data_7HHM
# 
_entry.id   7HHM 
# 
_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   7HHM         pdb_00007hhm 10.2210/pdb7hhm/pdb 
WWPDB D_1001407484 ?            ?                   
# 
_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                        7HHM 
_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 'N-methyl-1-([1,2,4]triazolo[4,3-a]pyridin-3-yl)methanamine' 162.192   2   ? ?    ? ? 
5 water       nat water                                                        18.015    234 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                SO4 
3 1,2-ETHANEDIOL                                               EDO 
4 'N-methyl-1-([1,2,4]triazolo[4,3-a]pyridin-3-yl)methanamine' UWD 
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  
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 
UWD non-polymer         . 'N-methyl-1-([1,2,4]triazolo[4,3-a]pyridin-3-yl)methanamine' ?                 'C8 H10 N4'      162.192 
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 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UWD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UWD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 UWD 1   103 102 UWD LIG B . 
K 2 SO4 1   101 5   SO4 SO4 C . 
L 4 UWD 1   102 101 UWD LIG C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 84  HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 333 HOH HOH A . 
M 5 HOH 5   205 304 HOH HOH A . 
M 5 HOH 6   206 91  HOH HOH A . 
M 5 HOH 7   207 208 HOH HOH A . 
M 5 HOH 8   208 66  HOH HOH A . 
M 5 HOH 9   209 94  HOH HOH A . 
M 5 HOH 10  210 26  HOH HOH A . 
M 5 HOH 11  211 97  HOH HOH A . 
M 5 HOH 12  212 292 HOH HOH A . 
M 5 HOH 13  213 289 HOH HOH A . 
M 5 HOH 14  214 71  HOH HOH A . 
M 5 HOH 15  215 259 HOH HOH A . 
M 5 HOH 16  216 290 HOH HOH A . 
M 5 HOH 17  217 334 HOH HOH A . 
M 5 HOH 18  218 27  HOH HOH A . 
M 5 HOH 19  219 85  HOH HOH A . 
M 5 HOH 20  220 139 HOH HOH A . 
M 5 HOH 21  221 60  HOH HOH A . 
M 5 HOH 22  222 55  HOH HOH A . 
M 5 HOH 23  223 28  HOH HOH A . 
M 5 HOH 24  224 37  HOH HOH A . 
M 5 HOH 25  225 8   HOH HOH A . 
M 5 HOH 26  226 87  HOH HOH A . 
M 5 HOH 27  227 32  HOH HOH A . 
M 5 HOH 28  228 142 HOH HOH A . 
M 5 HOH 29  229 167 HOH HOH A . 
M 5 HOH 30  230 278 HOH HOH A . 
M 5 HOH 31  231 7   HOH HOH A . 
M 5 HOH 32  232 93  HOH HOH A . 
M 5 HOH 33  233 293 HOH HOH A . 
M 5 HOH 34  234 41  HOH HOH A . 
M 5 HOH 35  235 86  HOH HOH A . 
M 5 HOH 36  236 165 HOH HOH A . 
M 5 HOH 37  237 111 HOH HOH A . 
M 5 HOH 38  238 179 HOH HOH A . 
M 5 HOH 39  239 23  HOH HOH A . 
M 5 HOH 40  240 1   HOH HOH A . 
M 5 HOH 41  241 199 HOH HOH A . 
M 5 HOH 42  242 188 HOH HOH A . 
M 5 HOH 43  243 2   HOH HOH A . 
M 5 HOH 44  244 267 HOH HOH A . 
M 5 HOH 45  245 42  HOH HOH A . 
M 5 HOH 46  246 12  HOH HOH A . 
M 5 HOH 47  247 78  HOH HOH A . 
M 5 HOH 48  248 38  HOH HOH A . 
M 5 HOH 49  249 218 HOH HOH A . 
M 5 HOH 50  250 99  HOH HOH A . 
M 5 HOH 51  251 260 HOH HOH A . 
M 5 HOH 52  252 274 HOH HOH A . 
M 5 HOH 53  253 152 HOH HOH A . 
M 5 HOH 54  254 95  HOH HOH A . 
M 5 HOH 55  255 109 HOH HOH A . 
M 5 HOH 56  256 116 HOH HOH A . 
M 5 HOH 57  257 34  HOH HOH A . 
M 5 HOH 58  258 301 HOH HOH A . 
M 5 HOH 59  259 164 HOH HOH A . 
M 5 HOH 60  260 145 HOH HOH A . 
M 5 HOH 61  261 143 HOH HOH A . 
M 5 HOH 62  262 18  HOH HOH A . 
M 5 HOH 63  263 203 HOH HOH A . 
M 5 HOH 64  264 190 HOH HOH A . 
M 5 HOH 65  265 20  HOH HOH A . 
M 5 HOH 66  266 222 HOH HOH A . 
M 5 HOH 67  267 288 HOH HOH A . 
M 5 HOH 68  268 300 HOH HOH A . 
M 5 HOH 69  269 115 HOH HOH A . 
M 5 HOH 70  270 47  HOH HOH A . 
M 5 HOH 71  271 9   HOH HOH A . 
M 5 HOH 72  272 21  HOH HOH A . 
M 5 HOH 73  273 318 HOH HOH A . 
M 5 HOH 74  274 58  HOH HOH A . 
M 5 HOH 75  275 31  HOH HOH A . 
M 5 HOH 76  276 281 HOH HOH A . 
M 5 HOH 77  277 297 HOH HOH A . 
M 5 HOH 78  278 14  HOH HOH A . 
M 5 HOH 79  279 131 HOH HOH A . 
M 5 HOH 80  280 16  HOH HOH A . 
M 5 HOH 81  281 19  HOH HOH A . 
M 5 HOH 82  282 22  HOH HOH A . 
M 5 HOH 83  283 77  HOH HOH A . 
M 5 HOH 84  284 73  HOH HOH A . 
M 5 HOH 85  285 113 HOH HOH A . 
M 5 HOH 86  286 327 HOH HOH A . 
M 5 HOH 87  287 210 HOH HOH A . 
M 5 HOH 88  288 211 HOH HOH A . 
M 5 HOH 89  289 83  HOH HOH A . 
M 5 HOH 90  290 63  HOH HOH A . 
M 5 HOH 91  291 108 HOH HOH A . 
M 5 HOH 92  292 270 HOH HOH A . 
M 5 HOH 93  293 185 HOH HOH A . 
M 5 HOH 94  294 219 HOH HOH A . 
M 5 HOH 95  295 283 HOH HOH A . 
M 5 HOH 96  296 205 HOH HOH A . 
M 5 HOH 97  297 156 HOH HOH A . 
M 5 HOH 98  298 57  HOH HOH A . 
M 5 HOH 99  299 75  HOH HOH A . 
M 5 HOH 100 300 35  HOH HOH A . 
M 5 HOH 101 301 313 HOH HOH A . 
M 5 HOH 102 302 125 HOH HOH A . 
M 5 HOH 103 303 332 HOH HOH A . 
N 5 HOH 1   201 123 HOH HOH B . 
N 5 HOH 2   202 258 HOH HOH B . 
N 5 HOH 3   203 247 HOH HOH B . 
N 5 HOH 4   204 329 HOH HOH B . 
N 5 HOH 5   205 89  HOH HOH B . 
N 5 HOH 6   206 98  HOH HOH B . 
N 5 HOH 7   207 249 HOH HOH B . 
N 5 HOH 8   208 172 HOH HOH B . 
N 5 HOH 9   209 215 HOH HOH B . 
N 5 HOH 10  210 331 HOH HOH B . 
N 5 HOH 11  211 119 HOH HOH B . 
N 5 HOH 12  212 54  HOH HOH B . 
N 5 HOH 13  213 69  HOH HOH B . 
N 5 HOH 14  214 272 HOH HOH B . 
N 5 HOH 15  215 68  HOH HOH B . 
N 5 HOH 16  216 59  HOH HOH B . 
N 5 HOH 17  217 279 HOH HOH B . 
N 5 HOH 18  218 117 HOH HOH B . 
N 5 HOH 19  219 101 HOH HOH B . 
N 5 HOH 20  220 96  HOH HOH B . 
N 5 HOH 21  221 6   HOH HOH B . 
N 5 HOH 22  222 302 HOH HOH B . 
N 5 HOH 23  223 175 HOH HOH B . 
N 5 HOH 24  224 153 HOH HOH B . 
N 5 HOH 25  225 17  HOH HOH B . 
N 5 HOH 26  226 10  HOH HOH B . 
N 5 HOH 27  227 261 HOH HOH B . 
N 5 HOH 28  228 5   HOH HOH B . 
N 5 HOH 29  229 168 HOH HOH B . 
N 5 HOH 30  230 150 HOH HOH B . 
N 5 HOH 31  231 224 HOH HOH B . 
N 5 HOH 32  232 320 HOH HOH B . 
N 5 HOH 33  233 25  HOH HOH B . 
N 5 HOH 34  234 46  HOH HOH B . 
N 5 HOH 35  235 169 HOH HOH B . 
N 5 HOH 36  236 137 HOH HOH B . 
N 5 HOH 37  237 61  HOH HOH B . 
N 5 HOH 38  238 197 HOH HOH B . 
N 5 HOH 39  239 214 HOH HOH B . 
N 5 HOH 40  240 74  HOH HOH B . 
N 5 HOH 41  241 280 HOH HOH B . 
N 5 HOH 42  242 315 HOH HOH B . 
N 5 HOH 43  243 36  HOH HOH B . 
N 5 HOH 44  244 76  HOH HOH B . 
N 5 HOH 45  245 44  HOH HOH B . 
N 5 HOH 46  246 79  HOH HOH B . 
N 5 HOH 47  247 217 HOH HOH B . 
N 5 HOH 48  248 303 HOH HOH B . 
N 5 HOH 49  249 242 HOH HOH B . 
N 5 HOH 50  250 335 HOH HOH B . 
N 5 HOH 51  251 223 HOH HOH B . 
N 5 HOH 52  252 24  HOH HOH B . 
N 5 HOH 53  253 182 HOH HOH B . 
N 5 HOH 54  254 72  HOH HOH B . 
N 5 HOH 55  255 316 HOH HOH B . 
N 5 HOH 56  256 13  HOH HOH B . 
N 5 HOH 57  257 120 HOH HOH B . 
N 5 HOH 58  258 163 HOH HOH B . 
N 5 HOH 59  259 104 HOH HOH B . 
N 5 HOH 60  260 201 HOH HOH B . 
N 5 HOH 61  261 157 HOH HOH B . 
N 5 HOH 62  262 291 HOH HOH B . 
N 5 HOH 63  263 170 HOH HOH B . 
N 5 HOH 64  264 160 HOH HOH B . 
N 5 HOH 65  265 177 HOH HOH B . 
N 5 HOH 66  266 322 HOH HOH B . 
N 5 HOH 67  267 314 HOH HOH B . 
N 5 HOH 68  268 107 HOH HOH B . 
N 5 HOH 69  269 309 HOH HOH B . 
N 5 HOH 70  270 92  HOH HOH B . 
N 5 HOH 71  271 312 HOH HOH B . 
N 5 HOH 72  272 310 HOH HOH B . 
O 5 HOH 1   201 161 HOH HOH C . 
O 5 HOH 2   202 184 HOH HOH C . 
O 5 HOH 3   203 317 HOH HOH C . 
O 5 HOH 4   204 226 HOH HOH C . 
O 5 HOH 5   205 321 HOH HOH C . 
O 5 HOH 6   206 323 HOH HOH C . 
O 5 HOH 7   207 296 HOH HOH C . 
O 5 HOH 8   208 134 HOH HOH C . 
O 5 HOH 9   209 49  HOH HOH C . 
O 5 HOH 10  210 15  HOH HOH C . 
O 5 HOH 11  211 269 HOH HOH C . 
O 5 HOH 12  212 189 HOH HOH C . 
O 5 HOH 13  213 149 HOH HOH C . 
O 5 HOH 14  214 254 HOH HOH C . 
O 5 HOH 15  215 173 HOH HOH C . 
O 5 HOH 16  216 90  HOH HOH C . 
O 5 HOH 17  217 284 HOH HOH C . 
O 5 HOH 18  218 45  HOH HOH C . 
O 5 HOH 19  219 4   HOH HOH C . 
O 5 HOH 20  220 82  HOH HOH C . 
O 5 HOH 21  221 40  HOH HOH C . 
O 5 HOH 22  222 294 HOH HOH C . 
O 5 HOH 23  223 271 HOH HOH C . 
O 5 HOH 24  224 295 HOH HOH C . 
O 5 HOH 25  225 209 HOH HOH C . 
O 5 HOH 26  226 118 HOH HOH C . 
O 5 HOH 27  227 132 HOH HOH C . 
O 5 HOH 28  228 122 HOH HOH C . 
O 5 HOH 29  229 148 HOH HOH C . 
O 5 HOH 30  230 43  HOH HOH C . 
O 5 HOH 31  231 102 HOH HOH C . 
O 5 HOH 32  232 56  HOH HOH C . 
O 5 HOH 33  233 126 HOH HOH C . 
O 5 HOH 34  234 53  HOH HOH C . 
O 5 HOH 35  235 151 HOH HOH C . 
O 5 HOH 36  236 287 HOH HOH C . 
O 5 HOH 37  237 171 HOH HOH C . 
O 5 HOH 38  238 275 HOH HOH C . 
O 5 HOH 39  239 62  HOH HOH C . 
O 5 HOH 40  240 48  HOH HOH C . 
O 5 HOH 41  241 298 HOH HOH C . 
O 5 HOH 42  242 67  HOH HOH C . 
O 5 HOH 43  243 328 HOH HOH C . 
O 5 HOH 44  244 299 HOH HOH C . 
O 5 HOH 45  245 135 HOH HOH C . 
O 5 HOH 46  246 198 HOH HOH C . 
O 5 HOH 47  247 130 HOH HOH C . 
O 5 HOH 48  248 246 HOH HOH C . 
O 5 HOH 49  249 65  HOH HOH C . 
O 5 HOH 50  250 305 HOH HOH C . 
O 5 HOH 51  251 146 HOH HOH C . 
O 5 HOH 52  252 64  HOH HOH C . 
O 5 HOH 53  253 241 HOH HOH C . 
O 5 HOH 54  254 330 HOH HOH C . 
O 5 HOH 55  255 319 HOH HOH C . 
O 5 HOH 56  256 70  HOH HOH C . 
O 5 HOH 57  257 324 HOH HOH C . 
O 5 HOH 58  258 103 HOH HOH C . 
O 5 HOH 59  259 206 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 LYS 34 ? CG  ? C LYS 35 CG  
46 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
47 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
48 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
49 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
50 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
51 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
52 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
53 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
54 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
55 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
56 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
57 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
58 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
59 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
60 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
61 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
62 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
63 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' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHM 
_cell.length_a           41.387 
_cell.length_b           42.061 
_cell.length_c           158.488 
_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                         7HHM 
_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          7HHM 
_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                     7HHM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.24 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   24937 
_reflns.percent_possible_obs         90.8 
_reflns.pdbx_Rmerge_I_obs            0.109 
_reflns.pdbx_netI_over_sigmaI        8.4 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.119 
_reflns.pdbx_Rpim_I_all              0.047 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     153312 
_reflns.pdbx_chi_squared             0.92 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.78 
_reflns_shell.d_res_low                   1.88 
_reflns_shell.number_measured_all         25187 
_reflns_shell.number_unique_obs           3829 
_reflns_shell.Rmerge_I_obs                1.937 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             6.6 
_reflns_shell.percent_possible_obs        97.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             2.101 
_reflns_shell.pdbx_Rpim_I_all             0.805 
_reflns_shell.pdbx_CC_half                0.416 
_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                                 7HHM 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23387 
_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                             79.24 
_refine.ls_d_res_high                            1.78 
_refine.ls_percent_reflns_obs                    90.08 
_refine.ls_R_factor_obs                          0.20085 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19795 
_refine.ls_R_factor_R_free                       0.25206 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1291 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.B_iso_mean                               39.493 
_refine.aniso_B[1][1]                            0.89 
_refine.aniso_B[2][2]                            -1.32 
_refine.aniso_B[3][3]                            0.42 
_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                       0.157 
_refine.pdbx_overall_ESU_R_Free                  0.153 
_refine.overall_SU_ML                            0.135 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.682 
_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        2122 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             234 
_refine_hist.number_atoms_total               2414 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        79.24 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.012  ? 2285 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.570  1.827  ? 3112 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.338  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.521  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.474 10.000 ? 296  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 1970 '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                  3.334  3.768  ? 1071 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.839  6.720  ? 1331 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.222  4.034  ? 1214 '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       9.961  54.98  ? 3546 '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                       1.781 
_refine_ls_shell.d_res_low                        1.827 
_refine_ls_shell.number_reflns_R_work             1875 
_refine_ls_shell.R_factor_R_work                  0.345 
_refine_ls_shell.percent_reflns_obs               98.89 
_refine_ls_shell.R_factor_R_free                  0.327 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             89 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHM 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z234898257' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHM 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHM A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHM B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHM 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 7HHM GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHM SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHM GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHM SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHM GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHM SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O 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 ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHM 
_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 O2 A SO4 104 ? ? O A HOH 201 ? ? 1.85 
2 1 O  B HOH 241 ? ? O B HOH 266 ? ? 1.93 
3 1 O  B HOH 248 ? ? O B HOH 266 ? ? 2.05 
4 1 O  C HOH 251 ? ? O C HOH 257 ? ? 2.08 
5 1 O  A HOH 209 ? ? O A HOH 285 ? ? 2.14 
6 1 O  A PRO 37  ? ? O A HOH 202 ? ? 2.18 
7 1 O  C HOH 222 ? ? O C HOH 255 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     212 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     266 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.19 
# 
_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                110.71 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            10.51 
_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 87 ? ? -155.17 62.55  
2 1 ASN B 38 ? ? 84.20   -13.27 
3 1 ASN B 87 ? ? -160.32 59.02  
4 1 ASN C 87 ? ? -154.37 55.85  
# 
_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            148.82 
# 
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 ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
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 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
UWD N1   N Y N 387 
UWD N3   N Y N 388 
UWD C4   C Y N 389 
UWD C5   C Y N 390 
UWD C6   C Y N 391 
UWD C7   C Y N 392 
UWD N    N N N 393 
UWD C    C N N 394 
UWD C1   C N N 395 
UWD C2   C Y N 396 
UWD C3   C Y N 397 
UWD N2   N Y N 398 
UWD H1   H N N 399 
UWD H2   H N N 400 
UWD H3   H N N 401 
UWD H4   H N N 402 
UWD H5   H N N 403 
UWD H7   H N N 404 
UWD H8   H N N 405 
UWD H9   H N N 406 
UWD H10  H N N 407 
UWD H11  H N N 408 
VAL N    N N N 409 
VAL CA   C N S 410 
VAL C    C N N 411 
VAL O    O N N 412 
VAL CB   C N N 413 
VAL CG1  C N N 414 
VAL CG2  C N N 415 
VAL OXT  O N N 416 
VAL H    H N N 417 
VAL H2   H N N 418 
VAL HA   H N N 419 
VAL HB   H N N 420 
VAL HG11 H N N 421 
VAL HG12 H N N 422 
VAL HG13 H N N 423 
VAL HG21 H N N 424 
VAL HG22 H N N 425 
VAL HG23 H N N 426 
VAL HXT  H N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
UWD C   N    sing N N 371 
UWD N2  N1   sing Y N 372 
UWD N2  C3   doub Y N 373 
UWD N1  C2   doub Y N 374 
UWD C3  C4   sing Y N 375 
UWD C3  N3   sing Y N 376 
UWD N   C1   sing N N 377 
UWD C2  C1   sing N N 378 
UWD C2  N3   sing Y N 379 
UWD C4  C5   doub Y N 380 
UWD N3  C7   sing Y N 381 
UWD C5  C6   sing Y N 382 
UWD C7  C6   doub Y N 383 
UWD C4  H1   sing N N 384 
UWD C5  H2   sing N N 385 
UWD C6  H3   sing N N 386 
UWD C7  H4   sing N N 387 
UWD N   H5   sing N N 388 
UWD C   H7   sing N N 389 
UWD C   H8   sing N N 390 
UWD C   H9   sing N N 391 
UWD C1  H10  sing N N 392 
UWD C1  H11  sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
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                    7HHM 
_atom_sites.fract_transf_matrix[1][1]   0.024162 
_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]   0.023775 
_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]   0.006310 
_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  ? 0.563   4.380   2.436   1.00 46.56  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.487  3.605   1.724   1.00 55.08  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.149   2.523   0.850   1.00 48.34  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.289   2.655   0.406   1.00 46.96  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.409  4.500   0.882   1.00 57.27  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.514  5.214   1.658   1.00 71.00  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.665  4.290   2.707   1.00 73.69  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -2.640  4.016   4.162   1.00 80.70  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.555  1.382   0.650   1.00 45.15  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.111  0.318   -0.262  1.00 43.30  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.123   0.699   -1.729  1.00 46.84  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.580  1.536   -2.303  1.00 47.43  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.310  -0.694  -0.112  1.00 42.63  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.797  -0.476  1.312   1.00 40.73  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.791  1.029   1.377   1.00 43.48  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.124   0.055   -2.335  1.00 39.01  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.326   0.148   -3.761  1.00 39.64  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.769   -1.143  -4.352  1.00 36.80  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.276   -1.989  -3.607  1.00 39.07  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.825   0.283   -4.076  1.00 46.25  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.493   1.563   -3.671  1.00 56.32  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.311   2.211   -2.466  1.00 61.52  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.402   2.296   -4.342  1.00 66.00  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.065   3.302   -2.427  1.00 58.75  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.738   3.371   -3.555  1.00 64.93  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.865   -1.287  -5.679  1.00 31.04  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.612   -2.547  -6.355  1.00 29.16  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.700   -3.555  -5.982  1.00 29.21  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.790   -3.196  -5.511  1.00 27.80  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.522   -2.331  -7.859  1.00 32.12  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.398   -4.836  -6.185  1.00 31.04  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.392   -5.866  -5.935  1.00 32.54  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.569   -5.709  -6.900  1.00 34.75  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.388   -5.380  -8.070  1.00 33.40  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.802   -7.273  -6.017  1.00 28.96  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.060   -7.677  -4.749  1.00 30.18  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.745   -7.890  -3.549  1.00 28.21  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.319  -7.875  -4.772  1.00 27.02  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.066   -8.272  -2.394  1.00 27.25  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.986  -8.285  -3.622  1.00 24.48  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.304  -8.478  -2.439  1.00 25.16  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.779   -5.997  -6.412  1.00 28.53  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.917   -5.961  -7.310  1.00 28.51  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.841   -7.139  -7.008  1.00 25.16  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.841   -7.685  -5.911  1.00 23.30  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.597   -4.596  -7.153  1.00 29.47  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.360   -4.505  -5.865  1.00 30.18  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.858   -3.100  -5.531  1.00 36.93  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.636   -3.120  -4.258  1.00 36.39  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.768   -3.281  -3.088  1.00 33.40  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.666   -7.570  -7.987  1.00 26.93  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.621   -8.652  -7.760  1.00 26.32  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.446   -8.402  -6.497  1.00 25.91  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.874   -7.276  -6.237  1.00 24.55  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.485   -8.626  -9.055  1.00 28.76  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.575   -8.020  -10.122 1.00 30.78  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.730   -7.007  -9.353  1.00 29.10  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.602   -9.452  -5.673  1.00 23.81  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.285  -9.330  -4.398  1.00 21.12  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.354   -9.197  -3.190  1.00 24.85  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.775   -9.458  -2.059  1.00 24.70  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.102   -8.763  -3.386  1.00 20.88  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.170   -8.702  -2.266  1.00 22.72  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.947   -10.094 -1.670  1.00 20.00  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.816   -11.074 -2.402  1.00 19.74  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.819   -8.098  -2.661  1.00 20.53  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.837   -6.602  -2.933  1.00 24.18  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.811   -5.971  -2.522  1.00 23.66  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.895   -6.087  -3.573  1.00 22.47  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.857   -10.161 -0.335  1.00 19.20  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.667   -11.426 0.358   1.00 20.17  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.206   -11.502 0.778   1.00 23.03  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.650   -10.500 1.260   1.00 24.07  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.576   -11.449 1.583   1.00 19.86  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.065   -11.244 1.271   1.00 19.65  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.891   -11.341 2.527   1.00 21.55  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.492   -12.243 0.190   1.00 20.64  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.630   -12.700 0.640   1.00 21.42  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.199   -12.900 0.866   1.00 21.12  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.949   -14.270 1.500   1.00 24.43  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.848   -15.130 1.559   1.00 22.78  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.421   -12.752 -0.458  1.00 19.08  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.582   -11.343 -1.032  1.00 19.11  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.777   -13.815 -1.512  1.00 18.62  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.722   -14.455 2.002   1.00 21.39  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.124   -15.780 2.083   1.00 22.50  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.170   -15.865 0.903   1.00 24.41  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.611  -14.945 0.703   1.00 23.65  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.359   -16.167 3.367   1.00 21.82  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.292   -16.252 4.569   1.00 25.12  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.635   -15.103 5.283   1.00 25.30  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.812   -17.474 4.987   1.00 25.12  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.524   -15.165 6.339   1.00 29.84  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.689   -17.537 6.059   1.00 30.90  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.036   -16.395 6.742   1.00 31.13  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.312   -16.927 0.088   1.00 25.68  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.488  -17.105 -1.114  1.00 25.84  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.459  -18.267 -0.882  1.00 27.04  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.078  -19.309 -0.327  1.00 26.09  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.413   -17.359 -2.312  1.00 22.62  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.725  -18.038 -1.240  1.00 26.64  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.799  -18.984 -0.974  1.00 27.46  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.189  -19.675 -2.283  1.00 28.79  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.490  -19.018 -3.287  1.00 30.50  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.033  -18.312 -0.350  1.00 29.20  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.135  -19.306 0.082   1.00 33.97  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.723  -20.288 1.184   1.00 36.47  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.850  -21.166 1.731   1.00 34.46  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.145  -22.233 0.768   1.00 33.87  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.121  -21.009 -2.266  1.00 29.31  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.702  -21.805 -3.330  1.00 31.82  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.705  -22.795 -2.746  1.00 35.38  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.547  -23.233 -1.613  1.00 33.01  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.607  -22.560 -4.077  1.00 35.52  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.659  -21.563 -4.730  1.00 38.97  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.833  -22.256 -6.155  1.00 43.83  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -3.153  -22.967 -7.144  1.00 57.65  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.720  -23.129 -3.552  1.00 40.60  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.770  -24.075 -3.202  1.00 40.02  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.138  -25.323 -2.608  1.00 40.04  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.234  -25.896 -3.212  1.00 38.69  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.519  -24.486 -4.477  1.00 46.27  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.958  -24.926 -4.243  1.00 52.91  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.791 -23.987 -3.367  1.00 54.76  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.593  -25.710 -1.405  1.00 36.86  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.181  -26.976 -0.832  1.00 37.50  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.814  -26.895 -0.167  1.00 44.86  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.304  -27.911 0.288   1.00 48.28  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.225  -25.694 -0.079  1.00 36.92  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.983  -25.591 0.666   1.00 35.03  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.116  -24.487 1.697   1.00 33.11  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.875  -23.545 1.480   1.00 34.34  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.788  -25.246 -0.221  1.00 43.02  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.417  -26.280 -1.270  1.00 42.65  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.509  -27.291 -0.993  1.00 50.90  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.960  -26.216 -2.547  1.00 48.74  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.160  -28.218 -1.963  1.00 58.04  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.622  -27.135 -3.528  1.00 50.59  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.719  -28.139 -3.229  1.00 60.68  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.401  -29.041 -4.203  1.00 75.59  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.374  -24.544 2.831   1.00 29.05  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.364  -23.416 3.773   1.00 31.23  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.594  -22.282 3.078   1.00 30.40  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.865  -22.541 2.106   1.00 27.83  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.596  -24.022 4.972   1.00 30.63  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.610  -24.999 4.320   1.00 29.26  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.432  -25.613 3.197   1.00 34.05  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.831  -21.044 3.534   1.00 26.54  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.086  -19.852 3.166   1.00 27.91  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.589  -20.156 3.288   1.00 28.77  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.116  -20.606 4.340   1.00 28.76  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.553  -18.646 4.000   1.00 27.00  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.021  -18.316 3.870   1.00 29.71  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.015  -19.028 4.525   1.00 31.07  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.659  -17.344 3.179   1.00 29.72  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.212  -18.509 4.226   1.00 30.79  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.024  -17.478 3.412   1.00 32.58  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.141   -19.947 2.186   1.00 27.03  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.457   -20.556 2.030   1.00 26.83  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.522   -19.480 1.820   1.00 25.71  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.333   -18.593 1.003   1.00 26.30  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.442   -21.519 0.836   1.00 24.57  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.546   -22.542 0.887   1.00 28.13  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.883   -22.360 0.662   1.00 27.78  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.371   -23.944 1.189   1.00 27.51  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.553   -23.552 0.791   1.00 30.31  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.651   -24.547 1.100   1.00 30.23  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.260   -24.744 1.478   1.00 31.52  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.853   -25.912 1.338   1.00 32.51  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.459   -26.099 1.687   1.00 34.30  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.741   -26.668 1.645   1.00 34.38  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.661   -19.545 2.544   1.00 23.58  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.714   -18.531 2.440   1.00 23.85  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.223   -18.547 1.004   1.00 22.88  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.485   -19.629 0.437   1.00 22.26  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.764   -18.992 3.489   1.00 26.37  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.519   -20.493 3.635   1.00 23.05  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 3.988   -20.599 3.508   1.00 23.55  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.257   -17.343 0.414   1.00 19.10  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.573   -17.184 -0.991  1.00 21.28  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.153   -15.805 -1.310  1.00 21.71  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.263   -14.919 -0.456  1.00 20.90  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.339   -17.527 -1.839  1.00 23.41  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.621   -15.647 -2.556  1.00 23.24  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.081   -14.335 -2.985  1.00 22.76  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.544   -14.050 -4.379  1.00 21.60  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.231   -14.980 -5.142  1.00 22.75  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.610   -14.215 -2.915  1.00 20.35  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.354   -15.165 -3.840  1.00 20.73  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.874  -14.903 -3.855  1.00 22.45  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.591  -15.713 -4.859  1.00 22.72  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.834  -16.178 -4.720  1.00 24.95  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.516  -15.986 -3.601  1.00 21.77  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.384  -16.864 -5.704  1.00 25.12  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.469   -12.764 -4.727  1.00 22.08  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.226   -12.412 -6.121  1.00 23.19  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.553   -12.542 -6.859  1.00 26.00  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.517   -11.894 -6.459  1.00 24.01  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.700   -10.971 -6.261  1.00 27.79  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.516   -10.668 -5.323  1.00 30.70  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.427   -10.648 -7.745  1.00 23.59  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.164   -11.082 -5.836  1.00 34.35  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.598   -13.372 -7.911  1.00 25.69  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.830   -13.534 -8.661  1.00 29.76  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.969   -12.501 -9.778  1.00 30.94  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.010   -11.877 -10.209 1.00 27.17  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.981   -14.915 -9.271  1.00 31.14  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.903   -15.851 -8.509  1.00 32.54  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.442  -15.430 -7.469  1.00 36.01  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.064  -16.993 -8.954  1.00 31.97  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.223  -12.321 -10.214 1.00 31.27  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.532  -11.718 -11.494 1.00 35.04  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.213  -12.740 -12.584 1.00 32.99  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.034  -13.918 -12.311 1.00 32.18  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.007  -11.358 -11.566 1.00 39.48  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.433  -10.150 -10.746 1.00 46.56  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.048  -9.017  -11.126 1.00 48.80  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.143  -10.356 -9.735  1.00 49.72  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.099  -12.274 -13.819 1.00 35.45  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.012  -13.174 -14.960 1.00 34.79  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.353  -13.035 -15.667 1.00 35.50  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.711  -11.914 -16.008 1.00 37.34  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.892   -12.667 -15.874 1.00 40.23  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.536   -12.647 -15.151 1.00 45.00  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.860   -13.419 -17.211 1.00 31.71  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.614   -11.542 -15.641 1.00 46.03  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.091  -14.139 -15.827 1.00 33.50  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.393  -14.111 -16.487 1.00 36.62  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.213  -13.704 -17.955 1.00 34.22  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.167  -13.936 -18.570 1.00 32.97  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.064  -15.462 -16.350 1.00 35.67  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.218  -13.012 -18.495 1.00 34.12  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.246  -12.764 -19.926 1.00 32.01  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.077  -14.111 -20.619 1.00 28.11  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.738  -15.077 -20.252 1.00 30.13  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.569  -12.118 -20.325 1.00 32.49  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.649  -10.613 -20.111 1.00 34.25  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.600  -9.970  -20.044 1.00 42.55  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.766  -10.088 -20.043 1.00 38.49  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.136  -14.184 -21.559 1.00 32.40  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.940  -15.365 -22.383 1.00 30.84  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.012  -16.402 -21.758 1.00 38.66  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.751  -17.436 -22.376 1.00 32.61  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.530  -16.123 -20.541 1.00 33.53  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.668  -17.049 -19.821 1.00 36.05  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.190   -16.715 -20.060 1.00 34.06  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.827   -15.593 -20.442 1.00 32.72  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.037  -17.040 -18.334 1.00 36.09  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.334   -17.719 -19.815 1.00 38.25  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.888   -17.629 -19.984 1.00 34.65  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.310   -16.601 -19.015 1.00 31.90  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.535   -16.683 -17.816 1.00 36.35  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.247   -19.014 -19.763 1.00 41.81  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.733   -18.969 -19.955 1.00 40.85  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 6.867   -20.065 -20.684 1.00 45.92  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.571   -15.643 -19.569 1.00 35.10  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.902   -14.579 -18.845 1.00 38.82  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.611   -15.145 -18.259 1.00 44.72  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.076   -16.112 -18.804 1.00 37.30  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.564   -13.415 -19.788 1.00 40.55  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.780   -12.576 -20.221 1.00 39.13  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.485   -11.415 -21.168 1.00 39.29  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.219   -11.800 -22.591 1.00 38.82  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.779   -10.647 -23.375 1.00 40.15  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.113   -14.577 -17.130 1.00 41.78  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.808   -14.938 -16.568 1.00 39.28  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.707   -14.416 -17.482 1.00 39.03  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.945   -13.519 -18.277 1.00 44.30  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.748   -14.215 -15.206 1.00 35.79  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.163   -13.704 -14.946 1.00 41.79  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.791   -13.550 -16.327 1.00 43.66  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.545  -14.917 -17.356 1.00 39.28  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.701  -14.272 -17.985 1.00 40.20  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.859  -12.848 -17.465 1.00 43.54  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.253  -12.499 -16.443 1.00 38.49  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.897  -15.135 -17.543 1.00 38.50  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.305  -16.437 -17.073 1.00 35.44  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.902  -16.123 -16.592 1.00 35.50  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.693  -12.009 -18.132 1.00 43.64  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.074  -10.692 -17.611 1.00 45.93  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.668  -10.708 -16.204 1.00 37.20  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.418  -11.602 -15.855 1.00 41.70  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.087  -10.160 -18.646 1.00 46.00  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.516  -11.383 -19.426 1.00 43.15  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.291  -12.278 -19.456 1.00 50.06  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.288  -9.715  -15.406 1.00 40.29  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.732  -9.543  -14.030 1.00 43.93  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.237  -10.658 -13.107 1.00 38.63  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.667  -10.700 -11.961 1.00 36.62  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.235  -9.290  -13.923 1.00 50.57  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.642  -8.091  -14.744 1.00 52.68  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.649  -6.963  -14.237 1.00 47.89  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -5.904  -8.305  -16.024 1.00 51.22  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.325  -11.529 -13.573 1.00 32.40  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.800  -12.578 -12.696 1.00 29.11  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.318  -12.313 -12.420 1.00 28.42  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.348   -11.652 -13.218 1.00 29.75  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.018  -14.006 -13.207 1.00 30.50  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.479  -14.445 -13.462 1.00 36.09  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.399  -14.146 -12.284 1.00 39.36  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.869  -14.489 -12.474 1.00 44.04  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.033  -15.932 -12.671 1.00 39.52  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.154   -12.790 -11.261 1.00 23.81  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.554   -12.650 -10.872 1.00 25.10  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.180   -14.029 -10.789 1.00 23.63  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.508   -15.004 -10.425 1.00 24.43  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.710   -11.980 -9.497  1.00 23.70  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.231   -10.538 -9.498  1.00 27.69  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.132  -10.236 -9.416  1.00 31.77  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.121   -9.486  -9.619  1.00 29.22  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.585  -8.926  -9.487  1.00 33.44  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.690   -8.167  -9.653  1.00 33.33  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.333   -7.894  -9.579  1.00 36.69  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.103  -6.608  -9.631  1.00 38.54  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.497   -14.153 -11.087 1.00 23.48  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.206   -15.419 -10.895 1.00 22.97  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.513   -15.543 -9.410  1.00 23.60  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.194   -14.680 -8.842  1.00 25.98  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.499   -15.278 -11.707 1.00 22.43  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.667   -13.821 -11.965 1.00 22.84  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.378   -13.066 -11.577 1.00 25.78  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.967   -16.580 -8.777  1.00 23.14  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.146   -16.737 -7.342  1.00 21.09  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.105   -17.897 -7.124  1.00 25.56  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.838   -19.017 -7.575  1.00 25.02  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.798   -16.968 -6.634  1.00 22.97  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.800   -15.843 -6.934  1.00 21.74  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.030   -17.171 -5.130  1.00 21.67  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.316   -14.424 -6.618  1.00 20.83  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.207   -17.632 -6.402  1.00 22.24  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.090   -18.705 -5.996  1.00 22.76  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.781   -19.117 -4.554  1.00 23.50  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.844   -18.303 -3.627  1.00 23.20  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.530   -18.203 -6.184  1.00 22.80  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.568   -19.225 -5.741  1.00 24.08  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.954   -20.265 -6.597  1.00 26.46  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.105  -19.178 -4.455  1.00 25.94  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.911  -21.186 -6.194  1.00 27.34  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.045  -20.121 -4.053  1.00 29.59  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.457  -21.104 -4.931  1.00 26.55  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.431   -20.398 -4.365  1.00 24.47  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.054   -20.903 -3.049  1.00 22.37  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.333   -21.410 -2.392  1.00 25.04  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.036   -22.254 -2.990  1.00 25.97  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.049   -22.067 -3.217  1.00 26.71  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.686   -21.579 -3.691  1.00 25.10  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.425   -21.389 -5.051  1.00 27.83  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.687   -21.274 -2.770  1.00 27.54  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.196   -20.877 -5.479  1.00 29.26  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.455   -20.798 -3.200  1.00 25.92  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.215   -20.597 -4.550  1.00 28.34  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.641   -20.875 -1.198  1.00 24.11  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.772   -21.356 -0.416  1.00 26.94  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.509   -22.809 0.015   1.00 26.14  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.360   -23.246 0.180   1.00 26.73  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.151   -20.412 0.745   1.00 26.13  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.551   -18.988 0.355   1.00 24.38  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.785  -18.720 -0.245  1.00 22.45  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.723   -17.903 0.645   1.00 23.21  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.151  -17.410 -0.575  1.00 23.06  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.080   -16.592 0.288   1.00 23.39  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.306  -16.346 -0.331  1.00 24.71  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.601   -23.557 0.177   1.00 24.61  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.551   -24.926 0.658   1.00 25.89  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.322   -25.904 -0.488  1.00 32.24  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.185  -26.737 -0.742  1.00 31.89  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.195   -25.776 -1.210  1.00 29.98  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 7.916   -26.665 -2.333  1.00 32.88  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.716   -26.229 -3.548  1.00 35.26  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.063   -27.054 -4.395  1.00 34.93  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.436   -26.708 -2.685  1.00 31.62  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.142   -25.364 -3.063  1.00 33.24  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.592   -27.248 -1.552  1.00 30.29  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.965   -24.919 -3.621  1.00 28.92  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.675   -24.272 -4.711  1.00 29.56  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.902   -24.368 -6.022  1.00 31.68  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.518   -24.325 -7.085  1.00 31.68  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.125  -24.781 -4.842  1.00 30.44  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.859  -24.814 -3.554  1.00 33.63  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.632  -25.886 -3.176  1.00 34.33  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.907  -23.924 -2.527  1.00 31.24  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.152  -25.641 -1.975  1.00 41.87  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.744  -24.444 -1.574  1.00 38.18  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.568   -24.486 -5.951  1.00 34.88  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.729   -24.477 -7.141  1.00 34.61  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.262   -23.056 -7.457  1.00 32.37  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.240   -22.211 -6.569  1.00 30.74  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.503   -25.341 -6.866  1.00 35.68  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.898   -26.785 -6.589  1.00 47.51  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.765   -27.643 -6.066  1.00 54.58  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.592   -27.188 -5.953  1.00 51.24  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.116   -28.799 -5.742  1.00 62.41  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.962   -22.803 -8.738  1.00 28.88  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.387   -21.551 -9.208  1.00 31.12  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.928   -21.769 -9.614  1.00 30.84  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.608   -22.776 -10.246 1.00 32.93  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.198   -20.999 -10.384 1.00 35.00  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.477   -20.647 -9.868  1.00 30.26  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.594   -19.733 -10.977 1.00 37.24  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.058   -20.807 -9.267  1.00 28.61  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.731   -20.715 -9.852  1.00 30.18  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.429   -19.254 -10.177 1.00 30.40  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.114   -18.335 -9.721  1.00 26.81  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.671   -21.319 -8.931  1.00 31.25  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.371   -19.054 -10.960 1.00 28.81  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.032  -17.721 -11.359 1.00 28.98  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.269  -17.363 -10.555 1.00 31.97  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.258  -18.095 -10.614 1.00 34.33  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.325  -17.743 -12.860 1.00 29.86  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.902   -18.031 -13.705 1.00 34.09  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.061   -17.276 -13.549 1.00 35.28  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.890   -19.053 -14.652 1.00 37.87  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.189   -17.544 -14.317 1.00 46.90  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.019   -19.314 -15.417 1.00 39.95  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.159   -18.563 -15.253 1.00 39.59  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.196  -16.257 -9.801  1.00 27.98  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.306  -15.870 -8.946  1.00 28.74  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.591  -14.377 -9.067  1.00 28.87  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.679  -13.589 -9.326  1.00 25.90  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.943  -16.207 -7.499  1.00 28.68  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.957  -17.687 -7.121  1.00 31.25  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.478  -17.768 -5.681  1.00 31.75  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.380  -18.241 -7.222  1.00 34.67  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.862  -14.005 -8.830  1.00 25.77  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.239  -12.601 -8.739  1.00 23.68  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.227  -12.121 -7.284  1.00 22.76  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.161  -12.925 -6.348  1.00 22.56  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.280  -10.794 -7.066  1.00 23.68  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.255  -10.209 -5.719  1.00 23.90  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.214  -10.748 -4.663  1.00 25.58  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.888  -10.720 -3.480  1.00 23.37  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.471  -8.721  -5.973  1.00 25.57  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.947  -8.517  -7.359  1.00 26.10  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.281  -9.780  -8.133  1.00 24.21  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.396  -11.238 -5.082  1.00 23.42  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.342  -11.803 -4.120  1.00 24.86  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.734  -12.913 -3.264  1.00 24.65  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.194  -13.165 -2.141  1.00 23.28  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.606  -12.366 -4.790  1.00 27.50  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.437  -13.598 -5.665  1.00 32.64  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.700  -13.960 -6.457  1.00 43.61  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.571  -15.274 -7.179  1.00 46.03  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.412  -16.410 -6.254  1.00 48.01  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.715  -13.588 -3.805  1.00 25.57  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.102  -14.745 -3.189  1.00 24.79  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.764  -14.419 -2.511  1.00 24.47  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.131  -15.333 -1.980  1.00 27.53  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.034  -15.880 -4.205  1.00 26.14  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.419  -16.469 -4.432  1.00 30.18  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.184  -16.477 -3.443  1.00 28.85  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.733  -16.844 -5.573  1.00 26.05  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.392  -13.131 -2.450  1.00 23.55  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.073  -12.698 -1.985  1.00 22.42  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.215  -11.853 -0.707  1.00 20.28  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.822  -10.793 -0.737  1.00 23.42  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.431  -11.914 -3.139  1.00 21.04  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.320  -12.667 -4.468  1.00 20.53  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.651  -11.852 -5.518  1.00 21.89  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.559  -13.984 -4.297  1.00 19.98  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.700  -12.357 0.423   1.00 21.64  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.772  -11.663 1.709   1.00 23.34  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.386  -11.161 2.069   1.00 25.75  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.524   -11.961 2.292   1.00 27.29  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.226  -12.663 2.771   1.00 25.40  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.676  -13.077 2.513   1.00 23.97  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.976  -13.987 1.498   1.00 22.63  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.719  -12.537 3.260   1.00 26.26  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.297  -14.358 1.239   1.00 29.60  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.040  -12.916 3.005   1.00 27.12  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.327  -13.825 2.007   1.00 26.82  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.153  -9.841  2.146   1.00 27.69  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.168   -9.374  2.591   1.00 26.01  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.734   -9.996  3.875   1.00 26.29  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.065   -10.108 4.900   1.00 26.66  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 0.983   -7.846  2.640   1.00 28.62  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.084  -7.604  1.558   1.00 31.64  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.079  -8.757  1.759   1.00 26.44  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.010   -10.402 3.801   1.00 26.96  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.656   -11.221 4.817   1.00 27.18  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.639   -10.543 6.195   1.00 26.60  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.228   -11.177 7.164   1.00 30.94  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.072   -11.618 4.363   1.00 28.72  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.830   -12.381 5.436   1.00 28.39  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.522   -13.705 5.722   1.00 27.42  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.885   -11.789 6.137   1.00 30.24  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.203   -14.417 6.703   1.00 29.44  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.583   -12.499 7.106   1.00 28.25  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.249   -13.814 7.381   1.00 31.46  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.924   -14.522 8.344   1.00 37.03  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.117   -9.297  6.279   1.00 28.18  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.202   -8.587  7.557   1.00 32.68  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.849   -8.598  8.276   1.00 34.01  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.731   -9.113  9.385   1.00 37.26  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.779   -7.188  7.383   1.00 33.11  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.813   -8.088  7.599   1.00 34.62  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.454   -8.045  8.126   1.00 34.59  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? -0.053  -9.427  8.561   1.00 35.37  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.807  -9.514  9.533   1.00 35.11  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.495  -7.411  7.098   1.00 34.72  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.952  -7.252  7.580   1.00 39.02  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.765  -6.409  6.608   1.00 38.17  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.882  -5.664  7.284   1.00 41.97  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.870  -6.587  7.837   1.00 41.85  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.328   -10.508 7.848   1.00 31.91  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.407  -11.766 7.943   1.00 31.90  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.345   -12.824 8.745   1.00 32.34  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.230  -13.877 9.001   1.00 29.99  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.709  -12.339 6.571   1.00 33.40  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.417  -11.396 5.787   1.00 42.43  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.624   -12.571 9.083   1.00 32.07  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.477   -13.631 9.620   1.00 35.39  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 1.986   -14.199 10.957  1.00 33.98  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.111   -15.403 11.190  1.00 33.08  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 3.971   -13.287 9.645   1.00 36.16  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.421   -12.151 10.527  1.00 40.00  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 5.935   -12.125 10.382  1.00 48.19  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.576   -11.004 11.143  1.00 54.91  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.127   -9.701  10.645  1.00 63.98  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.426   -13.340 11.820  0.50 33.30  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.453   -13.338 11.834  0.50 33.48  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 0.954   -13.771 13.132  0.50 35.28  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 0.951   -13.808 13.119  0.50 35.56  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? -0.194  -14.779 12.995  0.50 35.93  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? -0.097  -14.899 12.898  0.50 35.96  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.357  -15.655 13.838  0.50 38.22  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? -0.095  -15.928 13.573  0.50 36.07  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.707   -12.592 14.068  0.50 35.52  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.413   -12.676 13.983  0.50 37.20  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 1.943   -11.791 14.460  0.50 39.05  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? -0.005  -13.093 15.386  0.50 41.41  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.069   -12.286 14.226  0.50 40.25  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.894   -13.242 16.247  0.50 38.91  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.780   -10.659 14.966  0.50 34.79  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.220  -13.318 15.592  0.50 42.32  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.966  -14.691 11.906  1.00 36.66  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -2.070  -15.606 11.675  1.00 36.22  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.623  -16.877 10.951  1.00 40.25  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -2.095  -17.980 11.246  1.00 36.81  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -3.090  -14.850 10.821  1.00 40.15  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.402  -15.576 10.620  1.00 42.17  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.406  -14.643 9.947   1.00 47.80  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.811  -15.176 9.967   1.00 52.13  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.716  -14.302 9.215   1.00 53.90  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.771  -16.717 9.935   1.00 33.70  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.586  -17.799 8.983   1.00 30.70  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 0.788   -18.437 9.164   1.00 29.69  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.042   -19.486 8.592   1.00 31.15  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.755  -17.318 7.532   1.00 29.06  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -2.153  -16.853 7.143   1.00 32.20  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.295  -17.549 7.553   1.00 35.48  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.334  -15.716 6.351   1.00 28.93  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.571  -17.133 7.180   1.00 35.12  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.600  -15.303 5.956   1.00 31.53  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.719  -16.002 6.382   1.00 33.19  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.947  -15.552 5.996   1.00 35.82  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.658   -17.796 9.944   1.00 29.68  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.054   -18.191 9.959   1.00 32.28  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.310   -19.208 11.075  1.00 35.15  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.148   -18.971 11.921  1.00 35.27  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.583   -20.328 11.053  1.00 39.76  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.686   -21.337 12.096  1.00 41.55  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 2.925   -22.690 11.435  1.00 40.10  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.524   -22.885 10.291  1.00 30.45  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.419   -21.370 12.960  1.00 40.23  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.319   -20.219 13.963  1.00 49.23  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? -0.103  -19.949 14.449  1.00 50.53  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.596   -23.650 12.123  1.00 37.26  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 3.911   -24.949 11.520  1.00 35.70  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.681   -25.648 10.962  1.00 36.30  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.576   -25.451 11.450  1.00 39.86  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.545   -25.740 12.680  1.00 40.54  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.109   -24.661 13.574  1.00 41.09  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.115   -23.506 13.496  1.00 37.81  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 2.895   -26.433 9.911   1.00 36.82  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.830   -27.126 9.217   1.00 42.26  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.394   -28.465 8.770   1.00 48.52  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.598   -28.584 8.552   1.00 50.22  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.304   -26.276 8.065   1.00 45.84  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? -0.011  -26.768 7.515   1.00 49.09  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? -0.031  -27.644 6.644   1.00 47.86  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -1.112  -26.195 7.982   1.00 50.77  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.510   -29.457 8.640   1.00 51.02  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 1.906   -30.828 8.385   1.00 49.21  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.287   -30.977 6.915   1.00 51.30  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.058   -31.872 6.556   1.00 49.28  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.760   -31.767 8.795   1.00 57.30  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.457  -31.783 7.856   1.00 56.55  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.747   -30.086 6.073   1.00 46.82  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 1.883   -30.219 4.629   1.00 46.53  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.352   -30.200 4.213   1.00 41.16  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.180   -29.495 4.804   1.00 38.83  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 0.974   -29.223 3.901   1.00 49.29  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.465  -29.540 4.272   1.00 52.52  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -1.099  -30.573 3.351   1.00 48.81  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -2.113  -29.916 2.514   1.00 66.25  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -3.260  -29.350 2.940   1.00 66.68  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -4.097  -28.830 2.055   1.00 63.53  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.585  -29.311 4.230   1.00 62.96  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.643   -30.988 3.175   1.00 38.57  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 4.999   -31.195 2.701   1.00 40.93  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.558   -29.857 2.220   1.00 38.53  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 4.922   -29.165 1.426   1.00 32.05  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 4.957   -32.189 1.539   1.00 40.30  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.223   -32.324 0.721   1.00 40.80  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.122   -33.493 -0.258  1.00 48.36  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.448   -33.883 -0.836  1.00 48.77  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.755   -29.504 2.704   1.00 35.20  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.410   -28.302 2.221   1.00 31.85  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.083   -27.066 3.060   1.00 33.68  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.801   -26.073 2.989   1.00 32.51  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.023   -27.125 3.866   1.00 31.88  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.526   -25.932 4.530   1.00 32.54  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.528   -25.341 5.527   1.00 34.93  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.765   -24.134 5.551   1.00 29.37  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.217   -26.232 5.252   1.00 30.57  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.464   -24.952 5.587   1.00 30.50  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.675   -24.288 6.791   1.00 29.62  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.517   -24.436 4.708   1.00 31.16  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 2.993   -23.110 7.086   1.00 31.77  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.832   -23.270 5.015   1.00 25.68  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.065   -22.615 6.209   1.00 27.03  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.074   -26.176 6.409   1.00 34.56  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 7.907   -25.648 7.478   1.00 33.78  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.267   -25.212 6.925   1.00 31.46  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 9.892   -24.282 7.451   1.00 29.45  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.048   -26.642 8.624   1.00 38.40  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.719   -26.950 9.275   1.00 45.01  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 5.846   -26.079 9.366   1.00 38.18  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.549   -28.177 9.745   1.00 43.52  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.729   -25.924 5.892   1.00 28.50  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 10.862  -25.442 5.123   1.00 31.50  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.529  -24.065 4.555   1.00 28.75  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.355  -23.157 4.612   1.00 28.11  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.345  -26.402 4.037   1.00 31.85  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.582  -25.898 3.296   1.00 35.51  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.213  -26.883 2.319   1.00 41.88  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.565  -27.899 2.023   1.00 44.73  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.368  -26.671 1.880   1.00 43.45  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.314   -23.914 4.026   1.00 27.57  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 8.895   -22.629 3.485   1.00 27.38  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 8.937   -21.501 4.520   1.00 25.89  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.341   -20.366 4.211   1.00 27.86  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.518   -21.803 5.749   1.00 24.80  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.539   -20.778 6.788   1.00 26.78  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 9.972   -20.316 7.051   1.00 27.17  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.206  -19.127 7.296   1.00 23.91  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 7.883   -21.234 8.087   1.00 27.57  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.398   -21.595 7.984   1.00 29.07  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.052   -22.207 9.327   1.00 29.73  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.477   -20.412 7.659   1.00 25.79  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 10.915  -21.275 7.075   1.00 26.67  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.301  -20.919 7.348   1.00 26.15  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.787  -19.989 6.242   1.00 25.81  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.444  -19.000 6.520   1.00 27.21  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.218  -22.152 7.501   1.00 27.70  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.663  -21.797 7.737   1.00 28.59  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.272  -21.617 8.947   1.00 28.12  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.652  -21.485 6.728   1.00 26.36  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.580  -21.271 8.755   1.00 28.78  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 16.832  -21.148 7.412   1.00 29.62  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.636  -21.436 5.327   1.00 27.37  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.002  -20.776 6.742   1.00 28.79  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.776  -21.045 4.657   1.00 30.49  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 17.948  -20.722 5.368   1.00 30.39  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.444  -20.308 4.993   1.00 26.43  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 12.981  -19.580 3.851   1.00 23.44  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.479  -18.136 3.855   1.00 27.67  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.244  -17.206 3.627   1.00 25.34  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.624  -20.283 2.545   1.00 22.94  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.348  -21.610 2.329   1.00 24.71  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 12.900  -22.319 1.054   1.00 29.32  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 11.977  -21.826 0.371   1.00 28.41  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.485  -23.374 0.703   1.00 31.10  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.174  -17.951 4.088   1.00 22.98  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.608  -16.625 3.990   1.00 22.13  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.161  -15.734 5.110   1.00 21.89  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.270  -14.523 4.934   1.00 23.68  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.065   -16.663 3.995   1.00 22.05  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.454   -15.288 3.598   1.00 22.44  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.545   -17.128 5.358   1.00 20.17  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.028   -15.368 3.045   1.00 21.79  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.482  -16.327 6.276   1.00 22.64  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 11.968  -15.544 7.399   1.00 24.37  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.475  -15.324 7.253   1.00 27.25  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 13.948  -14.247 7.606   1.00 30.82  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.618  -16.262 8.708   1.00 26.00  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.011  -15.535 9.992   1.00 36.06  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.388  -16.156 11.240  1.00 44.62  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.159  -17.375 11.331  1.00 44.06  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.065  -15.306 12.207  1.00 43.01  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.206  -16.319 6.710   1.00 24.89  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.668  -16.314 6.790   1.00 26.42  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.380  -15.923 5.487   1.00 27.62  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.472  -15.332 5.563   1.00 27.67  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.188  -17.535 7.556   1.00 26.97  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.661  -17.557 8.977   1.00 29.02  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 15.994  -16.684 9.791   1.00 32.30  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.740  -18.458 9.276   1.00 26.19  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 15.832  -16.272 4.297   1.00 24.78  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.499  -15.915 3.045   1.00 26.17  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.471  -15.842 1.914   1.00 23.27  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.503  -16.608 0.927   1.00 24.27  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.697  -16.830 2.744   1.00 26.92  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.759  -16.182 1.882   1.00 29.49  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.519  -15.165 1.213   1.00 26.16  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 19.946  -16.786 1.844   1.00 28.06  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.513  -14.909 2.051   1.00 23.49  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.366  -14.854 1.149   1.00 22.39  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.736  -14.427 -0.276  1.00 22.69  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 12.963  -14.667 -1.181  1.00 23.43  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.422  -13.870 1.872   1.00 20.29  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.334  -12.975 2.689   1.00 21.80  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.470  -13.881 3.115   1.00 21.83  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 14.933  -13.855 -0.491  1.00 21.07  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.289  -13.320 -1.805  1.00 23.05  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.406  -14.138 -2.470  1.00 24.44  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 16.937  -13.764 -3.530  1.00 23.40  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.650  -11.831 -1.674  1.00 23.47  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.565  -10.986 -1.085  1.00 23.95  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.293  -10.918 -1.636  1.00 21.60  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.559  -10.178 -0.008  1.00 22.79  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.552  -10.052 -0.922  1.00 20.85  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.291  -9.622  0.098   1.00 23.53  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.730  -15.295 -1.877  1.00 24.14  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.778  -16.171 -2.400  1.00 23.28  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.341  -16.854 -3.694  1.00 27.44  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.155  -17.012 -3.960  1.00 30.25  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.152  -17.221 -1.365  1.00 21.75  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.317  -17.359 -4.451  1.00 26.75  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 17.998  -18.249 -5.566  1.00 30.34  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.690  -19.653 -5.042  1.00 31.84  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.492  -20.233 -4.315  1.00 35.41  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.140  -18.307 -6.520  1.00 32.35  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 18.941  -19.396 -7.402  1.00 42.82  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.526  -20.201 -5.395  1.00 28.57  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.175  -21.538 -4.951  1.00 30.77  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.075  -22.477 -6.153  1.00 38.39  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.453  -23.532 -6.049  1.00 46.29  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 14.849  -21.572 -4.178  1.00 32.88  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 14.981  -20.983 -2.783  1.00 30.32  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.390  -21.769 -1.706  1.00 31.09  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.725  -19.634 -2.562  1.00 31.14  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.563  -21.209 -0.446  1.00 33.22  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.853  -19.080 -1.299  1.00 29.87  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.282  -19.866 -0.240  1.00 29.80  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.430  -19.322 1.007   1.00 28.38  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.650  -22.066 -7.285  1.00 46.27  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.825  -22.930 -8.443  1.00 65.85  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.518  -24.222 -7.978  1.00 80.10  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 18.727  -24.137 -7.630  1.00 84.40  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.632  -22.244 -9.532  1.00 64.98  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 17.258  -20.883 -9.694  1.00 71.24  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 16.818  -25.262 -7.936  1.00 90.48  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.798  -11.171 -41.904 1.00 74.50  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.427  -12.059 -43.038 1.00 76.77  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 36.905  -12.206 -43.074 1.00 72.01  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.290  -12.524 -42.056 1.00 66.28  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.099  -13.432 -42.895 1.00 84.87  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.177  -14.245 -44.184 1.00 98.37  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.313  -13.614 -45.440 1.00 98.92  ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 41.849  -13.450 -44.518 1.00 97.53  ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.247  -11.984 -44.240 1.00 66.07  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.794  -12.134 -44.333 1.00 63.93  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.429  -13.562 -43.928 1.00 62.56  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.222  -14.487 -44.114 1.00 57.65  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.469  -11.818 -45.806 1.00 63.91  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.683  -11.054 -46.305 1.00 58.77  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.862  -11.608 -45.525 1.00 60.45  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.248  -13.719 -43.318 1.00 57.99  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.806  -15.030 -42.865 1.00 59.80  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.430  -15.360 -43.445 1.00 54.99  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.783  -14.505 -44.063 1.00 49.01  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 32.942  -15.149 -41.345 1.00 61.68  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.345  -15.366 -40.861 1.00 71.73  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.221  -16.252 -41.456 1.00 71.54  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.003  -14.838 -39.807 1.00 62.30  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.366  -16.247 -40.783 1.00 68.87  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.252  -15.397 -39.780 1.00 67.79  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 30.998  -16.619 -43.265 1.00 48.86  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.694  -17.029 -43.756 1.00 45.97  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.682  -16.012 -43.253 1.00 44.98  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.921  -15.463 -44.047 1.00 49.62  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.354  -18.405 -43.254 1.00 48.47  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.727  -15.771 -41.933 1.00 43.39  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 27.937  -14.750 -41.252 1.00 50.55  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.814  -13.522 -40.987 1.00 46.76  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 29.963  -13.655 -40.571 1.00 48.30  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.331  -15.276 -39.939 1.00 48.57  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.223  -16.314 -40.095 1.00 41.13  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.907  -15.924 -40.334 1.00 36.32  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.498  -17.674 -40.010 1.00 40.54  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.902  -16.863 -40.496 1.00 37.00  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.491  -18.616 -40.186 1.00 34.20  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.193  -18.215 -40.409 