data_8P3H
# 
_entry.id   8P3H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8P3H         pdb_00008p3h 10.2210/pdb8p3h/pdb 
WWPDB D_1292129004 ?            ?                   
# 
_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       2024-11-27 
# 
_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.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8P3H 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              e.tate@imperial.ac.uk 
_pdbx_contact_author.name_first         Edward 
_pdbx_contact_author.name_last          Tate 
_pdbx_contact_author.name_mi            W 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2213-5814 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'De Vita, E.'     1 0000-0003-4707-8342 
'Brustur, D.'     2 ?                   
'Tersa, M.'       3 0000-0002-2370-7776 
'Petracca, R.'    4 ?                   
'Morgan, R.M.L.'  5 0000-0002-9760-3638 
'Lanyon-Hogg, T.' 6 0000-0002-7092-8096 
'Norman, J.C.'    7 ?                   
'Cota, E.'        8 ?                   
'Tate, E.W.'      9 0000-0003-2213-5814 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Targeted covalent inhibitors of the small GTPase Rab27A' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'De Vita, E.'     1 0000-0003-4707-8342 
primary 'Brustur, D.'     2 ?                   
primary 'Tersa, M.'       3 0000-0002-2370-7776 
primary 'Petracca, R.'    4 ?                   
primary 'Morgan, R.M.L.'  5 0000-0002-9760-3638 
primary 'Lanyon-Hogg, T.' 6 0000-0002-7092-8096 
primary 'Norman, J.C.'    7 ?                   
primary 'Cota, E.'        8 ?                   
primary 'Tate, E.W.'      9 0000-0003-2213-5814 
# 
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 'Synaptotagmin-like protein 2,Ras-related protein Rab-27A'                     25914.211 2  3.6.5.2 Q78L,C188S ? 
? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                                  522.196   2  ?       ?          ? 
? 
3 non-polymer syn GLYCEROL                                                                       92.094    4  ?       ?          ? 
? 
4 non-polymer syn 'methyl (2~{S})-1-[4-(propanoylamino)phenyl]sulfonylpyrrolidine-2-carboxylate' 340.395   2  ?       ?          ? 
? 
5 non-polymer syn 'MAGNESIUM ION'                                                                24.305    2  ?       ?          ? 
? 
6 water       nat water                                                                          18.015    47 ?       ?          ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Breast cancer-associated antigen SGA-72M,Exophilin-4,Rab-27,GTP-binding protein Ram' 
# 
_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       
;GHMSFLTEEEQEAIMKVLQRDAALKRAEEERGSGSGSGMSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTV
GIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGLERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAY
CENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMSFLTEEEQEAIMKVLQRDAALKRAEEERGSGSGSGMSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTV
GIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGLERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAY
CENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                                  GNP 
3 GLYCEROL                                                                       GOL 
4 'methyl (2~{S})-1-[4-(propanoylamino)phenyl]sulfonylpyrrolidine-2-carboxylate' WTO 
5 'MAGNESIUM ION'                                                                MG  
6 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   HIS n 
1 3   MET n 
1 4   SER n 
1 5   PHE n 
1 6   LEU n 
1 7   THR n 
1 8   GLU n 
1 9   GLU n 
1 10  GLU n 
1 11  GLN n 
1 12  GLU n 
1 13  ALA n 
1 14  ILE n 
1 15  MET n 
1 16  LYS n 
1 17  VAL n 
1 18  LEU n 
1 19  GLN n 
1 20  ARG n 
1 21  ASP n 
1 22  ALA n 
1 23  ALA n 
1 24  LEU n 
1 25  LYS n 
1 26  ARG n 
1 27  ALA n 
1 28  GLU n 
1 29  GLU n 
1 30  GLU n 
1 31  ARG n 
1 32  GLY n 
1 33  SER n 
1 34  GLY n 
1 35  SER n 
1 36  GLY n 
1 37  SER n 
1 38  GLY n 
1 39  MET n 
1 40  SER n 
1 41  ASP n 
1 42  GLY n 
1 43  ASP n 
1 44  TYR n 
1 45  ASP n 
1 46  TYR n 
1 47  LEU n 
1 48  ILE n 
1 49  LYS n 
1 50  PHE n 
1 51  LEU n 
1 52  ALA n 
1 53  LEU n 
1 54  GLY n 
1 55  ASP n 
1 56  SER n 
1 57  GLY n 
1 58  VAL n 
1 59  GLY n 
1 60  LYS n 
1 61  THR n 
1 62  SER n 
1 63  VAL n 
1 64  LEU n 
1 65  TYR n 
1 66  GLN n 
1 67  TYR n 
1 68  THR n 
1 69  ASP n 
1 70  GLY n 
1 71  LYS n 
1 72  PHE n 
1 73  ASN n 
1 74  SER n 
1 75  LYS n 
1 76  PHE n 
1 77  ILE n 
1 78  THR n 
1 79  THR n 
1 80  VAL n 
1 81  GLY n 
1 82  ILE n 
1 83  ASP n 
1 84  PHE n 
1 85  ARG n 
1 86  GLU n 
1 87  LYS n 
1 88  ARG n 
1 89  VAL n 
1 90  VAL n 
1 91  TYR n 
1 92  ARG n 
1 93  ALA n 
1 94  SER n 
1 95  GLY n 
1 96  PRO n 
1 97  ASP n 
1 98  GLY n 
1 99  ALA n 
1 100 THR n 
1 101 GLY n 
1 102 ARG n 
1 103 GLY n 
1 104 GLN n 
1 105 ARG n 
1 106 ILE n 
1 107 HIS n 
1 108 LEU n 
1 109 GLN n 
1 110 LEU n 
1 111 TRP n 
1 112 ASP n 
1 113 THR n 
1 114 ALA n 
1 115 GLY n 
1 116 LEU n 
1 117 GLU n 
1 118 ARG n 
1 119 PHE n 
1 120 ARG n 
1 121 SER n 
1 122 LEU n 
1 123 THR n 
1 124 THR n 
1 125 ALA n 
1 126 PHE n 
1 127 PHE n 
1 128 ARG n 
1 129 ASP n 
1 130 ALA n 
1 131 MET n 
1 132 GLY n 
1 133 PHE n 
1 134 LEU n 
1 135 LEU n 
1 136 LEU n 
1 137 PHE n 
1 138 ASP n 
1 139 LEU n 
1 140 THR n 
1 141 ASN n 
1 142 GLU n 
1 143 GLN n 
1 144 SER n 
1 145 PHE n 
1 146 LEU n 
1 147 ASN n 
1 148 VAL n 
1 149 ARG n 
1 150 ASN n 
1 151 TRP n 
1 152 ILE n 
1 153 SER n 
1 154 GLN n 
1 155 LEU n 
1 156 GLN n 
1 157 MET n 
1 158 HIS n 
1 159 ALA n 
1 160 TYR n 
1 161 CYS n 
1 162 GLU n 
1 163 ASN n 
1 164 PRO n 
1 165 ASP n 
1 166 ILE n 
1 167 VAL n 
1 168 LEU n 
1 169 CYS n 
1 170 GLY n 
1 171 ASN n 
1 172 LYS n 
1 173 SER n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 ASP n 
1 178 GLN n 
1 179 ARG n 
1 180 VAL n 
1 181 VAL n 
1 182 LYS n 
1 183 GLU n 
1 184 GLU n 
1 185 GLU n 
1 186 ALA n 
1 187 ILE n 
1 188 ALA n 
1 189 LEU n 
1 190 ALA n 
1 191 GLU n 
1 192 LYS n 
1 193 TYR n 
1 194 GLY n 
1 195 ILE n 
1 196 PRO n 
1 197 TYR n 
1 198 PHE n 
1 199 GLU n 
1 200 THR n 
1 201 SER n 
1 202 ALA n 
1 203 ALA n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 ASN n 
1 208 ILE n 
1 209 SER n 
1 210 GLN n 
1 211 ALA n 
1 212 ILE n 
1 213 GLU n 
1 214 MET n 
1 215 LEU n 
1 216 LEU n 
1 217 ASP n 
1 218 LEU n 
1 219 ILE n 
1 220 MET n 
1 221 LYS n 
1 222 ARG n 
1 223 MET n 
1 224 GLU n 
1 225 ARG n 
1 226 SER n 
1 227 VAL n 
1 228 ASP n 
1 229 LYS n 
1 230 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
_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 
1 1 sample 'Biological sequence' 1  32  human ? 'SYTL2, KIAA1597, SGA72M, SLP2, SLP2A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? 
? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 33 230 human ? 'RAB27A, RAB27'                        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? 
? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                                  ? 'C10 H17 N6 O13 P3' 
522.196 
GOL non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
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 
MG  non-polymer         . 'MAGNESIUM ION'                                                                ? 'Mg 2'              
24.305  
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 
THR 'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'        
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'     
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'       
181.189 
VAL 'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'       
117.146 
WTO non-polymer         . 'methyl (2~{S})-1-[4-(propanoylamino)phenyl]sulfonylpyrrolidine-2-carboxylate' ? 'C15 H20 N2 O5 S'   
340.395 
# 
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   -38 ?   ?   ?   A . n 
A 1 2   HIS 2   -37 ?   ?   ?   A . n 
A 1 3   MET 3   -36 ?   ?   ?   A . n 
A 1 4   SER 4   -35 -35 SER SER A . n 
A 1 5   PHE 5   -34 -34 PHE PHE A . n 
A 1 6   LEU 6   -33 -33 LEU LEU A . n 
A 1 7   THR 7   -32 -32 THR THR A . n 
A 1 8   GLU 8   -31 -31 GLU GLU A . n 
A 1 9   GLU 9   -30 -30 GLU GLU A . n 
A 1 10  GLU 10  -29 -29 GLU GLU A . n 
A 1 11  GLN 11  -28 -28 GLN GLN A . n 
A 1 12  GLU 12  -27 -27 GLU GLU A . n 
A 1 13  ALA 13  -26 -26 ALA ALA A . n 
A 1 14  ILE 14  -25 -25 ILE ILE A . n 
A 1 15  MET 15  -24 -24 MET MET A . n 
A 1 16  LYS 16  -23 -23 LYS LYS A . n 
A 1 17  VAL 17  -22 -22 VAL VAL A . n 
A 1 18  LEU 18  -21 -21 LEU LEU A . n 
A 1 19  GLN 19  -20 -20 GLN GLN A . n 
A 1 20  ARG 20  -19 -19 ARG ARG A . n 
A 1 21  ASP 21  -18 -18 ASP ASP A . n 
A 1 22  ALA 22  -17 -17 ALA ALA A . n 
A 1 23  ALA 23  -16 -16 ALA ALA A . n 
A 1 24  LEU 24  -15 -15 LEU LEU A . n 
A 1 25  LYS 25  -14 -14 LYS LYS A . n 
A 1 26  ARG 26  -13 -13 ARG ARG A . n 
A 1 27  ALA 27  -12 -12 ALA ALA A . n 
A 1 28  GLU 28  -11 -11 GLU GLU A . n 
A 1 29  GLU 29  -10 -10 GLU GLU A . n 
A 1 30  GLU 30  -9  -9  GLU GLU A . n 
A 1 31  ARG 31  -9  ?   ?   ?   A A n 
A 1 32  GLY 32  -9  ?   ?   ?   A B n 
A 1 33  SER 33  -9  ?   ?   ?   A C n 
A 1 34  GLY 34  -9  ?   ?   ?   A D n 
A 1 35  SER 35  -9  ?   ?   ?   A E n 
A 1 36  GLY 36  -9  ?   ?   ?   A F n 
A 1 37  SER 37  -9  ?   ?   ?   A G n 
A 1 38  GLY 38  -9  ?   ?   ?   A H n 
A 1 39  MET 39  -9  ?   ?   ?   A I n 
A 1 40  SER 40  -9  ?   ?   ?   A J n 
A 1 41  ASP 41  -9  ?   ?   ?   A K n 
A 1 42  GLY 42  -9  ?   ?   ?   A L n 
A 1 43  ASP 43  -9  ?   ?   ?   A M n 
A 1 44  TYR 44  -8  6   TYR TYR A . n 
A 1 45  ASP 45  -7  7   ASP ASP A . n 
A 1 46  TYR 46  -6  8   TYR TYR A . n 
A 1 47  LEU 47  -5  9   LEU LEU A . n 
A 1 48  ILE 48  -4  10  ILE ILE A . n 
A 1 49  LYS 49  -3  11  LYS LYS A . n 
A 1 50  PHE 50  -2  12  PHE PHE A . n 
A 1 51  LEU 51  -1  13  LEU LEU A . n 
A 1 52  ALA 52  0   14  ALA ALA A . n 
A 1 53  LEU 53  1   15  LEU LEU A . n 
A 1 54  GLY 54  2   16  GLY GLY A . n 
A 1 55  ASP 55  3   17  ASP ASP A . n 
A 1 56  SER 56  4   18  SER SER A . n 
A 1 57  GLY 57  5   19  GLY GLY A . n 
A 1 58  VAL 58  6   20  VAL VAL A . n 
A 1 59  GLY 59  7   21  GLY GLY A . n 
A 1 60  LYS 60  8   22  LYS LYS A . n 
A 1 61  THR 61  9   23  THR THR A . n 
A 1 62  SER 62  10  24  SER SER A . n 
A 1 63  VAL 63  11  25  VAL VAL A . n 
A 1 64  LEU 64  12  26  LEU LEU A . n 
A 1 65  TYR 65  13  27  TYR TYR A . n 
A 1 66  GLN 66  14  28  GLN GLN A . n 
A 1 67  TYR 67  15  29  TYR TYR A . n 
A 1 68  THR 68  16  30  THR THR A . n 
A 1 69  ASP 69  17  31  ASP ASP A . n 
A 1 70  GLY 70  18  32  GLY GLY A . n 
A 1 71  LYS 71  19  33  LYS LYS A . n 
A 1 72  PHE 72  20  34  PHE PHE A . n 
A 1 73  ASN 73  21  35  ASN ASN A . n 
A 1 74  SER 74  22  36  SER SER A . n 
A 1 75  LYS 75  23  37  LYS LYS A . n 
A 1 76  PHE 76  24  38  PHE PHE A . n 
A 1 77  ILE 77  25  39  ILE ILE A . n 
A 1 78  THR 78  26  40  THR THR A . n 
A 1 79  THR 79  27  41  THR THR A . n 
A 1 80  VAL 80  28  42  VAL VAL A . n 
A 1 81  GLY 81  29  43  GLY GLY A . n 
A 1 82  ILE 82  30  44  ILE ILE A . n 
A 1 83  ASP 83  31  45  ASP ASP A . n 
A 1 84  PHE 84  32  46  PHE PHE A . n 
A 1 85  ARG 85  33  47  ARG ARG A . n 
A 1 86  GLU 86  34  48  GLU GLU A . n 
A 1 87  LYS 87  35  49  LYS LYS A . n 
A 1 88  ARG 88  36  50  ARG ARG A . n 
A 1 89  VAL 89  37  51  VAL VAL A . n 
A 1 90  VAL 90  38  52  VAL VAL A . n 
A 1 91  TYR 91  39  53  TYR TYR A . n 
A 1 92  ARG 92  40  54  ARG ARG A . n 
A 1 93  ALA 93  41  55  ALA ALA A . n 
A 1 94  SER 94  42  56  SER SER A . n 
A 1 95  GLY 95  42  ?   ?   ?   A A n 
A 1 96  PRO 96  42  ?   ?   ?   A B n 
A 1 97  ASP 97  42  ?   ?   ?   A C n 
A 1 98  GLY 98  42  ?   ?   ?   A D n 
A 1 99  ALA 99  43  61  ALA ALA A . n 
A 1 100 THR 100 44  62  THR THR A . n 
A 1 101 GLY 101 45  63  GLY GLY A . n 
A 1 102 ARG 102 46  64  ARG ALA A . n 
A 1 103 GLY 103 47  65  GLY GLY A . n 
A 1 104 GLN 104 48  66  GLN GLN A . n 
A 1 105 ARG 105 49  67  ARG ARG A . n 
A 1 106 ILE 106 50  68  ILE ILE A . n 
A 1 107 HIS 107 51  69  HIS HIS A . n 
A 1 108 LEU 108 52  70  LEU LEU A . n 
A 1 109 GLN 109 53  71  GLN GLN A . n 
A 1 110 LEU 110 54  72  LEU LEU A . n 
A 1 111 TRP 111 55  73  TRP TRP A . n 
A 1 112 ASP 112 56  74  ASP ASP A . n 
A 1 113 THR 113 57  75  THR THR A . n 
A 1 114 ALA 114 58  76  ALA ALA A . n 
A 1 115 GLY 115 59  77  GLY GLY A . n 
A 1 116 LEU 116 60  78  LEU LEU A . n 
A 1 117 GLU 117 61  79  GLU GLU A . n 
A 1 118 ARG 118 62  80  ARG ARG A . n 
A 1 119 PHE 119 63  81  PHE PHE A . n 
A 1 120 ARG 120 64  82  ARG ARG A . n 
A 1 121 SER 121 65  83  SER SER A . n 
A 1 122 LEU 122 66  84  LEU LEU A . n 
A 1 123 THR 123 67  85  THR THR A . n 
A 1 124 THR 124 68  86  THR THR A . n 
A 1 125 ALA 125 69  87  ALA ALA A . n 
A 1 126 PHE 126 70  88  PHE PHE A . n 
A 1 127 PHE 127 71  89  PHE PHE A . n 
A 1 128 ARG 128 72  90  ARG ARG A . n 
A 1 129 ASP 129 73  91  ASP ASP A . n 
A 1 130 ALA 130 74  92  ALA ALA A . n 
A 1 131 MET 131 75  93  MET MET A . n 
A 1 132 GLY 132 76  94  GLY GLY A . n 
A 1 133 PHE 133 77  95  PHE PHE A . n 
A 1 134 LEU 134 78  96  LEU LEU A . n 
A 1 135 LEU 135 79  97  LEU LEU A . n 
A 1 136 LEU 136 80  98  LEU LEU A . n 
A 1 137 PHE 137 81  99  PHE PHE A . n 
A 1 138 ASP 138 82  100 ASP ASP A . n 
A 1 139 LEU 139 83  101 LEU LEU A . n 
A 1 140 THR 140 84  102 THR THR A . n 
A 1 141 ASN 141 85  103 ASN ASN A . n 
A 1 142 GLU 142 86  104 GLU GLU A . n 
A 1 143 GLN 143 87  105 GLN GLN A . n 
A 1 144 SER 144 88  106 SER SER A . n 
A 1 145 PHE 145 89  107 PHE PHE A . n 
A 1 146 LEU 146 90  108 LEU LEU A . n 
A 1 147 ASN 147 91  109 ASN ASN A . n 
A 1 148 VAL 148 92  110 VAL VAL A . n 
A 1 149 ARG 149 93  111 ARG ARG A . n 
A 1 150 ASN 150 94  112 ASN ASN A . n 
A 1 151 TRP 151 95  113 TRP TRP A . n 
A 1 152 ILE 152 96  114 ILE ILE A . n 
A 1 153 SER 153 97  115 SER SER A . n 
A 1 154 GLN 154 98  116 GLN GLN A . n 
A 1 155 LEU 155 99  117 LEU LEU A . n 
A 1 156 GLN 156 100 118 GLN GLN A . n 
A 1 157 MET 157 101 119 MET MET A . n 
A 1 158 HIS 158 102 120 HIS HIS A . n 
A 1 159 ALA 159 103 121 ALA ALA A . n 
A 1 160 TYR 160 104 122 TYR TYR A . n 
A 1 161 CYS 161 105 123 CYS CC4 A . n 
A 1 162 GLU 162 106 124 GLU GLU A . n 
A 1 163 ASN 163 107 125 ASN ASN A . n 
A 1 164 PRO 164 108 126 PRO PRO A . n 
A 1 165 ASP 165 109 127 ASP ASP A . n 
A 1 166 ILE 166 110 128 ILE ILE A . n 
A 1 167 VAL 167 111 129 VAL VAL A . n 
A 1 168 LEU 168 112 130 LEU LEU A . n 
A 1 169 CYS 169 113 131 CYS CYS A . n 
A 1 170 GLY 170 114 132 GLY GLY A . n 
A 1 171 ASN 171 115 133 ASN ASN A . n 
A 1 172 LYS 172 116 134 LYS LYS A . n 
A 1 173 SER 173 117 135 SER SER A . n 
A 1 174 ASP 174 118 136 ASP ASP A . n 
A 1 175 LEU 175 119 137 LEU LEU A . n 
A 1 176 GLU 176 120 138 GLU GLU A . n 
A 1 177 ASP 177 121 139 ASP ASP A . n 
A 1 178 GLN 178 122 140 GLN GLN A . n 
A 1 179 ARG 179 123 141 ARG ARG A . n 
A 1 180 VAL 180 124 142 VAL VAL A . n 
A 1 181 VAL 181 125 143 VAL VAL A . n 
