data_7HHA
# 
_entry.id   7HHA 
# 
_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   7HHA         pdb_00007hha 10.2210/pdb7hha/pdb 
WWPDB D_1001407472 ?            ?                   
# 
_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                        7HHA 
_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           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn '1-(ethanesulfonyl)piperidine-4-carboxylic acid'   221.274   3   ? ?    ? ? 
5 water       nat water                                              18.015    230 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                    SO4 
3 1,2-ETHANEDIOL                                   EDO 
4 '1-(ethanesulfonyl)piperidine-4-carboxylic acid' TE0 
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 
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  
TE0 non-polymer         . '1-(ethanesulfonyl)piperidine-4-carboxylic acid' ?                 'C8 H15 N O4 S'  221.274 
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  ?  ?   ?   C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 29 ?  ?   ?   C A n 
C 1 32 GLY 32 29 ?  ?   ?   C B n 
C 1 33 ALA 33 29 ?  ?   ?   C C n 
C 1 34 VAL 34 32 32 VAL ALA 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        TE0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TE0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 4 TE0 1   104 101 TE0 LIG A . 
H 2 SO4 1   105 4   SO4 SO4 A . 
I 2 SO4 1   101 1   SO4 SO4 B . 
J 2 SO4 1   102 3   SO4 SO4 B . 
K 4 TE0 1   103 101 TE0 LIG B . 
L 2 SO4 1   101 5   SO4 SO4 C . 
M 4 TE0 1   102 101 TE0 LIG C . 
N 5 HOH 1   201 202 HOH HOH A . 
N 5 HOH 2   202 304 HOH HOH A . 
N 5 HOH 3   203 307 HOH HOH A . 
N 5 HOH 4   204 84  HOH HOH A . 
N 5 HOH 5   205 38  HOH HOH A . 
N 5 HOH 6   206 208 HOH HOH A . 
N 5 HOH 7   207 66  HOH HOH A . 
N 5 HOH 8   208 26  HOH HOH A . 
N 5 HOH 9   209 260 HOH HOH A . 
N 5 HOH 10  210 27  HOH HOH A . 
N 5 HOH 11  211 292 HOH HOH A . 
N 5 HOH 12  212 71  HOH HOH A . 
N 5 HOH 13  213 97  HOH HOH A . 
N 5 HOH 14  214 28  HOH HOH A . 
N 5 HOH 15  215 95  HOH HOH A . 
N 5 HOH 16  216 87  HOH HOH A . 
N 5 HOH 17  217 293 HOH HOH A . 
N 5 HOH 18  218 60  HOH HOH A . 
N 5 HOH 19  219 165 HOH HOH A . 
N 5 HOH 20  220 85  HOH HOH A . 
N 5 HOH 21  221 167 HOH HOH A . 
N 5 HOH 22  222 259 HOH HOH A . 
N 5 HOH 23  223 139 HOH HOH A . 
N 5 HOH 24  224 8   HOH HOH A . 
N 5 HOH 25  225 55  HOH HOH A . 
N 5 HOH 26  226 91  HOH HOH A . 
N 5 HOH 27  227 142 HOH HOH A . 
N 5 HOH 28  228 37  HOH HOH A . 
N 5 HOH 29  229 23  HOH HOH A . 
N 5 HOH 30  230 290 HOH HOH A . 
N 5 HOH 31  231 58  HOH HOH A . 
N 5 HOH 32  232 289 HOH HOH A . 
N 5 HOH 33  233 7   HOH HOH A . 
N 5 HOH 34  234 86  HOH HOH A . 
N 5 HOH 35  235 32  HOH HOH A . 
N 5 HOH 36  236 188 HOH HOH A . 
N 5 HOH 37  237 1   HOH HOH A . 
N 5 HOH 38  238 41  HOH HOH A . 
N 5 HOH 39  239 287 HOH HOH A . 
N 5 HOH 40  240 34  HOH HOH A . 
N 5 HOH 41  241 12  HOH HOH A . 
N 5 HOH 42  242 301 HOH HOH A . 
N 5 HOH 43  243 77  HOH HOH A . 
N 5 HOH 44  244 199 HOH HOH A . 
N 5 HOH 45  245 274 HOH HOH A . 
N 5 HOH 46  246 99  HOH HOH A . 
N 5 HOH 47  247 2   HOH HOH A . 
N 5 HOH 48  248 222 HOH HOH A . 
N 5 HOH 49  249 218 HOH HOH A . 
N 5 HOH 50  250 190 HOH HOH A . 
N 5 HOH 51  251 300 HOH HOH A . 
N 5 HOH 52  252 18  HOH HOH A . 
N 5 HOH 53  253 152 HOH HOH A . 
N 5 HOH 54  254 78  HOH HOH A . 
N 5 HOH 55  255 179 HOH HOH A . 
N 5 HOH 56  256 267 HOH HOH A . 
N 5 HOH 57  257 42  HOH HOH A . 
N 5 HOH 58  258 115 HOH HOH A . 
N 5 HOH 59  259 297 HOH HOH A . 
N 5 HOH 60  260 116 HOH HOH A . 
N 5 HOH 61  261 111 HOH HOH A . 
N 5 HOH 62  262 203 HOH HOH A . 
N 5 HOH 63  263 93  HOH HOH A . 
N 5 HOH 64  264 109 HOH HOH A . 
N 5 HOH 65  265 211 HOH HOH A . 
N 5 HOH 66  266 151 HOH HOH A . 
N 5 HOH 67  267 145 HOH HOH A . 
N 5 HOH 68  268 20  HOH HOH A . 
N 5 HOH 69  269 21  HOH HOH A . 
N 5 HOH 70  270 131 HOH HOH A . 
N 5 HOH 71  271 164 HOH HOH A . 
N 5 HOH 72  272 9   HOH HOH A . 
N 5 HOH 73  273 281 HOH HOH A . 
N 5 HOH 74  274 47  HOH HOH A . 
N 5 HOH 75  275 19  HOH HOH A . 
N 5 HOH 76  276 288 HOH HOH A . 
N 5 HOH 77  277 299 HOH HOH A . 
N 5 HOH 78  278 94  HOH HOH A . 
N 5 HOH 79  279 14  HOH HOH A . 
N 5 HOH 80  280 16  HOH HOH A . 
N 5 HOH 81  281 22  HOH HOH A . 
N 5 HOH 82  282 143 HOH HOH A . 
N 5 HOH 83  283 73  HOH HOH A . 
N 5 HOH 84  284 113 HOH HOH A . 
N 5 HOH 85  285 327 HOH HOH A . 
N 5 HOH 86  286 83  HOH HOH A . 
N 5 HOH 87  287 31  HOH HOH A . 
N 5 HOH 88  288 318 HOH HOH A . 
N 5 HOH 89  289 210 HOH HOH A . 
N 5 HOH 90  290 63  HOH HOH A . 
N 5 HOH 91  291 270 HOH HOH A . 
N 5 HOH 92  292 64  HOH HOH A . 
N 5 HOH 93  293 219 HOH HOH A . 
N 5 HOH 94  294 185 HOH HOH A . 
N 5 HOH 95  295 75  HOH HOH A . 
N 5 HOH 96  296 296 HOH HOH A . 
N 5 HOH 97  297 156 HOH HOH A . 
N 5 HOH 98  298 205 HOH HOH A . 
N 5 HOH 99  299 35  HOH HOH A . 
N 5 HOH 100 300 57  HOH HOH A . 
N 5 HOH 101 301 283 HOH HOH A . 
N 5 HOH 102 302 332 HOH HOH A . 
O 5 HOH 1   201 247 HOH HOH B . 
O 5 HOH 2   202 329 HOH HOH B . 
O 5 HOH 3   203 123 HOH HOH B . 
O 5 HOH 4   204 68  HOH HOH B . 
O 5 HOH 5   205 242 HOH HOH B . 
O 5 HOH 6   206 69  HOH HOH B . 
O 5 HOH 7   207 258 HOH HOH B . 
O 5 HOH 8   208 272 HOH HOH B . 
O 5 HOH 9   209 117 HOH HOH B . 
O 5 HOH 10  210 89  HOH HOH B . 
O 5 HOH 11  211 279 HOH HOH B . 
O 5 HOH 12  212 98  HOH HOH B . 
O 5 HOH 13  213 249 HOH HOH B . 
O 5 HOH 14  214 101 HOH HOH B . 
O 5 HOH 15  215 224 HOH HOH B . 
O 5 HOH 16  216 119 HOH HOH B . 
O 5 HOH 17  217 54  HOH HOH B . 
O 5 HOH 18  218 184 HOH HOH B . 
O 5 HOH 19  219 331 HOH HOH B . 
O 5 HOH 20  220 169 HOH HOH B . 
O 5 HOH 21  221 172 HOH HOH B . 
O 5 HOH 22  222 137 HOH HOH B . 
O 5 HOH 23  223 17  HOH HOH B . 
O 5 HOH 24  224 10  HOH HOH B . 
O 5 HOH 25  225 150 HOH HOH B . 
O 5 HOH 26  226 72  HOH HOH B . 
O 5 HOH 27  227 6   HOH HOH B . 
O 5 HOH 28  228 24  HOH HOH B . 
O 5 HOH 29  229 59  HOH HOH B . 
O 5 HOH 30  230 261 HOH HOH B . 
O 5 HOH 31  231 61  HOH HOH B . 
O 5 HOH 32  232 5   HOH HOH B . 
O 5 HOH 33  233 25  HOH HOH B . 
O 5 HOH 34  234 96  HOH HOH B . 
O 5 HOH 35  235 315 HOH HOH B . 
O 5 HOH 36  236 215 HOH HOH B . 
O 5 HOH 37  237 36  HOH HOH B . 
O 5 HOH 38  238 76  HOH HOH B . 
O 5 HOH 39  239 217 HOH HOH B . 
O 5 HOH 40  240 303 HOH HOH B . 
O 5 HOH 41  241 74  HOH HOH B . 
O 5 HOH 42  242 157 HOH HOH B . 
O 5 HOH 43  243 320 HOH HOH B . 
O 5 HOH 44  244 280 HOH HOH B . 
O 5 HOH 45  245 175 HOH HOH B . 
O 5 HOH 46  246 168 HOH HOH B . 
O 5 HOH 47  247 197 HOH HOH B . 
O 5 HOH 48  248 153 HOH HOH B . 
O 5 HOH 49  249 214 HOH HOH B . 
O 5 HOH 50  250 13  HOH HOH B . 
O 5 HOH 51  251 120 HOH HOH B . 
O 5 HOH 52  252 170 HOH HOH B . 
O 5 HOH 53  253 44  HOH HOH B . 
O 5 HOH 54  254 79  HOH HOH B . 
O 5 HOH 55  255 223 HOH HOH B . 
O 5 HOH 56  256 201 HOH HOH B . 
O 5 HOH 57  257 46  HOH HOH B . 
O 5 HOH 58  258 104 HOH HOH B . 
O 5 HOH 59  259 177 HOH HOH B . 
O 5 HOH 60  260 182 HOH HOH B . 
O 5 HOH 61  261 319 HOH HOH B . 
O 5 HOH 62  262 70  HOH HOH B . 
O 5 HOH 63  263 163 HOH HOH B . 
O 5 HOH 64  264 316 HOH HOH B . 
O 5 HOH 65  265 160 HOH HOH B . 
O 5 HOH 66  266 322 HOH HOH B . 
O 5 HOH 67  267 314 HOH HOH B . 
O 5 HOH 68  268 309 HOH HOH B . 
O 5 HOH 69  269 107 HOH HOH B . 
O 5 HOH 70  270 92  HOH HOH B . 
O 5 HOH 71  271 312 HOH HOH B . 
O 5 HOH 72  272 313 HOH HOH B . 
O 5 HOH 73  273 310 HOH HOH B . 
P 5 HOH 1   201 317 HOH HOH C . 
P 5 HOH 2   202 161 HOH HOH C . 
P 5 HOH 3   203 323 HOH HOH C . 
P 5 HOH 4   204 209 HOH HOH C . 
P 5 HOH 5   205 90  HOH HOH C . 
P 5 HOH 6   206 254 HOH HOH C . 
P 5 HOH 7   207 118 HOH HOH C . 
P 5 HOH 8   208 102 HOH HOH C . 
P 5 HOH 9   209 271 HOH HOH C . 
P 5 HOH 10  210 15  HOH HOH C . 
P 5 HOH 11  211 134 HOH HOH C . 
P 5 HOH 12  212 284 HOH HOH C . 
P 5 HOH 13  213 149 HOH HOH C . 
P 5 HOH 14  214 269 HOH HOH C . 
P 5 HOH 15  215 275 HOH HOH C . 
P 5 HOH 16  216 321 HOH HOH C . 
P 5 HOH 17  217 226 HOH HOH C . 
P 5 HOH 18  218 45  HOH HOH C . 
P 5 HOH 19  219 126 HOH HOH C . 
P 5 HOH 20  220 49  HOH HOH C . 
P 5 HOH 21  221 135 HOH HOH C . 
P 5 HOH 22  222 173 HOH HOH C . 
P 5 HOH 23  223 4   HOH HOH C . 
P 5 HOH 24  224 295 HOH HOH C . 
P 5 HOH 25  225 43  HOH HOH C . 
P 5 HOH 26  226 122 HOH HOH C . 
P 5 HOH 27  227 40  HOH HOH C . 
P 5 HOH 28  228 82  HOH HOH C . 
P 5 HOH 29  229 67  HOH HOH C . 
P 5 HOH 30  230 56  HOH HOH C . 
P 5 HOH 31  231 48  HOH HOH C . 
P 5 HOH 32  232 189 HOH HOH C . 
P 5 HOH 33  233 132 HOH HOH C . 
P 5 HOH 34  234 198 HOH HOH C . 
P 5 HOH 35  235 148 HOH HOH C . 
P 5 HOH 36  236 294 HOH HOH C . 
P 5 HOH 37  237 62  HOH HOH C . 
P 5 HOH 38  238 171 HOH HOH C . 
P 5 HOH 39  239 130 HOH HOH C . 
P 5 HOH 40  240 298 HOH HOH C . 
P 5 HOH 41  241 108 HOH HOH C . 
P 5 HOH 42  242 65  HOH HOH C . 
P 5 HOH 43  243 302 HOH HOH C . 
P 5 HOH 44  244 53  HOH HOH C . 
P 5 HOH 45  245 330 HOH HOH C . 
P 5 HOH 46  246 246 HOH HOH C . 
P 5 HOH 47  247 328 HOH HOH C . 
P 5 HOH 48  248 305 HOH HOH C . 
P 5 HOH 49  249 146 HOH HOH C . 
P 5 HOH 50  250 291 HOH HOH C . 
P 5 HOH 51  251 241 HOH HOH C . 
P 5 HOH 52  252 103 HOH HOH C . 
P 5 HOH 53  253 324 HOH HOH C . 
P 5 HOH 54  254 125 HOH HOH C . 
P 5 HOH 55  255 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
15 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
16 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
17 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
18 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
19 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
20 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
21 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
22 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
23 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
24 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
25 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
26 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
27 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
28 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
29 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
30 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
31 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
32 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
33 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
34 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
35 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
36 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
37 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
38 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
39 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
40 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
41 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
42 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
43 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
44 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
45 1 Y 1 C VAL 32 ? CG1 ? C VAL 34 CG1 
46 1 Y 1 C VAL 32 ? CG2 ? C VAL 34 CG2 
47 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
48 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
49 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
50 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
51 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
52 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
53 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
54 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
55 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
56 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
57 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
58 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
59 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
60 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
61 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
62 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
63 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
64 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
65 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHA 
_cell.length_a           41.530 
_cell.length_b           41.970 
_cell.length_c           158.160 
_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                         7HHA 
_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          7HHA 
_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                     7HHA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             41.53 
_reflns.d_resolution_high            1.80 
_reflns.number_obs                   26571 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.109 
_reflns.pdbx_netI_over_sigmaI        8.7 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.119 
_reflns.pdbx_Rpim_I_all              0.048 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     165639 
_reflns.pdbx_chi_squared             0.98 
_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                  1.80 
_reflns_shell.d_res_low                   1.85 
_reflns_shell.number_measured_all         12754 
_reflns_shell.number_unique_obs           1918 
_reflns_shell.Rmerge_I_obs                2.296 
_reflns_shell.pdbx_chi_squared            0.80 
_reflns_shell.pdbx_redundancy             6.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.491 
_reflns_shell.pdbx_Rpim_I_all             0.955 
_reflns_shell.pdbx_CC_half                0.321 
_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                                 7HHA 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25146 
_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                             40.60 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_obs                          0.21065 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20799 
_refine.ls_R_factor_R_free                       0.25777 
_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                  1362 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               41.244 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[2][2]                            -0.05 
_refine.aniso_B[3][3]                            -0.74 
_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                       0.152 
_refine.pdbx_overall_ESU_R_Free                  0.147 
_refine.overall_SU_ML                            0.138 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.841 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        2130 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_refine_hist.number_atoms_solvent             230 
_refine_hist.number_atoms_total               2436 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        40.60 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.012  ? 2308 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.646  1.827  ? 3145 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.343  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.715  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.809 10.000 ? 296  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.134  0.200  ? 296  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1866 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.669  3.965  ? 1076 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.239  7.077  ? 1341 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.514  4.218  ? 1232 '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       9.532  59.85  ? 3576 '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                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_R_work             1808 
_refine_ls_shell.R_factor_R_work                  0.359 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.393 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             99 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHA 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z53825020' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHA 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 4 ? 
L N N 2 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHA A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHA B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHA 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 7HHA GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHA SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHA GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHA SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHA GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHA SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O LEU B 54 ? O LEU B 53 N TYR B 41 ? N TYR B 40 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O 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                   7HHA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 244 ? ? O B HOH 266 ? ? 1.94 
2 1 O   B HOH 240 ? ? O B HOH 266 ? ? 2.04 
3 1 O4  A SO4 105 ? ? O A HOH 201 ? ? 2.05 
4 1 O   B ASP 27  ? A O B HOH 201 ? ? 2.06 
5 1 OD1 C ASP 26  ? ? O C HOH 201 ? ? 2.10 
6 1 OH  A TYR 18  ? ? O A HOH 202 ? ? 2.11 
7 1 O2  A SO4 105 ? ? O A HOH 203 ? ? 2.14 
8 1 O   C THR 47  ? ? O C HOH 202 ? ? 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 299 ? ? 1_555 O A HOH 301 ? ? 4_545 1.87 
2 1 O B HOH 261 ? ? 1_555 O C HOH 236 ? ? 4_435 1.92 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                112.43 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            12.23 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 38 ? ? 74.46   -0.37  
2 1 ASN A 87 ? ? -155.92 62.00  
3 1 ASN B 38 ? ? 83.66   -16.71 
4 1 ASN B 87 ? ? -160.86 59.71  
5 1 ASN C 87 ? ? -151.37 53.48  
# 
_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            148.69 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   C 
_pdbx_validate_polymer_linkage.auth_comp_id_1   VAL 
_pdbx_validate_polymer_linkage.auth_seq_id_1    32 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   C 
_pdbx_validate_polymer_linkage.auth_comp_id_2   LYS 
_pdbx_validate_polymer_linkage.auth_seq_id_2    34 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             4.09 
# 
_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                       302 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.36 
_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 HIS 3  ? C HIS 4  
11 1 Y 1 C ASP 29 A C ASP 31 
12 1 Y 1 C GLY 29 B C GLY 32 
13 1 Y 1 C ALA 29 C C ALA 33 
14 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
TE0 C4   C N N 319 
TE0 C5   C N N 320 
TE0 C6   C N N 321 
TE0 C7   C N N 322 
TE0 N    N N N 323 
TE0 C    C N N 324 
TE0 O    O N N 325 
TE0 C1   C N N 326 
TE0 C2   C N N 327 
TE0 C3   C N N 328 
TE0 O1   O N N 329 
TE0 O2   O N N 330 
TE0 O3   O N N 331 
TE0 S    S N N 332 
TE0 H1   H N N 333 
TE0 H2   H N N 334 
TE0 H3   H N N 335 
TE0 H4   H N N 336 
TE0 H5   H N N 337 
TE0 H6   H N N 338 
TE0 H7   H N N 339 
TE0 H8   H N N 340 
TE0 H9   H N N 341 
TE0 H10  H N N 342 
TE0 H11  H N N 343 
TE0 H12  H N N 344 
TE0 H13  H N N 345 
TE0 H14  H N N 346 
TE0 H15  H N N 347 
THR N    N N N 348 
THR CA   C N S 349 
THR C    C N N 350 
THR O    O N N 351 
THR CB   C N R 352 
THR OG1  O N N 353 
THR CG2  C N N 354 
THR OXT  O N N 355 
THR H    H N N 356 
THR H2   H N N 357 
THR HA   H N N 358 
THR HB   H N N 359 
THR HG1  H N N 360 
THR HG21 H N N 361 
THR HG22 H N N 362 
THR HG23 H N N 363 
THR HXT  H N N 364 
TRP N    N N N 365 
TRP CA   C N S 366 
TRP C    C N N 367 
TRP O    O N N 368 
TRP CB   C N N 369 
TRP CG   C Y N 370 
TRP CD1  C Y N 371 
TRP CD2  C Y N 372 
TRP NE1  N Y N 373 
TRP CE2  C Y N 374 
TRP CE3  C Y N 375 
TRP CZ2  C Y N 376 
TRP CZ3  C Y N 377 
TRP CH2  C Y N 378 
TRP OXT  O N N 379 
TRP H    H N N 380 
TRP H2   H N N 381 
TRP HA   H N N 382 
TRP HB2  H N N 383 
TRP HB3  H N N 384 
TRP HD1  H N N 385 
TRP HE1  H N N 386 
TRP HE3  H N N 387 
TRP HZ2  H N N 388 
TRP HZ3  H N N 389 
TRP HH2  H N N 390 
TRP HXT  H N N 391 
TYR N    N N N 392 
TYR CA   C N S 393 
TYR C    C N N 394 
TYR O    O N N 395 
TYR CB   C N N 396 
TYR CG   C Y N 397 
TYR CD1  C Y N 398 
TYR CD2  C Y N 399 
TYR CE1  C Y N 400 
TYR CE2  C Y N 401 
TYR CZ   C Y N 402 
TYR OH   O N N 403 
TYR OXT  O N N 404 
TYR H    H N N 405 
TYR H2   H N N 406 
TYR HA   H N N 407 
TYR HB2  H N N 408 
TYR HB3  H N N 409 
TYR HD1  H N N 410 
TYR HD2  H N N 411 
TYR HE1  H N N 412 
TYR HE2  H N N 413 
TYR HH   H N N 414 
TYR HXT  H N N 415 
VAL N    N N N 416 
VAL CA   C N S 417 
VAL C    C N N 418 
VAL O    O N N 419 
VAL CB   C N N 420 
VAL CG1  C N N 421 
VAL CG2  C N N 422 
VAL OXT  O N N 423 
VAL H    H N N 424 
VAL H2   H N N 425 
VAL HA   H N N 426 
VAL HB   H N N 427 
VAL HG11 H N N 428 
VAL HG12 H N N 429 
VAL HG13 H N N 430 
VAL HG21 H N N 431 
VAL HG22 H N N 432 
VAL HG23 H N N 433 
VAL HXT  H N N 434 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
TE0 C   C1   sing N N 303 
TE0 C1  S    sing N N 304 
TE0 C2  N    sing N N 305 
TE0 C2  C3   sing N N 306 
TE0 O1  S    doub N N 307 
TE0 S   N    sing N N 308 
TE0 S   O    doub N N 309 
TE0 N   C6   sing N N 310 
TE0 C6  C5   sing N N 311 
TE0 C5  C4   sing N N 312 
TE0 C3  C4   sing N N 313 
TE0 C4  C7   sing N N 314 
TE0 C7  O2   doub N N 315 
TE0 C7  O3   sing N N 316 
TE0 C4  H1   sing N N 317 
TE0 C5  H2   sing N N 318 
TE0 C5  H3   sing N N 319 
TE0 C6  H4   sing N N 320 
TE0 C6  H5   sing N N 321 
TE0 C   H6   sing N N 322 
TE0 C   H7   sing N N 323 
TE0 C   H8   sing N N 324 
TE0 C1  H9   sing N N 325 
TE0 C1  H10  sing N N 326 
TE0 C2  H11  sing N N 327 
TE0 C2  H12  sing N N 328 
TE0 C3  H13  sing N N 329 
TE0 C3  H14  sing N N 330 
TE0 O3  H15  sing N N 331 
THR N   CA   sing N N 332 
THR N   H    sing N N 333 
THR N   H2   sing N N 334 
THR CA  C    sing N N 335 
THR CA  CB   sing N N 336 
THR CA  HA   sing N N 337 
THR C   O    doub N N 338 
THR C   OXT  sing N N 339 
THR CB  OG1  sing N N 340 
THR CB  CG2  sing N N 341 
THR CB  HB   sing N N 342 
THR OG1 HG1  sing N N 343 
THR CG2 HG21 sing N N 344 
THR CG2 HG22 sing N N 345 
THR CG2 HG23 sing N N 346 
THR OXT HXT  sing N N 347 
TRP N   CA   sing N N 348 
TRP N   H    sing N N 349 
TRP N   H2   sing N N 350 
TRP CA  C    sing N N 351 
TRP CA  CB   sing N N 352 
TRP CA  HA   sing N N 353 
TRP C   O    doub N N 354 
TRP C   OXT  sing N N 355 
TRP CB  CG   sing N N 356 
TRP CB  HB2  sing N N 357 
TRP CB  HB3  sing N N 358 
TRP CG  CD1  doub Y N 359 
TRP CG  CD2  sing Y N 360 
TRP CD1 NE1  sing Y N 361 
TRP CD1 HD1  sing N N 362 
TRP CD2 CE2  doub Y N 363 
TRP CD2 CE3  sing Y N 364 
TRP NE1 CE2  sing Y N 365 
TRP NE1 HE1  sing N N 366 
TRP CE2 CZ2  sing Y N 367 
TRP CE3 CZ3  doub Y N 368 
TRP CE3 HE3  sing N N 369 
TRP CZ2 CH2  doub Y N 370 
TRP CZ2 HZ2  sing N N 371 
TRP CZ3 CH2  sing Y N 372 
TRP CZ3 HZ3  sing N N 373 
TRP CH2 HH2  sing N N 374 
TRP OXT HXT  sing N N 375 
TYR N   CA   sing N N 376 
TYR N   H    sing N N 377 
TYR N   H2   sing N N 378 
TYR CA  C    sing N N 379 
TYR CA  CB   sing N N 380 
TYR CA  HA   sing N N 381 
TYR C   O    doub N N 382 
TYR C   OXT  sing N N 383 
TYR CB  CG   sing N N 384 
TYR CB  HB2  sing N N 385 
TYR CB  HB3  sing N N 386 
TYR CG  CD1  doub Y N 387 
TYR CG  CD2  sing Y N 388 
TYR CD1 CE1  sing Y N 389 
TYR CD1 HD1  sing N N 390 
TYR CD2 CE2  doub Y N 391 
TYR CD2 HD2  sing N N 392 
TYR CE1 CZ   doub Y N 393 
TYR CE1 HE1  sing N N 394 
TYR CE2 CZ   sing Y N 395 
TYR CE2 HE2  sing N N 396 
TYR CZ  OH   sing N N 397 
TYR OH  HH   sing N N 398 
TYR OXT HXT  sing N N 399 
VAL N   CA   sing N N 400 
VAL N   H    sing N N 401 
VAL N   H2   sing N N 402 
VAL CA  C    sing N N 403 
VAL CA  CB   sing N N 404 
VAL CA  HA   sing N N 405 
VAL C   O    doub N N 406 
VAL C   OXT  sing N N 407 
VAL CB  CG1  sing N N 408 
VAL CB  CG2  sing N N 409 
VAL CB  HB   sing N N 410 
VAL CG1 HG11 sing N N 411 
VAL CG1 HG12 sing N N 412 
VAL CG1 HG13 sing N N 413 
VAL CG2 HG21 sing N N 414 
VAL CG2 HG22 sing N N 415 
VAL CG2 HG23 sing N N 416 
VAL OXT HXT  sing N N 417 
# 
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                    7HHA 
_atom_sites.fract_transf_matrix[1][1]   0.024079 
_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]   0.023827 
_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]   0.006323 
_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  ? 0.516   4.147   2.754   1.00 60.76  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.549  3.508   1.934   1.00 60.16  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.069   2.483   0.984   1.00 56.96  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.209   2.630   0.555   1.00 51.25  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.419  4.541   1.203   1.00 64.00  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.417  5.260   2.106   1.00 67.78  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.736  4.292   2.881   1.00 68.51  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.651  5.616   3.680   1.00 74.21  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.650  1.372   0.698   1.00 49.96  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.149  0.300   -0.169  1.00 45.40  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.025   0.704   -1.634  1.00 43.21  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.757  1.506   -2.156  1.00 47.03  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.255  -0.803  -0.022  1.00 45.82  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -2.011  -0.445  1.247   1.00 50.03  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.982  1.073   1.254   1.00 53.91  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.036   0.119   -2.289  1.00 38.51  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.184   0.200   -3.734  1.00 39.56  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.656   -1.108  -4.328  1.00 38.30  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.233   -1.975  -3.574  1.00 37.02  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.660   0.405   -4.099  1.00 51.30  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.248   1.701   -3.632  1.00 61.71  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.018   2.252   -2.388  1.00 68.89  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.079   2.545   -4.261  1.00 66.41  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.681   3.396   -2.282  1.00 66.97  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.331   3.593   -3.411  1.00 68.90  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.687   -1.247  -5.665  1.00 32.81  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.446   -2.516  -6.323  1.00 31.65  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.583   -3.466  -5.962  1.00 30.21  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.628   -3.024  -5.542  1.00 32.59  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.364   -2.296  -7.824  1.00 37.40  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.361   -4.771  -6.101  1.00 32.43  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.389   -5.759  -5.857  1.00 31.99  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.546   -5.586  -6.845  1.00 36.70  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.307   -5.293  -8.018  1.00 33.50  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.748   -7.147  -5.976  1.00 28.21  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.991   -7.575  -4.721  1.00 33.08  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.675   -7.789  -3.520  1.00 30.40  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.388  -7.804  -4.748  1.00 28.47  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.001   -8.141  -2.350  1.00 31.46  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.048  -8.220  -3.589  1.00 24.60  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.357  -8.373  -2.386  1.00 26.24  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.779   -5.866  -6.385  1.00 32.25  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.932   -5.827  -7.272  1.00 31.84  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.848   -7.035  -7.025  1.00 30.35  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.854   -7.613  -5.952  1.00 28.30  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.645   -4.487  -7.028  1.00 32.83  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.293   -4.383  -5.652  1.00 33.52  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.850   -2.993  -5.345  1.00 36.20  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.553   -2.974  -4.020  1.00 38.64  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.661   -3.340  -2.918  1.00 36.55  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.657   -7.479  -8.012  1.00 30.00  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.634   -8.544  -7.777  1.00 31.08  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.399   -8.279  -6.477  1.00 28.76  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.783   -7.142  -6.212  1.00 29.06  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.533   -8.434  -9.056  1.00 31.03  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.557   -8.001  -10.119 1.00 36.07  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.643   -6.991  -9.408  1.00 31.63  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.585   -9.330  -5.659  1.00 26.11  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.296  -9.275  -4.387  1.00 23.78  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.362   -9.148  -3.178  1.00 28.86  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.771   -9.410  -2.034  1.00 30.09  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.105   -8.743  -3.396  1.00 25.92  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.163   -8.671  -2.279  1.00 23.44  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.931   -10.051 -1.660  1.00 24.15  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.749   -11.018 -2.381  1.00 24.89  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.834   -8.048  -2.694  1.00 23.99  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.872   -6.537  -2.884  1.00 29.26  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.878   -5.918  -2.485  1.00 28.16  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.950   -6.005  -3.497  1.00 28.88  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.822   -10.132 -0.318  1.00 24.83  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.620   -11.412 0.369   1.00 27.55  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.161   -11.486 0.824   1.00 28.76  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.564   -10.465 1.176   1.00 27.94  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.574   -11.533 1.577   1.00 25.31  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.057   -11.310 1.243   1.00 24.99  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.999   -11.358 2.433   1.00 27.09  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.472   -12.271 0.147   1.00 26.04  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.591   -12.700 0.825   1.00 22.41  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.157   -12.857 0.973   1.00 24.48  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.932   -14.251 1.544   1.00 28.71  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.830   -15.119 1.499   1.00 27.56  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.384   -12.734 -0.376  1.00 23.96  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.507   -11.343 -1.008  1.00 26.13  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.818   -13.801 -1.378  1.00 24.43  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.714   -14.438 2.052   1.00 27.33  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.104   -15.764 2.092   1.00 27.05  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.157   -15.846 0.902   1.00 28.46  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.603  -14.913 0.656   1.00 25.17  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.327   -16.025 3.393   1.00 27.19  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.258   -16.155 4.582   1.00 27.13  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.619   -15.033 5.326   1.00 29.89  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.820   -17.380 4.910   1.00 29.34  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.482   -15.150 6.402   1.00 33.35  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.691   -17.488 5.994   1.00 32.44  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.031   -16.382 6.724   1.00 34.10  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.246   -16.947 0.136   1.00 26.20  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.514  -17.051 -1.095  1.00 27.37  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.521  -18.182 -0.900  1.00 31.01  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.153  -19.267 -0.423  1.00 30.82  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.400   -17.293 -2.287  1.00 22.05  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.775  -17.918 -1.269  1.00 32.41  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.822  -18.878 -0.963  1.00 30.77  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.230  -19.582 -2.250  1.00 34.42  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.618  -18.936 -3.223  1.00 37.81  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.046  -18.234 -0.295  1.00 32.03  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.148  -19.232 0.122   1.00 38.08  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.630  -20.330 1.059   1.00 39.49  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.690  -21.179 1.719   1.00 42.70  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.418  -21.979 0.729   1.00 40.28  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.129  -20.919 -2.236  1.00 35.93  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.771  -21.689 -3.286  1.00 37.22  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.711  -22.731 -2.692  1.00 36.81  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.517  -23.173 -1.559  1.00 32.49  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.744  -22.372 -4.182  1.00 43.39  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.193  -21.400 -5.210  1.00 49.62  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.820  -22.209 -6.023  1.00 53.91  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -2.781  -23.355 -7.015  1.00 56.30  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.741  -23.051 -3.480  1.00 41.98  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.797  -23.995 -3.128  1.00 48.29  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.185  -25.248 -2.523  1.00 46.35  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.270  -25.823 -3.105  1.00 41.44  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.537  -24.431 -4.400  1.00 59.46  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -10.003 -24.812 -4.215  1.00 67.46  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.947 -23.610 -4.225  1.00 74.41  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.690  -25.648 -1.346  1.00 42.10  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.280  -26.905 -0.742  1.00 46.71  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.888  -26.841 -0.112  1.00 50.25  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.338  -27.866 0.285   1.00 47.44  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.311  -25.641 0.005   1.00 42.92  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -4.069  -25.549 0.752   1.00 41.56  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.188  -24.449 1.791   1.00 38.09  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.896  -23.471 1.570   1.00 37.81  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.839  -25.188 -0.089  1.00 48.56  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.507  -26.192 -1.180  1.00 46.80  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.573  -27.199 -0.977  1.00 52.27  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.133  -26.113 -2.416  1.00 50.85  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.278  -28.108 -1.984  1.00 63.74  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.844  -27.009 -3.430  1.00 59.76  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.920  -28.011 -3.210  1.00 65.91  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.673  -28.868 -4.245  1.00 81.11  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.412  -24.544 2.891   1.00 35.38  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.338  -23.466 3.879   1.00 37.20  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.605  -22.298 3.205   1.00 36.40  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.864  -22.515 2.236   1.00 33.47  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.538  -24.143 5.012   1.00 38.19  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.635  -25.155 4.321   1.00 35.37  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.489  -25.655 3.174   1.00 41.46  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.882  -21.067 3.660   1.00 30.49  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.141  -19.887 3.225   1.00 31.52  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.635  -20.149 3.342   1.00 32.61  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.141  -20.521 4.417   1.00 33.26  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.588  -18.644 4.007   1.00 30.03  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.043  -18.309 3.888   1.00 35.06  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.028  -19.032 4.534   1.00 36.90  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.683  -17.295 3.263   1.00 33.90  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.223  -18.526 4.230   1.00 33.64  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.038  -17.467 3.463   1.00 36.47  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.097   -19.944 2.227   1.00 28.23  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.425   -20.534 2.076   1.00 28.73  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.483   -19.436 1.917   1.00 32.41  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.283   -18.505 1.149   1.00 32.42  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.449   -21.480 0.867   1.00 25.94  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.530   -22.534 0.922   1.00 28.30  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.868   -22.363 0.691   1.00 26.85  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.347   -23.942 1.200   1.00 27.37  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.537   -23.556 0.812   1.00 31.43  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.628   -24.549 1.114   1.00 31.04  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.232   -24.743 1.489   1.00 35.11  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.828   -25.915 1.333   1.00 32.72  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.427   -26.104 1.675   1.00 33.16  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.710   -26.672 1.635   1.00 35.74  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.649   -19.514 2.617   1.00 27.95  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.682   -18.475 2.480   1.00 27.98  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.132   -18.468 1.011   1.00 25.68  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.305   -19.528 0.402   1.00 26.38  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.782   -18.920 3.491   1.00 26.19  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.567   -20.466 3.595   1.00 25.83  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.023   -20.589 3.535   1.00 26.96  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.262   -17.268 0.424   1.00 21.04  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.619   -17.159 -0.987  1.00 21.90  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.191   -15.781 -1.329  1.00 23.71  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.208   -14.880 -0.499  1.00 25.61  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.349   -17.431 -1.800  1.00 25.44  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.669   -15.598 -2.571  1.00 24.40  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.098   -14.255 -2.956  1.00 26.00  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.577   -13.996 -4.375  1.00 25.63  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.261   -14.944 -5.097  1.00 25.71  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.627   -14.125 -2.854  1.00 23.29  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.318   -14.977 -3.921  1.00 24.74  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.876  -14.935 -3.842  1.00 23.91  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.565  -15.750 -4.858  1.00 25.91  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.827  -16.206 -4.791  1.00 25.83  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.520  -16.161 -3.683  1.00 23.88  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.390  -16.748 -5.854  1.00 27.69  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.404   -12.719 -4.747  1.00 21.80  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.209   -12.365 -6.151  1.00 23.16  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.566   -12.481 -6.831  1.00 27.64  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.525   -11.834 -6.395  1.00 26.75  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.711   -10.904 -6.288  1.00 30.33  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.567   -10.534 -5.311  1.00 35.36  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.392   -10.558 -7.754  1.00 29.07  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.226   -11.154 -5.607  1.00 36.00  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.630   -13.298 -7.891  1.00 30.06  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.842   -13.492 -8.662  1.00 33.83  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.948   -12.481 -9.793  1.00 35.08  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 7.956   -11.881 -10.241 1.00 31.09  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.938   -14.875 -9.280  1.00 33.86  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.851   -15.852 -8.559  1.00 31.43  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.431  -15.483 -7.528  1.00 36.40  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 9.968   -16.985 -9.028  1.00 35.80  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.210  -12.284 -10.199 1.00 35.68  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.555  -11.674 -11.467 1.00 39.56  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.241  -12.675 -12.573 1.00 35.00  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.160  -13.880 -12.346 1.00 37.97  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.041  -11.342 -11.501 1.00 44.76  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.452  -10.063 -10.785 1.00 53.89  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.062  -8.967  -11.272 1.00 59.59  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.157  -10.173 -9.750  1.00 56.64  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.092  -12.166 -13.787 1.00 40.08  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.073  -13.011 -14.969 1.00 38.45  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.426  -12.782 -15.629 1.00 38.45  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.754  -11.638 -15.910 1.00 31.90  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.941   -12.526 -15.893 1.00 40.11  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.597   -12.533 -15.144 1.00 40.57  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.911   -13.312 -17.214 1.00 31.94  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.665   -11.406 -15.546 1.00 45.91  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.196  -13.851 -15.836 1.00 32.78  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.506  -13.741 -16.467 1.00 35.74  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.307  -13.468 -17.961 1.00 33.45  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.296  -13.847 -18.547 1.00 29.06  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.289  -15.025 -16.248 1.00 38.33  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.251  -12.744 -18.569 1.00 31.49  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.289  -12.630 -20.023 1.00 27.03  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.049  -14.005 -20.627 1.00 25.57  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.687  -14.967 -20.218 1.00 29.83  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.657  -12.071 -20.410 1.00 30.15  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.781  -10.561 -20.250 1.00 32.03  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.740  -9.900  -20.214 1.00 33.36  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.920  -10.053 -20.188 1.00 36.07  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.130  -14.085 -21.608 1.00 31.31  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.920  -15.298 -22.387 1.00 30.06  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.006  -16.327 -21.725 1.00 32.90  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.768  -17.379 -22.314 1.00 34.69  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.564  -16.045 -20.488 1.00 30.49  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.719  -16.923 -19.680 1.00 32.76  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.243   -16.649 -19.976 1.00 30.39  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.870   -15.549 -20.356 1.00 31.97  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.009  -16.710 -18.181 1.00 32.75  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.399   -17.665 -19.765 1.00 35.81  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.955   -17.545 -19.919 1.00 32.27  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.364   -16.506 -18.969 1.00 30.10  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.567   -16.565 -17.755 1.00 33.72  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.278   -18.914 -19.711 1.00 35.96  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.759   -18.769 -19.776 1.00 38.18  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 6.759   -19.912 -20.767 1.00 38.24  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.633   -15.558 -19.558 1.00 34.45  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.925   -14.510 -18.848 1.00 35.84  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.609   -15.063 -18.317 1.00 39.07  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.016   -15.942 -18.934 1.00 36.43  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.615   -13.310 -19.752 1.00 35.98  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.860   -12.465 -20.106 1.00 34.83  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.480   -11.312 -21.029 1.00 36.87  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.364   -11.746 -22.459 1.00 38.19  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.811   -10.690 -23.311 1.00 38.52  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.131   -14.552 -17.157 1.00 40.68  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.817   -14.914 -16.623 1.00 38.59  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.677   -14.316 -17.437 1.00 41.21  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.879   -13.350 -18.160 1.00 37.63  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.825   -14.332 -15.191 1.00 40.61  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.861   -13.208 -15.212 1.00 44.31  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.835   -13.564 -16.324 1.00 40.80  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.567  -14.837 -17.313 1.00 41.14  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.727  -14.180 -17.919 1.00 43.92  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.852  -12.760 -17.378 1.00 43.45  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.249  -12.425 -16.348 1.00 38.44  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.935  -15.056 -17.542 1.00 38.38  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.320  -16.378 -17.130 1.00 37.89  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.910  -16.094 -16.623 1.00 39.65  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.638  -11.888 -18.052 1.00 48.53  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.860  -10.521 -17.574 1.00 47.89  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.598  -10.576 -16.242 1.00 45.61  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.404  -11.470 -16.011 1.00 44.59  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.740  -9.915  -18.679 1.00 52.15  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.432  -11.108 -19.289 1.00 45.38  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.355  -12.177 -19.309 1.00 54.36  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.280  -9.614  -15.374 1.00 45.49  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.848  -9.492  -14.042 1.00 47.99  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.278  -10.537 -13.082 1.00 43.25  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.655  -10.530 -11.916 1.00 45.36  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.370  -9.359  -14.073 1.00 51.97  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.800  -8.164  -14.887 1.00 55.46  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.536  -7.019  -14.504 1.00 52.88  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.423  -8.410  -16.028 1.00 63.52  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.371  -11.410 -13.551 1.00 37.01  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.800  -12.453 -12.697 1.00 31.47  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.305  -12.192 -12.448 1.00 31.34  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.355   -11.544 -13.256 1.00 35.78  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.058  -13.872 -13.219 1.00 30.21  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.521  -14.230 -13.527 1.00 39.72  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.469  -14.017 -12.352 1.00 41.85  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.925  -14.346 -12.617 1.00 47.79  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.091  -15.807 -12.721 1.00 46.98  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.197   -12.678 -11.299 1.00 27.18  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.589   -12.527 -10.875 1.00 25.84  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.186   -13.917 -10.825 1.00 26.13  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.459   -14.868 -10.539 1.00 28.15  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.649   -11.934 -9.450  1.00 25.45  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.232   -10.473 -9.436  1.00 28.03  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.115  -10.118 -9.380  1.00 34.33  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.169   -9.459  -9.530  1.00 31.24  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.509  -8.792  -9.446  1.00 31.05  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.793   -8.128  -9.577  1.00 32.96  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.451   -7.802  -9.513  1.00 34.31  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? 0.078   -6.486  -9.561  1.00 39.81  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.509   -14.083 -11.081 1.00 26.01  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.172   -15.369 -10.866 1.00 23.90  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.459   -15.499 -9.364  1.00 25.67  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.105   -14.637 -8.761  1.00 28.66  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.464   -15.262 -11.680 1.00 28.59  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.726   -13.785 -11.801 1.00 27.63  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.439   -13.007 -11.478 1.00 31.06  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.991   -16.584 -8.757  1.00 20.87  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.142   -16.705 -7.302  1.00 20.43  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.075   -17.879 -7.066  1.00 26.72  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.763   -19.005 -7.455  1.00 29.33  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.788   -16.939 -6.612  1.00 22.52  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.770   -15.822 -6.939  1.00 21.97  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 2.998   -17.094 -5.079  1.00 22.29  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.236   -14.391 -6.622  1.00 20.61  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.228   -17.619 -6.442  1.00 25.83  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.102   -18.717 -6.057  1.00 27.50  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.775   -19.126 -4.617  1.00 27.22  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.844   -18.310 -3.712  1.00 29.04  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.530   -18.166 -6.187  1.00 24.52  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.555   -19.210 -5.762  1.00 29.53  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.969   -20.209 -6.650  1.00 29.80  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.048  -19.230 -4.451  1.00 29.89  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.892  -21.162 -6.243  1.00 32.93  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 10.971  -20.196 -4.059  1.00 33.32  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.395  -21.141 -4.958  1.00 29.24  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.383   -20.394 -4.390  1.00 27.39  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 5.992   -20.832 -3.058  1.00 24.73  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.252   -21.380 -2.407  1.00 28.10  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 7.940   -22.242 -3.002  1.00 28.06  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.008   -22.018 -3.191  1.00 25.95  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.637   -21.552 -3.677  1.00 28.52  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.351   -21.418 -5.048  1.00 28.47  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.643   -21.212 -2.761  1.00 27.77  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.112   -20.931 -5.484  1.00 28.54  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.407   -20.754 -3.204  1.00 28.19  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.135   -20.623 -4.558  1.00 31.12  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.554   -20.868 -1.210  1.00 29.10  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.679   -21.363 -0.431  1.00 31.46  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.422   -22.820 -0.040  1.00 29.55  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.265   -23.256 0.046   1.00 31.27  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 8.959   -20.404 0.722   1.00 29.42  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.428   -19.009 0.315   1.00 25.98  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.697  -18.810 -0.243  1.00 25.07  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.646   -17.887 0.589   1.00 25.22  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.142  -17.531 -0.586  1.00 26.46  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.105   -16.605 0.250   1.00 24.40  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.359  -16.428 -0.336  1.00 25.35  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.517   -23.576 0.136   1.00 31.68  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.430   -24.955 0.601   1.00 34.87  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.235   -25.919 -0.567  1.00 35.89  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.122  -26.714 -0.872  1.00 38.52  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.103   -25.805 -1.263  1.00 37.76  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 7.834   -26.639 -2.428  1.00 38.75  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.660   -26.162 -3.616  1.00 39.06  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 8.937   -26.930 -4.536  1.00 36.29  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.340   -26.613 -2.754  1.00 37.69  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.031   -25.240 -2.997  1.00 36.75  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.484   -27.138 -1.621  1.00 41.95  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.966   -24.855 -3.644  1.00 30.65  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.658   -24.256 -4.769  1.00 32.57  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.863   -24.370 -6.061  1.00 34.07  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.455   -24.328 -7.144  1.00 37.70  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.099  -24.783 -4.911  1.00 32.98  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.803  -24.801 -3.607  1.00 33.99  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.617  -25.836 -3.216  1.00 38.00  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.795  -23.907 -2.591  1.00 31.89  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.080  -25.575 -1.992  1.00 39.57  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.620  -24.391 -1.613  1.00 36.63  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.532   -24.448 -5.961  1.00 36.83  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.681   -24.427 -7.145  1.00 35.65  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.241   -23.006 -7.493  1.00 32.46  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.306   -22.130 -6.644  1.00 33.53  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.457   -25.289 -6.865  1.00 39.54  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.858   -26.749 -6.685  1.00 51.27  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.717   -27.676 -6.341  1.00 60.67  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.548   -27.225 -6.351  1.00 57.98  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.027   -28.850 -6.028  1.00 71.48  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.872   -22.776 -8.768  1.00 30.04  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.314   -21.501 -9.212  1.00 32.52  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.862   -21.695 -9.677  1.00 31.44  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.533   -22.673 -10.342 1.00 36.14  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.191   -20.901 -10.325 1.00 37.20  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.503   -20.601 -9.843  1.00 33.53  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.602   -19.630 -10.923 1.00 37.35  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 2.980   -20.748 -9.338  1.00 28.37  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.667   -20.661 -9.957  1.00 27.95  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.374   -19.188 -10.194 1.00 31.18  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.051   -18.338 -9.622  1.00 27.73  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.590   -21.282 -9.063  1.00 30.80  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.356   -18.922 -11.013 1.00 30.60  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.046  -17.575 -11.376 1.00 35.24  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.296  -17.232 -10.576 1.00 37.50  