1.00 33.24  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.247  -12.329 -41.194 1.00 49.45  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 28.970  -11.081 -40.999 1.00 47.86  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.180  -10.137 -40.084 1.00 47.64  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 26.943  -10.174 -40.044 1.00 38.40  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.242  -10.478 -42.377 1.00 47.41  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 28.004  -10.190 -43.207 1.00 51.60  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.370  -9.621  -44.572 1.00 57.92  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 27.235  -8.935  -45.268 1.00 58.30  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 26.126  -9.851  -45.555 1.00 67.88  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.870  -9.219  -39.359 1.00 48.13  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.203  -8.308  -38.423 1.00 37.49  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.069  -7.593  -39.142 1.00 36.78  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.229  -7.185  -40.293 1.00 41.65  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.373  -7.383  -38.083 1.00 44.50  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.568  -8.325  -38.087 1.00 44.55  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.324  -8.983  -39.429 1.00 47.45  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.895  -7.529  -38.494 1.00 32.63  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.726  -6.892  -39.075 1.00 30.40  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.782  -7.903  -39.722 1.00 33.09  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.656  -7.565  -40.068 1.00 31.40  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.239  -9.150  -39.895 1.00 33.93  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.374  -10.191 -40.442 1.00 32.68  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.259  -10.497 -39.441 1.00 28.52  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.511  -10.555 -38.240 1.00 29.67  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.179  -11.448 -40.724 1.00 36.29  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.884  -11.510 -42.075 1.00 43.98  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.542  -10.703 -42.959 1.00 41.59  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.755  -12.395 -42.236 1.00 42.41  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 21.027  -10.622 -39.941 1.00 28.31  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.866  -10.854 -39.101 1.00 33.98  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.515  -12.333 -39.113 1.00 31.99  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.465  -12.940 -40.177 1.00 34.51  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.692  -10.015 -39.595 1.00 30.32  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 18.974  -8.511  -39.711 1.00 30.01  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.665  -7.824  -40.075 1.00 29.15  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.514  -8.021  -38.383 1.00 28.98  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.231  -12.889 -37.932 1.00 30.94  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 18.970  -14.321 -37.834 1.00 28.28  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.847  -14.560 -36.829 1.00 30.90  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.427  -13.649 -36.107 1.00 26.63  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.252  -15.064 -37.400 1.00 31.88  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.386  -14.937 -38.425 1.00 30.46  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.711  -14.673 -35.994 1.00 30.63  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.354  -15.797 -36.793 1.00 29.74  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.837  -16.340 -35.550 1.00 27.44  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 17.922  -17.235 -34.977 1.00 27.57  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.501  -18.024 -35.740 1.00 29.41  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.626  -17.221 -35.831 1.00 28.79  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.423  -16.408 -36.254 1.00 30.84  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.185  -16.143 -37.595 1.00 32.24  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.547  -15.896 -35.303 1.00 32.19  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.091  -15.382 -37.977 1.00 34.07  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.438  -15.153 -35.691 1.00 32.34  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.223  -14.889 -37.023 1.00 36.79  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.150  -17.117 -33.651 1.00 23.50  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.191  -17.855 -32.956 1.00 27.06  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.577  -18.783 -31.905 1.00 26.07  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.641  -18.407 -31.201 1.00 29.64  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.200  -16.905 -32.365 1.00 25.31  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.080  -20.018 -31.833 1.00 27.78  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.416  -21.068 -31.058 1.00 28.56  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.271  -21.411 -29.845 1.00 28.81  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.463  -21.688 -29.985 1.00 34.56  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.167  -22.341 -31.893 1.00 30.34  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.398  -23.481 -31.167 1.00 27.25  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 15.969  -23.033 -30.831 1.00 30.69  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.047  -24.115 -30.268 1.00 27.66  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.522  -24.417 -28.916 1.00 26.91  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.680  -21.311 -28.650 1.00 30.82  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.326  -21.833 -27.455 1.00 37.67  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.404  -22.886 -26.841 1.00 35.44  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.184  -22.753 -26.925 1.00 30.31  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.509  -20.745 -26.388 1.00 43.02  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.108  -19.431 -26.853 1.00 43.96  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.741  -18.944 -26.260 1.00 46.82  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 22.046  -19.610 -24.618 1.00 48.15  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 18.994  -23.876 -26.154 1.00 35.68  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.203  -24.868 -25.432 1.00 37.71  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.285  -24.165 -24.424 1.00 33.61  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.722  -23.259 -23.718 1.00 35.80  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.141  -25.920 -24.822 1.00 44.19  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 18.469  -26.970 -23.927 1.00 45.74  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 19.481  -27.825 -23.164 1.00 50.63  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 15.999  -24.534 -24.418 1.00 35.08  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.032  -23.989 -23.477 1.00 36.66  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.229  -22.810 -24.031 1.00 37.87  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.355  -22.290 -23.341 1.00 41.52  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.498  -22.401 -25.280 1.00 34.82  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 13.902  -21.180 -25.798 1.00 31.22  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.543  -21.379 -27.266 1.00 29.21  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.208  -22.130 -27.976 1.00 32.01  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 14.854  -19.986 -25.662 1.00 32.41  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.377  -19.717 -24.257 1.00 38.95  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.735  -18.815 -23.410 1.00 41.05  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.502  -20.383 -23.771 1.00 39.40  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 15.202  -18.587 -22.122 1.00 45.63  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 16.976  -20.162 -22.488 1.00 45.29  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.327  -19.256 -21.664 1.00 47.92  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.803  -19.042 -20.407 1.00 53.74  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.500  -20.701 -27.778 1.00 28.39  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.213  -20.740 -29.215 1.00 26.68  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.316  -20.020 -30.000 1.00 28.12  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 14.007  -19.157 -29.451 1.00 25.87  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 10.891  -19.996 -29.277 1.00 25.10  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 10.996  -18.981 -28.136 1.00 28.16  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.589  -19.827 -27.017 1.00 26.11  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.489  -20.410 -31.272 1.00 26.99  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.294  -19.638 -32.226 1.00 28.56  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.007  -18.146 -32.067 1.00 25.58  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 12.874  -17.698 -32.263 1.00 25.70  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 13.964  -20.084 -33.659 1.00 28.56  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.178  -21.560 -33.841 1.00 30.72  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.238  -22.473 -33.402 1.00 29.14  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.205  -22.288 -34.343 1.00 29.49  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.665  -23.705 -33.669 1.00 31.09  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 14.861  -23.623 -34.217 1.00 28.62  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.049  -17.374 -31.760 1.00 25.99  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 14.840  -16.040 -31.219 1.00 25.85  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.380  -14.979 -32.178 1.00 26.84  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.518  -15.114 -32.627 1.00 27.30  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.582  -15.956 -29.882 1.00 26.33  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.075  -14.817 -29.045 1.00 27.40  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.349  -13.484 -29.195 1.00 29.05  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.141  -14.928 -27.948 1.00 28.25  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.664  -12.753 -28.251 1.00 29.25  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 13.921  -13.618 -27.466 1.00 29.03  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.504  -16.009 -27.319 1.00 28.05  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.070  -13.364 -26.391 1.00 27.55  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.669  -15.761 -26.246 1.00 27.04  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.436  -14.445 -25.811 1.00 27.12  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.626  -13.899 -32.504 1.00 26.44  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.131  -12.841 -33.395 1.00 26.97  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.434  -12.254 -32.849 1.00 28.28  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.540  -11.880 -31.680 1.00 29.51  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 13.964  -11.818 -33.465 1.00 27.95  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.117  -12.127 -32.236 1.00 29.02  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.244  -13.638 -32.068 1.00 27.16  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.469  -12.227 -33.689 1.00 27.49  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.795  -11.860 -33.224 1.00 24.19  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.617  -11.264 -34.366 1.00 25.44  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.164  -11.213 -35.506 1.00 28.47  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.505  -13.039 -32.604 1.00 25.54  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.825  -10.800 -34.016 1.00 28.15  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.738  -10.266 -35.010 1.00 29.76  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.142  -10.730 -34.658 1.00 28.39  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.423  -11.030 -33.497 1.00 30.74  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.674  -8.740  -35.110 1.00 29.36  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.404  -8.013  -33.986 1.00 33.93  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.116  -6.504  -34.049 1.00 35.25  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.732  -5.724  -32.971 1.00 32.55  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.386  -4.475  -32.647 1.00 32.82  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.420  -3.853  -33.313 1.00 28.73  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.040  -3.864  -31.684 1.00 29.49  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.000  -10.787 -35.691 1.00 30.88  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.437  -10.958 -35.516 1.00 30.73  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.009  -9.581  -35.192 1.00 34.04  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.820  -8.644  -35.966 1.00 37.00  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.102  -11.482 -36.800 1.00 32.84  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.348  -12.670 -37.405 1.00 32.38  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.588  -11.775 -36.566 1.00 34.94  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.349  -13.914 -36.540 1.00 30.04  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.723  -9.500  -34.073 1.00 35.50  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.445  -8.306  -33.658 1.00 45.73  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.933  -8.404  -34.021 1.00 53.96  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.463  -9.503  -34.175 1.00 49.66  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.336  -8.155  -32.149 1.00 40.28  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.102  -7.432  -31.625 1.00 41.24  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.331  -6.876  -32.451 1.00 38.49  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 25.946  -7.392  -30.384 1.00 38.23  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.597  -7.240  -34.122 0.50 60.70  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.594  -7.238  -34.119 0.50 60.04  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 31.044  -7.131  -34.278 0.50 62.56  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 31.041  -7.124  -34.246 0.50 61.53  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.740  -7.380  -32.939 0.50 65.71  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.716  -7.506  -32.933 0.50 65.27  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 31.115  -7.259  -31.886 0.50 64.51  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.064  -7.570  -31.893 0.50 64.19  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.415  -5.769  -34.894 0.50 60.02  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.465  -5.692  -34.525 0.50 57.98  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.295  -4.717  -34.736 0.50 59.46  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 31.314  -5.230  -35.963 0.50 56.44  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 29.946  -4.078  -35.763 0.50 59.73  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 32.103  -5.699  -36.809 0.50 50.53  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.767  -4.564  -33.599 0.50 60.52  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 30.409  -4.409  -36.218 0.50 60.04  ? 27  ASP B OD2 1 
ATOM   980  N N   . ILE B 1 29 ? 33.035  -7.732  -32.999 1.00 72.85  ? 28  ILE B N   1 
ATOM   981  C CA  . ILE B 1 29 ? 33.844  -8.007  -31.816 1.00 72.90  ? 28  ILE B CA  1 
ATOM   982  C C   . ILE B 1 29 ? 34.783  -6.812  -31.580 1.00 77.95  ? 28  ILE B C   1 
ATOM   983  O O   . ILE B 1 29 ? 34.360  -5.884  -30.852 1.00 78.40  ? 28  ILE B O   1 
ATOM   984  C CB  . ILE B 1 29 ? 34.630  -9.324  -31.961 1.00 68.75  ? 28  ILE B CB  1 
ATOM   985  N N   . VAL B 1 34 ? 36.164  -9.894  -24.424 1.00 78.37  ? 33  VAL B N   1 
ATOM   986  C CA  . VAL B 1 34 ? 36.334  -11.322 -24.828 1.00 75.15  ? 33  VAL B CA  1 
ATOM   987  C C   . VAL B 1 34 ? 36.509  -11.362 -26.344 1.00 75.57  ? 33  VAL B C   1 
ATOM   988  O O   . VAL B 1 34 ? 36.507  -10.319 -26.992 1.00 84.09  ? 33  VAL B O   1 
ATOM   989  C CB  . VAL B 1 34 ? 35.053  -12.048 -24.373 1.00 73.85  ? 33  VAL B CB  1 
ATOM   990  C CG1 . VAL B 1 34 ? 33.828  -11.559 -25.140 1.00 75.95  ? 33  VAL B CG1 1 
ATOM   991  C CG2 . VAL B 1 34 ? 35.174  -13.566 -24.448 1.00 65.68  ? 33  VAL B CG2 1 
ATOM   992  N N   . LYS B 1 35 ? 36.709  -12.565 -26.892 1.00 77.50  ? 34  LYS B N   1 
ATOM   993  C CA  . LYS B 1 35 ? 36.461  -12.854 -28.300 1.00 74.72  ? 34  LYS B CA  1 
ATOM   994  C C   . LYS B 1 35 ? 35.663  -14.159 -28.384 1.00 73.02  ? 34  LYS B C   1 
ATOM   995  O O   . LYS B 1 35 ? 35.746  -14.997 -27.478 1.00 70.47  ? 34  LYS B O   1 
ATOM   996  C CB  . LYS B 1 35 ? 37.751  -12.872 -29.134 1.00 68.14  ? 34  LYS B CB  1 
ATOM   997  N N   . PRO B 1 36 ? 34.851  -14.382 -29.450 1.00 68.02  ? 35  PRO B N   1 
ATOM   998  C CA  . PRO B 1 36 ? 34.066  -15.618 -29.559 1.00 58.40  ? 35  PRO B CA  1 
ATOM   999  C C   . PRO B 1 36 ? 35.014  -16.810 -29.566 1.00 52.51  ? 35  PRO B C   1 
ATOM   1000 O O   . PRO B 1 36 ? 36.115  -16.699 -30.098 1.00 54.26  ? 35  PRO B O   1 
ATOM   1001 C CB  . PRO B 1 36 ? 33.311  -15.455 -30.892 1.00 57.27  ? 35  PRO B CB  1 
ATOM   1002 C CG  . PRO B 1 36 ? 34.136  -14.446 -31.675 1.00 62.91  ? 35  PRO B CG  1 
ATOM   1003 C CD  . PRO B 1 36 ? 34.668  -13.489 -30.610 1.00 65.20  ? 35  PRO B CD  1 
ATOM   1004 N N   . PRO B 1 37 ? 34.650  -17.965 -28.958 1.00 51.22  ? 36  PRO B N   1 
ATOM   1005 C CA  . PRO B 1 37 ? 35.455  -19.175 -29.100 1.00 54.25  ? 36  PRO B CA  1 
ATOM   1006 C C   . PRO B 1 37 ? 35.469  -19.505 -30.593 1.00 60.81  ? 36  PRO B C   1 
ATOM   1007 O O   . PRO B 1 37 ? 34.647  -18.989 -31.356 1.00 54.57  ? 36  PRO B O   1 
ATOM   1008 C CB  . PRO B 1 37 ? 34.732  -20.256 -28.269 1.00 53.25  ? 36  PRO B CB  1 
ATOM   1009 C CG  . PRO B 1 37 ? 33.688  -19.511 -27.452 1.00 53.98  ? 36  PRO B CG  1 
ATOM   1010 C CD  . PRO B 1 37 ? 33.456  -18.167 -28.121 1.00 51.17  ? 36  PRO B CD  1 
ATOM   1011 N N   . PRO B 1 38 ? 36.386  -20.380 -31.069 1.00 64.51  ? 37  PRO B N   1 
ATOM   1012 C CA  . PRO B 1 38 ? 36.442  -20.714 -32.496 1.00 65.65  ? 37  PRO B CA  1 
ATOM   1013 C C   . PRO B 1 38 ? 35.128  -21.308 -33.014 1.00 58.53  ? 37  PRO B C   1 
ATOM   1014 O O   . PRO B 1 38 ? 34.467  -22.073 -32.312 1.00 57.00  ? 37  PRO B O   1 
ATOM   1015 C CB  . PRO B 1 38 ? 37.626  -21.703 -32.603 1.00 70.22  ? 37  PRO B CB  1 
ATOM   1016 C CG  . PRO B 1 38 ? 38.413  -21.514 -31.310 1.00 67.98  ? 37  PRO B CG  1 
ATOM   1017 C CD  . PRO B 1 38 ? 37.394  -21.092 -30.262 1.00 72.18  ? 37  PRO B CD  1 
ATOM   1018 N N   . ASN B 1 39 ? 34.754  -20.922 -34.242 1.00 54.02  ? 38  ASN B N   1 
ATOM   1019 C CA  . ASN B 1 39 ? 33.550  -21.395 -34.919 1.00 52.80  ? 38  ASN B CA  1 
ATOM   1020 C C   . ASN B 1 39 ? 32.297  -20.608 -34.527 1.00 49.38  ? 38  ASN B C   1 
ATOM   1021 O O   . ASN B 1 39 ? 31.281  -20.752 -35.193 1.00 45.90  ? 38  ASN B O   1 
ATOM   1022 C CB  . ASN B 1 39 ? 33.262  -22.877 -34.685 1.00 51.53  ? 38  ASN B CB  1 
ATOM   1023 C CG  . ASN B 1 39 ? 34.402  -23.770 -35.103 1.00 61.57  ? 38  ASN B CG  1 
ATOM   1024 O OD1 . ASN B 1 39 ? 34.722  -24.731 -34.392 1.00 69.02  ? 38  ASN B OD1 1 
ATOM   1025 N ND2 . ASN B 1 39 ? 35.022  -23.475 -36.239 1.00 59.94  ? 38  ASN B ND2 1 
ATOM   1026 N N   . LYS B 1 40 ? 32.355  -19.797 -33.457 1.00 49.27  ? 39  LYS B N   1 
ATOM   1027 C CA  . LYS B 1 40 ? 31.148  -19.191 -32.914 1.00 47.48  ? 39  LYS B CA  1 
ATOM   1028 C C   . LYS B 1 40 ? 31.098  -17.698 -33.221 1.00 46.77  ? 39  LYS B C   1 
ATOM   1029 O O   . LYS B 1 40 ? 32.104  -17.091 -33.561 1.00 42.16  ? 39  LYS B O   1 
ATOM   1030 C CB  . LYS B 1 40 ? 31.011  -19.544 -31.432 1.00 48.24  ? 39  LYS B CB  1 
ATOM   1031 C CG  . LYS B 1 40 ? 30.988  -21.048 -31.185 1.00 49.19  ? 39  LYS B CG  1 
ATOM   1032 C CD  . LYS B 1 40 ? 31.118  -21.413 -29.713 1.00 56.67  ? 39  LYS B CD  1 
ATOM   1033 C CE  . LYS B 1 40 ? 29.851  -21.510 -28.910 1.00 62.98  ? 39  LYS B CE  1 
ATOM   1034 N NZ  . LYS B 1 40 ? 29.347  -22.885 -28.844 1.00 63.80  ? 39  LYS B NZ  1 
ATOM   1035 N N   . TYR B 1 41 ? 29.900  -17.121 -33.126 1.00 47.12  ? 40  TYR B N   1 
ATOM   1036 C CA  . TYR B 1 41 ? 29.733  -15.702 -33.388 1.00 43.09  ? 40  TYR B CA  1 
ATOM   1037 C C   . TYR B 1 41 ? 29.168  -14.993 -32.157 1.00 43.76  ? 40  TYR B C   1 
ATOM   1038 O O   . TYR B 1 41 ? 28.432  -15.589 -31.378 1.00 40.49  ? 40  TYR B O   1 
ATOM   1039 C CB  . TYR B 1 41 ? 28.768  -15.542 -34.564 1.00 42.59  ? 40  TYR B CB  1 
ATOM   1040 C CG  . TYR B 1 41 ? 29.296  -15.996 -35.916 1.00 44.42  ? 40  TYR B CG  1 
ATOM   1041 C CD1 . TYR B 1 41 ? 29.934  -15.096 -36.763 1.00 43.04  ? 40  TYR B CD1 1 
ATOM   1042 C CD2 . TYR B 1 41 ? 29.134  -17.307 -36.352 1.00 44.99  ? 40  TYR B CD2 1 
ATOM   1043 C CE1 . TYR B 1 41 ? 30.424  -15.494 -37.999 1.00 46.45  ? 40  TYR B CE1 1 
ATOM   1044 C CE2 . TYR B 1 41 ? 29.607  -17.712 -37.592 1.00 47.74  ? 40  TYR B CE2 1 
ATOM   1045 C CZ  . TYR B 1 41 ? 30.262  -16.804 -38.414 1.00 47.15  ? 40  TYR B CZ  1 
ATOM   1046 O OH  . TYR B 1 41 ? 30.743  -17.174 -39.640 1.00 46.62  ? 40  TYR B OH  1 
ATOM   1047 N N   . PRO B 1 42 ? 29.437  -13.674 -31.996 1.00 41.65  ? 41  PRO B N   1 
ATOM   1048 C CA  . PRO B 1 42 ? 28.727  -12.860 -31.013 1.00 37.99  ? 41  PRO B CA  1 
ATOM   1049 C C   . PRO B 1 42 ? 27.304  -12.609 -31.496 1.00 35.40  ? 41  PRO B C   1 
ATOM   1050 O O   . PRO B 1 42 ? 27.097  -11.959 -32.527 1.00 38.81  ? 41  PRO B O   1 
ATOM   1051 C CB  . PRO B 1 42 ? 29.548  -11.549 -30.922 1.00 40.34  ? 41  PRO B CB  1 
ATOM   1052 C CG  . PRO B 1 42 ? 30.376  -11.495 -32.198 1.00 40.70  ? 41  PRO B CG  1 
ATOM   1053 C CD  . PRO B 1 42 ? 30.415  -12.897 -32.782 1.00 40.93  ? 41  PRO B CD  1 
ATOM   1054 N N   . ILE B 1 43 ? 26.333  -13.117 -30.720 1.00 31.74  ? 42  ILE B N   1 
ATOM   1055 C CA  . ILE B 1 43 ? 24.918  -12.922 -31.009 1.00 30.64  ? 42  ILE B CA  1 
ATOM   1056 C C   . ILE B 1 43 ? 24.310  -11.886 -30.068 1.00 29.60  ? 42  ILE B C   1 
ATOM   1057 O O   . ILE B 1 43 ? 24.556  -11.931 -28.873 1.00 33.57  ? 42  ILE B O   1 
ATOM   1058 C CB  . ILE B 1 43 ? 24.157  -14.250 -30.874 1.00 27.16  ? 42  ILE B CB  1 
ATOM   1059 C CG1 . ILE B 1 43 ? 24.807  -15.352 -31.749 1.00 30.12  ? 42  ILE B CG1 1 
ATOM   1060 C CG2 . ILE B 1 43 ? 22.689  -14.034 -31.230 1.00 28.87  ? 42  ILE B CG2 1 
ATOM   1061 C CD1 . ILE B 1 43 ? 25.142  -14.907 -33.162 1.00 27.92  ? 42  ILE B CD1 1 
ATOM   1062 N N   . PHE B 1 44 ? 23.453  -11.025 -30.625 1.00 31.97  ? 43  PHE B N   1 
ATOM   1063 C CA  . PHE B 1 44 ? 22.654  -10.088 -29.850 1.00 32.69  ? 43  PHE B CA  1 
ATOM   1064 C C   . PHE B 1 44 ? 21.180  -10.458 -29.999 1.00 30.25  ? 43  PHE B C   1 
ATOM   1065 O O   . PHE B 1 44 ? 20.638  -10.443 -31.108 1.00 30.29  ? 43  PHE B O   1 
ATOM   1066 C CB  . PHE B 1 44 ? 22.919  -8.626  -30.250 1.00 29.47  ? 43  PHE B CB  1 
ATOM   1067 C CG  . PHE B 1 44 ? 22.007  -7.602  -29.579 1.00 29.75  ? 43  PHE B CG  1 
ATOM   1068 C CD1 . PHE B 1 44 ? 20.823  -7.190  -30.191 1.00 29.98  ? 43  PHE B CD1 1 
ATOM   1069 C CD2 . PHE B 1 44 ? 22.337  -7.039  -28.342 1.00 36.70  ? 43  PHE B CD2 1 
ATOM   1070 C CE1 . PHE B 1 44 ? 20.002  -6.229  -29.591 1.00 34.88  ? 43  PHE B CE1 1 
ATOM   1071 C CE2 . PHE B 1 44 ? 21.517  -6.078  -27.739 1.00 29.63  ? 43  PHE B CE2 1 
ATOM   1072 C CZ  . PHE B 1 44 ? 20.349  -5.685  -28.366 1.00 35.02  ? 43  PHE B CZ  1 
ATOM   1073 N N   . PHE B 1 45 ? 20.522  -10.787 -28.870 1.00 29.51  ? 44  PHE B N   1 
ATOM   1074 C CA  . PHE B 1 45 ? 19.104  -11.110 -28.930 1.00 26.87  ? 44  PHE B CA  1 
ATOM   1075 C C   . PHE B 1 45 ? 18.263  -9.842  -28.855 1.00 27.40  ? 44  PHE B C   1 
ATOM   1076 O O   . PHE B 1 45 ? 18.298  -9.130  -27.854 1.00 29.11  ? 44  PHE B O   1 
ATOM   1077 C CB  . PHE B 1 45 ? 18.693  -12.078 -27.809 1.00 28.81  ? 44  PHE B CB  1 
ATOM   1078 C CG  . PHE B 1 45 ? 19.422  -13.413 -27.896 1.00 28.98  ? 44  PHE B CG  1 
ATOM   1079 C CD1 . PHE B 1 45 ? 20.571  -13.654 -27.158 1.00 33.43  ? 44  PHE B CD1 1 
ATOM   1080 C CD2 . PHE B 1 45 ? 18.956  -14.423 -28.736 1.00 29.48  ? 44  PHE B CD2 1 
ATOM   1081 C CE1 . PHE B 1 45 ? 21.225  -14.876 -27.236 1.00 37.00  ? 44  PHE B CE1 1 
ATOM   1082 C CE2 . PHE B 1 45 ? 19.606  -15.653 -28.806 1.00 33.88  ? 44  PHE B CE2 1 
ATOM   1083 C CZ  . PHE B 1 45 ? 20.748  -15.871 -28.074 1.00 34.33  ? 44  PHE B CZ  1 
ATOM   1084 N N   . PHE B 1 46 ? 17.400  -9.623  -29.853 1.00 27.83  ? 45  PHE B N   1 
ATOM   1085 C CA  . PHE B 1 46 ? 16.465  -8.509  -29.771 1.00 28.40  ? 45  PHE B CA  1 
ATOM   1086 C C   . PHE B 1 46 ? 15.430  -8.732  -28.653 1.00 32.75  ? 45  PHE B C   1 
ATOM   1087 O O   . PHE B 1 46 ? 15.169  -9.862  -28.238 1.00 28.22  ? 45  PHE B O   1 
ATOM   1088 C CB  . PHE B 1 46 ? 15.769  -8.288  -31.105 1.00 26.98  ? 45  PHE B CB  1 
ATOM   1089 C CG  . PHE B 1 46 ? 16.715  -7.854  -32.218 1.00 32.42  ? 45  PHE B CG  1 
ATOM   1090 C CD1 . PHE B 1 46 ? 17.160  -6.530  -32.297 1.00 35.19  ? 45  PHE B CD1 1 
ATOM   1091 C CD2 . PHE B 1 46 ? 17.081  -8.740  -33.239 1.00 30.72  ? 45  PHE B CD2 1 
ATOM   1092 C CE1 . PHE B 1 46 ? 17.993  -6.117  -33.337 1.00 32.18  ? 45  PHE B CE1 1 
ATOM   1093 C CE2 . PHE B 1 46 ? 17.923  -8.326  -34.277 1.00 30.62  ? 45  PHE B CE2 1 
ATOM   1094 C CZ  . PHE B 1 46 ? 18.367  -7.008  -34.322 1.00 29.11  ? 45  PHE B CZ  1 
ATOM   1095 N N   . GLY B 1 47 ? 14.853  -7.625  -28.158 1.00 33.11  ? 46  GLY B N   1 
ATOM   1096 C CA  . GLY B 1 47 ? 13.845  -7.646  -27.106 1.00 32.66  ? 46  GLY B CA  1 
ATOM   1097 C C   . GLY B 1 47 ? 14.498  -7.730  -25.731 1.00 32.73  ? 46  GLY B C   1 
ATOM   1098 O O   . GLY B 1 47 ? 14.362  -6.817  -24.924 1.00 33.61  ? 46  GLY B O   1 
ATOM   1099 N N   . THR B 1 48 ? 15.211  -8.821  -25.461 1.00 30.85  ? 47  THR B N   1 
ATOM   1100 C CA  . THR B 1 48 ? 15.862  -8.968  -24.172 1.00 31.26  ? 47  THR B CA  1 
ATOM   1101 C C   . THR B 1 48 ? 17.190  -8.220  -24.178 1.00 34.15  ? 47  THR B C   1 
ATOM   1102 O O   . THR B 1 48 ? 17.699  -7.878  -23.120 1.00 33.93  ? 47  THR B O   1 
ATOM   1103 C CB  . THR B 1 48 ? 16.089  -10.439 -23.821 1.00 30.61  ? 47  THR B CB  1 
ATOM   1104 O OG1 . THR B 1 48 ? 17.071  -10.932 -24.732 1.00 27.42  ? 47  THR B OG1 1 
ATOM   1105 C CG2 . THR B 1 48 ? 14.803  -11.252 -23.817 1.00 32.02  ? 47  THR B CG2 1 
ATOM   1106 N N   . HIS B 1 49 ? 17.791  -8.073  -25.363 1.00 31.04  ? 48  HIS B N   1 
ATOM   1107 C CA  . HIS B 1 49 ? 19.059  -7.377  -25.520 1.00 34.76  ? 48  HIS B CA  1 
ATOM   1108 C C   . HIS B 1 49 ? 20.163  -8.106  -24.775 1.00 35.48  ? 48  HIS B C   1 
ATOM   1109 O O   . HIS B 1 49 ? 21.135  -7.458  -24.390 1.00 38.29  ? 48  HIS B O   1 
ATOM   1110 C CB  . HIS B 1 49 ? 19.002  -5.907  -25.050 1.00 34.27  ? 48  HIS B CB  1 
ATOM   1111 C CG  . HIS B 1 49 ? 17.868  -5.148  -25.641 1.00 32.95  ? 48  HIS B CG  1 
ATOM   1112 N ND1 . HIS B 1 49 ? 17.085  -4.308  -24.881 1.00 35.63  ? 48  HIS B ND1 1 
ATOM   1113 C CD2 . HIS B 1 49 ? 17.323  -5.148  -26.878 1.00 32.42  ? 48  HIS B CD2 1 
ATOM   1114 C CE1 . HIS B 1 49 ? 16.123  -3.795  -25.645 1.00 39.90  ? 48  HIS B CE1 1 
ATOM   1115 N NE2 . HIS B 1 49 ? 16.237  -4.304  -26.862 1.00 36.89  ? 48  HIS B NE2 1 
ATOM   1116 N N   . GLU B 1 50 ? 20.024  -9.431  -24.593 1.00 31.90  ? 49  GLU B N   1 
ATOM   1117 C CA  . GLU B 1 50 ? 21.096  -10.245 -24.034 1.00 35.96  ? 49  GLU B CA  1 
ATOM   1118 C C   . GLU B 1 50 ? 22.024  -10.710 -25.153 1.00 34.82  ? 49  GLU B C   1 
ATOM   1119 O O   . GLU B 1 50 ? 21.709  -10.505 -26.320 1.00 32.21  ? 49  GLU B O   1 
ATOM   1120 C CB  . GLU B 1 50 ? 20.539  -11.442 -23.270 1.00 41.22  ? 49  GLU B CB  1 
ATOM   1121 C CG  . GLU B 1 50 ? 19.939  -11.001 -21.939 1.00 46.29  ? 49  GLU B CG  1 
ATOM   1122 C CD  . GLU B 1 50 ? 19.757  -12.097 -20.906 1.00 52.56  ? 49  GLU B CD  1 
ATOM   1123 O OE1 . GLU B 1 50 ? 19.041  -11.838 -19.916 1.00 58.87  ? 49  GLU B OE1 1 
ATOM   1124 O OE2 . GLU B 1 50 ? 20.337  -13.190 -21.063 1.00 56.14  ? 49  GLU B OE2 1 
ATOM   1125 N N   . THR B 1 51 ? 23.170  -11.301 -24.789 1.00 32.95  ? 50  THR B N   1 
ATOM   1126 C CA  . THR B 1 51 ? 24.155  -11.749 -25.765 1.00 34.82  ? 50  THR B CA  1 