A 1 182 LYS 182 126 144 LYS LYS A . n 
A 1 183 GLU 183 127 145 GLU GLU A . n 
A 1 184 GLU 184 128 146 GLU GLU A . n 
A 1 185 GLU 185 129 147 GLU GLU A . n 
A 1 186 ALA 186 130 148 ALA ALA A . n 
A 1 187 ILE 187 131 149 ILE ILE A . n 
A 1 188 ALA 188 132 150 ALA ALA A . n 
A 1 189 LEU 189 133 151 LEU LEU A . n 
A 1 190 ALA 190 134 152 ALA ALA A . n 
A 1 191 GLU 191 135 153 GLU GLU A . n 
A 1 192 LYS 192 136 154 LYS LYS A . n 
A 1 193 TYR 193 137 155 TYR TYR A . n 
A 1 194 GLY 194 138 156 GLY GLY A . n 
A 1 195 ILE 195 139 157 ILE ILE A . n 
A 1 196 PRO 196 140 158 PRO PRO A . n 
A 1 197 TYR 197 141 159 TYR TYR A . n 
A 1 198 PHE 198 142 160 PHE PHE A . n 
A 1 199 GLU 199 143 161 GLU GLU A . n 
A 1 200 THR 200 144 162 THR THR A . n 
A 1 201 SER 201 145 163 SER SER A . n 
A 1 202 ALA 202 146 164 ALA ALA A . n 
A 1 203 ALA 203 147 165 ALA ALA A . n 
A 1 204 ASN 204 148 166 ASN ASN A . n 
A 1 205 GLY 205 149 167 GLY GLY A . n 
A 1 206 THR 206 150 168 THR THR A . n 
A 1 207 ASN 207 151 169 ASN ASN A . n 
A 1 208 ILE 208 152 170 ILE ILE A . n 
A 1 209 SER 209 153 171 SER SER A . n 
A 1 210 GLN 210 154 172 GLN GLN A . n 
A 1 211 ALA 211 155 173 ALA ALA A . n 
A 1 212 ILE 212 156 174 ILE ILE A . n 
A 1 213 GLU 213 157 175 GLU GLU A . n 
A 1 214 MET 214 158 176 MET MET A . n 
A 1 215 LEU 215 159 177 LEU LEU A . n 
A 1 216 LEU 216 160 178 LEU LEU A . n 
A 1 217 ASP 217 161 179 ASP ASP A . n 
A 1 218 LEU 218 162 180 LEU LEU A . n 
A 1 219 ILE 219 163 181 ILE ILE A . n 
A 1 220 MET 220 164 182 MET MET A . n 
A 1 221 LYS 221 165 183 LYS LYS A . n 
A 1 222 ARG 222 166 184 ARG ARG A . n 
A 1 223 MET 223 167 185 MET MET A . n 
A 1 224 GLU 224 168 186 GLU GLU A . n 
A 1 225 ARG 225 169 187 ARG ARG A . n 
A 1 226 SER 226 170 188 SER SER A . n 
A 1 227 VAL 227 171 ?   ?   ?   A . n 
A 1 228 ASP 228 172 ?   ?   ?   A . n 
A 1 229 LYS 229 173 ?   ?   ?   A . n 
A 1 230 SER 230 174 ?   ?   ?   A . n 
B 1 1   GLY 1   -38 ?   ?   ?   B . n 
B 1 2   HIS 2   -37 ?   ?   ?   B . n 
B 1 3   MET 3   -36 ?   ?   ?   B . n 
B 1 4   SER 4   -35 -35 SER SER B . n 
B 1 5   PHE 5   -34 -34 PHE PHE B . n 
B 1 6   LEU 6   -33 -33 LEU LEU B . n 
B 1 7   THR 7   -32 -32 THR THR B . n 
B 1 8   GLU 8   -31 -31 GLU GLU B . n 
B 1 9   GLU 9   -30 -30 GLU GLU B . n 
B 1 10  GLU 10  -29 -29 GLU GLU B . n 
B 1 11  GLN 11  -28 -28 GLN GLN B . n 
B 1 12  GLU 12  -27 -27 GLU GLU B . n 
B 1 13  ALA 13  -26 -26 ALA ALA B . n 
B 1 14  ILE 14  -25 -25 ILE ILE B . n 
B 1 15  MET 15  -24 -24 MET MET B . n 
B 1 16  LYS 16  -23 -23 LYS LYS B . n 
B 1 17  VAL 17  -22 -22 VAL VAL B . n 
B 1 18  LEU 18  -21 -21 LEU LEU B . n 
B 1 19  GLN 19  -20 -20 GLN GLN B . n 
B 1 20  ARG 20  -19 -19 ARG ARG B . n 
B 1 21  ASP 21  -18 -18 ASP ASP B . n 
B 1 22  ALA 22  -17 -17 ALA ALA B . n 
B 1 23  ALA 23  -16 -16 ALA ALA B . n 
B 1 24  LEU 24  -15 -15 LEU LEU B . n 
B 1 25  LYS 25  -14 -14 LYS LYS B . n 
B 1 26  ARG 26  -13 -13 ARG ARG B . n 
B 1 27  ALA 27  -12 -12 ALA ALA B . n 
B 1 28  GLU 28  -11 -11 GLU GLU B . n 
B 1 29  GLU 29  -10 -10 GLU GLU B . n 
B 1 30  GLU 30  -9  -9  GLU GLU B . n 
B 1 31  ARG 31  -9  ?   ?   ?   B A n 
B 1 32  GLY 32  -9  ?   ?   ?   B B n 
B 1 33  SER 33  -9  ?   ?   ?   B C n 
B 1 34  GLY 34  -9  ?   ?   ?   B D n 
B 1 35  SER 35  -9  ?   ?   ?   B E n 
B 1 36  GLY 36  -9  ?   ?   ?   B F n 
B 1 37  SER 37  -9  ?   ?   ?   B G n 
B 1 38  GLY 38  -9  ?   ?   ?   B H n 
B 1 39  MET 39  -9  ?   ?   ?   B I n 
B 1 40  SER 40  -9  ?   ?   ?   B J n 
B 1 41  ASP 41  -9  ?   ?   ?   B K n 
B 1 42  GLY 42  -9  ?   ?   ?   B L n 
B 1 43  ASP 43  -9  ?   ?   ?   B M n 
B 1 44  TYR 44  -8  6   TYR TYR B . n 
B 1 45  ASP 45  -7  7   ASP ASP B . n 
B 1 46  TYR 46  -6  8   TYR TYR B . n 
B 1 47  LEU 47  -5  9   LEU LEU B . n 
B 1 48  ILE 48  -4  10  ILE ILE B . n 
B 1 49  LYS 49  -3  11  LYS LYS B . n 
B 1 50  PHE 50  -2  12  PHE PHE B . n 
B 1 51  LEU 51  -1  13  LEU LEU B . n 
B 1 52  ALA 52  0   14  ALA ALA B . n 
B 1 53  LEU 53  1   15  LEU LEU B . n 
B 1 54  GLY 54  2   16  GLY GLY B . n 
B 1 55  ASP 55  3   17  ASP ASP B . n 
B 1 56  SER 56  4   18  SER SER B . n 
B 1 57  GLY 57  5   19  GLY GLY B . n 
B 1 58  VAL 58  6   20  VAL VAL B . n 
B 1 59  GLY 59  7   21  GLY GLY B . n 
B 1 60  LYS 60  8   22  LYS LYS B . n 
B 1 61  THR 61  9   23  THR THR B . n 
B 1 62  SER 62  10  24  SER SER B . n 
B 1 63  VAL 63  11  25  VAL VAL B . n 
B 1 64  LEU 64  12  26  LEU LEU B . n 
B 1 65  TYR 65  13  27  TYR TYR B . n 
B 1 66  GLN 66  14  28  GLN GLN B . n 
B 1 67  TYR 67  15  29  TYR TYR B . n 
B 1 68  THR 68  16  30  THR THR B . n 
B 1 69  ASP 69  17  31  ASP ASP B . n 
B 1 70  GLY 70  18  32  GLY GLY B . n 
B 1 71  LYS 71  19  33  LYS LYS B . n 
B 1 72  PHE 72  20  34  PHE PHE B . n 
B 1 73  ASN 73  21  35  ASN ASN B . n 
B 1 74  SER 74  22  36  SER SER B . n 
B 1 75  LYS 75  23  37  LYS LYS B . n 
B 1 76  PHE 76  24  38  PHE PHE B . n 
B 1 77  ILE 77  25  39  ILE ILE B . n 
B 1 78  THR 78  26  40  THR THR B . n 
B 1 79  THR 79  27  41  THR THR B . n 
B 1 80  VAL 80  28  42  VAL VAL B . n 
B 1 81  GLY 81  29  43  GLY GLY B . n 
B 1 82  ILE 82  30  44  ILE ILE B . n 
B 1 83  ASP 83  31  45  ASP ASP B . n 
B 1 84  PHE 84  32  46  PHE PHE B . n 
B 1 85  ARG 85  33  47  ARG ARG B . n 
B 1 86  GLU 86  34  48  GLU GLU B . n 
B 1 87  LYS 87  35  49  LYS LYS B . n 
B 1 88  ARG 88  36  50  ARG ARG B . n 
B 1 89  VAL 89  37  51  VAL VAL B . n 
B 1 90  VAL 90  38  52  VAL VAL B . n 
B 1 91  TYR 91  39  53  TYR TYR B . n 
B 1 92  ARG 92  40  54  ARG ARG B . n 
B 1 93  ALA 93  41  55  ALA ALA B . n 
B 1 94  SER 94  41  ?   ?   ?   B A n 
B 1 95  GLY 95  41  ?   ?   ?   B B n 
B 1 96  PRO 96  41  ?   ?   ?   B C n 
B 1 97  ASP 97  41  ?   ?   ?   B D n 
B 1 98  GLY 98  41  ?   ?   ?   B E n 
B 1 99  ALA 99  41  ?   ?   ?   B F n 
B 1 100 THR 100 41  ?   ?   ?   B G n 
B 1 101 GLY 101 42  63  GLY GLY B . n 
B 1 102 ARG 102 43  64  ARG ARG B . n 
B 1 103 GLY 103 44  65  GLY GLY B . n 
B 1 104 GLN 104 45  66  GLN GLN B . n 
B 1 105 ARG 105 46  67  ARG ARG B . n 
B 1 106 ILE 106 47  68  ILE ILE B . n 
B 1 107 HIS 107 48  69  HIS HIS B . n 
B 1 108 LEU 108 49  70  LEU LEU B . n 
B 1 109 GLN 109 50  71  GLN GLN B . n 
B 1 110 LEU 110 51  72  LEU LEU B . n 
B 1 111 TRP 111 52  73  TRP TRP B . n 
B 1 112 ASP 112 53  74  ASP ASP B . n 
B 1 113 THR 113 54  75  THR THR B . n 
B 1 114 ALA 114 55  76  ALA ALA B . n 
B 1 115 GLY 115 56  77  GLY GLY B . n 
B 1 116 LEU 116 57  78  LEU LEU B . n 
B 1 117 GLU 117 58  79  GLU GLU B . n 
B 1 118 ARG 118 59  80  ARG ARG B . n 
B 1 119 PHE 119 60  81  PHE PHE B . n 
B 1 120 ARG 120 61  82  ARG ARG B . n 
B 1 121 SER 121 62  83  SER SER B . n 
B 1 122 LEU 122 63  84  LEU LEU B . n 
B 1 123 THR 123 64  85  THR THR B . n 
B 1 124 THR 124 65  86  THR THR B . n 
B 1 125 ALA 125 66  87  ALA ALA B . n 
B 1 126 PHE 126 67  88  PHE PHE B . n 
B 1 127 PHE 127 68  89  PHE PHE B . n 
B 1 128 ARG 128 69  90  ARG ARG B . n 
B 1 129 ASP 129 70  91  ASP ASP B . n 
B 1 130 ALA 130 71  92  ALA ALA B . n 
B 1 131 MET 131 72  93  MET MET B . n 
B 1 132 GLY 132 73  94  GLY GLY B . n 
B 1 133 PHE 133 74  95  PHE PHE B . n 
B 1 134 LEU 134 75  96  LEU LEU B . n 
B 1 135 LEU 135 76  97  LEU LEU B . n 
B 1 136 LEU 136 77  98  LEU LEU B . n 
B 1 137 PHE 137 78  99  PHE PHE B . n 
B 1 138 ASP 138 79  100 ASP ASP B . n 
B 1 139 LEU 139 80  101 LEU LEU B . n 
B 1 140 THR 140 81  102 THR THR B . n 
B 1 141 ASN 141 82  103 ASN ASN B . n 
B 1 142 GLU 142 83  104 GLU GLU B . n 
B 1 143 GLN 143 84  105 GLN GLN B . n 
B 1 144 SER 144 85  106 SER SER B . n 
B 1 145 PHE 145 86  107 PHE PHE B . n 
B 1 146 LEU 146 87  108 LEU LEU B . n 
B 1 147 ASN 147 88  109 ASN ASN B . n 
B 1 148 VAL 148 89  110 VAL VAL B . n 
B 1 149 ARG 149 90  111 ARG ARG B . n 
B 1 150 ASN 150 91  112 ASN ASN B . n 
B 1 151 TRP 151 92  113 TRP TRP B . n 
B 1 152 ILE 152 93  114 ILE ILE B . n 
B 1 153 SER 153 94  115 SER SER B . n 
B 1 154 GLN 154 95  116 GLN GLN B . n 
B 1 155 LEU 155 96  117 LEU LEU B . n 
B 1 156 GLN 156 97  118 GLN GLN B . n 
B 1 157 MET 157 98  119 MET MET B . n 
B 1 158 HIS 158 99  120 HIS HIS B . n 
B 1 159 ALA 159 100 121 ALA ALA B . n 
B 1 160 TYR 160 101 122 TYR TYR B . n 
B 1 161 CYS 161 102 123 CYS CC4 B . n 
B 1 162 GLU 162 103 124 GLU GLU B . n 
B 1 163 ASN 163 104 125 ASN ASN B . n 
B 1 164 PRO 164 105 126 PRO PRO B . n 
B 1 165 ASP 165 106 127 ASP ASP B . n 
B 1 166 ILE 166 107 128 ILE ILE B . n 
B 1 167 VAL 167 108 129 VAL VAL B . n 
B 1 168 LEU 168 109 130 LEU LEU B . n 
B 1 169 CYS 169 110 131 CYS CYS B . n 
B 1 170 GLY 170 111 132 GLY GLY B . n 
B 1 171 ASN 171 112 133 ASN ASN B . n 
B 1 172 LYS 172 113 134 LYS LYS B . n 
B 1 173 SER 173 114 135 SER SER B . n 
B 1 174 ASP 174 115 136 ASP ASP B . n 
B 1 175 LEU 175 116 137 LEU LEU B . n 
B 1 176 GLU 176 117 138 GLU GLU B . n 
B 1 177 ASP 177 118 139 ASP ASP B . n 
B 1 178 GLN 178 119 140 GLN GLN B . n 
B 1 179 ARG 179 120 141 ARG ARG B . n 
B 1 180 VAL 180 121 142 VAL VAL B . n 
B 1 181 VAL 181 122 143 VAL VAL B . n 
B 1 182 LYS 182 123 144 LYS LYS B . n 
B 1 183 GLU 183 124 145 GLU GLU B . n 
B 1 184 GLU 184 125 146 GLU GLU B . n 
B 1 185 GLU 185 126 147 GLU GLU B . n 
B 1 186 ALA 186 127 148 ALA ALA B . n 
B 1 187 ILE 187 128 149 ILE ILE B . n 
B 1 188 ALA 188 129 150 ALA ALA B . n 
B 1 189 LEU 189 130 151 LEU LEU B . n 
B 1 190 ALA 190 131 152 ALA ALA B . n 
B 1 191 GLU 191 132 153 GLU GLU B . n 
B 1 192 LYS 192 133 154 LYS LYS B . n 
B 1 193 TYR 193 134 155 TYR TYR B . n 
B 1 194 GLY 194 135 156 GLY GLY B . n 
B 1 195 ILE 195 136 157 ILE ILE B . n 
B 1 196 PRO 196 137 158 PRO PRO B . n 
B 1 197 TYR 197 138 159 TYR TYR B . n 
B 1 198 PHE 198 139 160 PHE PHE B . n 
B 1 199 GLU 199 140 161 GLU GLU B . n 
B 1 200 THR 200 141 162 THR THR B . n 
B 1 201 SER 201 142 163 SER SER B . n 
B 1 202 ALA 202 143 164 ALA ALA B . n 
B 1 203 ALA 203 144 165 ALA ALA B . n 
B 1 204 ASN 204 145 166 ASN ASN B . n 
B 1 205 GLY 205 146 167 GLY GLY B . n 
B 1 206 THR 206 147 168 THR THR B . n 
B 1 207 ASN 207 148 169 ASN ASN B . n 
B 1 208 ILE 208 149 170 ILE ILE B . n 
B 1 209 SER 209 150 171 SER SER B . n 
B 1 210 GLN 210 151 172 GLN GLN B . n 
B 1 211 ALA 211 152 173 ALA ALA B . n 
B 1 212 ILE 212 153 174 ILE ILE B . n 
B 1 213 GLU 213 154 175 GLU GLU B . n 
B 1 214 MET 214 155 176 MET MET B . n 
B 1 215 LEU 215 156 177 LEU LEU B . n 
B 1 216 LEU 216 157 178 LEU LEU B . n 
B 1 217 ASP 217 158 179 ASP ASP B . n 
B 1 218 LEU 218 159 180 LEU LEU B . n 
B 1 219 ILE 219 160 181 ILE ILE B . n 
B 1 220 MET 220 161 182 MET MET B . n 
B 1 221 LYS 221 162 183 LYS LYS B . n 
B 1 222 ARG 222 163 184 ARG ARG B . n 
B 1 223 MET 223 164 185 MET MET B . n 
B 1 224 GLU 224 165 186 GLU GLU B . n 
B 1 225 ARG 225 166 187 ARG ARG B . n 
B 1 226 SER 226 167 188 SER SER B . n 
B 1 227 VAL 227 168 ?   ?   ?   B . n 
B 1 228 ASP 228 169 ?   ?   ?   B . n 
B 1 229 LYS 229 170 ?   ?   ?   B . n 
B 1 230 SER 230 171 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WTO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WTO 
_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 
C 2 GNP 1  201 201 GNP GNP A . 
D 3 GOL 1  202 301 GOL GOL A . 
E 3 GOL 1  203 401 GOL GOL A . 
F 3 GOL 1  204 501 GOL GOL A . 
G 4 WTO 1  205 123 WTO CC4 A . 
H 5 MG  1  206 4   MG  MG  A . 
I 2 GNP 1  201 201 GNP GNP B . 
J 3 GOL 1  202 301 GOL GOL B . 
K 4 WTO 1  203 123 WTO CC4 B . 
L 5 MG  1  204 3   MG  MG  B . 
M 6 HOH 1  301 5   HOH HOH A . 
M 6 HOH 2  302 25  HOH HOH A . 
M 6 HOH 3  303 31  HOH HOH A . 
M 6 HOH 4  304 60  HOH HOH A . 
M 6 HOH 5  305 3   HOH HOH A . 
M 6 HOH 6  306 13  HOH HOH A . 
M 6 HOH 7  307 26  HOH HOH A . 
M 6 HOH 8  308 4   HOH HOH A . 
M 6 HOH 9  309 16  HOH HOH A . 
M 6 HOH 10 310 8   HOH HOH A . 
M 6 HOH 11 311 27  HOH HOH A . 
M 6 HOH 12 312 39  HOH HOH A . 
M 6 HOH 13 313 59  HOH HOH A . 
M 6 HOH 14 314 58  HOH HOH A . 
M 6 HOH 15 315 17  HOH HOH A . 
M 6 HOH 16 316 18  HOH HOH A . 
M 6 HOH 17 317 9   HOH HOH A . 
M 6 HOH 18 318 56  HOH HOH A . 
M 6 HOH 19 319 10  HOH HOH A . 
M 6 HOH 20 320 32  HOH HOH A . 
M 6 HOH 21 321 50  HOH HOH A . 
M 6 HOH 22 322 52  HOH HOH A . 
M 6 HOH 23 323 51  HOH HOH A . 
N 6 HOH 1  301 42  HOH HOH B . 
N 6 HOH 2  302 54  HOH HOH B . 
N 6 HOH 3  303 35  HOH HOH B . 
N 6 HOH 4  304 36  HOH HOH B . 
N 6 HOH 5  305 47  HOH HOH B . 
N 6 HOH 6  306 24  HOH HOH B . 
N 6 HOH 7  307 57  HOH HOH B . 
N 6 HOH 8  308 61  HOH HOH B . 
N 6 HOH 9  309 46  HOH HOH B . 
N 6 HOH 10 310 41  HOH HOH B . 
N 6 HOH 11 311 55  HOH HOH B . 
N 6 HOH 12 312 48  HOH HOH B . 
N 6 HOH 13 313 2   HOH HOH B . 
N 6 HOH 14 314 11  HOH HOH B . 
N 6 HOH 15 315 7   HOH HOH B . 
N 6 HOH 16 316 62  HOH HOH B . 
N 6 HOH 17 317 40  HOH HOH B . 
N 6 HOH 18 318 45  HOH HOH B . 
N 6 HOH 19 319 44  HOH HOH B . 
N 6 HOH 20 320 43  HOH HOH B . 
N 6 HOH 21 321 6   HOH HOH B . 
N 6 HOH 22 322 23  HOH HOH B . 
N 6 HOH 23 323 49  HOH HOH B . 
N 6 HOH 24 324 37  HOH HOH B . 
# 
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 TYR -8  ? CG  ? A TYR 44  CG  
2  1 Y 1 A TYR -8  ? CD1 ? A TYR 44  CD1 
3  1 Y 1 A TYR -8  ? CD2 ? A TYR 44  CD2 
4  1 Y 1 A TYR -8  ? CE1 ? A TYR 44  CE1 
5  1 Y 1 A TYR -8  ? CE2 ? A TYR 44  CE2 
6  1 Y 1 A TYR -8  ? CZ  ? A TYR 44  CZ  
7  1 Y 1 A TYR -8  ? OH  ? A TYR 44  OH  
8  1 Y 1 A ARG 46  ? CG  ? A ARG 102 CG  
9  1 Y 1 A ARG 46  ? CD  ? A ARG 102 CD  
10 1 Y 1 A ARG 46  ? NE  ? A ARG 102 NE  
11 1 Y 1 A ARG 46  ? CZ  ? A ARG 102 CZ  
12 1 Y 1 A ARG 46  ? NH1 ? A ARG 102 NH1 
13 1 Y 1 A ARG 46  ? NH2 ? A ARG 102 NH2 
14 1 Y 1 B GLU -31 ? CG  ? B GLU 8   CG  
15 1 Y 1 B GLU -31 ? CD  ? B GLU 8   CD  
16 1 Y 1 B GLU -31 ? OE1 ? B GLU 8   OE1 
17 1 Y 1 B GLU -31 ? OE2 ? B GLU 8   OE2 
18 1 Y 1 B GLU -30 ? CG  ? B GLU 9   CG  
19 1 Y 1 B GLU -30 ? CD  ? B GLU 9   CD  
20 1 Y 1 B GLU -30 ? OE1 ? B GLU 9   OE1 
21 1 Y 1 B GLU -30 ? OE2 ? B GLU 9   OE2 
22 1 Y 1 B GLU -9  ? CG  ? B GLU 30  CG  
23 1 Y 1 B GLU -9  ? CD  ? B GLU 30  CD  
24 1 Y 1 B GLU -9  ? OE1 ? B GLU 30  OE1 
25 1 Y 1 B GLU -9  ? OE2 ? B GLU 30  OE2 
26 1 Y 1 B GLU 132 ? CG  ? B GLU 191 CG  
27 1 Y 1 B GLU 132 ? CD  ? B GLU 191 CD  
28 1 Y 1 B GLU 132 ? OE1 ? B GLU 191 OE1 
29 1 Y 1 B GLU 132 ? OE2 ? B GLU 191 OE2 
30 1 Y 1 B LYS 133 ? CG  ? B LYS 192 CG  
31 1 Y 1 B LYS 133 ? CD  ? B LYS 192 CD  
32 1 Y 1 B LYS 133 ? CE  ? B LYS 192 CE  
33 1 Y 1 B LYS 133 ? NZ  ? B LYS 192 NZ  
34 1 Y 1 B GLU 165 ? CG  ? B GLU 224 CG  
35 1 Y 1 B GLU 165 ? CD  ? B GLU 224 CD  
36 1 Y 1 B GLU 165 ? OE1 ? B GLU 224 OE1 
37 1 Y 1 B GLU 165 ? OE2 ? B GLU 224 OE2 
38 1 Y 1 B ARG 166 ? CG  ? B ARG 225 CG  
39 1 Y 1 B ARG 166 ? CD  ? B ARG 225 CD  
40 1 Y 1 B ARG 166 ? NE  ? B ARG 225 NE  
41 1 Y 1 B ARG 166 ? CZ  ? B ARG 225 CZ  
42 1 Y 1 B ARG 166 ? NH1 ? B ARG 225 NH1 
43 1 Y 1 B ARG 166 ? NH2 ? B ARG 225 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.17_3644: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8P3H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.172 
_cell.length_a_esd                 ? 