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.294  -17.954 -10.660 1.00 38.98  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.289  -17.632 -12.893 1.00 33.15  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.918   -17.939 -13.778 1.00 36.36  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.172   -17.378 -13.516 1.00 37.38  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.785   -18.743 -14.915 1.00 38.03  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.262   -17.654 -14.342 1.00 47.95  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.874   -19.004 -15.744 1.00 39.33  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.113   -18.473 -15.448 1.00 41.27  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.227  -16.135 -9.805  1.00 30.29  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.318  -15.756 -8.936  1.00 29.58  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.608  -14.264 -9.059  1.00 31.02  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.725  -13.459 -9.382  1.00 30.80  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.971  -16.122 -7.485  1.00 28.77  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.736  -17.601 -7.160  1.00 33.64  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.451  -17.674 -5.654  1.00 35.26  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.961  -18.407 -7.479  1.00 39.69  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.873  -13.901 -8.802  1.00 30.90  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.236  -12.495 -8.697  1.00 29.26  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.235  -12.035 -7.235  1.00 30.42  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.122  -12.859 -6.330  1.00 28.01  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.300  -10.705 -6.994  1.00 28.66  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.267  -10.115 -5.652  1.00 28.50  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.246  -10.689 -4.634  1.00 28.45  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.955  -10.715 -3.432  1.00 28.14  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.539  -8.630  -5.898  1.00 29.59  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -4.089  -8.417  -7.328  1.00 31.50  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.361  -9.702  -8.061  1.00 30.20  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.413  -11.149 -5.105  1.00 28.53  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.393  -11.674 -4.154  1.00 28.92  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.804  -12.791 -3.289  1.00 31.66  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.270  -13.031 -2.166  1.00 29.37  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.661  -12.187 -4.849  1.00 34.09  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.528  -13.489 -5.622  1.00 38.53  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.782  -13.851 -6.428  1.00 46.40  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.619  -15.143 -7.172  1.00 48.59  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.462  -16.297 -6.273  1.00 50.09  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.765  -13.466 -3.798  1.00 28.17  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.208  -14.608 -3.108  1.00 27.39  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.853  -14.283 -2.460  1.00 27.46  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.171  -15.200 -1.994  1.00 30.45  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.146  -15.810 -4.043  1.00 32.05  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.506  -16.401 -4.386  1.00 34.93  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.347  -16.452 -3.457  1.00 35.35  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.709  -16.768 -5.577  1.00 33.32  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.481  -12.993 -2.415  1.00 25.80  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.133  -12.600 -1.994  1.00 25.61  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.234  -11.754 -0.718  1.00 25.85  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.868  -10.694 -0.734  1.00 28.62  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.410  -11.858 -3.124  1.00 26.78  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.300  -12.604 -4.457  1.00 26.03  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.647  -11.755 -5.497  1.00 27.27  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.507  -13.917 -4.315  1.00 25.33  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.627  -12.242 0.372   1.00 24.36  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.731  -11.594 1.686   1.00 24.32  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.344  -11.143 2.106   1.00 23.06  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.553   -11.969 2.307   1.00 26.47  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.245  -12.609 2.709   1.00 26.69  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.693  -13.024 2.460   1.00 31.16  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -4.014  -13.955 1.471   1.00 28.88  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.723  -12.518 3.255   1.00 31.12  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.339  -14.308 1.230   1.00 37.34  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.051  -12.884 3.024   1.00 31.50  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.357  -13.799 2.040   1.00 30.65  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.112  -9.820  2.185   1.00 25.01  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.215   -9.309  2.531   1.00 26.51  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.760   -9.860  3.850   1.00 28.07  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.076   -9.908  4.867   1.00 27.30  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.101   -7.759  2.509   1.00 26.32  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.216  -7.494  1.753   1.00 29.43  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.086  -8.762  1.855   1.00 24.85  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.029   -10.271 3.798   1.00 28.08  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.636   -11.151 4.783   1.00 28.57  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.671   -10.485 6.157   1.00 26.36  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.279   -11.118 7.118   1.00 33.38  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.046   -11.579 4.331   1.00 30.51  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.809   -12.355 5.400   1.00 32.46  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.531   -13.700 5.631   1.00 32.12  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.839   -11.766 6.135   1.00 33.22  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.225   -14.424 6.590   1.00 34.43  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.545   -12.488 7.093   1.00 36.08  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.234   -13.818 7.316   1.00 39.01  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.895   -14.559 8.259   1.00 42.67  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.094   -9.214  6.246   1.00 32.22  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.259   -8.559  7.543   1.00 34.15  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.925   -8.542  8.298   1.00 36.79  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.834   -9.010  9.435   1.00 38.11  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.912   -7.193  7.388   1.00 31.46  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.867   -8.077  7.619   1.00 37.00  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.527   -8.012  8.199   1.00 34.70  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? -0.015  -9.383  8.614   1.00 33.62  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.789  -9.465  9.560   1.00 39.06  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.430  -7.341  7.203   1.00 35.39  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.888  -7.295  7.642   1.00 38.07  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.667  -6.462  6.645   1.00 38.21  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.707  -5.660  7.367   1.00 45.12  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.906  -6.432  7.670   1.00 47.73  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.368   -10.462 7.925   1.00 32.97  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.360  -11.732 8.007   1.00 34.49  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.377   -12.808 8.786   1.00 36.84  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.189  -13.880 9.016   1.00 34.23  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.621  -12.288 6.619   1.00 36.46  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.508  -11.419 5.946   1.00 43.92  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.645   -12.548 9.131   1.00 34.99  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.501   -13.612 9.637   1.00 38.29  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.011   -14.115 10.998  1.00 37.81  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.086   -15.313 11.284  1.00 35.93  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 3.991   -13.253 9.590   1.00 43.93  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.429   -12.035 10.379  1.00 44.71  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 5.947   -12.096 10.490  1.00 54.96  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.561   -10.973 11.274  1.00 60.91  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.300   -9.671  10.653  1.00 64.73  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.465   -13.213 11.818  0.50 38.08  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.508   -13.206 11.837  0.50 38.04  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.009   -13.613 13.145  0.50 41.41  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.010   -13.655 13.130  0.50 40.93  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? -0.212  -14.533 13.040  0.50 41.25  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? -0.048  -14.734 12.908  0.50 40.54  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.516  -15.275 13.968  0.50 44.34  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? -0.075  -15.752 13.600  0.50 37.66  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.913   -12.424 14.094  0.50 40.45  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.489   -12.519 13.998  0.50 41.17  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 2.252   -11.803 14.475  0.50 42.99  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? 0.145   -12.945 15.416  0.50 44.70  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.287   -12.466 14.261  0.50 42.96  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 1.094   -13.189 16.198  0.50 46.38  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 2.254   -10.648 14.949  0.50 41.17  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.063  -13.114 15.702  0.50 47.09  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.889  -14.536 11.886  1.00 39.46  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -2.003  -15.445 11.682  1.00 39.57  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.580  -16.744 10.992  1.00 41.51  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -2.082  -17.822 11.336  1.00 38.41  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -3.136  -14.715 10.955  1.00 45.72  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.432  -15.496 10.873  1.00 45.71  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.447  -14.551 10.240  1.00 51.35  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.844  -15.074 10.089  1.00 53.08  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.663  -14.101 9.352   1.00 51.70  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.717  -16.635 9.971   1.00 35.66  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.538  -17.727 9.029   1.00 33.29  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 0.834   -18.394 9.199   1.00 33.85  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.029   -19.508 8.716   1.00 34.78  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.712  -17.251 7.575   1.00 31.02  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -2.121  -16.804 7.183   1.00 34.32  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.254  -17.541 7.539   1.00 37.41  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.321  -15.631 6.455   1.00 34.24  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.536  -17.135 7.179   1.00 40.22  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.597  -15.214 6.088   1.00 38.88  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.706  -15.962 6.456   1.00 40.59  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.965  -15.561 6.103   1.00 36.93  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.746   -17.747 9.919   1.00 32.64  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.137   -18.169 9.996   1.00 39.24  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.356   -19.142 11.156  1.00 40.95  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.139   -18.871 12.048  1.00 42.75  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.655   -20.276 11.108  1.00 37.55  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.698   -21.282 12.152  1.00 40.68  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 2.961   -22.616 11.476  1.00 39.10  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.590   -22.791 10.318  1.00 37.50  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.417   -21.287 12.999  1.00 42.08  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.273   -20.048 13.889  1.00 48.03  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? -0.149  -19.604 14.225  1.00 52.34  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.663   -23.563 12.136  1.00 38.92  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 3.915   -24.877 11.536  1.00 38.13  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.665   -25.585 11.041  1.00 39.10  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.609   -25.488 11.649  1.00 44.97  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.629   -25.649 12.667  1.00 45.59  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.307   -24.549 13.458  1.00 46.21  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.311   -23.390 13.452  1.00 39.94  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 2.805   -26.261 9.905   1.00 38.97  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.729   -27.000 9.279   1.00 47.55  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.302   -28.358 8.893   1.00 54.16  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.507   -28.482 8.663   1.00 56.59  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.172   -26.211 8.100   1.00 49.81  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? -0.118  -26.777 7.557   1.00 51.83  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? -0.097  -27.773 6.834   1.00 57.31  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -1.242  -26.139 7.852   1.00 53.45  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.426   -29.364 8.817   1.00 60.40  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 1.842   -30.734 8.563   1.00 58.26  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.230   -30.917 7.090   1.00 60.07  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.099   -31.735 6.779   1.00 55.62  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.798   -31.709 9.135   1.00 59.86  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.521  -31.886 8.376   1.00 59.08  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.624   -30.116 6.199   1.00 52.64  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 1.752   -30.282 4.753   1.00 52.00  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.209   -30.220 4.296   1.00 46.65  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.009   -29.477 4.859   1.00 48.46  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 0.907   -29.247 3.997   1.00 51.18  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.576  -29.337 4.318   1.00 50.31  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -1.172  -30.546 3.606   1.00 53.35  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.938  -30.167 2.414   1.00 72.17  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -3.120  -29.554 2.462   1.00 75.37  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.752  -29.258 1.341   1.00 72.88  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.671  -29.251 3.631   1.00 79.94  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.511   -30.982 3.234   1.00 41.67  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 4.839   -31.160 2.666   1.00 41.97  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.427   -29.825 2.228   1.00 39.95  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 4.860   -29.143 1.374   1.00 37.14  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 4.770   -32.021 1.400   1.00 43.41  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.071   -32.284 0.670   1.00 47.06  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 5.964   -33.577 -0.137  1.00 52.87  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.167   -33.836 -0.991  1.00 49.69  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.595   -29.506 2.796   1.00 38.73  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.367   -28.358 2.369   1.00 34.85  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 6.961   -27.073 3.086   1.00 34.40  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.642   -26.064 2.925   1.00 34.25  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 5.889   -27.097 3.888   1.00 34.44  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.435   -25.887 4.568   1.00 36.91  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.461   -25.317 5.565   1.00 36.97  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.696   -24.091 5.641   1.00 32.95  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.089   -26.148 5.250   1.00 35.45  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.372   -24.855 5.622   1.00 34.55  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.666   -24.179 6.804   1.00 35.16  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.401   -24.323 4.782   1.00 35.08  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.028   -22.986 7.126   1.00 34.00  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.762   -23.127 5.098   1.00 28.24  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.055   -22.487 6.294   1.00 29.50  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.034   -26.187 6.396   1.00 34.31  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 7.893   -25.689 7.462   1.00 35.47  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.242   -25.232 6.899   1.00 36.76  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 9.838   -24.266 7.412   1.00 34.19  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.018   -26.662 8.633   1.00 39.97  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.685   -26.933 9.295   1.00 46.47  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 5.826   -26.049 9.341   1.00 36.69  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.492   -28.142 9.811   1.00 36.92  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.696   -25.927 5.843   1.00 35.83  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 10.827  -25.472 5.034   1.00 32.00  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.522  -24.063 4.538   1.00 30.47  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.340  -23.148 4.688   1.00 26.54  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.188  -26.431 3.902   1.00 35.06  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.434  -26.025 3.111   1.00 39.74  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 12.908  -27.032 2.073   1.00 45.92  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.330  -28.116 2.014   1.00 48.50  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 13.860  -26.765 1.328   1.00 51.89  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.306   -23.901 3.995   1.00 32.12  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 8.811   -22.625 3.492   1.00 30.33  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 8.868   -21.493 4.512   1.00 26.56  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.268   -20.359 4.189   1.00 30.05  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.435   -21.777 5.739   1.00 27.99  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.515   -20.806 6.818   1.00 29.21  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 9.953   -20.363 7.073   1.00 29.78  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.197  -19.164 7.276   1.00 26.28  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 7.866   -21.273 8.114   1.00 28.97  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.363   -21.571 8.058   1.00 31.43  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 5.954   -22.187 9.396   1.00 30.58  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.570   -20.276 7.853   1.00 30.60  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 10.893  -21.323 7.094   1.00 27.98  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.290  -20.969 7.317   1.00 28.67  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.782  -20.025 6.226   1.00 29.72  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.435  -19.031 6.522   1.00 33.05  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.199  -22.209 7.412   1.00 31.54  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.642  -21.833 7.638   1.00 32.72  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.263  -21.652 8.844   1.00 35.57  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.621  -21.518 6.628   1.00 28.71  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.572  -21.291 8.652   1.00 35.08  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 16.813  -21.183 7.306   1.00 32.48  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.600  -21.498 5.225   1.00 28.16  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 17.975  -20.828 6.624   1.00 30.11  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.740  -21.134 4.549   1.00 32.99  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 17.920  -20.811 5.250   1.00 34.02  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.450  -20.332 4.960   1.00 31.09  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 12.989  -19.593 3.829   1.00 25.34  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.464  -18.155 3.832   1.00 26.90  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.245  -17.218 3.698   1.00 26.45  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.701  -20.290 2.502   1.00 27.42  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.282  -21.703 2.373   1.00 29.60  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 12.867  -22.445 1.095   1.00 34.36  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 11.970  -21.912 0.430   1.00 30.91  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.349  -23.579 0.753   1.00 33.14  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.145  -17.971 4.031   1.00 26.86  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.571  -16.627 4.018   1.00 24.38  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.160  -15.733 5.119   1.00 30.05  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.265  -14.491 4.970   1.00 30.22  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.026   -16.672 4.048   1.00 27.16  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.433   -15.280 3.624   1.00 27.91  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.457   -17.162 5.400   1.00 24.85  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.039   -15.353 3.014   1.00 24.87  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.499  -16.341 6.268   1.00 29.15  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 11.998  -15.573 7.398   1.00 28.35  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.504  -15.337 7.234   1.00 32.62  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 13.969  -14.251 7.576   1.00 31.79  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.646  -16.329 8.686   1.00 33.34  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.018  -15.622 9.991   1.00 43.36  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.321  -16.179 11.228  1.00 50.77  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.020  -17.385 11.344  1.00 42.28  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.040  -15.279 12.167  1.00 43.38  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.235  -16.333 6.692   1.00 27.62  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.697  -16.367 6.765   1.00 29.08  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.411  -16.016 5.459   1.00 27.70  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.507  -15.454 5.528   1.00 29.89  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.221  -17.589 7.519   1.00 32.54  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.661  -17.626 8.934   1.00 33.91  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 15.966  -16.750 9.751   1.00 38.68  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.771  -18.558 9.231   1.00 32.85  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 15.842  -16.324 4.279   1.00 27.40  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.515  -15.979 3.023   1.00 30.39  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.477  -15.866 1.895   1.00 27.59  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.510  -16.608 0.913   1.00 29.87  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.691  -16.906 2.693   1.00 33.40  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.770  -16.234 1.868   1.00 35.32  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.520  -15.207 1.218   1.00 28.73  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 19.990  -16.784 1.881   1.00 33.70  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.520  -14.918 2.014   1.00 27.49  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.376  -14.864 1.106   1.00 24.20  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.740  -14.444 -0.319  1.00 27.30  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 12.949  -14.695 -1.213  1.00 28.48  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.436  -13.880 1.807   1.00 25.11  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.378  -12.933 2.565   1.00 27.29  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.457  -13.893 3.074   1.00 27.91  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 14.931  -13.830 -0.530  1.00 26.89  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.340  -13.298 -1.825  1.00 25.76  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.442  -14.143 -2.489  1.00 29.24  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 16.936  -13.786 -3.574  1.00 29.71  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.684  -11.800 -1.691  1.00 25.62  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.596  -10.968 -1.108  1.00 28.44  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.372  -10.757 -1.729  1.00 28.09  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.535  -10.321 0.068   1.00 28.59  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.627  -9.962  -0.964  1.00 25.00  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.310  -9.703  0.144   1.00 30.12  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.742  -15.323 -1.918  1.00 30.11  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.768  -16.208 -2.463  1.00 29.08  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.308  -16.873 -3.754  1.00 30.66  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.123  -16.905 -4.078  1.00 29.26  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.186  -17.240 -1.454  1.00 27.15  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.282  -17.421 -4.488  1.00 30.83  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 17.992  -18.325 -5.590  1.00 35.40  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.696  -19.728 -5.045  1.00 36.41  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.458  -20.252 -4.230  1.00 40.72  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.132  -18.330 -6.576  1.00 38.20  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 18.868  -19.339 -7.536  1.00 48.46  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.546  -20.295 -5.423  1.00 35.59  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.147  -21.632 -4.996  1.00 39.71  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.018  -22.586 -6.182  1.00 45.93  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.443  -23.655 -6.031  1.00 50.55  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 14.800  -21.643 -4.250  1.00 35.99  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 14.939  -21.035 -2.866  1.00 33.35  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.345  -21.804 -1.776  1.00 33.63  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.690  -19.679 -2.663  1.00 34.22  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.490  -21.249 -0.514  1.00 35.86  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.810  -19.111 -1.405  1.00 32.04  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.225  -19.896 -0.337  1.00 32.86  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.399  -19.323 0.873   1.00 29.57  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.549  -22.190 -7.346  1.00 52.95  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.439  -22.947 -8.587  1.00 64.86  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 16.940  -24.389 -8.386  1.00 72.79  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 17.976  -24.556 -7.692  1.00 78.15  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.197  -22.263 -9.701  1.00 64.48  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 17.018  -20.852 -9.647  1.00 75.28  ? 93  SER A OG  1 