ATOM   1127 C C   . THR B 1 51 ? 24.531  -13.197 -25.458 1.00 39.23  ? 50  THR B C   1 
ATOM   1128 O O   . THR B 1 51 ? 24.260  -13.698 -24.375 1.00 37.86  ? 50  THR B O   1 
ATOM   1129 C CB  . THR B 1 51 ? 25.382  -10.824 -25.831 1.00 39.38  ? 50  THR B CB  1 
ATOM   1130 O OG1 . THR B 1 51 ? 25.993  -10.858 -24.548 1.00 40.83  ? 50  THR B OG1 1 
ATOM   1131 C CG2 . THR B 1 51 ? 25.055  -9.365  -26.103 1.00 36.51  ? 50  THR B CG2 1 
ATOM   1132 N N   . ALA B 1 52 ? 25.115  -13.885 -26.447 1.00 38.26  ? 51  ALA B N   1 
ATOM   1133 C CA  . ALA B 1 52 ? 25.679  -15.210 -26.250 1.00 40.43  ? 51  ALA B CA  1 
ATOM   1134 C C   . ALA B 1 52 ? 26.645  -15.474 -27.396 1.00 39.74  ? 51  ALA B C   1 
ATOM   1135 O O   . ALA B 1 52 ? 26.679  -14.696 -28.355 1.00 43.02  ? 51  ALA B O   1 
ATOM   1136 C CB  . ALA B 1 52 ? 24.594  -16.262 -26.206 1.00 36.37  ? 51  ALA B CB  1 
ATOM   1137 N N   . PHE B 1 53 ? 27.404  -16.568 -27.276 1.00 35.86  ? 52  PHE B N   1 
ATOM   1138 C CA  . PHE B 1 53 ? 28.205  -17.067 -28.383 1.00 45.04  ? 52  PHE B CA  1 
ATOM   1139 C C   . PHE B 1 53 ? 27.557  -18.330 -28.956 1.00 45.75  ? 52  PHE B C   1 
ATOM   1140 O O   . PHE B 1 53 ? 27.368  -19.328 -28.251 1.00 42.30  ? 52  PHE B O   1 
ATOM   1141 C CB  . PHE B 1 53 ? 29.665  -17.351 -28.010 1.00 46.30  ? 52  PHE B CB  1 
ATOM   1142 C CG  . PHE B 1 53 ? 30.427  -16.124 -27.539 1.00 47.09  ? 52  PHE B CG  1 
ATOM   1143 C CD1 . PHE B 1 53 ? 30.682  -15.076 -28.412 1.00 49.77  ? 52  PHE B CD1 1 
ATOM   1144 C CD2 . PHE B 1 53 ? 30.895  -16.031 -26.231 1.00 48.99  ? 52  PHE B CD2 1 
ATOM   1145 C CE1 . PHE B 1 53 ? 31.363  -13.948 -27.978 1.00 52.08  ? 52  PHE B CE1 1 
ATOM   1146 C CE2 . PHE B 1 53 ? 31.569  -14.896 -25.800 1.00 50.90  ? 52  PHE B CE2 1 
ATOM   1147 C CZ  . PHE B 1 53 ? 31.801  -13.860 -26.672 1.00 47.78  ? 52  PHE B CZ  1 
ATOM   1148 N N   . LEU B 1 54 ? 27.266  -18.289 -30.261 1.00 38.62  ? 53  LEU B N   1 
ATOM   1149 C CA  . LEU B 1 54 ? 26.611  -19.413 -30.914 1.00 39.31  ? 53  LEU B CA  1 
ATOM   1150 C C   . LEU B 1 54 ? 27.330  -19.755 -32.214 1.00 38.04  ? 53  LEU B C   1 
ATOM   1151 O O   . LEU B 1 54 ? 27.883  -18.873 -32.878 1.00 37.48  ? 53  LEU B O   1 
ATOM   1152 C CB  . LEU B 1 54 ? 25.136  -19.131 -31.194 1.00 36.48  ? 53  LEU B CB  1 
ATOM   1153 C CG  . LEU B 1 54 ? 24.203  -19.075 -29.982 1.00 36.87  ? 53  LEU B CG  1 
ATOM   1154 C CD1 . LEU B 1 54 ? 22.871  -18.587 -30.503 1.00 36.94  ? 53  LEU B CD1 1 
ATOM   1155 C CD2 . LEU B 1 54 ? 24.051  -20.459 -29.329 1.00 33.72  ? 53  LEU B CD2 1 
ATOM   1156 N N   . GLY B 1 55 ? 27.226  -21.034 -32.587 1.00 35.88  ? 54  GLY B N   1 
ATOM   1157 C CA  . GLY B 1 55 ? 27.754  -21.551 -33.831 1.00 33.50  ? 54  GLY B CA  1 
ATOM   1158 C C   . GLY B 1 55 ? 26.666  -21.616 -34.899 1.00 33.33  ? 54  GLY B C   1 
ATOM   1159 O O   . GLY B 1 55 ? 25.469  -21.520 -34.607 1.00 35.14  ? 54  GLY B O   1 
ATOM   1160 N N   . PRO B 1 56 ? 27.063  -21.810 -36.177 1.00 32.79  ? 55  PRO B N   1 
ATOM   1161 C CA  . PRO B 1 56 ? 26.121  -21.838 -37.295 1.00 30.33  ? 55  PRO B CA  1 
ATOM   1162 C C   . PRO B 1 56 ? 24.922  -22.771 -37.180 1.00 28.27  ? 55  PRO B C   1 
ATOM   1163 O O   . PRO B 1 56 ? 23.873  -22.469 -37.732 1.00 28.59  ? 55  PRO B O   1 
ATOM   1164 C CB  . PRO B 1 56 ? 26.980  -22.208 -38.515 1.00 33.05  ? 55  PRO B CB  1 
ATOM   1165 C CG  . PRO B 1 56 ? 28.398  -21.963 -38.098 1.00 33.65  ? 55  PRO B CG  1 
ATOM   1166 C CD  . PRO B 1 56 ? 28.449  -22.061 -36.589 1.00 33.93  ? 55  PRO B CD  1 
ATOM   1167 N N   . LYS B 1 57 ? 25.075  -23.909 -36.487 1.00 31.87  ? 56  LYS B N   1 
ATOM   1168 C CA  . LYS B 1 57 ? 24.007  -24.902 -36.443 1.00 33.11  ? 56  LYS B CA  1 
ATOM   1169 C C   . LYS B 1 57 ? 22.785  -24.293 -35.764 1.00 31.87  ? 56  LYS B C   1 
ATOM   1170 O O   . LYS B 1 57 ? 21.653  -24.752 -35.954 1.00 29.78  ? 56  LYS B O   1 
ATOM   1171 C CB  . LYS B 1 57 ? 24.396  -26.189 -35.701 1.00 37.03  ? 56  LYS B CB  1 
ATOM   1172 C CG  . LYS B 1 57 ? 24.655  -26.088 -34.212 1.00 38.98  ? 56  LYS B CG  1 
ATOM   1173 C CD  . LYS B 1 57 ? 24.744  -27.474 -33.581 1.00 37.57  ? 56  LYS B CD  1 
ATOM   1174 C CE  . LYS B 1 57 ? 25.134  -27.443 -32.129 1.00 45.41  ? 56  LYS B CE  1 
ATOM   1175 N NZ  . LYS B 1 57 ? 24.153  -26.845 -31.219 1.00 47.80  ? 56  LYS B NZ  1 
ATOM   1176 N N   . ASP B 1 58 ? 23.042  -23.254 -34.966 1.00 31.21  ? 57  ASP B N   1 
ATOM   1177 C CA  . ASP B 1 58 ? 21.981  -22.618 -34.200 1.00 32.06  ? 57  ASP B CA  1 
ATOM   1178 C C   . ASP B 1 58 ? 21.596  -21.259 -34.774 1.00 30.36  ? 57  ASP B C   1 
ATOM   1179 O O   . ASP B 1 58 ? 20.850  -20.517 -34.113 1.00 30.07  ? 57  ASP B O   1 
ATOM   1180 C CB  . ASP B 1 58 ? 22.353  -22.504 -32.732 1.00 31.60  ? 57  ASP B CB  1 
ATOM   1181 C CG  . ASP B 1 58 ? 22.446  -23.837 -32.009 1.00 36.54  ? 57  ASP B CG  1 
ATOM   1182 O OD1 . ASP B 1 58 ? 21.470  -24.610 -32.097 1.00 32.54  ? 57  ASP B OD1 1 
ATOM   1183 O OD2 . ASP B 1 58 ? 23.480  -24.062 -31.352 1.00 41.00  ? 57  ASP B OD2 1 
ATOM   1184 N N   . LEU B 1 59 ? 22.063  -20.951 -35.998 1.00 29.13  ? 58  LEU B N   1 
ATOM   1185 C CA  . LEU B 1 59 ? 21.798  -19.642 -36.594 1.00 27.05  ? 58  LEU B CA  1 
ATOM   1186 C C   . LEU B 1 59 ? 21.055  -19.803 -37.911 1.00 27.48  ? 58  LEU B C   1 
ATOM   1187 O O   . LEU B 1 59 ? 21.512  -20.504 -38.808 1.00 31.11  ? 58  LEU B O   1 
ATOM   1188 C CB  . LEU B 1 59 ? 23.130  -18.913 -36.787 1.00 29.25  ? 58  LEU B CB  1 
ATOM   1189 C CG  . LEU B 1 59 ? 23.927  -18.686 -35.505 1.00 29.48  ? 58  LEU B CG  1 
ATOM   1190 C CD1 . LEU B 1 59 ? 25.258  -17.986 -35.790 1.00 32.06  ? 58  LEU B CD1 1 
ATOM   1191 C CD2 . LEU B 1 59 ? 23.070  -17.865 -34.549 1.00 30.41  ? 58  LEU B CD2 1 
ATOM   1192 N N   . PHE B 1 60 ? 19.893  -19.178 -37.994 1.00 27.82  ? 59  PHE B N   1 
ATOM   1193 C CA  . PHE B 1 60 ? 18.980  -19.349 -39.105 1.00 27.85  ? 59  PHE B CA  1 
ATOM   1194 C C   . PHE B 1 60 ? 18.770  -17.989 -39.770 1.00 29.83  ? 59  PHE B C   1 
ATOM   1195 O O   . PHE B 1 60 ? 18.094  -17.128 -39.211 1.00 27.67  ? 59  PHE B O   1 
ATOM   1196 C CB  . PHE B 1 60 ? 17.624  -19.917 -38.672 1.00 25.98  ? 59  PHE B CB  1 
ATOM   1197 C CG  . PHE B 1 60 ? 17.700  -21.323 -38.085 1.00 26.48  ? 59  PHE B CG  1 
ATOM   1198 C CD1 . PHE B 1 60 ? 18.165  -21.534 -36.791 1.00 29.68  ? 59  PHE B CD1 1 
ATOM   1199 C CD2 . PHE B 1 60 ? 17.289  -22.427 -38.830 1.00 28.69  ? 59  PHE B CD2 1 
ATOM   1200 C CE1 . PHE B 1 60 ? 18.250  -22.824 -36.263 1.00 31.41  ? 59  PHE B CE1 1 
ATOM   1201 C CE2 . PHE B 1 60 ? 17.346  -23.713 -38.291 1.00 33.11  ? 59  PHE B CE2 1 
ATOM   1202 C CZ  . PHE B 1 60 ? 17.840  -23.909 -37.016 1.00 31.48  ? 59  PHE B CZ  1 
ATOM   1203 N N   . PRO B 1 61 ? 19.331  -17.774 -40.985 1.00 33.46  ? 60  PRO B N   1 
ATOM   1204 C CA  . PRO B 1 61 ? 19.108  -16.524 -41.734 1.00 34.52  ? 60  PRO B CA  1 
ATOM   1205 C C   . PRO B 1 61 ? 17.662  -16.024 -41.699 1.00 33.56  ? 60  PRO B C   1 
ATOM   1206 O O   . PRO B 1 61 ? 16.722  -16.762 -41.999 1.00 33.37  ? 60  PRO B O   1 
ATOM   1207 C CB  . PRO B 1 61 ? 19.607  -16.871 -43.157 1.00 33.46  ? 60  PRO B CB  1 
ATOM   1208 C CG  . PRO B 1 61 ? 20.738  -17.849 -42.879 1.00 41.99  ? 60  PRO B CG  1 
ATOM   1209 C CD  . PRO B 1 61 ? 20.235  -18.707 -41.686 1.00 36.52  ? 60  PRO B CD  1 
ATOM   1210 N N   . TYR B 1 62 ? 17.494  -14.743 -41.332 1.00 32.05  ? 61  TYR B N   1 
ATOM   1211 C CA  . TYR B 1 62 ? 16.196  -14.211 -40.952 1.00 33.00  ? 61  TYR B CA  1 
ATOM   1212 C C   . TYR B 1 62 ? 15.216  -14.242 -42.111 1.00 33.83  ? 61  TYR B C   1 
ATOM   1213 O O   . TYR B 1 62 ? 14.062  -14.625 -41.927 1.00 37.15  ? 61  TYR B O   1 
ATOM   1214 C CB  . TYR B 1 62 ? 16.324  -12.753 -40.497 1.00 34.22  ? 61  TYR B CB  1 
ATOM   1215 C CG  . TYR B 1 62 ? 15.006  -12.024 -40.283 1.00 36.07  ? 61  TYR B CG  1 
ATOM   1216 C CD1 . TYR B 1 62 ? 14.227  -12.269 -39.154 1.00 36.44  ? 61  TYR B CD1 1 
ATOM   1217 C CD2 . TYR B 1 62 ? 14.586  -11.039 -41.176 1.00 37.86  ? 61  TYR B CD2 1 
ATOM   1218 C CE1 . TYR B 1 62 ? 13.054  -11.569 -38.934 1.00 39.57  ? 61  TYR B CE1 1 
ATOM   1219 C CE2 . TYR B 1 62 ? 13.411  -10.336 -40.968 1.00 41.82  ? 61  TYR B CE2 1 
ATOM   1220 C CZ  . TYR B 1 62 ? 12.650  -10.605 -39.843 1.00 40.61  ? 61  TYR B CZ  1 
ATOM   1221 O OH  . TYR B 1 62 ? 11.499  -9.912  -39.642 1.00 46.18  ? 61  TYR B OH  1 
ATOM   1222 N N   . ASP B 1 63 ? 15.688  -13.820 -43.290 1.00 41.12  ? 62  ASP B N   1 
ATOM   1223 C CA  . ASP B 1 63 ? 14.844  -13.750 -44.474 1.00 46.93  ? 62  ASP B CA  1 
ATOM   1224 C C   . ASP B 1 63 ? 14.305  -15.128 -44.835 1.00 41.98  ? 62  ASP B C   1 
ATOM   1225 O O   . ASP B 1 63 ? 13.099  -15.289 -44.988 1.00 41.26  ? 62  ASP B O   1 
ATOM   1226 C CB  . ASP B 1 63 ? 15.526  -13.051 -45.634 1.00 54.26  ? 62  ASP B CB  1 
ATOM   1227 C CG  . ASP B 1 63 ? 14.870  -11.734 -46.013 1.00 70.00  ? 62  ASP B CG  1 
ATOM   1228 O OD1 . ASP B 1 63 ? 14.889  -10.794 -45.175 1.00 74.27  ? 62  ASP B OD1 1 
ATOM   1229 O OD2 . ASP B 1 63 ? 14.300  -11.680 -47.126 1.00 76.06  ? 62  ASP B OD2 1 
ATOM   1230 N N   . LYS B 1 64 ? 15.197  -16.118 -44.919 1.00 43.79  ? 63  LYS B N   1 
ATOM   1231 C CA  . LYS B 1 64 ? 14.775  -17.485 -45.182 1.00 44.24  ? 63  LYS B CA  1 
ATOM   1232 C C   . LYS B 1 64 ? 13.726  -17.981 -44.178 1.00 42.27  ? 63  LYS B C   1 
ATOM   1233 O O   . LYS B 1 64 ? 12.855  -18.756 -44.546 1.00 43.21  ? 63  LYS B O   1 
ATOM   1234 C CB  . LYS B 1 64 ? 15.958  -18.458 -45.140 1.00 49.20  ? 63  LYS B CB  1 
ATOM   1235 C CG  . LYS B 1 64 ? 15.556  -19.883 -45.540 1.00 44.55  ? 63  LYS B CG  1 
ATOM   1236 C CD  . LYS B 1 64 ? 16.728  -20.834 -45.735 1.00 48.00  ? 63  LYS B CD  1 
ATOM   1237 C CE  . LYS B 1 64 ? 16.401  -22.064 -46.564 1.00 46.24  ? 63  LYS B CE  1 
ATOM   1238 N NZ  . LYS B 1 64 ? 15.085  -22.665 -46.337 1.00 45.51  ? 63  LYS B NZ  1 
ATOM   1239 N N   . SER B 1 65 ? 13.812  -17.573 -42.905 1.00 46.37  ? 64  SER B N   1 
ATOM   1240 C CA  . SER B 1 65 ? 13.144  -18.354 -41.867 1.00 45.13  ? 64  SER B CA  1 
ATOM   1241 C C   . SER B 1 65 ? 12.047  -17.589 -41.120 1.00 42.57  ? 64  SER B C   1 
ATOM   1242 O O   . SER B 1 65 ? 11.407  -18.154 -40.235 1.00 38.93  ? 64  SER B O   1 
ATOM   1243 C CB  . SER B 1 65 ? 14.142  -19.027 -40.941 1.00 42.23  ? 64  SER B CB  1 
ATOM   1244 O OG  . SER B 1 65 ? 15.051  -18.076 -40.407 1.00 53.22  ? 64  SER B OG  1 
ATOM   1245 N N   . LYS B 1 66 ? 11.748  -16.351 -41.543 1.00 39.14  ? 65  LYS B N   1 
ATOM   1246 C CA  . LYS B 1 66 ? 10.877  -15.483 -40.761 1.00 39.37  ? 65  LYS B CA  1 
ATOM   1247 C C   . LYS B 1 66 ? 9.435   -15.991 -40.692 1.00 44.13  ? 65  LYS B C   1 
ATOM   1248 O O   . LYS B 1 66 ? 8.743   -15.767 -39.695 1.00 44.62  ? 65  LYS B O   1 
ATOM   1249 C CB  . LYS B 1 66 ? 10.956  -14.004 -41.173 1.00 38.80  ? 65  LYS B CB  1 
ATOM   1250 C CG  . LYS B 1 66 ? 10.674  -13.712 -42.636 1.00 33.97  ? 65  LYS B CG  1 
ATOM   1251 N N   . ASP B 1 67 ? 8.937   -16.662 -41.732 1.00 47.09  ? 66  ASP B N   1 
ATOM   1252 C CA  . ASP B 1 67 ? 7.537   -17.052 -41.624 1.00 52.04  ? 66  ASP B CA  1 
ATOM   1253 C C   . ASP B 1 67 ? 7.422   -18.308 -40.762 1.00 47.82  ? 66  ASP B C   1 
ATOM   1254 O O   . ASP B 1 67 ? 6.372   -18.567 -40.170 1.00 46.27  ? 66  ASP B O   1 
ATOM   1255 C CB  . ASP B 1 67 ? 6.760   -16.936 -42.928 1.00 63.57  ? 66  ASP B CB  1 
ATOM   1256 C CG  . ASP B 1 67 ? 7.433   -17.488 -44.176 1.00 76.08  ? 66  ASP B CG  1 
ATOM   1257 O OD1 . ASP B 1 67 ? 6.941   -17.187 -45.294 1.00 74.00  ? 66  ASP B OD1 1 
ATOM   1258 O OD2 . ASP B 1 67 ? 8.435   -18.218 -44.021 1.00 76.90  ? 66  ASP B OD2 1 
ATOM   1259 N N   . LYS B 1 68 ? 8.530   -19.048 -40.654 1.00 44.95  ? 67  LYS B N   1 
ATOM   1260 C CA  . LYS B 1 68 ? 8.558   -20.227 -39.802 1.00 41.96  ? 67  LYS B CA  1 
ATOM   1261 C C   . LYS B 1 68 ? 8.684   -19.813 -38.334 1.00 39.75  ? 67  LYS B C   1 
ATOM   1262 O O   . LYS B 1 68 ? 7.927   -20.298 -37.492 1.00 38.39  ? 67  LYS B O   1 
ATOM   1263 C CB  . LYS B 1 68 ? 9.591   -21.228 -40.324 1.00 48.46  ? 67  LYS B CB  1 
ATOM   1264 C CG  . LYS B 1 68 ? 9.695   -22.542 -39.570 1.00 57.51  ? 67  LYS B CG  1 
ATOM   1265 C CD  . LYS B 1 68 ? 10.443  -23.536 -40.453 1.00 68.82  ? 67  LYS B CD  1 
ATOM   1266 C CE  . LYS B 1 68 ? 11.130  -24.646 -39.710 1.00 72.50  ? 67  LYS B CE  1 
ATOM   1267 N NZ  . LYS B 1 68 ? 10.225  -25.518 -38.957 1.00 74.60  ? 67  LYS B NZ  1 
ATOM   1268 N N   . TYR B 1 69 ? 9.605   -18.890 -38.027 1.00 33.68  ? 68  TYR B N   1 
ATOM   1269 C CA  . TYR B 1 69 ? 9.989   -18.684 -36.635 1.00 33.41  ? 68  TYR B CA  1 
ATOM   1270 C C   . TYR B 1 69 ? 9.478   -17.357 -36.084 1.00 36.84  ? 68  TYR B C   1 
ATOM   1271 O O   . TYR B 1 69 ? 9.596   -17.118 -34.881 1.00 36.88  ? 68  TYR B O   1 
ATOM   1272 C CB  . TYR B 1 69 ? 11.510  -18.736 -36.454 1.00 32.74  ? 68  TYR B CB  1 
ATOM   1273 C CG  . TYR B 1 69 ? 12.091  -20.117 -36.735 1.00 35.50  ? 68  TYR B CG  1 
ATOM   1274 C CD1 . TYR B 1 69 ? 11.527  -21.269 -36.185 1.00 38.16  ? 68  TYR B CD1 1 
ATOM   1275 C CD2 . TYR B 1 69 ? 13.191  -20.263 -37.576 1.00 36.84  ? 68  TYR B CD2 1 
ATOM   1276 C CE1 . TYR B 1 69 ? 12.058  -22.526 -36.452 1.00 40.79  ? 68  TYR B CE1 1 
ATOM   1277 C CE2 . TYR B 1 69 ? 13.719  -21.509 -37.864 1.00 37.69  ? 68  TYR B CE2 1 
ATOM   1278 C CZ  . TYR B 1 69 ? 13.156  -22.640 -37.289 1.00 40.11  ? 68  TYR B CZ  1 
ATOM   1279 O OH  . TYR B 1 69 ? 13.699  -23.853 -37.575 1.00 34.63  ? 68  TYR B OH  1 
ATOM   1280 N N   . GLY B 1 70 ? 8.937   -16.505 -36.966 1.00 34.73  ? 69  GLY B N   1 
ATOM   1281 C CA  . GLY B 1 70 ? 8.695   -15.120 -36.610 1.00 37.96  ? 69  GLY B CA  1 
ATOM   1282 C C   . GLY B 1 70 ? 7.273   -14.907 -36.109 1.00 41.23  ? 69  GLY B C   1 
ATOM   1283 O O   . GLY B 1 70 ? 6.672   -13.881 -36.409 1.00 44.41  ? 69  GLY B O   1 
ATOM   1284 N N   . LYS B 1 71 ? 6.738   -15.895 -35.385 1.00 43.80  ? 70  LYS B N   1 
ATOM   1285 C CA  . LYS B 1 71 ? 5.391   -15.790 -34.865 1.00 45.23  ? 70  LYS B CA  1 
ATOM   1286 C C   . LYS B 1 71 ? 5.475   -15.414 -33.396 1.00 49.02  ? 70  LYS B C   1 
ATOM   1287 O O   . LYS B 1 71 ? 6.300   -15.965 -32.665 1.00 47.79  ? 70  LYS B O   1 
ATOM   1288 C CB  . LYS B 1 71 ? 4.583   -17.076 -35.061 1.00 47.23  ? 70  LYS B CB  1 
ATOM   1289 C CG  . LYS B 1 71 ? 4.222   -17.267 -36.528 1.00 52.59  ? 70  LYS B CG  1 
ATOM   1290 C CD  . LYS B 1 71 ? 3.946   -18.706 -36.945 1.00 51.57  ? 70  LYS B CD  1 
ATOM   1291 C CE  . LYS B 1 71 ? 3.447   -18.800 -38.353 1.00 53.20  ? 70  LYS B CE  1 
ATOM   1292 N NZ  . LYS B 1 71 ? 4.252   -17.999 -39.286 1.00 61.42  ? 70  LYS B NZ  1 
ATOM   1293 N N   . PRO B 1 72 ? 4.617   -14.476 -32.934 1.00 49.53  ? 71  PRO B N   1 
ATOM   1294 C CA  . PRO B 1 72 ? 4.629   -14.057 -31.530 1.00 46.36  ? 71  PRO B CA  1 
ATOM   1295 C C   . PRO B 1 72 ? 4.285   -15.208 -30.582 1.00 49.07  ? 71  PRO B C   1 
ATOM   1296 O O   . PRO B 1 72 ? 3.611   -16.162 -30.984 1.00 40.93  ? 71  PRO B O   1 
ATOM   1297 C CB  . PRO B 1 72 ? 3.633   -12.876 -31.447 1.00 45.60  ? 71  PRO B CB  1 
ATOM   1298 C CG  . PRO B 1 72 ? 2.808   -12.991 -32.709 1.00 47.46  ? 71  PRO B CG  1 
ATOM   1299 C CD  . PRO B 1 72 ? 3.602   -13.779 -33.744 1.00 46.29  ? 71  PRO B CD  1 
ATOM   1300 N N   . ASN B 1 73 ? 4.789   -15.112 -29.337 1.00 40.55  ? 72  ASN B N   1 
ATOM   1301 C CA  . ASN B 1 73 ? 4.496   -16.080 -28.289 1.00 39.48  ? 72  ASN B CA  1 
ATOM   1302 C C   . ASN B 1 73 ? 4.460   -15.361 -26.934 1.00 43.15  ? 72  ASN B C   1 
ATOM   1303 O O   . ASN B 1 73 ? 4.447   -14.131 -26.873 1.00 41.14  ? 72  ASN B O   1 
ATOM   1304 C CB  . ASN B 1 73 ? 5.478   -17.250 -28.324 1.00 36.77  ? 72  ASN B CB  1 
ATOM   1305 C CG  . ASN B 1 73 ? 6.903   -16.782 -28.165 1.00 35.72  ? 72  ASN B CG  1 
ATOM   1306 O OD1 . ASN B 1 73 ? 7.189   -15.975 -27.270 1.00 37.35  ? 72  ASN B OD1 1 
ATOM   1307 N ND2 . ASN B 1 73 ? 7.803   -17.243 -29.025 1.00 34.67  ? 72  ASN B ND2 1 
ATOM   1308 N N   . LYS B 1 74 ? 4.489   -16.141 -25.849 1.00 42.57  ? 73  LYS B N   1 
ATOM   1309 C CA  . LYS B 1 74 ? 4.339   -15.618 -24.497 1.00 46.76  ? 73  LYS B CA  1 
ATOM   1310 C C   . LYS B 1 74 ? 5.691   -15.481 -23.780 1.00 42.37  ? 73  LYS B C   1 
ATOM   1311 O O   . LYS B 1 74 ? 5.711   -15.321 -22.567 1.00 41.62  ? 73  LYS B O   1 
ATOM   1312 C CB  . LYS B 1 74 ? 3.431   -16.572 -23.699 1.00 42.59  ? 73  LYS B CB  1 
ATOM   1313 N N   . ARG B 1 75 ? 6.817   -15.594 -24.499 1.00 35.28  ? 74  ARG B N   1 
ATOM   1314 C CA  . ARG B 1 75 ? 8.121   -15.501 -23.857 1.00 32.72  ? 74  ARG B CA  1 
ATOM   1315 C C   . ARG B 1 75 ? 8.480   -14.022 -23.679 1.00 35.56  ? 74  ARG B C   1 
ATOM   1316 O O   . ARG B 1 75 ? 8.330   -13.218 -24.607 1.00 37.20  ? 74  ARG B O   1 
ATOM   1317 C CB  . ARG B 1 75 ? 9.211   -16.328 -24.553 1.00 36.08  ? 74  ARG B CB  1 
ATOM   1318 C CG  . ARG B 1 75 ? 8.979   -17.824 -24.712 1.00 31.50  ? 74  ARG B CG  1 
ATOM   1319 C CD  . ARG B 1 75 ? 8.895   -18.611 -23.400 1.00 37.02  ? 74  ARG B CD  1 
ATOM   1320 N NE  . ARG B 1 75 ? 9.124   -20.042 -23.640 1.00 37.29  ? 74  ARG B NE  1 
ATOM   1321 C CZ  . ARG B 1 75 ? 10.285  -20.622 -23.421 1.00 33.32  ? 74  ARG B CZ  1 
ATOM   1322 N NH1 . ARG B 1 75 ? 11.309  -19.917 -22.970 1.00 37.69  ? 74  ARG B NH1 1 
ATOM   1323 N NH2 . ARG B 1 75 ? 10.454  -21.898 -23.704 1.00 39.68  ? 74  ARG B NH2 1 
ATOM   1324 N N   . LYS B 1 76 ? 8.889   -13.651 -22.454 1.00 30.95  ? 75  LYS B N   1 
ATOM   1325 C CA  . LYS B 1 76 ? 9.184   -12.262 -22.143 1.00 28.17  ? 75  LYS B CA  1 
ATOM   1326 C C   . LYS B 1 76 ? 10.282  -11.728 -23.075 1.00 26.48  ? 75  LYS B C   1 
ATOM   1327 O O   . LYS B 1 76 ? 11.399  -12.273 -23.123 1.00 29.02  ? 75  LYS B O   1 
ATOM   1328 C CB  . LYS B 1 76 ? 9.651   -12.149 -20.689 1.00 31.89  ? 75  LYS B CB  1 
ATOM   1329 C CG  . LYS B 1 76 ? 10.078  -10.721 -20.295 1.00 32.95  ? 75  LYS B CG  1 
ATOM   1330 C CD  . LYS B 1 76 ? 10.805  -10.646 -18.955 1.00 33.47  ? 75  LYS B CD  1 
ATOM   1331 C CE  . LYS B 1 76 ? 11.053  -9.212  -18.548 1.00 39.70  ? 75  LYS B CE  1 
ATOM   1332 N NZ  . LYS B 1 76 ? 11.236  -9.100  -17.099 1.00 43.68  ? 75  LYS B NZ  1 
ATOM   1333 N N   . GLY B 1 77 ? 9.950   -10.671 -23.812 1.00 29.24  ? 76  GLY B N   1 
ATOM   1334 C CA  . GLY B 1 77 ? 10.916  -9.956  -24.637 1.00 28.74  ? 76  GLY B CA  1 
ATOM   1335 C C   . GLY B 1 77 ? 10.825  -10.380 -26.105 1.00 34.17  ? 76  GLY B C   1 
ATOM   1336 O O   . GLY B 1 77 ? 11.433  -9.752  -26.966 1.00 31.86  ? 76  GLY B O   1 
ATOM   1337 N N   . PHE B 1 78 ? 10.036  -11.432 -26.391 1.00 30.35  ? 77  PHE B N   1 
ATOM   1338 C CA  . PHE B 1 78 ? 9.997   -12.004 -27.733 1.00 29.42  ? 77  PHE B CA  1 
ATOM   1339 C C   . PHE B 1 78 ? 9.247   -11.091 -28.692 1.00 31.58  ? 77  PHE B C   1 
ATOM   1340 O O   . PHE B 1 78 ? 9.700   -10.856 -29.805 1.00 30.45  ? 77  PHE B O   1 
ATOM   1341 C CB  . PHE B 1 78 ? 9.288   -13.358 -27.773 1.00 29.45  ? 77  PHE B CB  1 
ATOM   1342 C CG  . PHE B 1 78 ? 9.525   -14.102 -29.078 1.00 29.81  ? 77  PHE B CG  1 
ATOM   1343 C CD1 . PHE B 1 78 ? 10.635  -14.937 -29.222 1.00 31.38  ? 77  PHE B CD1 1 
ATOM   1344 C CD2 . PHE B 1 78 ? 8.651   -13.959 -30.142 1.00 31.41  ? 77  PHE B CD2 1 
ATOM   1345 C CE1 . PHE B 1 78 ? 10.867  -15.617 -30.406 1.00 32.52  ? 77  PHE B CE1 1 
ATOM   1346 C CE2 . PHE B 1 78 ? 8.885   -14.649 -31.332 1.00 34.07  ? 77  PHE B CE2 1 
ATOM   1347 C CZ  . PHE B 1 78 ? 9.990   -15.476 -31.449 1.00 32.80  ? 77  PHE B CZ  1 
ATOM   1348 N N   . ASN B 1 79 ? 8.077   -10.596 -28.284 1.00 32.32  ? 78  ASN B N   1 
ATOM   1349 C CA  . ASN B 1 79 ? 7.342   -9.767  -29.220 1.00 32.15  ? 78  ASN B CA  1 
ATOM   1350 C C   . ASN B 1 79 ? 8.079   -8.439  -29.419 1.00 31.45  ? 78  ASN B C   1 
ATOM   1351 O O   . ASN B 1 79 ? 8.019   -7.848  -30.493 1.00 34.58  ? 78  ASN B O   1 
ATOM   1352 C CB  . ASN B 1 79 ? 5.867   -9.628  -28.850 1.00 35.52  ? 78  ASN B CB  1 
ATOM   1353 C CG  . ASN B 1 79 ? 5.136   -10.952 -28.857 1.00 42.95  ? 78  ASN B CG  1 
ATOM   1354 O OD1 . ASN B 1 79 ? 5.653   -11.952 -29.371 1.00 39.07  ? 78  ASN B OD1 1 
ATOM   1355 N ND2 . ASN B 1 79 ? 3.946   -10.997 -28.264 1.00 40.69  ? 78  ASN B ND2 1 
ATOM   1356 N N   . GLU B 1 80 ? 8.771   -7.975  -28.385 1.00 31.75  ? 79  GLU B N   1 
ATOM   1357 C CA  . GLU B 1 80 ? 9.570   -6.766  -28.511 1.00 36.04  ? 79  GLU B CA  1 
ATOM   1358 C C   . GLU B 1 80 ? 10.694  -7.003  -29.516 1.00 30.22  ? 79  GLU B C   1 
ATOM   1359 O O   . GLU B 1 80 ? 11.004  -6.111  -30.292 1.00 32.69  ? 79  GLU B O   1 
ATOM   1360 C CB  . GLU B 1 80 ? 10.107  -6.255  -27.181 1.00 34.54  ? 79  GLU B CB  1 
ATOM   1361 C CG  . GLU B 1 80 ? 9.042   -5.489  -26.401 1.00 41.61  ? 79  GLU B CG  1 
ATOM   1362 N N   . GLY B 1 81 ? 11.258  -8.220  -29.510 1.00 28.32  ? 80  GLY B N   1 
ATOM   1363 C CA  . GLY B 1 81 ? 12.332  -8.627  -30.411 1.00 27.48  ? 80  GLY B CA  1 
ATOM   1364 C C   . GLY B 1 81 ? 11.871  -8.655  -31.863 1.00 30.01  ? 80  GLY B C   1 
ATOM   1365 O O   . GLY B 1 81 ? 12.588  -8.188  -32.753 1.00 33.14  ? 80  GLY B O   1 
ATOM   1366 N N   . LEU B 1 82 ? 10.639  -9.135  -32.076 1.00 27.30  ? 81  LEU B N   1 
ATOM   1367 C CA  . LEU B 1 82 ? 10.040  -9.165  -33.399 1.00 31.60  ? 81  LEU B CA  1 
ATOM   1368 C C   . LEU B 1 82 ? 9.913   -7.737  -33.916 1.00 33.14  ? 81  LEU B C   1 
ATOM   1369 O O   . LEU B 1 82 ? 10.173  -7.483  -35.088 1.00 33.49  ? 81  LEU B O   1 
ATOM   1370 C CB  . LEU B 1 82 ? 8.709   -9.924  -33.438 1.00 30.99  ? 81  LEU B CB  1 
ATOM   1371 C CG  . LEU B 1 82 ? 8.793   -11.432 -33.164 1.00 30.90  ? 81  LEU B CG  1 
ATOM   1372 C CD1 . LEU B 1 82 ? 7.399   -12.086 -33.283 1.00 32.80  ? 81  LEU B CD1 1 
ATOM   1373 C CD2 . LEU B 1 82 ? 9.791   -12.130 -34.074 1.00 27.25  ? 81  LEU B CD2 1 
ATOM   1374 N N   . TRP B 1 83 ? 9.547   -6.805  -33.028 1.00 29.68  ? 82  TRP B N   1 
ATOM   1375 C CA  . TRP B 1 83 ? 9.463   -5.399  -33.390 1.00 31.97  ? 82  TRP B CA  1 
ATOM   1376 C C   . TRP B 1 83 ? 10.833  -4.844  -33.785 1.00 29.57  ? 82  TRP B C   1 
ATOM   1377 O O   . TRP B 1 83 ? 10.937  -4.133  -34.781 1.00 35.34  ? 82  TRP B O   1 
ATOM   1378 C CB  . TRP B 1 83 ? 8.824   -4.560  -32.268 1.00 31.26  ? 82  TRP B CB  1 
ATOM   1379 C CG  . TRP B 1 83 ? 8.541   -3.159  -32.739 1.00 35.12  ? 82  TRP B CG  1 
ATOM   1380 C CD1 . TRP B 1 83 ? 7.409   -2.710  -33.353 1.00 38.46  ? 82  TRP B CD1 1 
ATOM   1381 C CD2 . TRP B 1 83 ? 9.468   -2.049  -32.743 1.00 36.27  ? 82  TRP B CD2 1 
ATOM   1382 N NE1 . TRP B 1 83 ? 7.552   -1.389  -33.703 1.00 37.34  ? 82  TRP B NE1 1 
ATOM   1383 C CE2 . TRP B 1 83 ? 8.807   -0.962  -33.355 1.00 38.07  ? 82  TRP B CE2 1 
ATOM   1384 C CE3 . TRP B 1 83 ? 10.786  -1.869  -32.295 1.00 39.09  ? 82  TRP B CE3 1 
ATOM   1385 C CZ2 . TRP B 1 83 ? 9.410   0.289   -33.501 1.00 39.81  ? 82  TRP B CZ2 1 
ATOM   1386 C CZ3 . TRP B 1 83 ? 11.388  -0.634  -32.452 1.00 41.75  ? 82  TRP B CZ3 1 
ATOM   1387 C CH2 . TRP B 1 83 ? 10.713  0.424   -33.062 1.00 41.76  ? 82  TRP B CH2 1 
ATOM   1388 N N   . GLU B 1 84 ? 11.860  -5.150  -32.981 1.00 28.70  ? 83  GLU B N   1 
ATOM   1389 C CA  . GLU B 1 84 ? 13.196  -4.603  -33.174 1.00 30.61  ? 83  GLU B CA  1 
ATOM   1390 C C   . GLU B 1 84 ? 13.829  -5.106  -34.473 1.00 32.86  ? 83  GLU B C   1 
ATOM   1391 O O   . GLU B 1 84 ? 14.411  -4.320  -35.223 1.00 31.50  ? 83  GLU B O   1 
ATOM   1392 C CB  . GLU B 1 84 ? 14.135  -4.872  -32.003 1.00 30.22  ? 83  GLU B CB  1 
ATOM   1393 C CG  . GLU B 1 84 ? 13.709  -4.100  -30.754 1.00 34.04  ? 83  GLU B CG  1 
ATOM   1394 C CD  . GLU B 1 84 ? 14.516  -4.491  -29.542 1.00 33.42  ? 83  GLU B CD  1 
ATOM   1395 O OE1 . GLU B 1 84 ? 15.381  -5.384  -29.678 1.00 32.17  ? 83  GLU B OE1 1 
ATOM   1396 O OE2 . GLU B 1 84 ? 14.292  -3.910  -28.447 1.00 36.51  ? 83  GLU B OE2 1 
ATOM   1397 N N   . ILE B 1 85 ? 13.727  -6.412  -34.725 1.00 29.46  ? 84  ILE B N   1 
ATOM   1398 C CA  . ILE B 1 85 ? 14.382  -6.980  -35.886 1.00 30.04  ? 84  ILE B CA  1 
ATOM   1399 C C   . ILE B 1 85 ? 13.721  -6.404  -37.139 1.00 29.13  ? 84  ILE B C   1 
ATOM   1400 O O   . ILE B 1 85 ? 14.380  -6.237  -38.156 1.00 29.92  ? 84  ILE B O   1 
ATOM   1401 C CB  . ILE B 1 85 ? 14.377  -8.519  -35.854 1.00 29.83  ? 84  ILE B CB  1 
ATOM   1402 C CG1 . ILE B 1 85 ? 15.382  -9.085  -36.871 1.00 29.66  ? 84  ILE B CG1 1 
ATOM   1403 C CG2 . ILE B 1 85 ? 12.958  -9.054  -36.072 1.00 27.09  ? 84  ILE B CG2 1 
ATOM   1404 C CD1 . ILE B 1 85 ? 15.851  -10.507 -36.586 1.00 31.27  ? 84  ILE B CD1 1 
ATOM   1405 N N   . GLN B 1 86 ? 12.418  -6.092  -37.046 1.00 30.31  ? 85  GLN B N   1 
ATOM   1406 C CA  . GLN B 1 86 ? 11.642  -5.589  -38.170 1.00 32.68  ? 85  GLN B CA  1 
ATOM   1407 C C   . GLN B 1 86 ? 11.824  -4.084  -38.389 1.00 32.29  ? 85  GLN B C   1 
ATOM   1408 O O   . GLN B 1 86 ? 11.864  -3.644  -39.535 1.00 34.68  ? 85  GLN B O   1 
ATOM   1409 C CB  . GLN B 1 86 ? 10.148  -5.861  -37.982 1.00 34.53  ? 85  GLN B CB  1 
ATOM   1410 N N   . ASN B 1 87 ? 11.932  -3.280  -37.321 1.00 29.32  ? 86  ASN B N   1 
ATOM   1411 C CA  . ASN B 1 87 ? 11.802  -1.834  -37.507 1.00 32.81  ? 86  ASN B CA  1 
ATOM   1412 C C   . ASN B 1 87 ? 13.111  -1.078  -37.306 1.00 32.59  ? 86  ASN B C   1 
ATOM   1413 O O   . ASN B 1 87 ? 13.233  0.067   -37.751 1.00 34.54  ? 86  ASN B O   1 
ATOM   1414 C CB  . ASN B 1 87 ? 10.721  -1.264  -36.587 1.00 35.63  ? 86  ASN B CB  1 
ATOM   1415 C CG  . ASN B 1 87 ? 9.380   -1.878  -36.910 1.00 40.77  ? 86  ASN B CG  1 
ATOM   1416 O OD1 . ASN B 1 87 ? 8.786   -1.537  -37.932 1.00 45.81  ? 86  ASN B OD1 1 
ATOM   1417 N ND2 . ASN B 1 87 ? 8.920   -2.830  -36.110 1.00 44.49  ? 86  ASN B ND2 1 
ATOM   1418 N N   . ASN B 1 88 ? 14.066  -1.677  -36.586 1.00 28.90  ? 87  ASN B N   1 
ATOM   1419 C CA  . ASN B 1 88 ? 15.321  -1.000  -36.322 1.00 32.63  ? 87  ASN B CA  1 
ATOM   1420 C C   . ASN B 1 88 ? 16.385  -2.022  -35.933 1.00 29.46  ? 87  ASN B C   1 
ATOM   1421 O O   . ASN B 1 88 ? 16.955  -1.941  -34.850 1.00 28.71  ? 87  ASN B O   1 
ATOM   1422 C CB  . ASN B 1 88 ? 15.162  0.128   -35.297 1.00 34.30  ? 87  ASN B CB  1 
ATOM   1423 C CG  . ASN B 1 88 ? 16.202  1.211   -35.498 1.00 36.39  ? 87  ASN B CG  1 
ATOM   1424 O OD1 . ASN B 1 88 ? 17.231  1.001   -36.149 1.00 33.88  ? 87  ASN B OD1 1 
ATOM   1425 N ND2 . ASN B 1 88 ? 15.973  2.385   -34.936 1.00 38.68  ? 87  ASN B ND2 1 
ATOM   1426 N N   . PRO B 1 89 ? 16.695  -3.013  -36.806 1.00 31.27  ? 88  PRO B N   1 
ATOM   1427 C CA  . PRO B 1 89 ? 17.646  -4.074  -36.462 1.00 27.20  ? 88  PRO B CA  1 
ATOM   1428 C C   . PRO B 1 89 ? 19.062  -3.620  -36.137 1.00 29.48  ? 88  PRO B C   1 
ATOM   1429 O O   . PRO B 1 89 ? 19.804  -4.358  -35.487 1.00 27.47  ? 88  PRO B O   1 
ATOM   1430 C CB  . PRO B 1 89 ? 17.674  -4.979  -37.729 1.00 26.16  ? 88  PRO B CB  1 
ATOM   1431 C CG  . PRO B 1 89 ? 17.159  -4.091  -38.839 1.00 26.94  ? 88  PRO B CG  1 
ATOM   1432 C CD  . PRO B 1 89 ? 16.121  -3.185  -38.154 1.00 29.88  ? 88  PRO B CD  1 
ATOM   1433 N N   . HIS B 1 90 ? 19.465  -2.448  -36.663 1.00 28.28  ? 89  HIS B N   1 
ATOM   1434 C CA  . HIS B 1 90 ? 20.863  -2.058  -36.536 1.00 28.34  ? 89  HIS B CA  1 
ATOM   1435 C C   . HIS B 1 90 ? 21.073  -0.934  -35.517 1.00 30.57  ? 89  HIS B C   1 
ATOM   1436 O O   . HIS B 1 90 ? 22.182  -0.402  -35.405 1.00 31.80  ? 89  HIS B O   1 
ATOM   1437 C CB  . HIS B 1 90 ? 21.443  -1.697  -37.908 1.00 31.24  ? 89  HIS B CB  1 
ATOM   1438 C CG  . HIS B 1 90 ? 21.243  -2.777  -38.925 1.00 32.55  ? 89  HIS B CG  1 
ATOM   1439 N ND1 . HIS B 1 90 ? 21.869  -4.005  -38.831 1.00 30.73  ? 89  HIS B ND1 1 
ATOM   1440 C CD2 . HIS B 1 90 ? 20.478  -2.823  -40.034 1.00 30.09  ? 89  HIS B CD2 1 
ATOM   1441 C CE1 . HIS B 1 90 ? 21.504  -4.749  -39.871 1.00 29.71  ? 89  HIS B CE1 1 
ATOM   1442 N NE2 . HIS B 1 90 ? 20.696  -4.034  -40.626 1.00 30.64  ? 89  HIS B NE2 1 
ATOM   1443 N N   . ALA B 1 91 ? 20.050  -0.644  -34.709 1.00 30.67  ? 90  ALA B N   1 
ATOM   1444 C CA  . ALA B 1 91 ? 20.173  0.406   -33.701 1.00 31.08  ? 90  ALA B CA  1 
ATOM   1445 C C   . ALA B 1 91 ? 21.137  -0.021  -32.596 1.00 35.49  ? 90  ALA B C   1 
ATOM   1446 O O   . ALA B 1 91 ? 21.438  -1.201  -32.435 1.00 33.20  ? 90  ALA B O   1 
ATOM   1447 C CB  . ALA B 1 91 ? 18.810  0.716   -33.117 1.00 26.67  ? 90  ALA B CB  1 
ATOM   1448 N N   . SER B 1 92 ? 21.583  0.968   -31.813 1.00 35.66  ? 91  SER B N   1 
ATOM   1449 C CA  . SER B 1 92 ? 22.233  0.757   -30.532 1.00 41.25  ? 91  SER B CA  1 
ATOM   1450 C C   . SER B 1 92 ? 21.157  0.531   -29.467 1.00 42.71  ? 91  SER B C   1 
ATOM   1451 O O   . SER B 1 92 ? 20.233  1.338   -29.349 1.00 42.66  ? 91  SER B O   1 
ATOM   1452 C CB  . SER B 1 92 ? 23.085  1.966   -30.191 1.00 39.41  ? 91  SER B CB  1 
ATOM   1453 O OG  . SER B 1 92 ? 23.544  1.855   -28.855 1.00 46.94  ? 91  SER B OG  1 
ATOM   1454 N N   . TYR B 1 93 ? 21.268  -0.590  -28.737 1.00 42.09  ? 92  TYR B N   1 
ATOM   1455 C CA  . TYR B 1 93 ? 20.336  -0.983  -27.686 1.00 42.31  ? 92  TYR B CA  1 
ATOM   1456 C C   . TYR B 1 93 ? 21.081  -0.929  -26.358 1.00 51.64  ? 92  TYR B C   1 
ATOM   1457 O O   . TYR B 1 93 ? 20.689  -1.574  -25.391 1.00 50.64  ? 92  TYR B O   1 