_cell.length_b                     77.696 
_cell.length_b_esd                 ? 
_cell.length_c                     116.150 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8P3H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8P3H 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.70 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.15 M NH4SO4, 0.1 M MES, pH 6.0, 15% PEG 4K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8P3H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.76 
_reflns.d_resolution_low                               58.08 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     14556 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.68 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.21 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.972 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.76 
_reflns_shell.d_res_low                                     2.859 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1419 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.227 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8P3H 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.76 
_refine.ls_d_res_low                             58.08 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     14547 
_refine.ls_number_reflns_R_free                  724 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.39 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2309 
_refine.ls_R_factor_R_free                       0.3128 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2267 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.96 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3311 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         90 
_refine_hist.number_atoms_solvent             47 
_refine_hist.number_atoms_total               3448 
_refine_hist.d_res_high                       2.76 
_refine_hist.d_res_low                        58.08 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 3460 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.131  ? 4662 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 24.332 ? 477  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 509  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 580  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.76 2.97  . . 143 2662 98.00  . . . . 0.3005 . . . . . . . . . . . 0.3895 
'X-RAY DIFFRACTION' 2.97 3.27  . . 150 2713 100.00 . . . . 0.2503 . . . . . . . . . . . 0.3377 
'X-RAY DIFFRACTION' 3.27 3.74  . . 144 2741 100.00 . . . . 0.2299 . . . . . . . . . . . 0.3017 
'X-RAY DIFFRACTION' 3.74 4.71  . . 139 2784 100.00 . . . . 0.1909 . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 4.71 58.08 . . 148 2923 100.00 . . . . 0.2293 . . . . . . . . . . . 0.2876 
# 
_struct.entry_id                     8P3H 
_struct.title                        'Fusion hSlp2-a_Rab27A bound to covalent hit fragment IMP-1712' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8P3H 
_struct_keywords.text            
;Small GTPase, Targeted Covalent Inhibitors, High Throughput screening, Drug Discovery, Vesicle trafficking, Breast Cancer, CYTOSOLIC PROTEIN
;
_struct_keywords.pdbx_keywords   'CYTOSOLIC PROTEIN' 
# 
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 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SYTL2_HUMAN Q9HCH5 ? 1 SFLTEEEQEAIMKVLQRDAALKRAEEER 5 
2 UNP RB27A_HUMAN P51159 ? 1 
;MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGQER
FRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYF
ETSAANGTNISQAIEMLLDLIMKRMERCVDKS
;
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 8P3H A 4  ? 31  A Q9HCH5 5 ? 32  ? -35 -9  
2 2 8P3H A 39 I 230 ? P51159 1 ? 192 ? -9  174 
3 1 8P3H B 4  ? 31  A Q9HCH5 5 ? 32  ? -35 -9  
4 2 8P3H B 39 I 230 ? P51159 1 ? 192 ? -9  171 
# 
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 8P3H GLY A 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 1  
1 8P3H HIS A 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 2  
1 8P3H MET A 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 3  
1 8P3H GLY A 32  B UNP Q9HCH5 ?   ?   linker                -9  4  
1 8P3H SER A 33  C UNP Q9HCH5 ?   ?   linker                -9  5  
1 8P3H GLY A 34  D UNP Q9HCH5 ?   ?   linker                -9  6  
1 8P3H SER A 35  E UNP Q9HCH5 ?   ?   linker                -9  7  
1 8P3H GLY A 36  F UNP Q9HCH5 ?   ?   linker                -9  8  
1 8P3H SER A 37  G UNP Q9HCH5 ?   ?   linker                -9  9  
1 8P3H GLY A 38  H UNP Q9HCH5 ?   ?   linker                -9  10 
2 8P3H LEU A 116 ? UNP P51159 GLN 78  'engineered mutation' 60  11 
2 8P3H SER A 226 ? UNP P51159 CYS 188 'engineered mutation' 170 12 
3 8P3H GLY B 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 13 
3 8P3H HIS B 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 14 
3 8P3H MET B 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 15 
3 8P3H GLY B 32  B UNP Q9HCH5 ?   ?   linker                -9  16 
3 8P3H SER B 33  C UNP Q9HCH5 ?   ?   linker                -9  17 
3 8P3H GLY B 34  D UNP Q9HCH5 ?   ?   linker                -9  18 
3 8P3H SER B 35  E UNP Q9HCH5 ?   ?   linker                -9  19 
3 8P3H GLY B 36  F UNP Q9HCH5 ?   ?   linker                -9  20 
3 8P3H SER B 37  G UNP Q9HCH5 ?   ?   linker                -9  21 
3 8P3H GLY B 38  H UNP Q9HCH5 ?   ?   linker                -9  22 
4 8P3H LEU B 116 ? UNP P51159 GLN 78  'engineered mutation' 57  23 
4 8P3H SER B 226 ? UNP P51159 CYS 188 'engineered mutation' 167 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5900  ? 
1 MORE         -47   ? 
1 'SSA (A^2)'  18140 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 7   ? ARG A 26  ? THR A -32 ARG A -13 1 ? 20 
HELX_P HELX_P2  AA2 GLY A 59  ? GLY A 70  ? GLY A 7   GLY A 18  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 116 ? ARG A 118 ? LEU A 60  ARG A 62  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 119 ? ALA A 125 ? PHE A 63  ALA A 69  1 ? 7  
HELX_P HELX_P5  AA5 ASN A 141 ? ALA A 159 ? ASN A 85  ALA A 103 1 ? 19 
HELX_P HELX_P6  AA6 LYS A 182 ? GLY A 194 ? LYS A 126 GLY A 138 1 ? 13 
HELX_P HELX_P7  AA7 ASN A 207 ? LYS A 221 ? ASN A 151 LYS A 165 1 ? 15 
HELX_P HELX_P8  AA8 THR B 7   ? GLU B 29  ? THR B -32 GLU B -10 1 ? 23 
HELX_P HELX_P9  AA9 GLY B 59  ? GLY B 70  ? GLY B 7   GLY B 18  1 ? 12 
HELX_P HELX_P10 AB1 PHE B 119 ? PHE B 127 ? PHE B 60  PHE B 68  1 ? 9  
HELX_P HELX_P11 AB2 ASN B 141 ? ASN B 147 ? ASN B 82  ASN B 88  1 ? 7  
HELX_P HELX_P12 AB3 ASN B 147 ? HIS B 158 ? ASN B 88  HIS B 99  1 ? 12 
HELX_P HELX_P13 AB4 LYS B 182 ? GLY B 194 ? LYS B 123 GLY B 135 1 ? 13 
HELX_P HELX_P14 AB5 ASN B 207 ? MET B 223 ? ASN B 148 MET B 164 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale none ? A CYS 161 SG  ? ? ? 1_555 G WTO . C08 ? ? A CYS 105 A WTO 205 1_555 ? ? ? ? ? ? ? 1.830 ? ? 
covale2  covale none ? B CYS 161 SG  ? ? ? 1_555 K WTO . C08 ? ? B CYS 102 B WTO 203 1_555 ? ? ? ? ? ? ? 1.828 ? ? 
metalc1  metalc ?    ? A THR 61  OG1 ? ? ? 1_555 H MG  . MG  ? ? A THR 9   A MG  206 1_555 ? ? ? ? ? ? ? 1.951 ? ? 
metalc2  metalc ?    ? A THR 79  OG1 ? ? ? 1_555 H MG  . MG  ? ? A THR 27  A MG  206 1_555 ? ? ? ? ? ? ? 1.904 ? ? 
metalc3  metalc ?    ? C GNP .   O3G ? ? ? 1_555 H MG  . MG  ? ? A GNP 201 A MG  206 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc4  metalc ?    ? C GNP .   O1B ? ? ? 1_555 H MG  . MG  ? ? A GNP 201 A MG  206 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc5  metalc ?    ? H MG  .   MG  ? ? ? 1_555 M HOH . O   ? ? A MG  206 A HOH 305 1_555 ? ? ? ? ? ? ? 1.839 ? ? 
metalc6  metalc ?    ? H MG  .   MG  ? ? ? 1_555 M HOH . O   ? ? A MG  206 A HOH 308 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc7  metalc ?    ? B THR 61  OG1 ? ? ? 1_555 L MG  . MG  ? ? B THR 9   B MG  204 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc8  metalc ?    ? B THR 79  OG1 ? ? ? 1_555 L MG  . MG  ? ? B THR 27  B MG  204 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc9  metalc ?    ? I GNP .   O2G ? ? ? 1_555 L MG  . MG  ? ? B GNP 201 B MG  204 1_555 ? ? ? ? ? ? ? 1.762 ? ? 
metalc10 metalc ?    ? I GNP .   O1B ? ? ? 1_555 L MG  . MG  ? ? B GNP 201 B MG  204 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc11 metalc ?    ? L MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? B MG  204 B HOH 303 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc12 metalc ?    ? L MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? B MG  204 B HOH 304 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 61 ? A THR 9   ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 OG1 ? A THR 79 ? A THR 27  ? 1_555 83.8  ? 
2  OG1 ? A THR 61 ? A THR 9   ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O3G ? C GNP .  ? A GNP 201 ? 1_555 174.5 ? 
3  OG1 ? A THR 79 ? A THR 27  ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O3G ? C GNP .  ? A GNP 201 ? 1_555 91.5  ? 
4  OG1 ? A THR 61 ? A THR 9   ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 100.3 ? 
5  OG1 ? A THR 79 ? A THR 27  ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 162.3 ? 
6  O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 85.0  ? 
7  OG1 ? A THR 61 ? A THR 9   ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 305 ? 1_555 94.7  ? 
8  OG1 ? A THR 79 ? A THR 27  ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 305 ? 1_555 83.6  ? 
9  O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 305 ? 1_555 82.1  ? 
10 O1B ? C GNP .  ? A GNP 201 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 305 ? 1_555 113.0 ? 
11 OG1 ? A THR 61 ? A THR 9   ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 308 ? 1_555 85.1  ? 
12 OG1 ? A THR 79 ? A THR 27  ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 308 ? 1_555 84.0  ? 
13 O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 308 ? 1_555 97.1  ? 
14 O1B ? C GNP .  ? A GNP 201 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 308 ? 1_555 79.3  ? 
15 O   ? M HOH .  ? A HOH 305 ? 1_555 MG ? H MG . ? A MG 206 ? 1_555 O   ? M HOH .  ? A HOH 308 ? 1_555 167.5 ? 
16 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 OG1 ? B THR 79 ? B THR 27  ? 1_555 80.2  ? 
17 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O2G ? I GNP .  ? B GNP 201 ? 1_555 160.8 ? 
18 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O2G ? I GNP .  ? B GNP 201 ? 1_555 109.3 ? 
19 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 85.1  ? 
20 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 164.8 ? 
21 O2G ? I GNP .  ? B GNP 201 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 83.7  ? 
22 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 303 ? 1_555 86.7  ? 
23 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 303 ? 1_555 98.2  ? 
24 O2G ? I GNP .  ? B GNP 201 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 303 ? 1_555 75.6  ? 
25 O1B ? I GNP .  ? B GNP 201 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 303 ? 1_555 76.7  ? 
26 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 304 ? 1_555 96.5  ? 
27 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 304 ? 1_555 111.7 ? 
28 O2G ? I GNP .  ? B GNP 201 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 304 ? 1_555 95.3  ? 
29 O1B ? I GNP .  ? B GNP 201 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 304 ? 1_555 73.9  ? 
30 O   ? N HOH .  ? B HOH 303 ? 1_555 MG ? L MG . ? B MG 204 ? 1_555 O   ? N HOH .  ? B HOH 304 ? 1_555 150.0 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 WTO G . ? CYS A 161 ? WTO A 205 ? 1_555 CYS A 105 ? 1_555 C08 SG CYS 1 WTO None 'Covalent chemical modification' 
2 WTO K . ? CYS B 161 ? WTO B 203 ? 1_555 CYS B 102 ? 1_555 C08 SG CYS 1 WTO None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? 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 ILE A 82  ? ARG A 92  ? ILE A 30  ARG A 40  
AA1 2 GLY A 103 ? THR A 113 ? GLY A 47  THR A 57  
AA1 3 TYR A 46  ? LEU A 53  ? TYR A -6  LEU A 1   
AA1 4 PHE A 133 ? ASP A 138 ? PHE A 77  ASP A 82  
AA1 5 ILE A 166 ? ASN A 171 ? ILE A 110 ASN A 115 
AA1 6 TYR A 197 ? PHE A 198 ? TYR A 141 PHE A 142 
AA2 1 ILE B 82  ? TYR B 91  ? ILE B 30  TYR B 39  
AA2 2 GLN B 104 ? THR B 113 ? GLN B 45  THR B 54  
AA2 3 TYR B 46  ? GLY B 54  ? TYR B -6  GLY B 2   
AA2 4 GLY B 132 ? ASP B 138 ? GLY B 73  ASP B 79  
AA2 5 ASP B 165 ? ASN B 171 ? ASP B 106 ASN B 112 
AA2 6 TYR B 197 ? GLU B 199 ? TYR B 138 GLU B 140 
# 
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 N TYR A 91  ? N TYR A 39  O GLN A 104 ? O GLN A 48  
AA1 2 3 O TRP A 111 ? O TRP A 55  N PHE A 50  ? N PHE A -2  
AA1 3 4 N LEU A 53  ? N LEU A 1   O LEU A 136 ? O LEU A 80  
AA1 4 5 N LEU A 135 ? N LEU A 79  O CYS A 169 ? O CYS A 113 
AA1 5 6 N GLY A 170 ? N GLY A 114 O PHE A 198 ? O PHE A 142 
AA2 1 2 N ASP B 83  ? N ASP B 31  O ASP B 112 ? O ASP B 53  
AA2 2 3 O TRP B 111 ? O TRP B 52  N PHE B 50  ? N PHE B -2  
AA2 3 4 N LEU B 53  ? N LEU B 1   O LEU B 136 ? O LEU B 77  
AA2 4 5 N PHE B 137 ? N PHE B 78  O ASN B 171 ? O ASN B 112 
AA2 5 6 N GLY B 170 ? N GLY B 111 O PHE B 198 ? O PHE B 139 
# 
_pdbx_entry_details.entry_id                   8P3H 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B TYR 101 ? ? N   B CYS 102 ? ? 1.64 
2 1 NH2 A ARG 72  ? ? OD2 B ASP -18 ? ? 2.15 
3 1 O   A GLN 100 ? ? O   A HOH 301 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O  A TYR 104 ? ? C A TYR 104 ? ? N  A CYS 105 ? ? 89.90  122.70 -32.80 1.60 Y 
2 1 C  A CYS 105 ? ? N A GLU 106 ? ? CA A GLU 106 ? ? 88.09  121.70 -33.61 2.50 Y 
3 1 CA B TYR 101 ? ? C B TYR 101 ? ? N  B CYS 102 ? ? 130.64 117.20 13.44  2.20 Y 
4 1 O  B TYR 101 ? ? C B TYR 101 ? ? N  B CYS 102 ? ? 76.06  122.70 -46.64 1.60 Y 
5 1 C  B TYR 101 ? ? N B CYS 102 ? ? CA B CYS 102 ? ? 136.75 121.70 15.05  2.50 Y 
6 1 O  B CYS 102 ? ? C B CYS 102 ? ? N  B GLU 103 ? ? 104.08 122.70 -18.62 1.60 Y 
# 
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 THR A 44  ? ? -138.77 -158.85 
2  1 CYS A 105 ? ? -27.55  142.62  
3  1 GLU A 106 ? ? -122.76 -169.68 
4  1 LEU A 119 ? ? -107.03 60.08   
5  1 PRO A 140 ? ? -46.91  152.36  
6  1 ASN A 151 ? ? 65.72   -8.11   
7  1 GLU A 168 ? ? -40.08  -73.79  
8  1 ARG A 169 ? ? -102.81 52.18   
9  1 PHE B -34 ? ? 33.29   65.91   
10 1 LEU B -33 ? ? 162.60  99.92   
11 1 ASP B -7  ? ? -81.89  -80.13  
12 1 LYS B 35  ? ? -175.41 130.34  
13 1 ARG B 43  ? ? -179.77 149.79  
14 1 CYS B 102 ? ? -175.39 131.50  
15 1 LYS B 113 ? ? 72.29   38.49   
16 1 LEU B 116 ? ? -103.92 48.40   
17 1 VAL B 121 ? ? -136.91 -36.46  
18 1 ASN B 148 ? ? 65.49   -0.45   
19 1 MET B 164 ? ? -61.81  73.25   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 CYS A 105 ? ? GLU A 106 ? ? 136.18  
2 1 CYS B 102 ? ? GLU B 103 ? ? -138.55 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 TYR A 104 ? ? 34.88  
2 1 TYR B 101 ? ? -46.40 
3 1 CYS B 102 ? ? 27.18  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       323 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   8.29 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -38 ? A GLY 1   
2  1 Y 1 A HIS -37 ? A HIS 2   
