? -7.167  -19.147 7.843   1.00 60.61  ? 306 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? -10.461 -28.414 -1.922  1.00 68.94  ? 307 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? 4.719   -9.737  -11.332 1.00 56.16  ? 308 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? 8.265   -21.862 -19.392 1.00 58.96  ? 309 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? -11.338 -13.236 -2.971  1.00 51.72  ? 310 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? 4.234   -3.319  2.086   1.00 67.54  ? 311 HOH   A O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 30.896  -8.390  -30.085 1.00 58.40  ? 201 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 27.773  -7.792  -29.161 1.00 54.53  ? 202 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 20.093  -22.297 -23.076 1.00 57.10  ? 203 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 6.564   -12.201 -25.964 1.00 47.11  ? 204 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 27.655  -17.414 -25.328 1.00 54.30  ? 205 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 34.654  -22.937 -30.390 1.00 58.39  ? 206 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 25.978  -4.718  -33.899 1.00 54.81  ? 207 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 10.180  -19.575 -43.265 1.00 54.44  ? 208 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 10.007  -11.284 -38.105 1.00 56.96  ? 209 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 7.596   -12.595 -38.470 1.00 73.50  ? 210 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 24.959  -5.115  -29.814 1.00 53.63  ? 211 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 30.335  -19.665 -40.359 1.00 37.90  ? 212 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 32.482  -18.337 -42.289 1.00 68.50  ? 213 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 24.331  -1.684  -36.455 1.00 52.81  ? 214 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 8.733   -8.534  -16.513 1.00 47.06  ? 215 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 12.551  -4.963  -41.689 1.00 64.19  ? 216 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 6.175   -7.260  -32.014 1.00 62.49  ? 217 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 25.473  -6.021  -36.171 1.00 51.70  ? 218 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 22.452  -10.324 -20.950 1.00 60.41  ? 219 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 23.530  -2.301  -29.194 1.00 44.72  ? 220 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 25.972  -23.057 -31.257 1.00 44.51  ? 221 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 8.444   -27.270 -38.051 1.00 68.81  ? 222 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 4.315   -18.703 -25.773 1.00 59.94  ? 223 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 10.462  -18.779 -32.956 1.00 32.46  ? 224 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 20.984  -25.350 -29.835 1.00 53.79  ? 225 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 18.094  -0.477  -38.457 1.00 35.57  ? 226 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 17.630  -19.610 -42.235 1.00 58.80  ? 227 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 22.431  -23.313 -28.875 1.00 48.28  ? 228 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 16.703  -19.271 -28.890 1.00 29.06  ? 229 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 7.410   -18.251 -31.641 1.00 44.69  ? 230 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 10.381  -16.793 -44.203 1.00 60.09  ? 231 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 23.755  -4.270  -36.960 1.00 34.80  ? 232 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 19.592  -25.709 -34.087 1.00 46.92  ? 233 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 21.044  -13.540 -42.622 1.00 44.61  ? 234 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 19.714  -2.425  -23.081 1.00 75.37  ? 235 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 14.577  -6.089  -41.185 1.00 50.73  ? 236 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 7.050   -19.023 -35.043 1.00 58.90  ? 237 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 21.875  3.835   -32.697 1.00 46.54  ? 238 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 18.096  4.370   -34.461 1.00 39.83  ? 239 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 20.509  -10.006 -42.996 1.00 38.52  ? 240 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 21.215  -6.462  -42.629 1.00 47.90  ? 241 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 12.706  -22.480 -20.621 1.00 58.80  ? 242 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 31.568  -12.286 -38.762 1.00 62.36  ? 243 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 10.568  -21.775 -32.802 1.00 43.33  ? 244 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 1.679   -12.874 -28.514 1.00 59.73  ? 245 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 24.079  -11.279 -22.106 1.00 64.31  ? 246 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 18.448  -0.015  -25.884 1.00 63.93  ? 247 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 7.348   -8.034  -20.883 1.00 60.38  ? 248 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 27.156  -10.155 -29.248 1.00 65.58  ? 249 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 17.998  -15.872 -45.845 1.00 48.83  ? 250 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 31.819  -21.442 -38.389 1.00 54.13  ? 251 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 27.849  -24.754 -35.265 1.00 46.79  ? 252 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 18.403  -26.082 -28.905 1.00 49.92  ? 253 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 26.002  -0.518  -29.544 1.00 51.76  ? 254 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 2.862   -8.073  -27.712 1.00 51.35  ? 255 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 17.534  -3.210  -22.007 1.00 59.03  ? 256 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 24.834  -6.443  -42.504 1.00 51.06  ? 257 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 17.439  -24.612 -20.988 1.00 73.67  ? 258 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 14.312  -24.537 -40.618 1.00 51.25  ? 259 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 6.330   -20.515 -25.283 1.00 52.98  ? 260 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 12.303  -20.244 -19.805 1.00 62.71  ? 261 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 38.554  -13.023 -39.753 1.00 66.87  ? 262 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 17.084  -9.493  -43.734 1.00 47.75  ? 263 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 7.259   -23.487 -24.245 1.00 67.48  ? 264 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 33.719  -17.240 -37.151 1.00 71.44  ? 265 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 9.752   -6.307  -41.029 1.00 51.53  ? 266 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 19.989  3.933   -33.317 1.00 42.33  ? 267 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 16.474  -0.466  -25.601 1.00 52.43  ? 268 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 15.374  -21.901 -41.770 1.00 61.13  ? 