ATOM   753  N N   . MET B 1 2  ? 38.888  -10.973 -41.584 1.00 81.98  ? 1   MET B N   1 
ATOM   754  C CA  . MET B 1 2  ? 38.544  -11.853 -42.731 1.00 78.23  ? 1   MET B CA  1 
ATOM   755  C C   . MET B 1 2  ? 37.021  -11.986 -42.827 1.00 71.70  ? 1   MET B C   1 
ATOM   756  O O   . MET B 1 2  ? 36.350  -12.197 -41.817 1.00 69.75  ? 1   MET B O   1 
ATOM   757  C CB  . MET B 1 2  ? 39.197  -13.230 -42.554 1.00 89.01  ? 1   MET B CB  1 
ATOM   758  C CG  . MET B 1 2  ? 39.428  -13.988 -43.853 1.00 104.77 ? 1   MET B CG  1 
ATOM   759  S SD  . MET B 1 2  ? 40.731  -13.259 -44.869 1.00 108.84 ? 1   MET B SD  1 
ATOM   760  C CE  . MET B 1 2  ? 42.115  -13.398 -43.728 1.00 111.05 ? 1   MET B CE  1 
ATOM   761  N N   . PRO B 1 3  ? 36.410  -11.848 -44.031 1.00 62.58  ? 2   PRO B N   1 
ATOM   762  C CA  . PRO B 1 3  ? 34.969  -12.057 -44.178 1.00 59.34  ? 2   PRO B CA  1 
ATOM   763  C C   . PRO B 1 3  ? 34.587  -13.480 -43.765 1.00 57.84  ? 2   PRO B C   1 
ATOM   764  O O   . PRO B 1 3  ? 35.357  -14.418 -43.977 1.00 48.96  ? 2   PRO B O   1 
ATOM   765  C CB  . PRO B 1 3  ? 34.681  -11.750 -45.662 1.00 61.85  ? 2   PRO B CB  1 
ATOM   766  C CG  . PRO B 1 3  ? 35.878  -10.935 -46.107 1.00 59.97  ? 2   PRO B CG  1 
ATOM   767  C CD  . PRO B 1 3  ? 37.055  -11.456 -45.295 1.00 57.48  ? 2   PRO B CD  1 
ATOM   768  N N   . HIS B 1 4  ? 33.414  -13.609 -43.128 1.00 54.49  ? 3   HIS B N   1 
ATOM   769  C CA  . HIS B 1 4  ? 32.922  -14.889 -42.647 1.00 57.79  ? 3   HIS B CA  1 
ATOM   770  C C   . HIS B 1 4  ? 31.544  -15.142 -43.251 1.00 53.86  ? 3   HIS B C   1 
ATOM   771  O O   . HIS B 1 4  ? 30.945  -14.225 -43.816 1.00 49.22  ? 3   HIS B O   1 
ATOM   772  C CB  . HIS B 1 4  ? 32.966  -14.949 -41.117 1.00 62.31  ? 3   HIS B CB  1 
ATOM   773  C CG  . HIS B 1 4  ? 34.345  -15.091 -40.554 1.00 78.35  ? 3   HIS B CG  1 
ATOM   774  N ND1 . HIS B 1 4  ? 35.300  -15.936 -41.084 1.00 86.95  ? 3   HIS B ND1 1 
ATOM   775  C CD2 . HIS B 1 4  ? 34.916  -14.509 -39.486 1.00 71.87  ? 3   HIS B CD2 1 
ATOM   776  C CE1 . HIS B 1 4  ? 36.405  -15.855 -40.356 1.00 81.64  ? 3   HIS B CE1 1 
ATOM   777  N NE2 . HIS B 1 4  ? 36.191  -14.991 -39.382 1.00 76.05  ? 3   HIS B NE2 1 
ATOM   778  N N   . ALA B 1 5  ? 31.072  -16.400 -43.162 1.00 45.04  ? 4   ALA B N   1 
ATOM   779  C CA  . ALA B 1 5  ? 29.762  -16.756 -43.671 1.00 43.67  ? 4   ALA B CA  1 
ATOM   780  C C   . ALA B 1 5  ? 28.761  -15.717 -43.184 1.00 47.77  ? 4   ALA B C   1 
ATOM   781  O O   . ALA B 1 5  ? 28.007  -15.172 -43.988 1.00 44.70  ? 4   ALA B O   1 
ATOM   782  C CB  . ALA B 1 5  ? 29.364  -18.134 -43.195 1.00 49.64  ? 4   ALA B CB  1 
ATOM   783  N N   . PHE B 1 6  ? 28.792  -15.482 -41.862 1.00 45.86  ? 5   PHE B N   1 
ATOM   784  C CA  . PHE B 1 6  ? 28.000  -14.462 -41.194 1.00 50.64  ? 5   PHE B CA  1 
ATOM   785  C C   . PHE B 1 6  ? 28.865  -13.234 -40.916 1.00 48.58  ? 5   PHE B C   1 
ATOM   786  O O   . PHE B 1 6  ? 29.986  -13.336 -40.413 1.00 50.65  ? 5   PHE B O   1 
ATOM   787  C CB  . PHE B 1 6  ? 27.389  -14.984 -39.885 1.00 44.84  ? 5   PHE B CB  1 
ATOM   788  C CG  . PHE B 1 6  ? 26.299  -16.044 -40.012 1.00 38.42  ? 5   PHE B CG  1 
ATOM   789  C CD1 . PHE B 1 6  ? 24.960  -15.685 -40.171 1.00 35.68  ? 5   PHE B CD1 1 
ATOM   790  C CD2 . PHE B 1 6  ? 26.612  -17.397 -39.924 1.00 38.44  ? 5   PHE B CD2 1 
ATOM   791  C CE1 . PHE B 1 6  ? 23.968  -16.651 -40.280 1.00 35.32  ? 5   PHE B CE1 1 
ATOM   792  C CE2 . PHE B 1 6  ? 25.619  -18.364 -40.038 1.00 35.00  ? 5   PHE B CE2 1 
ATOM   793  C CZ  . PHE B 1 6  ? 24.298  -17.996 -40.194 1.00 33.31  ? 5   PHE B CZ  1 
ATOM   794  N N   . LYS B 1 7  ? 28.306  -12.060 -41.206 1.00 50.90  ? 6   LYS B N   1 
ATOM   795  C CA  . LYS B 1 7  ? 29.034  -10.814 -41.026 1.00 51.76  ? 6   LYS B CA  1 
ATOM   796  C C   . LYS B 1 7  ? 28.267  -9.908  -40.060 1.00 55.61  ? 6   LYS B C   1 
ATOM   797  O O   . LYS B 1 7  ? 27.027  -9.930  -40.027 1.00 45.49  ? 6   LYS B O   1 
ATOM   798  C CB  . LYS B 1 7  ? 29.281  -10.198 -42.406 1.00 52.92  ? 6   LYS B CB  1 
ATOM   799  C CG  . LYS B 1 7  ? 28.058  -9.864  -43.244 1.00 58.20  ? 6   LYS B CG  1 
ATOM   800  C CD  . LYS B 1 7  ? 28.455  -9.422  -44.648 1.00 62.47  ? 6   LYS B CD  1 
ATOM   801  C CE  . LYS B 1 7  ? 27.346  -8.813  -45.437 1.00 62.27  ? 6   LYS B CE  1 
ATOM   802  N NZ  . LYS B 1 7  ? 26.276  -9.773  -45.720 1.00 70.24  ? 6   LYS B NZ  1 
ATOM   803  N N   . PRO B 1 8  ? 28.971  -9.049  -39.280 1.00 54.70  ? 7   PRO B N   1 
ATOM   804  C CA  . PRO B 1 8  ? 28.309  -8.170  -38.316 1.00 47.96  ? 7   PRO B CA  1 
ATOM   805  C C   . PRO B 1 8  ? 27.175  -7.417  -38.984 1.00 41.38  ? 7   PRO B C   1 
ATOM   806  O O   . PRO B 1 8  ? 27.301  -6.957  -40.118 1.00 53.19  ? 7   PRO B O   1 
ATOM   807  C CB  . PRO B 1 8  ? 29.476  -7.273  -37.927 1.00 52.41  ? 7   PRO B CB  1 
ATOM   808  C CG  . PRO B 1 8  ? 30.636  -8.244  -37.919 1.00 52.63  ? 7   PRO B CG  1 
ATOM   809  C CD  . PRO B 1 8  ? 30.436  -8.856  -39.293 1.00 54.94  ? 7   PRO B CD  1 
ATOM   810  N N   . GLY B 1 9  ? 26.034  -7.354  -38.293 1.00 38.20  ? 8   GLY B N   1 
ATOM   811  C CA  . GLY B 1 9  ? 24.862  -6.718  -38.863 1.00 34.26  ? 8   GLY B CA  1 
ATOM   812  C C   . GLY B 1 9  ? 23.908  -7.714  -39.514 1.00 37.02  ? 8   GLY B C   1 
ATOM   813  O O   . GLY B 1 9  ? 22.797  -7.344  -39.873 1.00 34.33  ? 8   GLY B O   1 
ATOM   814  N N   . ASP B 1 10 ? 24.324  -8.986  -39.644 1.00 34.68  ? 9   ASP B N   1 
ATOM   815  C CA  . ASP B 1 10 ? 23.474  -10.001 -40.262 1.00 32.97  ? 9   ASP B CA  1 
ATOM   816  C C   . ASP B 1 10 ? 22.279  -10.313 -39.355 1.00 29.74  ? 9   ASP B C   1 
ATOM   817  O O   . ASP B 1 10 ? 22.444  -10.386 -38.141 1.00 31.92  ? 9   ASP B O   1 
ATOM   818  C CB  . ASP B 1 10 ? 24.269  -11.272 -40.541 1.00 33.18  ? 9   ASP B CB  1 
ATOM   819  C CG  . ASP B 1 10 ? 24.946  -11.353 -41.915 1.00 43.02  ? 9   ASP B CG  1 
ATOM   820  O OD1 . ASP B 1 10 ? 24.700  -10.470 -42.758 1.00 42.87  ? 9   ASP B OD1 1 
ATOM   821  O OD2 . ASP B 1 10 ? 25.698  -12.330 -42.144 1.00 45.86  ? 9   ASP B OD2 1 
ATOM   822  N N   . LEU B 1 11 ? 21.075  -10.424 -39.918 1.00 28.82  ? 10  LEU B N   1 
ATOM   823  C CA  . LEU B 1 11 ? 19.932  -10.667 -39.050 1.00 31.75  ? 10  LEU B CA  1 
ATOM   824  C C   . LEU B 1 11 ? 19.620  -12.162 -39.046 1.00 31.20  ? 10  LEU B C   1 
ATOM   825  O O   . LEU B 1 11 ? 19.675  -12.777 -40.093 1.00 30.82  ? 10  LEU B O   1 
ATOM   826  C CB  . LEU B 1 11 ? 18.761  -9.844  -39.560 1.00 28.47  ? 10  LEU B CB  1 
ATOM   827  C CG  . LEU B 1 11 ? 19.077  -8.335  -39.606 1.00 25.63  ? 10  LEU B CG  1 
ATOM   828  C CD1 . LEU B 1 11 ? 17.847  -7.602  -40.114 1.00 29.97  ? 10  LEU B CD1 1 
ATOM   829  C CD2 . LEU B 1 11 ? 19.527  -7.874  -38.221 1.00 28.79  ? 10  LEU B CD2 1 
ATOM   830  N N   . VAL B 1 12 ? 19.257  -12.714 -37.885 1.00 28.02  ? 11  VAL B N   1 
ATOM   831  C CA  . VAL B 1 12 ? 18.984  -14.154 -37.810 1.00 28.29  ? 11  VAL B CA  1 
ATOM   832  C C   . VAL B 1 12 ? 17.860  -14.445 -36.814 1.00 31.80  ? 11  VAL B C   1 
ATOM   833  O O   . VAL B 1 12 ? 17.434  -13.566 -36.064 1.00 27.27  ? 11  VAL B O   1 
ATOM   834  C CB  . VAL B 1 12 ? 20.271  -14.887 -37.397 1.00 28.54  ? 11  VAL B CB  1 
ATOM   835  C CG1 . VAL B 1 12 ? 21.447  -14.651 -38.364 1.00 26.78  ? 11  VAL B CG1 1 
ATOM   836  C CG2 . VAL B 1 12 ? 20.666  -14.601 -35.940 1.00 29.30  ? 11  VAL B CG2 1 
ATOM   837  N N   . PHE B 1 13 ? 17.389  -15.709 -36.788 1.00 28.41  ? 12  PHE B N   1 
ATOM   838  C CA  . PHE B 1 13 ? 16.892  -16.234 -35.528 1.00 28.02  ? 12  PHE B CA  1 
ATOM   839  C C   . PHE B 1 13 ? 17.973  -17.123 -34.932 1.00 31.58  ? 12  PHE B C   1 
ATOM   840  O O   . PHE B 1 13 ? 18.533  -17.949 -35.673 1.00 28.86  ? 12  PHE B O   1 
ATOM   841  C CB  . PHE B 1 13 ? 15.615  -17.067 -35.678 1.00 26.50  ? 12  PHE B CB  1 
ATOM   842  C CG  . PHE B 1 13 ? 14.425  -16.222 -36.096 1.00 31.96  ? 12  PHE B CG  1 
ATOM   843  C CD1 . PHE B 1 13 ? 14.164  -15.990 -37.446 1.00 35.82  ? 12  PHE B CD1 1 
ATOM   844  C CD2 . PHE B 1 13 ? 13.537  -15.723 -35.155 1.00 30.70  ? 12  PHE B CD2 1 
ATOM   845  C CE1 . PHE B 1 13 ? 13.058  -15.246 -37.831 1.00 36.52  ? 12  PHE B CE1 1 
ATOM   846  C CE2 . PHE B 1 13 ? 12.437  -14.958 -35.541 1.00 32.09  ? 12  PHE B CE2 1 
ATOM   847  C CZ  . PHE B 1 13 ? 12.199  -14.730 -36.879 1.00 37.69  ? 12  PHE B CZ  1 
ATOM   848  N N   . ALA B 1 14 ? 18.213  -16.961 -33.605 1.00 27.78  ? 13  ALA B N   1 
ATOM   849  C CA  . ALA B 1 14 ? 19.251  -17.699 -32.890 1.00 29.27  ? 13  ALA B CA  1 
ATOM   850  C C   . ALA B 1 14 ? 18.615  -18.673 -31.896 1.00 28.54  ? 13  ALA B C   1 
ATOM   851  O O   . ALA B 1 14 ? 17.708  -18.283 -31.152 1.00 27.44  ? 13  ALA B O   1 
ATOM   852  C CB  . ALA B 1 14 ? 20.147  -16.731 -32.159 1.00 29.04  ? 13  ALA B CB  1 
ATOM   853  N N   . LYS B 1 15 ? 19.076  -19.932 -31.890 1.00 29.98  ? 14  LYS B N   1 
ATOM   854  C CA  . LYS B 1 15 ? 18.396  -20.971 -31.106 1.00 30.02  ? 14  LYS B CA  1 
ATOM   855  C C   . LYS B 1 15 ? 19.247  -21.327 -29.895 1.00 30.02  ? 14  LYS B C   1 
ATOM   856  O O   . LYS B 1 15 ? 20.423  -21.676 -30.054 1.00 35.60  ? 14  LYS B O   1 
ATOM   857  C CB  . LYS B 1 15 ? 18.151  -22.260 -31.919 1.00 29.64  ? 14  LYS B CB  1 
ATOM   858  C CG  . LYS B 1 15 ? 17.398  -23.388 -31.126 1.00 29.43  ? 14  LYS B CG  1 
ATOM   859  C CD  . LYS B 1 15 ? 15.968  -22.956 -30.797 1.00 30.08  ? 14  LYS B CD  1 
ATOM   860  C CE  . LYS B 1 15 ? 15.057  -24.057 -30.204 1.00 29.05  ? 14  LYS B CE  1 
ATOM   861  N NZ  . LYS B 1 15 ? 15.524  -24.291 -28.839 1.00 28.05  ? 14  LYS B NZ  1 
ATOM   862  N N   . MET B 1 16 ? 18.655  -21.210 -28.694 1.00 30.21  ? 15  MET B N   1 
ATOM   863  C CA  . MET B 1 16 ? 19.283  -21.721 -27.486 1.00 38.21  ? 15  MET B CA  1 
ATOM   864  C C   . MET B 1 16 ? 18.350  -22.694 -26.778 1.00 35.13  ? 15  MET B C   1 
ATOM   865  O O   . MET B 1 16 ? 17.122  -22.527 -26.807 1.00 31.87  ? 15  MET B O   1 
ATOM   866  C CB  . MET B 1 16 ? 19.599  -20.596 -26.499 1.00 38.38  ? 15  MET B CB  1 
ATOM   867  C CG  . MET B 1 16 ? 20.336  -19.453 -27.137 1.00 45.93  ? 15  MET B CG  1 
ATOM   868  S SD  . MET B 1 16 ? 21.581  -18.588 -26.165 1.00 46.38  ? 15  MET B SD  1 
ATOM   869  C CE  . MET B 1 16 ? 21.612  -19.130 -24.452 1.00 44.36  ? 15  MET B CE  1 
ATOM   870  N N   . LYS B 1 17 ? 18.960  -23.674 -26.105 1.00 32.70  ? 16  LYS B N   1 
ATOM   871  C CA  . LYS B 1 17 ? 18.219  -24.667 -25.335 1.00 37.04  ? 16  LYS B CA  1 
ATOM   872  C C   . LYS B 1 17 ? 17.305  -23.964 -24.322 1.00 31.18  ? 16  LYS B C   1 
ATOM   873  O O   . LYS B 1 17 ? 17.735  -23.042 -23.636 1.00 38.87  ? 16  LYS B O   1 
ATOM   874  C CB  . LYS B 1 17 ? 19.157  -25.700 -24.690 1.00 42.83  ? 16  LYS B CB  1 
ATOM   875  C CG  . LYS B 1 17 ? 18.410  -26.779 -23.881 1.00 50.10  ? 16  LYS B CG  1 
ATOM   876  C CD  . LYS B 1 17 ? 19.231  -27.986 -23.429 1.00 55.20  ? 16  LYS B CD  1 
ATOM   877  N N   . GLY B 1 18 ? 16.024  -24.353 -24.315 1.00 34.30  ? 17  GLY B N   1 
ATOM   878  C CA  . GLY B 1 18 ? 15.024  -23.827 -23.387 1.00 34.83  ? 17  GLY B CA  1 
ATOM   879  C C   . GLY B 1 18 ? 14.207  -22.652 -23.951 1.00 34.75  ? 17  GLY B C   1 
ATOM   880  O O   . GLY B 1 18 ? 13.334  -22.120 -23.272 1.00 36.96  ? 17  GLY B O   1 
ATOM   881  N N   . TYR B 1 19 ? 14.450  -22.263 -25.214 1.00 33.39  ? 18  TYR B N   1 
ATOM   882  C CA  . TYR B 1 19 ? 13.848  -21.052 -25.755 1.00 30.11  ? 18  TYR B CA  1 
ATOM   883  C C   . TYR B 1 19 ? 13.482  -21.292 -27.219 1.00 31.74  ? 18  TYR B C   1 
ATOM   884  O O   . TYR B 1 19 ? 14.168  -22.027 -27.928 1.00 35.79  ? 18  TYR B O   1 
ATOM   885  C CB  . TYR B 1 19 ? 14.876  -19.914 -25.683 1.00 27.97  ? 18  TYR B CB  1 
ATOM   886  C CG  . TYR B 1 19 ? 15.363  -19.605 -24.277 1.00 32.74  ? 18  TYR B CG  1 
ATOM   887  C CD1 . TYR B 1 19 ? 14.556  -18.908 -23.364 1.00 32.82  ? 18  TYR B CD1 1 
ATOM   888  C CD2 . TYR B 1 19 ? 16.622  -20.016 -23.859 1.00 35.77  ? 18  TYR B CD2 1 
ATOM   889  C CE1 . TYR B 1 19 ? 14.988  -18.680 -22.065 1.00 33.67  ? 18  TYR B CE1 1 
ATOM   890  C CE2 . TYR B 1 19 ? 17.076  -19.755 -22.573 1.00 34.15  ? 18  TYR B CE2 1 
ATOM   891  C CZ  . TYR B 1 19 ? 16.262  -19.075 -21.687 1.00 35.61  ? 18  TYR B CZ  1 
ATOM   892  O OH  . TYR B 1 19 ? 16.762  -18.881 -20.436 1.00 41.30  ? 18  TYR B OH  1 
ATOM   893  N N   . PRO B 1 20 ? 12.418  -20.659 -27.754 1.00 28.10  ? 19  PRO B N   1 
ATOM   894  C CA  . PRO B 1 20 ? 12.171  -20.735 -29.200 1.00 25.70  ? 19  PRO B CA  1 
ATOM   895  C C   . PRO B 1 20 ? 13.261  -19.965 -29.952 1.00 26.69  ? 19  PRO B C   1 
ATOM   896  O O   . PRO B 1 20 ? 13.923  -19.104 -29.368 1.00 27.10  ? 19  PRO B O   1 
ATOM   897  C CB  . PRO B 1 20 ? 10.804  -20.089 -29.330 1.00 26.15  ? 19  PRO B CB  1 
ATOM   898  C CG  . PRO B 1 20 ? 10.792  -19.054 -28.182 1.00 32.14  ? 19  PRO B CG  1 
ATOM   899  C CD  . PRO B 1 20 ? 11.473  -19.798 -27.031 1.00 29.56  ? 19  PRO B CD  1 
ATOM   900  N N   . HIS B 1 21 ? 13.418  -20.273 -31.252 1.00 25.60  ? 20  HIS B N   1 
ATOM   901  C CA  . HIS B 1 21 ? 14.324  -19.551 -32.134 1.00 26.66  ? 20  HIS B CA  1 
ATOM   902  C C   . HIS B 1 21 ? 14.053  -18.067 -31.936 1.00 25.36  ? 20  HIS B C   1 
ATOM   903  O O   . HIS B 1 21 ? 12.882  -17.642 -31.999 1.00 28.65  ? 20  HIS B O   1 
ATOM   904  C CB  . HIS B 1 21 ? 14.080  -19.984 -33.596 1.00 25.46  ? 20  HIS B CB  1 
ATOM   905  C CG  . HIS B 1 21 ? 14.219  -21.489 -33.796 1.00 26.45  ? 20  HIS B CG  1 
ATOM   906  N ND1 . HIS B 1 21 ? 13.276  -22.428 -33.437 1.00 30.79  ? 20  HIS B ND1 1 
ATOM   907  C CD2 . HIS B 1 21 ? 15.247  -22.205 -34.287 1.00 28.90  ? 20  HIS B CD2 1 
ATOM   908  C CE1 . HIS B 1 21 ? 13.707  -23.667 -33.730 1.00 27.32  ? 20  HIS B CE1 1 
ATOM   909  N NE2 . HIS B 1 21 ? 14.911  -23.555 -34.224 1.00 28.12  ? 20  HIS B NE2 1 
ATOM   910  N N   . TRP B 1 22 ? 15.121  -17.277 -31.779 1.00 22.64  ? 21  TRP B N   1 
ATOM   911  C CA  . TRP B 1 22 ? 14.909  -15.934 -31.223 1.00 25.79  ? 21  TRP B CA  1 
ATOM   912  C C   . TRP B 1 22 ? 15.436  -14.828 -32.138 1.00 30.58  ? 21  TRP B C   1 
ATOM   913  O O   . TRP B 1 22 ? 16.575  -14.927 -32.578 1.00 32.65  ? 21  TRP B O   1 
ATOM   914  C CB  . TRP B 1 22 ? 15.584  -15.828 -29.836 1.00 26.59  ? 21  TRP B CB  1 
ATOM   915  C CG  . TRP B 1 22 ? 15.074  -14.682 -28.987 1.00 27.38  ? 21  TRP B CG  1 
ATOM   916  C CD1 . TRP B 1 22 ? 15.323  -13.336 -29.100 1.00 31.02  ? 21  TRP B CD1 1 
ATOM   917  C CD2 . TRP B 1 22 ? 14.152  -14.819 -27.884 1.00 31.01  ? 21  TRP B CD2 1 
ATOM   918  N NE1 . TRP B 1 22 ? 14.615  -12.616 -28.159 1.00 27.54  ? 21  TRP B NE1 1 
ATOM   919  C CE2 . TRP B 1 22 ? 13.880  -13.513 -27.399 1.00 29.72  ? 21  TRP B CE2 1 
ATOM   920  C CE3 . TRP B 1 22 ? 13.530  -15.928 -27.277 1.00 29.79  ? 21  TRP B CE3 1 
ATOM   921  C CZ2 . TRP B 1 22 ? 13.026  -13.303 -26.310 1.00 29.36  ? 21  TRP B CZ2 1 
ATOM   922  C CZ3 . TRP B 1 22 ? 12.676  -15.715 -26.209 1.00 30.18  ? 21  TRP B CZ3 1 
ATOM   923  C CH2 . TRP B 1 22 ? 12.398  -14.407 -25.765 1.00 31.17  ? 21  TRP B CH2 1 
ATOM   924  N N   . PRO B 1 23 ? 14.672  -13.738 -32.433 1.00 28.36  ? 22  PRO B N   1 
ATOM   925  C CA  . PRO B 1 23 ? 15.122  -12.720 -33.388 1.00 30.17  ? 22  PRO B CA  1 
ATOM   926  C C   . PRO B 1 23 ? 16.413  -12.142 -32.828 1.00 27.61  ? 22  PRO B C   1 
ATOM   927  O O   . PRO B 1 23 ? 16.515  -11.863 -31.635 1.00 29.27  ? 22  PRO B O   1 
ATOM   928  C CB  . PRO B 1 23 ? 13.919  -11.695 -33.394 1.00 27.67  ? 22  PRO B CB  1 
ATOM   929  C CG  . PRO B 1 23 ? 13.328  -11.862 -32.003 1.00 26.40  ? 22  PRO B CG  1 
ATOM   930  C CD  . PRO B 1 23 ? 13.327  -13.421 -31.917 1.00 27.38  ? 22  PRO B CD  1 
ATOM   931  N N   . ALA B 1 24 ? 17.445  -12.020 -33.671 1.00 29.10  ? 23  ALA B N   1 
ATOM   932  C CA  . ALA B 1 24 ? 18.755  -11.647 -33.170 1.00 28.61  ? 23  ALA B CA  1 
ATOM   933  C C   . ALA B 1 24 ? 19.615  -11.083 -34.304 1.00 26.86  ? 23  ALA B C   1 
ATOM   934  O O   . ALA B 1 24 ? 19.189  -11.060 -35.459 1.00 29.56  ? 23  ALA B O   1 
ATOM   935  C CB  . ALA B 1 24 ? 19.434  -12.824 -32.466 1.00 27.16  ? 23  ALA B CB  1 
ATOM   936  N N   . ARG B 1 25 ? 20.826  -10.626 -33.951 1.00 30.84  ? 24  ARG B N   1 
ATOM   937  C CA  . ARG B 1 25 ? 21.762  -10.126 -34.950 1.00 31.58  ? 24  ARG B CA  1 
ATOM   938  C C   . ARG B 1 25 ? 23.163  -10.604 -34.610 1.00 27.05  ? 24  ARG B C   1 
ATOM   939  O O   . ARG B 1 25 ? 23.464  -10.875 -33.454 1.00 29.91  ? 24  ARG B O   1 
ATOM   940  C CB  . ARG B 1 25 ? 21.756  -8.590  -35.006 1.00 27.82  ? 24  ARG B CB  1 
ATOM   941  C CG  . ARG B 1 25 ? 22.310  -7.874  -33.788 1.00 30.49  ? 24  ARG B CG  1 
ATOM   942  C CD  . ARG B 1 25 ? 22.008  -6.363  -33.977 1.00 31.40  ? 24  ARG B CD  1 
ATOM   943  N NE  . ARG B 1 25 ? 22.681  -5.634  -32.903 1.00 32.39  ? 24  ARG B NE  1 
ATOM   944  C CZ  . ARG B 1 25 ? 22.423  -4.377  -32.538 1.00 32.58  ? 24  ARG B CZ  1 
ATOM   945  N NH1 . ARG B 1 25 ? 21.508  -3.676  -33.179 1.00 28.70  ? 24  ARG B NH1 1 
ATOM   946  N NH2 . ARG B 1 25 ? 23.082  -3.859  -31.526 1.00 31.25  ? 24  ARG B NH2 1 
ATOM   947  N N   . ILE B 1 26 ? 24.020  -10.678 -35.639 1.00 27.90  ? 25  ILE B N   1 
ATOM   948  C CA  . ILE B 1 26 ? 25.448  -10.854 -35.430 1.00 31.08  ? 25  ILE B CA  1 
ATOM   949  C C   . ILE B 1 26 ? 26.004  -9.476  -35.074 1.00 34.74  ? 25  ILE B C   1 
ATOM   950  O O   . ILE B 1 26 ? 25.762  -8.519  -35.807 1.00 33.76  ? 25  ILE B O   1 
ATOM   951  C CB  . ILE B 1 26 ? 26.098  -11.364 -36.729 1.00 34.12  ? 25  ILE B CB  1 
ATOM   952  C CG1 . ILE B 1 26 ? 25.338  -12.569 -37.308 1.00 38.34  ? 25  ILE B CG1 1 
ATOM   953  C CG2 . ILE B 1 26 ? 27.600  -11.623 -36.543 1.00 37.71  ? 25  ILE B CG2 1 
ATOM   954  C CD1 . ILE B 1 26 ? 25.344  -13.801 -36.422 1.00 32.86  ? 25  ILE B CD1 1 
ATOM   955  N N   . ASP B 1 27 ? 26.722  -9.409  -33.952 1.00 36.53  ? 26  ASP B N   1 
ATOM   956  C CA  . ASP B 1 27 ? 27.401  -8.209  -33.485 1.00 42.47  ? 26  ASP B CA  1 
ATOM   957  C C   . ASP B 1 27 ? 28.891  -8.224  -33.871 1.00 52.56  ? 26  ASP B C   1 
ATOM   958  O O   . ASP B 1 27 ? 29.474  -9.288  -34.117 1.00 46.59  ? 26  ASP B O   1 
ATOM   959  C CB  . ASP B 1 27 ? 27.258  -8.110  -31.972 1.00 41.08  ? 26  ASP B CB  1 
ATOM   960  C CG  . ASP B 1 27 ? 26.065  -7.316  -31.450 1.00 39.30  ? 26  ASP B CG  1 
ATOM   961  O OD1 . ASP B 1 27 ? 25.376  -6.692  -32.287 1.00 37.82  ? 26  ASP B OD1 1 
ATOM   962  O OD2 . ASP B 1 27 ? 25.878  -7.281  -30.197 1.00 38.68  ? 26  ASP B OD2 1 
ATOM   963  N N   A ASP B 1 28 ? 29.482  -7.017  -33.911 0.50 57.16  ? 27  ASP B N   1 
ATOM   964  N N   B ASP B 1 28 ? 29.507  -7.033  -33.911 0.50 58.05  ? 27  ASP B N   1 
ATOM   965  C CA  A ASP B 1 28 ? 30.914  -6.772  -34.029 0.50 60.31  ? 27  ASP B CA  1 
ATOM   966  C CA  B ASP B 1 28 ? 30.941  -6.907  -34.133 0.50 61.31  ? 27  ASP B CA  1 
ATOM   967  C C   A ASP B 1 28 ? 31.621  -7.220  -32.753 0.50 62.96  ? 27  ASP B C   1 
ATOM   968  C C   B ASP B 1 28 ? 31.662  -7.074  -32.796 0.50 62.98  ? 27  ASP B C   1 
ATOM   969  O O   A ASP B 1 28 ? 31.001  -7.255  -31.691 0.50 63.77  ? 27  ASP B O   1 
ATOM   970  O O   B ASP B 1 28 ? 31.089  -6.787  -31.744 0.50 61.19  ? 27  ASP B O   1 
ATOM   971  C CB  A ASP B 1 28 ? 31.199  -5.287  -34.206 0.50 53.78  ? 27  ASP B CB  1 
ATOM   972  C CB  B ASP B 1 28 ? 31.287  -5.601  -34.836 0.50 60.31  ? 27  ASP B CB  1 
ATOM   973  C CG  A ASP B 1 28 ? 30.999  -4.745  -35.612 0.50 56.74  ? 27  ASP B CG  1 
ATOM   974  C CG  B ASP B 1 28 ? 32.463  -5.678  -35.802 0.50 60.44  ? 27  ASP B CG  1 
ATOM   975  O OD1 A ASP B 1 28 ? 31.649  -5.274  -36.540 0.50 58.97  ? 27  ASP B OD1 1 
ATOM   976  O OD1 B ASP B 1 28 ? 33.538  -6.156  -35.384 0.50 63.69  ? 27  ASP B OD1 1 
ATOM   977  O OD2 A ASP B 1 28 ? 30.211  -3.790  -35.768 0.50 53.36  ? 27  ASP B OD2 1 
ATOM   978  O OD2 B ASP B 1 28 ? 32.294  -5.267  -36.970 0.50 60.47  ? 27  ASP B OD2 1 
ATOM   979  N N   . ILE B 1 29 ? 32.926  -7.520  -32.864 1.00 70.12  ? 28  ILE B N   1 
ATOM   980  C CA  . ILE B 1 29 ? 33.727  -7.948  -31.717 1.00 64.85  ? 28  ILE B CA  1 
ATOM   981  C C   . ILE B 1 29 ? 34.370  -6.736  -31.014 1.00 65.69  ? 28  ILE B C   1 
ATOM   982  O O   . ILE B 1 29 ? 34.590  -5.706  -31.698 1.00 70.96  ? 28  ILE B O   1 
ATOM   983  C CB  . ILE B 1 29 ? 34.783  -8.990  -32.135 1.00 65.03  ? 28  ILE B CB  1 
ATOM   984  N N   . VAL B 1 34 ? 35.851  -9.923  -24.374 1.00 71.15  ? 33  VAL B N   1 
ATOM   985  C CA  . VAL B 1 34 ? 36.378  -11.287 -24.684 1.00 74.50  ? 33  VAL B CA  1 
ATOM   986  C C   . VAL B 1 34 ? 35.968  -11.666 -26.104 1.00 77.24  ? 33  VAL B C   1 
ATOM   987  O O   . VAL B 1 34 ? 34.807  -11.497 -26.469 1.00 87.99  ? 33  VAL B O   1 
ATOM   988  C CB  . VAL B 1 34 ? 35.922  -12.319 -23.629 1.00 72.17  ? 33  VAL B CB  1 
ATOM   989  C CG1 . VAL B 1 34 ? 35.053  -11.691 -22.544 1.00 70.06  ? 33  VAL B CG1 1 
ATOM   990  C CG2 . VAL B 1 34 ? 35.280  -13.568 -24.234 1.00 63.25  ? 33  VAL B CG2 1 
ATOM   991  N N   . LYS B 1 35 ? 36.934  -12.163 -26.892 1.00 77.51  ? 34  LYS B N   1 
ATOM   992  C CA  . LYS B 1 35 ? 36.695  -12.579 -28.271 1.00 74.38  ? 34  LYS B CA  1 
ATOM   993  C C   . LYS B 1 35 ? 35.969  -13.929 -28.295 1.00 71.36  ? 34  LYS B C   1 
ATOM   994  O O   . LYS B 1 35 ? 36.284  -14.821 -27.500 1.00 67.08  ? 34  LYS B O   1 
ATOM   995  C CB  . LYS B 1 35 ? 37.984  -12.600 -29.106 1.00 66.13  ? 34  LYS B CB  1 
ATOM   996  N N   . PRO B 1 36 ? 34.978  -14.119 -29.207 1.00 66.76  ? 35  PRO B N   1 
ATOM   997  C CA  . PRO B 1 36 ? 34.169  -15.347 -29.252 1.00 58.98  ? 35  PRO B CA  1 
ATOM   998  C C   . PRO B 1 36 ? 35.014  -16.611 -29.376 1.00 54.37  ? 35  PRO B C   1 
ATOM   999  O O   . PRO B 1 36 ? 36.078  -16.570 -29.984 1.00 52.66  ? 35  PRO B O   1 
ATOM   1000 C CB  . PRO B 1 36 ? 33.280  -15.133 -30.495 1.00 58.14  ? 35  PRO B CB  1 
ATOM   1001 C CG  . PRO B 1 36 ? 34.017  -14.096 -31.310 1.00 65.33  ? 35  PRO B CG  1 
ATOM   1002 C CD  . PRO B 1 36 ? 34.597  -13.161 -30.260 1.00 67.19  ? 35  PRO B CD  1 
ATOM   1003 N N   . PRO B 1 37 ? 34.594  -17.767 -28.803 1.00 57.77  ? 36  PRO B N   1 
ATOM   1004 C CA  . PRO B 1 37 ? 35.354  -19.005 -28.960 1.00 54.75  ? 36  PRO B CA  1 
ATOM   1005 C C   . PRO B 1 37 ? 35.468  -19.313 -30.453 1.00 60.58  ? 36  PRO B C   1 
ATOM   1006 O O   . PRO B 1 37 ? 34.708  -18.777 -31.266 1.00 56.43  ? 36  PRO B O   1 
ATOM   1007 C CB  . PRO B 1 37 ? 34.540  -20.074 -28.203 1.00 54.57  ? 36  PRO B CB  1 
ATOM   1008 C CG  . PRO B 1 37 ? 33.591  -19.290 -27.307 1.00 52.30  ? 36  PRO B CG  1 
ATOM   1009 C CD  . PRO B 1 37 ? 33.387  -17.942 -27.976 1.00 56.06  ? 36  PRO B CD  1 
ATOM   1010 N N   . PRO B 1 38 ? 36.413  -20.189 -30.868 1.00 63.61  ? 37  PRO B N   1 
ATOM   1011 C CA  . PRO B 1 38 ? 36.482  -20.630 -32.265 1.00 64.94  ? 37  PRO B CA  1 
ATOM   1012 C C   . PRO B 1 38 ? 35.137  -21.155 -32.780 1.00 61.04  ? 37  PRO B C   1 
ATOM   1013 O O   . PRO B 1 38 ? 34.405  -21.824 -32.048 1.00 60.07  ? 37  PRO B O   1 
ATOM   1014 C CB  . PRO B 1 38 ? 37.566  -21.735 -32.228 1.00 68.83  ? 37  PRO B CB  1 
ATOM   1015 C CG  . PRO B 1 38 ? 38.429  -21.396 -31.023 1.00 63.69  ? 37  PRO B CG  1 
ATOM   1016 C CD  . PRO B 1 38 ? 37.453  -20.799 -30.018 1.00 71.33  ? 37  PRO B CD  1 
ATOM   1017 N N   . ASN B 1 39 ? 34.826  -20.817 -34.041 1.00 52.59  ? 38  ASN B N   1 
ATOM   1018 C CA  . ASN B 1 39 ? 33.644  -21.268 -34.767 1.00 54.09  ? 38  ASN B CA  1 
ATOM   1019 C C   . ASN B 1 39 ? 32.400  -20.422 -34.464 1.00 52.25  ? 38  ASN B C   1 
ATOM   1020 O O   . ASN B 1 39 ? 31.435  -20.478 -35.212 1.00 51.08  ? 38  ASN B O   1 
ATOM   1021 C CB  . ASN B 1 39 ? 33.353  -22.751 -34.562 1.00 53.86  ? 38  ASN B CB  1 
ATOM   1022 C CG  . ASN B 1 39 ? 34.479  -23.647 -35.025 1.00 65.58  ? 38  ASN B CG  1 
ATOM   1023 O OD1 . ASN B 1 39 ? 34.699  -24.709 -34.435 1.00 70.80  ? 38  ASN B OD1 1 
ATOM   1024 N ND2 . ASN B 1 39 ? 35.184  -23.263 -36.081 1.00 71.68  ? 38  ASN B ND2 1 
ATOM   1025 N N   . LYS B 1 40 ? 32.415  -19.639 -33.379 1.00 46.56  ? 39  LYS B N   1 
ATOM   1026 C CA  . LYS B 1 40 ? 31.198  -19.052 -32.845 1.00 45.29  ? 39  LYS B CA  1 
ATOM   1027 C C   . LYS B 1 40 ? 31.188  -17.552 -33.095 1.00 49.61  ? 39  LYS B C   1 
ATOM   1028 O O   . LYS B 1 40 ? 32.223  -16.949 -33.367 1.00 48.83  ? 39  LYS B O   1 
ATOM   1029 C CB  . LYS B 1 40 ? 31.149  -19.349 -31.346 1.00 43.17  ? 39  LYS B CB  1 
ATOM   1030 C CG  . LYS B 1 40 ? 30.883  -20.802 -30.943 1.00 42.27  ? 39  LYS B CG  1 
ATOM   1031 C CD  . LYS B 1 40 ? 30.948  -20.869 -29.421 1.00 55.48  ? 39  LYS B CD  1 
ATOM   1032 C CE  . LYS B 1 40 ? 29.865  -21.636 -28.712 1.00 59.15  ? 39  LYS B CE  1 
ATOM   1033 N NZ  . LYS B 1 40 ? 29.979  -23.093 -28.779 1.00 60.58  ? 39  LYS B NZ  1 
ATOM   1034 N N   . TYR B 1 41 ? 30.000  -16.953 -32.982 1.00 43.71  ? 40  TYR B N   1 
ATOM   1035 C CA  . TYR B 1 41 ? 29.874  -15.520 -33.178 1.00 42.76  ? 40  TYR B CA  1 
ATOM   1036 C C   . TYR B 1 41 ? 29.268  -14.870 -31.941 1.00 42.20  ? 40  TYR B C   1 
ATOM   1037 O O   . TYR B 1 41 ? 28.527  -15.517 -31.204 1.00 39.48  ? 40  TYR B O   1 
ATOM   1038 C CB  . TYR B 1 41 ? 28.913  -15.257 -34.338 1.00 37.31  ? 40  TYR B CB  1 
ATOM   1039 C CG  . TYR B 1 41 ? 29.415  -15.732 -35.695 1.00 42.36  ? 40  TYR B CG  1 
ATOM   1040 C CD1 . TYR B 1 41 ? 30.118  -14.869 -36.526 1.00 37.84  ? 40  TYR B CD1 1 
ATOM   1041 C CD2 . TYR B 1 41 ? 29.165  -17.024 -36.149 1.00 39.19  ? 40  TYR B CD2 1 
ATOM   1042 C CE1 . TYR B 1 41 ? 30.589  -15.282 -37.765 1.00 44.83  ? 40  TYR B CE1 1 
ATOM   1043 C CE2 . TYR B 1 41 ? 29.626  -17.448 -37.392 1.00 39.51  ? 40  TYR B CE2 1 
ATOM   1044 C CZ  . TYR B 1 41 ? 30.355  -16.581 -38.193 1.00 44.44  ? 40  TYR B CZ  1 
ATOM   1045 O OH  . TYR B 1 41 ? 30.813  -16.981 -39.428 1.00 44.17  ? 40  TYR B OH  1 
ATOM   1046 N N   . PRO B 1 42 ? 29.499  -13.548 -31.753 1.00 40.60  ? 41  PRO B N   1 
ATOM   1047 C CA  . PRO B 1 42 ? 28.716  -12.751 -30.816 1.00 35.88  ? 41  PRO B CA  1 
ATOM   1048 C C   . PRO B 1 42 ? 27.306  -12.500 -31.331 1.00 36.72  ? 41  PRO B C   1 
ATOM   1049 O O   . PRO B 1 42 ? 27.103  -11.864 -32.366 1.00 39.35  ? 41  PRO B O   1 
ATOM   1050 C CB  . PRO B 1 42 ? 29.508  -11.425 -30.706 1.00 35.79  ? 41  PRO B CB  1 
ATOM   1051 C CG  . PRO B 1 42 ? 30.288  -11.324 -31.996 1.00 36.54  ? 41  PRO B CG  1 
ATOM   1052 C CD  . PRO B 1 42 ? 30.521  -12.754 -32.460 1.00 41.54  ? 41  PRO B CD  1 
ATOM   1053 N N   . ILE B 1 43 ? 26.337  -12.959 -30.544 1.00 31.58  ? 42  ILE B N   1 
ATOM   1054 C CA  . ILE B 1 43 ? 24.930  -12.742 -30.830 1.00 33.84  ? 42  ILE B CA  1 
ATOM   1055 C C   . ILE B 1 43 ? 24.360  -11.701 -29.872 1.00 31.65  ? 42  ILE B C   1 
ATOM   1056 O O   . ILE B 1 43 ? 24.682  -11.705 -28.681 1.00 34.22  ? 42  ILE B O   1 
ATOM   1057 C CB  . ILE B 1 43 ? 24.201  -14.089 -30.687 1.00 25.80  ? 42  ILE B CB  1 
ATOM   1058 C CG1 . ILE B 1 43 ? 25.014  -15.206 -31.359 1.00 29.97  ? 42  ILE B CG1 1 
ATOM   1059 C CG2 . ILE B 1 43 ? 22.776  -13.986 -31.236 1.00 32.76  ? 42  ILE B CG2 1 
ATOM   1060 C CD1 . ILE B 1 43 ? 25.270  -15.001 -32.846 1.00 29.11  ? 42  ILE B CD1 1 
ATOM   1061 N N   . PHE B 1 44 ? 23.491  -10.839 -30.421 1.00 31.49  ? 43  PHE B N   1 
ATOM   1062 C CA  . PHE B 1 44 ? 22.657  -9.910  -29.669 1.00 31.68  ? 43  PHE B CA  1 
ATOM   1063 C C   . PHE B 1 44 ? 21.195  -10.283 -29.899 1.00 25.94  ? 43  PHE B C   1 
ATOM   1064 O O   . PHE B 1 44 ? 20.702  -10.306 -31.041 1.00 30.03  ? 43  PHE B O   1 
ATOM   1065 C CB  . PHE B 1 44 ? 22.889  -8.446  -30.080 1.00 28.70  ? 43  PHE B CB  1 
ATOM   1066 C CG  . PHE B 1 44 ? 21.958  -7.435  -29.417 1.00 28.36  ? 43  PHE B CG  1 
ATOM   1067 C CD1 . PHE B 1 44 ? 20.809  -6.992  -30.069 1.00 33.07  ? 43  PHE B CD1 1 
ATOM   1068 C CD2 . PHE B 1 44 ? 22.259  -6.885  -28.168 1.00 36.76  ? 43  PHE B CD2 1 
ATOM   1069 C CE1 . PHE B 1 44 ? 19.988  -6.019  -29.482 1.00 32.74  ? 43  PHE B CE1 1 
ATOM   1070 C CE2 . PHE B 1 44 ? 21.441  -5.918  -27.575 1.00 30.30  ? 43  PHE B CE2 1 
ATOM   1071 C CZ  . PHE B 1 44 ? 20.297  -5.504  -28.239 1.00 32.30  ? 43  PHE B CZ  1 
ATOM   1072 N N   . PHE B 1 45 ? 20.493  -10.584 -28.796 1.00 32.67  ? 44  PHE B N   1 
ATOM   1073 C CA  . PHE B 1 45 ? 19.092  -10.955 -28.872 1.00 27.27  ? 44  PHE B CA  1 
ATOM   1074 C C   . PHE B 1 45 ? 18.216  -9.715  -28.736 1.00 28.76  ? 44  PHE B C   1 
ATOM   1075 O O   . PHE B 1 45 ? 18.245  -9.047  -27.715 1.00 29.77  ? 44  PHE B O   1 
ATOM   1076 C CB  . PHE B 1 45 ? 18.764  -11.948 -27.757 1.00 25.17  ? 44  PHE B CB  1 
ATOM   1077 C CG  . PHE B 1 45 ? 19.500  -13.276 -27.925 1.00 25.71  ? 44  PHE B CG  1 
ATOM   1078 C CD1 . PHE B 1 45 ? 20.801  -13.434 -27.471 1.00 28.34  ? 44  PHE B CD1 1 
ATOM   1079 C CD2 . PHE B 1 45 ? 18.864  -14.382 -28.469 1.00 28.11  ? 44  PHE B CD2 1 
ATOM   1080 C CE1 . PHE B 1 45 ? 21.467  -14.645 -27.622 1.00 33.23  ? 44  PHE B CE1 1 
ATOM   1081 C CE2 . PHE B 1 45 ? 19.517  -15.603 -28.585 1.00 31.16  ? 44  PHE B CE2 1 
ATOM   1082 C CZ  . PHE B 1 45 ? 20.830  -15.725 -28.184 1.00 30.96  ? 44  PHE B CZ  1 
ATOM   1083 N N   . PHE B 1 46 ? 17.363  -9.467  -29.732 1.00 28.48  ? 45  PHE B N   1 
ATOM   1084 C CA  . PHE B 1 46 ? 16.433  -8.345  -29.679 1.00 31.87  ? 45  PHE B CA  1 
ATOM   1085 C C   . PHE B 1 46 ? 15.392  -8.540  -28.558 1.00 35.10  ? 45  PHE B C   1 
ATOM   1086 O O   . PHE B 1 46 ? 15.084  -9.669  -28.134 1.00 28.64  ? 45  PHE B O   1 
ATOM   1087 C CB  . PHE B 1 46 ? 15.776  -8.207  -31.045 1.00 29.05  ? 45  PHE B CB  1 
ATOM   1088 C CG  . PHE B 1 46 ? 16.703  -7.698  -32.142 1.00 34.36  ? 45  PHE B CG  1 
ATOM   1089 C CD1 . PHE B 1 46 ? 17.098  -6.350  -32.173 1.00 35.06  ? 45  PHE B CD1 1 