3  1 Y 1 A MET -36 ? A MET 3   
4  1 Y 1 A ARG -9  A A ARG 31  
5  1 Y 1 A GLY -9  B A GLY 32  
6  1 Y 1 A SER -9  C A SER 33  
7  1 Y 1 A GLY -9  D A GLY 34  
8  1 Y 1 A SER -9  E A SER 35  
9  1 Y 1 A GLY -9  F A GLY 36  
10 1 Y 1 A SER -9  G A SER 37  
11 1 Y 1 A GLY -9  H A GLY 38  
12 1 Y 1 A MET -9  I A MET 39  
13 1 Y 1 A SER -9  J A SER 40  
14 1 Y 1 A ASP -9  K A ASP 41  
15 1 Y 1 A GLY -9  L A GLY 42  
16 1 Y 1 A ASP -9  M A ASP 43  
17 1 Y 1 A GLY 42  A A GLY 95  
18 1 Y 1 A PRO 42  B A PRO 96  
19 1 Y 1 A ASP 42  C A ASP 97  
20 1 Y 1 A GLY 42  D A GLY 98  
21 1 Y 1 A VAL 171 ? A VAL 227 
22 1 Y 1 A ASP 172 ? A ASP 228 
23 1 Y 1 A LYS 173 ? A LYS 229 
24 1 Y 1 A SER 174 ? A SER 230 
25 1 Y 1 B GLY -38 ? B GLY 1   
26 1 Y 1 B HIS -37 ? B HIS 2   
27 1 Y 1 B MET -36 ? B MET 3   
28 1 Y 1 B ARG -9  A B ARG 31  
29 1 Y 1 B GLY -9  B B GLY 32  
30 1 Y 1 B SER -9  C B SER 33  
31 1 Y 1 B GLY -9  D B GLY 34  
32 1 Y 1 B SER -9  E B SER 35  
33 1 Y 1 B GLY -9  F B GLY 36  
34 1 Y 1 B SER -9  G B SER 37  
35 1 Y 1 B GLY -9  H B GLY 38  
36 1 Y 1 B MET -9  I B MET 39  
37 1 Y 1 B SER -9  J B SER 40  
38 1 Y 1 B ASP -9  K B ASP 41  
39 1 Y 1 B GLY -9  L B GLY 42  
40 1 Y 1 B ASP -9  M B ASP 43  
41 1 Y 1 B SER 41  A B SER 94  
42 1 Y 1 B GLY 41  B B GLY 95  
43 1 Y 1 B PRO 41  C B PRO 96  
44 1 Y 1 B ASP 41  D B ASP 97  
45 1 Y 1 B GLY 41  E B GLY 98  
46 1 Y 1 B ALA 41  F B ALA 99  
47 1 Y 1 B THR 41  G B THR 100 
48 1 Y 1 B VAL 168 ? B VAL 227 
49 1 Y 1 B ASP 169 ? B ASP 228 
50 1 Y 1 B LYS 170 ? B LYS 229 
51 1 Y 1 B SER 171 ? B SER 230 
# 
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  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GNP PG     P  N N 137 
GNP O1G    O  N N 138 
GNP O2G    O  N N 139 
GNP O3G    O  N N 140 
GNP N3B    N  N N 141 
GNP PB     P  N R 142 
GNP O1B    O  N N 143 
GNP O2B    O  N N 144 
GNP O3A    O  N N 145 
GNP PA     P  N S 146 
GNP O1A    O  N N 147 
GNP O2A    O  N N 148 
GNP "O5'"  O  N N 149 
GNP "C5'"  C  N N 150 
GNP "C4'"  C  N R 151 
GNP "O4'"  O  N N 152 
GNP "C3'"  C  N S 153 
GNP "O3'"  O  N N 154 
GNP "C2'"  C  N R 155 
GNP "O2'"  O  N N 156 
GNP "C1'"  C  N R 157 
GNP N9     N  Y N 158 
GNP C8     C  Y N 159 
GNP N7     N  Y N 160 
GNP C5     C  Y N 161 
GNP C6     C  Y N 162 
GNP O6     O  N N 163 
GNP N1     N  Y N 164 
GNP C2     C  Y N 165 
GNP N2     N  N N 166 
GNP N3     N  Y N 167 
GNP C4     C  Y N 168 
GNP HOG2   H  N N 169 
GNP HOG3   H  N N 170 
GNP HNB3   H  N N 171 
GNP HOB2   H  N N 172 
GNP HOA2   H  N N 173 
GNP "H5'2" H  N N 174 
GNP "H5'1" H  N N 175 
GNP "H4'"  H  N N 176 
GNP "H3'"  H  N N 177 
GNP "HO3'" H  N N 178 
GNP "H2'"  H  N N 179 
GNP "HO2'" H  N N 180 
GNP "H1'"  H  N N 181 
GNP H8     H  N N 182 
GNP HN1    H  N N 183 
GNP HN21   H  N N 184 
GNP HN22   H  N N 185 
GOL C1     C  N N 186 
GOL O1     O  N N 187 
GOL C2     C  N N 188 
GOL O2     O  N N 189 
GOL C3     C  N N 190 
GOL O3     O  N N 191 
GOL H11    H  N N 192 
GOL H12    H  N N 193 
GOL HO1    H  N N 194 
GOL H2     H  N N 195 
GOL HO2    H  N N 196 
GOL H31    H  N N 197 
GOL H32    H  N N 198 
GOL HO3    H  N N 199 
HIS N      N  N N 200 
HIS CA     C  N S 201 
HIS C      C  N N 202 
HIS O      O  N N 203 
HIS CB     C  N N 204 
HIS CG     C  Y N 205 
HIS ND1    N  Y N 206 
HIS CD2    C  Y N 207 
HIS CE1    C  Y N 208 
HIS NE2    N  Y N 209 
HIS OXT    O  N N 210 
HIS H      H  N N 211 
HIS H2     H  N N 212 
HIS HA     H  N N 213 
HIS HB2    H  N N 214 
HIS HB3    H  N N 215 
HIS HD1    H  N N 216 
HIS HD2    H  N N 217 
HIS HE1    H  N N 218 
HIS HE2    H  N N 219 
HIS HXT    H  N N 220 
HOH O      O  N N 221 
HOH H1     H  N N 222 
HOH H2     H  N N 223 
ILE N      N  N N 224 
ILE CA     C  N S 225 
ILE C      C  N N 226 
ILE O      O  N N 227 
ILE CB     C  N S 228 
ILE CG1    C  N N 229 
ILE CG2    C  N N 230 
ILE CD1    C  N N 231 
ILE OXT    O  N N 232 
ILE H      H  N N 233 
ILE H2     H  N N 234 
ILE HA     H  N N 235 
ILE HB     H  N N 236 
ILE HG12   H  N N 237 
ILE HG13   H  N N 238 
ILE HG21   H  N N 239 
ILE HG22   H  N N 240 
ILE HG23   H  N N 241 
ILE HD11   H  N N 242 
ILE HD12   H  N N 243 
ILE HD13   H  N N 244 
ILE HXT    H  N N 245 
LEU N      N  N N 246 
LEU CA     C  N S 247 
LEU C      C  N N 248 
LEU O      O  N N 249 
LEU CB     C  N N 250 
LEU CG     C  N N 251 
LEU CD1    C  N N 252 
LEU CD2    C  N N 253 
LEU OXT    O  N N 254 
LEU H      H  N N 255 
LEU H2     H  N N 256 
LEU HA     H  N N 257 
LEU HB2    H  N N 258 
LEU HB3    H  N N 259 
LEU HG     H  N N 260 
LEU HD11   H  N N 261 
LEU HD12   H  N N 262 
LEU HD13   H  N N 263 
LEU HD21   H  N N 264 
LEU HD22   H  N N 265 
LEU HD23   H  N N 266 
LEU HXT    H  N N 267 
LYS N      N  N N 268 
LYS CA     C  N S 269 
LYS C      C  N N 270 
LYS O      O  N N 271 
LYS CB     C  N N 272 
LYS CG     C  N N 273 
LYS CD     C  N N 274 
LYS CE     C  N N 275 
LYS NZ     N  N N 276 
LYS OXT    O  N N 277 
LYS H      H  N N 278 
LYS H2     H  N N 279 
LYS HA     H  N N 280 
LYS HB2    H  N N 281 
LYS HB3    H  N N 282 
LYS HG2    H  N N 283 
LYS HG3    H  N N 284 
LYS HD2    H  N N 285 
LYS HD3    H  N N 286 
LYS HE2    H  N N 287 
LYS HE3    H  N N 288 
LYS HZ1    H  N N 289 
LYS HZ2    H  N N 290 
LYS HZ3    H  N N 291 
LYS HXT    H  N N 292 
MET N      N  N N 293 
MET CA     C  N S 294 
MET C      C  N N 295 
MET O      O  N N 296 
MET CB     C  N N 297 
MET CG     C  N N 298 
MET SD     S  N N 299 
MET CE     C  N N 300 
MET OXT    O  N N 301 
MET H      H  N N 302 
MET H2     H  N N 303 
MET HA     H  N N 304 
MET HB2    H  N N 305 
MET HB3    H  N N 306 
MET HG2    H  N N 307 
MET HG3    H  N N 308 
MET HE1    H  N N 309 
MET HE2    H  N N 310 
MET HE3    H  N N 311 
MET HXT    H  N N 312 
MG  MG     MG N N 313 
PHE N      N  N N 314 
PHE CA     C  N S 315 
PHE C      C  N N 316 
PHE O      O  N N 317 
PHE CB     C  N N 318 
PHE CG     C  Y N 319 
PHE CD1    C  Y N 320 
PHE CD2    C  Y N 321 
PHE CE1    C  Y N 322 
PHE CE2    C  Y N 323 
PHE CZ     C  Y N 324 
PHE OXT    O  N N 325 
PHE H      H  N N 326 
PHE H2     H  N N 327 
PHE HA     H  N N 328 
PHE HB2    H  N N 329 
PHE HB3    H  N N 330 
PHE HD1    H  N N 331 
PHE HD2    H  N N 332 
PHE HE1    H  N N 333 
PHE HE2    H  N N 334 
PHE HZ     H  N N 335 
PHE HXT    H  N N 336 
PRO N      N  N N 337 
PRO CA     C  N S 338 
PRO C      C  N N 339 
PRO O      O  N N 340 
PRO CB     C  N N 341 
PRO CG     C  N N 342 
PRO CD     C  N N 343 
PRO OXT    O  N N 344 
PRO H      H  N N 345 
PRO HA     H  N N 346 
PRO HB2    H  N N 347 
PRO HB3    H  N N 348 
PRO HG2    H  N N 349 
PRO HG3    H  N N 350 
PRO HD2    H  N N 351 
PRO HD3    H  N N 352 
PRO HXT    H  N N 353 
SER N      N  N N 354 
SER CA     C  N S 355 
SER C      C  N N 356 
SER O      O  N N 357 
SER CB     C  N N 358 
SER OG     O  N N 359 
SER OXT    O  N N 360 
SER H      H  N N 361 
SER H2     H  N N 362 
SER HA     H  N N 363 
SER HB2    H  N N 364 
SER HB3    H  N N 365 
SER HG     H  N N 366 
SER HXT    H  N N 367 
THR N      N  N N 368 
THR CA     C  N S 369 
THR C      C  N N 370 
THR O      O  N N 371 
THR CB     C  N R 372 
THR OG1    O  N N 373 
THR CG2    C  N N 374 
THR OXT    O  N N 375 
THR H      H  N N 376 
THR H2     H  N N 377 
THR HA     H  N N 378 
THR HB     H  N N 379 
THR HG1    H  N N 380 
THR HG21   H  N N 381 
THR HG22   H  N N 382 
THR HG23   H  N N 383 
THR HXT    H  N N 384 
TRP N      N  N N 385 
TRP CA     C  N S 386 
TRP C      C  N N 387 
TRP O      O  N N 388 
TRP CB     C  N N 389 
TRP CG     C  Y N 390 
TRP CD1    C  Y N 391 
TRP CD2    C  Y N 392 
TRP NE1    N  Y N 393 
TRP CE2    C  Y N 394 
TRP CE3    C  Y N 395 
TRP CZ2    C  Y N 396 
TRP CZ3    C  Y N 397 
TRP CH2    C  Y N 398 
TRP OXT    O  N N 399 
TRP H      H  N N 400 
TRP H2     H  N N 401 
TRP HA     H  N N 402 
TRP HB2    H  N N 403 
TRP HB3    H  N N 404 
TRP HD1    H  N N 405 
TRP HE1    H  N N 406 
TRP HE3    H  N N 407 
TRP HZ2    H  N N 408 
TRP HZ3    H  N N 409 
TRP HH2    H  N N 410 
TRP HXT    H  N N 411 
TYR N      N  N N 412 
TYR CA     C  N S 413 
TYR C      C  N N 414 
TYR O      O  N N 415 
TYR CB     C  N N 416 
TYR CG     C  Y N 417 
TYR CD1    C  Y N 418 
TYR CD2    C  Y N 419 
TYR CE1    C  Y N 420 
TYR CE2    C  Y N 421 
TYR CZ     C  Y N 422 
TYR OH     O  N N 423 
TYR OXT    O  N N 424 
TYR H      H  N N 425 
TYR H2     H  N N 426 
TYR HA     H  N N 427 
TYR HB2    H  N N 428 
TYR HB3    H  N N 429 
TYR HD1    H  N N 430 
TYR HD2    H  N N 431 
TYR HE1    H  N N 432 
TYR HE2    H  N N 433 
TYR HH     H  N N 434 
TYR HXT    H  N N 435 
VAL N      N  N N 436 
VAL CA     C  N S 437 
VAL C      C  N N 438 
VAL O      O  N N 439 
VAL CB     C  N N 440 
VAL CG1    C  N N 441 
VAL CG2    C  N N 442 
VAL OXT    O  N N 443 
VAL H      H  N N 444 
VAL H2     H  N N 445 
VAL HA     H  N N 446 
VAL HB     H  N N 447 
VAL HG11   H  N N 448 
VAL HG12   H  N N 449 
VAL HG13   H  N N 450 
VAL HG21   H  N N 451 
VAL HG22   H  N N 452 
VAL HG23   H  N N 453 
VAL HXT    H  N N 454 
WTO C08    C  N N 455 
WTO C09    C  N N 456 
WTO C10    C  N N 457 
WTO C12    C  Y N 458 
WTO C13    C  Y N 459 
WTO C14    C  Y N 460 
WTO C15    C  Y N 461 
WTO C16    C  Y N 462 
WTO C17    C  Y N 463 
WTO C21    C  N S 464 
WTO C22    C  N N 465 
WTO C24    C  N N 466 
WTO C26    C  N N 467 
WTO C27    C  N N 468 
WTO C28    C  N N 469 
WTO N11    N  N N 470 
WTO N20    N  N N 471 
WTO O19    O  N N 472 
WTO O23    O  N N 473 
WTO O25    O  N N 474 
WTO O29    O  N N 475 
WTO O30    O  N N 476 
WTO S18    S  N N 477 
WTO H1     H  N N 478 
WTO H2     H  N N 479 
WTO H3     H  N N 480 
WTO H4     H  N N 481 
WTO H5     H  N N 482 
WTO H6     H  N N 483 
WTO H7     H  N N 484 
WTO H8     H  N N 485 
WTO H9     H  N N 486 
WTO H10    H  N N 487 
WTO H11    H  N N 488 
WTO H12    H  N N 489 
WTO H13    H  N N 490 
WTO H14    H  N N 491 
WTO H15    H  N N 492 
WTO H16    H  N N 493 
WTO H17    H  N N 494 
WTO H18    H  N N 495 
WTO H19    H  N N 496 
WTO H20    H  N N 497 
# 
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  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GNP PG    O1G    doub N N 129 
GNP PG    O2G    sing N N 130 
GNP PG    O3G    sing N N 131 
GNP PG    N3B    sing N N 132 
GNP O2G   HOG2   sing N N 133 
GNP O3G   HOG3   sing N N 134 
GNP N3B   PB     sing N N 135 
GNP N3B   HNB3   sing N N 136 
GNP PB    O1B    doub N N 137 
GNP PB    O2B    sing N N 138 
GNP PB    O3A    sing N N 139 
GNP O2B   HOB2   sing N N 140 
GNP O3A   PA     sing N N 141 
GNP PA    O1A    doub N N 142 
GNP PA    O2A    sing N N 143 
GNP PA    "O5'"  sing N N 144 
GNP O2A   HOA2   sing N N 145 
GNP "O5'" "C5'"  sing N N 146 
GNP "C5'" "C4'"  sing N N 147 
GNP "C5'" "H5'2" sing N N 148 
GNP "C5'" "H5'1" sing N N 149 
GNP "C4'" "O4'"  sing N N 150 
GNP "C4'" "C3'"  sing N N 151 
GNP "C4'" "H4'"  sing N N 152 
GNP "O4'" "C1'"  sing N N 153 
GNP "C3'" "O3'"  sing N N 154 
GNP "C3'" "C2'"  sing N N 155 
GNP "C3'" "H3'"  sing N N 156 
GNP "O3'" "HO3'" sing N N 157 
GNP "C2'" "O2'"  sing N N 158 
GNP "C2'" "C1'"  sing N N 159 
GNP "C2'" "H2'"  sing N N 160 
GNP "O2'" "HO2'" sing N N 161 
GNP "C1'" N9     sing N N 162 
GNP "C1'" "H1'"  sing N N 163 
GNP N9    C8     sing Y N 164 
GNP N9    C4     sing Y N 165 
GNP C8    N7     doub Y N 166 
GNP C8    H8     sing N N 167 
GNP N7    C5     sing Y N 168 
GNP C5    C6     sing Y N 169 
GNP C5    C4     doub Y N 170 
GNP C6    O6     doub N N 171 
GNP C6    N1     sing Y N 172 
GNP N1    C2     sing Y N 173 
GNP N1    HN1    sing N N 174 
GNP C2    N2     sing N N 175 
GNP C2    N3     doub Y N 176 
GNP N2    HN21   sing N N 177 
GNP N2    HN22   sing N N 178 
GNP N3    C4     sing Y N 179 
GOL C1    O1     sing N N 180 
GOL C1    C2     sing N N 181 
GOL C1    H11    sing N N 182 
GOL C1    H12    sing N N 183 
GOL O1    HO1    sing N N 184 
GOL C2    O2     sing N N 185 
GOL C2    C3     sing N N 186 
GOL C2    H2     sing N N 187 
GOL O2    HO2    sing N N 188 
GOL C3    O3     sing N N 189 
GOL C3    H31    sing N N 190 
GOL C3    H32    sing N N 191 
GOL O3    HO3    sing N N 192 
HIS N     CA     sing N N 193 
HIS N     H      sing N N 194 
HIS N     H2     sing N N 195 
HIS CA    C      sing N N 196 
HIS CA    CB     sing N N 197 
HIS CA    HA     sing N N 198 
HIS C     O      doub N N 199 
HIS C     OXT    sing N N 200 
HIS CB    CG     sing N N 201 
HIS CB    HB2    sing N N 202 
HIS CB    HB3    sing N N 203 
HIS CG    ND1    sing Y N 204 
HIS CG    CD2    doub Y N 205 
HIS ND1   CE1    doub Y N 206 
HIS ND1   HD1    sing N N 207 
HIS CD2   NE2    sing Y N 208 
HIS CD2   HD2    sing N N 209 
HIS CE1   NE2    sing Y N 210 
HIS CE1   HE1    sing N N 211 
HIS NE2   HE2    sing N N 212 
HIS OXT   HXT    sing N N 213 
HOH O     H1     sing N N 214 
HOH O     H2     sing N N 215 
ILE N     CA     sing N N 216 
ILE N     H      sing N N 217 
ILE N     H2     sing N N 218 
ILE CA    C      sing N N 219 
ILE CA    CB     sing N N 220 
ILE CA    HA     sing N N 221 
ILE C     O      doub N N 222 
ILE C     OXT    sing N N 223 
ILE CB    CG1    sing N N 224 
ILE CB    CG2    sing N N 225 
ILE CB    HB     sing N N 226 
ILE CG1   CD1    sing N N 227 
ILE CG1   HG12   sing N N 228 
ILE CG1   HG13   sing N N 229 
ILE CG2   HG21   sing N N 230 
ILE CG2   HG22   sing N N 231 
ILE CG2   HG23   sing N N 232 
ILE CD1   HD11   sing N N 233 
ILE CD1   HD12   sing N N 234 
ILE CD1   HD13   sing N N 235 
ILE OXT   HXT    sing N N 236 
LEU N     CA     sing N N 237 
LEU N     H      sing N N 238 
LEU N     H2     sing N N 239 
LEU CA    C      sing N N 240 
LEU CA    CB     sing N N 241 
LEU CA    HA     sing N N 242 
LEU C     O      doub N N 243 
LEU C     OXT    sing N N 244 
LEU CB    CG     sing N N 245 
LEU CB    HB2    sing N N 246 
LEU CB    HB3    sing N N 247 
LEU CG    CD1    sing N N 248 
LEU CG    CD2    sing N N 249 
LEU CG    HG     sing N N 250 
LEU CD1   HD11   sing N N 251 
LEU CD1   HD12   sing N N 252 
LEU CD1   HD13   sing N N 253 
LEU CD2   HD21   sing N N 254 
LEU CD2   HD22   sing N N 255 
LEU CD2   HD23   sing N N 256 
LEU OXT   HXT    sing N N 257 
LYS N     CA     sing N N 258 
LYS N     H      sing N N 259 
LYS N     H2     sing N N 260 
LYS CA    C      sing N N 261 
LYS CA    CB     sing N N 262 
LYS CA    HA     sing N N 263 
LYS C     O      doub N N 264 
LYS C     OXT    sing N N 265 
LYS CB    CG     sing N N 266 
LYS CB    HB2    sing N N 267 
LYS CB    HB3    sing N N 268 
LYS CG    CD     sing N N 269 
LYS CG    HG2    sing N N 270 
LYS CG    HG3    sing N N 271 
LYS CD    CE     sing N N 272 
LYS CD    HD2    sing N N 273 
LYS CD    HD3    sing N N 274 
LYS CE    NZ     sing N N 275 
LYS CE    HE2    sing N N 276 
LYS CE    HE3    sing N N 277 
LYS NZ    HZ1    sing N N 278 
LYS NZ    HZ2    sing N N 279 
LYS NZ    HZ3    sing N N 280 
LYS OXT   HXT    sing N N 281 
MET N     CA     sing N N 282 
MET N     H      sing N N 283 
MET N     H2     sing N N 284 
MET CA    C      sing N N 285 
MET CA    CB     sing N N 286 