ATOM   1458 C CB  . TYR B 1 93 ? 19.674  -2.348  -27.937 1.00 34.63  ? 92  TYR B CB  1 
ATOM   1459 C CG  . TYR B 1 93 ? 18.674  -2.261  -29.075 1.00 30.31  ? 92  TYR B CG  1 
ATOM   1460 C CD1 . TYR B 1 93 ? 17.401  -1.751  -28.871 1.00 32.57  ? 92  TYR B CD1 1 
ATOM   1461 C CD2 . TYR B 1 93 ? 19.021  -2.666  -30.362 1.00 31.82  ? 92  TYR B CD2 1 
ATOM   1462 C CE1 . TYR B 1 93 ? 16.509  -1.617  -29.919 1.00 32.48  ? 92  TYR B CE1 1 
ATOM   1463 C CE2 . TYR B 1 93 ? 18.127  -2.549  -31.416 1.00 30.56  ? 92  TYR B CE2 1 
ATOM   1464 C CZ  . TYR B 1 93 ? 16.870  -2.029  -31.192 1.00 32.40  ? 92  TYR B CZ  1 
ATOM   1465 O OH  . TYR B 1 93 ? 15.988  -1.928  -32.237 1.00 32.07  ? 92  TYR B OH  1 
ATOM   1466 N N   . SER B 1 94 ? 22.140  -0.107  -26.350 1.00 62.88  ? 93  SER B N   1 
ATOM   1467 C CA  . SER B 1 94 ? 23.073  0.066   -25.250 1.00 70.81  ? 93  SER B CA  1 
ATOM   1468 C C   . SER B 1 94 ? 22.393  0.749   -24.053 1.00 81.10  ? 93  SER B C   1 
ATOM   1469 O O   . SER B 1 94 ? 21.267  1.281   -24.243 1.00 79.40  ? 93  SER B O   1 
ATOM   1470 C CB  . SER B 1 94 ? 24.256  0.868   -25.707 1.00 71.79  ? 93  SER B CB  1 
ATOM   1471 O OG  . SER B 1 94 ? 25.066  0.106   -26.587 1.00 76.26  ? 93  SER B OG  1 
ATOM   1472 O OXT . SER B 1 94 ? 23.025  0.739   -22.966 1.00 86.65  ? 93  SER B OXT 1 
ATOM   1473 N N   . ALA C 1 5  ? 29.815  -22.401 29.312  1.00 60.86  ? 4   ALA C N   1 
ATOM   1474 C CA  . ALA C 1 5  ? 28.897  -23.462 29.792  1.00 63.12  ? 4   ALA C CA  1 
ATOM   1475 C C   . ALA C 1 5  ? 27.433  -23.057 29.599  1.00 70.68  ? 4   ALA C C   1 
ATOM   1476 O O   . ALA C 1 5  ? 27.137  -22.051 28.951  1.00 74.26  ? 4   ALA C O   1 
ATOM   1477 C CB  . ALA C 1 5  ? 29.208  -23.798 31.225  1.00 67.40  ? 4   ALA C CB  1 
ATOM   1478 N N   . PHE C 1 6  ? 26.520  -23.853 30.177  1.00 60.89  ? 5   PHE C N   1 
ATOM   1479 C CA  . PHE C 1 6  ? 25.136  -23.878 29.740  1.00 57.82  ? 5   PHE C CA  1 
ATOM   1480 C C   . PHE C 1 6  ? 24.221  -24.061 30.949  1.00 66.48  ? 5   PHE C C   1 
ATOM   1481 O O   . PHE C 1 6  ? 24.500  -24.907 31.797  1.00 79.89  ? 5   PHE C O   1 
ATOM   1482 C CB  . PHE C 1 6  ? 24.998  -25.091 28.802  1.00 50.45  ? 5   PHE C CB  1 
ATOM   1483 C CG  . PHE C 1 6  ? 25.824  -25.115 27.515  1.00 44.99  ? 5   PHE C CG  1 
ATOM   1484 C CD1 . PHE C 1 6  ? 26.940  -25.937 27.390  1.00 42.78  ? 5   PHE C CD1 1 
ATOM   1485 C CD2 . PHE C 1 6  ? 25.491  -24.310 26.426  1.00 48.48  ? 5   PHE C CD2 1 
ATOM   1486 C CE1 . PHE C 1 6  ? 27.686  -25.957 26.214  1.00 49.58  ? 5   PHE C CE1 1 
ATOM   1487 C CE2 . PHE C 1 6  ? 26.240  -24.339 25.248  1.00 45.92  ? 5   PHE C CE2 1 
ATOM   1488 C CZ  . PHE C 1 6  ? 27.332  -25.159 25.141  1.00 46.41  ? 5   PHE C CZ  1 
ATOM   1489 N N   . LYS C 1 7  ? 23.123  -23.291 31.008  1.00 58.36  ? 6   LYS C N   1 
ATOM   1490 C CA  . LYS C 1 7  ? 22.116  -23.426 32.057  1.00 58.56  ? 6   LYS C CA  1 
ATOM   1491 C C   . LYS C 1 7  ? 20.777  -23.786 31.413  1.00 54.79  ? 6   LYS C C   1 
ATOM   1492 O O   . LYS C 1 7  ? 20.635  -23.676 30.196  1.00 56.02  ? 6   LYS C O   1 
ATOM   1493 C CB  . LYS C 1 7  ? 22.040  -22.162 32.927  1.00 61.51  ? 6   LYS C CB  1 
ATOM   1494 N N   . PRO C 1 8  ? 19.744  -24.225 32.175  1.00 58.54  ? 7   PRO C N   1 
ATOM   1495 C CA  . PRO C 1 8  ? 18.449  -24.570 31.570  1.00 57.77  ? 7   PRO C CA  1 
ATOM   1496 C C   . PRO C 1 8  ? 17.829  -23.416 30.777  1.00 64.68  ? 7   PRO C C   1 
ATOM   1497 O O   . PRO C 1 8  ? 17.760  -22.291 31.266  1.00 68.28  ? 7   PRO C O   1 
ATOM   1498 C CB  . PRO C 1 8  ? 17.581  -25.002 32.765  1.00 58.97  ? 7   PRO C CB  1 
ATOM   1499 C CG  . PRO C 1 8  ? 18.590  -25.390 33.830  1.00 57.54  ? 7   PRO C CG  1 
ATOM   1500 C CD  . PRO C 1 8  ? 19.770  -24.449 33.632  1.00 59.51  ? 7   PRO C CD  1 
ATOM   1501 N N   . GLY C 1 9  ? 17.407  -23.694 29.536  1.00 64.12  ? 8   GLY C N   1 
ATOM   1502 C CA  . GLY C 1 9  ? 16.746  -22.698 28.706  1.00 54.89  ? 8   GLY C CA  1 
ATOM   1503 C C   . GLY C 1 9  ? 17.670  -22.106 27.640  1.00 53.33  ? 8   GLY C C   1 
ATOM   1504 O O   . GLY C 1 9  ? 17.180  -21.484 26.697  1.00 57.44  ? 8   GLY C O   1 
ATOM   1505 N N   . ASP C 1 10 ? 18.994  -22.281 27.801  1.00 45.77  ? 9   ASP C N   1 
ATOM   1506 C CA  . ASP C 1 10 ? 19.976  -21.932 26.785  1.00 43.84  ? 9   ASP C CA  1 
ATOM   1507 C C   . ASP C 1 10 ? 19.674  -22.665 25.475  1.00 48.83  ? 9   ASP C C   1 
ATOM   1508 O O   . ASP C 1 10 ? 19.403  -23.860 25.455  1.00 44.70  ? 9   ASP C O   1 
ATOM   1509 C CB  . ASP C 1 10 ? 21.406  -22.207 27.227  1.00 46.67  ? 9   ASP C CB  1 
ATOM   1510 C CG  . ASP C 1 10 ? 22.000  -21.272 28.276  1.00 57.17  ? 9   ASP C CG  1 
ATOM   1511 O OD1 . ASP C 1 10 ? 21.252  -20.402 28.781  1.00 63.57  ? 9   ASP C OD1 1 
ATOM   1512 O OD2 . ASP C 1 10 ? 23.215  -21.418 28.585  1.00 55.73  ? 9   ASP C OD2 1 
ATOM   1513 N N   . LEU C 1 11 ? 19.725  -21.926 24.366  1.00 49.94  ? 10  LEU C N   1 
ATOM   1514 C CA  . LEU C 1 11 ? 19.384  -22.473 23.066  1.00 47.55  ? 10  LEU C CA  1 
ATOM   1515 C C   . LEU C 1 11 ? 20.657  -22.929 22.350  1.00 42.38  ? 10  LEU C C   1 
ATOM   1516 O O   . LEU C 1 11 ? 21.655  -22.218 22.306  1.00 39.74  ? 10  LEU C O   1 
ATOM   1517 C CB  . LEU C 1 11 ? 18.611  -21.405 22.290  1.00 44.31  ? 10  LEU C CB  1 
ATOM   1518 C CG  . LEU C 1 11 ? 17.285  -20.937 22.897  1.00 44.22  ? 10  LEU C CG  1 
ATOM   1519 C CD1 . LEU C 1 11 ? 16.658  -19.919 21.958  1.00 46.70  ? 10  LEU C CD1 1 
ATOM   1520 C CD2 . LEU C 1 11 ? 16.289  -22.066 23.162  1.00 46.01  ? 10  LEU C CD2 1 
ATOM   1521 N N   . VAL C 1 12 ? 20.616  -24.142 21.787  1.00 38.66  ? 11  VAL C N   1 
ATOM   1522 C CA  . VAL C 1 12 ? 21.804  -24.752 21.215  1.00 34.01  ? 11  VAL C CA  1 
ATOM   1523 C C   . VAL C 1 12 ? 21.402  -25.491 19.933  1.00 33.40  ? 11  VAL C C   1 
ATOM   1524 O O   . VAL C 1 12 ? 20.217  -25.687 19.675  1.00 31.80  ? 11  VAL C O   1 
ATOM   1525 C CB  . VAL C 1 12 ? 22.417  -25.749 22.226  1.00 35.94  ? 11  VAL C CB  1 
ATOM   1526 C CG1 . VAL C 1 12 ? 22.772  -25.114 23.577  1.00 36.56  ? 11  VAL C CG1 1 
ATOM   1527 C CG2 . VAL C 1 12 ? 21.512  -26.955 22.436  1.00 30.00  ? 11  VAL C CG2 1 
ATOM   1528 N N   . PHE C 1 13 ? 22.418  -25.895 19.155  1.00 31.28  ? 12  PHE C N   1 
ATOM   1529 C CA  . PHE C 1 13 ? 22.387  -27.052 18.276  1.00 30.81  ? 12  PHE C CA  1 
ATOM   1530 C C   . PHE C 1 13 ? 23.100  -28.218 18.970  1.00 31.55  ? 12  PHE C C   1 
ATOM   1531 O O   . PHE C 1 13 ? 24.195  -28.068 19.517  1.00 34.41  ? 12  PHE C O   1 
ATOM   1532 C CB  . PHE C 1 13 ? 23.017  -26.709 16.920  1.00 37.03  ? 12  PHE C CB  1 
ATOM   1533 C CG  . PHE C 1 13 ? 22.190  -25.775 16.047  1.00 38.47  ? 12  PHE C CG  1 
ATOM   1534 C CD1 . PHE C 1 13 ? 21.178  -26.274 15.229  1.00 36.22  ? 12  PHE C CD1 1 
ATOM   1535 C CD2 . PHE C 1 13 ? 22.430  -24.400 16.041  1.00 38.55  ? 12  PHE C CD2 1 
ATOM   1536 C CE1 . PHE C 1 13 ? 20.422  -25.416 14.442  1.00 38.40  ? 12  PHE C CE1 1 
ATOM   1537 C CE2 . PHE C 1 13 ? 21.665  -23.543 15.255  1.00 41.39  ? 12  PHE C CE2 1 
ATOM   1538 C CZ  . PHE C 1 13 ? 20.667  -24.054 14.457  1.00 41.01  ? 12  PHE C CZ  1 
ATOM   1539 N N   . ALA C 1 14 ? 22.445  -29.381 18.950  1.00 30.10  ? 13  ALA C N   1 
ATOM   1540 C CA  . ALA C 1 14 ? 22.878  -30.564 19.670  1.00 29.11  ? 13  ALA C CA  1 
ATOM   1541 C C   . ALA C 1 14 ? 23.123  -31.698 18.676  1.00 33.40  ? 13  ALA C C   1 
ATOM   1542 O O   . ALA C 1 14 ? 22.254  -32.018 17.860  1.00 28.72  ? 13  ALA C O   1 
ATOM   1543 C CB  . ALA C 1 14 ? 21.823  -30.945 20.681  1.00 31.63  ? 13  ALA C CB  1 
ATOM   1544 N N   . LYS C 1 15 ? 24.321  -32.286 18.750  1.00 33.71  ? 14  LYS C N   1 
ATOM   1545 C CA  . LYS C 1 15 ? 24.758  -33.298 17.802  1.00 35.71  ? 14  LYS C CA  1 
ATOM   1546 C C   . LYS C 1 15 ? 24.746  -34.652 18.500  1.00 36.91  ? 14  LYS C C   1 
ATOM   1547 O O   . LYS C 1 15 ? 25.418  -34.818 19.510  1.00 35.07  ? 14  LYS C O   1 
ATOM   1548 C CB  . LYS C 1 15 ? 26.206  -33.059 17.349  1.00 39.05  ? 14  LYS C CB  1 
ATOM   1549 C CG  . LYS C 1 15 ? 26.688  -34.019 16.243  1.00 41.87  ? 14  LYS C CG  1 
ATOM   1550 C CD  . LYS C 1 15 ? 25.784  -33.990 15.007  1.00 36.98  ? 14  LYS C CD  1 
ATOM   1551 C CE  . LYS C 1 15 ? 26.291  -34.824 13.825  1.00 36.63  ? 14  LYS C CE  1 
ATOM   1552 N NZ  . LYS C 1 15 ? 26.053  -36.246 14.104  1.00 32.81  ? 14  LYS C NZ  1 
ATOM   1553 N N   . MET C 1 16 ? 23.965  -35.588 17.957  1.00 35.01  ? 15  MET C N   1 
ATOM   1554 C CA  . MET C 1 16 ? 24.000  -36.981 18.362  1.00 34.82  ? 15  MET C CA  1 
ATOM   1555 C C   . MET C 1 16 ? 24.492  -37.779 17.161  1.00 37.30  ? 15  MET C C   1 
ATOM   1556 O O   . MET C 1 16 ? 24.329  -37.360 16.011  1.00 31.33  ? 15  MET C O   1 
ATOM   1557 C CB  . MET C 1 16 ? 22.607  -37.534 18.691  1.00 34.59  ? 15  MET C CB  1 
ATOM   1558 C CG  . MET C 1 16 ? 21.807  -36.725 19.689  1.00 45.61  ? 15  MET C CG  1 
ATOM   1559 S SD  . MET C 1 16 ? 20.571  -37.615 20.664  1.00 54.47  ? 15  MET C SD  1 
ATOM   1560 C CE  . MET C 1 16 ? 19.994  -39.023 19.704  1.00 67.87  ? 15  MET C CE  1 
ATOM   1561 N N   . LYS C 1 17 ? 25.070  -38.948 17.435  1.00 39.48  ? 16  LYS C N   1 
ATOM   1562 C CA  . LYS C 1 17 ? 25.496  -39.822 16.351  1.00 39.98  ? 16  LYS C CA  1 
ATOM   1563 C C   . LYS C 1 17 ? 24.242  -40.281 15.607  1.00 33.50  ? 16  LYS C C   1 
ATOM   1564 O O   . LYS C 1 17 ? 23.292  -40.793 16.210  1.00 34.78  ? 16  LYS C O   1 
ATOM   1565 C CB  . LYS C 1 17 ? 26.242  -41.035 16.929  1.00 41.08  ? 16  LYS C CB  1 
ATOM   1566 C CG  . LYS C 1 17 ? 26.882  -41.978 15.922  1.00 44.47  ? 16  LYS C CG  1 
ATOM   1567 C CD  . LYS C 1 17 ? 28.048  -41.330 15.187  1.00 49.23  ? 16  LYS C CD  1 
ATOM   1568 C CE  . LYS C 1 17 ? 28.746  -42.338 14.319  1.00 55.63  ? 16  LYS C CE  1 
ATOM   1569 N NZ  . LYS C 1 17 ? 29.955  -41.755 13.739  1.00 53.64  ? 16  LYS C NZ  1 
ATOM   1570 N N   . GLY C 1 18 ? 24.251  -40.089 14.294  1.00 32.11  ? 17  GLY C N   1 
ATOM   1571 C CA  . GLY C 1 18 ? 23.176  -40.588 13.456  1.00 32.76  ? 17  GLY C CA  1 
ATOM   1572 C C   . GLY C 1 18 ? 22.216  -39.466 13.036  1.00 36.94  ? 17  GLY C C   1 
ATOM   1573 O O   . GLY C 1 18 ? 21.188  -39.741 12.427  1.00 34.35  ? 17  GLY C O   1 
ATOM   1574 N N   . TYR C 1 19 ? 22.545  -38.211 13.382  1.00 37.26  ? 18  TYR C N   1 
ATOM   1575 C CA  . TYR C 1 19 ? 21.608  -37.098 13.239  1.00 32.50  ? 18  TYR C CA  1 
ATOM   1576 C C   . TYR C 1 19 ? 22.381  -35.821 12.956  1.00 31.26  ? 18  TYR C C   1 
ATOM   1577 O O   . TYR C 1 19 ? 23.472  -35.623 13.468  1.00 30.18  ? 18  TYR C O   1 
ATOM   1578 C CB  . TYR C 1 19 ? 20.787  -36.832 14.501  1.00 31.41  ? 18  TYR C CB  1 
ATOM   1579 C CG  . TYR C 1 19 ? 19.953  -38.042 14.872  1.00 33.72  ? 18  TYR C CG  1 
ATOM   1580 C CD1 . TYR C 1 19 ? 20.470  -39.043 15.697  1.00 30.10  ? 18  TYR C CD1 1 
ATOM   1581 C CD2 . TYR C 1 19 ? 18.667  -38.181 14.378  1.00 34.43  ? 18  TYR C CD2 1 
ATOM   1582 C CE1 . TYR C 1 19 ? 19.718  -40.160 16.008  1.00 32.99  ? 18  TYR C CE1 1 
ATOM   1583 C CE2 . TYR C 1 19 ? 17.911  -39.299 14.685  1.00 38.77  ? 18  TYR C CE2 1 
ATOM   1584 C CZ  . TYR C 1 19 ? 18.443  -40.286 15.495  1.00 37.93  ? 18  TYR C CZ  1 
ATOM   1585 O OH  . TYR C 1 19 ? 17.685  -41.375 15.808  1.00 45.29  ? 18  TYR C OH  1 
ATOM   1586 N N   . PRO C 1 20 ? 21.827  -34.928 12.118  1.00 32.47  ? 19  PRO C N   1 
ATOM   1587 C CA  . PRO C 1 20 ? 22.445  -33.626 11.868  1.00 31.40  ? 19  PRO C CA  1 
ATOM   1588 C C   . PRO C 1 20 ? 22.396  -32.780 13.152  1.00 30.69  ? 19  PRO C C   1 
ATOM   1589 O O   . PRO C 1 20 ? 21.675  -33.098 14.104  1.00 27.16  ? 19  PRO C O   1 
ATOM   1590 C CB  . PRO C 1 20 ? 21.564  -33.048 10.728  1.00 31.89  ? 19  PRO C CB  1 
ATOM   1591 C CG  . PRO C 1 20 ? 20.214  -33.717 10.941  1.00 29.70  ? 19  PRO C CG  1 
ATOM   1592 C CD  . PRO C 1 20 ? 20.536  -35.126 11.433  1.00 29.82  ? 19  PRO C CD  1 
ATOM   1593 N N   . HIS C 1 21 ? 23.248  -31.753 13.214  1.00 32.21  ? 20  HIS C N   1 
ATOM   1594 C CA  . HIS C 1 21 ? 23.220  -30.835 14.346  1.00 31.05  ? 20  HIS C CA  1 
ATOM   1595 C C   . HIS C 1 21 ? 21.792  -30.305 14.481  1.00 30.69  ? 20  HIS C C   1 
ATOM   1596 O O   . HIS C 1 21 ? 21.241  -29.772 13.508  1.00 31.64  ? 20  HIS C O   1 
ATOM   1597 C CB  . HIS C 1 21 ? 24.193  -29.680 14.114  1.00 35.27  ? 20  HIS C CB  1 
ATOM   1598 C CG  . HIS C 1 21 ? 25.615  -30.116 14.166  1.00 36.35  ? 20  HIS C CG  1 
ATOM   1599 N ND1 . HIS C 1 21 ? 26.262  -30.713 13.107  1.00 40.49  ? 20  HIS C ND1 1 
ATOM   1600 C CD2 . HIS C 1 21 ? 26.505  -30.048 15.169  1.00 43.18  ? 20  HIS C CD2 1 
ATOM   1601 C CE1 . HIS C 1 21 ? 27.504  -30.998 13.473  1.00 43.27  ? 20  HIS C CE1 1 
ATOM   1602 N NE2 . HIS C 1 21 ? 27.673  -30.591 14.720  1.00 39.85  ? 20  HIS C NE2 1 
ATOM   1603 N N   . TRP C 1 22 ? 21.208  -30.455 15.681  1.00 28.36  ? 21  TRP C N   1 
ATOM   1604 C CA  . TRP C 1 22 ? 19.763  -30.344 15.828  1.00 28.46  ? 21  TRP C CA  1 
ATOM   1605 C C   . TRP C 1 22 ? 19.424  -29.183 16.758  1.00 29.43  ? 21  TRP C C   1 
ATOM   1606 O O   . TRP C 1 22 ? 20.022  -29.045 17.829  1.00 30.55  ? 21  TRP C O   1 
ATOM   1607 C CB  . TRP C 1 22 ? 19.164  -31.655 16.367  1.00 31.83  ? 21  TRP C CB  1 
ATOM   1608 C CG  . TRP C 1 22 ? 17.707  -31.859 16.010  1.00 30.04  ? 21  TRP C CG  1 
ATOM   1609 C CD1 . TRP C 1 22 ? 16.610  -31.279 16.595  1.00 29.24  ? 21  TRP C CD1 1 
ATOM   1610 C CD2 . TRP C 1 22 ? 17.200  -32.735 14.970  1.00 27.67  ? 21  TRP C CD2 1 
ATOM   1611 N NE1 . TRP C 1 22 ? 15.462  -31.719 15.979  1.00 27.11  ? 21  TRP C NE1 1 
ATOM   1612 C CE2 . TRP C 1 22 ? 15.790  -32.614 14.988  1.00 27.92  ? 21  TRP C CE2 1 
ATOM   1613 C CE3 . TRP C 1 22 ? 17.793  -33.597 14.032  1.00 26.18  ? 21  TRP C CE3 1 
ATOM   1614 C CZ2 . TRP C 1 22 ? 14.991  -33.335 14.094  1.00 29.15  ? 21  TRP C CZ2 1 
ATOM   1615 C CZ3 . TRP C 1 22 ? 17.002  -34.305 13.145  1.00 26.59  ? 21  TRP C CZ3 1 
ATOM   1616 C CH2 . TRP C 1 22 ? 15.612  -34.189 13.198  1.00 27.31  ? 21  TRP C CH2 1 
ATOM   1617 N N   . PRO C 1 23 ? 18.448  -28.324 16.380  1.00 29.30  ? 22  PRO C N   1 
ATOM   1618 C CA  . PRO C 1 23 ? 18.009  -27.240 17.254  1.00 28.95  ? 22  PRO C CA  1 
ATOM   1619 C C   . PRO C 1 23 ? 17.402  -27.809 18.535  1.00 27.43  ? 22  PRO C C   1 
ATOM   1620 O O   . PRO C 1 23 ? 16.557  -28.695 18.499  1.00 28.15  ? 22  PRO C O   1 
ATOM   1621 C CB  . PRO C 1 23 ? 16.975  -26.534 16.362  1.00 27.16  ? 22  PRO C CB  1 
ATOM   1622 C CG  . PRO C 1 23 ? 16.419  -27.645 15.478  1.00 27.05  ? 22  PRO C CG  1 
ATOM   1623 C CD  . PRO C 1 23 ? 17.722  -28.341 15.086  1.00 29.52  ? 22  PRO C CD  1 
ATOM   1624 N N   . ALA C 1 24 ? 17.851  -27.286 19.674  1.00 29.20  ? 23  ALA C N   1 
ATOM   1625 C CA  . ALA C 1 24 ? 17.483  -27.831 20.969  1.00 29.66  ? 23  ALA C CA  1 
ATOM   1626 C C   . ALA C 1 24 ? 17.676  -26.759 22.046  1.00 32.89  ? 23  ALA C C   1 
ATOM   1627 O O   . ALA C 1 24 ? 18.174  -25.676 21.758  1.00 33.70  ? 23  ALA C O   1 
ATOM   1628 C CB  . ALA C 1 24 ? 18.378  -29.039 21.248  1.00 27.57  ? 23  ALA C CB  1 
ATOM   1629 N N   . ARG C 1 25 ? 17.328  -27.086 23.299  1.00 36.94  ? 24  ARG C N   1 
ATOM   1630 C CA  . ARG C 1 25 ? 17.711  -26.270 24.444  1.00 38.04  ? 24  ARG C CA  1 
ATOM   1631 C C   . ARG C 1 25 ? 18.131  -27.175 25.607  1.00 38.42  ? 24  ARG C C   1 
ATOM   1632 O O   . ARG C 1 25 ? 17.794  -28.362 25.631  1.00 37.48  ? 24  ARG C O   1 
ATOM   1633 C CB  . ARG C 1 25 ? 16.511  -25.440 24.918  1.00 40.21  ? 24  ARG C CB  1 
ATOM   1634 C CG  . ARG C 1 25 ? 15.240  -26.206 25.259  1.00 42.07  ? 24  ARG C CG  1 
ATOM   1635 C CD  . ARG C 1 25 ? 14.191  -25.300 25.930  1.00 47.04  ? 24  ARG C CD  1 
ATOM   1636 N NE  . ARG C 1 25 ? 13.028  -26.114 26.308  1.00 53.32  ? 24  ARG C NE  1 
ATOM   1637 C CZ  . ARG C 1 25 ? 11.755  -25.934 25.969  1.00 58.54  ? 24  ARG C CZ  1 
ATOM   1638 N NH1 . ARG C 1 25 ? 11.369  -24.843 25.330  1.00 56.44  ? 24  ARG C NH1 1 
ATOM   1639 N NH2 . ARG C 1 25 ? 10.857  -26.849 26.295  1.00 63.69  ? 24  ARG C NH2 1 
ATOM   1640 N N   . ILE C 1 26 ? 18.806  -26.575 26.592  1.00 39.76  ? 25  ILE C N   1 
ATOM   1641 C CA  . ILE C 1 26 ? 19.147  -27.205 27.861  1.00 46.25  ? 25  ILE C CA  1 
ATOM   1642 C C   . ILE C 1 26 ? 17.893  -27.271 28.736  1.00 51.71  ? 25  ILE C C   1 
ATOM   1643 O O   . ILE C 1 26 ? 17.155  -26.294 28.872  1.00 53.47  ? 25  ILE C O   1 
ATOM   1644 C CB  . ILE C 1 26 ? 20.269  -26.412 28.562  1.00 46.40  ? 25  ILE C CB  1 
ATOM   1645 C CG1 . ILE C 1 26 ? 21.360  -25.951 27.606  1.00 47.17  ? 25  ILE C CG1 1 
ATOM   1646 C CG2 . ILE C 1 26 ? 20.848  -27.163 29.762  1.00 47.23  ? 25  ILE C CG2 1 
ATOM   1647 C CD1 . ILE C 1 26 ? 22.403  -26.994 27.252  1.00 47.86  ? 25  ILE C CD1 1 
ATOM   1648 N N   . ASP C 1 27 ? 17.661  -28.441 29.332  1.00 55.25  ? 26  ASP C N   1 
ATOM   1649 C CA  . ASP C 1 27 ? 16.570  -28.635 30.273  1.00 62.70  ? 26  ASP C CA  1 
ATOM   1650 C C   . ASP C 1 27 ? 17.041  -28.469 31.717  1.00 69.63  ? 26  ASP C C   1 
ATOM   1651 O O   . ASP C 1 27 ? 18.240  -28.409 31.981  1.00 74.37  ? 26  ASP C O   1 
ATOM   1652 C CB  . ASP C 1 27 ? 15.924  -29.997 30.092  1.00 66.35  ? 26  ASP C CB  1 
ATOM   1653 C CG  . ASP C 1 27 ? 14.607  -29.971 29.340  1.00 69.00  ? 26  ASP C CG  1 
ATOM   1654 O OD1 . ASP C 1 27 ? 14.282  -28.880 28.812  1.00 63.46  ? 26  ASP C OD1 1 
ATOM   1655 O OD2 . ASP C 1 27 ? 13.913  -31.021 29.340  1.00 61.60  ? 26  ASP C OD2 1 
ATOM   1656 N N   . ASP C 1 28 ? 16.062  -28.398 32.635  1.00 80.63  ? 27  ASP C N   1 
ATOM   1657 C CA  . ASP C 1 28 ? 16.261  -28.464 34.075  1.00 73.27  ? 27  ASP C CA  1 
ATOM   1658 C C   . ASP C 1 28 ? 16.340  -29.932 34.482  1.00 77.35  ? 27  ASP C C   1 
ATOM   1659 O O   . ASP C 1 28 ? 15.990  -30.802 33.691  1.00 84.13  ? 27  ASP C O   1 
ATOM   1660 C CB  . ASP C 1 28 ? 15.091  -27.829 34.810  1.00 75.99  ? 27  ASP C CB  1 
ATOM   1661 N N   . ILE C 1 29 ? 16.799  -30.195 35.714  1.00 79.99  ? 28  ILE C N   1 
ATOM   1662 C CA  . ILE C 1 29 ? 16.681  -31.515 36.315  1.00 78.45  ? 28  ILE C CA  1 
ATOM   1663 C C   . ILE C 1 29 ? 15.673  -31.429 37.477  1.00 80.19  ? 28  ILE C C   1 
ATOM   1664 O O   . ILE C 1 29 ? 15.162  -32.498 37.892  1.00 85.21  ? 28  ILE C O   1 
ATOM   1665 C CB  . ILE C 1 29 ? 18.055  -32.038 36.776  1.00 77.21  ? 28  ILE C CB  1 
ATOM   1666 N N   . LYS C 1 35 ? 19.344  -38.944 37.768  1.00 68.04  ? 34  LYS C N   1 
ATOM   1667 C CA  . LYS C 1 35 ? 20.333  -37.842 37.610  1.00 68.48  ? 34  LYS C CA  1 
ATOM   1668 C C   . LYS C 1 35 ? 21.126  -38.083 36.325  1.00 66.42  ? 34  LYS C C   1 
ATOM   1669 O O   . LYS C 1 35 ? 21.243  -39.228 35.882  1.00 60.41  ? 34  LYS C O   1 
ATOM   1670 C CB  . LYS C 1 35 ? 21.212  -37.715 38.864  1.00 67.01  ? 34  LYS C CB  1 
ATOM   1671 N N   . PRO C 1 36 ? 21.693  -37.028 35.682  1.00 65.21  ? 35  PRO C N   1 
ATOM   1672 C CA  . PRO C 1 36 ? 22.441  -37.207 34.437  1.00 63.33  ? 35  PRO C CA  1 
ATOM   1673 C C   . PRO C 1 36 ? 23.679  -38.086 34.632  1.00 66.20  ? 35  PRO C C   1 
ATOM   1674 O O   . PRO C 1 36 ? 24.252  -38.149 35.724  1.00 57.07  ? 35  PRO C O   1 
ATOM   1675 C CB  . PRO C 1 36 ? 22.819  -35.776 33.975  1.00 64.85  ? 35  PRO C CB  1 
ATOM   1676 C CG  . PRO C 1 36 ? 22.066  -34.834 34.896  1.00 63.47  ? 35  PRO C CG  1 
ATOM   1677 C CD  . PRO C 1 36 ? 21.675  -35.626 36.136  1.00 65.48  ? 35  PRO C CD  1 
ATOM   1678 N N   . PRO C 1 37 ? 24.135  -38.813 33.588  1.00 61.09  ? 36  PRO C N   1 
ATOM   1679 C CA  . PRO C 1 37 ? 25.490  -39.368 33.599  1.00 59.15  ? 36  PRO C CA  1 
ATOM   1680 C C   . PRO C 1 37 ? 26.493  -38.248 33.884  1.00 57.84  ? 36  PRO C C   1 
ATOM   1681 O O   . PRO C 1 37 ? 26.191  -37.072 33.653  1.00 51.63  ? 36  PRO C O   1 
ATOM   1682 C CB  . PRO C 1 37 ? 25.648  -39.981 32.197  1.00 52.45  ? 36  PRO C CB  1 
ATOM   1683 C CG  . PRO C 1 37 ? 24.223  -40.280 31.779  1.00 53.46  ? 36  PRO C CG  1 
ATOM   1684 C CD  . PRO C 1 37 ? 23.367  -39.182 32.391  1.00 58.25  ? 36  PRO C CD  1 
ATOM   1685 N N   . PRO C 1 38 ? 27.676  -38.570 34.467  1.00 51.82  ? 37  PRO C N   1 
ATOM   1686 C CA  . PRO C 1 38 ? 28.708  -37.570 34.739  1.00 51.77  ? 37  PRO C CA  1 
ATOM   1687 C C   . PRO C 1 38 ? 28.945  -36.666 33.539  1.00 47.07  ? 37  PRO C C   1 
ATOM   1688 O O   . PRO C 1 38 ? 29.188  -37.151 32.430  1.00 43.96  ? 37  PRO C O   1 
ATOM   1689 C CB  . PRO C 1 38 ? 29.932  -38.452 35.058  1.00 51.60  ? 37  PRO C CB  1 
ATOM   1690 C CG  . PRO C 1 38 ? 29.321  -39.644 35.755  1.00 53.18  ? 37  PRO C CG  1 
ATOM   1691 C CD  . PRO C 1 38 ? 28.056  -39.912 34.949  1.00 53.09  ? 37  PRO C CD  1 
ATOM   1692 N N   . ASN C 1 39 ? 28.781  -35.359 33.782  1.00 43.16  ? 38  ASN C N   1 
ATOM   1693 C CA  . ASN C 1 39 ? 29.179  -34.316 32.851  1.00 44.10  ? 38  ASN C CA  1 
ATOM   1694 C C   . ASN C 1 39 ? 28.262  -34.290 31.621  1.00 45.14  ? 38  ASN C C   1 
ATOM   1695 O O   . ASN C 1 39 ? 28.690  -33.836 30.557  1.00 49.06  ? 38  ASN C O   1 
ATOM   1696 C CB  . ASN C 1 39 ? 30.634  -34.501 32.443  1.00 44.96  ? 38  ASN C CB  1 
ATOM   1697 C CG  . ASN C 1 39 ? 31.202  -33.270 31.779  1.00 60.45  ? 38  ASN C CG  1 
ATOM   1698 O OD1 . ASN C 1 39 ? 30.692  -32.158 31.970  1.00 67.07  ? 38  ASN C OD1 1 
ATOM   1699 N ND2 . ASN C 1 39 ? 32.256  -33.448 30.999  1.00 64.18  ? 38  ASN C ND2 1 
ATOM   1700 N N   . LYS C 1 40 ? 27.014  -34.772 31.758  1.00 39.07  ? 39  LYS C N   1 
ATOM   1701 C CA  . LYS C 1 40 ? 26.051  -34.688 30.666  1.00 39.64  ? 39  LYS C CA  1 
ATOM   1702 C C   . LYS C 1 40 ? 24.932  -33.714 31.033  1.00 40.91  ? 39  LYS C C   1 
ATOM   1703 O O   . LYS C 1 40 ? 24.504  -33.656 32.180  1.00 44.45  ? 39  LYS C O   1 
ATOM   1704 C CB  . LYS C 1 40 ? 25.417  -36.050 30.356  1.00 37.22  ? 39  LYS C CB  1 
ATOM   1705 C CG  . LYS C 1 40 ? 26.413  -37.158 30.080  1.00 39.03  ? 39  LYS C CG  1 
ATOM   1706 C CD  . LYS C 1 40 ? 27.027  -37.106 28.693  1.00 41.82  ? 39  LYS C CD  1 
ATOM   1707 C CE  . LYS C 1 40 ? 27.955  -38.263 28.472  1.00 45.77  ? 39  LYS C CE  1 
ATOM   1708 N NZ  . LYS C 1 40 ? 28.967  -37.894 27.471  1.00 50.76  ? 39  LYS C NZ  1 
ATOM   1709 N N   . TYR C 1 41 ? 24.460  -32.956 30.039  1.00 38.34  ? 40  TYR C N   1 
ATOM   1710 C CA  . TYR C 1 41 ? 23.333  -32.046 30.205  1.00 36.88  ? 40  TYR C CA  1 
ATOM   1711 C C   . TYR C 1 41 ? 22.071  -32.707 29.665  1.00 39.25  ? 40  TYR C C   1 
ATOM   1712 O O   . TYR C 1 41 ? 22.136  -33.483 28.701  1.00 39.17  ? 40  TYR C O   1 
ATOM   1713 C CB  . TYR C 1 41 ? 23.522  -30.827 29.295  1.00 35.80  ? 40  TYR C CB  1 
ATOM   1714 C CG  . TYR C 1 41 ? 24.653  -29.906 29.711  1.00 39.98  ? 40  TYR C CG  1 
ATOM   1715 C CD1 . TYR C 1 41 ? 25.953  -30.101 29.245  1.00 43.68  ? 40  TYR C CD1 1 
ATOM   1716 C CD2 . TYR C 1 41 ? 24.413  -28.838 30.573  1.00 38.40  ? 40  TYR C CD2 1 
ATOM   1717 C CE1 . TYR C 1 41 ? 26.983  -29.262 29.636  1.00 48.51  ? 40  TYR C CE1 1 
ATOM   1718 C CE2 . TYR C 1 41 ? 25.433  -27.978 30.943  1.00 45.95  ? 40  TYR C CE2 1 
ATOM   1719 C CZ  . TYR C 1 41 ? 26.716  -28.196 30.481  1.00 47.47  ? 40  TYR C CZ  1 
ATOM   1720 O OH  . TYR C 1 41 ? 27.710  -27.350 30.862  1.00 57.84  ? 40  TYR C OH  1 
ATOM   1721 N N   . PRO C 1 42 ? 20.889  -32.394 30.248  1.00 40.30  ? 41  PRO C N   1 
ATOM   1722 C CA  . PRO C 1 42 ? 19.614  -32.849 29.695  1.00 37.99  ? 41  PRO C CA  1 
ATOM   1723 C C   . PRO C 1 42 ? 19.259  -31.906 28.546  1.00 38.14  ? 41  PRO C C   1 
ATOM   1724 O O   . PRO C 1 42 ? 19.261  -30.686 28.715  1.00 35.42  ? 41  PRO C O   1 
ATOM   1725 C CB  . PRO C 1 42 ? 18.640  -32.756 30.863  1.00 35.56  ? 41  PRO C CB  1 
ATOM   1726 C CG  . PRO C 1 42 ? 19.226  -31.676 31.738  1.00 39.26  ? 41  PRO C CG  1 
ATOM   1727 C CD  . PRO C 1 42 ? 20.722  -31.581 31.467  1.00 40.12  ? 41  PRO C CD  1 
ATOM   1728 N N   . ILE C 1 43 ? 18.991  -32.505 27.379  1.00 37.39  ? 42  ILE C N   1 
ATOM   1729 C CA  . ILE C 1 43 ? 18.665  -31.782 26.160  1.00 35.76  ? 42  ILE C CA  1 
ATOM   1730 C C   . ILE C 1 43 ? 17.216  -32.074 25.787  1.00 38.53  ? 42  ILE C C   1 
ATOM   1731 O O   . ILE C 1 43 ? 16.770  -33.222 25.815  1.00 39.01  ? 42  ILE C O   1 
ATOM   1732 C CB  . ILE C 1 43 ? 19.638  -32.179 25.028  1.00 33.99  ? 42  ILE C CB  1 
ATOM   1733 C CG1 . ILE C 1 43 ? 21.109  -31.901 25.443  1.00 34.14  ? 42  ILE C CG1 1 
ATOM   1734 C CG2 . ILE C 1 43 ? 19.280  -31.500 23.693  1.00 32.76  ? 42  ILE C CG2 1 
ATOM   1735 C CD1 . ILE C 1 43 ? 21.388  -30.471 25.869  1.00 33.57  ? 42  ILE C CD1 1 
ATOM   1736 N N   . PHE C 1 44 ? 16.493  -31.019 25.396  1.00 38.29  ? 43  PHE C N   1 
ATOM   1737 C CA  . PHE C 1 44 ? 15.218  -31.185 24.722  1.00 31.30  ? 43  PHE C CA  1 
ATOM   1738 C C   . PHE C 1 44 ? 15.407  -30.769 23.266  1.00 28.58  ? 43  PHE C C   1 
ATOM   1739 O O   . PHE C 1 44 ? 15.924  -29.687 23.008  1.00 32.98  ? 43  PHE C O   1 
ATOM   1740 C CB  . PHE C 1 44 ? 14.274  -30.167 25.367  1.00 31.53  ? 43  PHE C CB  1 
ATOM   1741 C CG  . PHE C 1 44 ? 12.892  -30.134 24.732  1.00 34.66  ? 43  PHE C CG  1 
ATOM   1742 C CD1 . PHE C 1 44 ? 11.930  -31.096 25.064  1.00 38.96  ? 43  PHE C CD1 1 
ATOM   1743 C CD2 . PHE C 1 44 ? 12.542  -29.115 23.841  1.00 37.01  ? 43  PHE C CD2 1 
ATOM   1744 C CE1 . PHE C 1 44 ? 10.655  -31.061 24.499  1.00 42.44  ? 43  PHE C CE1 1 
ATOM   1745 C CE2 . PHE C 1 44 ? 11.277  -29.091 23.264  1.00 35.63  ? 43  PHE C CE2 1 
ATOM   1746 C CZ  . PHE C 1 44 ? 10.331  -30.052 23.604  1.00 41.71  ? 43  PHE C CZ  1 
ATOM   1747 N N   . PHE C 1 45 ? 14.947  -31.603 22.332  1.00 30.48  ? 44  PHE C N   1 
ATOM   1748 C CA  . PHE C 1 45 ? 15.106  -31.359 20.910  1.00 29.39  ? 44  PHE C CA  1 
ATOM   1749 C C   . PHE C 1 45 ? 13.849  -30.697 20.365  1.00 33.08  ? 44  PHE C C   1 
ATOM   1750 O O   . PHE C 1 45 ? 12.756  -31.217 20.563  1.00 32.52  ? 44  PHE C O   1 
ATOM   1751 C CB  . PHE C 1 45 ? 15.342  -32.686 20.196  1.00 29.86  ? 44  PHE C CB  1 
ATOM   1752 C CG  . PHE C 1 45 ? 16.734  -33.229 20.472  1.00 30.36  ? 44  PHE C CG  1 
ATOM   1753 C CD1 . PHE C 1 45 ? 17.818  -32.787 19.722  1.00 30.10  ? 44  PHE C CD1 1 
ATOM   1754 C CD2 . PHE C 1 45 ? 16.958  -34.141 21.508  1.00 33.89  ? 44  PHE C CD2 1 
ATOM   1755 C CE1 . PHE C 1 45 ? 19.091  -33.298 19.959  1.00 32.73  ? 44  PHE C CE1 1 
ATOM   1756 C CE2 . PHE C 1 45 ? 18.235  -34.650 21.745  1.00 34.89  ? 44  PHE C CE2 1 
ATOM   1757 C CZ  . PHE C 1 45 ? 19.290  -34.222 20.976  1.00 36.42  ? 44  PHE C CZ  1 
ATOM   1758 N N   . PHE C 1 46 ? 14.015  -29.551 19.681  1.00 32.30  ? 45  PHE C N   1 
ATOM   1759 C CA  . PHE C 1 46 ? 12.867  -28.912 19.055  1.00 30.36  ? 45  PHE C CA  1 
ATOM   1760 C C   . PHE C 1 46 ? 12.383  -29.776 17.897  1.00 31.70  ? 45  PHE C C   1 
ATOM   1761 O O   . PHE C 1 46 ? 13.167  -30.523 17.314  1.00 31.22  ? 45  PHE C O   1 
ATOM   1762 C CB  . PHE C 1 46 ? 13.104  -27.465 18.600  1.00 29.23  ? 45  PHE C CB  1 
ATOM   1763 C CG  . PHE C 1 46 ? 13.409  -26.500 19.731  1.00 29.67  ? 45  PHE C CG  1 
ATOM   1764 C CD1 . PHE C 1 46 ? 12.389  -26.057 20.574  1.00 32.72  ? 45  PHE C CD1 1 
ATOM   1765 C CD2 . PHE C 1 46 ? 14.712  -26.066 19.965  1.00 29.36  ? 45  PHE C CD2 1 
ATOM   1766 C CE1 . PHE C 1 46 ? 12.675  -25.190 21.627  1.00 33.40  ? 45  PHE C CE1 1 
ATOM   1767 C CE2 . PHE C 1 46 ? 14.983  -25.173 20.998  1.00 30.78  ? 45  PHE C CE2 1 
ATOM   1768 C CZ  . PHE C 1 46 ? 13.966  -24.740 21.831  1.00 29.64  ? 45  PHE C CZ  1 
ATOM   1769 N N   . GLY C 1 47 ? 11.084  -29.662 17.578  1.00 32.68  ? 46  GLY C N   1 
ATOM   1770 C CA  . GLY C 1 47 ? 10.550  -30.371 16.424  1.00 36.94  ? 46  GLY C CA  1 
ATOM   1771 C C   . GLY C 1 47 ? 10.124  -31.788 16.802  1.00 40.89  ? 46  GLY C C   1 
ATOM   1772 O O   . GLY C 1 47 ? 8.944   -32.128 16.704  1.00 39.50  ? 46  GLY C O   1 
ATOM   1773 N N   . THR C 1 48 ? 11.077  -32.615 17.247  1.00 39.66  ? 47  THR C N   1 
ATOM   1774 C CA  . THR C 1 48 ? 10.690  -33.952 17.683  1.00 39.06  ? 47  THR C CA  1 
ATOM   1775 C C   . THR C 1 48 ? 10.164  -33.911 19.117  1.00 38.21  ? 47  THR C C   1 
ATOM   1776 O O   . THR C 1 48 ? 9.364   -34.770 19.492  1.00 44.42  ? 47  THR C O   1 
ATOM   1777 C CB  . THR C 1 48 ? 11.807  -34.984 17.541  1.00 37.81  ? 47  THR C CB  1 
ATOM   1778 O OG1 . THR C 1 48 ? 12.713  -34.545 18.544  1.00 36.52  ? 47  THR C OG1 1 
ATOM   1779 C CG2 . THR C 1 48 ? 12.425  -35.033 16.155  1.00 36.70  ? 47  THR C CG2 1 
ATOM   1780 N N   . HIS C 1 49 ? 10.620  -32.930 19.909  1.00 33.73  ? 48  HIS C N   1 
ATOM   1781 C CA  . HIS C 1 49 ? 10.247  -32.793 21.316  1.00 40.43  ? 48  HIS C CA  1 
ATOM   1782 C C   . HIS C 1 49 ? 10.682  -34.006 22.141  1.00 40.68  ? 48  HIS C C   1 
ATOM   1783 O O   . HIS C 1 49 ? 9.984   -34.403 23.065  1.00 38.85  ? 48  HIS C O   1 
ATOM   1784 C CB  . HIS C 1 49 ? 8.742   -32.541 21.501  1.00 40.31  ? 48  HIS C CB  1 
ATOM   1785 C CG  . HIS C 1 49 ? 8.201   -31.495 20.581  1.00 43.32  ? 48  HIS C CG  1 
ATOM   1786 N ND1 . HIS C 1 49 ? 7.076   -31.706 19.810  1.00 45.84  ? 48  HIS C ND1 1 
ATOM   1787 C CD2 . HIS C 1 49 ? 8.657   -30.273 20.256  1.00 40.70  ? 48  HIS C CD2 1 
ATOM   1788 C CE1 . HIS C 1 49 ? 6.856   -30.631 19.061  1.00 49.92  ? 48  HIS C CE1 1 