ATOM   1090 C CD2 . PHE B 1 46 ? 17.120  -8.536  -33.180 1.00 32.48  ? 45  PHE B CD2 1 
ATOM   1091 C CE1 . PHE B 1 46 ? 17.932  -5.873  -33.191 1.00 35.50  ? 45  PHE B CE1 1 
ATOM   1092 C CE2 . PHE B 1 46 ? 17.962  -8.055  -34.184 1.00 31.21  ? 45  PHE B CE2 1 
ATOM   1093 C CZ  . PHE B 1 46 ? 18.348  -6.715  -34.202 1.00 30.34  ? 45  PHE B CZ  1 
ATOM   1094 N N   . GLY B 1 47 ? 14.838  -7.414  -28.089 1.00 31.47  ? 46  GLY B N   1 
ATOM   1095 C CA  . GLY B 1 47 ? 13.780  -7.451  -27.084 1.00 32.52  ? 46  GLY B CA  1 
ATOM   1096 C C   . GLY B 1 47 ? 14.376  -7.571  -25.680 1.00 35.43  ? 46  GLY B C   1 
ATOM   1097 O O   . GLY B 1 47 ? 14.195  -6.690  -24.854 1.00 33.70  ? 46  GLY B O   1 
ATOM   1098 N N   . THR B 1 48 ? 15.103  -8.661  -25.420 1.00 32.55  ? 47  THR B N   1 
ATOM   1099 C CA  . THR B 1 48 ? 15.720  -8.891  -24.133 1.00 29.48  ? 47  THR B CA  1 
ATOM   1100 C C   . THR B 1 48 ? 17.020  -8.111  -24.052 1.00 32.09  ? 47  THR B C   1 
ATOM   1101 O O   . THR B 1 48 ? 17.484  -7.823  -22.945 1.00 29.58  ? 47  THR B O   1 
ATOM   1102 C CB  . THR B 1 48 ? 16.019  -10.381 -23.923 1.00 31.20  ? 47  THR B CB  1 
ATOM   1103 O OG1 . THR B 1 48 ? 16.917  -10.772 -24.964 1.00 28.24  ? 47  THR B OG1 1 
ATOM   1104 C CG2 . THR B 1 48 ? 14.762  -11.237 -23.943 1.00 31.07  ? 47  THR B CG2 1 
ATOM   1105 N N   . HIS B 1 49 ? 17.665  -7.928  -25.212 1.00 27.37  ? 48  HIS B N   1 
ATOM   1106 C CA  . HIS B 1 49 ? 18.979  -7.305  -25.308 1.00 31.39  ? 48  HIS B CA  1 
ATOM   1107 C C   . HIS B 1 49 ? 20.041  -8.125  -24.599 1.00 32.29  ? 48  HIS B C   1 
ATOM   1108 O O   . HIS B 1 49 ? 21.041  -7.551  -24.176 1.00 40.25  ? 48  HIS B O   1 
ATOM   1109 C CB  . HIS B 1 49 ? 18.985  -5.816  -24.900 1.00 29.47  ? 48  HIS B CB  1 
ATOM   1110 C CG  . HIS B 1 49 ? 17.861  -5.080  -25.528 1.00 30.79  ? 48  HIS B CG  1 
ATOM   1111 N ND1 . HIS B 1 49 ? 17.107  -4.169  -24.826 1.00 36.85  ? 48  HIS B ND1 1 
ATOM   1112 C CD2 . HIS B 1 49 ? 17.311  -5.138  -26.765 1.00 32.25  ? 48  HIS B CD2 1 
ATOM   1113 C CE1 . HIS B 1 49 ? 16.152  -3.685  -25.615 1.00 39.49  ? 48  HIS B CE1 1 
ATOM   1114 N NE2 . HIS B 1 49 ? 16.244  -4.263  -26.800 1.00 34.03  ? 48  HIS B NE2 1 
ATOM   1115 N N   . GLU B 1 50 ? 19.856  -9.452  -24.516 1.00 30.54  ? 49  GLU B N   1 
ATOM   1116 C CA  . GLU B 1 50 ? 20.860  -10.347 -23.957 1.00 31.82  ? 49  GLU B CA  1 
ATOM   1117 C C   . GLU B 1 50 ? 21.922  -10.626 -25.024 1.00 32.63  ? 49  GLU B C   1 
ATOM   1118 O O   . GLU B 1 50 ? 21.679  -10.328 -26.189 1.00 34.18  ? 49  GLU B O   1 
ATOM   1119 C CB  . GLU B 1 50 ? 20.215  -11.712 -23.694 1.00 39.28  ? 49  GLU B CB  1 
ATOM   1120 C CG  . GLU B 1 50 ? 19.213  -11.689 -22.534 1.00 35.42  ? 49  GLU B CG  1 
ATOM   1121 C CD  . GLU B 1 50 ? 19.827  -11.864 -21.155 1.00 41.86  ? 49  GLU B CD  1 
ATOM   1122 O OE1 . GLU B 1 50 ? 19.163  -11.485 -20.173 1.00 40.25  ? 49  GLU B OE1 1 
ATOM   1123 O OE2 . GLU B 1 50 ? 20.934  -12.402 -21.045 1.00 45.98  ? 49  GLU B OE2 1 
ATOM   1124 N N   . THR B 1 51 ? 23.059  -11.232 -24.639 1.00 33.83  ? 50  THR B N   1 
ATOM   1125 C CA  . THR B 1 51 ? 24.075  -11.638 -25.608 1.00 38.46  ? 50  THR B CA  1 
ATOM   1126 C C   . THR B 1 51 ? 24.527  -13.068 -25.303 1.00 35.89  ? 50  THR B C   1 
ATOM   1127 O O   . THR B 1 51 ? 24.420  -13.541 -24.180 1.00 35.63  ? 50  THR B O   1 
ATOM   1128 C CB  . THR B 1 51 ? 25.255  -10.652 -25.610 1.00 40.25  ? 50  THR B CB  1 
ATOM   1129 O OG1 . THR B 1 51 ? 25.775  -10.692 -24.287 1.00 45.72  ? 50  THR B OG1 1 
ATOM   1130 C CG2 . THR B 1 51 ? 24.847  -9.204  -25.836 1.00 42.17  ? 50  THR B CG2 1 
ATOM   1131 N N   . ALA B 1 52 ? 25.041  -13.774 -26.309 1.00 36.59  ? 51  ALA B N   1 
ATOM   1132 C CA  . ALA B 1 52 ? 25.742  -15.030 -26.080 1.00 36.26  ? 51  ALA B CA  1 
ATOM   1133 C C   . ALA B 1 52 ? 26.667  -15.314 -27.257 1.00 34.46  ? 51  ALA B C   1 
ATOM   1134 O O   . ALA B 1 52 ? 26.680  -14.555 -28.219 1.00 37.44  ? 51  ALA B O   1 
ATOM   1135 C CB  . ALA B 1 52 ? 24.781  -16.177 -25.851 1.00 36.17  ? 51  ALA B CB  1 
ATOM   1136 N N   . PHE B 1 53 ? 27.398  -16.431 -27.180 1.00 35.78  ? 52  PHE B N   1 
ATOM   1137 C CA  . PHE B 1 53 ? 28.200  -16.898 -28.300 1.00 43.04  ? 52  PHE B CA  1 
ATOM   1138 C C   . PHE B 1 53 ? 27.519  -18.139 -28.884 1.00 40.46  ? 52  PHE B C   1 
ATOM   1139 O O   . PHE B 1 53 ? 27.275  -19.104 -28.166 1.00 41.78  ? 52  PHE B O   1 
ATOM   1140 C CB  . PHE B 1 53 ? 29.660  -17.159 -27.880 1.00 43.95  ? 52  PHE B CB  1 
ATOM   1141 C CG  . PHE B 1 53 ? 30.449  -15.932 -27.448 1.00 45.59  ? 52  PHE B CG  1 
ATOM   1142 C CD1 . PHE B 1 53 ? 30.612  -14.851 -28.307 1.00 46.27  ? 52  PHE B CD1 1 
ATOM   1143 C CD2 . PHE B 1 53 ? 30.974  -15.837 -26.162 1.00 53.34  ? 52  PHE B CD2 1 
ATOM   1144 C CE1 . PHE B 1 53 ? 31.310  -13.721 -27.904 1.00 46.35  ? 52  PHE B CE1 1 
ATOM   1145 C CE2 . PHE B 1 53 ? 31.668  -14.699 -25.757 1.00 50.65  ? 52  PHE B CE2 1 
ATOM   1146 C CZ  . PHE B 1 53 ? 31.831  -13.644 -26.622 1.00 44.22  ? 52  PHE B CZ  1 
ATOM   1147 N N   . LEU B 1 54 ? 27.219  -18.110 -30.194 1.00 33.68  ? 53  LEU B N   1 
ATOM   1148 C CA  . LEU B 1 54 ? 26.617  -19.267 -30.846 1.00 33.26  ? 53  LEU B CA  1 
ATOM   1149 C C   . LEU B 1 54 ? 27.367  -19.586 -32.145 1.00 35.10  ? 53  LEU B C   1 
ATOM   1150 O O   . LEU B 1 54 ? 27.916  -18.692 -32.797 1.00 33.61  ? 53  LEU B O   1 
ATOM   1151 C CB  . LEU B 1 54 ? 25.120  -19.103 -31.128 1.00 31.77  ? 53  LEU B CB  1 
ATOM   1152 C CG  . LEU B 1 54 ? 24.191  -19.015 -29.910 1.00 34.08  ? 53  LEU B CG  1 
ATOM   1153 C CD1 . LEU B 1 54 ? 22.829  -18.610 -30.471 1.00 31.07  ? 53  LEU B CD1 1 
ATOM   1154 C CD2 . LEU B 1 54 ? 24.077  -20.380 -29.201 1.00 33.23  ? 53  LEU B CD2 1 
ATOM   1155 N N   . GLY B 1 55 ? 27.339  -20.869 -32.512 1.00 32.65  ? 54  GLY B N   1 
ATOM   1156 C CA  . GLY B 1 55 ? 27.905  -21.347 -33.759 1.00 32.45  ? 54  GLY B CA  1 
ATOM   1157 C C   . GLY B 1 55 ? 26.808  -21.438 -34.814 1.00 36.74  ? 54  GLY B C   1 
ATOM   1158 O O   . GLY B 1 55 ? 25.611  -21.412 -34.497 1.00 35.97  ? 54  GLY B O   1 
ATOM   1159 N N   . PRO B 1 56 ? 27.186  -21.566 -36.103 1.00 32.80  ? 55  PRO B N   1 
ATOM   1160 C CA  . PRO B 1 56 ? 26.205  -21.639 -37.183 1.00 30.70  ? 55  PRO B CA  1 
ATOM   1161 C C   . PRO B 1 56 ? 25.018  -22.603 -37.130 1.00 32.57  ? 55  PRO B C   1 
ATOM   1162 O O   . PRO B 1 56 ? 24.003  -22.317 -37.742 1.00 32.63  ? 55  PRO B O   1 
ATOM   1163 C CB  . PRO B 1 56 ? 27.008  -21.804 -38.470 1.00 32.43  ? 55  PRO B CB  1 
ATOM   1164 C CG  . PRO B 1 56 ? 28.464  -21.764 -38.060 1.00 36.14  ? 55  PRO B CG  1 
ATOM   1165 C CD  . PRO B 1 56 ? 28.583  -21.590 -36.556 1.00 36.04  ? 55  PRO B CD  1 
ATOM   1166 N N   . LYS B 1 57 ? 25.139  -23.742 -36.430 1.00 35.13  ? 56  LYS B N   1 
ATOM   1167 C CA  . LYS B 1 57 ? 24.076  -24.746 -36.397 1.00 35.86  ? 56  LYS B CA  1 
ATOM   1168 C C   . LYS B 1 57 ? 22.826  -24.138 -35.761 1.00 35.89  ? 56  LYS B C   1 
ATOM   1169 O O   . LYS B 1 57 ? 21.708  -24.581 -36.054 1.00 33.58  ? 56  LYS B O   1 
ATOM   1170 C CB  . LYS B 1 57 ? 24.458  -26.049 -35.675 1.00 38.28  ? 56  LYS B CB  1 
ATOM   1171 C CG  . LYS B 1 57 ? 24.831  -25.939 -34.191 1.00 41.75  ? 56  LYS B CG  1 
ATOM   1172 C CD  . LYS B 1 57 ? 24.948  -27.282 -33.473 1.00 42.26  ? 56  LYS B CD  1 
ATOM   1173 C CE  . LYS B 1 57 ? 25.227  -27.199 -31.994 1.00 44.17  ? 56  LYS B CE  1 
ATOM   1174 N NZ  . LYS B 1 57 ? 24.139  -26.545 -31.254 1.00 46.82  ? 56  LYS B NZ  1 
ATOM   1175 N N   . ASP B 1 58 ? 23.041  -23.080 -34.958 1.00 32.95  ? 57  ASP B N   1 
ATOM   1176 C CA  . ASP B 1 58 ? 21.997  -22.464 -34.157 1.00 32.15  ? 57  ASP B CA  1 
ATOM   1177 C C   . ASP B 1 58 ? 21.569  -21.104 -34.724 1.00 31.46  ? 57  ASP B C   1 
ATOM   1178 O O   . ASP B 1 58 ? 20.772  -20.398 -34.078 1.00 28.22  ? 57  ASP B O   1 
ATOM   1179 C CB  . ASP B 1 58 ? 22.397  -22.421 -32.683 1.00 29.91  ? 57  ASP B CB  1 
ATOM   1180 C CG  . ASP B 1 58 ? 22.595  -23.768 -32.007 1.00 34.95  ? 57  ASP B CG  1 
ATOM   1181 O OD1 . ASP B 1 58 ? 21.701  -24.634 -32.155 1.00 34.49  ? 57  ASP B OD1 1 
ATOM   1182 O OD2 . ASP B 1 58 ? 23.587  -23.891 -31.254 1.00 37.59  ? 57  ASP B OD2 1 
ATOM   1183 N N   . LEU B 1 59 ? 22.037  -20.770 -35.944 1.00 31.50  ? 58  LEU B N   1 
ATOM   1184 C CA  . LEU B 1 59 ? 21.812  -19.451 -36.535 1.00 30.95  ? 58  LEU B CA  1 
ATOM   1185 C C   . LEU B 1 59 ? 21.099  -19.620 -37.863 1.00 32.89  ? 58  LEU B C   1 
ATOM   1186 O O   . LEU B 1 59 ? 21.596  -20.308 -38.745 1.00 35.05  ? 58  LEU B O   1 
ATOM   1187 C CB  . LEU B 1 59 ? 23.122  -18.679 -36.720 1.00 33.16  ? 58  LEU B CB  1 
ATOM   1188 C CG  . LEU B 1 59 ? 23.963  -18.467 -35.458 1.00 32.60  ? 58  LEU B CG  1 
ATOM   1189 C CD1 . LEU B 1 59 ? 25.283  -17.777 -35.797 1.00 32.37  ? 58  LEU B CD1 1 
ATOM   1190 C CD2 . LEU B 1 59 ? 23.217  -17.659 -34.392 1.00 29.73  ? 58  LEU B CD2 1 
ATOM   1191 N N   . PHE B 1 60 ? 19.912  -19.030 -37.948 1.00 29.31  ? 59  PHE B N   1 
ATOM   1192 C CA  . PHE B 1 60 ? 19.008  -19.204 -39.062 1.00 31.55  ? 59  PHE B CA  1 
ATOM   1193 C C   . PHE B 1 60 ? 18.827  -17.837 -39.715 1.00 36.51  ? 59  PHE B C   1 
ATOM   1194 O O   . PHE B 1 60 ? 18.258  -16.941 -39.116 1.00 31.99  ? 59  PHE B O   1 
ATOM   1195 C CB  . PHE B 1 60 ? 17.688  -19.771 -38.537 1.00 30.60  ? 59  PHE B CB  1 
ATOM   1196 C CG  . PHE B 1 60 ? 17.801  -21.178 -37.957 1.00 28.28  ? 59  PHE B CG  1 
ATOM   1197 C CD1 . PHE B 1 60 ? 18.212  -21.374 -36.639 1.00 30.64  ? 59  PHE B CD1 1 
ATOM   1198 C CD2 . PHE B 1 60 ? 17.422  -22.286 -38.712 1.00 29.93  ? 59  PHE B CD2 1 
ATOM   1199 C CE1 . PHE B 1 60 ? 18.336  -22.659 -36.122 1.00 31.29  ? 59  PHE B CE1 1 
ATOM   1200 C CE2 . PHE B 1 60 ? 17.502  -23.563 -38.181 1.00 29.85  ? 59  PHE B CE2 1 
ATOM   1201 C CZ  . PHE B 1 60 ? 17.964  -23.742 -36.881 1.00 30.24  ? 59  PHE B CZ  1 
ATOM   1202 N N   . PRO B 1 61 ? 19.362  -17.611 -40.937 1.00 40.23  ? 60  PRO B N   1 
ATOM   1203 C CA  . PRO B 1 61 ? 19.158  -16.331 -41.626 1.00 36.82  ? 60  PRO B CA  1 
ATOM   1204 C C   . PRO B 1 61 ? 17.701  -15.866 -41.599 1.00 34.75  ? 60  PRO B C   1 
ATOM   1205 O O   . PRO B 1 61 ? 16.781  -16.642 -41.849 1.00 30.56  ? 60  PRO B O   1 
ATOM   1206 C CB  . PRO B 1 61 ? 19.706  -16.614 -43.050 1.00 36.96  ? 60  PRO B CB  1 
ATOM   1207 C CG  . PRO B 1 61 ? 20.799  -17.635 -42.806 1.00 44.23  ? 60  PRO B CG  1 
ATOM   1208 C CD  . PRO B 1 61 ? 20.267  -18.523 -41.661 1.00 41.83  ? 60  PRO B CD  1 
ATOM   1209 N N   . TYR B 1 62 ? 17.494  -14.557 -41.342 1.00 31.44  ? 61  TYR B N   1 
ATOM   1210 C CA  . TYR B 1 62 ? 16.184  -14.052 -40.973 1.00 33.14  ? 61  TYR B CA  1 
ATOM   1211 C C   . TYR B 1 62 ? 15.204  -14.095 -42.133 1.00 35.61  ? 61  TYR B C   1 
ATOM   1212 O O   . TYR B 1 62 ? 14.063  -14.527 -41.972 1.00 36.88  ? 61  TYR B O   1 
ATOM   1213 C CB  . TYR B 1 62 ? 16.317  -12.601 -40.494 1.00 38.03  ? 61  TYR B CB  1 
ATOM   1214 C CG  . TYR B 1 62 ? 14.993  -11.897 -40.232 1.00 37.75  ? 61  TYR B CG  1 
ATOM   1215 C CD1 . TYR B 1 62 ? 14.258  -12.149 -39.082 1.00 37.61  ? 61  TYR B CD1 1 
ATOM   1216 C CD2 . TYR B 1 62 ? 14.534  -10.915 -41.104 1.00 43.02  ? 61  TYR B CD2 1 
ATOM   1217 C CE1 . TYR B 1 62 ? 13.082  -11.473 -38.817 1.00 39.82  ? 61  TYR B CE1 1 
ATOM   1218 C CE2 . TYR B 1 62 ? 13.352  -10.236 -40.855 1.00 46.62  ? 61  TYR B CE2 1 
ATOM   1219 C CZ  . TYR B 1 62 ? 12.634  -10.509 -39.706 1.00 40.63  ? 61  TYR B CZ  1 
ATOM   1220 O OH  . TYR B 1 62 ? 11.477  -9.831  -39.486 1.00 42.33  ? 61  TYR B OH  1 
ATOM   1221 N N   . ASP B 1 63 ? 15.668  -13.642 -43.302 1.00 44.84  ? 62  ASP B N   1 
ATOM   1222 C CA  . ASP B 1 63 ? 14.815  -13.559 -44.476 1.00 45.45  ? 62  ASP B CA  1 
ATOM   1223 C C   . ASP B 1 63 ? 14.259  -14.935 -44.822 1.00 40.54  ? 62  ASP B C   1 
ATOM   1224 O O   . ASP B 1 63 ? 13.045  -15.083 -44.963 1.00 40.76  ? 62  ASP B O   1 
ATOM   1225 C CB  . ASP B 1 63 ? 15.471  -12.775 -45.594 1.00 50.54  ? 62  ASP B CB  1 
ATOM   1226 C CG  . ASP B 1 63 ? 14.820  -11.421 -45.834 1.00 64.84  ? 62  ASP B CG  1 
ATOM   1227 O OD1 . ASP B 1 63 ? 14.581  -10.683 -44.836 1.00 56.30  ? 62  ASP B OD1 1 
ATOM   1228 O OD2 . ASP B 1 63 ? 14.523  -11.133 -47.014 1.00 69.20  ? 62  ASP B OD2 1 
ATOM   1229 N N   . LYS B 1 64 ? 15.148  -15.932 -44.866 1.00 41.41  ? 63  LYS B N   1 
ATOM   1230 C CA  . LYS B 1 64 ? 14.747  -17.307 -45.140 1.00 40.22  ? 63  LYS B CA  1 
ATOM   1231 C C   . LYS B 1 64 ? 13.737  -17.850 -44.118 1.00 43.72  ? 63  LYS B C   1 
ATOM   1232 O O   . LYS B 1 64 ? 12.846  -18.609 -44.493 1.00 44.54  ? 63  LYS B O   1 
ATOM   1233 C CB  . LYS B 1 64 ? 15.976  -18.216 -45.183 1.00 40.18  ? 63  LYS B CB  1 
ATOM   1234 C CG  . LYS B 1 64 ? 15.672  -19.661 -45.575 1.00 39.86  ? 63  LYS B CG  1 
ATOM   1235 C CD  . LYS B 1 64 ? 16.942  -20.459 -45.797 1.00 44.69  ? 63  LYS B CD  1 
ATOM   1236 C CE  . LYS B 1 64 ? 16.710  -21.800 -46.447 1.00 47.79  ? 63  LYS B CE  1 
ATOM   1237 N NZ  . LYS B 1 64 ? 15.659  -22.602 -45.829 1.00 46.49  ? 63  LYS B NZ  1 
ATOM   1238 N N   . SER B 1 65 ? 13.876  -17.495 -42.831 1.00 41.51  ? 64  SER B N   1 
ATOM   1239 C CA  . SER B 1 65 ? 13.248  -18.304 -41.787 1.00 44.92  ? 64  SER B CA  1 
ATOM   1240 C C   . SER B 1 65 ? 12.114  -17.583 -41.054 1.00 41.50  ? 64  SER B C   1 
ATOM   1241 O O   . SER B 1 65 ? 11.490  -18.160 -40.161 1.00 38.40  ? 64  SER B O   1 
ATOM   1242 C CB  . SER B 1 65 ? 14.281  -18.830 -40.823 1.00 44.08  ? 64  SER B CB  1 
ATOM   1243 O OG  . SER B 1 65 ? 14.970  -17.745 -40.216 1.00 52.19  ? 64  SER B OG  1 
ATOM   1244 N N   . LYS B 1 66 ? 11.813  -16.334 -41.444 1.00 37.43  ? 65  LYS B N   1 
ATOM   1245 C CA  . LYS B 1 66 ? 10.907  -15.512 -40.647 1.00 40.79  ? 65  LYS B CA  1 
ATOM   1246 C C   . LYS B 1 66 ? 9.463   -16.019 -40.676 1.00 43.92  ? 65  LYS B C   1 
ATOM   1247 O O   . LYS B 1 66 ? 8.741   -15.881 -39.690 1.00 47.31  ? 65  LYS B O   1 
ATOM   1248 C CB  . LYS B 1 66 ? 10.946  -14.008 -40.962 1.00 34.79  ? 65  LYS B CB  1 
ATOM   1249 C CG  . LYS B 1 66 ? 10.704  -13.641 -42.412 1.00 37.61  ? 65  LYS B CG  1 
ATOM   1250 N N   . ASP B 1 67 ? 8.997   -16.607 -41.774 1.00 45.60  ? 66  ASP B N   1 
ATOM   1251 C CA  . ASP B 1 67 ? 7.597   -17.001 -41.682 1.00 53.80  ? 66  ASP B CA  1 
ATOM   1252 C C   . ASP B 1 67 ? 7.456   -18.254 -40.821 1.00 49.61  ? 66  ASP B C   1 
ATOM   1253 O O   . ASP B 1 67 ? 6.372   -18.542 -40.309 1.00 50.16  ? 66  ASP B O   1 
ATOM   1254 C CB  . ASP B 1 67 ? 6.799   -16.856 -42.973 1.00 69.82  ? 66  ASP B CB  1 
ATOM   1255 C CG  . ASP B 1 67 ? 7.450   -17.306 -44.273 1.00 83.28  ? 66  ASP B CG  1 
ATOM   1256 O OD1 . ASP B 1 67 ? 6.808   -17.122 -45.340 1.00 83.07  ? 66  ASP B OD1 1 
ATOM   1257 O OD2 . ASP B 1 67 ? 8.584   -17.829 -44.211 1.00 85.48  ? 66  ASP B OD2 1 
ATOM   1258 N N   . LYS B 1 68 ? 8.568   -18.964 -40.615 1.00 43.31  ? 67  LYS B N   1 
ATOM   1259 C CA  . LYS B 1 68 ? 8.558   -20.126 -39.745 1.00 41.29  ? 67  LYS B CA  1 
ATOM   1260 C C   . LYS B 1 68 ? 8.710   -19.702 -38.282 1.00 41.19  ? 67  LYS B C   1 
ATOM   1261 O O   . LYS B 1 68 ? 7.934   -20.150 -37.438 1.00 39.37  ? 67  LYS B O   1 
ATOM   1262 C CB  . LYS B 1 68 ? 9.573   -21.149 -40.262 1.00 44.35  ? 67  LYS B CB  1 
ATOM   1263 C CG  . LYS B 1 68 ? 9.691   -22.443 -39.471 1.00 56.14  ? 67  LYS B CG  1 
ATOM   1264 C CD  . LYS B 1 68 ? 10.301  -23.518 -40.365 1.00 67.46  ? 67  LYS B CD  1 
ATOM   1265 C CE  . LYS B 1 68 ? 10.917  -24.677 -39.646 1.00 73.58  ? 67  LYS B CE  1 
ATOM   1266 N NZ  . LYS B 1 68 ? 9.956   -25.471 -38.878 1.00 77.22  ? 67  LYS B NZ  1 
ATOM   1267 N N   . TYR B 1 69 ? 9.684   -18.822 -37.985 1.00 39.87  ? 68  TYR B N   1 
ATOM   1268 C CA  . TYR B 1 69 ? 10.074  -18.554 -36.600 1.00 36.54  ? 68  TYR B CA  1 
ATOM   1269 C C   . TYR B 1 69 ? 9.520   -17.218 -36.085 1.00 37.94  ? 68  TYR B C   1 
ATOM   1270 O O   . TYR B 1 69 ? 9.637   -16.913 -34.894 1.00 32.85  ? 68  TYR B O   1 
ATOM   1271 C CB  . TYR B 1 69 ? 11.596  -18.661 -36.433 1.00 35.33  ? 68  TYR B CB  1 
ATOM   1272 C CG  . TYR B 1 69 ? 12.183  -20.032 -36.763 1.00 35.34  ? 68  TYR B CG  1 
ATOM   1273 C CD1 . TYR B 1 69 ? 11.588  -21.205 -36.315 1.00 37.60  ? 68  TYR B CD1 1 
ATOM   1274 C CD2 . TYR B 1 69 ? 13.328  -20.144 -37.535 1.00 34.95  ? 68  TYR B CD2 1 
ATOM   1275 C CE1 . TYR B 1 69 ? 12.125  -22.456 -36.599 1.00 37.55  ? 68  TYR B CE1 1 
ATOM   1276 C CE2 . TYR B 1 69 ? 13.882  -21.381 -37.820 1.00 37.12  ? 68  TYR B CE2 1 
ATOM   1277 C CZ  . TYR B 1 69 ? 13.261  -22.536 -37.377 1.00 36.52  ? 68  TYR B CZ  1 
ATOM   1278 O OH  . TYR B 1 69 ? 13.820  -23.740 -37.661 1.00 34.66  ? 68  TYR B OH  1 
ATOM   1279 N N   . GLY B 1 70 ? 8.914   -16.423 -36.969 1.00 35.51  ? 69  GLY B N   1 
ATOM   1280 C CA  . GLY B 1 70 ? 8.607   -15.044 -36.615 1.00 42.56  ? 69  GLY B CA  1 
ATOM   1281 C C   . GLY B 1 70 ? 7.189   -14.833 -36.081 1.00 48.65  ? 69  GLY B C   1 
ATOM   1282 O O   . GLY B 1 70 ? 6.597   -13.786 -36.336 1.00 49.25  ? 69  GLY B O   1 
ATOM   1283 N N   . LYS B 1 71 ? 6.661   -15.803 -35.328 1.00 45.94  ? 70  LYS B N   1 
ATOM   1284 C CA  . LYS B 1 71 ? 5.319   -15.681 -34.780 1.00 50.05  ? 70  LYS B CA  1 
ATOM   1285 C C   . LYS B 1 71 ? 5.419   -15.261 -33.317 1.00 49.87  ? 70  LYS B C   1 
ATOM   1286 O O   . LYS B 1 71 ? 6.303   -15.744 -32.610 1.00 47.47  ? 70  LYS B O   1 
ATOM   1287 C CB  . LYS B 1 71 ? 4.481   -16.965 -34.862 1.00 49.75  ? 70  LYS B CB  1 
ATOM   1288 C CG  . LYS B 1 71 ? 3.789   -17.232 -36.203 1.00 61.55  ? 70  LYS B CG  1 
ATOM   1289 C CD  . LYS B 1 71 ? 4.467   -18.230 -37.135 1.00 58.58  ? 70  LYS B CD  1 
ATOM   1290 C CE  . LYS B 1 71 ? 3.838   -18.364 -38.500 1.00 67.11  ? 70  LYS B CE  1 
ATOM   1291 N NZ  . LYS B 1 71 ? 4.200   -17.313 -39.469 1.00 61.76  ? 70  LYS B NZ  1 
ATOM   1292 N N   . PRO B 1 72 ? 4.518   -14.374 -32.815 1.00 50.26  ? 71  PRO B N   1 
ATOM   1293 C CA  . PRO B 1 72 ? 4.547   -13.971 -31.405 1.00 43.54  ? 71  PRO B CA  1 
ATOM   1294 C C   . PRO B 1 72 ? 4.316   -15.163 -30.488 1.00 43.21  ? 71  PRO B C   1 
ATOM   1295 O O   . PRO B 1 72 ? 3.692   -16.141 -30.901 1.00 36.83  ? 71  PRO B O   1 
ATOM   1296 C CB  . PRO B 1 72 ? 3.444   -12.907 -31.283 1.00 42.90  ? 71  PRO B CB  1 
ATOM   1297 C CG  . PRO B 1 72 ? 3.250   -12.448 -32.707 1.00 49.77  ? 71  PRO B CG  1 
ATOM   1298 C CD  . PRO B 1 72 ? 3.442   -13.701 -33.565 1.00 45.53  ? 71  PRO B CD  1 
ATOM   1299 N N   . ASN B 1 73 ? 4.843   -15.066 -29.253 1.00 39.50  ? 72  ASN B N   1 
ATOM   1300 C CA  . ASN B 1 73 ? 4.577   -16.064 -28.231 1.00 38.27  ? 72  ASN B CA  1 
ATOM   1301 C C   . ASN B 1 73 ? 4.544   -15.358 -26.866 1.00 38.94  ? 72  ASN B C   1 
ATOM   1302 O O   . ASN B 1 73 ? 4.611   -14.132 -26.789 1.00 44.37  ? 72  ASN B O   1 
ATOM   1303 C CB  . ASN B 1 73 ? 5.569   -17.223 -28.326 1.00 36.14  ? 72  ASN B CB  1 
ATOM   1304 C CG  . ASN B 1 73 ? 6.985   -16.743 -28.133 1.00 36.62  ? 72  ASN B CG  1 
ATOM   1305 O OD1 . ASN B 1 73 ? 7.260   -16.001 -27.178 1.00 35.29  ? 72  ASN B OD1 1 
ATOM   1306 N ND2 . ASN B 1 73 ? 7.880   -17.102 -29.048 1.00 34.98  ? 72  ASN B ND2 1 
ATOM   1307 N N   . LYS B 1 74 ? 4.547   -16.140 -25.792 1.00 38.99  ? 73  LYS B N   1 
ATOM   1308 C CA  . LYS B 1 74 ? 4.373   -15.639 -24.432 1.00 43.90  ? 73  LYS B CA  1 
ATOM   1309 C C   . LYS B 1 74 ? 5.708   -15.489 -23.685 1.00 41.69  ? 73  LYS B C   1 
ATOM   1310 O O   . LYS B 1 74 ? 5.701   -15.244 -22.476 1.00 34.91  ? 73  LYS B O   1 
ATOM   1311 C CB  . LYS B 1 74 ? 3.460   -16.637 -23.694 1.00 41.17  ? 73  LYS B CB  1 
ATOM   1312 N N   . ARG B 1 75 ? 6.856   -15.640 -24.374 1.00 32.95  ? 74  ARG B N   1 
ATOM   1313 C CA  . ARG B 1 75 ? 8.146   -15.451 -23.722 1.00 32.17  ? 74  ARG B CA  1 
ATOM   1314 C C   . ARG B 1 75 ? 8.464   -13.954 -23.592 1.00 35.11  ? 74  ARG B C   1 
ATOM   1315 O O   . ARG B 1 75 ? 8.239   -13.188 -24.534 1.00 34.57  ? 74  ARG B O   1 
ATOM   1316 C CB  . ARG B 1 75 ? 9.252   -16.208 -24.463 1.00 36.94  ? 74  ARG B CB  1 
ATOM   1317 C CG  . ARG B 1 75 ? 9.017   -17.694 -24.724 1.00 34.83  ? 74  ARG B CG  1 
ATOM   1318 C CD  . ARG B 1 75 ? 9.004   -18.514 -23.443 1.00 35.68  ? 74  ARG B CD  1 
ATOM   1319 N NE  . ARG B 1 75 ? 9.133   -19.954 -23.701 1.00 33.45  ? 74  ARG B NE  1 
ATOM   1320 C CZ  . ARG B 1 75 ? 10.224  -20.608 -23.403 1.00 31.82  ? 74  ARG B CZ  1 
ATOM   1321 N NH1 . ARG B 1 75 ? 11.259  -19.965 -22.897 1.00 32.13  ? 74  ARG B NH1 1 
ATOM   1322 N NH2 . ARG B 1 75 ? 10.307  -21.902 -23.636 1.00 32.68  ? 74  ARG B NH2 1 
ATOM   1323 N N   . LYS B 1 76 ? 8.966   -13.544 -22.406 1.00 30.98  ? 75  LYS B N   1 
ATOM   1324 C CA  . LYS B 1 76 ? 9.285   -12.152 -22.099 1.00 30.86  ? 75  LYS B CA  1 
ATOM   1325 C C   . LYS B 1 76 ? 10.342  -11.626 -23.078 1.00 29.58  ? 75  LYS B C   1 
ATOM   1326 O O   . LYS B 1 76 ? 11.424  -12.205 -23.209 1.00 29.15  ? 75  LYS B O   1 
ATOM   1327 C CB  . LYS B 1 76 ? 9.880   -12.037 -20.687 1.00 33.54  ? 75  LYS B CB  1 
ATOM   1328 C CG  . LYS B 1 76 ? 10.337  -10.616 -20.260 1.00 34.16  ? 75  LYS B CG  1 
ATOM   1329 C CD  . LYS B 1 76 ? 10.698  -10.520 -18.779 1.00 37.19  ? 75  LYS B CD  1 
ATOM   1330 C CE  . LYS B 1 76 ? 11.100  -9.119  -18.319 1.00 42.40  ? 75  LYS B CE  1 
ATOM   1331 N NZ  . LYS B 1 76 ? 11.444  -9.150  -16.883 1.00 41.04  ? 75  LYS B NZ  1 
ATOM   1332 N N   . GLY B 1 77 ? 10.019  -10.523 -23.752 1.00 31.91  ? 76  GLY B N   1 
ATOM   1333 C CA  . GLY B 1 77 ? 10.982  -9.838  -24.605 1.00 33.26  ? 76  GLY B CA  1 
ATOM   1334 C C   . GLY B 1 77 ? 10.829  -10.256 -26.071 1.00 35.59  ? 76  GLY B C   1 
ATOM   1335 O O   . GLY B 1 77 ? 11.395  -9.641  -26.954 1.00 32.49  ? 76  GLY B O   1 
ATOM   1336 N N   . PHE B 1 78 ? 10.044  -11.308 -26.350 1.00 35.81  ? 77  PHE B N   1 
ATOM   1337 C CA  . PHE B 1 78 ? 10.002  -11.862 -27.695 1.00 32.96  ? 77  PHE B CA  1 
ATOM   1338 C C   . PHE B 1 78 ? 9.274   -10.946 -28.671 1.00 33.24  ? 77  PHE B C   1 
ATOM   1339 O O   . PHE B 1 78 ? 9.744   -10.713 -29.783 1.00 30.86  ? 77  PHE B O   1 
ATOM   1340 C CB  . PHE B 1 78 ? 9.292   -13.217 -27.713 1.00 31.64  ? 77  PHE B CB  1 
ATOM   1341 C CG  . PHE B 1 78 ? 9.533   -13.966 -29.008 1.00 31.56  ? 77  PHE B CG  1 
ATOM   1342 C CD1 . PHE B 1 78 ? 10.645  -14.798 -29.138 1.00 31.77  ? 77  PHE B CD1 1 
ATOM   1343 C CD2 . PHE B 1 78 ? 8.648   -13.853 -30.070 1.00 31.09  ? 77  PHE B CD2 1 
ATOM   1344 C CE1 . PHE B 1 78 ? 10.868  -15.506 -30.304 1.00 31.32  ? 77  PHE B CE1 1 
ATOM   1345 C CE2 . PHE B 1 78 ? 8.888   -14.544 -31.247 1.00 34.22  ? 77  PHE B CE2 1 
ATOM   1346 C CZ  . PHE B 1 78 ? 9.990   -15.374 -31.354 1.00 32.70  ? 77  PHE B CZ  1 
ATOM   1347 N N   . ASN B 1 79 ? 8.090   -10.483 -28.295 1.00 32.93  ? 78  ASN B N   1 
ATOM   1348 C CA  . ASN B 1 79 ? 7.329   -9.665  -29.224 1.00 32.39  ? 78  ASN B CA  1 
ATOM   1349 C C   . ASN B 1 79 ? 8.026   -8.319  -29.439 1.00 31.83  ? 78  ASN B C   1 
ATOM   1350 O O   . ASN B 1 79 ? 7.933   -7.743  -30.521 1.00 32.35  ? 78  ASN B O   1 
ATOM   1351 C CB  . ASN B 1 79 ? 5.863   -9.521  -28.821 1.00 33.73  ? 78  ASN B CB  1 
ATOM   1352 C CG  . ASN B 1 79 ? 5.160   -10.860 -28.848 1.00 40.20  ? 78  ASN B CG  1 
ATOM   1353 O OD1 . ASN B 1 79 ? 5.732   -11.857 -29.296 1.00 43.05  ? 78  ASN B OD1 1 
ATOM   1354 N ND2 . ASN B 1 79 ? 3.973   -10.937 -28.271 1.00 40.26  ? 78  ASN B ND2 1 
ATOM   1355 N N   . GLU B 1 80 ? 8.666   -7.811  -28.403 1.00 32.15  ? 79  GLU B N   1 
ATOM   1356 C CA  . GLU B 1 80 ? 9.467   -6.598  -28.517 1.00 40.19  ? 79  GLU B CA  1 
ATOM   1357 C C   . GLU B 1 80 ? 10.619  -6.842  -29.495 1.00 32.37  ? 79  GLU B C   1 
ATOM   1358 O O   . GLU B 1 80 ? 11.014  -5.925  -30.199 1.00 31.73  ? 79  GLU B O   1 
ATOM   1359 C CB  . GLU B 1 80 ? 10.145  -6.239  -27.196 1.00 35.61  ? 79  GLU B CB  1 
ATOM   1360 C CG  . GLU B 1 80 ? 9.208   -5.558  -26.204 1.00 47.39  ? 79  GLU B CG  1 
ATOM   1361 N N   . GLY B 1 81 ? 11.149  -8.084  -29.513 1.00 28.97  ? 80  GLY B N   1 
ATOM   1362 C CA  . GLY B 1 81 ? 12.320  -8.415  -30.311 1.00 26.18  ? 80  GLY B CA  1 
ATOM   1363 C C   . GLY B 1 81 ? 11.902  -8.505  -31.773 1.00 29.53  ? 80  GLY B C   1 
ATOM   1364 O O   . GLY B 1 81 ? 12.624  -8.049  -32.669 1.00 33.35  ? 80  GLY B O   1 
ATOM   1365 N N   . LEU B 1 82 ? 10.691  -9.034  -31.988 1.00 26.67  ? 81  LEU B N   1 
ATOM   1366 C CA  . LEU B 1 82 ? 10.115  -9.040  -33.323 1.00 30.45  ? 81  LEU B CA  1 
ATOM   1367 C C   . LEU B 1 82 ? 9.967   -7.590  -33.779 1.00 30.25  ? 81  LEU B C   1 
ATOM   1368 O O   . LEU B 1 82 ? 10.219  -7.274  -34.939 1.00 29.49  ? 81  LEU B O   1 
ATOM   1369 C CB  . LEU B 1 82 ? 8.781   -9.798  -33.394 1.00 27.35  ? 81  LEU B CB  1 
ATOM   1370 C CG  . LEU B 1 82 ? 8.876   -11.309 -33.119 1.00 28.65  ? 81  LEU B CG  1 
ATOM   1371 C CD1 . LEU B 1 82 ? 7.507   -11.964 -33.188 1.00 32.15  ? 81  LEU B CD1 1 
ATOM   1372 C CD2 . LEU B 1 82 ? 9.801   -11.940 -34.139 1.00 25.79  ? 81  LEU B CD2 1 
ATOM   1373 N N   . TRP B 1 83 ? 9.565   -6.701  -32.877 1.00 29.35  ? 82  TRP B N   1 
ATOM   1374 C CA  . TRP B 1 83 ? 9.437   -5.302  -33.289 1.00 33.18  ? 82  TRP B CA  1 
ATOM   1375 C C   . TRP B 1 83 ? 10.789  -4.725  -33.708 1.00 30.44  ? 82  TRP B C   1 
ATOM   1376 O O   . TRP B 1 83 ? 10.881  -4.093  -34.758 1.00 33.72  ? 82  TRP B O   1 
ATOM   1377 C CB  . TRP B 1 83 ? 8.790   -4.434  -32.205 1.00 34.91  ? 82  TRP B CB  1 
ATOM   1378 C CG  . TRP B 1 83 ? 8.475   -3.039  -32.681 1.00 37.04  ? 82  TRP B CG  1 
ATOM   1379 C CD1 . TRP B 1 83 ? 7.295   -2.620  -33.220 1.00 43.67  ? 82  TRP B CD1 1 
ATOM   1380 C CD2 . TRP B 1 83 ? 9.359   -1.891  -32.708 1.00 40.69  ? 82  TRP B CD2 1 
ATOM   1381 N NE1 . TRP B 1 83 ? 7.371   -1.294  -33.555 1.00 43.75  ? 82  TRP B NE1 1 
ATOM   1382 C CE2 . TRP B 1 83 ? 8.620   -0.819  -33.256 1.00 39.55  ? 82  TRP B CE2 1 
ATOM   1383 C CE3 . TRP B 1 83 ? 10.689  -1.663  -32.320 1.00 38.75  ? 82  TRP B CE3 1 
ATOM   1384 C CZ2 . TRP B 1 83 ? 9.166   0.454   -33.428 1.00 43.51  ? 82  TRP B CZ2 1 
ATOM   1385 C CZ3 . TRP B 1 83 ? 11.227  -0.401  -32.488 1.00 41.14  ? 82  TRP B CZ3 1 
ATOM   1386 C CH2 . TRP B 1 83 ? 10.476  0.635   -33.042 1.00 44.45  ? 82  TRP B CH2 1 
ATOM   1387 N N   . GLU B 1 84 ? 11.830  -4.967  -32.900 1.00 29.52  ? 83  GLU B N   1 
ATOM   1388 C CA  . GLU B 1 84 ? 13.142  -4.376  -33.121 1.00 34.01  ? 83  GLU B CA  1 
ATOM   1389 C C   . GLU B 1 84 ? 13.804  -4.850  -34.424 1.00 35.03  ? 83  GLU B C   1 
ATOM   1390 O O   . GLU B 1 84 ? 14.364  -4.029  -35.162 1.00 29.89  ? 83  GLU B O   1 
ATOM   1391 C CB  . GLU B 1 84 ? 14.063  -4.590  -31.928 1.00 33.55  ? 83  GLU B CB  1 
ATOM   1392 C CG  . GLU B 1 84 ? 13.562  -3.903  -30.653 1.00 35.53  ? 83  GLU B CG  1 
ATOM   1393 C CD  . GLU B 1 84 ? 14.405  -4.303  -29.463 1.00 35.41  ? 83  GLU B CD  1 
ATOM   1394 O OE1 . GLU B 1 84 ? 15.258  -5.199  -29.638 1.00 31.60  ? 83  GLU B OE1 1 
ATOM   1395 O OE2 . GLU B 1 84 ? 14.234  -3.736  -28.357 1.00 38.52  ? 83  GLU B OE2 1 
ATOM   1396 N N   . ILE B 1 85 ? 13.784  -6.173  -34.675 1.00 30.70  ? 84  ILE B N   1 
ATOM   1397 C CA  . ILE B 1 85 ? 14.460  -6.760  -35.832 1.00 29.71  ? 84  ILE B CA  1 
ATOM   1398 C C   . ILE B 1 85 ? 13.815  -6.241  -37.116 1.00 32.90  ? 84  ILE B C   1 
ATOM   1399 O O   . ILE B 1 85 ? 14.478  -6.117  -38.146 1.00 31.88  ? 84  ILE B O   1 
ATOM   1400 C CB  . ILE B 1 85 ? 14.420  -8.305  -35.784 1.00 29.33  ? 84  ILE B CB  1 
ATOM   1401 C CG1 . ILE B 1 85 ? 15.438  -8.911  -36.768 1.00 32.75  ? 84  ILE B CG1 1 
ATOM   1402 C CG2 . ILE B 1 85 ? 12.995  -8.823  -36.046 1.00 29.94  ? 84  ILE B CG2 1 
ATOM   1403 C CD1 . ILE B 1 85 ? 15.795  -10.370 -36.506 1.00 31.16  ? 84  ILE B CD1 1 
ATOM   1404 N N   . GLN B 1 86 ? 12.517  -5.909  -37.043 1.00 31.60  ? 85  GLN B N   1 
ATOM   1405 C CA  . GLN B 1 86 ? 11.771  -5.420  -38.188 1.00 32.27  ? 85  GLN B CA  1 
ATOM   1406 C C   . GLN B 1 86 ? 11.872  -3.893  -38.324 1.00 32.78  ? 85  GLN B C   1 
ATOM   1407 O O   . GLN B 1 86 ? 11.839  -3.383  -39.435 1.00 34.89  ? 85  GLN B O   1 
ATOM   1408 C CB  . GLN B 1 86 ? 10.304  -5.832  -38.032 1.00 35.72  ? 85  GLN B CB  1 
ATOM   1409 N N   . ASN B 1 87 ? 11.979  -3.141  -37.228 1.00 28.64  ? 86  ASN B N   1 
ATOM   1410 C CA  . ASN B 1 87 ? 11.825  -1.691  -37.393 1.00 30.25  ? 86  ASN B CA  1 
ATOM   1411 C C   . ASN B 1 87 ? 13.132  -0.927  -37.225 1.00 32.52  ? 86  ASN B C   1 
ATOM   1412 O O   . ASN B 1 87 ? 13.238  0.219   -37.688 1.00 34.96  ? 86  ASN B O   1 
ATOM   1413 C CB  . ASN B 1 87 ? 10.725  -1.111  -36.499 1.00 37.08  ? 86  ASN B CB  1 
ATOM   1414 C CG  . ASN B 1 87 ? 9.377   -1.692  -36.869 1.00 38.63  ? 86  ASN B CG  1 
ATOM   1415 O OD1 . ASN B 1 87 ? 8.822   -1.342  -37.912 1.00 47.40  ? 86  ASN B OD1 1 
ATOM   1416 N ND2 . ASN B 1 87 ? 8.886   -2.647  -36.096 1.00 38.00  ? 86  ASN B ND2 1 
ATOM   1417 N N   . ASN B 1 88 ? 14.094  -1.516  -36.507 1.00 31.77  ? 87  ASN B N   1 
ATOM   1418 C CA  . ASN B 1 88 ? 15.355  -0.831  -36.256 1.00 35.99  ? 87  ASN B CA  1 
ATOM   1419 C C   . ASN B 1 88 ? 16.425  -1.843  -35.852 1.00 29.90  ? 87  ASN B C   1 
ATOM   1420 O O   . ASN B 1 88 ? 16.942  -1.796  -34.743 1.00 28.80  ? 87  ASN B O   1 
ATOM   1421 C CB  . ASN B 1 88 ? 15.218  0.314   -35.250 1.00 37.33  ? 87  ASN B CB  1 
ATOM   1422 C CG  . ASN B 1 88 ? 16.279  1.377   -35.455 1.00 36.26  ? 87  ASN B CG  1 
ATOM   1423 O OD1 . ASN B 1 88 ? 17.287  1.155   -36.129 1.00 35.50  ? 87  ASN B OD1 1 
ATOM   1424 N ND2 . ASN B 1 88 ? 16.090  2.550   -34.877 1.00 38.30  ? 87  ASN B ND2 1 
ATOM   1425 N N   . PRO B 1 89 ? 16.743  -2.833  -36.711 1.00 32.26  ? 88  PRO B N   1 
ATOM   1426 C CA  . PRO B 1 89 ? 17.626  -3.931  -36.311 1.00 29.53  ? 88  PRO B CA  1 
ATOM   1427 C C   . PRO B 1 89 ? 19.065  -3.470  -36.062 1.00 33.41  ? 88  PRO B C   1 
ATOM   1428 O O   . PRO B 1 89 ? 19.854  -4.214  -35.493 1.00 31.88  ? 88  PRO B O   1 
ATOM   1429 C CB  . PRO B 1 89 ? 17.520  -4.872  -37.524 1.00 28.36  ? 88  PRO B CB  1 
ATOM   1430 C CG  . PRO B 1 89 ? 17.282  -3.926  -38.696 1.00 28.66  ? 88  PRO B CG  1 