MET CA    HA     sing N N 287 
MET C     O      doub N N 288 
MET C     OXT    sing N N 289 
MET CB    CG     sing N N 290 
MET CB    HB2    sing N N 291 
MET CB    HB3    sing N N 292 
MET CG    SD     sing N N 293 
MET CG    HG2    sing N N 294 
MET CG    HG3    sing N N 295 
MET SD    CE     sing N N 296 
MET CE    HE1    sing N N 297 
MET CE    HE2    sing N N 298 
MET CE    HE3    sing N N 299 
MET OXT   HXT    sing N N 300 
PHE N     CA     sing N N 301 
PHE N     H      sing N N 302 
PHE N     H2     sing N N 303 
PHE CA    C      sing N N 304 
PHE CA    CB     sing N N 305 
PHE CA    HA     sing N N 306 
PHE C     O      doub N N 307 
PHE C     OXT    sing N N 308 
PHE CB    CG     sing N N 309 
PHE CB    HB2    sing N N 310 
PHE CB    HB3    sing N N 311 
PHE CG    CD1    doub Y N 312 
PHE CG    CD2    sing Y N 313 
PHE CD1   CE1    sing Y N 314 
PHE CD1   HD1    sing N N 315 
PHE CD2   CE2    doub Y N 316 
PHE CD2   HD2    sing N N 317 
PHE CE1   CZ     doub Y N 318 
PHE CE1   HE1    sing N N 319 
PHE CE2   CZ     sing Y N 320 
PHE CE2   HE2    sing N N 321 
PHE CZ    HZ     sing N N 322 
PHE OXT   HXT    sing N N 323 
PRO N     CA     sing N N 324 
PRO N     CD     sing N N 325 
PRO N     H      sing N N 326 
PRO CA    C      sing N N 327 
PRO CA    CB     sing N N 328 
PRO CA    HA     sing N N 329 
PRO C     O      doub N N 330 
PRO C     OXT    sing N N 331 
PRO CB    CG     sing N N 332 
PRO CB    HB2    sing N N 333 
PRO CB    HB3    sing N N 334 
PRO CG    CD     sing N N 335 
PRO CG    HG2    sing N N 336 
PRO CG    HG3    sing N N 337 
PRO CD    HD2    sing N N 338 
PRO CD    HD3    sing N N 339 
PRO OXT   HXT    sing N N 340 
SER N     CA     sing N N 341 
SER N     H      sing N N 342 
SER N     H2     sing N N 343 
SER CA    C      sing N N 344 
SER CA    CB     sing N N 345 
SER CA    HA     sing N N 346 
SER C     O      doub N N 347 
SER C     OXT    sing N N 348 
SER CB    OG     sing N N 349 
SER CB    HB2    sing N N 350 
SER CB    HB3    sing N N 351 
SER OG    HG     sing N N 352 
SER OXT   HXT    sing N N 353 
THR N     CA     sing N N 354 
THR N     H      sing N N 355 
THR N     H2     sing N N 356 
THR CA    C      sing N N 357 
THR CA    CB     sing N N 358 
THR CA    HA     sing N N 359 
THR C     O      doub N N 360 
THR C     OXT    sing N N 361 
THR CB    OG1    sing N N 362 
THR CB    CG2    sing N N 363 
THR CB    HB     sing N N 364 
THR OG1   HG1    sing N N 365 
THR CG2   HG21   sing N N 366 
THR CG2   HG22   sing N N 367 
THR CG2   HG23   sing N N 368 
THR OXT   HXT    sing N N 369 
TRP N     CA     sing N N 370 
TRP N     H      sing N N 371 
TRP N     H2     sing N N 372 
TRP CA    C      sing N N 373 
TRP CA    CB     sing N N 374 
TRP CA    HA     sing N N 375 
TRP C     O      doub N N 376 
TRP C     OXT    sing N N 377 
TRP CB    CG     sing N N 378 
TRP CB    HB2    sing N N 379 
TRP CB    HB3    sing N N 380 
TRP CG    CD1    doub Y N 381 
TRP CG    CD2    sing Y N 382 
TRP CD1   NE1    sing Y N 383 
TRP CD1   HD1    sing N N 384 
TRP CD2   CE2    doub Y N 385 
TRP CD2   CE3    sing Y N 386 
TRP NE1   CE2    sing Y N 387 
TRP NE1   HE1    sing N N 388 
TRP CE2   CZ2    sing Y N 389 
TRP CE3   CZ3    doub Y N 390 
TRP CE3   HE3    sing N N 391 
TRP CZ2   CH2    doub Y N 392 
TRP CZ2   HZ2    sing N N 393 
TRP CZ3   CH2    sing Y N 394 
TRP CZ3   HZ3    sing N N 395 
TRP CH2   HH2    sing N N 396 
TRP OXT   HXT    sing N N 397 
TYR N     CA     sing N N 398 
TYR N     H      sing N N 399 
TYR N     H2     sing N N 400 
TYR CA    C      sing N N 401 
TYR CA    CB     sing N N 402 
TYR CA    HA     sing N N 403 
TYR C     O      doub N N 404 
TYR C     OXT    sing N N 405 
TYR CB    CG     sing N N 406 
TYR CB    HB2    sing N N 407 
TYR CB    HB3    sing N N 408 
TYR CG    CD1    doub Y N 409 
TYR CG    CD2    sing Y N 410 
TYR CD1   CE1    sing Y N 411 
TYR CD1   HD1    sing N N 412 
TYR CD2   CE2    doub Y N 413 
TYR CD2   HD2    sing N N 414 
TYR CE1   CZ     doub Y N 415 
TYR CE1   HE1    sing N N 416 
TYR CE2   CZ     sing Y N 417 
TYR CE2   HE2    sing N N 418 
TYR CZ    OH     sing N N 419 
TYR OH    HH     sing N N 420 
TYR OXT   HXT    sing N N 421 
VAL N     CA     sing N N 422 
VAL N     H      sing N N 423 
VAL N     H2     sing N N 424 
VAL CA    C      sing N N 425 
VAL CA    CB     sing N N 426 
VAL CA    HA     sing N N 427 
VAL C     O      doub N N 428 
VAL C     OXT    sing N N 429 
VAL CB    CG1    sing N N 430 
VAL CB    CG2    sing N N 431 
VAL CB    HB     sing N N 432 
VAL CG1   HG11   sing N N 433 
VAL CG1   HG12   sing N N 434 
VAL CG1   HG13   sing N N 435 
VAL CG2   HG21   sing N N 436 
VAL CG2   HG22   sing N N 437 
VAL CG2   HG23   sing N N 438 
VAL OXT   HXT    sing N N 439 
WTO O29   S18    doub N N 440 
WTO O19   S18    doub N N 441 
WTO O25   C22    doub N N 442 
WTO S18   C17    sing N N 443 
WTO S18   N20    sing N N 444 
WTO C16   C15    doub Y N 445 
WTO C16   C17    sing Y N 446 
WTO C22   O23    sing N N 447 
WTO C22   C21    sing N N 448 
WTO C15   C12    sing Y N 449 
WTO C17   C14    doub Y N 450 
WTO N20   C21    sing N N 451 
WTO N20   C28    sing N N 452 
WTO C26   C21    sing N N 453 
WTO C26   C27    sing N N 454 
WTO O23   C24    sing N N 455 
WTO C28   C27    sing N N 456 
WTO O30   C10    doub N N 457 
WTO C12   N11    sing N N 458 
WTO C12   C13    doub Y N 459 
WTO C08   C09    sing N N 460 
WTO C14   C13    sing Y N 461 
WTO C10   N11    sing N N 462 
WTO C10   C09    sing N N 463 
WTO C08   H1     sing N N 464 
WTO C08   H2     sing N N 465 
WTO C08   H3     sing N N 466 
WTO C09   H4     sing N N 467 
WTO C09   H5     sing N N 468 
WTO C13   H6     sing N N 469 
WTO C14   H7     sing N N 470 
WTO C15   H8     sing N N 471 
WTO C16   H9     sing N N 472 
WTO C21   H10    sing N N 473 
WTO C24   H11    sing N N 474 
WTO C24   H12    sing N N 475 
WTO C24   H13    sing N N 476 
WTO C26   H14    sing N N 477 
WTO C26   H15    sing N N 478 
WTO C27   H16    sing N N 479 
WTO C27   H17    sing N N 480 
WTO C28   H18    sing N N 481 
WTO C28   H19    sing N N 482 
WTO N11   H20    sing N N 483 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           C29637/A20781 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7OPP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8P3H 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.016619 
_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]   0.012871 
_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]   0.008610 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
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     . SER A 1 4   ? 23.137  -11.416 9.044   1.00 83.56  ? -35 SER A N     1 
ATOM   2    C  CA    . SER A 1 4   ? 24.219  -10.441 9.213   1.00 89.79  ? -35 SER A CA    1 
ATOM   3    C  C     . SER A 1 4   ? 23.817  -9.151  9.966   1.00 90.79  ? -35 SER A C     1 
ATOM   4    O  O     . SER A 1 4   ? 22.636  -8.882  10.202  1.00 91.57  ? -35 SER A O     1 
ATOM   5    C  CB    . SER A 1 4   ? 24.790  -10.062 7.849   1.00 87.06  ? -35 SER A CB    1 
ATOM   6    O  OG    . SER A 1 4   ? 25.417  -8.791  7.914   1.00 87.25  ? -35 SER A OG    1 
ATOM   7    N  N     . PHE A 1 5   ? 24.815  -8.369  10.364  1.00 92.85  ? -34 PHE A N     1 
ATOM   8    C  CA    . PHE A 1 5   ? 24.581  -6.994  10.778  1.00 90.67  ? -34 PHE A CA    1 
ATOM   9    C  C     . PHE A 1 5   ? 24.653  -6.097  9.546   1.00 84.03  ? -34 PHE A C     1 
ATOM   10   O  O     . PHE A 1 5   ? 25.045  -6.529  8.462   1.00 84.62  ? -34 PHE A O     1 
ATOM   11   C  CB    . PHE A 1 5   ? 25.589  -6.559  11.843  1.00 89.62  ? -34 PHE A CB    1 
ATOM   12   C  CG    . PHE A 1 5   ? 24.967  -5.813  12.981  1.00 89.02  ? -34 PHE A CG    1 
ATOM   13   C  CD1   . PHE A 1 5   ? 24.599  -4.487  12.833  1.00 86.71  ? -34 PHE A CD1   1 
ATOM   14   C  CD2   . PHE A 1 5   ? 24.726  -6.444  14.195  1.00 93.89  ? -34 PHE A CD2   1 
ATOM   15   C  CE1   . PHE A 1 5   ? 24.011  -3.798  13.876  1.00 82.68  ? -34 PHE A CE1   1 
ATOM   16   C  CE2   . PHE A 1 5   ? 24.138  -5.762  15.244  1.00 92.68  ? -34 PHE A CE2   1 
ATOM   17   C  CZ    . PHE A 1 5   ? 23.782  -4.433  15.083  1.00 84.08  ? -34 PHE A CZ    1 
ATOM   18   N  N     . LEU A 1 6   ? 24.252  -4.841  9.700   1.00 79.72  ? -33 LEU A N     1 
ATOM   19   C  CA    . LEU A 1 6   ? 24.150  -3.988  8.524   1.00 74.38  ? -33 LEU A CA    1 
ATOM   20   C  C     . LEU A 1 6   ? 25.529  -3.555  8.053   1.00 76.27  ? -33 LEU A C     1 
ATOM   21   O  O     . LEU A 1 6   ? 26.374  -3.142  8.857   1.00 82.95  ? -33 LEU A O     1 
ATOM   22   C  CB    . LEU A 1 6   ? 23.286  -2.766  8.812   1.00 74.91  ? -33 LEU A CB    1 
ATOM   23   C  CG    . LEU A 1 6   ? 21.798  -2.995  9.041   1.00 70.65  ? -33 LEU A CG    1 
ATOM   24   C  CD1   . LEU A 1 6   ? 21.052  -1.770  8.545   1.00 64.50  ? -33 LEU A CD1   1 
ATOM   25   C  CD2   . LEU A 1 6   ? 21.316  -4.264  8.341   1.00 64.49  ? -33 LEU A CD2   1 
ATOM   26   N  N     . THR A 1 7   ? 25.769  -3.675  6.753   1.00 73.01  ? -32 THR A N     1 
ATOM   27   C  CA    . THR A 1 7   ? 26.929  -3.032  6.171   1.00 68.67  ? -32 THR A CA    1 
ATOM   28   C  C     . THR A 1 7   ? 26.816  -1.539  6.443   1.00 71.97  ? -32 THR A C     1 
ATOM   29   O  O     . THR A 1 7   ? 25.718  -1.009  6.640   1.00 70.71  ? -32 THR A O     1 
ATOM   30   C  CB    . THR A 1 7   ? 26.970  -3.329  4.668   1.00 74.32  ? -32 THR A CB    1 
ATOM   31   O  OG1   . THR A 1 7   ? 27.155  -4.739  4.460   1.00 86.30  ? -32 THR A OG1   1 
ATOM   32   C  CG2   . THR A 1 7   ? 28.094  -2.580  3.934   1.00 71.24  ? -32 THR A CG2   1 
ATOM   33   N  N     . GLU A 1 8   ? 27.950  -0.851  6.501   1.00 74.32  ? -31 GLU A N     1 
ATOM   34   C  CA    . GLU A 1 8   ? 27.867  0.587   6.664   1.00 71.65  ? -31 GLU A CA    1 
ATOM   35   C  C     . GLU A 1 8   ? 27.631  1.279   5.339   1.00 69.00  ? -31 GLU A C     1 
ATOM   36   O  O     . GLU A 1 8   ? 27.330  2.473   5.333   1.00 75.09  ? -31 GLU A O     1 
ATOM   37   C  CB    . GLU A 1 8   ? 29.123  1.132   7.356   1.00 83.98  ? -31 GLU A CB    1 
ATOM   38   C  CG    . GLU A 1 8   ? 29.302  0.677   8.840   1.00 84.25  ? -31 GLU A CG    1 
ATOM   39   C  CD    . GLU A 1 8   ? 28.219  1.203   9.804   1.00 87.50  ? -31 GLU A CD    1 
ATOM   40   O  OE1   . GLU A 1 8   ? 28.179  2.439   10.039  1.00 89.29  ? -31 GLU A OE1   1 
ATOM   41   O  OE2   . GLU A 1 8   ? 27.442  0.375   10.363  1.00 79.82  ? -31 GLU A OE2   1 
ATOM   42   N  N     . GLU A 1 9   ? 27.737  0.548   4.227   1.00 78.92  ? -30 GLU A N     1 
ATOM   43   C  CA    . GLU A 1 9   ? 27.229  0.990   2.935   1.00 74.04  ? -30 GLU A CA    1 
ATOM   44   C  C     . GLU A 1 9   ? 25.790  0.554   2.718   1.00 69.85  ? -30 GLU A C     1 
ATOM   45   O  O     . GLU A 1 9   ? 25.063  1.195   1.950   1.00 64.53  ? -30 GLU A O     1 
ATOM   46   C  CB    . GLU A 1 9   ? 28.118  0.454   1.812   1.00 68.86  ? -30 GLU A CB    1 
ATOM   47   C  CG    . GLU A 1 9   ? 28.024  1.221   0.486   1.00 81.78  ? -30 GLU A CG    1 
ATOM   48   C  CD    . GLU A 1 9   ? 28.465  2.684   0.584   1.00 87.51  ? -30 GLU A CD    1 
ATOM   49   O  OE1   . GLU A 1 9   ? 28.079  3.475   -0.304  1.00 87.34  ? -30 GLU A OE1   1 
ATOM   50   O  OE2   . GLU A 1 9   ? 29.188  3.051   1.541   1.00 88.95  ? -30 GLU A OE2   1 
ATOM   51   N  N     . GLU A 1 10  ? 25.365  -0.523  3.390   1.00 67.60  ? -29 GLU A N     1 
ATOM   52   C  CA    . GLU A 1 10  ? 23.944  -0.832  3.464   1.00 62.86  ? -29 GLU A CA    1 
ATOM   53   C  C     . GLU A 1 10  ? 23.180  0.217   4.253   1.00 64.62  ? -29 GLU A C     1 
ATOM   54   O  O     . GLU A 1 10  ? 21.963  0.329   4.083   1.00 62.85  ? -29 GLU A O     1 
ATOM   55   C  CB    . GLU A 1 10  ? 23.708  -2.211  4.092   1.00 63.82  ? -29 GLU A CB    1 
ATOM   56   C  CG    . GLU A 1 10  ? 23.784  -3.378  3.108   1.00 70.32  ? -29 GLU A CG    1 
ATOM   57   C  CD    . GLU A 1 10  ? 23.751  -4.741  3.778   1.00 74.49  ? -29 GLU A CD    1 
ATOM   58   O  OE1   . GLU A 1 10  ? 23.950  -4.802  5.013   1.00 72.19  ? -29 GLU A OE1   1 
ATOM   59   O  OE2   . GLU A 1 10  ? 23.556  -5.759  3.062   1.00 81.00  ? -29 GLU A OE2   1 
ATOM   60   N  N     . GLN A 1 11  ? 23.859  0.989   5.114   1.00 73.20  ? -28 GLN A N     1 
ATOM   61   C  CA    . GLN A 1 11  ? 23.197  2.055   5.862   1.00 65.45  ? -28 GLN A CA    1 
ATOM   62   C  C     . GLN A 1 11  ? 23.177  3.383   5.113   1.00 63.74  ? -28 GLN A C     1 
ATOM   63   O  O     . GLN A 1 11  ? 22.254  4.172   5.327   1.00 65.22  ? -28 GLN A O     1 
ATOM   64   C  CB    . GLN A 1 11  ? 23.845  2.225   7.237   1.00 65.21  ? -28 GLN A CB    1 
ATOM   65   C  CG    . GLN A 1 11  ? 23.693  0.982   8.127   1.00 68.80  ? -28 GLN A CG    1 
ATOM   66   C  CD    . GLN A 1 11  ? 23.879  1.273   9.617   1.00 68.36  ? -28 GLN A CD    1 
ATOM   67   O  OE1   . GLN A 1 11  ? 23.168  2.103   10.198  1.00 56.50  ? -28 GLN A OE1   1 
ATOM   68   N  NE2   . GLN A 1 11  ? 24.838  0.584   10.240  1.00 68.36  ? -28 GLN A NE2   1 
ATOM   69   N  N     . GLU A 1 12  ? 24.146  3.647   4.222   1.00 65.20  ? -27 GLU A N     1 
ATOM   70   C  CA    . GLU A 1 12  ? 23.982  4.749   3.271   1.00 65.81  ? -27 GLU A CA    1 
ATOM   71   C  C     . GLU A 1 12  ? 22.678  4.594   2.498   1.00 64.50  ? -27 GLU A C     1 
ATOM   72   O  O     . GLU A 1 12  ? 21.840  5.503   2.477   1.00 60.96  ? -27 GLU A O     1 
ATOM   73   C  CB    . GLU A 1 12  ? 25.158  4.810   2.286   1.00 74.73  ? -27 GLU A CB    1 
ATOM   74   C  CG    . GLU A 1 12  ? 25.049  5.933   1.203   1.00 80.81  ? -27 GLU A CG    1 
ATOM   75   C  CD    . GLU A 1 12  ? 24.849  5.420   -0.242  1.00 86.62  ? -27 GLU A CD    1 
ATOM   76   O  OE1   . GLU A 1 12  ? 25.566  4.484   -0.672  1.00 87.22  ? -27 GLU A OE1   1 
ATOM   77   O  OE2   . GLU A 1 12  ? 23.988  5.990   -0.960  1.00 81.21  ? -27 GLU A OE2   1 
ATOM   78   N  N     . ALA A 1 13  ? 22.502  3.437   1.854   1.00 63.28  ? -26 ALA A N     1 
ATOM   79   C  CA    . ALA A 1 13  ? 21.281  3.132   1.116   1.00 60.86  ? -26 ALA A CA    1 
ATOM   80   C  C     . ALA A 1 13  ? 20.032  3.422   1.936   1.00 62.11  ? -26 ALA A C     1 
ATOM   81   O  O     . ALA A 1 13  ? 19.201  4.259   1.557   1.00 60.22  ? -26 ALA A O     1 
ATOM   82   C  CB    . ALA A 1 13  ? 21.291  1.663   0.702   1.00 69.71  ? -26 ALA A CB    1 
ATOM   83   N  N     . ILE A 1 14  ? 19.896  2.732   3.078   1.00 63.88  ? -25 ILE A N     1 
ATOM   84   C  CA    . ILE A 1 14  ? 18.669  2.772   3.869   1.00 55.68  ? -25 ILE A CA    1 
ATOM   85   C  C     . ILE A 1 14  ? 18.322  4.195   4.255   1.00 54.61  ? -25 ILE A C     1 
ATOM   86   O  O     . ILE A 1 14  ? 17.141  4.540   4.395   1.00 55.72  ? -25 ILE A O     1 
ATOM   87   C  CB    . ILE A 1 14  ? 18.799  1.866   5.109   1.00 56.21  ? -25 ILE A CB    1 
ATOM   88   C  CG1   . ILE A 1 14  ? 18.894  0.395   4.705   1.00 52.96  ? -25 ILE A CG1   1 
ATOM   89   C  CG2   . ILE A 1 14  ? 17.594  2.021   6.011   1.00 60.24  ? -25 ILE A CG2   1 
ATOM   90   C  CD1   . ILE A 1 14  ? 18.697  -0.552  5.859   1.00 58.76  ? -25 ILE A CD1   1 