269 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 7.402   -9.876  -18.692 1.00 63.23  ? 270 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 15.140  -7.906  -42.815 1.00 45.63  ? 271 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 19.288  -8.518  -43.793 1.00 58.20  ? 272 HOH   B O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 8.314   -36.230 18.627  1.00 64.60  ? 201 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 19.916  -20.119 29.960  1.00 63.63  ? 202 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 15.181  -27.049 28.554  1.00 66.58  ? 203 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 7.389   -31.374 12.482  1.00 54.06  ? 204 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 26.466  -37.488 9.986   1.00 54.83  ? 205 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 9.176   -29.985 11.138  1.00 58.52  ? 206 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 12.019  -28.477 28.037  1.00 62.63  ? 207 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 22.771  -41.389 18.392  1.00 47.98  ? 208 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 26.214  -39.096 12.764  1.00 53.21  ? 209 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 17.363  -17.113 15.005  1.00 55.68  ? 210 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 19.928  -41.788 12.229  1.00 35.37  ? 211 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 33.384  -24.284 31.199  1.00 58.07  ? 212 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 14.472  -39.039 16.766  1.00 54.77  ? 213 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 12.610  -31.302 8.137   1.00 42.25  ? 214 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 15.505  -17.674 19.295  1.00 43.41  ? 215 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 25.322  -19.606 6.321   1.00 42.06  ? 216 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 22.133  -28.353 11.072  1.00 34.48  ? 217 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 27.787  -37.317 15.905  1.00 58.52  ? 218 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 16.175  -37.783 19.828  1.00 72.39  ? 219 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 30.005  -40.148 9.412   1.00 40.72  ? 220 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 29.981  -31.383 15.870  1.00 62.97  ? 221 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 31.543  -43.268 11.971  1.00 54.12  ? 222 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 13.673  -37.071 13.756  1.00 52.95  ? 223 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 15.059  -21.009 12.442  1.00 45.89  ? 224 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 20.769  -29.017 4.710   1.00 59.80  ? 225 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 18.985  -19.987 10.598  1.00 47.75  ? 226 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 25.587  -33.691 34.676  1.00 59.33  ? 227 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 5.513   -26.299 16.852  1.00 52.74  ? 228 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 31.063  -43.290 15.776  1.00 57.40  ? 229 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 25.059  -31.213 10.798  1.00 35.18  ? 230 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 27.839  -15.239 13.057  1.00 56.52  ? 231 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 6.941   -17.969 10.838  1.00 45.26  ? 232 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 21.863  -34.333 16.523  1.00 34.62  ? 233 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 30.911  -39.749 27.102  1.00 56.37  ? 234 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 30.522  -29.054 12.319  1.00 57.51  ? 235 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 29.571  -39.667 31.620  1.00 44.68  ? 236 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 23.119  -18.396 21.710  1.00 51.66  ? 237 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 30.787  -29.264 32.004  1.00 72.40  ? 238 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 19.968  -40.982 39.118  1.00 63.19  ? 239 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 20.692  -28.609 8.539   1.00 36.83  ? 240 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 19.204  -26.591 3.228   1.00 52.78  ? 241 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 25.619  -17.725 13.909  1.00 44.99  ? 242 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 27.711  -37.381 24.990  1.00 54.31  ? 243 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 2.760   -28.897 14.283  1.00 64.50  ? 244 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 31.625  -33.266 25.874  1.00 50.66  ? 245 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 25.398  -39.469 20.177  1.00 44.31  ? 246 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 20.561  -39.897 26.300  1.00 42.44  ? 247 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 25.235  -17.796 21.056  1.00 62.38  ? 248 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 19.691  -19.013 25.160  1.00 48.48  ? 249 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 14.301  -29.423 4.064   1.00 49.67  ? 250 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 30.446  -25.101 32.109  1.00 73.22  ? 251 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 17.714  -21.186 12.778  1.00 54.00  ? 252 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 14.195  -38.669 9.621   1.00 56.42  ? 253 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 8.865   -18.765 23.398  1.00 60.05  ? 254 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 30.189  -32.439 18.317  1.00 61.65  ? 255 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 4.965   -24.060 18.616  1.00 56.32  ? 256 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 30.742  -17.101 9.949   1.00 54.87  ? 257 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 30.849  -35.407 28.452  1.00 63.84  ? 258 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 20.280  -13.055 13.318  1.00 45.23  ? 259 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 17.667  -37.042 29.009  1.00 76.30  ? 260 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 27.977  -24.774 33.126  1.00 82.63  ? 261 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 29.032  -41.523 27.136  1.00 52.27  ? 262 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 25.501  -14.093 11.084  1.00 44.45  ? 263 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 31.961  -38.738 30.803  1.00 75.40  ? 264 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 13.241  -22.752 27.977  1.00 82.55  ? 265 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 22.315  -13.757 13.253  1.00 58.99  ? 266 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 28.849  -17.895 28.632  1.00 56.30  ? 267 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 33.281  -44.249 15.167  1.00 46.85  ? 268 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 28.397  -41.364 30.158  1.00 56.19  ? 269 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 15.580  -41.916 8.129   1.00 56.37  ? 270 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 37.243  -25.366 26.427  1.00 74.49  ? 271 HOH   C O   1 
# 