ATOM   1431 C CD  . PRO B 1 89 ? 16.274  -2.945  -38.110 1.00 30.10  ? 88  PRO B CD  1 
ATOM   1432 N N   . HIS B 1 90 ? 19.412  -2.244  -36.497 1.00 30.47  ? 89  HIS B N   1 
ATOM   1433 C CA  . HIS B 1 90 ? 20.815  -1.808  -36.496 1.00 32.61  ? 89  HIS B CA  1 
ATOM   1434 C C   . HIS B 1 90 ? 21.087  -0.765  -35.412 1.00 33.82  ? 89  HIS B C   1 
ATOM   1435 O O   . HIS B 1 90 ? 22.213  -0.270  -35.279 1.00 31.30  ? 89  HIS B O   1 
ATOM   1436 C CB  . HIS B 1 90 ? 21.269  -1.411  -37.917 1.00 31.46  ? 89  HIS B CB  1 
ATOM   1437 C CG  . HIS B 1 90 ? 21.183  -2.557  -38.875 1.00 30.26  ? 89  HIS B CG  1 
ATOM   1438 N ND1 . HIS B 1 90 ? 21.808  -3.768  -38.632 1.00 29.94  ? 89  HIS B ND1 1 
ATOM   1439 C CD2 . HIS B 1 90 ? 20.557  -2.681  -40.078 1.00 29.93  ? 89  HIS B CD2 1 
ATOM   1440 C CE1 . HIS B 1 90 ? 21.545  -4.603  -39.631 1.00 30.38  ? 89  HIS B CE1 1 
ATOM   1441 N NE2 . HIS B 1 90 ? 20.790  -3.962  -40.518 1.00 29.49  ? 89  HIS B NE2 1 
ATOM   1442 N N   . ALA B 1 91 ? 20.084  -0.524  -34.558 1.00 34.96  ? 90  ALA B N   1 
ATOM   1443 C CA  . ALA B 1 91 ? 20.184  0.534   -33.559 1.00 35.95  ? 90  ALA B CA  1 
ATOM   1444 C C   . ALA B 1 91 ? 21.123  0.115   -32.430 1.00 39.12  ? 90  ALA B C   1 
ATOM   1445 O O   . ALA B 1 91 ? 21.441  -1.058  -32.258 1.00 35.43  ? 90  ALA B O   1 
ATOM   1446 C CB  . ALA B 1 91 ? 18.817  0.941   -33.020 1.00 30.29  ? 90  ALA B CB  1 
ATOM   1447 N N   . SER B 1 92 ? 21.587  1.113   -31.678 1.00 36.16  ? 91  SER B N   1 
ATOM   1448 C CA  . SER B 1 92 ? 22.254  0.889   -30.405 1.00 39.09  ? 91  SER B CA  1 
ATOM   1449 C C   . SER B 1 92 ? 21.187  0.677   -29.329 1.00 43.42  ? 91  SER B C   1 
ATOM   1450 O O   . SER B 1 92 ? 20.280  1.510   -29.197 1.00 43.36  ? 91  SER B O   1 
ATOM   1451 C CB  . SER B 1 92 ? 23.115  2.084   -30.075 1.00 39.58  ? 91  SER B CB  1 
ATOM   1452 O OG  . SER B 1 92 ? 23.562  1.972   -28.736 1.00 51.08  ? 91  SER B OG  1 
ATOM   1453 N N   . TYR B 1 93 ? 21.290  -0.455  -28.614 1.00 37.36  ? 92  TYR B N   1 
ATOM   1454 C CA  . TYR B 1 93 ? 20.377  -0.849  -27.545 1.00 42.64  ? 92  TYR B CA  1 
ATOM   1455 C C   . TYR B 1 93 ? 21.151  -0.882  -26.225 1.00 51.60  ? 92  TYR B C   1 
ATOM   1456 O O   . TYR B 1 93 ? 20.737  -1.527  -25.267 1.00 56.84  ? 92  TYR B O   1 
ATOM   1457 C CB  . TYR B 1 93 ? 19.705  -2.202  -27.855 1.00 34.11  ? 92  TYR B CB  1 
ATOM   1458 C CG  . TYR B 1 93 ? 18.723  -2.126  -29.014 1.00 32.74  ? 92  TYR B CG  1 
ATOM   1459 C CD1 . TYR B 1 93 ? 17.455  -1.589  -28.829 1.00 36.50  ? 92  TYR B CD1 1 
ATOM   1460 C CD2 . TYR B 1 93 ? 19.056  -2.571  -30.291 1.00 32.38  ? 92  TYR B CD2 1 
ATOM   1461 C CE1 . TYR B 1 93 ? 16.558  -1.461  -29.876 1.00 33.85  ? 92  TYR B CE1 1 
ATOM   1462 C CE2 . TYR B 1 93 ? 18.147  -2.484  -31.336 1.00 31.90  ? 92  TYR B CE2 1 
ATOM   1463 C CZ  . TYR B 1 93 ? 16.899  -1.925  -31.131 1.00 33.04  ? 92  TYR B CZ  1 
ATOM   1464 O OH  . TYR B 1 93 ? 15.986  -1.816  -32.152 1.00 31.62  ? 92  TYR B OH  1 
ATOM   1465 N N   . SER B 1 94 ? 22.270  -0.146  -26.195 1.00 65.44  ? 93  SER B N   1 
ATOM   1466 C CA  . SER B 1 94 ? 23.227  -0.113  -25.099 1.00 67.39  ? 93  SER B CA  1 
ATOM   1467 C C   . SER B 1 94 ? 22.538  0.341   -23.803 1.00 69.47  ? 93  SER B C   1 
ATOM   1468 O O   . SER B 1 94 ? 21.719  1.286   -23.895 1.00 69.65  ? 93  SER B O   1 
ATOM   1469 C CB  . SER B 1 94 ? 24.369  0.804   -25.439 1.00 72.38  ? 93  SER B CB  1 
ATOM   1470 O OG  . SER B 1 94 ? 24.918  0.501   -26.714 1.00 73.19  ? 93  SER B OG  1 
ATOM   1471 N N   . ALA C 1 5  ? 29.846  -22.277 28.848  1.00 66.40  ? 4   ALA C N   1 
ATOM   1472 C CA  . ALA C 1 5  ? 28.987  -23.313 29.470  1.00 70.76  ? 4   ALA C CA  1 
ATOM   1473 C C   . ALA C 1 5  ? 27.508  -22.932 29.374  1.00 81.32  ? 4   ALA C C   1 
ATOM   1474 O O   . ALA C 1 5  ? 27.168  -21.873 28.844  1.00 82.80  ? 4   ALA C O   1 
ATOM   1475 C CB  . ALA C 1 5  ? 29.422  -23.554 30.887  1.00 72.06  ? 4   ALA C CB  1 
ATOM   1476 N N   . PHE C 1 6  ? 26.638  -23.805 29.909  1.00 73.82  ? 5   PHE C N   1 
ATOM   1477 C CA  . PHE C 1 6  ? 25.243  -23.846 29.502  1.00 68.09  ? 5   PHE C CA  1 
ATOM   1478 C C   . PHE C 1 6  ? 24.339  -24.054 30.713  1.00 72.86  ? 5   PHE C C   1 
ATOM   1479 O O   . PHE C 1 6  ? 24.556  -24.980 31.493  1.00 79.42  ? 5   PHE C O   1 
ATOM   1480 C CB  . PHE C 1 6  ? 25.091  -25.052 28.568  1.00 64.28  ? 5   PHE C CB  1 
ATOM   1481 C CG  . PHE C 1 6  ? 25.966  -25.103 27.319  1.00 57.26  ? 5   PHE C CG  1 
ATOM   1482 C CD1 . PHE C 1 6  ? 27.068  -25.947 27.251  1.00 54.46  ? 5   PHE C CD1 1 
ATOM   1483 C CD2 . PHE C 1 6  ? 25.670  -24.326 26.201  1.00 59.44  ? 5   PHE C CD2 1 
ATOM   1484 C CE1 . PHE C 1 6  ? 27.848  -26.020 26.097  1.00 55.05  ? 5   PHE C CE1 1 
ATOM   1485 C CE2 . PHE C 1 6  ? 26.455  -24.389 25.055  1.00 51.01  ? 5   PHE C CE2 1 
ATOM   1486 C CZ  . PHE C 1 6  ? 27.538  -25.241 25.002  1.00 55.42  ? 5   PHE C CZ  1 
ATOM   1487 N N   . LYS C 1 7  ? 23.299  -23.218 30.830  1.00 63.44  ? 6   LYS C N   1 
ATOM   1488 C CA  . LYS C 1 7  ? 22.338  -23.310 31.921  1.00 59.84  ? 6   LYS C CA  1 
ATOM   1489 C C   . LYS C 1 7  ? 20.962  -23.662 31.354  1.00 60.15  ? 6   LYS C C   1 
ATOM   1490 O O   . LYS C 1 7  ? 20.731  -23.506 30.155  1.00 59.58  ? 6   LYS C O   1 
ATOM   1491 C CB  . LYS C 1 7  ? 22.328  -22.000 32.723  1.00 70.89  ? 6   LYS C CB  1 
ATOM   1492 N N   . PRO C 1 8  ? 20.001  -24.152 32.173  1.00 60.20  ? 7   PRO C N   1 
ATOM   1493 C CA  . PRO C 1 8  ? 18.675  -24.519 31.661  1.00 62.83  ? 7   PRO C CA  1 
ATOM   1494 C C   . PRO C 1 8  ? 17.988  -23.403 30.868  1.00 69.16  ? 7   PRO C C   1 
ATOM   1495 O O   . PRO C 1 8  ? 17.810  -22.295 31.368  1.00 77.04  ? 7   PRO C O   1 
ATOM   1496 C CB  . PRO C 1 8  ? 17.894  -24.920 32.928  1.00 66.27  ? 7   PRO C CB  1 
ATOM   1497 C CG  . PRO C 1 8  ? 18.969  -25.323 33.919  1.00 62.67  ? 7   PRO C CG  1 
ATOM   1498 C CD  . PRO C 1 8  ? 20.150  -24.416 33.616  1.00 61.42  ? 7   PRO C CD  1 
ATOM   1499 N N   . GLY C 1 9  ? 17.639  -23.692 29.610  1.00 65.31  ? 8   GLY C N   1 
ATOM   1500 C CA  . GLY C 1 9  ? 16.875  -22.759 28.795  1.00 65.53  ? 8   GLY C CA  1 
ATOM   1501 C C   . GLY C 1 9  ? 17.695  -22.196 27.636  1.00 59.34  ? 8   GLY C C   1 
ATOM   1502 O O   . GLY C 1 9  ? 17.123  -21.674 26.681  1.00 63.89  ? 8   GLY C O   1 
ATOM   1503 N N   . ASP C 1 10 ? 19.028  -22.304 27.751  1.00 49.07  ? 9   ASP C N   1 
ATOM   1504 C CA  . ASP C 1 10 ? 19.989  -21.930 26.728  1.00 43.06  ? 9   ASP C CA  1 
ATOM   1505 C C   . ASP C 1 10 ? 19.727  -22.685 25.424  1.00 48.60  ? 9   ASP C C   1 
ATOM   1506 O O   . ASP C 1 10 ? 19.460  -23.890 25.425  1.00 42.90  ? 9   ASP C O   1 
ATOM   1507 C CB  . ASP C 1 10 ? 21.409  -22.198 27.188  1.00 50.12  ? 9   ASP C CB  1 
ATOM   1508 C CG  . ASP C 1 10 ? 21.979  -21.245 28.231  1.00 63.94  ? 9   ASP C CG  1 
ATOM   1509 O OD1 . ASP C 1 10 ? 21.187  -20.464 28.811  1.00 73.41  ? 9   ASP C OD1 1 
ATOM   1510 O OD2 . ASP C 1 10 ? 23.219  -21.279 28.440  1.00 64.62  ? 9   ASP C OD2 1 
ATOM   1511 N N   . LEU C 1 11 ? 19.829  -21.956 24.304  1.00 46.67  ? 10  LEU C N   1 
ATOM   1512 C CA  . LEU C 1 11 ? 19.439  -22.467 22.998  1.00 47.99  ? 10  LEU C CA  1 
ATOM   1513 C C   . LEU C 1 11 ? 20.683  -22.950 22.259  1.00 43.06  ? 10  LEU C C   1 
ATOM   1514 O O   . LEU C 1 11 ? 21.695  -22.262 22.224  1.00 43.14  ? 10  LEU C O   1 
ATOM   1515 C CB  . LEU C 1 11 ? 18.679  -21.383 22.228  1.00 46.23  ? 10  LEU C CB  1 
ATOM   1516 C CG  . LEU C 1 11 ? 17.360  -20.915 22.859  1.00 46.88  ? 10  LEU C CG  1 
ATOM   1517 C CD1 . LEU C 1 11 ? 16.590  -19.961 21.953  1.00 46.16  ? 10  LEU C CD1 1 
ATOM   1518 C CD2 . LEU C 1 11 ? 16.475  -22.085 23.251  1.00 40.40  ? 10  LEU C CD2 1 
ATOM   1519 N N   . VAL C 1 12 ? 20.615  -24.155 21.685  1.00 42.65  ? 11  VAL C N   1 
ATOM   1520 C CA  . VAL C 1 12 ? 21.809  -24.766 21.115  1.00 41.73  ? 11  VAL C CA  1 
ATOM   1521 C C   . VAL C 1 12 ? 21.437  -25.496 19.823  1.00 37.45  ? 11  VAL C C   1 
ATOM   1522 O O   . VAL C 1 12 ? 20.260  -25.709 19.559  1.00 34.95  ? 11  VAL C O   1 
ATOM   1523 C CB  . VAL C 1 12 ? 22.438  -25.748 22.130  1.00 38.16  ? 11  VAL C CB  1 
ATOM   1524 C CG1 . VAL C 1 12 ? 22.753  -25.084 23.465  1.00 38.76  ? 11  VAL C CG1 1 
ATOM   1525 C CG2 . VAL C 1 12 ? 21.570  -26.986 22.355  1.00 36.01  ? 11  VAL C CG2 1 
ATOM   1526 N N   . PHE C 1 13 ? 22.452  -25.878 19.031  1.00 35.79  ? 12  PHE C N   1 
ATOM   1527 C CA  . PHE C 1 13 ? 22.324  -27.024 18.150  1.00 33.89  ? 12  PHE C CA  1 
ATOM   1528 C C   . PHE C 1 13 ? 22.969  -28.196 18.867  1.00 32.91  ? 12  PHE C C   1 
ATOM   1529 O O   . PHE C 1 13 ? 24.030  -28.048 19.489  1.00 38.77  ? 12  PHE C O   1 
ATOM   1530 C CB  . PHE C 1 13 ? 22.918  -26.760 16.757  1.00 35.50  ? 12  PHE C CB  1 
ATOM   1531 C CG  . PHE C 1 13 ? 22.107  -25.785 15.926  1.00 37.22  ? 12  PHE C CG  1 
ATOM   1532 C CD1 . PHE C 1 13 ? 21.099  -26.242 15.085  1.00 38.88  ? 12  PHE C CD1 1 
ATOM   1533 C CD2 . PHE C 1 13 ? 22.347  -24.409 15.996  1.00 39.30  ? 12  PHE C CD2 1 
ATOM   1534 C CE1 . PHE C 1 13 ? 20.339  -25.349 14.342  1.00 41.33  ? 12  PHE C CE1 1 
ATOM   1535 C CE2 . PHE C 1 13 ? 21.583  -23.518 15.255  1.00 43.32  ? 12  PHE C CE2 1 
ATOM   1536 C CZ  . PHE C 1 13 ? 20.588  -23.992 14.424  1.00 41.04  ? 12  PHE C CZ  1 
ATOM   1537 N N   . ALA C 1 14 ? 22.321  -29.359 18.800  1.00 30.02  ? 13  ALA C N   1 
ATOM   1538 C CA  . ALA C 1 14 ? 22.841  -30.487 19.556  1.00 30.91  ? 13  ALA C CA  1 
ATOM   1539 C C   . ALA C 1 14 ? 23.095  -31.656 18.616  1.00 34.38  ? 13  ALA C C   1 
ATOM   1540 O O   . ALA C 1 14 ? 22.245  -31.963 17.790  1.00 30.93  ? 13  ALA C O   1 
ATOM   1541 C CB  . ALA C 1 14 ? 21.847  -30.830 20.638  1.00 30.51  ? 13  ALA C CB  1 
ATOM   1542 N N   . LYS C 1 15 ? 24.278  -32.287 18.734  1.00 34.27  ? 14  LYS C N   1 
ATOM   1543 C CA  . LYS C 1 15 ? 24.705  -33.304 17.787  1.00 35.51  ? 14  LYS C CA  1 
ATOM   1544 C C   . LYS C 1 15 ? 24.758  -34.643 18.500  1.00 33.68  ? 14  LYS C C   1 
ATOM   1545 O O   . LYS C 1 15 ? 25.506  -34.816 19.469  1.00 34.95  ? 14  LYS C O   1 
ATOM   1546 C CB  . LYS C 1 15 ? 26.112  -33.101 17.199  1.00 39.40  ? 14  LYS C CB  1 
ATOM   1547 C CG  . LYS C 1 15 ? 26.550  -34.137 16.149  1.00 38.49  ? 14  LYS C CG  1 
ATOM   1548 C CD  . LYS C 1 15 ? 25.713  -34.087 14.872  1.00 35.17  ? 14  LYS C CD  1 
ATOM   1549 C CE  . LYS C 1 15 ? 26.171  -34.964 13.722  1.00 33.51  ? 14  LYS C CE  1 
ATOM   1550 N NZ  . LYS C 1 15 ? 25.954  -36.384 14.055  1.00 33.07  ? 14  LYS C NZ  1 
ATOM   1551 N N   . MET C 1 16 ? 23.962  -35.564 17.968  1.00 33.40  ? 15  MET C N   1 
ATOM   1552 C CA  . MET C 1 16 ? 23.808  -36.945 18.398  1.00 34.71  ? 15  MET C CA  1 
ATOM   1553 C C   . MET C 1 16 ? 24.262  -37.832 17.244  1.00 39.71  ? 15  MET C C   1 
ATOM   1554 O O   . MET C 1 16 ? 23.988  -37.545 16.073  1.00 32.40  ? 15  MET C O   1 
ATOM   1555 C CB  . MET C 1 16 ? 22.323  -37.198 18.674  1.00 34.34  ? 15  MET C CB  1 
ATOM   1556 C CG  . MET C 1 16 ? 21.933  -38.545 19.252  1.00 54.32  ? 15  MET C CG  1 
ATOM   1557 S SD  . MET C 1 16 ? 20.391  -38.509 20.211  1.00 60.57  ? 15  MET C SD  1 
ATOM   1558 C CE  . MET C 1 16 ? 20.740  -37.126 21.287  1.00 46.65  ? 15  MET C CE  1 
ATOM   1559 N N   . LYS C 1 17 ? 24.924  -38.947 17.568  1.00 40.96  ? 16  LYS C N   1 
ATOM   1560 C CA  . LYS C 1 17 ? 25.393  -39.828 16.505  1.00 39.34  ? 16  LYS C CA  1 
ATOM   1561 C C   . LYS C 1 17 ? 24.179  -40.310 15.714  1.00 29.85  ? 16  LYS C C   1 
ATOM   1562 O O   . LYS C 1 17 ? 23.204  -40.785 16.288  1.00 31.87  ? 16  LYS C O   1 
ATOM   1563 C CB  . LYS C 1 17 ? 26.144  -41.012 17.135  1.00 37.56  ? 16  LYS C CB  1 
ATOM   1564 C CG  . LYS C 1 17 ? 26.771  -42.006 16.168  1.00 46.77  ? 16  LYS C CG  1 
ATOM   1565 C CD  . LYS C 1 17 ? 27.951  -41.390 15.437  1.00 50.40  ? 16  LYS C CD  1 
ATOM   1566 C CE  . LYS C 1 17 ? 28.636  -42.379 14.541  1.00 61.07  ? 16  LYS C CE  1 
ATOM   1567 N NZ  . LYS C 1 17 ? 29.755  -41.752 13.823  1.00 53.14  ? 16  LYS C NZ  1 
ATOM   1568 N N   . GLY C 1 18 ? 24.242  -40.215 14.384  1.00 31.38  ? 17  GLY C N   1 
ATOM   1569 C CA  . GLY C 1 18 ? 23.128  -40.685 13.575  1.00 33.15  ? 17  GLY C CA  1 
ATOM   1570 C C   . GLY C 1 18 ? 22.139  -39.585 13.160  1.00 38.94  ? 17  GLY C C   1 
ATOM   1571 O O   . GLY C 1 18 ? 21.136  -39.902 12.512  1.00 37.08  ? 17  GLY C O   1 
ATOM   1572 N N   . TYR C 1 19 ? 22.423  -38.309 13.497  1.00 37.81  ? 18  TYR C N   1 
ATOM   1573 C CA  . TYR C 1 19 ? 21.482  -37.213 13.284  1.00 34.07  ? 18  TYR C CA  1 
ATOM   1574 C C   . TYR C 1 19 ? 22.226  -35.918 12.979  1.00 35.48  ? 18  TYR C C   1 
ATOM   1575 O O   . TYR C 1 19 ? 23.328  -35.673 13.467  1.00 31.04  ? 18  TYR C O   1 
ATOM   1576 C CB  . TYR C 1 19 ? 20.610  -36.912 14.513  1.00 34.89  ? 18  TYR C CB  1 
ATOM   1577 C CG  . TYR C 1 19 ? 19.829  -38.130 14.972  1.00 37.81  ? 18  TYR C CG  1 
ATOM   1578 C CD1 . TYR C 1 19 ? 20.414  -39.087 15.798  1.00 35.64  ? 18  TYR C CD1 1 
ATOM   1579 C CD2 . TYR C 1 19 ? 18.520  -38.329 14.554  1.00 36.35  ? 18  TYR C CD2 1 
ATOM   1580 C CE1 . TYR C 1 19 ? 19.714  -40.217 16.190  1.00 40.45  ? 18  TYR C CE1 1 
ATOM   1581 C CE2 . TYR C 1 19 ? 17.811  -39.451 14.948  1.00 42.29  ? 18  TYR C CE2 1 
ATOM   1582 C CZ  . TYR C 1 19 ? 18.411  -40.397 15.759  1.00 45.42  ? 18  TYR C CZ  1 
ATOM   1583 O OH  . TYR C 1 19 ? 17.700  -41.497 16.133  1.00 46.86  ? 18  TYR C OH  1 
ATOM   1584 N N   . PRO C 1 20 ? 21.659  -35.042 12.126  1.00 36.45  ? 19  PRO C N   1 
ATOM   1585 C CA  . PRO C 1 20 ? 22.290  -33.740 11.875  1.00 36.03  ? 19  PRO C CA  1 
ATOM   1586 C C   . PRO C 1 20 ? 22.314  -32.883 13.149  1.00 30.57  ? 19  PRO C C   1 
ATOM   1587 O O   . PRO C 1 20 ? 21.579  -33.142 14.093  1.00 29.94  ? 19  PRO C O   1 
ATOM   1588 C CB  . PRO C 1 20 ? 21.381  -33.180 10.747  1.00 34.35  ? 19  PRO C CB  1 
ATOM   1589 C CG  . PRO C 1 20 ? 20.032  -33.793 11.022  1.00 34.87  ? 19  PRO C CG  1 
ATOM   1590 C CD  . PRO C 1 20 ? 20.372  -35.236 11.421  1.00 36.72  ? 19  PRO C CD  1 
ATOM   1591 N N   . HIS C 1 21 ? 23.173  -31.856 13.182  1.00 32.70  ? 20  HIS C N   1 
ATOM   1592 C CA  . HIS C 1 21 ? 23.130  -30.873 14.249  1.00 35.37  ? 20  HIS C CA  1 
ATOM   1593 C C   . HIS C 1 21 ? 21.693  -30.367 14.375  1.00 34.63  ? 20  HIS C C   1 
ATOM   1594 O O   . HIS C 1 21 ? 21.095  -29.960 13.377  1.00 36.51  ? 20  HIS C O   1 
ATOM   1595 C CB  . HIS C 1 21 ? 24.144  -29.749 14.020  1.00 36.15  ? 20  HIS C CB  1 
ATOM   1596 C CG  . HIS C 1 21 ? 25.551  -30.206 14.092  1.00 39.87  ? 20  HIS C CG  1 
ATOM   1597 N ND1 . HIS C 1 21 ? 26.148  -30.885 13.047  1.00 43.83  ? 20  HIS C ND1 1 
ATOM   1598 C CD2 . HIS C 1 21 ? 26.461  -30.112 15.069  1.00 44.06  ? 20  HIS C CD2 1 
ATOM   1599 C CE1 . HIS C 1 21 ? 27.394  -31.183 13.389  1.00 47.62  ? 20  HIS C CE1 1 
ATOM   1600 N NE2 . HIS C 1 21 ? 27.613  -30.700 14.610  1.00 48.74  ? 20  HIS C NE2 1 
ATOM   1601 N N   . TRP C 1 22 ? 21.134  -30.438 15.598  1.00 31.81  ? 21  TRP C N   1 
ATOM   1602 C CA  . TRP C 1 22 ? 19.682  -30.340 15.736  1.00 29.27  ? 21  TRP C CA  1 
ATOM   1603 C C   . TRP C 1 22 ? 19.337  -29.185 16.670  1.00 28.87  ? 21  TRP C C   1 
ATOM   1604 O O   . TRP C 1 22 ? 19.961  -29.058 17.736  1.00 28.85  ? 21  TRP C O   1 
ATOM   1605 C CB  . TRP C 1 22 ? 19.111  -31.651 16.292  1.00 31.68  ? 21  TRP C CB  1 
ATOM   1606 C CG  . TRP C 1 22 ? 17.642  -31.854 15.994  1.00 36.84  ? 21  TRP C CG  1 
ATOM   1607 C CD1 . TRP C 1 22 ? 16.560  -31.272 16.597  1.00 32.96  ? 21  TRP C CD1 1 
ATOM   1608 C CD2 . TRP C 1 22 ? 17.100  -32.768 15.009  1.00 35.57  ? 21  TRP C CD2 1 
ATOM   1609 N NE1 . TRP C 1 22 ? 15.391  -31.713 16.029  1.00 34.40  ? 21  TRP C NE1 1 
ATOM   1610 C CE2 . TRP C 1 22 ? 15.690  -32.650 15.069  1.00 36.30  ? 21  TRP C CE2 1 
ATOM   1611 C CE3 . TRP C 1 22 ? 17.666  -33.660 14.087  1.00 33.46  ? 21  TRP C CE3 1 
ATOM   1612 C CZ2 . TRP C 1 22 ? 14.858  -33.407 14.244  1.00 36.54  ? 21  TRP C CZ2 1 
ATOM   1613 C CZ3 . TRP C 1 22 ? 16.838  -34.415 13.279  1.00 34.93  ? 21  TRP C CZ3 1 
ATOM   1614 C CH2 . TRP C 1 22 ? 15.455  -34.307 13.386  1.00 35.33  ? 21  TRP C CH2 1 
ATOM   1615 N N   . PRO C 1 23 ? 18.313  -28.357 16.343  1.00 28.79  ? 22  PRO C N   1 
ATOM   1616 C CA  . PRO C 1 23 ? 17.923  -27.260 17.220  1.00 31.10  ? 22  PRO C CA  1 
ATOM   1617 C C   . PRO C 1 23 ? 17.311  -27.780 18.527  1.00 31.30  ? 22  PRO C C   1 
ATOM   1618 O O   . PRO C 1 23 ? 16.458  -28.665 18.513  1.00 29.42  ? 22  PRO C O   1 
ATOM   1619 C CB  . PRO C 1 23 ? 16.923  -26.475 16.330  1.00 32.82  ? 22  PRO C CB  1 
ATOM   1620 C CG  . PRO C 1 23 ? 16.280  -27.552 15.482  1.00 31.77  ? 22  PRO C CG  1 
ATOM   1621 C CD  . PRO C 1 23 ? 17.496  -28.408 15.107  1.00 30.73  ? 22  PRO C CD  1 
ATOM   1622 N N   . ALA C 1 24 ? 17.809  -27.257 19.652  1.00 32.99  ? 23  ALA C N   1 
ATOM   1623 C CA  . ALA C 1 24 ? 17.525  -27.819 20.970  1.00 34.85  ? 23  ALA C CA  1 
ATOM   1624 C C   . ALA C 1 24 ? 17.703  -26.757 22.046  1.00 36.77  ? 23  ALA C C   1 
ATOM   1625 O O   . ALA C 1 24 ? 18.219  -25.674 21.771  1.00 39.15  ? 23  ALA C O   1 
ATOM   1626 C CB  . ALA C 1 24 ? 18.463  -28.989 21.256  1.00 31.95  ? 23  ALA C CB  1 
ATOM   1627 N N   . ARG C 1 25 ? 17.318  -27.106 23.288  1.00 36.59  ? 24  ARG C N   1 
ATOM   1628 C CA  . ARG C 1 25 ? 17.700  -26.306 24.440  1.00 39.72  ? 24  ARG C CA  1 
ATOM   1629 C C   . ARG C 1 25 ? 18.157  -27.204 25.590  1.00 35.95  ? 24  ARG C C   1 
ATOM   1630 O O   . ARG C 1 25 ? 17.773  -28.378 25.648  1.00 37.14  ? 24  ARG C O   1 
ATOM   1631 C CB  . ARG C 1 25 ? 16.527  -25.450 24.929  1.00 41.76  ? 24  ARG C CB  1 
ATOM   1632 C CG  . ARG C 1 25 ? 15.241  -26.212 25.209  1.00 43.09  ? 24  ARG C CG  1 
ATOM   1633 C CD  . ARG C 1 25 ? 14.195  -25.339 25.916  1.00 43.36  ? 24  ARG C CD  1 
ATOM   1634 N NE  . ARG C 1 25 ? 13.027  -26.190 26.168  1.00 50.66  ? 24  ARG C NE  1 
ATOM   1635 C CZ  . ARG C 1 25 ? 11.756  -25.818 26.073  1.00 56.74  ? 24  ARG C CZ  1 
ATOM   1636 N NH1 . ARG C 1 25 ? 11.458  -24.568 25.762  1.00 54.56  ? 24  ARG C NH1 1 
ATOM   1637 N NH2 . ARG C 1 25 ? 10.791  -26.697 26.303  1.00 60.56  ? 24  ARG C NH2 1 
ATOM   1638 N N   . ILE C 1 26 ? 18.929  -26.609 26.509  1.00 37.38  ? 25  ILE C N   1 
ATOM   1639 C CA  . ILE C 1 26 ? 19.261  -27.155 27.828  1.00 41.37  ? 25  ILE C CA  1 
ATOM   1640 C C   . ILE C 1 26 ? 18.012  -27.207 28.705  1.00 49.41  ? 25  ILE C C   1 
ATOM   1641 O O   . ILE C 1 26 ? 17.384  -26.184 28.974  1.00 52.06  ? 25  ILE C O   1 
ATOM   1642 C CB  . ILE C 1 26 ? 20.364  -26.333 28.531  1.00 44.91  ? 25  ILE C CB  1 
ATOM   1643 C CG1 . ILE C 1 26 ? 21.524  -25.974 27.628  1.00 42.08  ? 25  ILE C CG1 1 
ATOM   1644 C CG2 . ILE C 1 26 ? 20.851  -27.002 29.824  1.00 44.04  ? 25  ILE C CG2 1 
ATOM   1645 C CD1 . ILE C 1 26 ? 22.280  -27.153 27.050  1.00 44.77  ? 25  ILE C CD1 1 
ATOM   1646 N N   . ASP C 1 27 ? 17.663  -28.412 29.157  1.00 47.16  ? 26  ASP C N   1 
ATOM   1647 C CA  . ASP C 1 27 ? 16.638  -28.583 30.174  1.00 58.16  ? 26  ASP C CA  1 
ATOM   1648 C C   . ASP C 1 27 ? 17.228  -28.360 31.564  1.00 60.89  ? 26  ASP C C   1 
ATOM   1649 O O   . ASP C 1 27 ? 18.448  -28.354 31.738  1.00 54.27  ? 26  ASP C O   1 
ATOM   1650 C CB  . ASP C 1 27 ? 16.003  -29.964 30.105  1.00 64.66  ? 26  ASP C CB  1 
ATOM   1651 C CG  . ASP C 1 27 ? 14.637  -30.005 29.443  1.00 69.90  ? 26  ASP C CG  1 
ATOM   1652 O OD1 . ASP C 1 27 ? 14.270  -28.969 28.849  1.00 67.94  ? 26  ASP C OD1 1 
ATOM   1653 O OD2 . ASP C 1 27 ? 13.940  -31.049 29.575  1.00 63.36  ? 26  ASP C OD2 1 
ATOM   1654 N N   . ASP C 1 28 ? 16.335  -28.174 32.548  1.00 74.80  ? 27  ASP C N   1 
ATOM   1655 C CA  . ASP C 1 28 ? 16.678  -28.355 33.949  1.00 79.55  ? 27  ASP C CA  1 
ATOM   1656 C C   . ASP C 1 28 ? 16.498  -29.831 34.290  1.00 83.74  ? 27  ASP C C   1 
ATOM   1657 O O   . ASP C 1 28 ? 15.696  -30.513 33.655  1.00 83.43  ? 27  ASP C O   1 
ATOM   1658 C CB  . ASP C 1 28 ? 15.858  -27.453 34.858  1.00 81.42  ? 27  ASP C CB  1 
ATOM   1659 N N   . ILE C 1 29 ? 17.272  -30.314 35.271  1.00 80.37  ? 28  ILE C N   1 
ATOM   1660 C CA  . ILE C 1 29 ? 17.111  -31.659 35.799  1.00 84.14  ? 28  ILE C CA  1 
ATOM   1661 C C   . ILE C 1 29 ? 16.323  -31.545 37.098  1.00 90.84  ? 28  ILE C C   1 
ATOM   1662 O O   . ILE C 1 29 ? 16.754  -30.845 38.012  1.00 104.98 ? 28  ILE C O   1 
ATOM   1663 C CB  . ILE C 1 29 ? 18.477  -32.337 36.016  1.00 82.66  ? 28  ILE C CB  1 
ATOM   1664 N N   . ALA C 1 30 ? 15.169  -32.225 37.159  1.00 88.89  ? 29  ALA C N   1 
ATOM   1665 C CA  . ALA C 1 30 ? 14.216  -32.069 38.251  1.00 80.61  ? 29  ALA C CA  1 
ATOM   1666 C C   . ALA C 1 30 ? 14.812  -32.563 39.574  1.00 70.90  ? 29  ALA C C   1 
ATOM   1667 O O   . ALA C 1 30 ? 15.473  -33.632 39.567  1.00 59.06  ? 29  ALA C O   1 
ATOM   1668 C CB  . ALA C 1 30 ? 12.914  -32.771 37.914  1.00 83.58  ? 29  ALA C CB  1 
ATOM   1669 N N   . VAL C 1 34 ? 14.470  -36.175 39.935  1.00 60.11  ? 32  VAL C N   1 
ATOM   1670 C CA  . VAL C 1 34 ? 14.457  -37.032 38.727  1.00 62.50  ? 32  VAL C CA  1 
ATOM   1671 C C   . VAL C 1 34 ? 15.505  -38.141 38.858  1.00 68.43  ? 32  VAL C C   1 
ATOM   1672 O O   . VAL C 1 34 ? 16.387  -37.991 39.731  1.00 76.56  ? 32  VAL C O   1 
ATOM   1673 C CB  . VAL C 1 34 ? 14.692  -36.191 37.494  1.00 58.30  ? 32  VAL C CB  1 
ATOM   1674 N N   . LYS C 1 35 ? 19.409  -38.722 37.782  1.00 75.42  ? 34  LYS C N   1 
ATOM   1675 C CA  . LYS C 1 35 ? 20.579  -37.811 37.643  1.00 72.21  ? 34  LYS C CA  1 
ATOM   1676 C C   . LYS C 1 35 ? 21.286  -38.099 36.317  1.00 64.45  ? 34  LYS C C   1 
ATOM   1677 O O   . LYS C 1 35 ? 21.406  -39.260 35.913  1.00 59.10  ? 34  LYS C O   1 
ATOM   1678 C CB  . LYS C 1 35 ? 21.521  -37.950 38.846  1.00 75.34  ? 34  LYS C CB  1 
ATOM   1679 N N   . PRO C 1 36 ? 21.779  -37.053 35.606  1.00 57.15  ? 35  PRO C N   1 
ATOM   1680 C CA  . PRO C 1 36 ? 22.486  -37.247 34.339  1.00 62.88  ? 35  PRO C CA  1 
ATOM   1681 C C   . PRO C 1 36 ? 23.726  -38.112 34.564  1.00 67.92  ? 35  PRO C C   1 
ATOM   1682 O O   . PRO C 1 36 ? 24.270  -38.143 35.675  1.00 56.06  ? 35  PRO C O   1 
ATOM   1683 C CB  . PRO C 1 36 ? 22.865  -35.822 33.866  1.00 60.36  ? 35  PRO C CB  1 
ATOM   1684 C CG  . PRO C 1 36 ? 22.059  -34.878 34.738  1.00 57.22  ? 35  PRO C CG  1 
ATOM   1685 C CD  . PRO C 1 36 ? 21.723  -35.638 36.014  1.00 57.62  ? 35  PRO C CD  1 
ATOM   1686 N N   . PRO C 1 37 ? 24.213  -38.843 33.531  1.00 57.91  ? 36  PRO C N   1 
ATOM   1687 C CA  . PRO C 1 37 ? 25.557  -39.418 33.592  1.00 57.19  ? 36  PRO C CA  1 
ATOM   1688 C C   . PRO C 1 37 ? 26.549  -38.286 33.876  1.00 57.47  ? 36  PRO C C   1 
ATOM   1689 O O   . PRO C 1 37 ? 26.243  -37.109 33.664  1.00 53.57  ? 36  PRO C O   1 
ATOM   1690 C CB  . PRO C 1 37 ? 25.722  -40.044 32.188  1.00 50.50  ? 36  PRO C CB  1 
ATOM   1691 C CG  . PRO C 1 37 ? 24.302  -40.386 31.806  1.00 52.87  ? 36  PRO C CG  1 
ATOM   1692 C CD  . PRO C 1 37 ? 23.506  -39.180 32.287  1.00 54.80  ? 36  PRO C CD  1 
ATOM   1693 N N   . PRO C 1 38 ? 27.753  -38.594 34.409  1.00 50.99  ? 37  PRO C N   1 
ATOM   1694 C CA  . PRO C 1 38 ? 28.720  -37.547 34.732  1.00 49.92  ? 37  PRO C CA  1 
ATOM   1695 C C   . PRO C 1 38 ? 28.983  -36.672 33.510  1.00 47.89  ? 37  PRO C C   1 
ATOM   1696 O O   . PRO C 1 38 ? 29.216  -37.185 32.414  1.00 39.11  ? 37  PRO C O   1 
ATOM   1697 C CB  . PRO C 1 38 ? 29.956  -38.366 35.139  1.00 52.67  ? 37  PRO C CB  1 
ATOM   1698 C CG  . PRO C 1 38 ? 29.366  -39.658 35.689  1.00 48.60  ? 37  PRO C CG  1 
ATOM   1699 C CD  . PRO C 1 38 ? 28.227  -39.953 34.737  1.00 48.76  ? 37  PRO C CD  1 
ATOM   1700 N N   . ASN C 1 39 ? 28.898  -35.352 33.728  1.00 46.69  ? 38  ASN C N   1 
ATOM   1701 C CA  . ASN C 1 39 ? 29.302  -34.337 32.770  1.00 43.69  ? 38  ASN C CA  1 
ATOM   1702 C C   . ASN C 1 39 ? 28.344  -34.281 31.577  1.00 45.01  ? 38  ASN C C   1 
ATOM   1703 O O   . ASN C 1 39 ? 28.745  -33.804 30.516  1.00 40.40  ? 38  ASN C O   1 
ATOM   1704 C CB  . ASN C 1 39 ? 30.724  -34.572 32.263  1.00 47.23  ? 38  ASN C CB  1 
ATOM   1705 C CG  . ASN C 1 39 ? 31.332  -33.333 31.641  1.00 56.66  ? 38  ASN C CG  1 
ATOM   1706 O OD1 . ASN C 1 39 ? 30.949  -32.203 31.975  1.00 59.05  ? 38  ASN C OD1 1 
ATOM   1707 N ND2 . ASN C 1 39 ? 32.294  -33.517 30.748  1.00 58.77  ? 38  ASN C ND2 1 
ATOM   1708 N N   . LYS C 1 40 ? 27.098  -34.759 31.738  1.00 41.13  ? 39  LYS C N   1 
ATOM   1709 C CA  . LYS C 1 40 ? 26.149  -34.695 30.628  1.00 41.59  ? 39  LYS C CA  1 
ATOM   1710 C C   . LYS C 1 40 ? 25.024  -33.722 30.957  1.00 40.32  ? 39  LYS C C   1 
ATOM   1711 O O   . LYS C 1 40 ? 24.553  -33.671 32.090  1.00 37.43  ? 39  LYS C O   1 
ATOM   1712 C CB  . LYS C 1 40 ? 25.470  -36.034 30.299  1.00 38.26  ? 39  LYS C CB  1 
ATOM   1713 C CG  . LYS C 1 40 ? 26.434  -37.149 29.911  1.00 42.10  ? 39  LYS C CG  1 
ATOM   1714 C CD  . LYS C 1 40 ? 27.262  -36.877 28.660  1.00 44.30  ? 39  LYS C CD  1 
ATOM   1715 C CE  . LYS C 1 40 ? 28.048  -38.069 28.204  1.00 49.32  ? 39  LYS C CE  1 
ATOM   1716 N NZ  . LYS C 1 40 ? 29.104  -37.711 27.240  1.00 49.25  ? 39  LYS C NZ  1 
ATOM   1717 N N   . TYR C 1 41 ? 24.551  -33.002 29.934  1.00 39.53  ? 40  TYR C N   1 
ATOM   1718 C CA  . TYR C 1 41 ? 23.450  -32.063 30.099  1.00 39.10  ? 40  TYR C CA  1 
ATOM   1719 C C   . TYR C 1 41 ? 22.153  -32.697 29.606  1.00 41.52  ? 40  TYR C C   1 
ATOM   1720 O O   . TYR C 1 41 ? 22.154  -33.428 28.610  1.00 40.95  ? 40  TYR C O   1 
ATOM   1721 C CB  . TYR C 1 41 ? 23.639  -30.834 29.207  1.00 36.34  ? 40  TYR C CB  1 
ATOM   1722 C CG  . TYR C 1 41 ? 24.793  -29.930 29.611  1.00 46.18  ? 40  TYR C CG  1 
ATOM   1723 C CD1 . TYR C 1 41 ? 26.091  -30.189 29.178  1.00 44.72  ? 40  TYR C CD1 1 
ATOM   1724 C CD2 . TYR C 1 41 ? 24.575  -28.803 30.407  1.00 46.31  ? 40  TYR C CD2 1 
ATOM   1725 C CE1 . TYR C 1 41 ? 27.141  -29.363 29.543  1.00 52.80  ? 40  TYR C CE1 1 
ATOM   1726 C CE2 . TYR C 1 41 ? 25.619  -27.962 30.757  1.00 48.63  ? 40  TYR C CE2 1 
ATOM   1727 C CZ  . TYR C 1 41 ? 26.904  -28.252 30.335  1.00 49.43  ? 40  TYR C CZ  1 
ATOM   1728 O OH  . TYR C 1 41 ? 27.948  -27.444 30.666  1.00 63.42  ? 40  TYR C OH  1 
ATOM   1729 N N   . PRO C 1 42 ? 21.005  -32.362 30.238  1.00 42.26  ? 41  PRO C N   1 
ATOM   1730 C CA  . PRO C 1 42 ? 19.692  -32.810 29.761  1.00 39.75  ? 41  PRO C CA  1 
ATOM   1731 C C   . PRO C 1 42 ? 19.314  -31.905 28.587  1.00 38.25  ? 41  PRO C C   1 
ATOM   1732 O O   . PRO C 1 42 ? 19.382  -30.672 28.704  1.00 39.30  ? 41  PRO C O   1 
ATOM   1733 C CB  . PRO C 1 42 ? 18.798  -32.640 31.015  1.00 36.10  ? 41  PRO C CB  1 
ATOM   1734 C CG  . PRO C 1 42 ? 19.443  -31.511 31.772  1.00 45.77  ? 41  PRO C CG  1 
ATOM   1735 C CD  . PRO C 1 42 ? 20.922  -31.483 31.418  1.00 43.14  ? 41  PRO C CD  1 
ATOM   1736 N N   . ILE C 1 43 ? 19.019  -32.528 27.435  1.00 39.39  ? 42  ILE C N   1 
ATOM   1737 C CA  . ILE C 1 43 ? 18.740  -31.815 26.188  1.00 36.35  ? 42  ILE C CA  1 
ATOM   1738 C C   . ILE C 1 43 ? 17.294  -32.087 25.776  1.00 37.38  ? 42  ILE C C   1 
ATOM   1739 O O   . ILE C 1 43 ? 16.839  -33.239 25.756  1.00 35.91  ? 42  ILE C O   1 
ATOM   1740 C CB  . ILE C 1 43 ? 19.747  -32.207 25.084  1.00 35.19  ? 42  ILE C CB  1 
ATOM   1741 C CG1 . ILE C 1 43 ? 21.220  -31.926 25.503  1.00 35.73  ? 42  ILE C CG1 1 
ATOM   1742 C CG2 . ILE C 1 43 ? 19.400  -31.571 23.716  1.00 34.90  ? 42  ILE C CG2 1 
ATOM   1743 C CD1 . ILE C 1 43 ? 21.508  -30.461 25.811  1.00 34.73  ? 42  ILE C CD1 1 
ATOM   1744 N N   . PHE C 1 44 ? 16.579  -31.010 25.413  1.00 34.03  ? 43  PHE C N   1 
ATOM   1745 C CA  . PHE C 1 44 ? 15.288  -31.147 24.752  1.00 33.65  ? 43  PHE C CA  1 
ATOM   1746 C C   . PHE C 1 44 ? 15.448  -30.736 23.287  1.00 31.30  ? 43  PHE C C   1 
ATOM   1747 O O   . PHE C 1 44 ? 15.931  -29.634 23.003  1.00 35.72  ? 43  PHE C O   1 
ATOM   1748 C CB  . PHE C 1 44 ? 14.295  -30.217 25.451  1.00 33.61  ? 43  PHE C CB  1 
ATOM   1749 C CG  . PHE C 1 44 ? 12.912  -30.159 24.807  1.00 42.27  ? 43  PHE C CG  1 
ATOM   1750 C CD1 . PHE C 1 44 ? 11.945  -31.125 25.097  1.00 43.29  ? 43  PHE C CD1 1 
ATOM   1751 C CD2 . PHE C 1 44 ? 12.555  -29.100 23.958  1.00 42.17  ? 43  PHE C CD2 1 
ATOM   1752 C CE1 . PHE C 1 44 ? 10.670  -31.062 24.533  1.00 46.42  ? 43  PHE C CE1 1 
ATOM   1753 C CE2 . PHE C 1 44 ? 11.286  -29.045 23.378  1.00 43.09  ? 43  PHE C CE2 1 
ATOM   1754 C CZ  . PHE C 1 44 ? 10.347  -30.027 23.665  1.00 47.38  ? 43  PHE C CZ  1 
ATOM   1755 N N   . PHE C 1 45 ? 15.018  -31.601 22.375  1.00 31.37  ? 44  PHE C N   1 
ATOM   1756 C CA  . PHE C 1 45 ? 15.122  -31.346 20.941  1.00 33.46  ? 44  PHE C CA  1 
ATOM   1757 C C   . PHE C 1 45 ? 13.837  -30.716 20.406  1.00 37.09  ? 44  PHE C C   1 
ATOM   1758 O O   . PHE C 1 45 ? 12.749  -31.297 20.521  1.00 36.10  ? 44  PHE C O   1 
ATOM   1759 C CB  . PHE C 1 45 ? 15.381  -32.657 20.195  1.00 33.76  ? 44  PHE C CB  1 
ATOM   1760 C CG  . PHE C 1 45 ? 16.748  -33.255 20.495  1.00 33.89  ? 44  PHE C CG  1 
ATOM   1761 C CD1 . PHE C 1 45 ? 17.859  -32.913 19.730  1.00 32.27  ? 44  PHE C CD1 1 
ATOM   1762 C CD2 . PHE C 1 45 ? 16.914  -34.147 21.558  1.00 34.49  ? 44  PHE C CD2 1 
ATOM   1763 C CE1 . PHE C 1 45 ? 19.109  -33.469 20.014  1.00 33.82  ? 44  PHE C CE1 1 
ATOM   1764 C CE2 . PHE C 1 45 ? 18.154  -34.711 21.831  1.00 38.08  ? 44  PHE C CE2 1 
ATOM   1765 C CZ  . PHE C 1 45 ? 19.253  -34.361 21.070  1.00 35.06  ? 44  PHE C CZ  1 
ATOM   1766 N N   . PHE C 1 46 ? 13.959  -29.524 19.801  1.00 34.77  ? 45  PHE C N   1 
ATOM   1767 C CA  . PHE C 1 46 ? 12.776  -28.915 19.197  1.00 34.27  ? 45  PHE C CA  1 
ATOM   1768 C C   . PHE C 1 46 ? 12.281  -29.761 18.032  1.00 32.04  ? 45  PHE C C   1 
ATOM   1769 O O   . PHE C 1 46 ? 13.044  -30.524 17.435  1.00 35.78  ? 45  PHE C O   1 
ATOM   1770 C CB  . PHE C 1 46 ? 13.020  -27.496 18.665  1.00 34.14  ? 45  PHE C CB  1 
ATOM   1771 C CG  . PHE C 1 46 ? 13.355  -26.508 19.765  1.00 32.68  ? 45  PHE C CG  1 