ATOM   91   N  N     . MET A 1 15  ? 19.322  5.062   4.380   1.00 55.46  ? -24 MET A N     1 
ATOM   92   C  CA    . MET A 1 15  ? 19.045  6.408   4.846   1.00 56.35  ? -24 MET A CA    1 
ATOM   93   C  C     . MET A 1 15  ? 18.906  7.433   3.735   1.00 56.86  ? -24 MET A C     1 
ATOM   94   O  O     . MET A 1 15  ? 18.349  8.506   3.983   1.00 55.28  ? -24 MET A O     1 
ATOM   95   C  CB    . MET A 1 15  ? 20.112  6.855   5.846   1.00 62.82  ? -24 MET A CB    1 
ATOM   96   C  CG    . MET A 1 15  ? 19.603  6.712   7.274   1.00 61.39  ? -24 MET A CG    1 
ATOM   97   S  SD    . MET A 1 15  ? 20.907  6.928   8.458   1.00 70.26  ? -24 MET A SD    1 
ATOM   98   C  CE    . MET A 1 15  ? 22.022  5.593   8.010   1.00 62.90  ? -24 MET A CE    1 
ATOM   99   N  N     . LYS A 1 16  ? 19.360  7.145   2.515   1.00 61.44  ? -23 LYS A N     1 
ATOM   100  C  CA    . LYS A 1 16  ? 18.889  7.999   1.438   1.00 56.15  ? -23 LYS A CA    1 
ATOM   101  C  C     . LYS A 1 16  ? 17.402  7.766   1.197   1.00 51.16  ? -23 LYS A C     1 
ATOM   102  O  O     . LYS A 1 16  ? 16.679  8.704   0.845   1.00 50.88  ? -23 LYS A O     1 
ATOM   103  C  CB    . LYS A 1 16  ? 19.727  7.807   0.171   1.00 60.26  ? -23 LYS A CB    1 
ATOM   104  C  CG    . LYS A 1 16  ? 20.082  9.165   -0.463  1.00 70.44  ? -23 LYS A CG    1 
ATOM   105  C  CD    . LYS A 1 16  ? 21.545  9.271   -0.910  1.00 80.27  ? -23 LYS A CD    1 
ATOM   106  C  CE    . LYS A 1 16  ? 21.951  10.737  -1.139  1.00 80.27  ? -23 LYS A CE    1 
ATOM   107  N  NZ    . LYS A 1 16  ? 23.430  10.939  -1.182  1.00 83.07  ? -23 LYS A NZ    1 
ATOM   108  N  N     . VAL A 1 17  ? 16.913  6.549   1.450   1.00 50.90  ? -22 VAL A N     1 
ATOM   109  C  CA    . VAL A 1 17  ? 15.479  6.300   1.313   1.00 49.83  ? -22 VAL A CA    1 
ATOM   110  C  C     . VAL A 1 17  ? 14.696  7.172   2.290   1.00 50.35  ? -22 VAL A C     1 
ATOM   111  O  O     . VAL A 1 17  ? 13.776  7.897   1.901   1.00 50.12  ? -22 VAL A O     1 
ATOM   112  C  CB    . VAL A 1 17  ? 15.156  4.804   1.506   1.00 49.11  ? -22 VAL A CB    1 
ATOM   113  C  CG1   . VAL A 1 17  ? 13.728  4.526   1.073   1.00 45.66  ? -22 VAL A CG1   1 
ATOM   114  C  CG2   . VAL A 1 17  ? 16.128  3.912   0.737   1.00 43.74  ? -22 VAL A CG2   1 
ATOM   115  N  N     . LEU A 1 18  ? 15.063  7.136   3.575   1.00 54.46  ? -21 LEU A N     1 
ATOM   116  C  CA    . LEU A 1 18  ? 14.370  7.985   4.546   1.00 55.73  ? -21 LEU A CA    1 
ATOM   117  C  C     . LEU A 1 18  ? 14.552  9.466   4.231   1.00 52.20  ? -21 LEU A C     1 
ATOM   118  O  O     . LEU A 1 18  ? 13.615  10.266  4.405   1.00 49.41  ? -21 LEU A O     1 
ATOM   119  C  CB    . LEU A 1 18  ? 14.838  7.665   5.971   1.00 60.16  ? -21 LEU A CB    1 
ATOM   120  C  CG    . LEU A 1 18  ? 15.033  6.194   6.352   1.00 60.21  ? -21 LEU A CG    1 
ATOM   121  C  CD1   . LEU A 1 18  ? 15.862  6.020   7.643   1.00 51.69  ? -21 LEU A CD1   1 
ATOM   122  C  CD2   . LEU A 1 18  ? 13.685  5.536   6.480   1.00 56.64  ? -21 LEU A CD2   1 
ATOM   123  N  N     . GLN A 1 19  ? 15.752  9.858   3.785   1.00 50.67  ? -20 GLN A N     1 
ATOM   124  C  CA    . GLN A 1 19  ? 15.939  11.193  3.239   1.00 45.14  ? -20 GLN A CA    1 
ATOM   125  C  C     . GLN A 1 19  ? 14.831  11.493  2.243   1.00 50.88  ? -20 GLN A C     1 
ATOM   126  O  O     . GLN A 1 19  ? 14.077  12.459  2.405   1.00 51.54  ? -20 GLN A O     1 
ATOM   127  C  CB    . GLN A 1 19  ? 17.316  11.288  2.590   1.00 50.52  ? -20 GLN A CB    1 
ATOM   128  C  CG    . GLN A 1 19  ? 17.956  12.664  2.514   1.00 57.63  ? -20 GLN A CG    1 
ATOM   129  C  CD    . GLN A 1 19  ? 19.492  12.592  2.369   1.00 65.84  ? -20 GLN A CD    1 
ATOM   130  O  OE1   . GLN A 1 19  ? 20.111  11.537  2.579   1.00 61.22  ? -20 GLN A OE1   1 
ATOM   131  N  NE2   . GLN A 1 19  ? 20.103  13.722  1.998   1.00 64.42  ? -20 GLN A NE2   1 
ATOM   132  N  N     A ARG A 1 20  ? 14.695  10.637  1.220   0.71 51.09  ? -19 ARG A N     1 
ATOM   133  N  N     B ARG A 1 20  ? 14.705  10.648  1.212   0.29 50.86  ? -19 ARG A N     1 
ATOM   134  C  CA    A ARG A 1 20  ? 13.638  10.797  0.228   0.71 50.03  ? -19 ARG A CA    1 
ATOM   135  C  CA    B ARG A 1 20  ? 13.634  10.803  0.232   0.29 50.34  ? -19 ARG A CA    1 
ATOM   136  C  C     A ARG A 1 20  ? 12.255  10.696  0.860   0.71 51.40  ? -19 ARG A C     1 
ATOM   137  C  C     B ARG A 1 20  ? 12.259  10.725  0.882   0.29 51.64  ? -19 ARG A C     1 
ATOM   138  O  O     A ARG A 1 20  ? 11.287  11.257  0.329   0.71 52.42  ? -19 ARG A O     1 
ATOM   139  O  O     B ARG A 1 20  ? 11.305  11.348  0.396   0.29 52.76  ? -19 ARG A O     1 
ATOM   140  C  CB    A ARG A 1 20  ? 13.797  9.744   -0.876  0.71 49.25  ? -19 ARG A CB    1 
ATOM   141  C  CB    B ARG A 1 20  ? 13.760  9.730   -0.855  0.29 49.58  ? -19 ARG A CB    1 
ATOM   142  C  CG    A ARG A 1 20  ? 13.538  10.271  -2.284  0.71 51.11  ? -19 ARG A CG    1 
ATOM   143  C  CG    B ARG A 1 20  ? 14.957  9.884   -1.778  0.29 49.92  ? -19 ARG A CG    1 
ATOM   144  C  CD    A ARG A 1 20  ? 13.608  9.156   -3.316  0.71 50.41  ? -19 ARG A CD    1 
ATOM   145  C  CD    B ARG A 1 20  ? 14.746  9.150   -3.100  0.29 48.60  ? -19 ARG A CD    1 
ATOM   146  N  NE    A ARG A 1 20  ? 14.529  8.088   -2.928  0.71 46.05  ? -19 ARG A NE    1 
ATOM   147  N  NE    B ARG A 1 20  ? 13.378  9.276   -3.603  0.29 50.29  ? -19 ARG A NE    1 
ATOM   148  C  CZ    A ARG A 1 20  ? 14.194  6.801   -2.866  0.71 46.71  ? -19 ARG A CZ    1 
ATOM   149  C  CZ    B ARG A 1 20  ? 12.880  10.366  -4.180  0.29 49.71  ? -19 ARG A CZ    1 
ATOM   150  N  NH1   A ARG A 1 20  ? 12.956  6.415   -3.158  0.71 43.10  ? -19 ARG A NH1   1 
ATOM   151  N  NH1   B ARG A 1 20  ? 13.628  11.449  -4.342  0.29 49.37  ? -19 ARG A NH1   1 
ATOM   152  N  NH2   A ARG A 1 20  ? 15.099  5.895   -2.512  0.71 45.07  ? -19 ARG A NH2   1 
ATOM   153  N  NH2   B ARG A 1 20  ? 11.623  10.372  -4.597  0.29 49.97  ? -19 ARG A NH2   1 
ATOM   154  N  N     . ASP A 1 21  ? 12.139  9.975   1.978   1.00 48.72  ? -18 ASP A N     1 
ATOM   155  C  CA    . ASP A 1 21  ? 10.837  9.750   2.593   1.00 48.08  ? -18 ASP A CA    1 
ATOM   156  C  C     . ASP A 1 21  ? 10.369  10.985  3.342   1.00 53.40  ? -18 ASP A C     1 
ATOM   157  O  O     . ASP A 1 21  ? 9.217   11.410  3.193   1.00 54.03  ? -18 ASP A O     1 
ATOM   158  C  CB    . ASP A 1 21  ? 10.911  8.538   3.525   1.00 53.48  ? -18 ASP A CB    1 
ATOM   159  C  CG    . ASP A 1 21  ? 9.620   8.309   4.306   1.00 57.44  ? -18 ASP A CG    1 
ATOM   160  O  OD1   . ASP A 1 21  ? 8.527   8.364   3.680   1.00 57.93  ? -18 ASP A OD1   1 
ATOM   161  O  OD2   . ASP A 1 21  ? 9.702   8.054   5.537   1.00 52.32  ? -18 ASP A OD2   1 
ATOM   162  N  N     . ALA A 1 22  ? 11.249  11.562  4.169   1.00 55.86  ? -17 ALA A N     1 
ATOM   163  C  CA    . ALA A 1 22  ? 10.949  12.836  4.817   1.00 58.45  ? -17 ALA A CA    1 
ATOM   164  C  C     . ALA A 1 22  ? 10.726  13.925  3.778   1.00 56.91  ? -17 ALA A C     1 
ATOM   165  O  O     . ALA A 1 22  ? 9.746   14.677  3.859   1.00 58.03  ? -17 ALA A O     1 
ATOM   166  C  CB    . ALA A 1 22  ? 12.079  13.227  5.777   1.00 57.75  ? -17 ALA A CB    1 
ATOM   167  N  N     . ALA A 1 23  ? 11.626  14.013  2.787   1.00 53.13  ? -16 ALA A N     1 
ATOM   168  C  CA    . ALA A 1 23  ? 11.447  14.945  1.675   1.00 50.87  ? -16 ALA A CA    1 
ATOM   169  C  C     . ALA A 1 23  ? 10.038  14.861  1.104   1.00 51.32  ? -16 ALA A C     1 
ATOM   170  O  O     . ALA A 1 23  ? 9.366   15.881  0.940   1.00 57.12  ? -16 ALA A O     1 
ATOM   171  C  CB    . ALA A 1 23  ? 12.478  14.673  0.586   1.00 51.31  ? -16 ALA A CB    1 
ATOM   172  N  N     . LEU A 1 24  ? 9.552   13.644  0.847   1.00 52.75  ? -15 LEU A N     1 
ATOM   173  C  CA    . LEU A 1 24  ? 8.185   13.480  0.350   1.00 57.16  ? -15 LEU A CA    1 
ATOM   174  C  C     . LEU A 1 24  ? 7.154   13.996  1.350   1.00 59.08  ? -15 LEU A C     1 
ATOM   175  O  O     . LEU A 1 24  ? 6.199   14.686  0.974   1.00 59.77  ? -15 LEU A O     1 
ATOM   176  C  CB    . LEU A 1 24  ? 7.916   12.009  0.020   1.00 56.45  ? -15 LEU A CB    1 
ATOM   177  C  CG    . LEU A 1 24  ? 6.576   11.564  -0.611  1.00 56.19  ? -15 LEU A CG    1 
ATOM   178  C  CD1   . LEU A 1 24  ? 6.701   10.109  -0.984  1.00 59.86  ? -15 LEU A CD1   1 
ATOM   179  C  CD2   . LEU A 1 24  ? 5.303   11.733  0.234   1.00 59.47  ? -15 LEU A CD2   1 
ATOM   180  N  N     . LYS A 1 25  ? 7.302   13.640  2.629   1.00 63.88  ? -14 LYS A N     1 
ATOM   181  C  CA    . LYS A 1 25  ? 6.271   13.983  3.607   1.00 64.96  ? -14 LYS A CA    1 
ATOM   182  C  C     . LYS A 1 25  ? 6.160   15.490  3.805   1.00 61.95  ? -14 LYS A C     1 
ATOM   183  O  O     . LYS A 1 25  ? 5.053   16.027  3.945   1.00 61.47  ? -14 LYS A O     1 
ATOM   184  C  CB    . LYS A 1 25  ? 6.554   13.284  4.932   1.00 61.23  ? -14 LYS A CB    1 
ATOM   185  C  CG    . LYS A 1 25  ? 6.372   11.798  4.837   1.00 59.12  ? -14 LYS A CG    1 
ATOM   186  C  CD    . LYS A 1 25  ? 4.957   11.369  5.134   1.00 57.93  ? -14 LYS A CD    1 
ATOM   187  C  CE    . LYS A 1 25  ? 4.715   10.035  4.467   1.00 62.57  ? -14 LYS A CE    1 
ATOM   188  N  NZ    . LYS A 1 25  ? 5.842   9.062   4.662   1.00 53.95  ? -14 LYS A NZ    1 
ATOM   189  N  N     . ARG A 1 26  ? 7.296   16.187  3.818   1.00 61.05  ? -13 ARG A N     1 
ATOM   190  C  CA    . ARG A 1 26  ? 7.298   17.643  3.878   1.00 68.82  ? -13 ARG A CA    1 
ATOM   191  C  C     . ARG A 1 26  ? 6.686   18.287  2.639   1.00 71.52  ? -13 ARG A C     1 
ATOM   192  O  O     . ARG A 1 26  ? 6.431   19.496  2.653   1.00 77.98  ? -13 ARG A O     1 
ATOM   193  C  CB    . ARG A 1 26  ? 8.731   18.144  4.074   1.00 65.57  ? -13 ARG A CB    1 
ATOM   194  C  CG    . ARG A 1 26  ? 9.339   17.699  5.381   1.00 66.49  ? -13 ARG A CG    1 
ATOM   195  C  CD    . ARG A 1 26  ? 10.656  18.382  5.653   1.00 67.92  ? -13 ARG A CD    1 
ATOM   196  N  NE    . ARG A 1 26  ? 11.801  17.488  5.483   1.00 61.39  ? -13 ARG A NE    1 
ATOM   197  C  CZ    . ARG A 1 26  ? 12.522  17.413  4.373   1.00 59.58  ? -13 ARG A CZ    1 
ATOM   198  N  NH1   . ARG A 1 26  ? 12.210  18.168  3.329   1.00 67.32  ? -13 ARG A NH1   1 
ATOM   199  N  NH2   . ARG A 1 26  ? 13.551  16.588  4.306   1.00 60.95  ? -13 ARG A NH2   1 
ATOM   200  N  N     . ALA A 1 27  ? 6.450   17.523  1.572   1.00 64.81  ? -12 ALA A N     1 
ATOM   201  C  CA    . ALA A 1 27  ? 5.817   18.050  0.374   1.00 71.49  ? -12 ALA A CA    1 
ATOM   202  C  C     . ALA A 1 27  ? 4.328   17.733  0.304   1.00 78.94  ? -12 ALA A C     1 
ATOM   203  O  O     . ALA A 1 27  ? 3.758   17.743  -0.790  1.00 91.19  ? -12 ALA A O     1 
ATOM   204  C  CB    . ALA A 1 27  ? 6.524   17.532  -0.881  1.00 61.28  ? -12 ALA A CB    1 
ATOM   205  N  N     . GLU A 1 28  ? 3.679   17.455  1.434   1.00 82.08  ? -11 GLU A N     1 
ATOM   206  C  CA    . GLU A 1 28  ? 2.223   17.369  1.427   1.00 91.86  ? -11 GLU A CA    1 
ATOM   207  C  C     . GLU A 1 28  ? 1.576   18.649  1.944   1.00 99.21  ? -11 GLU A C     1 
ATOM   208  O  O     . GLU A 1 28  ? 0.628   19.144  1.324   1.00 100.63 ? -11 GLU A O     1 
ATOM   209  C  CB    . GLU A 1 28  ? 1.727   16.145  2.218   1.00 90.92  ? -11 GLU A CB    1 
ATOM   210  C  CG    . GLU A 1 28  ? 0.212   15.923  2.083   1.00 94.08  ? -11 GLU A CG    1 
ATOM   211  C  CD    . GLU A 1 28  ? -0.225  15.539  0.667   1.00 94.83  ? -11 GLU A CD    1 
ATOM   212  O  OE1   . GLU A 1 28  ? 0.574   14.886  -0.043  1.00 93.83  ? -11 GLU A OE1   1 
ATOM   213  O  OE2   . GLU A 1 28  ? -1.350  15.922  0.255   1.00 98.16  ? -11 GLU A OE2   1 
ATOM   214  N  N     . GLU A 1 29  ? 2.083   19.220  3.042   1.00 98.24  ? -10 GLU A N     1 
ATOM   215  C  CA    . GLU A 1 29  ? 1.665   20.570  3.421   1.00 96.61  ? -10 GLU A CA    1 
ATOM   216  C  C     . GLU A 1 29  ? 2.289   21.612  2.495   1.00 104.28 ? -10 GLU A C     1 
ATOM   217  O  O     . GLU A 1 29  ? 1.578   22.397  1.850   1.00 111.14 ? -10 GLU A O     1 
ATOM   218  C  CB    . GLU A 1 29  ? 2.031   20.865  4.876   1.00 97.41  ? -10 GLU A CB    1 
ATOM   219  C  CG    . GLU A 1 29  ? 1.669   19.776  5.870   1.00 103.08 ? -10 GLU A CG    1 
ATOM   220  C  CD    . GLU A 1 29  ? 2.853   18.884  6.189   1.00 100.73 ? -10 GLU A CD    1 
ATOM   221  O  OE1   . GLU A 1 29  ? 3.949   19.424  6.475   1.00 94.14  ? -10 GLU A OE1   1 
ATOM   222  O  OE2   . GLU A 1 29  ? 2.683   17.645  6.144   1.00 100.71 ? -10 GLU A OE2   1 
ATOM   223  N  N     . GLU A 1 30  ? 3.619   21.633  2.412   1.00 98.65  ? -9  GLU A N     1 
ATOM   224  C  CA    . GLU A 1 30  ? 4.333   22.603  1.581   1.00 95.58  ? -9  GLU A CA    1 
ATOM   225  C  C     . GLU A 1 30  ? 4.129   22.319  0.091   1.00 103.30 ? -9  GLU A C     1 
ATOM   226  O  O     . GLU A 1 30  ? 3.071   22.612  -0.478  1.00 103.54 ? -9  GLU A O     1 
ATOM   227  C  CB    . GLU A 1 30  ? 5.823   22.597  1.934   1.00 87.34  ? -9  GLU A CB    1 
ATOM   228  C  CG    . GLU A 1 30  ? 6.101   23.020  3.376   1.00 90.44  ? -9  GLU A CG    1 
ATOM   229  C  CD    . GLU A 1 30  ? 7.152   22.157  4.067   1.00 92.08  ? -9  GLU A CD    1 
ATOM   230  O  OE1   . GLU A 1 30  ? 6.939   21.787  5.243   1.00 86.37  ? -9  GLU A OE1   1 
ATOM   231  O  OE2   . GLU A 1 30  ? 8.194   21.856  3.441   1.00 95.00  ? -9  GLU A OE2   1 
ATOM   232  N  N     . TYR A 1 44  ? -1.607  16.434  -5.876  1.00 85.24  ? -8  TYR A N     1 
ATOM   233  C  CA    . TYR A 1 44  ? -2.299  15.432  -5.081  1.00 80.85  ? -8  TYR A CA    1 
ATOM   234  C  C     . TYR A 1 44  ? -3.513  16.029  -4.374  1.00 87.96  ? -8  TYR A C     1 
ATOM   235  O  O     . TYR A 1 44  ? -3.536  17.221  -4.052  1.00 90.26  ? -8  TYR A O     1 
ATOM   236  C  CB    . TYR A 1 44  ? -1.350  14.813  -4.044  1.00 81.86  ? -8  TYR A CB    1 
ATOM   237  N  N     . ASP A 1 45  ? -4.527  15.188  -4.158  1.00 90.32  ? -7  ASP A N     1 
ATOM   238  C  CA    . ASP A 1 45  ? -5.623  15.453  -3.231  1.00 88.77  ? -7  ASP A CA    1 
ATOM   239  C  C     . ASP A 1 45  ? -5.381  14.772  -1.889  1.00 92.34  ? -7  ASP A C     1 
ATOM   240  O  O     . ASP A 1 45  ? -5.447  15.422  -0.840  1.00 97.98  ? -7  ASP A O     1 
ATOM   241  C  CB    . ASP A 1 45  ? -6.963  14.970  -3.812  1.00 88.50  ? -7  ASP A CB    1 
ATOM   242  C  CG    . ASP A 1 45  ? -7.379  15.717  -5.080  1.00 91.56  ? -7  ASP A CG    1 
ATOM   243  O  OD1   . ASP A 1 45  ? -8.457  15.368  -5.620  1.00 87.17  ? -7  ASP A OD1   1 
ATOM   244  O  OD2   . ASP A 1 45  ? -6.649  16.634  -5.541  1.00 89.71  ? -7  ASP A OD2   1 
ATOM   245  N  N     . TYR A 1 46  ? -5.092  13.466  -1.910  1.00 91.20  ? -6  TYR A N     1 
ATOM   246  C  CA    . TYR A 1 46  ? -4.798  12.674  -0.717  1.00 88.46  ? -6  TYR A CA    1 
ATOM   247  C  C     . TYR A 1 46  ? -3.465  11.959  -0.929  1.00 82.87  ? -6  TYR A C     1 
ATOM   248  O  O     . TYR A 1 46  ? -3.216  11.407  -2.008  1.00 73.09  ? -6  TYR A O     1 
ATOM   249  C  CB    . TYR A 1 46  ? -5.931  11.657  -0.412  1.00 85.15  ? -6  TYR A CB    1 