ATOM   1789 N NE2 . HIS C 1 49 ? 7.801   -29.750 19.320  1.00 49.61  ? 48  HIS C NE2 1 
ATOM   1790 N N   . GLU C 1 50 ? 11.854  -34.569 21.838  1.00 40.20  ? 49  GLU C N   1 
ATOM   1791 C CA  . GLU C 1 50 ? 12.334  -35.693 22.629  1.00 42.94  ? 49  GLU C CA  1 
ATOM   1792 C C   . GLU C 1 50 ? 13.515  -35.231 23.476  1.00 40.78  ? 49  GLU C C   1 
ATOM   1793 O O   . GLU C 1 50 ? 13.978  -34.100 23.337  1.00 37.53  ? 49  GLU C O   1 
ATOM   1794 C CB  . GLU C 1 50 ? 12.550  -36.907 21.733  1.00 49.51  ? 49  GLU C CB  1 
ATOM   1795 C CG  . GLU C 1 50 ? 13.658  -36.705 20.708  1.00 67.32  ? 49  GLU C CG  1 
ATOM   1796 C CD  . GLU C 1 50 ? 14.140  -37.999 20.091  1.00 74.32  ? 49  GLU C CD  1 
ATOM   1797 O OE1 . GLU C 1 50 ? 13.298  -38.760 19.561  1.00 76.26  ? 49  GLU C OE1 1 
ATOM   1798 O OE2 . GLU C 1 50 ? 15.368  -38.230 20.161  1.00 80.73  ? 49  GLU C OE2 1 
ATOM   1799 N N   . THR C 1 51 ? 13.952  -36.078 24.415  1.00 42.44  ? 50  THR C N   1 
ATOM   1800 C CA  . THR C 1 51 ? 15.004  -35.675 25.341  1.00 41.20  ? 50  THR C CA  1 
ATOM   1801 C C   . THR C 1 51 ? 16.187  -36.642 25.240  1.00 37.90  ? 50  THR C C   1 
ATOM   1802 O O   . THR C 1 51 ? 16.056  -37.750 24.724  1.00 37.40  ? 50  THR C O   1 
ATOM   1803 C CB  . THR C 1 51 ? 14.479  -35.540 26.775  1.00 45.55  ? 50  THR C CB  1 
ATOM   1804 O OG1 . THR C 1 51 ? 13.861  -36.793 27.055  1.00 45.81  ? 50  THR C OG1 1 
ATOM   1805 C CG2 . THR C 1 51 ? 13.557  -34.347 26.997  1.00 40.49  ? 50  THR C CG2 1 
ATOM   1806 N N   . ALA C 1 52 ? 17.361  -36.188 25.688  1.00 37.65  ? 51  ALA C N   1 
ATOM   1807 C CA  . ALA C 1 52 ? 18.535  -37.044 25.790  1.00 37.88  ? 51  ALA C CA  1 
ATOM   1808 C C   . ALA C 1 52 ? 19.575  -36.357 26.661  1.00 41.83  ? 51  ALA C C   1 
ATOM   1809 O O   . ALA C 1 52 ? 19.379  -35.223 27.084  1.00 42.23  ? 51  ALA C O   1 
ATOM   1810 C CB  . ALA C 1 52 ? 19.092  -37.398 24.422  1.00 36.38  ? 51  ALA C CB  1 
ATOM   1811 N N   . PHE C 1 53 ? 20.664  -37.076 26.951  1.00 45.26  ? 52  PHE C N   1 
ATOM   1812 C CA  . PHE C 1 53 ? 21.770  -36.536 27.722  1.00 42.99  ? 52  PHE C CA  1 
ATOM   1813 C C   . PHE C 1 53 ? 22.945  -36.385 26.778  1.00 41.74  ? 52  PHE C C   1 
ATOM   1814 O O   . PHE C 1 53 ? 23.355  -37.356 26.146  1.00 42.85  ? 52  PHE C O   1 
ATOM   1815 C CB  . PHE C 1 53 ? 22.191  -37.512 28.826  1.00 39.90  ? 52  PHE C CB  1 
ATOM   1816 C CG  . PHE C 1 53 ? 21.240  -37.448 30.007  1.00 39.94  ? 52  PHE C CG  1 
ATOM   1817 C CD1 . PHE C 1 53 ? 20.994  -36.238 30.652  1.00 41.99  ? 52  PHE C CD1 1 
ATOM   1818 C CD2 . PHE C 1 53 ? 20.567  -38.586 30.442  1.00 48.54  ? 52  PHE C CD2 1 
ATOM   1819 C CE1 . PHE C 1 53 ? 20.111  -36.168 31.723  1.00 45.71  ? 52  PHE C CE1 1 
ATOM   1820 C CE2 . PHE C 1 53 ? 19.689  -38.516 31.520  1.00 50.62  ? 52  PHE C CE2 1 
ATOM   1821 C CZ  . PHE C 1 53 ? 19.447  -37.303 32.146  1.00 47.42  ? 52  PHE C CZ  1 
ATOM   1822 N N   . LEU C 1 54 ? 23.469  -35.166 26.689  1.00 37.84  ? 53  LEU C N   1 
ATOM   1823 C CA  . LEU C 1 54 ? 24.618  -34.943 25.831  1.00 36.51  ? 53  LEU C CA  1 
ATOM   1824 C C   . LEU C 1 54 ? 25.725  -34.265 26.627  1.00 37.38  ? 53  LEU C C   1 
ATOM   1825 O O   . LEU C 1 54 ? 25.441  -33.522 27.562  1.00 35.18  ? 53  LEU C O   1 
ATOM   1826 C CB  . LEU C 1 54 ? 24.257  -34.166 24.565  1.00 35.16  ? 53  LEU C CB  1 
ATOM   1827 C CG  . LEU C 1 54 ? 23.413  -34.918 23.527  1.00 42.30  ? 53  LEU C CG  1 
ATOM   1828 C CD1 . LEU C 1 54 ? 23.028  -33.996 22.390  1.00 37.20  ? 53  LEU C CD1 1 
ATOM   1829 C CD2 . LEU C 1 54 ? 24.175  -36.103 22.955  1.00 46.09  ? 53  LEU C CD2 1 
ATOM   1830 N N   . GLY C 1 55 ? 26.973  -34.559 26.236  1.00 37.17  ? 54  GLY C N   1 
ATOM   1831 C CA  . GLY C 1 55 ? 28.158  -33.891 26.745  1.00 37.08  ? 54  GLY C CA  1 
ATOM   1832 C C   . GLY C 1 55 ? 28.366  -32.550 26.043  1.00 44.96  ? 54  GLY C C   1 
ATOM   1833 O O   . GLY C 1 55 ? 27.871  -32.331 24.927  1.00 41.47  ? 54  GLY C O   1 
ATOM   1834 N N   . PRO C 1 56 ? 29.117  -31.614 26.666  1.00 45.29  ? 55  PRO C N   1 
ATOM   1835 C CA  . PRO C 1 56 ? 29.146  -30.228 26.197  1.00 50.29  ? 55  PRO C CA  1 
ATOM   1836 C C   . PRO C 1 56 ? 29.852  -30.107 24.847  1.00 45.26  ? 55  PRO C C   1 
ATOM   1837 O O   . PRO C 1 56 ? 29.620  -29.155 24.102  1.00 51.34  ? 55  PRO C O   1 
ATOM   1838 C CB  . PRO C 1 56 ? 29.861  -29.474 27.343  1.00 50.94  ? 55  PRO C CB  1 
ATOM   1839 C CG  . PRO C 1 56 ? 30.766  -30.531 27.955  1.00 48.71  ? 55  PRO C CG  1 
ATOM   1840 C CD  . PRO C 1 56 ? 30.005  -31.849 27.819  1.00 50.19  ? 55  PRO C CD  1 
ATOM   1841 N N   . LYS C 1 57 ? 30.690  -31.102 24.542  1.00 43.98  ? 56  LYS C N   1 
ATOM   1842 C CA  . LYS C 1 57 ? 31.311  -31.286 23.241  1.00 46.17  ? 56  LYS C CA  1 
ATOM   1843 C C   . LYS C 1 57 ? 30.263  -31.281 22.129  1.00 49.54  ? 56  LYS C C   1 
ATOM   1844 O O   . LYS C 1 57 ? 30.533  -30.847 21.010  1.00 48.72  ? 56  LYS C O   1 
ATOM   1845 C CB  . LYS C 1 57 ? 31.941  -32.683 23.156  1.00 46.39  ? 56  LYS C CB  1 
ATOM   1846 N N   . ASP C 1 58 ? 29.081  -31.817 22.434  1.00 46.67  ? 57  ASP C N   1 
ATOM   1847 C CA  . ASP C 1 58 ? 28.090  -32.084 21.409  1.00 47.21  ? 57  ASP C CA  1 
ATOM   1848 C C   . ASP C 1 58 ? 27.136  -30.908 21.258  1.00 40.77  ? 57  ASP C C   1 
ATOM   1849 O O   . ASP C 1 58 ? 26.149  -31.016 20.538  1.00 40.86  ? 57  ASP C O   1 
ATOM   1850 C CB  . ASP C 1 58 ? 27.324  -33.352 21.727  1.00 47.41  ? 57  ASP C CB  1 
ATOM   1851 C CG  . ASP C 1 58 ? 28.197  -34.590 21.806  1.00 46.51  ? 57  ASP C CG  1 
ATOM   1852 O OD1 . ASP C 1 58 ? 29.135  -34.667 21.000  1.00 47.31  ? 57  ASP C OD1 1 
ATOM   1853 O OD2 . ASP C 1 58 ? 27.903  -35.463 22.645  1.00 49.54  ? 57  ASP C OD2 1 
ATOM   1854 N N   . LEU C 1 59 ? 27.438  -29.799 21.939  1.00 35.01  ? 58  LEU C N   1 
ATOM   1855 C CA  . LEU C 1 59 ? 26.515  -28.679 22.048  1.00 39.98  ? 58  LEU C CA  1 
ATOM   1856 C C   . LEU C 1 59 ? 27.164  -27.402 21.524  1.00 43.98  ? 58  LEU C C   1 
ATOM   1857 O O   . LEU C 1 59 ? 28.379  -27.235 21.657  1.00 48.23  ? 58  LEU C O   1 
ATOM   1858 C CB  . LEU C 1 59 ? 26.129  -28.531 23.518  1.00 37.54  ? 58  LEU C CB  1 
ATOM   1859 C CG  . LEU C 1 59 ? 25.514  -29.766 24.182  1.00 36.33  ? 58  LEU C CG  1 
ATOM   1860 C CD1 . LEU C 1 59 ? 25.267  -29.428 25.636  1.00 37.12  ? 58  LEU C CD1 1 
ATOM   1861 C CD2 . LEU C 1 59 ? 24.207  -30.177 23.501  1.00 32.16  ? 58  LEU C CD2 1 
ATOM   1862 N N   . PHE C 1 60 ? 26.327  -26.521 20.946  1.00 43.35  ? 59  PHE C N   1 
ATOM   1863 C CA  . PHE C 1 60 ? 26.747  -25.324 20.223  1.00 42.35  ? 59  PHE C CA  1 
ATOM   1864 C C   . PHE C 1 60 ? 25.750  -24.199 20.502  1.00 41.74  ? 59  PHE C C   1 
ATOM   1865 O O   . PHE C 1 60 ? 24.556  -24.345 20.236  1.00 38.48  ? 59  PHE C O   1 
ATOM   1866 C CB  . PHE C 1 60 ? 26.934  -25.601 18.725  1.00 41.42  ? 59  PHE C CB  1 
ATOM   1867 C CG  . PHE C 1 60 ? 27.908  -26.727 18.395  1.00 41.96  ? 59  PHE C CG  1 
ATOM   1868 C CD1 . PHE C 1 60 ? 27.481  -28.054 18.352  1.00 41.97  ? 59  PHE C CD1 1 
ATOM   1869 C CD2 . PHE C 1 60 ? 29.253  -26.459 18.119  1.00 45.51  ? 59  PHE C CD2 1 
ATOM   1870 C CE1 . PHE C 1 60 ? 28.367  -29.086 18.072  1.00 38.55  ? 59  PHE C CE1 1 
ATOM   1871 C CE2 . PHE C 1 60 ? 30.143  -27.496 17.840  1.00 43.26  ? 59  PHE C CE2 1 
ATOM   1872 C CZ  . PHE C 1 60 ? 29.697  -28.805 17.809  1.00 46.13  ? 59  PHE C CZ  1 
ATOM   1873 N N   . PRO C 1 61 ? 26.186  -23.054 21.093  1.00 44.52  ? 60  PRO C N   1 
ATOM   1874 C CA  . PRO C 1 61 ? 25.286  -21.921 21.328  1.00 43.65  ? 60  PRO C CA  1 
ATOM   1875 C C   . PRO C 1 61 ? 24.588  -21.540 20.025  1.00 43.22  ? 60  PRO C C   1 
ATOM   1876 O O   . PRO C 1 61 ? 25.231  -21.431 18.978  1.00 44.52  ? 60  PRO C O   1 
ATOM   1877 C CB  . PRO C 1 61 ? 26.174  -20.779 21.877  1.00 44.30  ? 60  PRO C CB  1 
ATOM   1878 C CG  . PRO C 1 61 ? 27.477  -21.451 22.265  1.00 41.52  ? 60  PRO C CG  1 
ATOM   1879 C CD  . PRO C 1 61 ? 27.562  -22.786 21.545  1.00 46.09  ? 60  PRO C CD  1 
ATOM   1880 N N   . TYR C 1 62 ? 23.263  -21.362 20.132  1.00 45.64  ? 61  TYR C N   1 
ATOM   1881 C CA  . TYR C 1 62 ? 22.351  -21.146 19.019  1.00 47.50  ? 61  TYR C CA  1 
ATOM   1882 C C   . TYR C 1 62 ? 22.777  -19.933 18.192  1.00 54.09  ? 61  TYR C C   1 
ATOM   1883 O O   . TYR C 1 62 ? 22.882  -20.031 16.967  1.00 53.33  ? 61  TYR C O   1 
ATOM   1884 C CB  . TYR C 1 62 ? 20.930  -20.910 19.539  1.00 43.35  ? 61  TYR C CB  1 
ATOM   1885 C CG  . TYR C 1 62 ? 19.943  -20.612 18.424  1.00 46.82  ? 61  TYR C CG  1 
ATOM   1886 C CD1 . TYR C 1 62 ? 19.836  -21.452 17.314  1.00 45.23  ? 61  TYR C CD1 1 
ATOM   1887 C CD2 . TYR C 1 62 ? 19.162  -19.459 18.466  1.00 47.58  ? 61  TYR C CD2 1 
ATOM   1888 C CE1 . TYR C 1 62 ? 18.951  -21.159 16.285  1.00 49.25  ? 61  TYR C CE1 1 
ATOM   1889 C CE2 . TYR C 1 62 ? 18.271  -19.163 17.450  1.00 48.12  ? 61  TYR C CE2 1 
ATOM   1890 C CZ  . TYR C 1 62 ? 18.174  -20.011 16.357  1.00 44.18  ? 61  TYR C CZ  1 
ATOM   1891 O OH  . TYR C 1 62 ? 17.283  -19.695 15.383  1.00 41.09  ? 61  TYR C OH  1 
ATOM   1892 N N   . ASP C 1 63 ? 23.027  -18.808 18.878  1.00 54.71  ? 62  ASP C N   1 
ATOM   1893 C CA  . ASP C 1 63 ? 23.293  -17.538 18.215  1.00 60.90  ? 62  ASP C CA  1 
ATOM   1894 C C   . ASP C 1 63 ? 24.666  -17.548 17.553  1.00 55.21  ? 62  ASP C C   1 
ATOM   1895 O O   . ASP C 1 63 ? 24.850  -16.922 16.513  1.00 64.84  ? 62  ASP C O   1 
ATOM   1896 C CB  . ASP C 1 63 ? 22.980  -16.346 19.106  1.00 69.95  ? 62  ASP C CB  1 
ATOM   1897 C CG  . ASP C 1 63 ? 21.536  -15.869 19.022  1.00 85.83  ? 62  ASP C CG  1 
ATOM   1898 O OD1 . ASP C 1 63 ? 20.785  -16.089 19.998  1.00 84.63  ? 62  ASP C OD1 1 
ATOM   1899 O OD2 . ASP C 1 63 ? 21.167  -15.289 17.971  1.00 89.12  ? 62  ASP C OD2 1 
ATOM   1900 N N   . LYS C 1 64 ? 25.609  -18.290 18.137  1.00 49.21  ? 63  LYS C N   1 
ATOM   1901 C CA  . LYS C 1 64 ? 26.959  -18.378 17.600  1.00 47.53  ? 63  LYS C CA  1 
ATOM   1902 C C   . LYS C 1 64 ? 26.998  -19.249 16.344  1.00 48.67  ? 63  LYS C C   1 
ATOM   1903 O O   . LYS C 1 64 ? 27.788  -18.969 15.443  1.00 41.30  ? 63  LYS C O   1 
ATOM   1904 C CB  . LYS C 1 64 ? 27.948  -18.887 18.656  1.00 51.48  ? 63  LYS C CB  1 
ATOM   1905 N N   . SER C 1 65 ? 26.142  -20.288 16.268  1.00 45.75  ? 64  SER C N   1 
ATOM   1906 C CA  . SER C 1 65 ? 26.340  -21.325 15.260  1.00 41.61  ? 64  SER C CA  1 
ATOM   1907 C C   . SER C 1 65 ? 25.180  -21.421 14.255  1.00 40.16  ? 64  SER C C   1 
ATOM   1908 O O   . SER C 1 65 ? 25.235  -22.213 13.316  1.00 37.62  ? 64  SER C O   1 
ATOM   1909 C CB  . SER C 1 65 ? 26.639  -22.661 15.922  1.00 48.02  ? 64  SER C CB  1 
ATOM   1910 O OG  . SER C 1 65 ? 25.492  -23.129 16.633  1.00 44.54  ? 64  SER C OG  1 
ATOM   1911 N N   . LYS C 1 66 ? 24.118  -20.629 14.441  1.00 39.62  ? 65  LYS C N   1 
ATOM   1912 C CA  . LYS C 1 66 ? 22.935  -20.772 13.595  1.00 43.15  ? 65  LYS C CA  1 
ATOM   1913 C C   . LYS C 1 66 ? 23.247  -20.544 12.115  1.00 45.14  ? 65  LYS C C   1 
ATOM   1914 O O   . LYS C 1 66 ? 22.717  -21.265 11.273  1.00 46.95  ? 65  LYS C O   1 
ATOM   1915 C CB  . LYS C 1 66 ? 21.716  -19.950 14.025  1.00 42.65  ? 65  LYS C CB  1 
ATOM   1916 C CG  . LYS C 1 66 ? 21.917  -18.446 14.000  1.00 39.72  ? 65  LYS C CG  1 
ATOM   1917 C CD  . LYS C 1 66 ? 20.618  -17.750 14.377  1.00 48.51  ? 65  LYS C CD  1 
ATOM   1918 C CE  . LYS C 1 66 ? 20.762  -16.265 14.456  1.00 51.43  ? 65  LYS C CE  1 
ATOM   1919 N NZ  . LYS C 1 66 ? 19.648  -15.773 15.263  1.00 56.93  ? 65  LYS C NZ  1 
ATOM   1920 N N   . ASP C 1 67 ? 24.108  -19.569 11.794  1.00 42.32  ? 66  ASP C N   1 
ATOM   1921 C CA  . ASP C 1 67 ? 24.521  -19.333 10.410  1.00 44.11  ? 66  ASP C CA  1 
ATOM   1922 C C   . ASP C 1 67 ? 25.019  -20.632 9.771   1.00 42.28  ? 66  ASP C C   1 
ATOM   1923 O O   . ASP C 1 67 ? 24.833  -20.845 8.573   1.00 40.84  ? 66  ASP C O   1 
ATOM   1924 C CB  . ASP C 1 67 ? 25.462  -18.138 10.253  1.00 48.59  ? 66  ASP C CB  1 
ATOM   1925 C CG  . ASP C 1 67 ? 26.823  -18.232 10.938  1.00 60.84  ? 66  ASP C CG  1 
ATOM   1926 O OD1 . ASP C 1 67 ? 27.096  -19.268 11.596  1.00 63.60  ? 66  ASP C OD1 1 
ATOM   1927 O OD2 . ASP C 1 67 ? 27.608  -17.255 10.828  1.00 61.13  ? 66  ASP C OD2 1 
ATOM   1928 N N   . LYS C 1 68 ? 25.612  -21.520 10.585  1.00 38.34  ? 67  LYS C N   1 
ATOM   1929 C CA  . LYS C 1 68 ? 26.157  -22.782 10.090  1.00 42.85  ? 67  LYS C CA  1 
ATOM   1930 C C   . LYS C 1 68 ? 25.129  -23.931 10.112  1.00 42.20  ? 67  LYS C C   1 
ATOM   1931 O O   . LYS C 1 68 ? 24.997  -24.653 9.124   1.00 44.25  ? 67  LYS C O   1 
ATOM   1932 C CB  . LYS C 1 68 ? 27.466  -23.067 10.833  1.00 41.18  ? 67  LYS C CB  1 
ATOM   1933 C CG  . LYS C 1 68 ? 28.212  -24.362 10.547  1.00 51.35  ? 67  LYS C CG  1 
ATOM   1934 C CD  . LYS C 1 68 ? 29.555  -24.303 11.278  1.00 56.83  ? 67  LYS C CD  1 
ATOM   1935 C CE  . LYS C 1 68 ? 30.191  -25.623 11.623  1.00 61.56  ? 67  LYS C CE  1 
ATOM   1936 N NZ  . LYS C 1 68 ? 30.574  -26.455 10.479  1.00 69.56  ? 67  LYS C NZ  1 
ATOM   1937 N N   . TYR C 1 69 ? 24.417  -24.131 11.234  1.00 35.55  ? 68  TYR C N   1 
ATOM   1938 C CA  . TYR C 1 69 ? 23.566  -25.309 11.369  1.00 34.36  ? 68  TYR C CA  1 
ATOM   1939 C C   . TYR C 1 69 ? 22.097  -24.959 11.130  1.00 35.65  ? 68  TYR C C   1 
ATOM   1940 O O   . TYR C 1 69 ? 21.280  -25.854 10.983  1.00 34.44  ? 68  TYR C O   1 
ATOM   1941 C CB  . TYR C 1 69 ? 23.722  -25.939 12.758  1.00 33.08  ? 68  TYR C CB  1 
ATOM   1942 C CG  . TYR C 1 69 ? 25.138  -26.389 13.076  1.00 36.24  ? 68  TYR C CG  1 
ATOM   1943 C CD1 . TYR C 1 69 ? 25.875  -27.180 12.195  1.00 37.10  ? 68  TYR C CD1 1 
ATOM   1944 C CD2 . TYR C 1 69 ? 25.749  -25.985 14.258  1.00 39.66  ? 68  TYR C CD2 1 
ATOM   1945 C CE1 . TYR C 1 69 ? 27.168  -27.593 12.503  1.00 35.02  ? 68  TYR C CE1 1 
ATOM   1946 C CE2 . TYR C 1 69 ? 27.042  -26.375 14.568  1.00 38.52  ? 68  TYR C CE2 1 
ATOM   1947 C CZ  . TYR C 1 69 ? 27.749  -27.179 13.691  1.00 38.15  ? 68  TYR C CZ  1 
ATOM   1948 O OH  . TYR C 1 69 ? 29.021  -27.523 14.055  1.00 43.90  ? 68  TYR C OH  1 
ATOM   1949 N N   . GLY C 1 70 ? 21.758  -23.663 11.156  1.00 32.60  ? 69  GLY C N   1 
ATOM   1950 C CA  . GLY C 1 70 ? 20.365  -23.254 11.046  1.00 38.89  ? 69  GLY C CA  1 
ATOM   1951 C C   . GLY C 1 70 ? 19.986  -23.106 9.580   1.00 41.23  ? 69  GLY C C   1 
ATOM   1952 O O   . GLY C 1 70 ? 19.974  -22.006 9.031   1.00 40.64  ? 69  GLY C O   1 
ATOM   1953 N N   . LYS C 1 71 ? 19.763  -24.249 8.942   1.00 40.13  ? 70  LYS C N   1 
ATOM   1954 C CA  . LYS C 1 71 ? 19.444  -24.318 7.527   1.00 40.61  ? 70  LYS C CA  1 
ATOM   1955 C C   . LYS C 1 71 ? 18.577  -25.557 7.384   1.00 39.39  ? 70  LYS C C   1 
ATOM   1956 O O   . LYS C 1 71 ? 18.815  -26.539 8.082   1.00 38.49  ? 70  LYS C O   1 
ATOM   1957 C CB  . LYS C 1 71 ? 20.723  -24.462 6.690   1.00 41.24  ? 70  LYS C CB  1 
ATOM   1958 C CG  . LYS C 1 71 ? 21.710  -25.502 7.231   1.00 50.86  ? 70  LYS C CG  1 
ATOM   1959 C CD  . LYS C 1 71 ? 22.904  -25.933 6.383   1.00 55.25  ? 70  LYS C CD  1 
ATOM   1960 C CE  . LYS C 1 71 ? 23.795  -26.895 7.131   1.00 57.29  ? 70  LYS C CE  1 
ATOM   1961 N N   . PRO C 1 72 ? 17.534  -25.557 6.525   1.00 35.99  ? 71  PRO C N   1 
ATOM   1962 C CA  . PRO C 1 72 ? 16.614  -26.687 6.493   1.00 32.14  ? 71  PRO C CA  1 
ATOM   1963 C C   . PRO C 1 72 ? 17.273  -28.026 6.172   1.00 35.12  ? 71  PRO C C   1 
ATOM   1964 O O   . PRO C 1 72 ? 18.329  -28.096 5.542   1.00 33.21  ? 71  PRO C O   1 
ATOM   1965 C CB  . PRO C 1 72 ? 15.655  -26.247 5.390   1.00 32.59  ? 71  PRO C CB  1 
ATOM   1966 C CG  . PRO C 1 72 ? 15.660  -24.745 5.540   1.00 33.80  ? 71  PRO C CG  1 
ATOM   1967 C CD  . PRO C 1 72 ? 17.155  -24.470 5.604   1.00 31.64  ? 71  PRO C CD  1 
ATOM   1968 N N   . ASN C 1 73 ? 16.607  -29.095 6.593   1.00 35.50  ? 72  ASN C N   1 
ATOM   1969 C CA  . ASN C 1 73 ? 16.862  -30.374 5.965   1.00 38.88  ? 72  ASN C CA  1 
ATOM   1970 C C   . ASN C 1 73 ? 15.638  -31.249 6.165   1.00 33.24  ? 72  ASN C C   1 
ATOM   1971 O O   . ASN C 1 73 ? 14.681  -30.836 6.815   1.00 31.25  ? 72  ASN C O   1 
ATOM   1972 C CB  . ASN C 1 73 ? 18.201  -31.005 6.335   1.00 46.11  ? 72  ASN C CB  1 
ATOM   1973 C CG  . ASN C 1 73 ? 18.171  -31.605 7.715   1.00 45.88  ? 72  ASN C CG  1 
ATOM   1974 O OD1 . ASN C 1 73 ? 17.450  -32.582 7.976   1.00 43.55  ? 72  ASN C OD1 1 
ATOM   1975 N ND2 . ASN C 1 73 ? 18.942  -31.009 8.605   1.00 46.10  ? 72  ASN C ND2 1 
ATOM   1976 N N   . LYS C 1 74 ? 15.696  -32.436 5.556   1.00 37.71  ? 73  LYS C N   1 
ATOM   1977 C CA  . LYS C 1 74 ? 14.500  -33.219 5.301   1.00 37.06  ? 73  LYS C CA  1 
ATOM   1978 C C   . LYS C 1 74 ? 14.262  -34.208 6.437   1.00 38.79  ? 73  LYS C C   1 
ATOM   1979 O O   . LYS C 1 74 ? 13.303  -34.967 6.373   1.00 39.74  ? 73  LYS C O   1 
ATOM   1980 C CB  . LYS C 1 74 ? 14.597  -33.849 3.900   1.00 40.60  ? 73  LYS C CB  1 
ATOM   1981 N N   . ARG C 1 75 ? 15.114  -34.205 7.475   1.00 35.50  ? 74  ARG C N   1 
ATOM   1982 C CA  . ARG C 1 75 ? 14.926  -35.172 8.555   1.00 35.31  ? 74  ARG C CA  1 
ATOM   1983 C C   . ARG C 1 75 ? 13.646  -34.842 9.313   1.00 39.43  ? 74  ARG C C   1 
ATOM   1984 O O   . ARG C 1 75 ? 13.333  -33.661 9.540   1.00 33.85  ? 74  ARG C O   1 
ATOM   1985 C CB  . ARG C 1 75 ? 16.092  -35.362 9.537   1.00 36.52  ? 74  ARG C CB  1 
ATOM   1986 C CG  . ARG C 1 75 ? 17.460  -35.469 8.868   1.00 42.39  ? 74  ARG C CG  1 
ATOM   1987 C CD  . ARG C 1 75 ? 17.815  -36.806 8.184   1.00 43.88  ? 74  ARG C CD  1 
ATOM   1988 N NE  . ARG C 1 75 ? 17.823  -37.853 9.211   1.00 40.93  ? 74  ARG C NE  1 
ATOM   1989 C CZ  . ARG C 1 75 ? 18.908  -38.326 9.833   1.00 37.29  ? 74  ARG C CZ  1 
ATOM   1990 N NH1 . ARG C 1 75 ? 18.774  -39.039 10.932  1.00 38.25  ? 74  ARG C NH1 1 
ATOM   1991 N NH2 . ARG C 1 75 ? 20.107  -38.011 9.392   1.00 36.09  ? 74  ARG C NH2 1 
ATOM   1992 N N   . LYS C 1 76 ? 12.936  -35.915 9.696   1.00 39.34  ? 75  LYS C N   1 
ATOM   1993 C CA  . LYS C 1 76 ? 11.663  -35.822 10.395  1.00 38.88  ? 75  LYS C CA  1 
ATOM   1994 C C   . LYS C 1 76 ? 11.774  -34.837 11.557  1.00 35.90  ? 75  LYS C C   1 
ATOM   1995 O O   . LYS C 1 76 ? 12.582  -35.010 12.474  1.00 34.10  ? 75  LYS C O   1 
ATOM   1996 C CB  . LYS C 1 76 ? 11.062  -37.174 10.824  1.00 41.93  ? 75  LYS C CB  1 
ATOM   1997 C CG  . LYS C 1 76 ? 9.524   -37.212 10.773  1.00 47.48  ? 75  LYS C CG  1 
ATOM   1998 C CD  . LYS C 1 76 ? 8.824   -38.208 11.702  1.00 51.48  ? 75  LYS C CD  1 
ATOM   1999 N N   . GLY C 1 77 ? 10.929  -33.804 11.510  1.00 33.84  ? 76  GLY C N   1 
ATOM   2000 C CA  . GLY C 1 77 ? 10.772  -32.926 12.659  1.00 32.38  ? 76  GLY C CA  1 
ATOM   2001 C C   . GLY C 1 77 ? 11.735  -31.739 12.597  1.00 29.36  ? 76  GLY C C   1 
ATOM   2002 O O   . GLY C 1 77 ? 11.593  -30.808 13.372  1.00 30.26  ? 76  GLY C O   1 
ATOM   2003 N N   . PHE C 1 78 ? 12.726  -31.775 11.693  1.00 31.91  ? 77  PHE C N   1 
ATOM   2004 C CA  . PHE C 1 78 ? 13.819  -30.810 11.753  1.00 29.97  ? 77  PHE C CA  1 
ATOM   2005 C C   . PHE C 1 78 ? 13.323  -29.380 11.485  1.00 32.39  ? 77  PHE C C   1 
ATOM   2006 O O   . PHE C 1 78 ? 13.688  -28.438 12.197  1.00 32.11  ? 77  PHE C O   1 
ATOM   2007 C CB  . PHE C 1 78 ? 14.930  -31.131 10.748  1.00 30.00  ? 77  PHE C CB  1 
ATOM   2008 C CG  . PHE C 1 78 ? 16.215  -30.350 11.021  1.00 32.25  ? 77  PHE C CG  1 
ATOM   2009 C CD1 . PHE C 1 78 ? 16.417  -29.082 10.491  1.00 34.23  ? 77  PHE C CD1 1 
ATOM   2010 C CD2 . PHE C 1 78 ? 17.239  -30.911 11.779  1.00 32.37  ? 77  PHE C CD2 1 
ATOM   2011 C CE1 . PHE C 1 78 ? 17.596  -28.381 10.736  1.00 33.25  ? 77  PHE C CE1 1 
ATOM   2012 C CE2 . PHE C 1 78 ? 18.411  -30.200 12.039  1.00 32.85  ? 77  PHE C CE2 1 
ATOM   2013 C CZ  . PHE C 1 78 ? 18.592  -28.942 11.516  1.00 34.83  ? 77  PHE C CZ  1 
ATOM   2014 N N   . ASN C 1 79 ? 12.561  -29.209 10.404  1.00 32.57  ? 78  ASN C N   1 
ATOM   2015 C CA  . ASN C 1 79 ? 12.199  -27.867 9.959   1.00 34.96  ? 78  ASN C CA  1 
ATOM   2016 C C   . ASN C 1 79 ? 11.212  -27.252 10.944  1.00 31.82  ? 78  ASN C C   1 
ATOM   2017 O O   . ASN C 1 79 ? 11.264  -26.057 11.263  1.00 28.39  ? 78  ASN C O   1 
ATOM   2018 C CB  . ASN C 1 79 ? 11.765  -27.876 8.497   1.00 32.00  ? 78  ASN C CB  1 
ATOM   2019 C CG  . ASN C 1 79 ? 12.935  -28.235 7.612   1.00 30.04  ? 78  ASN C CG  1 
ATOM   2020 O OD1 . ASN C 1 79 ? 14.087  -27.962 7.973   1.00 30.73  ? 78  ASN C OD1 1 
ATOM   2021 N ND2 . ASN C 1 79 ? 12.674  -28.767 6.430   1.00 30.57  ? 78  ASN C ND2 1 
ATOM   2022 N N   . GLU C 1 80 ? 10.332  -28.096 11.465  1.00 32.21  ? 79  GLU C N   1 
ATOM   2023 C CA  . GLU C 1 80 ? 9.442   -27.614 12.505  1.00 32.73  ? 79  GLU C CA  1 
ATOM   2024 C C   . GLU C 1 80 ? 10.257  -27.140 13.703  1.00 37.38  ? 79  GLU C C   1 
ATOM   2025 O O   . GLU C 1 80 ? 9.892   -26.146 14.334  1.00 37.73  ? 79  GLU C O   1 
ATOM   2026 C CB  . GLU C 1 80 ? 8.474   -28.709 12.947  1.00 35.89  ? 79  GLU C CB  1 
ATOM   2027 C CG  . GLU C 1 80 ? 7.551   -28.225 14.063  1.00 37.97  ? 79  GLU C CG  1 
ATOM   2028 C CD  . GLU C 1 80 ? 6.303   -29.075 14.170  1.00 52.46  ? 79  GLU C CD  1 
ATOM   2029 O OE1 . GLU C 1 80 ? 6.283   -30.178 13.577  1.00 51.93  ? 79  GLU C OE1 1 
ATOM   2030 O OE2 . GLU C 1 80 ? 5.337   -28.615 14.822  1.00 53.01  ? 79  GLU C OE2 1 
ATOM   2031 N N   . GLY C 1 81 ? 11.347  -27.876 14.005  1.00 34.83  ? 80  GLY C N   1 
ATOM   2032 C CA  . GLY C 1 81 ? 12.252  -27.528 15.096  1.00 31.24  ? 80  GLY C CA  1 
ATOM   2033 C C   . GLY C 1 81 ? 12.968  -26.202 14.869  1.00 31.00  ? 80  GLY C C   1 
ATOM   2034 O O   . GLY C 1 81 ? 13.189  -25.449 15.818  1.00 31.16  ? 80  GLY C O   1 
ATOM   2035 N N   . LEU C 1 82 ? 13.360  -25.938 13.611  1.00 30.79  ? 81  LEU C N   1 
ATOM   2036 C CA  . LEU C 1 82 ? 13.951  -24.641 13.289  1.00 33.85  ? 81  LEU C CA  1 
ATOM   2037 C C   . LEU C 1 82 ? 12.938  -23.525 13.551  1.00 32.68  ? 81  LEU C C   1 
ATOM   2038 O O   . LEU C 1 82 ? 13.314  -22.435 13.991  1.00 32.42  ? 81  LEU C O   1 
ATOM   2039 C CB  . LEU C 1 82 ? 14.496  -24.550 11.863  1.00 33.73  ? 81  LEU C CB  1 
ATOM   2040 C CG  . LEU C 1 82 ? 15.697  -25.434 11.512  1.00 30.55  ? 81  LEU C CG  1 
ATOM   2041 C CD1 . LEU C 1 82 ? 15.890  -25.338 9.999   1.00 31.34  ? 81  LEU C CD1 1 
ATOM   2042 C CD2 . LEU C 1 82 ? 16.940  -24.967 12.217  1.00 29.29  ? 81  LEU C CD2 1 
ATOM   2043 N N   . TRP C 1 83 ? 11.663  -23.783 13.246  1.00 33.59  ? 82  TRP C N   1 
ATOM   2044 C CA  . TRP C 1 83 ? 10.638  -22.772 13.500  1.00 38.79  ? 82  TRP C CA  1 
ATOM   2045 C C   . TRP C 1 83 ? 10.484  -22.487 15.003  1.00 41.49  ? 82  TRP C C   1 
ATOM   2046 O O   . TRP C 1 83 ? 10.336  -21.332 15.419  1.00 38.81  ? 82  TRP C O   1 
ATOM   2047 C CB  . TRP C 1 83 ? 9.293   -23.140 12.859  1.00 37.12  ? 82  TRP C CB  1 
ATOM   2048 C CG  . TRP C 1 83 ? 8.309   -21.999 12.963  1.00 45.24  ? 82  TRP C CG  1 
ATOM   2049 C CD1 . TRP C 1 83 ? 8.098   -20.999 12.057  1.00 44.33  ? 82  TRP C CD1 1 
ATOM   2050 C CD2 . TRP C 1 83 ? 7.443   -21.712 14.084  1.00 45.94  ? 82  TRP C CD2 1 
ATOM   2051 N NE1 . TRP C 1 83 ? 7.146   -20.130 12.517  1.00 42.45  ? 82  TRP C NE1 1 
ATOM   2052 C CE2 . TRP C 1 83 ? 6.730   -20.535 13.758  1.00 44.76  ? 82  TRP C CE2 1 
ATOM   2053 C CE3 . TRP C 1 83 ? 7.199   -22.335 15.319  1.00 43.69  ? 82  TRP C CE3 1 
ATOM   2054 C CZ2 . TRP C 1 83 ? 5.797   -19.975 14.626  1.00 46.93  ? 82  TRP C CZ2 1 
ATOM   2055 C CZ3 . TRP C 1 83 ? 6.282   -21.775 16.183  1.00 45.69  ? 82  TRP C CZ3 1 
ATOM   2056 C CH2 . TRP C 1 83 ? 5.596   -20.607 15.837  1.00 50.02  ? 82  TRP C CH2 1 
ATOM   2057 N N   . GLU C 1 84 ? 10.551  -23.544 15.820  1.00 38.78  ? 83  GLU C N   1 
ATOM   2058 C CA  . GLU C 1 84 ? 10.346  -23.431 17.257  1.00 38.64  ? 83  GLU C CA  1 
ATOM   2059 C C   . GLU C 1 84 ? 11.468  -22.637 17.896  1.00 37.34  ? 83  GLU C C   1 
ATOM   2060 O O   . GLU C 1 84 ? 11.186  -21.771 18.725  1.00 37.40  ? 83  GLU C O   1 
ATOM   2061 C CB  . GLU C 1 84 ? 10.207  -24.788 17.945  1.00 33.21  ? 83  GLU C CB  1 
ATOM   2062 C CG  . GLU C 1 84 ? 8.911   -25.460 17.525  1.00 35.09  ? 83  GLU C CG  1 
ATOM   2063 C CD  . GLU C 1 84 ? 8.812   -26.873 18.050  1.00 38.89  ? 83  GLU C CD  1 
ATOM   2064 O OE1 . GLU C 1 84 ? 9.791   -27.296 18.695  1.00 37.99  ? 83  GLU C OE1 1 
ATOM   2065 O OE2 . GLU C 1 84 ? 7.780   -27.538 17.788  1.00 37.24  ? 83  GLU C OE2 1 
ATOM   2066 N N   . ILE C 1 85 ? 12.722  -22.921 17.494  1.00 34.45  ? 84  ILE C N   1 
ATOM   2067 C CA  . ILE C 1 85 ? 13.868  -22.336 18.177  1.00 34.21  ? 84  ILE C CA  1 
ATOM   2068 C C   . ILE C 1 85 ? 13.996  -20.837 17.880  1.00 39.80  ? 84  ILE C C   1 
ATOM   2069 O O   . ILE C 1 85 ? 14.609  -20.118 18.668  1.00 37.48  ? 84  ILE C O   1 
ATOM   2070 C CB  . ILE C 1 85 ? 15.174  -23.106 17.914  1.00 31.41  ? 84  ILE C CB  1 
ATOM   2071 C CG1 . ILE C 1 85 ? 16.314  -22.651 18.864  1.00 32.20  ? 84  ILE C CG1 1 
ATOM   2072 C CG2 . ILE C 1 85 ? 15.593  -23.058 16.439  1.00 31.97  ? 84  ILE C CG2 1 
ATOM   2073 C CD1 . ILE C 1 85 ? 17.540  -23.559 18.859  1.00 34.54  ? 84  ILE C CD1 1 
ATOM   2074 N N   . GLN C 1 86 ? 13.414  -20.388 16.755  1.00 40.14  ? 85  GLN C N   1 
ATOM   2075 C CA  . GLN C 1 86 ? 13.443  -18.990 16.333  1.00 40.19  ? 85  GLN C CA  1 
ATOM   2076 C C   . GLN C 1 86 ? 12.242  -18.224 16.887  1.00 38.35  ? 85  GLN C C   1 
ATOM   2077 O O   . GLN C 1 86 ? 12.402  -17.071 17.276  1.00 39.98  ? 85  GLN C O   1 
ATOM   2078 C CB  . GLN C 1 86 ? 13.496  -18.877 14.803  1.00 40.55  ? 85  GLN C CB  1 
ATOM   2079 C CG  . GLN C 1 86 ? 13.742  -17.465 14.266  1.00 42.19  ? 85  GLN C CG  1 
ATOM   2080 C CD  . GLN C 1 86 ? 14.192  -17.441 12.811  1.00 42.27  ? 85  GLN C CD  1 
ATOM   2081 O OE1 . GLN C 1 86 ? 14.053  -18.411 12.052  1.00 42.11  ? 85  GLN C OE1 1 
ATOM   2082 N NE2 . GLN C 1 86 ? 14.770  -16.320 12.408  1.00 44.72  ? 85  GLN C NE2 1 
ATOM   2083 N N   . ASN C 1 87 ? 11.081  -18.892 16.950  1.00 41.12  ? 86  ASN C N   1 
ATOM   2084 C CA  . ASN C 1 87 ? 9.762   -18.280 17.076  1.00 49.01  ? 86  ASN C CA  1 
ATOM   2085 C C   . ASN C 1 87 ? 9.061   -18.611 18.401  1.00 49.71  ? 86  ASN C C   1 
ATOM   2086 O O   . ASN C 1 87 ? 8.180   -17.874 18.823  1.00 49.84  ? 86  ASN C O   1 
ATOM   2087 C CB  . ASN C 1 87 ? 8.882   -18.599 15.867  1.00 42.26  ? 86  ASN C CB  1 
ATOM   2088 C CG  . ASN C 1 87 ? 9.484   -18.008 14.611  1.00 47.32  ? 86  ASN C CG  1 
ATOM   2089 O OD1 . ASN C 1 87 ? 9.583   -16.781 14.508  1.00 43.86  ? 86  ASN C OD1 1 
ATOM   2090 N ND2 . ASN C 1 87 ? 9.975   -18.839 13.695  1.00 41.34  ? 86  ASN C ND2 1 
ATOM   2091 N N   . ASN C 1 88 ? 9.400   -19.732 19.049  1.00 47.05  ? 87  ASN C N   1 
ATOM   2092 C CA  . ASN C 1 88 ? 8.666   -20.130 20.251  1.00 46.19  ? 87  ASN C CA  1 
ATOM   2093 C C   . ASN C 1 88 ? 9.576   -20.993 21.119  1.00 43.96  ? 87  ASN C C   1 
ATOM   2094 O O   . ASN C 1 88 ? 9.235   -22.139 21.419  1.00 49.73  ? 87  ASN C O   1 
ATOM   2095 C CB  . ASN C 1 88 ? 7.376   -20.875 19.893  1.00 48.55  ? 87  ASN C CB  1 
ATOM   2096 C CG  . ASN C 1 88 ? 6.362   -20.952 21.016  1.00 54.04  ? 87  ASN C CG  1 
ATOM   2097 O OD1 . ASN C 1 88 ? 6.518   -20.295 22.052  1.00 56.81  ? 87  ASN C OD1 1 
ATOM   2098 N ND2 . ASN C 1 88 ? 5.319   -21.753 20.833  1.00 52.63  ? 87  ASN C ND2 1 
ATOM   2099 N N   . PRO C 1 89 ? 10.775  -20.501 21.507  1.00 42.59  ? 88  PRO C N   1 
ATOM   2100 C CA  . PRO C 1 89 ? 11.795  -21.366 22.094  1.00 44.30  ? 88  PRO C CA  1 
ATOM   2101 C C   . PRO C 1 89 ? 11.575  -21.815 23.535  1.00 49.55  ? 88  PRO C C   1 
ATOM   2102 O O   . PRO C 1 89 ? 12.348  -22.642 24.031  1.00 50.91  ? 88  PRO C O   1 
ATOM   2103 C CB  . PRO C 1 89 ? 13.096  -20.561 21.922  1.00 39.97  ? 88  PRO C CB  1 
ATOM   2104 C CG  . PRO C 1 89 ? 12.642  -19.118 21.977  1.00 42.25  ? 88  PRO C CG  1 
ATOM   2105 C CD  . PRO C 1 89 ? 11.235  -19.109 21.372  1.00 42.02  ? 88  PRO C CD  1 
ATOM   2106 N N   . HIS C 1 90 ? 10.525  -21.288 24.186  1.00 48.93  ? 89  HIS C N   1 
ATOM   2107 C CA  . HIS C 1 90 ? 10.280  -21.620 25.583  1.00 47.59  ? 89  HIS C CA  1 
ATOM   2108 C C   . HIS C 1 90 ? 8.831   -22.043 25.835  1.00 51.49  ? 89  HIS C C   1 
ATOM   2109 O O   . HIS C 1 90 ? 8.360   -21.986 26.966  1.00 56.64  ? 89  HIS C O   1 
ATOM   2110 C CB  . HIS C 1 90 ? 10.872  -20.566 26.526  1.00 42.55  ? 89  HIS C CB  1 
ATOM   2111 C CG  . HIS C 1 90 ? 12.303  -20.157 26.285  1.00 42.59  ? 89  HIS C CG  1 
ATOM   2112 N ND1 . HIS C 1 90 ? 12.640  -18.900 25.823  1.00 46.97  ? 89  HIS C ND1 1 
ATOM   2113 C CD2 . HIS C 1 90 ? 13.481  -20.772 26.514  1.00 42.14  ? 89  HIS C CD2 1 
ATOM   2114 C CE1 . HIS C 1 90 ? 13.969  -18.785 25.731  1.00 43.31  ? 89  HIS C CE1 1 
ATOM   2115 N NE2 . HIS C 1 90 ? 14.498  -19.908 26.155  1.00 45.02  ? 89  HIS C NE2 1 
ATOM   2116 N N   . ALA C 1 91 ? 8.131   -22.510 24.794  1.00 56.38  ? 90  ALA C N   1 
ATOM   2117 C CA  . ALA C 1 91 ? 6.834   -23.154 24.971  1.00 67.65  ? 90  ALA C CA  1 
ATOM   2118 C C   . ALA C 1 91 ? 7.010   -24.560 25.555  1.00 76.75  ? 90  ALA C C   1 
ATOM   2119 O O   . ALA C 1 91 ? 8.131   -25.058 25.652  1.00 73.76  ? 90  ALA C O   1 