ATOM   1772 C CD1 . PHE C 1 46 ? 12.359  -26.037 20.611  1.00 38.28  ? 45  PHE C CD1 1 
ATOM   1773 C CD2 . PHE C 1 46 ? 14.656  -26.038 19.945  1.00 33.17  ? 45  PHE C CD2 1 
ATOM   1774 C CE1 . PHE C 1 46 ? 12.668  -25.136 21.618  1.00 38.04  ? 45  PHE C CE1 1 
ATOM   1775 C CE2 . PHE C 1 46 ? 14.956  -25.121 20.945  1.00 33.84  ? 45  PHE C CE2 1 
ATOM   1776 C CZ  . PHE C 1 46 ? 13.962  -24.670 21.780  1.00 33.92  ? 45  PHE C CZ  1 
ATOM   1777 N N   . GLY C 1 47 ? 10.994  -29.611 17.699  1.00 34.91  ? 46  GLY C N   1 
ATOM   1778 C CA  . GLY C 1 47 ? 10.421  -30.329 16.573  1.00 40.01  ? 46  GLY C CA  1 
ATOM   1779 C C   . GLY C 1 47 ? 10.026  -31.755 16.942  1.00 48.44  ? 46  GLY C C   1 
ATOM   1780 O O   . GLY C 1 47 ? 8.836   -32.079 16.919  1.00 44.70  ? 46  GLY C O   1 
ATOM   1781 N N   . THR C 1 48 ? 11.019  -32.612 17.261  1.00 45.30  ? 47  THR C N   1 
ATOM   1782 C CA  . THR C 1 48 ? 10.679  -33.964 17.702  1.00 42.73  ? 47  THR C CA  1 
ATOM   1783 C C   . THR C 1 48 ? 10.103  -33.915 19.119  1.00 41.28  ? 47  THR C C   1 
ATOM   1784 O O   . THR C 1 48 ? 9.263   -34.749 19.455  1.00 47.57  ? 47  THR C O   1 
ATOM   1785 C CB  . THR C 1 48 ? 11.844  -34.955 17.644  1.00 37.92  ? 47  THR C CB  1 
ATOM   1786 O OG1 . THR C 1 48 ? 12.740  -34.468 18.641  1.00 38.78  ? 47  THR C OG1 1 
ATOM   1787 C CG2 . THR C 1 48 ? 12.478  -35.072 16.267  1.00 35.71  ? 47  THR C CG2 1 
ATOM   1788 N N   . HIS C 1 49 ? 10.592  -32.980 19.952  1.00 37.99  ? 48  HIS C N   1 
ATOM   1789 C CA  . HIS C 1 49 ? 10.213  -32.858 21.359  1.00 45.38  ? 48  HIS C CA  1 
ATOM   1790 C C   . HIS C 1 49 ? 10.736  -34.017 22.212  1.00 46.26  ? 48  HIS C C   1 
ATOM   1791 O O   . HIS C 1 49 ? 10.146  -34.345 23.236  1.00 42.85  ? 48  HIS C O   1 
ATOM   1792 C CB  . HIS C 1 49 ? 8.699   -32.647 21.532  1.00 51.90  ? 48  HIS C CB  1 
ATOM   1793 C CG  . HIS C 1 49 ? 8.195   -31.538 20.671  1.00 54.31  ? 48  HIS C CG  1 
ATOM   1794 N ND1 . HIS C 1 49 ? 7.285   -31.770 19.668  1.00 54.76  ? 48  HIS C ND1 1 
ATOM   1795 C CD2 . HIS C 1 49 ? 8.550   -30.241 20.569  1.00 50.15  ? 48  HIS C CD2 1 
ATOM   1796 C CE1 . HIS C 1 49 ? 7.069   -30.634 19.012  1.00 58.51  ? 48  HIS C CE1 1 
ATOM   1797 N NE2 . HIS C 1 49 ? 7.827   -29.697 19.542  1.00 56.03  ? 48  HIS C NE2 1 
ATOM   1798 N N   . GLU C 1 50 ? 11.855  -34.624 21.809  1.00 46.24  ? 49  GLU C N   1 
ATOM   1799 C CA  . GLU C 1 50 ? 12.442  -35.690 22.611  1.00 44.23  ? 49  GLU C CA  1 
ATOM   1800 C C   . GLU C 1 50 ? 13.559  -35.162 23.508  1.00 42.27  ? 49  GLU C C   1 
ATOM   1801 O O   . GLU C 1 50 ? 13.951  -33.999 23.421  1.00 39.18  ? 49  GLU C O   1 
ATOM   1802 C CB  . GLU C 1 50 ? 12.749  -36.878 21.714  1.00 51.57  ? 49  GLU C CB  1 
ATOM   1803 C CG  . GLU C 1 50 ? 11.501  -37.738 21.555  1.00 65.92  ? 49  GLU C CG  1 
ATOM   1804 C CD  . GLU C 1 50 ? 11.555  -38.616 20.333  1.00 62.42  ? 49  GLU C CD  1 
ATOM   1805 O OE1 . GLU C 1 50 ? 12.588  -39.282 20.101  1.00 70.66  ? 49  GLU C OE1 1 
ATOM   1806 O OE2 . GLU C 1 50 ? 10.535  -38.628 19.624  1.00 72.47  ? 49  GLU C OE2 1 
ATOM   1807 N N   . THR C 1 51 ? 14.001  -36.011 24.443  1.00 40.58  ? 50  THR C N   1 
ATOM   1808 C CA  . THR C 1 51 ? 15.041  -35.632 25.387  1.00 41.36  ? 50  THR C CA  1 
ATOM   1809 C C   . THR C 1 51 ? 16.207  -36.616 25.262  1.00 40.17  ? 50  THR C C   1 
ATOM   1810 O O   . THR C 1 51 ? 16.029  -37.735 24.785  1.00 39.66  ? 50  THR C O   1 
ATOM   1811 C CB  . THR C 1 51 ? 14.482  -35.557 26.809  1.00 42.79  ? 50  THR C CB  1 
ATOM   1812 O OG1 . THR C 1 51 ? 13.900  -36.845 26.989  1.00 47.05  ? 50  THR C OG1 1 
ATOM   1813 C CG2 . THR C 1 51 ? 13.453  -34.450 27.002  1.00 40.29  ? 50  THR C CG2 1 
ATOM   1814 N N   . ALA C 1 52 ? 17.407  -36.173 25.640  1.00 40.16  ? 51  ALA C N   1 
ATOM   1815 C CA  . ALA C 1 52 ? 18.553  -37.063 25.757  1.00 42.12  ? 51  ALA C CA  1 
ATOM   1816 C C   . ALA C 1 52 ? 19.578  -36.402 26.659  1.00 44.89  ? 51  ALA C C   1 
ATOM   1817 O O   . ALA C 1 52 ? 19.404  -35.238 27.034  1.00 43.21  ? 51  ALA C O   1 
ATOM   1818 C CB  . ALA C 1 52 ? 19.156  -37.373 24.399  1.00 39.61  ? 51  ALA C CB  1 
ATOM   1819 N N   . PHE C 1 53 ? 20.654  -37.145 26.969  1.00 41.85  ? 52  PHE C N   1 
ATOM   1820 C CA  . PHE C 1 53 ? 21.774  -36.576 27.713  1.00 41.60  ? 52  PHE C CA  1 
ATOM   1821 C C   . PHE C 1 53 ? 22.941  -36.420 26.749  1.00 38.63  ? 52  PHE C C   1 
ATOM   1822 O O   . PHE C 1 53 ? 23.318  -37.376 26.083  1.00 42.30  ? 52  PHE C O   1 
ATOM   1823 C CB  . PHE C 1 53 ? 22.172  -37.524 28.847  1.00 38.39  ? 52  PHE C CB  1 
ATOM   1824 C CG  . PHE C 1 53 ? 21.276  -37.466 30.065  1.00 42.82  ? 52  PHE C CG  1 
ATOM   1825 C CD1 . PHE C 1 53 ? 20.972  -36.250 30.671  1.00 45.80  ? 52  PHE C CD1 1 
ATOM   1826 C CD2 . PHE C 1 53 ? 20.711  -38.629 30.588  1.00 50.86  ? 52  PHE C CD2 1 
ATOM   1827 C CE1 . PHE C 1 53 ? 20.140  -36.199 31.788  1.00 47.89  ? 52  PHE C CE1 1 
ATOM   1828 C CE2 . PHE C 1 53 ? 19.894  -38.571 31.716  1.00 51.88  ? 52  PHE C CE2 1 
ATOM   1829 C CZ  . PHE C 1 53 ? 19.595  -37.354 32.297  1.00 45.62  ? 52  PHE C CZ  1 
ATOM   1830 N N   . LEU C 1 54 ? 23.523  -35.221 26.674  1.00 37.59  ? 53  LEU C N   1 
ATOM   1831 C CA  . LEU C 1 54 ? 24.671  -35.043 25.792  1.00 36.65  ? 53  LEU C CA  1 
ATOM   1832 C C   . LEU C 1 54 ? 25.771  -34.286 26.529  1.00 37.70  ? 53  LEU C C   1 
ATOM   1833 O O   . LEU C 1 54 ? 25.491  -33.497 27.431  1.00 36.21  ? 53  LEU C O   1 
ATOM   1834 C CB  . LEU C 1 54 ? 24.337  -34.356 24.461  1.00 35.85  ? 53  LEU C CB  1 
ATOM   1835 C CG  . LEU C 1 54 ? 23.388  -35.056 23.479  1.00 39.27  ? 53  LEU C CG  1 
ATOM   1836 C CD1 . LEU C 1 54 ? 23.054  -34.076 22.374  1.00 33.26  ? 53  LEU C CD1 1 
ATOM   1837 C CD2 . LEU C 1 54 ? 23.987  -36.296 22.833  1.00 43.90  ? 53  LEU C CD2 1 
ATOM   1838 N N   . GLY C 1 55 ? 27.015  -34.538 26.099  1.00 41.19  ? 54  GLY C N   1 
ATOM   1839 C CA  . GLY C 1 55 ? 28.217  -33.902 26.609  1.00 38.39  ? 54  GLY C CA  1 
ATOM   1840 C C   . GLY C 1 55 ? 28.441  -32.546 25.953  1.00 41.48  ? 54  GLY C C   1 
ATOM   1841 O O   . GLY C 1 55 ? 28.037  -32.322 24.804  1.00 45.10  ? 54  GLY C O   1 
ATOM   1842 N N   . PRO C 1 56 ? 29.121  -31.606 26.651  1.00 45.27  ? 55  PRO C N   1 
ATOM   1843 C CA  . PRO C 1 56 ? 29.191  -30.217 26.191  1.00 48.16  ? 55  PRO C CA  1 
ATOM   1844 C C   . PRO C 1 56 ? 29.851  -30.089 24.819  1.00 43.37  ? 55  PRO C C   1 
ATOM   1845 O O   . PRO C 1 56 ? 29.613  -29.122 24.105  1.00 49.31  ? 55  PRO C O   1 
ATOM   1846 C CB  . PRO C 1 56 ? 29.955  -29.491 27.318  1.00 47.47  ? 55  PRO C CB  1 
ATOM   1847 C CG  . PRO C 1 56 ? 30.787  -30.600 27.942  1.00 45.23  ? 55  PRO C CG  1 
ATOM   1848 C CD  . PRO C 1 56 ? 29.887  -31.836 27.896  1.00 48.13  ? 55  PRO C CD  1 
ATOM   1849 N N   . LYS C 1 57 ? 30.612  -31.116 24.438  1.00 40.18  ? 56  LYS C N   1 
ATOM   1850 C CA  . LYS C 1 57 ? 31.297  -31.187 23.153  1.00 44.80  ? 56  LYS C CA  1 
ATOM   1851 C C   . LYS C 1 57 ? 30.311  -31.329 21.992  1.00 47.28  ? 56  LYS C C   1 
ATOM   1852 O O   . LYS C 1 57 ? 30.674  -31.097 20.834  1.00 45.04  ? 56  LYS C O   1 
ATOM   1853 C CB  . LYS C 1 57 ? 32.158  -32.456 23.098  1.00 45.70  ? 56  LYS C CB  1 
ATOM   1854 N N   . ASP C 1 58 ? 29.094  -31.794 22.305  1.00 48.83  ? 57  ASP C N   1 
ATOM   1855 C CA  . ASP C 1 58 ? 28.073  -32.058 21.303  1.00 44.21  ? 57  ASP C CA  1 
ATOM   1856 C C   . ASP C 1 58 ? 27.145  -30.856 21.140  1.00 40.70  ? 57  ASP C C   1 
ATOM   1857 O O   . ASP C 1 58 ? 26.181  -30.940 20.385  1.00 39.33  ? 57  ASP C O   1 
ATOM   1858 C CB  . ASP C 1 58 ? 27.230  -33.259 21.691  1.00 44.65  ? 57  ASP C CB  1 
ATOM   1859 C CG  . ASP C 1 58 ? 27.999  -34.567 21.787  1.00 46.65  ? 57  ASP C CG  1 
ATOM   1860 O OD1 . ASP C 1 58 ? 29.095  -34.629 21.197  1.00 49.65  ? 57  ASP C OD1 1 
ATOM   1861 O OD2 . ASP C 1 58 ? 27.496  -35.498 22.464  1.00 43.98  ? 57  ASP C OD2 1 
ATOM   1862 N N   . LEU C 1 59 ? 27.464  -29.742 21.811  1.00 35.80  ? 58  LEU C N   1 
ATOM   1863 C CA  . LEU C 1 59 ? 26.540  -28.630 21.986  1.00 40.60  ? 58  LEU C CA  1 
ATOM   1864 C C   . LEU C 1 59 ? 27.171  -27.362 21.432  1.00 45.16  ? 58  LEU C C   1 
ATOM   1865 O O   . LEU C 1 59 ? 28.372  -27.167 21.613  1.00 45.18  ? 58  LEU C O   1 
ATOM   1866 C CB  . LEU C 1 59 ? 26.220  -28.463 23.475  1.00 37.39  ? 58  LEU C CB  1 
ATOM   1867 C CG  . LEU C 1 59 ? 25.667  -29.701 24.189  1.00 36.60  ? 58  LEU C CG  1 
ATOM   1868 C CD1 . LEU C 1 59 ? 25.372  -29.356 25.643  1.00 33.98  ? 58  LEU C CD1 1 
ATOM   1869 C CD2 . LEU C 1 59 ? 24.412  -30.218 23.481  1.00 28.04  ? 58  LEU C CD2 1 
ATOM   1870 N N   . PHE C 1 60 ? 26.346  -26.526 20.770  1.00 51.93  ? 59  PHE C N   1 
ATOM   1871 C CA  . PHE C 1 60 ? 26.774  -25.308 20.089  1.00 49.02  ? 59  PHE C CA  1 
ATOM   1872 C C   . PHE C 1 60 ? 25.782  -24.178 20.372  1.00 48.54  ? 59  PHE C C   1 
ATOM   1873 O O   . PHE C 1 60 ? 24.608  -24.310 20.045  1.00 49.65  ? 59  PHE C O   1 
ATOM   1874 C CB  . PHE C 1 60 ? 26.937  -25.575 18.588  1.00 43.63  ? 59  PHE C CB  1 
ATOM   1875 C CG  . PHE C 1 60 ? 27.931  -26.681 18.257  1.00 44.57  ? 59  PHE C CG  1 
ATOM   1876 C CD1 . PHE C 1 60 ? 27.540  -28.021 18.281  1.00 38.19  ? 59  PHE C CD1 1 
ATOM   1877 C CD2 . PHE C 1 60 ? 29.255  -26.376 17.919  1.00 42.69  ? 59  PHE C CD2 1 
ATOM   1878 C CE1 . PHE C 1 60 ? 28.451  -29.032 18.017  1.00 39.04  ? 59  PHE C CE1 1 
ATOM   1879 C CE2 . PHE C 1 60 ? 30.171  -27.394 17.665  1.00 44.02  ? 59  PHE C CE2 1 
ATOM   1880 C CZ  . PHE C 1 60 ? 29.765  -28.717 17.708  1.00 45.35  ? 59  PHE C CZ  1 
ATOM   1881 N N   . PRO C 1 61 ? 26.186  -23.044 21.011  1.00 49.75  ? 60  PRO C N   1 
ATOM   1882 C CA  . PRO C 1 61 ? 25.263  -21.927 21.241  1.00 47.48  ? 60  PRO C CA  1 
ATOM   1883 C C   . PRO C 1 61 ? 24.563  -21.548 19.939  1.00 47.40  ? 60  PRO C C   1 
ATOM   1884 O O   . PRO C 1 61 ? 25.203  -21.498 18.888  1.00 45.40  ? 60  PRO C O   1 
ATOM   1885 C CB  . PRO C 1 61 ? 26.115  -20.762 21.821  1.00 49.96  ? 60  PRO C CB  1 
ATOM   1886 C CG  . PRO C 1 61 ? 27.421  -21.412 22.246  1.00 46.76  ? 60  PRO C CG  1 
ATOM   1887 C CD  . PRO C 1 61 ? 27.540  -22.764 21.529  1.00 49.38  ? 60  PRO C CD  1 
ATOM   1888 N N   . TYR C 1 62 ? 23.238  -21.332 20.047  1.00 48.45  ? 61  TYR C N   1 
ATOM   1889 C CA  . TYR C 1 62 ? 22.323  -21.059 18.946  1.00 47.90  ? 61  TYR C CA  1 
ATOM   1890 C C   . TYR C 1 62 ? 22.791  -19.861 18.119  1.00 54.24  ? 61  TYR C C   1 
ATOM   1891 O O   . TYR C 1 62 ? 22.924  -19.977 16.901  1.00 50.37  ? 61  TYR C O   1 
ATOM   1892 C CB  . TYR C 1 62 ? 20.869  -20.902 19.413  1.00 43.54  ? 61  TYR C CB  1 
ATOM   1893 C CG  . TYR C 1 62 ? 19.904  -20.526 18.295  1.00 49.90  ? 61  TYR C CG  1 
ATOM   1894 C CD1 . TYR C 1 62 ? 19.691  -21.381 17.211  1.00 48.52  ? 61  TYR C CD1 1 
ATOM   1895 C CD2 . TYR C 1 62 ? 19.204  -19.318 18.325  1.00 49.81  ? 61  TYR C CD2 1 
ATOM   1896 C CE1 . TYR C 1 62 ? 18.819  -21.046 16.185  1.00 49.55  ? 61  TYR C CE1 1 
ATOM   1897 C CE2 . TYR C 1 62 ? 18.342  -18.967 17.299  1.00 46.96  ? 61  TYR C CE2 1 
ATOM   1898 C CZ  . TYR C 1 62 ? 18.153  -19.830 16.228  1.00 48.26  ? 61  TYR C CZ  1 
ATOM   1899 O OH  . TYR C 1 62 ? 17.292  -19.499 15.224  1.00 50.21  ? 61  TYR C OH  1 
ATOM   1900 N N   . ASP C 1 63 ? 23.072  -18.734 18.789  1.00 57.95  ? 62  ASP C N   1 
ATOM   1901 C CA  . ASP C 1 63 ? 23.440  -17.501 18.099  1.00 63.60  ? 62  ASP C CA  1 
ATOM   1902 C C   . ASP C 1 63 ? 24.789  -17.628 17.397  1.00 58.37  ? 62  ASP C C   1 
ATOM   1903 O O   . ASP C 1 63 ? 24.934  -17.197 16.254  1.00 66.77  ? 62  ASP C O   1 
ATOM   1904 C CB  . ASP C 1 63 ? 23.344  -16.279 18.997  1.00 69.95  ? 62  ASP C CB  1 
ATOM   1905 C CG  . ASP C 1 63 ? 21.986  -15.597 18.969  1.00 75.17  ? 62  ASP C CG  1 
ATOM   1906 O OD1 . ASP C 1 63 ? 21.339  -15.548 20.033  1.00 69.35  ? 62  ASP C OD1 1 
ATOM   1907 O OD2 . ASP C 1 63 ? 21.587  -15.138 17.871  1.00 82.11  ? 62  ASP C OD2 1 
ATOM   1908 N N   . LYS C 1 64 ? 25.769  -18.225 18.077  1.00 48.64  ? 63  LYS C N   1 
ATOM   1909 C CA  . LYS C 1 64 ? 27.093  -18.382 17.485  1.00 46.59  ? 63  LYS C CA  1 
ATOM   1910 C C   . LYS C 1 64 ? 27.048  -19.260 16.234  1.00 45.25  ? 63  LYS C C   1 
ATOM   1911 O O   . LYS C 1 64 ? 27.801  -19.010 15.295  1.00 45.39  ? 63  LYS C O   1 
ATOM   1912 C CB  . LYS C 1 64 ? 28.138  -18.908 18.477  1.00 44.93  ? 63  LYS C CB  1 
ATOM   1913 N N   . SER C 1 65 ? 26.167  -20.280 16.202  1.00 46.31  ? 64  SER C N   1 
ATOM   1914 C CA  . SER C 1 65 ? 26.324  -21.321 15.193  1.00 44.79  ? 64  SER C CA  1 
ATOM   1915 C C   . SER C 1 65 ? 25.132  -21.429 14.231  1.00 42.76  ? 64  SER C C   1 
ATOM   1916 O O   . SER C 1 65 ? 25.144  -22.246 13.311  1.00 36.40  ? 64  SER C O   1 
ATOM   1917 C CB  . SER C 1 65 ? 26.644  -22.655 15.842  1.00 48.83  ? 64  SER C CB  1 
ATOM   1918 O OG  . SER C 1 65 ? 25.495  -23.151 16.519  1.00 48.41  ? 64  SER C OG  1 
ATOM   1919 N N   . LYS C 1 66 ? 24.099  -20.601 14.406  1.00 40.15  ? 65  LYS C N   1 
ATOM   1920 C CA  . LYS C 1 66 ? 22.937  -20.768 13.538  1.00 43.16  ? 65  LYS C CA  1 
ATOM   1921 C C   . LYS C 1 66 ? 23.263  -20.525 12.063  1.00 44.93  ? 65  LYS C C   1 
ATOM   1922 O O   . LYS C 1 66 ? 22.683  -21.192 11.209  1.00 47.22  ? 65  LYS C O   1 
ATOM   1923 C CB  . LYS C 1 66 ? 21.696  -19.983 13.959  1.00 39.83  ? 65  LYS C CB  1 
ATOM   1924 C CG  . LYS C 1 66 ? 21.867  -18.496 13.814  1.00 40.39  ? 65  LYS C CG  1 
ATOM   1925 C CD  . LYS C 1 66 ? 20.632  -17.818 14.385  1.00 49.50  ? 65  LYS C CD  1 
ATOM   1926 C CE  . LYS C 1 66 ? 20.673  -16.341 14.283  1.00 49.11  ? 65  LYS C CE  1 
ATOM   1927 N NZ  . LYS C 1 66 ? 19.646  -15.877 15.214  1.00 61.55  ? 65  LYS C NZ  1 
ATOM   1928 N N   . ASP C 1 67 ? 24.178  -19.593 11.751  1.00 45.59  ? 66  ASP C N   1 
ATOM   1929 C CA  . ASP C 1 67 ? 24.560  -19.384 10.353  1.00 48.51  ? 66  ASP C CA  1 
ATOM   1930 C C   . ASP C 1 67 ? 25.032  -20.690 9.700   1.00 47.20  ? 66  ASP C C   1 
ATOM   1931 O O   . ASP C 1 67 ? 24.756  -20.934 8.526   1.00 46.86  ? 66  ASP C O   1 
ATOM   1932 C CB  . ASP C 1 67 ? 25.344  -18.097 10.092  1.00 51.09  ? 66  ASP C CB  1 
ATOM   1933 C CG  . ASP C 1 67 ? 26.736  -17.937 10.695  1.00 60.55  ? 66  ASP C CG  1 
ATOM   1934 O OD1 . ASP C 1 67 ? 27.546  -18.885 10.598  1.00 58.03  ? 66  ASP C OD1 1 
ATOM   1935 O OD2 . ASP C 1 67 ? 27.027  -16.831 11.212  1.00 67.12  ? 66  ASP C OD2 1 
ATOM   1936 N N   . LYS C 1 68 ? 25.679  -21.565 10.481  1.00 43.99  ? 67  LYS C N   1 
ATOM   1937 C CA  . LYS C 1 68 ? 26.182  -22.843 9.996   1.00 46.35  ? 67  LYS C CA  1 
ATOM   1938 C C   . LYS C 1 68 ? 25.133  -23.971 10.036  1.00 42.69  ? 67  LYS C C   1 
ATOM   1939 O O   . LYS C 1 68 ? 25.009  -24.712 9.060   1.00 39.42  ? 67  LYS C O   1 
ATOM   1940 C CB  . LYS C 1 68 ? 27.497  -23.161 10.724  1.00 45.50  ? 67  LYS C CB  1 
ATOM   1941 C CG  . LYS C 1 68 ? 28.148  -24.505 10.439  1.00 51.99  ? 67  LYS C CG  1 
ATOM   1942 C CD  . LYS C 1 68 ? 29.464  -24.572 11.210  1.00 65.74  ? 67  LYS C CD  1 
ATOM   1943 C CE  . LYS C 1 68 ? 30.199  -25.883 11.153  1.00 75.41  ? 67  LYS C CE  1 
ATOM   1944 N NZ  . LYS C 1 68 ? 30.520  -26.300 9.784   1.00 82.09  ? 67  LYS C NZ  1 
ATOM   1945 N N   . TYR C 1 69 ? 24.403  -24.148 11.155  1.00 35.25  ? 68  TYR C N   1 
ATOM   1946 C CA  . TYR C 1 69 ? 23.543  -25.328 11.265  1.00 38.52  ? 68  TYR C CA  1 
ATOM   1947 C C   . TYR C 1 69 ? 22.064  -24.966 11.097  1.00 36.97  ? 68  TYR C C   1 
ATOM   1948 O O   . TYR C 1 69 ? 21.218  -25.851 10.998  1.00 32.77  ? 68  TYR C O   1 
ATOM   1949 C CB  . TYR C 1 69 ? 23.720  -25.957 12.653  1.00 37.01  ? 68  TYR C CB  1 
ATOM   1950 C CG  . TYR C 1 69 ? 25.139  -26.402 12.969  1.00 39.28  ? 68  TYR C CG  1 
ATOM   1951 C CD1 . TYR C 1 69 ? 25.889  -27.149 12.061  1.00 39.11  ? 68  TYR C CD1 1 
ATOM   1952 C CD2 . TYR C 1 69 ? 25.737  -26.027 14.167  1.00 43.17  ? 68  TYR C CD2 1 
ATOM   1953 C CE1 . TYR C 1 69 ? 27.188  -27.554 12.359  1.00 40.93  ? 68  TYR C CE1 1 
ATOM   1954 C CE2 . TYR C 1 69 ? 27.029  -26.424 14.475  1.00 46.93  ? 68  TYR C CE2 1 
ATOM   1955 C CZ  . TYR C 1 69 ? 27.752  -27.189 13.573  1.00 45.09  ? 68  TYR C CZ  1 
ATOM   1956 O OH  . TYR C 1 69 ? 29.033  -27.521 13.911  1.00 51.03  ? 68  TYR C OH  1 
ATOM   1957 N N   . GLY C 1 70 ? 21.752  -23.663 11.151  1.00 30.99  ? 69  GLY C N   1 
ATOM   1958 C CA  . GLY C 1 70 ? 20.363  -23.239 11.083  1.00 39.69  ? 69  GLY C CA  1 
ATOM   1959 C C   . GLY C 1 70 ? 19.933  -23.117 9.622   1.00 45.74  ? 69  GLY C C   1 
ATOM   1960 O O   . GLY C 1 70 ? 19.854  -22.016 9.072   1.00 46.02  ? 69  GLY C O   1 
ATOM   1961 N N   . LYS C 1 71 ? 19.739  -24.273 8.987   1.00 41.88  ? 70  LYS C N   1 
ATOM   1962 C CA  . LYS C 1 71 ? 19.299  -24.344 7.605   1.00 43.44  ? 70  LYS C CA  1 
ATOM   1963 C C   . LYS C 1 71 ? 18.459  -25.603 7.468   1.00 43.72  ? 70  LYS C C   1 
ATOM   1964 O O   . LYS C 1 71 ? 18.683  -26.566 8.202   1.00 45.70  ? 70  LYS C O   1 
ATOM   1965 C CB  . LYS C 1 71 ? 20.472  -24.433 6.621   1.00 38.93  ? 70  LYS C CB  1 
ATOM   1966 C CG  . LYS C 1 71 ? 21.652  -25.248 7.135   1.00 46.94  ? 70  LYS C CG  1 
ATOM   1967 C CD  . LYS C 1 71 ? 22.522  -26.036 6.164   1.00 51.23  ? 70  LYS C CD  1 
ATOM   1968 C CE  . LYS C 1 71 ? 23.539  -26.829 6.949   1.00 58.23  ? 70  LYS C CE  1 
ATOM   1969 N N   . PRO C 1 72 ? 17.469  -25.629 6.544   1.00 37.58  ? 71  PRO C N   1 
ATOM   1970 C CA  . PRO C 1 72 ? 16.509  -26.721 6.502   1.00 36.02  ? 71  PRO C CA  1 
ATOM   1971 C C   . PRO C 1 72 ? 17.143  -28.065 6.185   1.00 39.63  ? 71  PRO C C   1 
ATOM   1972 O O   . PRO C 1 72 ? 18.212  -28.142 5.589   1.00 46.28  ? 71  PRO C O   1 
ATOM   1973 C CB  . PRO C 1 72 ? 15.577  -26.254 5.384   1.00 36.09  ? 71  PRO C CB  1 
ATOM   1974 C CG  . PRO C 1 72 ? 15.637  -24.748 5.524   1.00 36.80  ? 71  PRO C CG  1 
ATOM   1975 C CD  . PRO C 1 72 ? 17.149  -24.558 5.581   1.00 40.21  ? 71  PRO C CD  1 
ATOM   1976 N N   . ASN C 1 73 ? 16.429  -29.119 6.550   1.00 38.00  ? 72  ASN C N   1 
ATOM   1977 C CA  . ASN C 1 73 ? 16.735  -30.399 5.957   1.00 46.49  ? 72  ASN C CA  1 
ATOM   1978 C C   . ASN C 1 73 ? 15.501  -31.255 6.128   1.00 39.03  ? 72  ASN C C   1 
ATOM   1979 O O   . ASN C 1 73 ? 14.577  -30.841 6.823   1.00 37.95  ? 72  ASN C O   1 
ATOM   1980 C CB  . ASN C 1 73 ? 18.055  -30.995 6.439   1.00 54.44  ? 72  ASN C CB  1 
ATOM   1981 C CG  . ASN C 1 73 ? 17.945  -31.540 7.838   1.00 50.62  ? 72  ASN C CG  1 
ATOM   1982 O OD1 . ASN C 1 73 ? 17.276  -32.559 8.067   1.00 46.31  ? 72  ASN C OD1 1 
ATOM   1983 N ND2 . ASN C 1 73 ? 18.634  -30.884 8.752   1.00 54.25  ? 72  ASN C ND2 1 
ATOM   1984 N N   . LYS C 1 74 ? 15.536  -32.429 5.485   1.00 44.86  ? 73  LYS C N   1 
ATOM   1985 C CA  . LYS C 1 74 ? 14.342  -33.186 5.154   1.00 43.61  ? 73  LYS C CA  1 
ATOM   1986 C C   . LYS C 1 74 ? 13.966  -34.076 6.329   1.00 47.12  ? 73  LYS C C   1 
ATOM   1987 O O   . LYS C 1 74 ? 12.823  -34.517 6.404   1.00 51.32  ? 73  LYS C O   1 
ATOM   1988 C CB  . LYS C 1 74 ? 14.491  -33.927 3.816   1.00 40.07  ? 73  LYS C CB  1 
ATOM   1989 N N   . ARG C 1 75 ? 14.923  -34.295 7.245   1.00 51.10  ? 74  ARG C N   1 
ATOM   1990 C CA  . ARG C 1 75 ? 14.747  -35.197 8.378   1.00 51.67  ? 74  ARG C CA  1 
ATOM   1991 C C   . ARG C 1 75 ? 13.498  -34.828 9.160   1.00 48.99  ? 74  ARG C C   1 
ATOM   1992 O O   . ARG C 1 75 ? 13.263  -33.643 9.410   1.00 49.49  ? 74  ARG C O   1 
ATOM   1993 C CB  . ARG C 1 75 ? 15.831  -35.027 9.446   1.00 52.18  ? 74  ARG C CB  1 
ATOM   1994 C CG  . ARG C 1 75 ? 17.022  -35.945 9.267   1.00 59.39  ? 74  ARG C CG  1 
ATOM   1995 C CD  . ARG C 1 75 ? 16.568  -37.389 9.400   1.00 60.10  ? 74  ARG C CD  1 
ATOM   1996 N NE  . ARG C 1 75 ? 17.821  -38.119 9.590   1.00 57.00  ? 74  ARG C NE  1 
ATOM   1997 C CZ  . ARG C 1 75 ? 18.099  -38.909 10.609  1.00 53.88  ? 74  ARG C CZ  1 
ATOM   1998 N NH1 . ARG C 1 75 ? 17.151  -39.340 11.426  1.00 57.33  ? 74  ARG C NH1 1 
ATOM   1999 N NH2 . ARG C 1 75 ? 19.340  -39.296 10.770  1.00 54.09  ? 74  ARG C NH2 1 
ATOM   2000 N N   . LYS C 1 76 ? 12.776  -35.854 9.622   1.00 50.38  ? 75  LYS C N   1 
ATOM   2001 C CA  . LYS C 1 76 ? 11.465  -35.671 10.234  1.00 55.27  ? 75  LYS C CA  1 
ATOM   2002 C C   . LYS C 1 76 ? 11.567  -34.777 11.470  1.00 47.37  ? 75  LYS C C   1 
ATOM   2003 O O   . LYS C 1 76 ? 12.378  -35.018 12.373  1.00 46.43  ? 75  LYS C O   1 
ATOM   2004 C CB  . LYS C 1 76 ? 10.735  -36.990 10.530  1.00 55.13  ? 75  LYS C CB  1 
ATOM   2005 C CG  . LYS C 1 76 ? 9.210   -36.854 10.587  1.00 58.58  ? 75  LYS C CG  1 
ATOM   2006 C CD  . LYS C 1 76 ? 8.531   -37.813 11.567  1.00 58.33  ? 75  LYS C CD  1 
ATOM   2007 N N   . GLY C 1 77 ? 10.735  -33.727 11.491  1.00 47.73  ? 76  GLY C N   1 
ATOM   2008 C CA  . GLY C 1 77 ? 10.591  -32.907 12.686  1.00 42.19  ? 76  GLY C CA  1 
ATOM   2009 C C   . GLY C 1 77 ? 11.572  -31.731 12.672  1.00 38.90  ? 76  GLY C C   1 
ATOM   2010 O O   . GLY C 1 77 ? 11.399  -30.774 13.423  1.00 43.25  ? 76  GLY C O   1 
ATOM   2011 N N   . PHE C 1 78 ? 12.583  -31.801 11.800  1.00 35.81  ? 77  PHE C N   1 
ATOM   2012 C CA  . PHE C 1 78 ? 13.669  -30.839 11.802  1.00 33.34  ? 77  PHE C CA  1 
ATOM   2013 C C   . PHE C 1 78 ? 13.136  -29.421 11.590  1.00 36.84  ? 77  PHE C C   1 
ATOM   2014 O O   . PHE C 1 78 ? 13.545  -28.487 12.281  1.00 36.33  ? 77  PHE C O   1 
ATOM   2015 C CB  . PHE C 1 78 ? 14.753  -31.136 10.756  1.00 35.10  ? 77  PHE C CB  1 
ATOM   2016 C CG  . PHE C 1 78 ? 16.054  -30.389 11.021  1.00 32.93  ? 77  PHE C CG  1 
ATOM   2017 C CD1 . PHE C 1 78 ? 16.232  -29.079 10.593  1.00 36.95  ? 77  PHE C CD1 1 
ATOM   2018 C CD2 . PHE C 1 78 ? 17.094  -31.004 11.705  1.00 32.20  ? 77  PHE C CD2 1 
ATOM   2019 C CE1 . PHE C 1 78 ? 17.421  -28.397 10.846  1.00 40.04  ? 77  PHE C CE1 1 
ATOM   2020 C CE2 . PHE C 1 78 ? 18.274  -30.319 11.953  1.00 33.57  ? 77  PHE C CE2 1 
ATOM   2021 C CZ  . PHE C 1 78 ? 18.440  -29.018 11.531  1.00 36.99  ? 77  PHE C CZ  1 
ATOM   2022 N N   . ASN C 1 79 ? 12.307  -29.245 10.555  1.00 38.23  ? 78  ASN C N   1 
ATOM   2023 C CA  . ASN C 1 79 ? 12.038  -27.894 10.092  1.00 36.64  ? 78  ASN C CA  1 
ATOM   2024 C C   . ASN C 1 79 ? 11.073  -27.221 11.053  1.00 33.99  ? 78  ASN C C   1 
ATOM   2025 O O   . ASN C 1 79 ? 11.178  -26.020 11.324  1.00 35.46  ? 78  ASN C O   1 
ATOM   2026 C CB  . ASN C 1 79 ? 11.566  -27.875 8.644   1.00 38.78  ? 78  ASN C CB  1 
ATOM   2027 C CG  . ASN C 1 79 ? 12.643  -28.322 7.682   1.00 38.37  ? 78  ASN C CG  1 
ATOM   2028 O OD1 . ASN C 1 79 ? 13.839  -28.095 7.911   1.00 35.85  ? 78  ASN C OD1 1 
ATOM   2029 N ND2 . ASN C 1 79 ? 12.231  -28.873 6.551   1.00 39.95  ? 78  ASN C ND2 1 
ATOM   2030 N N   . GLU C 1 80 ? 10.136  -27.997 11.584  1.00 36.07  ? 79  GLU C N   1 
ATOM   2031 C CA  . GLU C 1 80 ? 9.328   -27.510 12.692  1.00 40.05  ? 79  GLU C CA  1 
ATOM   2032 C C   . GLU C 1 80 ? 10.214  -27.080 13.859  1.00 42.16  ? 79  GLU C C   1 
ATOM   2033 O O   . GLU C 1 80 ? 9.942   -26.052 14.505  1.00 37.30  ? 79  GLU C O   1 
ATOM   2034 C CB  . GLU C 1 80 ? 8.354   -28.599 13.131  1.00 41.15  ? 79  GLU C CB  1 
ATOM   2035 C CG  . GLU C 1 80 ? 7.407   -28.128 14.227  1.00 42.48  ? 79  GLU C CG  1 
ATOM   2036 C CD  . GLU C 1 80 ? 6.257   -29.096 14.405  1.00 53.71  ? 79  GLU C CD  1 
ATOM   2037 O OE1 . GLU C 1 80 ? 6.408   -30.277 14.026  1.00 61.56  ? 79  GLU C OE1 1 
ATOM   2038 O OE2 . GLU C 1 80 ? 5.198   -28.656 14.887  1.00 54.98  ? 79  GLU C OE2 1 
ATOM   2039 N N   . GLY C 1 81 ? 11.281  -27.872 14.109  1.00 36.21  ? 80  GLY C N   1 
ATOM   2040 C CA  . GLY C 1 81 ? 12.246  -27.563 15.168  1.00 33.79  ? 80  GLY C CA  1 
ATOM   2041 C C   . GLY C 1 81 ? 12.925  -26.214 14.938  1.00 30.91  ? 80  GLY C C   1 
ATOM   2042 O O   . GLY C 1 81 ? 13.208  -25.492 15.869  1.00 29.11  ? 80  GLY C O   1 
ATOM   2043 N N   . LEU C 1 82 ? 13.260  -25.918 13.685  1.00 29.27  ? 81  LEU C N   1 
ATOM   2044 C CA  . LEU C 1 82 ? 13.858  -24.646 13.320  1.00 33.68  ? 81  LEU C CA  1 
ATOM   2045 C C   . LEU C 1 82 ? 12.859  -23.506 13.559  1.00 28.23  ? 81  LEU C C   1 
ATOM   2046 O O   . LEU C 1 82 ? 13.271  -22.403 13.923  1.00 32.74  ? 81  LEU C O   1 
ATOM   2047 C CB  . LEU C 1 82 ? 14.256  -24.716 11.838  1.00 31.78  ? 81  LEU C CB  1 
ATOM   2048 C CG  . LEU C 1 82 ? 15.529  -25.493 11.460  1.00 32.16  ? 81  LEU C CG  1 
ATOM   2049 C CD1 . LEU C 1 82 ? 15.764  -25.332 9.962   1.00 34.54  ? 81  LEU C CD1 1 
ATOM   2050 C CD2 . LEU C 1 82 ? 16.740  -24.965 12.189  1.00 30.93  ? 81  LEU C CD2 1 
ATOM   2051 N N   . TRP C 1 83 ? 11.566  -23.740 13.294  1.00 30.87  ? 82  TRP C N   1 
ATOM   2052 C CA  . TRP C 1 83 ? 10.538  -22.736 13.583  1.00 35.59  ? 82  TRP C CA  1 
ATOM   2053 C C   . TRP C 1 83 ? 10.439  -22.432 15.091  1.00 37.94  ? 82  TRP C C   1 
ATOM   2054 O O   . TRP C 1 83 ? 10.419  -21.265 15.516  1.00 36.30  ? 82  TRP C O   1 
ATOM   2055 C CB  . TRP C 1 83 ? 9.173   -23.147 13.014  1.00 39.95  ? 82  TRP C CB  1 
ATOM   2056 C CG  . TRP C 1 83 ? 8.166   -22.025 13.108  1.00 49.09  ? 82  TRP C CG  1 
ATOM   2057 C CD1 . TRP C 1 83 ? 7.910   -21.069 12.169  1.00 48.05  ? 82  TRP C CD1 1 
ATOM   2058 C CD2 . TRP C 1 83 ? 7.319   -21.711 14.238  1.00 47.55  ? 82  TRP C CD2 1 
ATOM   2059 N NE1 . TRP C 1 83 ? 6.955   -20.200 12.619  1.00 49.34  ? 82  TRP C NE1 1 
ATOM   2060 C CE2 . TRP C 1 83 ? 6.573   -20.563 13.883  1.00 46.65  ? 82  TRP C CE2 1 
ATOM   2061 C CE3 . TRP C 1 83 ? 7.117   -22.286 15.501  1.00 44.82  ? 82  TRP C CE3 1 
ATOM   2062 C CZ2 . TRP C 1 83 ? 5.645   -19.989 14.747  1.00 50.51  ? 82  TRP C CZ2 1 
ATOM   2063 C CZ3 . TRP C 1 83 ? 6.200   -21.715 16.360  1.00 48.10  ? 82  TRP C CZ3 1 
ATOM   2064 C CH2 . TRP C 1 83 ? 5.475   -20.579 15.983  1.00 52.15  ? 82  TRP C CH2 1 
ATOM   2065 N N   . GLU C 1 84 ? 10.442  -23.484 15.911  1.00 37.27  ? 83  GLU C N   1 
ATOM   2066 C CA  . GLU C 1 84 ? 10.312  -23.333 17.361  1.00 34.60  ? 83  GLU C CA  1 
ATOM   2067 C C   . GLU C 1 84 ? 11.492  -22.576 17.956  1.00 39.07  ? 83  GLU C C   1 
ATOM   2068 O O   . GLU C 1 84 ? 11.277  -21.674 18.766  1.00 41.32  ? 83  GLU C O   1 
ATOM   2069 C CB  . GLU C 1 84 ? 10.175  -24.673 18.083  1.00 31.99  ? 83  GLU C CB  1 
ATOM   2070 C CG  . GLU C 1 84 ? 8.873   -25.379 17.734  1.00 37.34  ? 83  GLU C CG  1 
ATOM   2071 C CD  . GLU C 1 84 ? 8.848   -26.833 18.158  1.00 44.76  ? 83  GLU C CD  1 
ATOM   2072 O OE1 . GLU C 1 84 ? 9.871   -27.293 18.725  1.00 40.25  ? 83  GLU C OE1 1 
ATOM   2073 O OE2 . GLU C 1 84 ? 7.816   -27.505 17.901  1.00 42.53  ? 83  GLU C OE2 1 
ATOM   2074 N N   . ILE C 1 85 ? 12.735  -22.932 17.576  1.00 33.34  ? 84  ILE C N   1 
ATOM   2075 C CA  . ILE C 1 85 ? 13.891  -22.334 18.233  1.00 35.07  ? 84  ILE C CA  1 
ATOM   2076 C C   . ILE C 1 85 ? 13.929  -20.825 17.952  1.00 40.91  ? 84  ILE C C   1 
ATOM   2077 O O   . ILE C 1 85 ? 14.389  -20.065 18.796  1.00 39.99  ? 84  ILE C O   1 
ATOM   2078 C CB  . ILE C 1 85 ? 15.213  -23.039 17.874  1.00 34.57  ? 84  ILE C CB  1 
ATOM   2079 C CG1 . ILE C 1 85 ? 16.368  -22.626 18.814  1.00 36.06  ? 84  ILE C CG1 1 
ATOM   2080 C CG2 . ILE C 1 85 ? 15.588  -22.877 16.390  1.00 33.46  ? 84  ILE C CG2 1 
ATOM   2081 C CD1 . ILE C 1 85 ? 17.538  -23.607 18.852  1.00 37.65  ? 84  ILE C CD1 1 
ATOM   2082 N N   . GLN C 1 86 ? 13.439  -20.406 16.776  1.00 40.13  ? 85  GLN C N   1 
ATOM   2083 C CA  . GLN C 1 86 ? 13.516  -19.017 16.324  1.00 39.16  ? 85  GLN C CA  1 
ATOM   2084 C C   . GLN C 1 86 ? 12.335  -18.203 16.834  1.00 35.55  ? 85  GLN C C   1 
ATOM   2085 O O   . GLN C 1 86 ? 12.494  -17.022 17.130  1.00 40.60  ? 85  GLN C O   1 
ATOM   2086 C CB  . GLN C 1 86 ? 13.565  -18.885 14.794  1.00 36.57  ? 85  GLN C CB  1 
ATOM   2087 C CG  . GLN C 1 86 ? 13.826  -17.464 14.274  1.00 40.77  ? 85  GLN C CG  1 
ATOM   2088 C CD  . GLN C 1 86 ? 14.273  -17.431 12.818  1.00 40.90  ? 85  GLN C CD  1 
ATOM   2089 O OE1 . GLN C 1 86 ? 14.156  -18.416 12.080  1.00 44.99  ? 85  GLN C OE1 1 
ATOM   2090 N NE2 . GLN C 1 86 ? 14.814  -16.296 12.392  1.00 41.25  ? 85  GLN C NE2 1 
ATOM   2091 N N   . ASN C 1 87 ? 11.172  -18.844 16.916  1.00 39.14  ? 86  ASN C N   1 
ATOM   2092 C CA  . ASN C 1 87 ? 9.877   -18.197 17.074  1.00 45.60  ? 86  ASN C CA  1 
ATOM   2093 C C   . ASN C 1 87 ? 9.240   -18.515 18.430  1.00 47.07  ? 86  ASN C C   1 
ATOM   2094 O O   . ASN C 1 87 ? 8.429   -17.728 18.898  1.00 47.03  ? 86  ASN C O   1 
ATOM   2095 C CB  . ASN C 1 87 ? 8.949   -18.495 15.896  1.00 41.38  ? 86  ASN C CB  1 
ATOM   2096 C CG  . ASN C 1 87 ? 9.545   -17.944 14.617  1.00 48.18  ? 86  ASN C CG  1 
ATOM   2097 O OD1 . ASN C 1 87 ? 9.753   -16.728 14.504  1.00 44.36  ? 86  ASN C OD1 1 
ATOM   2098 N ND2 . ASN C 1 87 ? 9.905   -18.811 13.682  1.00 37.38  ? 86  ASN C ND2 1 
ATOM   2099 N N   . ASN C 1 88 ? 9.583   -19.652 19.060  1.00 45.98  ? 87  ASN C N   1 
ATOM   2100 C CA  . ASN C 1 88 ? 8.877   -20.069 20.274  1.00 48.97  ? 87  ASN C CA  1 
ATOM   2101 C C   . ASN C 1 88 ? 9.798   -20.897 21.173  1.00 48.96  ? 87  ASN C C   1 
ATOM   2102 O O   . ASN C 1 88 ? 9.455   -22.018 21.562  1.00 51.43  ? 87  ASN C O   1 
ATOM   2103 C CB  . ASN C 1 88 ? 7.600   -20.847 19.946  1.00 52.09  ? 87  ASN C CB  1 
ATOM   2104 C CG  . ASN C 1 88 ? 6.578   -20.812 21.060  1.00 57.92  ? 87  ASN C CG  1 
ATOM   2105 O OD1 . ASN C 1 88 ? 6.729   -20.040 22.014  1.00 57.48  ? 87  ASN C OD1 1 
ATOM   2106 N ND2 . ASN C 1 88 ? 5.533   -21.623 20.957  1.00 56.30  ? 87  ASN C ND2 1 
ATOM   2107 N N   . PRO C 1 89 ? 10.999  -20.393 21.532  1.00 42.46  ? 88  PRO C N   1 
ATOM   2108 C CA  . PRO C 1 89 ? 12.017  -21.250 22.132  1.00 43.44  ? 88  PRO C CA  1 
ATOM   2109 C C   . PRO C 1 89 ? 11.799  -21.683 23.580  1.00 48.82  ? 88  PRO C C   1 
ATOM   2110 O O   . PRO C 1 89 ? 12.546  -22.550 24.051  1.00 47.15  ? 88  PRO C O   1 
ATOM   2111 C CB  . PRO C 1 89 ? 13.301  -20.435 21.942  1.00 37.38  ? 88  PRO C CB  1 