ATOM   250  C  CG    . TYR A 1 46  ? -7.323  12.271  -0.234  1.00 96.30  ? -6  TYR A CG    1 
ATOM   251  C  CD1   . TYR A 1 46  ? -8.006  12.174  0.978   1.00 101.46 ? -6  TYR A CD1   1 
ATOM   252  C  CD2   . TYR A 1 46  ? -7.964  12.925  -1.288  1.00 96.88  ? -6  TYR A CD2   1 
ATOM   253  C  CE1   . TYR A 1 46  ? -9.283  12.740  1.133   1.00 107.34 ? -6  TYR A CE1   1 
ATOM   254  C  CE2   . TYR A 1 46  ? -9.225  13.498  -1.139  1.00 99.15  ? -6  TYR A CE2   1 
ATOM   255  C  CZ    . TYR A 1 46  ? -9.885  13.402  0.067   1.00 106.38 ? -6  TYR A CZ    1 
ATOM   256  O  OH    . TYR A 1 46  ? -11.142 13.969  0.199   1.00 104.26 ? -6  TYR A OH    1 
ATOM   257  N  N     . LEU A 1 47  ? -2.590  12.000  0.079   1.00 78.27  ? -5  LEU A N     1 
ATOM   258  C  CA    . LEU A 1 47  ? -1.341  11.239  0.042   1.00 71.67  ? -5  LEU A CA    1 
ATOM   259  C  C     . LEU A 1 47  ? -1.616  9.869   0.634   1.00 64.47  ? -5  LEU A C     1 
ATOM   260  O  O     . LEU A 1 47  ? -1.732  9.726   1.854   1.00 68.32  ? -5  LEU A O     1 
ATOM   261  C  CB    . LEU A 1 47  ? -0.220  11.927  0.817   1.00 76.40  ? -5  LEU A CB    1 
ATOM   262  C  CG    . LEU A 1 47  ? 0.980   11.007  1.097   1.00 65.79  ? -5  LEU A CG    1 
ATOM   263  C  CD1   . LEU A 1 47  ? 1.553   10.441  -0.206  1.00 63.44  ? -5  LEU A CD1   1 
ATOM   264  C  CD2   . LEU A 1 47  ? 2.060   11.715  1.890   1.00 61.61  ? -5  LEU A CD2   1 
ATOM   265  N  N     . ILE A 1 48  ? -1.703  8.860   -0.223  1.00 64.08  ? -4  ILE A N     1 
ATOM   266  C  CA    . ILE A 1 48  ? -2.014  7.506   0.202   1.00 61.44  ? -4  ILE A CA    1 
ATOM   267  C  C     . ILE A 1 48  ? -0.755  6.658   0.102   1.00 62.40  ? -4  ILE A C     1 
ATOM   268  O  O     . ILE A 1 48  ? -0.025  6.722   -0.896  1.00 57.51  ? -4  ILE A O     1 
ATOM   269  C  CB    . ILE A 1 48  ? -3.169  6.918   -0.617  1.00 58.94  ? -4  ILE A CB    1 
ATOM   270  C  CG1   . ILE A 1 48  ? -4.418  7.760   -0.354  1.00 62.68  ? -4  ILE A CG1   1 
ATOM   271  C  CG2   . ILE A 1 48  ? -3.376  5.434   -0.275  1.00 55.28  ? -4  ILE A CG2   1 
ATOM   272  C  CD1   . ILE A 1 48  ? -5.716  7.128   -0.804  1.00 68.29  ? -4  ILE A CD1   1 
ATOM   273  N  N     . LYS A 1 49  ? -0.489  5.892   1.161   1.00 62.78  ? -3  LYS A N     1 
ATOM   274  C  CA    . LYS A 1 49  ? 0.711   5.077   1.296   1.00 59.77  ? -3  LYS A CA    1 
ATOM   275  C  C     . LYS A 1 49  ? 0.296   3.650   1.585   1.00 55.40  ? -3  LYS A C     1 
ATOM   276  O  O     . LYS A 1 49  ? -0.518  3.418   2.482   1.00 55.87  ? -3  LYS A O     1 
ATOM   277  C  CB    . LYS A 1 49  ? 1.607   5.578   2.437   1.00 52.32  ? -3  LYS A CB    1 
ATOM   278  C  CG    . LYS A 1 49  ? 1.598   7.083   2.607   1.00 59.37  ? -3  LYS A CG    1 
ATOM   279  C  CD    . LYS A 1 49  ? 2.484   7.469   3.752   1.00 60.60  ? -3  LYS A CD    1 
ATOM   280  C  CE    . LYS A 1 49  ? 1.705   8.193   4.813   1.00 67.21  ? -3  LYS A CE    1 
ATOM   281  N  NZ    . LYS A 1 49  ? 2.339   8.006   6.142   1.00 68.07  ? -3  LYS A NZ    1 
ATOM   282  N  N     . PHE A 1 50  ? 0.843   2.693   0.839   1.00 53.43  ? -2  PHE A N     1 
ATOM   283  C  CA    . PHE A 1 50  ? 0.733   1.312   1.276   1.00 54.94  ? -2  PHE A CA    1 
ATOM   284  C  C     . PHE A 1 50  ? 2.091   0.631   1.176   1.00 48.65  ? -2  PHE A C     1 
ATOM   285  O  O     . PHE A 1 50  ? 3.050   1.175   0.618   1.00 46.26  ? -2  PHE A O     1 
ATOM   286  C  CB    . PHE A 1 50  ? -0.358  0.547   0.521   1.00 51.37  ? -2  PHE A CB    1 
ATOM   287  C  CG    . PHE A 1 50  ? -0.308  0.694   -0.950  1.00 56.38  ? -2  PHE A CG    1 
ATOM   288  C  CD1   . PHE A 1 50  ? 0.559   -0.085  -1.711  1.00 66.32  ? -2  PHE A CD1   1 
ATOM   289  C  CD2   . PHE A 1 50  ? -1.159  1.581   -1.598  1.00 61.89  ? -2  PHE A CD2   1 
ATOM   290  C  CE1   . PHE A 1 50  ? 0.598   0.034   -3.120  1.00 63.61  ? -2  PHE A CE1   1 
ATOM   291  C  CE2   . PHE A 1 50  ? -1.130  1.712   -2.986  1.00 67.16  ? -2  PHE A CE2   1 
ATOM   292  C  CZ    . PHE A 1 50  ? -0.252  0.928   -3.751  1.00 64.52  ? -2  PHE A CZ    1 
ATOM   293  N  N     . LEU A 1 51  ? 2.173   -0.547  1.795   1.00 47.21  ? -1  LEU A N     1 
ATOM   294  C  CA    . LEU A 1 51  ? 3.439   -1.223  2.047   1.00 47.34  ? -1  LEU A CA    1 
ATOM   295  C  C     . LEU A 1 51  ? 3.360   -2.653  1.549   1.00 46.60  ? -1  LEU A C     1 
ATOM   296  O  O     . LEU A 1 51  ? 2.318   -3.301  1.670   1.00 51.07  ? -1  LEU A O     1 
ATOM   297  C  CB    . LEU A 1 51  ? 3.792   -1.207  3.552   1.00 50.41  ? -1  LEU A CB    1 
ATOM   298  C  CG    . LEU A 1 51  ? 5.158   -1.764  3.947   1.00 44.82  ? -1  LEU A CG    1 
ATOM   299  C  CD1   . LEU A 1 51  ? 5.759   -0.929  5.008   1.00 44.46  ? -1  LEU A CD1   1 
ATOM   300  C  CD2   . LEU A 1 51  ? 5.009   -3.176  4.445   1.00 53.26  ? -1  LEU A CD2   1 
ATOM   301  N  N     . ALA A 1 52  ? 4.472   -3.145  1.014   1.00 46.84  ? 0   ALA A N     1 
ATOM   302  C  CA    . ALA A 1 52  ? 4.565   -4.484  0.448   1.00 48.91  ? 0   ALA A CA    1 
ATOM   303  C  C     . ALA A 1 52  ? 5.419   -5.361  1.356   1.00 48.57  ? 0   ALA A C     1 
ATOM   304  O  O     . ALA A 1 52  ? 6.550   -4.993  1.696   1.00 49.95  ? 0   ALA A O     1 
ATOM   305  C  CB    . ALA A 1 52  ? 5.160   -4.435  -0.961  1.00 44.89  ? 0   ALA A CB    1 
ATOM   306  N  N     . LEU A 1 53  ? 4.881   -6.514  1.750   1.00 45.60  ? 1   LEU A N     1 
ATOM   307  C  CA    . LEU A 1 53  ? 5.604   -7.412  2.631   1.00 49.63  ? 1   LEU A CA    1 
ATOM   308  C  C     . LEU A 1 53  ? 5.406   -8.853  2.179   1.00 48.49  ? 1   LEU A C     1 
ATOM   309  O  O     . LEU A 1 53  ? 4.445   -9.192  1.478   1.00 51.29  ? 1   LEU A O     1 
ATOM   310  C  CB    . LEU A 1 53  ? 5.166   -7.243  4.090   1.00 54.03  ? 1   LEU A CB    1 
ATOM   311  C  CG    . LEU A 1 53  ? 3.786   -7.808  4.429   1.00 53.58  ? 1   LEU A CG    1 
ATOM   312  C  CD1   . LEU A 1 53  ? 3.747   -8.136  5.894   1.00 54.07  ? 1   LEU A CD1   1 
ATOM   313  C  CD2   . LEU A 1 53  ? 2.678   -6.825  4.065   1.00 49.55  ? 1   LEU A CD2   1 
ATOM   314  N  N     . GLY A 1 54  ? 6.313   -9.698  2.633   1.00 44.76  ? 2   GLY A N     1 
ATOM   315  C  CA    . GLY A 1 54  ? 6.358   -11.086 2.228   1.00 41.96  ? 2   GLY A CA    1 
ATOM   316  C  C     . GLY A 1 54  ? 7.794   -11.550 2.183   1.00 42.57  ? 2   GLY A C     1 
ATOM   317  O  O     . GLY A 1 54  ? 8.728   -10.758 2.213   1.00 46.21  ? 2   GLY A O     1 
ATOM   318  N  N     . ASP A 1 55  ? 7.957   -12.868 2.111   1.00 44.67  ? 3   ASP A N     1 
ATOM   319  C  CA    . ASP A 1 55  ? 9.281   -13.472 2.183   1.00 48.60  ? 3   ASP A CA    1 
ATOM   320  C  C     . ASP A 1 55  ? 10.210  -12.858 1.148   1.00 50.79  ? 3   ASP A C     1 
ATOM   321  O  O     . ASP A 1 55  ? 9.739   -12.273 0.166   1.00 51.90  ? 3   ASP A O     1 
ATOM   322  C  CB    . ASP A 1 55  ? 9.202   -14.982 1.957   1.00 55.03  ? 3   ASP A CB    1 
ATOM   323  C  CG    . ASP A 1 55  ? 8.795   -15.748 3.199   1.00 58.12  ? 3   ASP A CG    1 
ATOM   324  O  OD1   . ASP A 1 55  ? 8.681   -15.148 4.299   1.00 58.51  ? 3   ASP A OD1   1 
ATOM   325  O  OD2   . ASP A 1 55  ? 8.611   -16.979 3.061   1.00 59.22  ? 3   ASP A OD2   1 
ATOM   326  N  N     . SER A 1 56  ? 11.520  -12.974 1.349   1.00 48.50  ? 4   SER A N     1 
ATOM   327  C  CA    . SER A 1 56  ? 12.423  -12.512 0.311   1.00 48.11  ? 4   SER A CA    1 
ATOM   328  C  C     . SER A 1 56  ? 12.207  -13.389 -0.916  1.00 54.15  ? 4   SER A C     1 
ATOM   329  O  O     . SER A 1 56  ? 11.957  -14.591 -0.796  1.00 59.73  ? 4   SER A O     1 
ATOM   330  C  CB    . SER A 1 56  ? 13.876  -12.572 0.771   1.00 44.87  ? 4   SER A CB    1 
ATOM   331  O  OG    . SER A 1 56  ? 14.738  -12.741 -0.348  1.00 48.46  ? 4   SER A OG    1 
ATOM   332  N  N     . GLY A 1 57  ? 12.224  -12.766 -2.096  1.00 51.59  ? 5   GLY A N     1 
ATOM   333  C  CA    . GLY A 1 57  ? 12.063  -13.485 -3.336  1.00 46.37  ? 5   GLY A CA    1 
ATOM   334  C  C     . GLY A 1 57  ? 10.642  -13.623 -3.842  1.00 47.59  ? 5   GLY A C     1 
ATOM   335  O  O     . GLY A 1 57  ? 10.447  -14.194 -4.930  1.00 48.44  ? 5   GLY A O     1 
ATOM   336  N  N     . VAL A 1 58  ? 9.638   -13.117 -3.112  1.00 47.91  ? 6   VAL A N     1 
ATOM   337  C  CA    . VAL A 1 58  ? 8.260   -13.314 -3.571  1.00 51.57  ? 6   VAL A CA    1 
ATOM   338  C  C     . VAL A 1 58  ? 7.966   -12.465 -4.803  1.00 48.61  ? 6   VAL A C     1 
ATOM   339  O  O     . VAL A 1 58  ? 7.095   -12.810 -5.614  1.00 46.17  ? 6   VAL A O     1 
ATOM   340  C  CB    . VAL A 1 58  ? 7.245   -13.033 -2.443  1.00 47.82  ? 6   VAL A CB    1 
ATOM   341  C  CG1   . VAL A 1 58  ? 7.485   -13.961 -1.287  1.00 52.97  ? 6   VAL A CG1   1 
ATOM   342  C  CG2   . VAL A 1 58  ? 7.314   -11.594 -1.990  1.00 45.82  ? 6   VAL A CG2   1 
ATOM   343  N  N     . GLY A 1 59  ? 8.682   -11.359 -4.969  1.00 51.57  ? 7   GLY A N     1 
ATOM   344  C  CA    . GLY A 1 59  ? 8.484   -10.464 -6.090  1.00 48.98  ? 7   GLY A CA    1 
ATOM   345  C  C     . GLY A 1 59  ? 8.027   -9.086  -5.641  1.00 54.47  ? 7   GLY A C     1 
ATOM   346  O  O     . GLY A 1 59  ? 7.559   -8.293  -6.462  1.00 52.47  ? 7   GLY A O     1 
ATOM   347  N  N     . LYS A 1 60  ? 8.177   -8.780  -4.345  1.00 52.02  ? 8   LYS A N     1 
ATOM   348  C  CA    . LYS A 1 60  ? 7.693   -7.512  -3.808  1.00 46.57  ? 8   LYS A CA    1 
ATOM   349  C  C     . LYS A 1 60  ? 8.182   -6.345  -4.648  1.00 50.87  ? 8   LYS A C     1 
ATOM   350  O  O     . LYS A 1 60  ? 7.387   -5.535  -5.144  1.00 53.42  ? 8   LYS A O     1 
ATOM   351  C  CB    . LYS A 1 60  ? 8.148   -7.343  -2.362  1.00 46.75  ? 8   LYS A CB    1 
ATOM   352  C  CG    . LYS A 1 60  ? 7.319   -8.085  -1.320  1.00 49.25  ? 8   LYS A CG    1 
ATOM   353  C  CD    . LYS A 1 60  ? 8.083   -8.106  0.003   1.00 45.43  ? 8   LYS A CD    1 
ATOM   354  C  CE    . LYS A 1 60  ? 9.377   -8.858  -0.188  1.00 42.66  ? 8   LYS A CE    1 
ATOM   355  N  NZ    . LYS A 1 60  ? 10.327  -8.727  0.923   1.00 48.76  ? 8   LYS A NZ    1 
ATOM   356  N  N     . THR A 1 61  ? 9.496   -6.264  -4.849  1.00 49.67  ? 9   THR A N     1 
ATOM   357  C  CA    . THR A 1 61  ? 10.046  -5.171  -5.639  1.00 48.78  ? 9   THR A CA    1 
ATOM   358  C  C     . THR A 1 61  ? 9.587   -5.252  -7.094  1.00 50.95  ? 9   THR A C     1 
ATOM   359  O  O     . THR A 1 61  ? 9.235   -4.236  -7.705  1.00 50.38  ? 9   THR A O     1 
ATOM   360  C  CB    . THR A 1 61  ? 11.568  -5.186  -5.529  1.00 47.15  ? 9   THR A CB    1 
ATOM   361  O  OG1   . THR A 1 61  ? 11.937  -4.986  -4.157  1.00 44.45  ? 9   THR A OG1   1 
ATOM   362  C  CG2   . THR A 1 61  ? 12.177  -4.096  -6.401  1.00 44.11  ? 9   THR A CG2   1 
ATOM   363  N  N     . SER A 1 62  ? 9.550   -6.453  -7.660  1.00 46.69  ? 10  SER A N     1 
ATOM   364  C  CA    . SER A 1 62  ? 9.120   -6.573  -9.044  1.00 49.40  ? 10  SER A CA    1 
ATOM   365  C  C     . SER A 1 62  ? 7.653   -6.188  -9.218  1.00 50.81  ? 10  SER A C     1 
ATOM   366  O  O     . SER A 1 62  ? 7.269   -5.616  -10.247 1.00 58.88  ? 10  SER A O     1 
ATOM   367  C  CB    . SER A 1 62  ? 9.396   -7.988  -9.554  1.00 48.21  ? 10  SER A CB    1 
ATOM   368  O  OG    . SER A 1 62  ? 10.729  -8.389  -9.254  1.00 49.13  ? 10  SER A OG    1 
ATOM   369  N  N     . VAL A 1 63  ? 6.817   -6.505  -8.236  1.00 44.78  ? 11  VAL A N     1 
ATOM   370  C  CA    . VAL A 1 63  ? 5.404   -6.156  -8.319  1.00 49.73  ? 11  VAL A CA    1 
ATOM   371  C  C     . VAL A 1 63  ? 5.224   -4.647  -8.342  1.00 52.13  ? 11  VAL A C     1 
ATOM   372  O  O     . VAL A 1 63  ? 4.396   -4.110  -9.089  1.00 50.75  ? 11  VAL A O     1 
ATOM   373  C  CB    . VAL A 1 63  ? 4.641   -6.809  -7.154  1.00 53.72  ? 11  VAL A CB    1 
ATOM   374  C  CG1   . VAL A 1 63  ? 3.266   -6.175  -6.956  1.00 47.32  ? 11  VAL A CG1   1 
ATOM   375  C  CG2   . VAL A 1 63  ? 4.494   -8.290  -7.426  1.00 52.43  ? 11  VAL A CG2   1 
ATOM   376  N  N     . LEU A 1 64  ? 6.002   -3.935  -7.537  1.00 52.58  ? 12  LEU A N     1 
ATOM   377  C  CA    . LEU A 1 64  ? 5.899   -2.484  -7.572  1.00 52.78  ? 12  LEU A CA    1 
ATOM   378  C  C     . LEU A 1 64  ? 6.501   -1.931  -8.860  1.00 50.52  ? 12  LEU A C     1 
ATOM   379  O  O     . LEU A 1 64  ? 5.926   -1.032  -9.487  1.00 48.53  ? 12  LEU A O     1 
ATOM   380  C  CB    . LEU A 1 64  ? 6.574   -1.908  -6.333  1.00 50.77  ? 12  LEU A CB    1 
ATOM   381  C  CG    . LEU A 1 64  ? 6.015   -2.490  -5.029  1.00 46.62  ? 12  LEU A CG    1 
ATOM   382  C  CD1   . LEU A 1 64  ? 6.740   -1.913  -3.822  1.00 43.95  ? 12  LEU A CD1   1 
ATOM   383  C  CD2   . LEU A 1 64  ? 4.521   -2.254  -4.904  1.00 38.49  ? 12  LEU A CD2   1 
ATOM   384  N  N     . TYR A 1 65  ? 7.643   -2.482  -9.281  1.00 48.01  ? 13  TYR A N     1 
ATOM   385  C  CA    . TYR A 1 65  ? 8.323   -1.970  -10.461 1.00 49.50  ? 13  TYR A CA    1 
ATOM   386  C  C     . TYR A 1 65  ? 7.439   -2.127  -11.689 1.00 54.25  ? 13  TYR A C     1 
ATOM   387  O  O     . TYR A 1 65  ? 7.292   -1.197  -12.492 1.00 51.66  ? 13  TYR A O     1 
ATOM   388  C  CB    . TYR A 1 65  ? 9.666   -2.683  -10.633 1.00 46.36  ? 13  TYR A CB    1 
ATOM   389  C  CG    . TYR A 1 65  ? 10.570  -2.093  -11.702 1.00 54.08  ? 13  TYR A CG    1 
ATOM   390  C  CD1   . TYR A 1 65  ? 10.489  -0.751  -12.059 1.00 52.79  ? 13  TYR A CD1   1 
ATOM   391  C  CD2   . TYR A 1 65  ? 11.493  -2.896  -12.374 1.00 60.35  ? 13  TYR A CD2   1 
ATOM   392  C  CE1   . TYR A 1 65  ? 11.314  -0.213  -13.047 1.00 54.41  ? 13  TYR A CE1   1 
ATOM   393  C  CE2   . TYR A 1 65  ? 12.320  -2.374  -13.365 1.00 61.01  ? 13  TYR A CE2   1 
ATOM   394  C  CZ    . TYR A 1 65  ? 12.226  -1.031  -13.697 1.00 61.61  ? 13  TYR A CZ    1 
ATOM   395  O  OH    . TYR A 1 65  ? 13.045  -0.526  -14.688 1.00 66.70  ? 13  TYR A OH    1 
ATOM   396  N  N     . GLN A 1 66  ? 6.814   -3.298  -11.829 1.00 53.37  ? 14  GLN A N     1 
ATOM   397  C  CA    . GLN A 1 66  ? 5.820   -3.506  -12.876 1.00 52.22  ? 14  GLN A CA    1 
ATOM   398  C  C     . GLN A 1 66  ? 4.697   -2.485  -12.810 1.00 48.15  ? 14  GLN A C     1 
ATOM   399  O  O     . GLN A 1 66  ? 4.162   -2.075  -13.837 1.00 53.69  ? 14  GLN A O     1 
ATOM   400  C  CB    . GLN A 1 66  ? 5.239   -4.911  -12.751 1.00 57.37  ? 14  GLN A CB    1 
ATOM   401  C  CG    . GLN A 1 66  ? 4.152   -5.208  -13.739 1.00 52.09  ? 14  GLN A CG    1 
ATOM   402  C  CD    . GLN A 1 66  ? 4.675   -5.149  -15.124 1.00 54.93  ? 14  GLN A CD    1 
ATOM   403  O  OE1   . GLN A 1 66  ? 4.261   -4.304  -15.923 1.00 53.97  ? 14  GLN A OE1   1 
ATOM   404  N  NE2   . GLN A 1 66  ? 5.628   -6.024  -15.425 1.00 54.08  ? 14  GLN A NE2   1 
ATOM   405  N  N     . TYR A 1 67  ? 4.321   -2.070  -11.618 1.00 53.97  ? 15  TYR A N     1 
ATOM   406  C  CA    . TYR A 1 67  ? 3.160   -1.207  -11.505 1.00 52.46  ? 15  TYR A CA    1 
ATOM   407  C  C     . TYR A 1 67  ? 3.521   0.243   -11.779 1.00 54.52  ? 15  TYR A C     1 
ATOM   408  O  O     . TYR A 1 67  ? 2.739   0.969   -12.404 1.00 57.77  ? 15  TYR A O     1 
ATOM   409  C  CB    . TYR A 1 67  ? 2.535   -1.351  -10.117 1.00 52.69  ? 15  TYR A CB    1 