ATOM   2120 C CB  . ALA C 1 91 ? 6.057   -23.169 23.667  1.00 61.73  ? 90  ALA C CB  1 
ATOM   2121 N N   . SER C 1 92 ? 5.884   -25.203 25.904  1.00 85.63  ? 91  SER C N   1 
ATOM   2122 C CA  . SER C 1 92 ? 5.851   -26.397 26.742  1.00 83.51  ? 91  SER C CA  1 
ATOM   2123 C C   . SER C 1 92 ? 6.096   -27.673 25.939  1.00 84.39  ? 91  SER C C   1 
ATOM   2124 O O   . SER C 1 92 ? 7.023   -28.426 26.238  1.00 79.52  ? 91  SER C O   1 
ATOM   2125 C CB  . SER C 1 92 ? 4.547   -26.485 27.496  1.00 80.75  ? 91  SER C CB  1 
ATOM   2126 O OG  . SER C 1 92 ? 4.423   -25.396 28.398  1.00 80.24  ? 91  SER C OG  1 
ATOM   2127 N N   . TYR C 1 93 ? 5.214   -27.921 24.960  1.00 84.73  ? 92  TYR C N   1 
ATOM   2128 C CA  . TYR C 1 93 ? 5.225   -29.104 24.108  1.00 80.03  ? 92  TYR C CA  1 
ATOM   2129 C C   . TYR C 1 93 ? 5.043   -30.373 24.971  1.00 85.55  ? 92  TYR C C   1 
ATOM   2130 O O   . TYR C 1 93 ? 3.913   -30.654 25.458  1.00 81.42  ? 92  TYR C O   1 
ATOM   2131 C CB  . TYR C 1 93 ? 6.461   -29.167 23.201  1.00 72.50  ? 92  TYR C CB  1 
ATOM   2132 C CG  . TYR C 1 93 ? 6.839   -27.893 22.446  1.00 68.09  ? 92  TYR C CG  1 
ATOM   2133 C CD1 . TYR C 1 93 ? 6.163   -27.508 21.288  1.00 61.26  ? 92  TYR C CD1 1 
ATOM   2134 C CD2 . TYR C 1 93 ? 7.895   -27.089 22.869  1.00 60.38  ? 92  TYR C CD2 1 
ATOM   2135 C CE1 . TYR C 1 93 ? 6.504   -26.356 20.598  1.00 57.80  ? 92  TYR C CE1 1 
ATOM   2136 C CE2 . TYR C 1 93 ? 8.258   -25.943 22.174  1.00 55.33  ? 92  TYR C CE2 1 
ATOM   2137 C CZ  . TYR C 1 93 ? 7.562   -25.576 21.036  1.00 57.54  ? 92  TYR C CZ  1 
ATOM   2138 O OH  . TYR C 1 93 ? 7.902   -24.436 20.358  1.00 58.42  ? 92  TYR C OH  1 
HETATM 2139 S S   . SO4 D 2 .  ? 0.817   -33.630 1.600   1.00 106.78 ? 101 SO4 A S   1 
HETATM 2140 O O1  . SO4 D 2 .  ? 1.508   -34.502 0.685   1.00 86.72  ? 101 SO4 A O1  1 
HETATM 2141 O O2  . SO4 D 2 .  ? 0.744   -32.300 1.047   1.00 108.42 ? 101 SO4 A O2  1 
HETATM 2142 O O3  . SO4 D 2 .  ? -0.516  -34.128 1.825   1.00 116.90 ? 101 SO4 A O3  1 
HETATM 2143 O O4  . SO4 D 2 .  ? 1.523   -33.582 2.848   1.00 96.17  ? 101 SO4 A O4  1 
HETATM 2144 S S   . SO4 E 2 .  ? -9.818  -24.643 1.166   1.00 100.32 ? 102 SO4 A S   1 
HETATM 2145 O O1  . SO4 E 2 .  ? -9.560  -24.488 -0.241  1.00 99.85  ? 102 SO4 A O1  1 
HETATM 2146 O O2  . SO4 E 2 .  ? -10.008 -23.349 1.766   1.00 98.42  ? 102 SO4 A O2  1 
HETATM 2147 O O3  . SO4 E 2 .  ? -11.006 -25.441 1.341   1.00 109.64 ? 102 SO4 A O3  1 
HETATM 2148 O O4  . SO4 E 2 .  ? -8.704  -25.301 1.798   1.00 96.31  ? 102 SO4 A O4  1 
HETATM 2149 C C1  . EDO F 3 .  ? 13.796  -19.435 -7.385  1.00 36.16  ? 103 EDO A C1  1 
HETATM 2150 O O1  . EDO F 3 .  ? 15.031  -18.730 -7.211  1.00 35.17  ? 103 EDO A O1  1 
HETATM 2151 C C2  . EDO F 3 .  ? 12.987  -18.949 -8.565  1.00 36.96  ? 103 EDO A C2  1 
HETATM 2152 O O2  . EDO F 3 .  ? 12.428  -17.668 -8.295  1.00 35.32  ? 103 EDO A O2  1 
HETATM 2153 S S   . SO4 G 2 .  ? 8.865   -29.335 5.780   1.00 60.99  ? 104 SO4 A S   1 
HETATM 2154 O O1  . SO4 G 2 .  ? 9.455   -28.454 4.826   1.00 60.52  ? 104 SO4 A O1  1 
HETATM 2155 O O2  . SO4 G 2 .  ? 8.455   -30.541 5.108   1.00 73.00  ? 104 SO4 A O2  1 
HETATM 2156 O O3  . SO4 G 2 .  ? 9.822   -29.645 6.819   1.00 67.10  ? 104 SO4 A O3  1 
HETATM 2157 O O4  . SO4 G 2 .  ? 7.705   -28.713 6.364   1.00 80.49  ? 104 SO4 A O4  1 
HETATM 2158 S S   . SO4 H 2 .  ? 7.334   -8.498  -24.843 1.00 81.34  ? 101 SO4 B S   1 
HETATM 2159 O O1  . SO4 H 2 .  ? 8.503   -8.557  -25.690 1.00 53.18  ? 101 SO4 B O1  1 
HETATM 2160 O O2  . SO4 H 2 .  ? 6.211   -9.124  -25.508 1.00 60.10  ? 101 SO4 B O2  1 
HETATM 2161 O O3  . SO4 H 2 .  ? 7.549   -9.194  -23.575 1.00 49.72  ? 101 SO4 B O3  1 
HETATM 2162 O O4  . SO4 H 2 .  ? 7.056   -7.102  -24.597 1.00 71.76  ? 101 SO4 B O4  1 
HETATM 2163 S S   . SO4 I 2 .  ? 14.331  -27.097 -26.512 1.00 60.89  ? 102 SO4 B S   1 
HETATM 2164 O O1  . SO4 I 2 .  ? 15.080  -26.474 -25.466 1.00 66.42  ? 102 SO4 B O1  1 
HETATM 2165 O O2  . SO4 I 2 .  ? 15.224  -27.930 -27.287 1.00 69.87  ? 102 SO4 B O2  1 
HETATM 2166 O O3  . SO4 I 2 .  ? 13.286  -27.908 -25.946 1.00 77.44  ? 102 SO4 B O3  1 
HETATM 2167 O O4  . SO4 I 2 .  ? 13.729  -26.093 -27.351 1.00 61.18  ? 102 SO4 B O4  1 
HETATM 2168 N N1  . UWD J 4 .  ? 17.648  -13.902 -22.735 0.82 39.90  ? 103 UWD B N1  1 
HETATM 2169 N N3  . UWD J 4 .  ? 17.674  -15.747 -23.938 0.82 38.29  ? 103 UWD B N3  1 
HETATM 2170 C C4  . UWD J 4 .  ? 16.953  -14.984 -26.095 0.82 35.40  ? 103 UWD B C4  1 
HETATM 2171 C C5  . UWD J 4 .  ? 17.100  -16.273 -26.549 0.82 31.65  ? 103 UWD B C5  1 
HETATM 2172 C C6  . UWD J 4 .  ? 17.564  -17.296 -25.700 0.82 31.78  ? 103 UWD B C6  1 
HETATM 2173 C C7  . UWD J 4 .  ? 17.836  -17.033 -24.402 0.82 32.95  ? 103 UWD B C7  1 
HETATM 2174 N N   . UWD J 4 .  ? 19.661  -16.064 -21.286 0.82 48.85  ? 103 UWD B N   1 
HETATM 2175 C C   . UWD J 4 .  ? 20.238  -17.179 -22.048 0.82 45.55  ? 103 UWD B C   1 
HETATM 2176 C C1  . UWD J 4 .  ? 18.209  -15.964 -21.457 0.82 43.49  ? 103 UWD B C1  1 
HETATM 2177 C C2  . UWD J 4 .  ? 17.871  -15.192 -22.693 0.82 42.61  ? 103 UWD B C2  1 
HETATM 2178 C C3  . UWD J 4 .  ? 17.264  -14.696 -24.750 0.82 38.91  ? 103 UWD B C3  1 
HETATM 2179 N N2  . UWD J 4 .  ? 17.253  -13.578 -24.044 0.82 39.84  ? 103 UWD B N2  1 
HETATM 2180 S S   . SO4 K 2 .  ? 28.705  -38.314 12.109  1.00 97.87  ? 101 SO4 C S   1 
HETATM 2181 O O1  . SO4 K 2 .  ? 30.010  -37.767 11.844  1.00 99.68  ? 101 SO4 C O1  1 
HETATM 2182 O O2  . SO4 K 2 .  ? 27.813  -38.000 11.021  1.00 88.47  ? 101 SO4 C O2  1 
HETATM 2183 O O3  . SO4 K 2 .  ? 28.801  -39.741 12.255  1.00 93.57  ? 101 SO4 C O3  1 
HETATM 2184 O O4  . SO4 K 2 .  ? 28.193  -37.748 13.326  1.00 108.30 ? 101 SO4 C O4  1 
HETATM 2185 N N1  . UWD L 4 .  ? 14.871  -39.192 16.457  0.52 40.85  ? 102 UWD C N1  1 
HETATM 2186 N N3  . UWD L 4 .  ? 16.435  -38.060 17.518  0.52 40.35  ? 102 UWD C N3  1 
HETATM 2187 C C4  . UWD L 4 .  ? 16.306  -35.891 16.498  0.52 39.36  ? 102 UWD C C4  1 
HETATM 2188 C C5  . UWD L 4 .  ? 17.345  -35.497 17.291  0.52 40.35  ? 102 UWD C C5  1 
HETATM 2189 C C6  . UWD L 4 .  ? 17.965  -36.408 18.202  0.52 40.70  ? 102 UWD C C6  1 
HETATM 2190 C C7  . UWD L 4 .  ? 17.498  -37.671 18.310  0.52 37.98  ? 102 UWD C C7  1 
HETATM 2191 N N   . UWD L 4 .  ? 14.870  -41.247 18.493  0.52 44.54  ? 102 UWD C N   1 
HETATM 2192 C C   . UWD L 4 .  ? 15.111  -42.335 19.443  0.52 37.03  ? 102 UWD C C   1 
HETATM 2193 C C1  . UWD L 4 .  ? 16.094  -40.488 18.199  0.52 41.81  ? 102 UWD C C1  1 
HETATM 2194 C C2  . UWD L 4 .  ? 15.789  -39.270 17.389  0.52 40.79  ? 102 UWD C C2  1 
HETATM 2195 C C3  . UWD L 4 .  ? 15.832  -37.214 16.593  0.52 41.34  ? 102 UWD C C3  1 
HETATM 2196 N N2  . UWD L 4 .  ? 14.893  -37.882 15.941  0.52 43.70  ? 102 UWD C N2  1 
HETATM 2197 O O   . HOH M 5 .  ? 8.442   -31.991 3.965   1.00 53.92  ? 201 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? -5.529  -13.333 -16.567 1.00 51.27  ? 202 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 5.518   -28.908 6.704   1.00 48.57  ? 203 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 15.205  -17.156 -19.117 1.00 46.97  ? 204 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? -3.067  -30.682 -3.575  1.00 67.61  ? 205 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? -2.452  3.114   -2.069  1.00 42.08  ? 206 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? 0.376   -24.601 13.430  1.00 71.48  ? 207 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 10.910  -29.549 3.092   1.00 42.35  ? 208 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -7.849  -21.126 -4.633  1.00 71.52  ? 209 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 10.745  -23.617 9.758   1.00 47.22  ? 210 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 10.620  -5.335  -7.711  1.00 33.37  ? 211 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 12.768  -9.554  -7.340  1.00 42.06  ? 212 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 13.887  -15.721 -9.080  1.00 33.96  ? 213 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 0.094   -33.775 4.967   1.00 47.70  ? 214 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 3.776   -34.355 3.895   1.00 59.04  ? 215 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 2.264   -25.018 -10.207 1.00 46.53  ? 216 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? -2.733  -11.767 14.126  1.00 51.57  ? 217 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 1.643   -4.755  -10.287 1.00 40.05  ? 218 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.074   -22.690 -9.435  1.00 41.70  ? 219 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 0.613   -10.561 -15.602 1.00 58.14  ? 220 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? -5.913  -19.459 -5.472  1.00 48.84  ? 221 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 8.828   -18.140 -10.998 1.00 31.68  ? 222 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 4.314   -3.510  -3.317  1.00 32.45  ? 223 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 4.460   -7.848  1.019   1.00 35.53  ? 224 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 19.556  -15.457 7.231   1.00 37.08  ? 225 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 6.853   -10.564 -12.230 1.00 42.95  ? 226 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -8.042  -15.841 -0.986  1.00 37.93  ? 227 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 4.646   -1.363  -6.149  1.00 44.42  ? 228 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? -0.743  -29.295 10.093  1.00 53.48  ? 229 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 2.021   -25.061 -6.490  1.00 51.09  ? 230 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? -0.955  -20.886 6.902   1.00 37.66  ? 231 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -4.850  -25.661 -5.539  1.00 53.62  ? 232 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -3.852  -10.824 6.862   1.00 45.06  ? 233 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 1.754   0.689   -7.331  1.00 50.26  ? 234 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 15.781  -24.329 1.827   1.00 46.52  ? 235 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 12.271  -15.479 -12.080 1.00 53.59  ? 236 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 2.940   -29.561 -0.431  1.00 42.88  ? 237 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 12.537  -28.413 -4.263  1.00 45.65  ? 238 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 11.161  -11.947 5.899   1.00 39.75  ? 239 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 16.974  -12.882 1.398   1.00 19.10  ? 240 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 8.083   -17.782 -15.804 1.00 52.75  ? 241 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -4.567  -21.200 6.185   1.00 48.09  ? 242 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -2.036  -21.918 -0.590  1.00 27.09  ? 243 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 13.078  -11.983 -4.187  1.00 22.50  ? 244 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -6.269  -11.473 -11.373 1.00 38.90  ? 245 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -5.807  -15.819 -8.019  1.00 28.81  ? 246 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? -8.387  -16.729 2.152   1.00 43.81  ? 247 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -8.742  -21.055 -1.180  1.00 40.92  ? 248 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -0.509  -21.035 10.326  1.00 82.56  ? 249 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 1.209   -18.184 -18.578 1.00 62.96  ? 250 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -8.053  -17.297 6.633   1.00 44.67  ? 251 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 11.276  -12.361 -6.125  1.00 28.65  ? 252 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 7.452   -1.394  -1.016  1.00 68.39  ? 253 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 12.505  -11.862 8.077   1.00 70.52  ? 254 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 11.070  -5.890  -4.078  1.00 53.66  ? 255 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 2.679   -10.030 -13.189 1.00 55.61  ? 256 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 9.572   -6.135  -1.821  1.00 45.11  ? 257 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 16.677  -18.085 -9.831  1.00 47.43  ? 258 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 12.444  -13.301 -8.680  1.00 40.86  ? 259 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -1.747  -7.571  11.438  1.00 50.17  ? 260 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 6.146   -5.713  0.271   1.00 62.83  ? 261 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 1.483   -10.463 11.625  1.00 38.62  ? 262 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -0.104  -23.446 9.242   1.00 42.39  ? 263 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 9.911   -12.929 9.721   1.00 41.32  ? 264 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 7.610   -7.837  1.223   1.00 31.15  ? 265 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -6.292  -12.723 6.573   1.00 39.18  ? 266 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 15.582  -11.978 -5.385  1.00 33.23  ? 267 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -1.413  -11.840 11.229  1.00 48.40  ? 268 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 6.369   -16.013 -14.953 1.00 51.44  ? 269 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 9.349   -20.149 -18.494 1.00 49.74  ? 270 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 10.874  -7.944  0.384   1.00 26.00  ? 271 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 8.614   -16.403 -13.079 1.00 38.17  ? 272 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -4.084  -7.798  10.461  1.00 48.49  ? 273 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 8.148   -17.510 8.812   1.00 51.33  ? 274 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -6.348  -26.496 3.341   1.00 46.71  ? 275 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 22.006  -16.617 -0.419  1.00 44.95  ? 276 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 2.281   -6.107  5.288   1.00 37.74  ? 277 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 4.914   -7.561  3.833   1.00 39.09  ? 278 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 16.639  -13.779 10.756  1.00 44.20  ? 279 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -7.370  -11.419 -8.075  1.00 31.01  ? 280 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 21.222  -16.641 -3.442  1.00 27.29  ? 281 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 8.839   -9.301  -13.732 1.00 36.90  ? 282 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 17.100  -12.591 -16.956 1.00 48.32  ? 283 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? -11.421 -16.417 -3.617  1.00 58.53  ? 284 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -8.701  -19.500 -3.526  1.00 39.47  ? 285 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -4.325  -26.995 6.611   1.00 54.39  ? 286 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -3.966  -10.807 9.601   1.00 52.61  ? 287 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 15.156  -28.083 -1.238  1.00 56.88  ? 288 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -7.358  -14.290 -9.050  1.00 46.10  ? 289 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -6.038  -23.335 -7.072  1.00 51.28  ? 290 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 4.762   -7.005  -11.028 1.00 43.68  ? 291 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 11.599  -20.952 10.712  1.00 40.24  ? 292 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -10.358 -28.202 -2.028  1.00 50.41  ? 293 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 10.613  -2.234  -0.817  1.00 50.94  ? 294 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -11.095 -13.081 -2.730  1.00 75.27  ? 295 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -6.381  -22.464 5.992   1.00 55.77  ? 296 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -7.297  -19.517 7.801   1.00 51.43  ? 297 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 4.706   -9.646  -11.276 1.00 57.96  ? 298 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 6.985   -30.591 -2.440  1.00 61.23  ? 299 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 7.906   -8.221  4.367   1.00 40.97  ? 300 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 8.580   -22.202 -19.322 1.00 60.95  ? 301 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -5.161  -20.990 -8.262  1.00 45.49  ? 302 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 5.324   -3.485  1.648   1.00 64.28  ? 303 HOH A O   1 
HETATM 2300 O O   . HOH N 5 .  ? 25.940  -4.873  -33.409 1.00 52.87  ? 201 HOH B O   1 
HETATM 2301 O O   . HOH N 5 .  ? 27.509  -8.130  -28.843 1.00 43.58  ? 202 HOH B O   1 
HETATM 2302 O O   . HOH N 5 .  ? 30.744  -8.304  -29.663 1.00 56.93  ? 203 HOH B O   1 
HETATM 2303 O O   . HOH N 5 .  ? 10.242  -19.576 -43.162 1.00 47.58  ? 204 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 6.493   -12.198 -25.928 1.00 42.71  ? 205 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 24.853  -5.215  -29.826 1.00 43.49  ? 206 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 24.303  -1.518  -36.151 1.00 68.92  ? 207 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 12.980  -4.842  -41.451 1.00 55.70  ? 208 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 34.787  -23.208 -30.055 1.00 59.54  ? 209 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 19.981  -22.231 -23.087 1.00 57.80  ? 210 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 32.569  -18.234 -41.996 1.00 64.01  ? 211 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 25.360  -6.088  -35.780 1.00 43.02  ? 212 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 30.255  -19.710 -40.162 1.00 42.48  ? 213 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 9.801   -11.210 -38.085 1.00 52.57  ? 214 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 10.553  -16.625 -44.034 1.00 87.72  ? 215 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 8.662   -8.763  -16.455 1.00 44.77  ? 216 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 25.833  -0.495  -29.087 1.00 48.62  ? 217 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 27.091  -18.228 -25.182 1.00 52.33  ? 218 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 7.414   -18.263 -31.793 1.00 48.42  ? 219 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 19.703  -25.547 -33.914 1.00 43.26  ? 220 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 10.517  -18.824 -32.976 1.00 29.95  ? 221 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 10.975  -29.323 -25.774 1.00 56.63  ? 222 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 26.911  -10.556 -28.940 1.00 48.84  ? 223 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 20.607  -25.165 -29.558 1.00 52.85  ? 224 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 26.045  -23.117 -31.098 1.00 32.93  ? 225 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 16.714  -19.232 -28.742 1.00 23.29  ? 226 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 22.383  -23.234 -28.744 1.00 47.90  ? 227 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 18.164  -0.457  -38.306 1.00 28.90  ? 228 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 8.330   -27.406 -38.213 1.00 61.66  ? 229 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 23.386  -2.350  -29.093 1.00 37.66  ? 230 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 20.411  -3.313  -23.236 1.00 68.17  ? 231 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 17.248  -19.506 -42.100 1.00 93.62  ? 232 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 23.722  -4.237  -36.704 1.00 30.57  ? 233 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 17.005  -9.484  -43.745 1.00 46.43  ? 234 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 12.455  -22.720 -20.614 1.00 53.75  ? 235 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 21.087  -13.382 -42.545 1.00 48.46  ? 236 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 20.651  -9.937  -42.761 1.00 39.97  ? 237 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 1.659   -12.838 -28.371 1.00 46.11  ? 238 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 17.976  -15.799 -45.834 1.00 43.20  ? 239 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 14.349  -24.578 -40.369 1.00 51.57  ? 240 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 21.292  3.815   -32.598 1.00 38.44  ? 241 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 7.090   -18.792 -34.805 1.00 64.19  ? 242 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 20.232  -27.280 -36.626 1.00 41.92  ? 243 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 7.527   -8.039  -20.823 1.00 46.82  ? 244 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 25.013  -6.546  -42.208 1.00 55.78  ? 245 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 17.937  -3.405  -22.139 1.00 50.36  ? 246 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 31.734  -21.381 -38.105 1.00 51.83  ? 247 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 17.921  4.691   -34.420 1.00 39.26  ? 248 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 6.743   -7.375  -34.120 1.00 57.28  ? 249 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 28.161  -13.024 -24.427 1.00 53.55  ? 250 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 2.836   -8.213  -27.482 1.00 55.50  ? 251 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 14.616  -6.433  -41.262 1.00 45.08  ? 252 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 6.374   -20.528 -25.063 1.00 53.30  ? 253 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 23.618  -11.574 -21.659 1.00 53.28  ? 254 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 39.163  -13.277 -39.529 1.00 76.34  ? 255 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 10.155  -21.656 -32.757 1.00 40.05  ? 256 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 18.364  -26.045 -28.915 1.00 39.70  ? 257 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 12.759  -20.482 -19.965 1.00 54.18  ? 258 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 27.907  -24.846 -34.847 1.00 35.92  ? 259 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 14.853  -8.144  -42.893 1.00 45.87  ? 260 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 7.639   -12.442 -40.084 1.00 71.01  ? 261 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 9.720   -6.144  -40.851 1.00 49.82  ? 262 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 31.577  -12.037 -37.775 1.00 56.48  ? 263 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 16.531  -26.284 -21.178 1.00 68.81  ? 264 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 16.976  -0.396  -25.372 1.00 47.35  ? 265 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 19.505  4.097   -33.260 1.00 41.47  ? 266 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 14.994  -21.924 -41.783 1.00 54.72  ? 267 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 7.300   -9.771  -18.737 1.00 45.51  ? 268 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 28.843  -17.571 -47.711 1.00 49.45  ? 269 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 7.424   -21.494 -29.980 1.00 46.60  ? 270 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 22.062  -29.247 -35.363 1.00 51.88  ? 271 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 16.138  3.215   -26.884 1.00 59.46  ? 272 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 8.419   -36.497 18.465  1.00 69.89  ? 201 HOH C O   1 
HETATM 2373 O O   . HOH O 5 .  ? 29.882  -27.860 31.206  1.00 54.92  ? 202 HOH C O   1 
HETATM 2374 O O   . HOH O 5 .  ? 12.182  -28.263 28.224  1.00 57.85  ? 203 HOH C O   1 
HETATM 2375 O O   . HOH O 5 .  ? 7.367   -31.450 12.028  1.00 60.52  ? 204 HOH C O   1 
HETATM 2376 O O   . HOH O 5 .  ? 25.894  -37.084 10.102  1.00 55.08  ? 205 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 19.857  -21.215 30.868  1.00 58.43  ? 206 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 21.010  -36.254 8.010   1.00 73.92  ? 207 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 22.616  -41.412 18.497  1.00 49.29  ? 208 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 27.867  -37.109 15.741  1.00 51.66  ? 209 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 19.690  -41.768 12.204  1.00 31.76  ? 210 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 14.754  -21.086 12.294  1.00 41.94  ? 211 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 13.700  -37.151 13.487  1.00 47.41  ? 212 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 31.465  -42.904 11.920  1.00 51.51  ? 213 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 26.116  -39.234 12.644  1.00 45.71  ? 214 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 5.512   -26.648 16.735  1.00 51.41  ? 215 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 12.510  -31.450 8.214   1.00 34.38  ? 216 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 30.001  -31.335 15.767  1.00 61.12  ? 217 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 21.931  -28.438 11.107  1.00 34.14  ? 218 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 21.813  -34.314 16.573  1.00 29.30  ? 219 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 25.546  -34.003 34.641  1.00 56.27  ? 220 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 6.732   -18.008 10.907  1.00 36.09  ? 221 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 27.750  -36.890 24.929  1.00 59.76  ? 222 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 18.530  -20.263 10.512  1.00 50.95  ? 223 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 20.337  -40.986 39.242  1.00 61.24  ? 224 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 27.045  -15.281 12.603  1.00 50.61  ? 225 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 17.216  -17.036 14.742  1.00 42.37  ? 226 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 19.169  -26.674 3.357   1.00 50.18  ? 227 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 20.740  -28.528 8.319   1.00 40.20  ? 228 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 8.801   -19.145 23.694  1.00 56.46  ? 229 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 20.747  -39.783 26.217  1.00 47.89  ? 230 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 24.937  -31.241 10.690  1.00 40.13  ? 231 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 30.909  -39.894 27.129  1.00 46.19  ? 232 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 15.650  -17.558 19.170  1.00 45.63  ? 233 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 22.766  -18.521 21.666  1.00 57.07  ? 234 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 30.245  -17.309 9.820   1.00 48.36  ? 235 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 14.093  -29.362 4.048   1.00 45.47  ? 236 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 2.553   -29.044 14.467  1.00 63.12  ? 237 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 25.713  -17.648 13.889  1.00 53.30  ? 238 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 25.374  -39.682 20.202  1.00 38.42  ? 239 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 29.370  -39.893 31.472  1.00 46.92  ? 240 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 30.489  -35.650 28.542  1.00 56.36  ? 241 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 25.162  -18.047 21.086  1.00 58.19  ? 242 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 14.134  -38.670 9.519   1.00 64.88  ? 243 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 9.358   -30.436 9.828   1.00 34.65  ? 244 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 30.988  -43.707 15.823  1.00 68.14  ? 245 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 19.502  -18.987 25.183  1.00 52.03  ? 246 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 20.878  -29.455 4.508   1.00 63.66  ? 247 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 4.809   -23.870 18.655  1.00 57.93  ? 248 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 29.929  -32.412 18.221  1.00 54.55  ? 249 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 28.867  -25.403 33.251  1.00 59.23  ? 250 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 19.960  -13.109 13.350  1.00 53.26  ? 251 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 28.712  -35.394 9.073   1.00 72.17  ? 252 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 16.666  -38.165 28.684  1.00 58.17  ? 253 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 12.727  -22.979 28.055  1.00 61.68  ? 254 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 27.458  -38.936 24.240  1.00 53.07  ? 255 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 28.916  -41.641 27.119  1.00 41.95  ? 256 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 21.980  -13.582 13.266  1.00 44.36  ? 257 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 31.846  -38.970 29.931  1.00 62.70  ? 258 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 33.319  -44.328 15.239  1.00 39.61  ? 259 HOH C O   1 
# 