ATOM   2112 C CG  . PRO C 1 89 ? 12.827  -18.984 22.031  1.00 40.05  ? 88  PRO C CG  1 
ATOM   2113 C CD  . PRO C 1 89 ? 11.444  -18.999 21.386  1.00 39.56  ? 88  PRO C CD  1 
ATOM   2114 N N   . HIS C 1 90 ? 10.759  -21.133 24.242  1.00 53.48  ? 89  HIS C N   1 
ATOM   2115 C CA  . HIS C 1 90 ? 10.465  -21.478 25.633  1.00 49.05  ? 89  HIS C CA  1 
ATOM   2116 C C   . HIS C 1 90 ? 9.000   -21.864 25.889  1.00 54.65  ? 89  HIS C C   1 
ATOM   2117 O O   . HIS C 1 90 ? 8.557   -21.842 27.033  1.00 59.33  ? 89  HIS C O   1 
ATOM   2118 C CB  . HIS C 1 90 ? 11.077  -20.483 26.627  1.00 46.98  ? 89  HIS C CB  1 
ATOM   2119 C CG  . HIS C 1 90 ? 12.497  -20.043 26.374  1.00 45.45  ? 89  HIS C CG  1 
ATOM   2120 N ND1 . HIS C 1 90 ? 12.804  -18.760 25.958  1.00 49.97  ? 89  HIS C ND1 1 
ATOM   2121 C CD2 . HIS C 1 90 ? 13.689  -20.656 26.531  1.00 45.16  ? 89  HIS C CD2 1 
ATOM   2122 C CE1 . HIS C 1 90 ? 14.126  -18.612 25.838  1.00 40.17  ? 89  HIS C CE1 1 
ATOM   2123 N NE2 . HIS C 1 90 ? 14.683  -19.759 26.176  1.00 46.86  ? 89  HIS C NE2 1 
ATOM   2124 N N   . ALA C 1 91 ? 8.251   -22.275 24.854  1.00 59.92  ? 90  ALA C N   1 
ATOM   2125 C CA  . ALA C 1 91 ? 6.964   -22.938 25.052  1.00 67.77  ? 90  ALA C CA  1 
ATOM   2126 C C   . ALA C 1 91 ? 7.153   -24.310 25.711  1.00 74.88  ? 90  ALA C C   1 
ATOM   2127 O O   . ALA C 1 91 ? 8.283   -24.760 25.888  1.00 78.92  ? 90  ALA C O   1 
ATOM   2128 C CB  . ALA C 1 91 ? 6.216   -23.048 23.740  1.00 68.61  ? 90  ALA C CB  1 
ATOM   2129 N N   . SER C 1 92 ? 6.041   -24.990 26.036  1.00 82.13  ? 91  SER C N   1 
ATOM   2130 C CA  . SER C 1 92 ? 6.054   -26.129 26.949  1.00 80.22  ? 91  SER C CA  1 
ATOM   2131 C C   . SER C 1 92 ? 6.169   -27.481 26.240  1.00 82.60  ? 91  SER C C   1 
ATOM   2132 O O   . SER C 1 92 ? 6.868   -28.373 26.724  1.00 77.05  ? 91  SER C O   1 
ATOM   2133 C CB  . SER C 1 92 ? 4.872   -26.095 27.890  1.00 71.86  ? 91  SER C CB  1 
ATOM   2134 O OG  . SER C 1 92 ? 5.102   -25.153 28.928  1.00 72.37  ? 91  SER C OG  1 
ATOM   2135 N N   . TYR C 1 93 ? 5.436   -27.647 25.133  1.00 85.96  ? 92  TYR C N   1 
ATOM   2136 C CA  . TYR C 1 93 ? 5.504   -28.847 24.311  1.00 89.23  ? 92  TYR C CA  1 
ATOM   2137 C C   . TYR C 1 93 ? 5.275   -30.095 25.180  1.00 96.31  ? 92  TYR C C   1 
ATOM   2138 O O   . TYR C 1 93 ? 5.309   -31.218 24.621  1.00 101.41 ? 92  TYR C O   1 
ATOM   2139 C CB  . TYR C 1 93 ? 6.834   -28.895 23.548  1.00 87.61  ? 92  TYR C CB  1 
ATOM   2140 C CG  . TYR C 1 93 ? 7.138   -27.648 22.726  1.00 79.14  ? 92  TYR C CG  1 
ATOM   2141 C CD1 . TYR C 1 93 ? 6.529   -27.438 21.490  1.00 73.86  ? 92  TYR C CD1 1 
ATOM   2142 C CD2 . TYR C 1 93 ? 8.032   -26.683 23.184  1.00 69.56  ? 92  TYR C CD2 1 
ATOM   2143 C CE1 . TYR C 1 93 ? 6.788   -26.303 20.739  1.00 66.66  ? 92  TYR C CE1 1 
ATOM   2144 C CE2 . TYR C 1 93 ? 8.311   -25.552 22.434  1.00 65.04  ? 92  TYR C CE2 1 
ATOM   2145 C CZ  . TYR C 1 93 ? 7.689   -25.364 21.212  1.00 62.97  ? 92  TYR C CZ  1 
ATOM   2146 O OH  . TYR C 1 93 ? 7.949   -24.242 20.486  1.00 66.76  ? 92  TYR C OH  1 
HETATM 2147 S S   . SO4 D 2 .  ? 0.871   -33.667 1.926   1.00 85.90  ? 101 SO4 A S   1 
HETATM 2148 O O1  . SO4 D 2 .  ? 1.398   -34.384 0.795   1.00 73.53  ? 101 SO4 A O1  1 
HETATM 2149 O O2  . SO4 D 2 .  ? 0.743   -32.274 1.587   1.00 95.28  ? 101 SO4 A O2  1 
HETATM 2150 O O3  . SO4 D 2 .  ? -0.423  -34.197 2.270   1.00 97.02  ? 101 SO4 A O3  1 
HETATM 2151 O O4  . SO4 D 2 .  ? 1.752   -33.803 3.051   1.00 86.15  ? 101 SO4 A O4  1 
HETATM 2152 S S   . SO4 E 2 .  ? -9.876  -24.687 1.252   1.00 109.29 ? 102 SO4 A S   1 
HETATM 2153 O O1  . SO4 E 2 .  ? -9.680  -24.361 -0.136  1.00 102.76 ? 102 SO4 A O1  1 
HETATM 2154 O O2  . SO4 E 2 .  ? -9.431  -23.591 2.072   1.00 104.23 ? 102 SO4 A O2  1 
HETATM 2155 O O3  . SO4 E 2 .  ? -11.275 -24.938 1.489   1.00 115.65 ? 102 SO4 A O3  1 
HETATM 2156 O O4  . SO4 E 2 .  ? -9.120  -25.865 1.589   1.00 112.01 ? 102 SO4 A O4  1 
HETATM 2157 C C1  . EDO F 3 .  ? 13.824  -19.497 -7.433  1.00 43.50  ? 103 EDO A C1  1 
HETATM 2158 O O1  . EDO F 3 .  ? 15.003  -18.723 -7.176  1.00 41.11  ? 103 EDO A O1  1 
HETATM 2159 C C2  . EDO F 3 .  ? 12.975  -19.057 -8.586  1.00 42.12  ? 103 EDO A C2  1 
HETATM 2160 O O2  . EDO F 3 .  ? 12.400  -17.774 -8.414  1.00 38.79  ? 103 EDO A O2  1 
HETATM 2161 C C4  . TE0 G 4 .  ? 0.142   -25.623 -7.039  0.74 57.58  ? 104 TE0 A C4  1 
HETATM 2162 C C5  . TE0 G 4 .  ? 1.482   -24.906 -7.009  0.74 54.92  ? 104 TE0 A C5  1 
HETATM 2163 C C6  . TE0 G 4 .  ? 1.770   -24.627 -5.545  0.74 55.96  ? 104 TE0 A C6  1 
HETATM 2164 C C7  . TE0 G 4 .  ? -0.590  -25.617 -8.358  0.74 52.01  ? 104 TE0 A C7  1 
HETATM 2165 N N   . TE0 G 4 .  ? 1.766   -25.854 -4.718  0.74 57.07  ? 104 TE0 A N   1 
HETATM 2166 C C   . TE0 G 4 .  ? 0.444   -23.764 -3.010  0.74 53.58  ? 104 TE0 A C   1 
HETATM 2167 O O   . TE0 G 4 .  ? 3.540   -25.002 -3.257  0.74 49.00  ? 104 TE0 A O   1 
HETATM 2168 C C1  . TE0 G 4 .  ? 1.175   -24.795 -2.206  0.74 53.82  ? 104 TE0 A C1  1 
HETATM 2169 C C2  . TE0 G 4 .  ? 0.601   -26.741 -4.933  0.74 55.22  ? 104 TE0 A C2  1 
HETATM 2170 C C3  . TE0 G 4 .  ? 0.323   -26.993 -6.409  0.74 54.51  ? 104 TE0 A C3  1 
HETATM 2171 O O1  . TE0 G 4 .  ? 2.335   -27.063 -2.659  0.74 61.88  ? 104 TE0 A O1  1 
HETATM 2172 O O2  . TE0 G 4 .  ? -0.224  -25.021 -9.333  0.74 46.27  ? 104 TE0 A O2  1 
HETATM 2173 O O3  . TE0 G 4 .  ? -1.715  -26.238 -8.275  0.74 54.16  ? 104 TE0 A O3  1 
HETATM 2174 S S   . TE0 G 4 .  ? 2.319   -25.737 -3.191  0.74 60.87  ? 104 TE0 A S   1 
HETATM 2175 S S   . SO4 H 2 .  ? 8.616   -29.383 5.768   1.00 68.01  ? 105 SO4 A S   1 
HETATM 2176 O O1  . SO4 H 2 .  ? 9.409   -28.613 4.857   1.00 67.94  ? 105 SO4 A O1  1 
HETATM 2177 O O2  . SO4 H 2 .  ? 8.179   -30.601 5.121   1.00 75.37  ? 105 SO4 A O2  1 
HETATM 2178 O O3  . SO4 H 2 .  ? 9.407   -29.691 6.937   1.00 68.09  ? 105 SO4 A O3  1 
HETATM 2179 O O4  . SO4 H 2 .  ? 7.451   -28.632 6.150   1.00 84.93  ? 105 SO4 A O4  1 
HETATM 2180 S S   . SO4 I 2 .  ? 7.375   -8.315  -24.686 1.00 71.54  ? 101 SO4 B S   1 
HETATM 2181 O O1  . SO4 I 2 .  ? 8.505   -8.429  -25.564 1.00 41.62  ? 101 SO4 B O1  1 
HETATM 2182 O O2  . SO4 I 2 .  ? 6.194   -8.751  -25.390 1.00 62.65  ? 101 SO4 B O2  1 
HETATM 2183 O O3  . SO4 I 2 .  ? 7.505   -9.148  -23.483 1.00 40.58  ? 101 SO4 B O3  1 
HETATM 2184 O O4  . SO4 I 2 .  ? 7.287   -6.908  -24.325 1.00 59.85  ? 101 SO4 B O4  1 
HETATM 2185 S S   . SO4 J 2 .  ? 14.259  -27.001 -26.439 1.00 54.93  ? 102 SO4 B S   1 
HETATM 2186 O O1  . SO4 J 2 .  ? 15.619  -26.763 -26.064 1.00 50.84  ? 102 SO4 B O1  1 
HETATM 2187 O O2  . SO4 J 2 .  ? 14.180  -28.274 -27.115 1.00 67.49  ? 102 SO4 B O2  1 
HETATM 2188 O O3  . SO4 J 2 .  ? 13.440  -27.028 -25.254 1.00 59.30  ? 102 SO4 B O3  1 
HETATM 2189 O O4  . SO4 J 2 .  ? 13.789  -25.954 -27.311 1.00 60.36  ? 102 SO4 B O4  1 
HETATM 2190 C C4  . TE0 K 4 .  ? 20.779  -15.754 -22.307 0.80 43.28  ? 103 TE0 B C4  1 
HETATM 2191 C C5  . TE0 K 4 .  ? 19.474  -16.234 -21.665 0.80 37.78  ? 103 TE0 B C5  1 
HETATM 2192 C C6  . TE0 K 4 .  ? 18.333  -16.268 -22.676 0.80 36.02  ? 103 TE0 B C6  1 
HETATM 2193 C C7  . TE0 K 4 .  ? 21.979  -16.405 -21.648 0.80 51.86  ? 103 TE0 B C7  1 
HETATM 2194 N N   . TE0 K 4 .  ? 18.453  -15.132 -23.609 0.80 31.65  ? 103 TE0 B N   1 
HETATM 2195 C C   . TE0 K 4 .  ? 16.848  -16.441 -26.150 0.80 25.81  ? 103 TE0 B C   1 
HETATM 2196 O O   . TE0 K 4 .  ? 17.392  -13.580 -25.160 0.80 32.53  ? 103 TE0 B O   1 
HETATM 2197 C C1  . TE0 K 4 .  ? 16.217  -15.929 -24.838 0.80 29.62  ? 103 TE0 B C1  1 
HETATM 2198 C C2  . TE0 K 4 .  ? 19.604  -15.262 -24.524 0.80 31.97  ? 103 TE0 B C2  1 
HETATM 2199 C C3  . TE0 K 4 .  ? 20.778  -15.965 -23.829 0.80 39.01  ? 103 TE0 B C3  1 
HETATM 2200 O O1  . TE0 K 4 .  ? 16.348  -14.082 -22.992 0.80 30.76  ? 103 TE0 B O1  1 
HETATM 2201 O O2  . TE0 K 4 .  ? 23.108  -16.347 -22.110 0.80 45.79  ? 103 TE0 B O2  1 
HETATM 2202 O O3  . TE0 K 4 .  ? 21.677  -17.035 -20.528 0.80 51.90  ? 103 TE0 B O3  1 
HETATM 2203 S S   . TE0 K 4 .  ? 17.075  -14.529 -24.141 0.80 31.89  ? 103 TE0 B S   1 
HETATM 2204 S S   . SO4 L 2 .  ? 29.148  -38.264 12.536  1.00 81.46  ? 101 SO4 C S   1 
HETATM 2205 O O1  . SO4 L 2 .  ? 30.260  -37.900 11.695  1.00 84.63  ? 101 SO4 C O1  1 
HETATM 2206 O O2  . SO4 L 2 .  ? 27.989  -37.495 12.151  1.00 85.66  ? 101 SO4 C O2  1 
HETATM 2207 O O3  . SO4 L 2 .  ? 28.853  -39.662 12.383  1.00 64.03  ? 101 SO4 C O3  1 
HETATM 2208 O O4  . SO4 L 2 .  ? 29.488  -37.987 13.916  1.00 82.81  ? 101 SO4 C O4  1 
HETATM 2209 C C4  . TE0 M 4 .  ? 16.015  -40.213 20.736  0.56 42.33  ? 102 TE0 C C4  1 
HETATM 2210 C C5  . TE0 M 4 .  ? 16.474  -40.500 19.315  0.56 38.22  ? 102 TE0 C C5  1 
HETATM 2211 C C6  . TE0 M 4 .  ? 15.952  -39.393 18.400  0.56 33.15  ? 102 TE0 C C6  1 
HETATM 2212 C C7  . TE0 M 4 .  ? 16.333  -41.316 21.701  0.56 46.52  ? 102 TE0 C C7  1 
HETATM 2213 N N   . TE0 M 4 .  ? 16.291  -38.038 18.885  0.56 33.97  ? 102 TE0 C N   1 
HETATM 2214 C C   . TE0 M 4 .  ? 18.566  -36.715 17.939  0.56 36.92  ? 102 TE0 C C   1 
HETATM 2215 O O   . TE0 M 4 .  ? 15.029  -35.953 18.795  0.56 28.18  ? 102 TE0 C O   1 
HETATM 2216 C C1  . TE0 M 4 .  ? 17.337  -35.923 17.577  0.56 33.45  ? 102 TE0 C C1  1 
HETATM 2217 C C2  . TE0 M 4 .  ? 16.022  -37.814 20.318  0.56 34.31  ? 102 TE0 C C2  1 
HETATM 2218 C C3  . TE0 M 4 .  ? 16.618  -38.897 21.183  0.56 42.18  ? 102 TE0 C C3  1 
HETATM 2219 O O1  . TE0 M 4 .  ? 15.283  -37.329 16.784  0.56 30.00  ? 102 TE0 C O1  1 
HETATM 2220 O O2  . TE0 M 4 .  ? 17.328  -41.319 22.374  0.56 49.95  ? 102 TE0 C O2  1 
HETATM 2221 O O3  . TE0 M 4 .  ? 15.401  -42.216 21.754  0.56 50.27  ? 102 TE0 C O3  1 
HETATM 2222 S S   . TE0 M 4 .  ? 15.838  -36.792 17.975  0.56 29.04  ? 102 TE0 C S   1 
HETATM 2223 O O   . HOH N 5 .  ? 5.510   -29.001 6.705   1.00 48.08  ? 201 HOH A O   1 
HETATM 2224 O O   . HOH N 5 .  ? -2.468  -30.762 -3.780  1.00 60.50  ? 202 HOH A O   1 
HETATM 2225 O O   . HOH N 5 .  ? 8.609   -32.286 3.870   1.00 61.62  ? 203 HOH A O   1 
HETATM 2226 O O   . HOH N 5 .  ? -5.748  -13.331 -16.316 1.00 45.72  ? 204 HOH A O   1 
HETATM 2227 O O   . HOH N 5 .  ? -8.665  -21.028 -1.017  1.00 50.45  ? 205 HOH A O   1 
HETATM 2228 O O   . HOH N 5 .  ? 0.971   -24.173 13.587  1.00 76.02  ? 206 HOH A O   1 
HETATM 2229 O O   . HOH N 5 .  ? 10.654  -29.620 3.023   1.00 49.71  ? 207 HOH A O   1 
HETATM 2230 O O   . HOH N 5 .  ? 10.686  -23.739 9.661   1.00 39.56  ? 208 HOH A O   1 
HETATM 2231 O O   . HOH N 5 .  ? -7.850  -17.041 6.713   1.00 45.35  ? 209 HOH A O   1 
HETATM 2232 O O   . HOH N 5 .  ? 1.584   -4.608  -10.246 1.00 42.86  ? 210 HOH A O   1 
HETATM 2233 O O   . HOH N 5 .  ? 12.754  -9.325  -7.422  1.00 44.48  ? 211 HOH A O   1 
HETATM 2234 O O   . HOH N 5 .  ? -0.252  -33.690 4.731   1.00 53.03  ? 212 HOH A O   1 
HETATM 2235 O O   . HOH N 5 .  ? 10.562  -5.222  -7.694  1.00 39.17  ? 213 HOH A O   1 
HETATM 2236 O O   . HOH N 5 .  ? 4.267   -3.557  -3.281  1.00 31.84  ? 214 HOH A O   1 
HETATM 2237 O O   . HOH N 5 .  ? 12.949  -11.936 7.931   1.00 61.11  ? 215 HOH A O   1 
HETATM 2238 O O   . HOH N 5 .  ? 6.887   -10.547 -12.149 1.00 39.15  ? 216 HOH A O   1 
HETATM 2239 O O   . HOH N 5 .  ? -3.900  -10.800 6.654   1.00 44.40  ? 217 HOH A O   1 
HETATM 2240 O O   . HOH N 5 .  ? -6.069  -19.255 -5.746  1.00 43.07  ? 218 HOH A O   1 
HETATM 2241 O O   . HOH N 5 .  ? 12.019  -15.659 -12.168 1.00 50.61  ? 219 HOH A O   1 
HETATM 2242 O O   . HOH N 5 .  ? 9.100   -22.608 -9.570  1.00 39.22  ? 220 HOH A O   1 
HETATM 2243 O O   . HOH N 5 .  ? -1.002  -29.275 9.736   1.00 60.80  ? 221 HOH A O   1 
HETATM 2244 O O   . HOH N 5 .  ? 4.202   -34.512 3.582   1.00 66.89  ? 222 HOH A O   1 
HETATM 2245 O O   . HOH N 5 .  ? 0.847   -10.551 -15.620 1.00 54.03  ? 223 HOH A O   1 
HETATM 2246 O O   . HOH N 5 .  ? 19.440  -15.452 7.300   1.00 35.47  ? 224 HOH A O   1 
HETATM 2247 O O   . HOH N 5 .  ? 8.744   -18.223 -10.992 1.00 34.74  ? 225 HOH A O   1 
HETATM 2248 O O   . HOH N 5 .  ? -2.680  3.294   -2.101  1.00 41.82  ? 226 HOH A O   1 
HETATM 2249 O O   . HOH N 5 .  ? 4.593   -1.389  -6.174  1.00 47.18  ? 227 HOH A O   1 
HETATM 2250 O O   . HOH N 5 .  ? 4.267   -7.849  1.016   1.00 35.54  ? 228 HOH A O   1 
HETATM 2251 O O   . HOH N 5 .  ? 11.202  -11.958 5.764   1.00 38.14  ? 229 HOH A O   1 
HETATM 2252 O O   . HOH N 5 .  ? 2.281   -25.036 -10.221 1.00 36.17  ? 230 HOH A O   1 
HETATM 2253 O O   . HOH N 5 .  ? 9.091   -18.279 9.531   1.00 63.11  ? 231 HOH A O   1 
HETATM 2254 O O   . HOH N 5 .  ? -6.922  -5.408  9.086   1.00 46.17  ? 232 HOH A O   1 
HETATM 2255 O O   . HOH N 5 .  ? -0.877  -20.724 6.978   1.00 36.65  ? 233 HOH A O   1 
HETATM 2256 O O   . HOH N 5 .  ? 15.577  -24.601 1.828   1.00 55.16  ? 234 HOH A O   1 
HETATM 2257 O O   . HOH N 5 .  ? -8.085  -15.560 -1.014  1.00 33.67  ? 235 HOH A O   1 
HETATM 2258 O O   . HOH N 5 .  ? -4.614  -21.145 6.171   1.00 44.15  ? 236 HOH A O   1 
HETATM 2259 O O   . HOH N 5 .  ? 17.040  -12.945 1.396   1.00 23.80  ? 237 HOH A O   1 
HETATM 2260 O O   . HOH N 5 .  ? 1.480   0.846   -7.230  1.00 50.07  ? 238 HOH A O   1 
HETATM 2261 O O   . HOH N 5 .  ? 13.844  -29.421 3.885   1.00 64.29  ? 239 HOH A O   1 
HETATM 2262 O O   . HOH N 5 .  ? 9.514   -6.164  -1.777  1.00 40.26  ? 240 HOH A O   1 
HETATM 2263 O O   . HOH N 5 .  ? -5.874  -15.669 -8.176  1.00 36.19  ? 241 HOH A O   1 
HETATM 2264 O O   . HOH N 5 .  ? 16.852  -18.109 -9.866  1.00 54.24  ? 242 HOH A O   1 
HETATM 2265 O O   . HOH N 5 .  ? 16.447  -11.957 -17.067 1.00 43.68  ? 243 HOH A O   1 
HETATM 2266 O O   . HOH N 5 .  ? 7.983   -17.798 -15.710 1.00 52.86  ? 244 HOH A O   1 
HETATM 2267 O O   . HOH N 5 .  ? 11.283  -12.268 -6.168  1.00 32.09  ? 245 HOH A O   1 
HETATM 2268 O O   . HOH N 5 .  ? 0.691   -17.455 -19.347 1.00 47.04  ? 246 HOH A O   1 
HETATM 2269 O O   . HOH N 5 .  ? -2.021  -21.934 -0.633  1.00 33.54  ? 247 HOH A O   1 
HETATM 2270 O O   . HOH N 5 .  ? -6.118  -12.808 6.664   1.00 46.77  ? 248 HOH A O   1 
HETATM 2271 O O   . HOH N 5 .  ? -0.159  -20.242 11.191  1.00 66.54  ? 249 HOH A O   1 
HETATM 2272 O O   . HOH N 5 .  ? 9.912   -13.149 9.678   1.00 49.74  ? 250 HOH A O   1 
HETATM 2273 O O   . HOH N 5 .  ? -1.236  -11.601 11.394  1.00 46.72  ? 251 HOH A O   1 
HETATM 2274 O O   . HOH N 5 .  ? 1.594   -10.157 11.743  1.00 38.59  ? 252 HOH A O   1 
HETATM 2275 O O   . HOH N 5 .  ? 7.850   -2.284  -0.265  1.00 83.86  ? 253 HOH A O   1 
HETATM 2276 O O   . HOH N 5 .  ? -8.221  -16.415 1.936   1.00 50.23  ? 254 HOH A O   1 
HETATM 2277 O O   . HOH N 5 .  ? 13.357  -28.146 -4.741  1.00 70.89  ? 255 HOH A O   1 
HETATM 2278 O O   . HOH N 5 .  ? 13.018  -12.043 -4.281  1.00 23.68  ? 256 HOH A O   1 
HETATM 2279 O O   . HOH N 5 .  ? -6.332  -11.394 -11.273 1.00 44.36  ? 257 HOH A O   1 
HETATM 2280 O O   . HOH N 5 .  ? 6.226   -16.112 -14.925 1.00 56.15  ? 258 HOH A O   1 
HETATM 2281 O O   . HOH N 5 .  ? 2.408   -6.302  5.392   1.00 45.42  ? 259 HOH A O   1 
HETATM 2282 O O   . HOH N 5 .  ? 2.771   -9.931  -13.221 1.00 60.84  ? 260 HOH A O   1 
HETATM 2283 O O   . HOH N 5 .  ? 2.723   -29.509 -0.568  1.00 47.41  ? 261 HOH A O   1 
HETATM 2284 O O   . HOH N 5 .  ? -0.109  -23.185 9.299   1.00 47.20  ? 262 HOH A O   1 
HETATM 2285 O O   . HOH N 5 .  ? -4.984  -25.596 -5.723  1.00 50.27  ? 263 HOH A O   1 
HETATM 2286 O O   . HOH N 5 .  ? 11.050  -5.955  -3.854  1.00 53.46  ? 264 HOH A O   1 
HETATM 2287 O O   . HOH N 5 .  ? 15.192  -28.193 -0.860  1.00 58.02  ? 265 HOH A O   1 
HETATM 2288 O O   . HOH N 5 .  ? -9.786  -15.872 10.334  1.00 65.83  ? 266 HOH A O   1 
HETATM 2289 O O   . HOH N 5 .  ? -1.694  -7.187  11.303  1.00 55.75  ? 267 HOH A O   1 
HETATM 2290 O O   . HOH N 5 .  ? 7.668   -7.656  1.171   1.00 32.89  ? 268 HOH A O   1 
HETATM 2291 O O   . HOH N 5 .  ? 8.534   -16.286 -13.194 1.00 42.36  ? 269 HOH A O   1 
HETATM 2292 O O   . HOH N 5 .  ? 14.423  -13.430 10.456  1.00 53.68  ? 270 HOH A O   1 
HETATM 2293 O O   . HOH N 5 .  ? 12.566  -13.338 -8.609  1.00 38.93  ? 271 HOH A O   1 
HETATM 2294 O O   . HOH N 5 .  ? 10.974  -7.785  0.390   1.00 30.01  ? 272 HOH A O   1 
HETATM 2295 O O   . HOH N 5 .  ? 22.334  -16.547 -0.081  1.00 42.64  ? 273 HOH A O   1 
HETATM 2296 O O   . HOH N 5 .  ? 9.578   -20.185 -18.468 1.00 40.35  ? 274 HOH A O   1 
HETATM 2297 O O   . HOH N 5 .  ? 21.071  -16.570 -3.503  1.00 32.33  ? 275 HOH A O   1 
HETATM 2298 O O   . HOH N 5 .  ? 15.545  -11.836 -5.511  1.00 37.26  ? 276 HOH A O   1 
HETATM 2299 O O   . HOH N 5 .  ? 9.198   -30.466 9.914   1.00 39.70  ? 277 HOH A O   1 
HETATM 2300 O O   . HOH N 5 .  ? -8.094  -21.021 -5.400  1.00 63.70  ? 278 HOH A O   1 
HETATM 2301 O O   . HOH N 5 .  ? 4.901   -7.403  3.839   1.00 38.01  ? 279 HOH A O   1 
HETATM 2302 O O   . HOH N 5 .  ? -7.373  -11.297 -8.081  1.00 35.74  ? 280 HOH A O   1 
HETATM 2303 O O   . HOH N 5 .  ? 8.945   -9.172  -13.751 1.00 41.32  ? 281 HOH A O   1 
HETATM 2304 O O   . HOH N 5 .  ? 6.142   -5.620  0.665   1.00 60.36  ? 282 HOH A O   1 
HETATM 2305 O O   . HOH N 5 .  ? -11.679 -16.049 -3.890  1.00 52.90  ? 283 HOH A O   1 
HETATM 2306 O O   . HOH N 5 .  ? -8.465  -19.547 -3.420  1.00 48.90  ? 284 HOH A O   1 
HETATM 2307 O O   . HOH N 5 .  ? -4.424  -26.765 6.939   1.00 56.82  ? 285 HOH A O   1 
HETATM 2308 O O   . HOH N 5 .  ? -7.240  -14.024 -9.116  1.00 60.10  ? 286 HOH A O   1 
HETATM 2309 O O   . HOH N 5 .  ? -6.332  -26.443 3.520   1.00 51.12  ? 287 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? -3.864  -8.192  10.464  1.00 42.15  ? 288 HOH A O   1 
HETATM 2311 O O   . HOH N 5 .  ? -3.976  -10.782 9.954   1.00 52.32  ? 289 HOH A O   1 
HETATM 2312 O O   . HOH N 5 .  ? -6.097  -23.237 -6.938  1.00 59.00  ? 290 HOH A O   1 
HETATM 2313 O O   . HOH N 5 .  ? 11.382  -21.036 10.582  1.00 44.40  ? 291 HOH A O   1 
HETATM 2314 O O   . HOH N 5 .  ? 7.832   -28.381 -8.142  1.00 74.52  ? 292 HOH A O   1 
HETATM 2315 O O   . HOH N 5 .  ? 10.629  -2.044  -1.410  1.00 58.46  ? 293 HOH A O   1 
HETATM 2316 O O   . HOH N 5 .  ? -10.494 -27.865 -1.567  1.00 62.30  ? 294 HOH A O   1 
HETATM 2317 O O   . HOH N 5 .  ? 5.570   -30.848 -3.078  1.00 61.53  ? 295 HOH A O   1 
HETATM 2318 O O   . HOH N 5 .  ? 1.506   -30.024 -7.344  1.00 60.66  ? 296 HOH A O   1 
HETATM 2319 O O   . HOH N 5 .  ? -7.410  -19.708 7.366   1.00 62.67  ? 297 HOH A O   1 
HETATM 2320 O O   . HOH N 5 .  ? -6.743  -22.454 5.763   1.00 59.52  ? 298 HOH A O   1 
HETATM 2321 O O   . HOH N 5 .  ? 7.806   -8.325  4.485   1.00 47.13  ? 299 HOH A O   1 
HETATM 2322 O O   . HOH N 5 .  ? 4.525   -9.693  -11.431 1.00 52.54  ? 300 HOH A O   1 
HETATM 2323 O O   . HOH N 5 .  ? -11.829 -13.285 -3.134  1.00 52.78  ? 301 HOH A O   1 
HETATM 2324 O O   . HOH N 5 .  ? 4.101   -2.732  2.497   1.00 62.18  ? 302 HOH A O   1 
HETATM 2325 O O   . HOH O 5 .  ? 31.095  -8.343  -29.950 1.00 54.25  ? 201 HOH B O   1 
HETATM 2326 O O   . HOH O 5 .  ? 9.943   -19.339 -43.032 1.00 67.71  ? 202 HOH B O   1 
HETATM 2327 O O   . HOH O 5 .  ? 25.898  -4.559  -33.221 1.00 46.76  ? 203 HOH B O   1 
HETATM 2328 O O   . HOH O 5 .  ? 10.547  -16.427 -44.279 1.00 66.80  ? 204 HOH B O   1 
HETATM 2329 O O   . HOH O 5 .  ? 6.254   -7.318  -32.273 1.00 63.08  ? 205 HOH B O   1 
HETATM 2330 O O   . HOH O 5 .  ? 30.407  -19.382 -40.071 1.00 37.54  ? 206 HOH B O   1 
HETATM 2331 O O   . HOH O 5 .  ? 27.664  -8.267  -28.672 1.00 48.40  ? 207 HOH B O   1 
HETATM 2332 O O   . HOH O 5 .  ? 9.909   -11.304 -38.102 1.00 50.97  ? 208 HOH B O   1 
HETATM 2333 O O   . HOH O 5 .  ? 27.569  -17.655 -24.895 1.00 46.51  ? 209 HOH B O   1 
HETATM 2334 O O   . HOH O 5 .  ? 6.315   -12.151 -25.960 1.00 41.80  ? 210 HOH B O   1 
HETATM 2335 O O   . HOH O 5 .  ? 25.922  -0.171  -29.040 1.00 58.96  ? 211 HOH B O   1 
HETATM 2336 O O   . HOH O 5 .  ? 24.884  -4.935  -29.543 1.00 43.94  ? 212 HOH B O   1 
HETATM 2337 O O   . HOH O 5 .  ? 24.346  -1.435  -36.289 1.00 58.45  ? 213 HOH B O   1 
HETATM 2338 O O   . HOH O 5 .  ? 7.413   -18.030 -31.818 1.00 48.97  ? 214 HOH B O   1 
HETATM 2339 O O   . HOH O 5 .  ? 22.004  -3.662  -24.294 1.00 76.31  ? 215 HOH B O   1 
HETATM 2340 O O   . HOH O 5 .  ? 32.471  -18.287 -41.895 1.00 48.69  ? 216 HOH B O   1 
HETATM 2341 O O   . HOH O 5 .  ? 25.508  -5.856  -35.667 1.00 55.84  ? 217 HOH B O   1 
HETATM 2342 O O   . HOH O 5 .  ? 30.550  -12.379 -45.723 1.00 56.02  ? 218 HOH B O   1 
HETATM 2343 O O   . HOH O 5 .  ? 20.093  -21.957 -22.939 1.00 56.80  ? 219 HOH B O   1 
HETATM 2344 O O   . HOH O 5 .  ? 12.922  -22.457 -20.631 1.00 53.07  ? 220 HOH B O   1 
HETATM 2345 O O   . HOH O 5 .  ? 27.441  -24.930 -37.191 1.00 94.62  ? 221 HOH B O   1 
HETATM 2346 O O   . HOH O 5 .  ? 20.922  -13.121 -42.464 1.00 44.15  ? 222 HOH B O   1 
HETATM 2347 O O   . HOH O 5 .  ? 26.113  -22.959 -30.936 1.00 35.71  ? 223 HOH B O   1 
HETATM 2348 O O   . HOH O 5 .  ? 16.644  -19.154 -28.813 1.00 26.27  ? 224 HOH B O   1 
HETATM 2349 O O   . HOH O 5 .  ? 23.399  -2.173  -28.874 1.00 46.49  ? 225 HOH B O   1 
HETATM 2350 O O   . HOH O 5 .  ? 23.466  -11.430 -21.655 1.00 44.39  ? 226 HOH B O   1 
HETATM 2351 O O   . HOH O 5 .  ? 10.493  -18.795 -32.875 1.00 31.38  ? 227 HOH B O   1 
HETATM 2352 O O   . HOH O 5 .  ? 14.434  -6.056  -40.939 1.00 54.67  ? 228 HOH B O   1 
HETATM 2353 O O   . HOH O 5 .  ? 8.705   -8.736  -16.513 1.00 42.06  ? 229 HOH B O   1 
HETATM 2354 O O   . HOH O 5 .  ? 22.552  -23.258 -28.736 1.00 44.47  ? 230 HOH B O   1 
HETATM 2355 O O   . HOH O 5 .  ? 20.718  -9.821  -42.624 1.00 36.55  ? 231 HOH B O   1 
HETATM 2356 O O   . HOH O 5 .  ? 18.049  -0.427  -38.308 1.00 34.00  ? 232 HOH B O   1 
HETATM 2357 O O   . HOH O 5 .  ? 23.745  -4.026  -36.619 1.00 29.89  ? 233 HOH B O   1 
HETATM 2358 O O   . HOH O 5 .  ? 19.921  -25.598 -34.135 1.00 36.92  ? 234 HOH B O   1 
HETATM 2359 O O   . HOH O 5 .  ? 7.062   -18.980 -35.027 1.00 58.43  ? 235 HOH B O   1 
HETATM 2360 O O   . HOH O 5 .  ? 35.122  -23.229 -29.699 1.00 71.89  ? 236 HOH B O   1 
HETATM 2361 O O   . HOH O 5 .  ? 20.329  -27.018 -36.467 1.00 44.85  ? 237 HOH B O   1 
HETATM 2362 O O   . HOH O 5 .  ? 7.456   -7.990  -20.863 1.00 43.56  ? 238 HOH B O   1 
HETATM 2363 O O   . HOH O 5 .  ? 31.844  -21.133 -37.986 1.00 47.88  ? 239 HOH B O   1 
HETATM 2364 O O   . HOH O 5 .  ? 17.963  4.722   -34.487 1.00 44.36  ? 240 HOH B O   1 
HETATM 2365 O O   . HOH O 5 .  ? 14.642  -24.467 -40.348 1.00 58.12  ? 241 HOH B O   1 
HETATM 2366 O O   . HOH O 5 .  ? 7.566   -12.548 -38.786 1.00 61.77  ? 242 HOH B O   1 
HETATM 2367 O O   . HOH O 5 .  ? 17.117  -19.547 -41.799 1.00 63.93  ? 243 HOH B O   1 
HETATM 2368 O O   . HOH O 5 .  ? 21.269  3.869   -32.633 1.00 37.27  ? 244 HOH B O   1 
HETATM 2369 O O   . HOH O 5 .  ? 27.440  -10.698 -28.437 1.00 49.54  ? 245 HOH B O   1 
HETATM 2370 O O   . HOH O 5 .  ? 8.209   -27.739 -38.142 1.00 64.82  ? 246 HOH B O   1 
HETATM 2371 O O   . HOH O 5 .  ? 1.641   -12.782 -28.305 1.00 51.88  ? 247 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 20.545  -26.636 -30.261 1.00 69.86  ? 248 HOH B O   1 
HETATM 2373 O O   . HOH O 5 .  ? 18.006  -15.576 -45.696 1.00 49.21  ? 249 HOH B O   1 
HETATM 2374 O O   . HOH O 5 .  ? 10.430  -21.575 -32.848 1.00 33.04  ? 250 HOH B O   1 
HETATM 2375 O O   . HOH O 5 .  ? 18.144  -25.835 -28.855 1.00 34.50  ? 251 HOH B O   1 
HETATM 2376 O O   . HOH O 5 .  ? 31.650  -11.991 -38.188 1.00 55.46  ? 252 HOH B O   1 
HETATM 2377 O O   . HOH O 5 .  ? 25.097  -6.706  -42.273 1.00 53.27  ? 253 HOH B O   1 
HETATM 2378 O O   . HOH O 5 .  ? 17.643  -3.448  -21.812 1.00 48.72  ? 254 HOH B O   1 
HETATM 2379 O O   . HOH O 5 .  ? 3.207   -8.185  -26.933 1.00 63.58  ? 255 HOH B O   1 
HETATM 2380 O O   . HOH O 5 .  ? 14.706  -8.139  -42.953 1.00 60.23  ? 256 HOH B O   1 
HETATM 2381 O O   . HOH O 5 .  ? 17.336  -9.462  -43.641 1.00 50.51  ? 257 HOH B O   1 
HETATM 2382 O O   . HOH O 5 .  ? 27.986  -24.602 -34.922 1.00 41.26  ? 258 HOH B O   1 
HETATM 2383 O O   . HOH O 5 .  ? 17.497  -0.549  -25.035 1.00 51.99  ? 259 HOH B O   1 
HETATM 2384 O O   . HOH O 5 .  ? 5.980   -20.291 -25.197 1.00 49.72  ? 260 HOH B O   1 
HETATM 2385 O O   . HOH O 5 .  ? 7.038   -23.306 -24.142 1.00 53.73  ? 261 HOH B O   1 
HETATM 2386 O O   . HOH O 5 .  ? 8.107   -21.208 -27.081 1.00 43.37  ? 262 HOH B O   1 
HETATM 2387 O O   . HOH O 5 .  ? 12.842  -19.985 -19.460 1.00 44.33  ? 263 HOH B O   1 
HETATM 2388 O O   . HOH O 5 .  ? 39.725  -13.668 -38.798 1.00 64.48  ? 264 HOH B O   1 
HETATM 2389 O O   . HOH O 5 .  ? 15.319  -26.030 -20.800 1.00 59.59  ? 265 HOH B O   1 
HETATM 2390 O O   . HOH O 5 .  ? 19.476  4.383   -33.159 1.00 49.79  ? 266 HOH B O   1 
HETATM 2391 O O   . HOH O 5 .  ? 14.789  -22.132 -41.704 1.00 63.99  ? 267 HOH B O   1 
HETATM 2392 O O   . HOH O 5 .  ? 29.114  -17.321 -47.611 1.00 65.48  ? 268 HOH B O   1 
HETATM 2393 O O   . HOH O 5 .  ? 7.408   -9.712  -18.444 1.00 48.14  ? 269 HOH B O   1 
HETATM 2394 O O   . HOH O 5 .  ? 7.500   -21.400 -29.730 1.00 47.84  ? 270 HOH B O   1 
HETATM 2395 O O   . HOH O 5 .  ? 22.036  -29.060 -35.529 1.00 45.13  ? 271 HOH B O   1 
HETATM 2396 O O   . HOH O 5 .  ? 8.935   -22.635 -19.252 1.00 48.34  ? 272 HOH B O   1 
HETATM 2397 O O   . HOH O 5 .  ? 16.319  3.353   -26.639 1.00 64.20  ? 273 HOH B O   1 
HETATM 2398 O O   . HOH P 5 .  ? 12.532  -27.886 28.382  1.00 59.26  ? 201 HOH C O   1 
HETATM 2399 O O   . HOH P 5 .  ? 8.466   -36.583 18.666  1.00 64.67  ? 202 HOH C O   1 
HETATM 2400 O O   . HOH P 5 .  ? 19.885  -20.956 30.734  1.00 75.13  ? 203 HOH C O   1 
HETATM 2401 O O   . HOH P 5 .  ? 27.735  -15.168 12.835  1.00 47.00  ? 204 HOH C O   1 
HETATM 2402 O O   . HOH P 5 .  ? 12.577  -31.462 8.103   1.00 47.19  ? 205 HOH C O   1 
HETATM 2403 O O   . HOH P 5 .  ? 26.291  -39.143 12.831  1.00 41.14  ? 206 HOH C O   1 
HETATM 2404 O O   . HOH P 5 .  ? 17.280  -17.051 14.735  1.00 43.01  ? 207 HOH C O   1 
HETATM 2405 O O   . HOH P 5 .  ? 24.914  -31.377 10.918  1.00 48.49  ? 208 HOH C O   1 
HETATM 2406 O O   . HOH P 5 .  ? 19.005  -20.182 10.605  1.00 41.45  ? 209 HOH C O   1 
HETATM 2407 O O   . HOH P 5 .  ? 19.428  -41.748 12.178  1.00 40.50  ? 210 HOH C O   1 
HETATM 2408 O O   . HOH P 5 .  ? 22.657  -41.567 18.652  1.00 41.12  ? 211 HOH C O   1 
HETATM 2409 O O   . HOH P 5 .  ? 29.872  -31.330 15.628  1.00 48.75  ? 212 HOH C O   1 
HETATM 2410 O O   . HOH P 5 .  ? 31.489  -42.830 12.219  1.00 49.08  ? 213 HOH C O   1 
HETATM 2411 O O   . HOH P 5 .  ? 14.652  -21.054 12.171  1.00 46.04  ? 214 HOH C O   1 
HETATM 2412 O O   . HOH P 5 .  ? 25.587  -17.735 13.781  1.00 51.62  ? 215 HOH C O   1 
HETATM 2413 O O   . HOH P 5 .  ? 26.377  -37.551 10.086  1.00 51.70  ? 216 HOH C O   1 
HETATM 2414 O O   . HOH P 5 .  ? 7.720   -31.032 11.882  1.00 66.99  ? 217 HOH C O   1 
HETATM 2415 O O   . HOH P 5 .  ? 21.827  -28.416 11.022  1.00 37.64  ? 218 HOH C O   1 
HETATM 2416 O O   . HOH P 5 .  ? 15.340  -17.636 19.264  1.00 45.16  ? 219 HOH C O   1 
HETATM 2417 O O   . HOH P 5 .  ? 27.661  -37.351 15.880  1.00 44.01  ? 220 HOH C O   1 
HETATM 2418 O O   . HOH P 5 .  ? 31.097  -43.108 15.708  1.00 56.95  ? 221 HOH C O   1 
HETATM 2419 O O   . HOH P 5 .  ? 5.367   -26.690 16.706  1.00 51.60  ? 222 HOH C O   1 
HETATM 2420 O O   . HOH P 5 .  ? 21.564  -34.324 16.625  1.00 31.51  ? 223 HOH C O   1 
HETATM 2421 O O   . HOH P 5 .  ? 20.405  -40.896 39.110  1.00 68.04  ? 224 HOH C O   1 
HETATM 2422 O O   . HOH P 5 .  ? 20.377  -39.807 26.295  1.00 45.63  ? 225 HOH C O   1 
HETATM 2423 O O   . HOH P 5 .  ? 20.475  -28.660 8.370   1.00 45.87  ? 226 HOH C O   1 
HETATM 2424 O O   . HOH P 5 .  ? 6.679   -17.963 10.992  1.00 43.69  ? 227 HOH C O   1 
HETATM 2425 O O   . HOH P 5 .  ? 25.555  -34.262 34.648  1.00 80.34  ? 228 HOH C O   1 
HETATM 2426 O O   . HOH P 5 .  ? 25.565  -17.843 20.857  1.00 50.56  ? 229 HOH C O   1 
HETATM 2427 O O   . HOH P 5 .  ? 31.052  -39.751 27.258  1.00 46.44  ? 230 HOH C O   1 
HETATM 2428 O O   . HOH P 5 .  ? 29.663  -39.848 31.438  1.00 39.58  ? 231 HOH C O   1 
HETATM 2429 O O   . HOH P 5 .  ? 12.707  -37.515 13.775  1.00 56.86  ? 232 HOH C O   1 
HETATM 2430 O O   . HOH P 5 .  ? 18.868  -26.811 3.117   1.00 47.61  ? 233 HOH C O   1 
HETATM 2431 O O   . HOH P 5 .  ? 19.915  -19.062 24.623  1.00 53.51  ? 234 HOH C O   1 
HETATM 2432 O O   . HOH P 5 .  ? 8.772   -18.983 23.803  1.00 54.32  ? 235 HOH C O   1 
HETATM 2433 O O   . HOH P 5 .  ? 27.556  -37.858 24.774  1.00 51.00  ? 236 HOH C O   1 
HETATM 2434 O O   . HOH P 5 .  ? 25.092  -39.698 20.435  1.00 39.32  ? 237 HOH C O   1 
HETATM 2435 O O   . HOH P 5 .  ? 2.238   -28.791 14.497  1.00 72.69  ? 238 HOH C O   1 
HETATM 2436 O O   . HOH P 5 .  ? 20.904  -29.201 4.686   1.00 66.00  ? 239 HOH C O   1 
HETATM 2437 O O   . HOH P 5 .  ? 30.739  -35.323 28.331  1.00 50.55  ? 240 HOH C O   1 
HETATM 2438 O O   . HOH P 5 .  ? 25.752  -14.015 11.018  1.00 57.49  ? 241 HOH C O   1 
HETATM 2439 O O   . HOH P 5 .  ? 30.085  -32.465 18.101  1.00 50.12  ? 242 HOH C O   1 
HETATM 2440 O O   . HOH P 5 .  ? 31.533  -33.881 25.562  1.00 61.62  ? 243 HOH C O   1 
HETATM 2441 O O   . HOH P 5 .  ? 22.007  -18.511 21.734  1.00 62.56  ? 244 HOH C O   1 
HETATM 2442 O O   . HOH P 5 .  ? 15.630  -19.591 29.287  1.00 70.53  ? 245 HOH C O   1 
HETATM 2443 O O   . HOH P 5 .  ? 4.812   -23.995 18.761  1.00 68.63  ? 246 HOH C O   1 
HETATM 2444 O O   . HOH P 5 .  ? 14.009  -39.187 10.257  1.00 72.68  ? 247 HOH C O   1 
HETATM 2445 O O   . HOH P 5 .  ? 29.976  -25.472 32.612  1.00 60.06  ? 248 HOH C O   1 
HETATM 2446 O O   . HOH P 5 .  ? 20.240  -13.076 13.252  1.00 53.83  ? 249 HOH C O   1 
HETATM 2447 O O   . HOH P 5 .  ? 11.140  -35.741 38.353  1.00 67.60  ? 250 HOH C O   1 
HETATM 2448 O O   . HOH P 5 .  ? 16.823  -36.647 29.398  1.00 58.60  ? 251 HOH C O   1 
HETATM 2449 O O   . HOH P 5 .  ? 31.840  -38.951 29.661  1.00 60.48  ? 252 HOH C O   1 
HETATM 2450 O O   . HOH P 5 .  ? 22.417  -13.872 13.231  1.00 50.93  ? 253 HOH C O   1 
HETATM 2451 O O   . HOH P 5 .  ? 15.594  -41.782 8.034   1.00 57.41  ? 254 HOH C O   1 
HETATM 2452 O O   . HOH P 5 .  ? 33.274  -44.447 15.238  1.00 47.39  ? 255 HOH C O   1 
# 