ATOM   410  C  CG    . TYR A 1 67  ? 1.304   -0.523  -9.949  1.00 50.24  ? 15  TYR A CG    1 
ATOM   411  C  CD1   . TYR A 1 67  ? 0.059   -1.037  -10.249 1.00 51.28  ? 15  TYR A CD1   1 
ATOM   412  C  CD2   . TYR A 1 67  ? 1.389   0.793   -9.508  1.00 54.04  ? 15  TYR A CD2   1 
ATOM   413  C  CE1   . TYR A 1 67  ? -1.087  -0.272  -10.104 1.00 54.69  ? 15  TYR A CE1   1 
ATOM   414  C  CE2   . TYR A 1 67  ? 0.258   1.572   -9.369  1.00 54.29  ? 15  TYR A CE2   1 
ATOM   415  C  CZ    . TYR A 1 67  ? -0.981  1.037   -9.671  1.00 53.57  ? 15  TYR A CZ    1 
ATOM   416  O  OH    . TYR A 1 67  ? -2.107  1.825   -9.538  1.00 55.27  ? 15  TYR A OH    1 
ATOM   417  N  N     . THR A 1 68  ? 4.689   0.693   -11.320 1.00 53.28  ? 16  THR A N     1 
ATOM   418  C  CA    . THR A 1 68  ? 5.023   2.100   -11.514 1.00 55.20  ? 16  THR A CA    1 
ATOM   419  C  C     . THR A 1 68  ? 5.596   2.379   -12.903 1.00 52.55  ? 16  THR A C     1 
ATOM   420  O  O     . THR A 1 68  ? 5.390   3.473   -13.443 1.00 54.03  ? 16  THR A O     1 
ATOM   421  C  CB    . THR A 1 68  ? 6.004   2.583   -10.438 1.00 49.36  ? 16  THR A CB    1 
ATOM   422  O  OG1   . THR A 1 68  ? 7.113   1.679   -10.342 1.00 48.98  ? 16  THR A OG1   1 
ATOM   423  C  CG2   . THR A 1 68  ? 5.306   2.689   -9.091  1.00 45.79  ? 16  THR A CG2   1 
ATOM   424  N  N     . ASP A 1 69  ? 6.324   1.435   -13.490 1.00 47.31  ? 17  ASP A N     1 
ATOM   425  C  CA    . ASP A 1 69  ? 6.974   1.676   -14.768 1.00 50.42  ? 17  ASP A CA    1 
ATOM   426  C  C     . ASP A 1 69  ? 6.645   0.644   -15.827 1.00 50.65  ? 17  ASP A C     1 
ATOM   427  O  O     . ASP A 1 69  ? 7.323   0.621   -16.860 1.00 55.33  ? 17  ASP A O     1 
ATOM   428  C  CB    . ASP A 1 69  ? 8.501   1.731   -14.612 1.00 52.05  ? 17  ASP A CB    1 
ATOM   429  C  CG    . ASP A 1 69  ? 8.946   2.786   -13.633 1.00 49.64  ? 17  ASP A CG    1 
ATOM   430  O  OD1   . ASP A 1 69  ? 8.542   2.683   -12.459 1.00 56.55  ? 17  ASP A OD1   1 
ATOM   431  O  OD2   . ASP A 1 69  ? 9.669   3.724   -14.041 1.00 50.97  ? 17  ASP A OD2   1 
ATOM   432  N  N     . GLY A 1 70  ? 5.649   -0.215  -15.604 1.00 50.51  ? 18  GLY A N     1 
ATOM   433  C  CA    . GLY A 1 70  ? 5.328   -1.274  -16.547 1.00 50.06  ? 18  GLY A CA    1 
ATOM   434  C  C     . GLY A 1 70  ? 6.521   -2.081  -17.013 1.00 51.06  ? 18  GLY A C     1 
ATOM   435  O  O     . GLY A 1 70  ? 6.473   -2.705  -18.077 1.00 54.07  ? 18  GLY A O     1 
ATOM   436  N  N     . LYS A 1 71  ? 7.608   -2.055  -16.267 1.00 48.99  ? 19  LYS A N     1 
ATOM   437  C  CA    . LYS A 1 71  ? 8.811   -2.788  -16.614 1.00 51.64  ? 19  LYS A CA    1 
ATOM   438  C  C     . LYS A 1 71  ? 8.926   -4.010  -15.707 1.00 53.96  ? 19  LYS A C     1 
ATOM   439  O  O     . LYS A 1 71  ? 8.063   -4.277  -14.865 1.00 55.00  ? 19  LYS A O     1 
ATOM   440  C  CB    . LYS A 1 71  ? 10.045  -1.885  -16.511 1.00 49.93  ? 19  LYS A CB    1 
ATOM   441  C  CG    . LYS A 1 71  ? 10.052  -0.722  -17.477 1.00 49.15  ? 19  LYS A CG    1 
ATOM   442  C  CD    . LYS A 1 71  ? 11.321  0.093   -17.303 1.00 56.45  ? 19  LYS A CD    1 
ATOM   443  C  CE    . LYS A 1 71  ? 11.553  1.099   -18.434 1.00 52.34  ? 19  LYS A CE    1 
ATOM   444  N  NZ    . LYS A 1 71  ? 12.942  1.631   -18.284 1.00 55.13  ? 19  LYS A NZ    1 
ATOM   445  N  N     . PHE A 1 72  ? 9.999   -4.771  -15.902 1.00 51.56  ? 20  PHE A N     1 
ATOM   446  C  CA    . PHE A 1 72  ? 10.246  -5.963  -15.106 1.00 49.22  ? 20  PHE A CA    1 
ATOM   447  C  C     . PHE A 1 72  ? 11.672  -6.394  -15.360 1.00 46.50  ? 20  PHE A C     1 
ATOM   448  O  O     . PHE A 1 72  ? 12.152  -6.318  -16.486 1.00 50.80  ? 20  PHE A O     1 
ATOM   449  C  CB    . PHE A 1 72  ? 9.295   -7.104  -15.453 1.00 50.27  ? 20  PHE A CB    1 
ATOM   450  C  CG    . PHE A 1 72  ? 9.759   -8.440  -14.962 1.00 56.60  ? 20  PHE A CG    1 
ATOM   451  C  CD1   . PHE A 1 72  ? 9.662   -8.767  -13.615 1.00 51.93  ? 20  PHE A CD1   1 
ATOM   452  C  CD2   . PHE A 1 72  ? 10.277  -9.383  -15.844 1.00 55.16  ? 20  PHE A CD2   1 
ATOM   453  C  CE1   . PHE A 1 72  ? 10.082  -10.004 -13.147 1.00 49.13  ? 20  PHE A CE1   1 
ATOM   454  C  CE2   . PHE A 1 72  ? 10.702  -10.630 -15.376 1.00 55.70  ? 20  PHE A CE2   1 
ATOM   455  C  CZ    . PHE A 1 72  ? 10.601  -10.934 -14.018 1.00 53.05  ? 20  PHE A CZ    1 
ATOM   456  N  N     . ASN A 1 73  ? 12.349  -6.797  -14.303 1.00 51.58  ? 21  ASN A N     1 
ATOM   457  C  CA    . ASN A 1 73  ? 13.724  -7.263  -14.369 1.00 52.01  ? 21  ASN A CA    1 
ATOM   458  C  C     . ASN A 1 73  ? 13.767  -8.667  -13.786 1.00 53.77  ? 21  ASN A C     1 
ATOM   459  O  O     . ASN A 1 73  ? 13.006  -8.988  -12.866 1.00 51.99  ? 21  ASN A O     1 
ATOM   460  C  CB    . ASN A 1 73  ? 14.683  -6.312  -13.620 1.00 51.99  ? 21  ASN A CB    1 
ATOM   461  C  CG    . ASN A 1 73  ? 16.148  -6.578  -13.949 1.00 54.58  ? 21  ASN A CG    1 
ATOM   462  O  OD1   . ASN A 1 73  ? 16.519  -7.665  -14.436 1.00 55.88  ? 21  ASN A OD1   1 
ATOM   463  N  ND2   . ASN A 1 73  ? 16.985  -5.574  -13.719 1.00 53.44  ? 21  ASN A ND2   1 
ATOM   464  N  N     . SER A 1 74  ? 14.623  -9.522  -14.344 1.00 57.68  ? 22  SER A N     1 
ATOM   465  C  CA    . SER A 1 74  ? 14.600  -10.915 -13.918 1.00 56.89  ? 22  SER A CA    1 
ATOM   466  C  C     . SER A 1 74  ? 15.760  -11.285 -13.011 1.00 52.22  ? 22  SER A C     1 
ATOM   467  O  O     . SER A 1 74  ? 15.647  -12.251 -12.249 1.00 57.88  ? 22  SER A O     1 
ATOM   468  C  CB    . SER A 1 74  ? 14.587  -11.865 -15.124 1.00 53.73  ? 22  SER A CB    1 
ATOM   469  O  OG    . SER A 1 74  ? 15.523  -11.469 -16.111 1.00 50.45  ? 22  SER A OG    1 
ATOM   470  N  N     . LYS A 1 75  ? 16.880  -10.577 -13.063 1.00 49.55  ? 23  LYS A N     1 
ATOM   471  C  CA    . LYS A 1 75  ? 17.940  -10.931 -12.135 1.00 62.84  ? 23  LYS A CA    1 
ATOM   472  C  C     . LYS A 1 75  ? 17.546  -10.440 -10.758 1.00 62.44  ? 23  LYS A C     1 
ATOM   473  O  O     . LYS A 1 75  ? 17.001  -9.345  -10.612 1.00 60.58  ? 23  LYS A O     1 
ATOM   474  C  CB    . LYS A 1 75  ? 19.289  -10.337 -12.531 1.00 64.62  ? 23  LYS A CB    1 
ATOM   475  C  CG    . LYS A 1 75  ? 20.421  -10.871 -11.623 1.00 74.85  ? 23  LYS A CG    1 
ATOM   476  C  CD    . LYS A 1 75  ? 20.533  -12.410 -11.710 1.00 72.05  ? 23  LYS A CD    1 
ATOM   477  C  CE    . LYS A 1 75  ? 20.734  -13.059 -10.350 1.00 78.43  ? 23  LYS A CE    1 
ATOM   478  N  NZ    . LYS A 1 75  ? 19.470  -13.669 -9.857  1.00 85.88  ? 23  LYS A NZ    1 
ATOM   479  N  N     . PHE A 1 76  ? 17.806  -11.255 -9.748  1.00 60.07  ? 24  PHE A N     1 
ATOM   480  C  CA    . PHE A 1 76  ? 17.327  -10.928 -8.414  1.00 58.53  ? 24  PHE A CA    1 
ATOM   481  C  C     . PHE A 1 76  ? 18.264  -9.906  -7.779  1.00 56.01  ? 24  PHE A C     1 
ATOM   482  O  O     . PHE A 1 76  ? 19.467  -10.152 -7.641  1.00 61.45  ? 24  PHE A O     1 
ATOM   483  C  CB    . PHE A 1 76  ? 17.209  -12.192 -7.568  1.00 52.50  ? 24  PHE A CB    1 
ATOM   484  C  CG    . PHE A 1 76  ? 16.557  -11.968 -6.270  1.00 57.39  ? 24  PHE A CG    1 
ATOM   485  C  CD1   . PHE A 1 76  ? 15.554  -11.013 -6.143  1.00 60.01  ? 24  PHE A CD1   1 
ATOM   486  C  CD2   . PHE A 1 76  ? 16.957  -12.686 -5.150  1.00 60.21  ? 24  PHE A CD2   1 
ATOM   487  C  CE1   . PHE A 1 76  ? 14.955  -10.771 -4.900  1.00 53.60  ? 24  PHE A CE1   1 
ATOM   488  C  CE2   . PHE A 1 76  ? 16.367  -12.466 -3.922  1.00 52.11  ? 24  PHE A CE2   1 
ATOM   489  C  CZ    . PHE A 1 76  ? 15.356  -11.508 -3.797  1.00 54.64  ? 24  PHE A CZ    1 
ATOM   490  N  N     . ILE A 1 77  ? 17.717  -8.745  -7.440  1.00 53.33  ? 25  ILE A N     1 
ATOM   491  C  CA    . ILE A 1 77  ? 18.401  -7.723  -6.649  1.00 59.84  ? 25  ILE A CA    1 
ATOM   492  C  C     . ILE A 1 77  ? 17.600  -7.587  -5.361  1.00 51.60  ? 25  ILE A C     1 
ATOM   493  O  O     . ILE A 1 77  ? 16.528  -6.965  -5.347  1.00 47.68  ? 25  ILE A O     1 
ATOM   494  C  CB    . ILE A 1 77  ? 18.494  -6.380  -7.384  1.00 59.81  ? 25  ILE A CB    1 
ATOM   495  C  CG1   . ILE A 1 77  ? 19.379  -6.509  -8.627  1.00 53.01  ? 25  ILE A CG1   1 
ATOM   496  C  CG2   . ILE A 1 77  ? 18.930  -5.251  -6.409  1.00 44.86  ? 25  ILE A CG2   1 
ATOM   497  C  CD1   . ILE A 1 77  ? 19.179  -5.365  -9.619  1.00 59.62  ? 25  ILE A CD1   1 
ATOM   498  N  N     . THR A 1 78  ? 18.092  -8.181  -4.281  1.00 52.34  ? 26  THR A N     1 
ATOM   499  C  CA    . THR A 1 78  ? 17.317  -8.180  -3.044  1.00 54.24  ? 26  THR A CA    1 
ATOM   500  C  C     . THR A 1 78  ? 17.328  -6.787  -2.418  1.00 45.82  ? 26  THR A C     1 
ATOM   501  O  O     . THR A 1 78  ? 18.343  -6.082  -2.438  1.00 44.50  ? 26  THR A O     1 
ATOM   502  C  CB    . THR A 1 78  ? 17.842  -9.257  -2.083  1.00 45.81  ? 26  THR A CB    1 
ATOM   503  O  OG1   . THR A 1 78  ? 16.806  -9.626  -1.171  1.00 42.45  ? 26  THR A OG1   1 
ATOM   504  C  CG2   . THR A 1 78  ? 19.098  -8.828  -1.337  1.00 38.76  ? 26  THR A CG2   1 
ATOM   505  N  N     . THR A 1 79  ? 16.163  -6.360  -1.930  1.00 41.20  ? 27  THR A N     1 
ATOM   506  C  CA    . THR A 1 79  ? 16.006  -4.986  -1.448  1.00 47.99  ? 27  THR A CA    1 
ATOM   507  C  C     . THR A 1 79  ? 16.839  -4.753  -0.185  1.00 51.88  ? 27  THR A C     1 
ATOM   508  O  O     . THR A 1 79  ? 16.671  -5.459  0.820   1.00 43.96  ? 27  THR A O     1 
ATOM   509  C  CB    . THR A 1 79  ? 14.536  -4.691  -1.161  1.00 45.47  ? 27  THR A CB    1 
ATOM   510  O  OG1   . THR A 1 79  ? 13.757  -4.939  -2.337  1.00 44.64  ? 27  THR A OG1   1 
ATOM   511  C  CG2   . THR A 1 79  ? 14.355  -3.236  -0.714  1.00 41.34  ? 27  THR A CG2   1 
ATOM   512  N  N     . VAL A 1 80  ? 17.717  -3.752  -0.221  1.00 48.66  ? 28  VAL A N     1 
ATOM   513  C  CA    . VAL A 1 80  ? 18.586  -3.473  0.920   1.00 46.89  ? 28  VAL A CA    1 
ATOM   514  C  C     . VAL A 1 80  ? 17.762  -2.692  1.941   1.00 52.61  ? 28  VAL A C     1 
ATOM   515  O  O     . VAL A 1 80  ? 17.570  -1.476  1.819   1.00 59.71  ? 28  VAL A O     1 
ATOM   516  C  CB    . VAL A 1 80  ? 19.852  -2.717  0.518   1.00 55.71  ? 28  VAL A CB    1 
ATOM   517  C  CG1   . VAL A 1 80  ? 20.591  -2.245  1.765   1.00 56.38  ? 28  VAL A CG1   1 
ATOM   518  C  CG2   . VAL A 1 80  ? 20.752  -3.597  -0.326  1.00 51.99  ? 28  VAL A CG2   1 
ATOM   519  N  N     . GLY A 1 81  ? 17.267  -3.396  2.953   1.00 49.59  ? 29  GLY A N     1 
ATOM   520  C  CA    . GLY A 1 81  ? 16.463  -2.778  3.981   1.00 48.25  ? 29  GLY A CA    1 
ATOM   521  C  C     . GLY A 1 81  ? 15.073  -2.390  3.531   1.00 43.85  ? 29  GLY A C     1 
ATOM   522  O  O     . GLY A 1 81  ? 14.114  -3.147  3.674   1.00 48.78  ? 29  GLY A O     1 
ATOM   523  N  N     . ILE A 1 82  ? 14.943  -1.189  2.997   1.00 46.56  ? 30  ILE A N     1 
ATOM   524  C  CA    . ILE A 1 82  ? 13.648  -0.703  2.559   1.00 46.25  ? 30  ILE A CA    1 
ATOM   525  C  C     . ILE A 1 82  ? 13.867  0.254   1.399   1.00 47.68  ? 30  ILE A C     1 
ATOM   526  O  O     . ILE A 1 82  ? 14.904  0.929   1.311   1.00 44.18  ? 30  ILE A O     1 
ATOM   527  C  CB    . ILE A 1 82  ? 12.880  -0.018  3.712   1.00 44.30  ? 30  ILE A CB    1 
ATOM   528  C  CG1   . ILE A 1 82  ? 11.424  0.187   3.303   1.00 48.56  ? 30  ILE A CG1   1 
ATOM   529  C  CG2   . ILE A 1 82  ? 13.528  1.337   4.080   1.00 43.94  ? 30  ILE A CG2   1 
ATOM   530  C  CD1   . ILE A 1 82  ? 10.436  0.058   4.420   1.00 50.88  ? 30  ILE A CD1   1 
ATOM   531  N  N     . ASP A 1 83  ? 12.891  0.283   0.491   1.00 47.33  ? 31  ASP A N     1 
ATOM   532  C  CA    . ASP A 1 83  ? 12.845  1.282   -0.565  1.00 49.79  ? 31  ASP A CA    1 
ATOM   533  C  C     . ASP A 1 83  ? 11.385  1.609   -0.848  1.00 50.47  ? 31  ASP A C     1 
ATOM   534  O  O     . ASP A 1 83  ? 10.470  0.998   -0.284  1.00 51.35  ? 31  ASP A O     1 
ATOM   535  C  CB    . ASP A 1 83  ? 13.590  0.797   -1.809  1.00 34.40  ? 31  ASP A CB    1 
ATOM   536  C  CG    . ASP A 1 83  ? 14.383  1.898   -2.461  1.00 51.15  ? 31  ASP A CG    1 
ATOM   537  O  OD1   . ASP A 1 83  ? 13.867  3.042   -2.517  1.00 56.80  ? 31  ASP A OD1   1 
ATOM   538  O  OD2   . ASP A 1 83  ? 15.555  1.650   -2.843  1.00 58.67  ? 31  ASP A OD2   1 
ATOM   539  N  N     . PHE A 1 84  ? 11.159  2.605   -1.699  1.00 45.73  ? 32  PHE A N     1 
ATOM   540  C  CA    . PHE A 1 84  ? 9.778   2.923   -2.031  1.00 52.76  ? 32  PHE A CA    1 
ATOM   541  C  C     . PHE A 1 84  ? 9.717   3.589   -3.396  1.00 52.41  ? 32  PHE A C     1 
ATOM   542  O  O     . PHE A 1 84  ? 10.455  4.541   -3.656  1.00 59.10  ? 32  PHE A O     1 
ATOM   543  C  CB    . PHE A 1 84  ? 9.124   3.800   -0.937  1.00 49.02  ? 32  PHE A CB    1 
ATOM   544  C  CG    . PHE A 1 84  ? 9.462   5.285   -1.012  1.00 52.03  ? 32  PHE A CG    1 
ATOM   545  C  CD1   . PHE A 1 84  ? 8.659   6.159   -1.736  1.00 52.12  ? 32  PHE A CD1   1 
ATOM   546  C  CD2   . PHE A 1 84  ? 10.538  5.815   -0.299  1.00 53.53  ? 32  PHE A CD2   1 
ATOM   547  C  CE1   . PHE A 1 84  ? 8.946   7.519   -1.790  1.00 51.31  ? 32  PHE A CE1   1 
ATOM   548  C  CE2   . PHE A 1 84  ? 10.832  7.180   -0.358  1.00 52.72  ? 32  PHE A CE2   1 
ATOM   549  C  CZ    . PHE A 1 84  ? 10.031  8.029   -1.102  1.00 50.75  ? 32  PHE A CZ    1 
ATOM   550  N  N     . ARG A 1 85  ? 8.858   3.069   -4.263  1.00 52.43  ? 33  ARG A N     1 
ATOM   551  C  CA    . ARG A 1 85  ? 8.543   3.712   -5.528  1.00 57.64  ? 33  ARG A CA    1 
ATOM   552  C  C     . ARG A 1 85  ? 7.392   4.684   -5.320  1.00 57.73  ? 33  ARG A C     1 
ATOM   553  O  O     . ARG A 1 85  ? 6.667   4.615   -4.321  1.00 52.90  ? 33  ARG A O     1 
ATOM   554  C  CB    . ARG A 1 85  ? 8.167   2.683   -6.604  1.00 53.95  ? 33  ARG A CB    1 
ATOM   555  C  CG    . ARG A 1 85  ? 9.155   1.519   -6.729  1.00 54.57  ? 33  ARG A CG    1 
ATOM   556  C  CD    . ARG A 1 85  ? 9.121   0.846   -8.118  1.00 49.67  ? 33  ARG A CD    1 
ATOM   557  N  NE    . ARG A 1 85  ? 9.592   1.727   -9.181  1.00 48.08  ? 33  ARG A NE    1 
ATOM   558  C  CZ    . ARG A 1 85  ? 10.865  2.072   -9.356  1.00 52.05  ? 33  ARG A CZ    1 
ATOM   559  N  NH1   . ARG A 1 85  ? 11.804  1.609   -8.534  1.00 50.06  ? 33  ARG A NH1   1 
ATOM   560  N  NH2   . ARG A 1 85  ? 11.205  2.887   -10.350 1.00 53.50  ? 33  ARG A NH2   1 
ATOM   561  N  N     . GLU A 1 86  ? 7.247   5.607   -6.274  1.00 60.67  ? 34  GLU A N     1 
ATOM   562  C  CA    . GLU A 1 86  ? 6.205   6.625   -6.259  1.00 56.16  ? 34  GLU A CA    1 
ATOM   563  C  C     . GLU A 1 86  ? 5.356   6.474   -7.513  1.00 53.43  ? 34  GLU A C     1 
ATOM   564  O  O     . GLU A 1 86  ? 5.837   5.987   -8.541  1.00 54.68  ? 34  GLU A O     1 
ATOM   565  C  CB    . GLU A 1 86  ? 6.819   8.043   -6.185  1.00 54.65  ? 34  GLU A CB    1 
ATOM   566  C  CG    . GLU A 1 86  ? 6.851   8.664   -4.788  1.00 52.88  ? 34  GLU A CG    1 
ATOM   567  C  CD    . GLU A 1 86  ? 7.798   9.872   -4.668  1.00 63.67  ? 34  GLU A CD    1 
ATOM   568  O  OE1   . GLU A 1 86  ? 9.045   9.699   -4.692  1.00 60.96  ? 34  GLU A OE1   1 
ATOM   569  O  OE2   . GLU A 1 86  ? 7.288   11.008  -4.536  1.00 64.50  ? 34  GLU A OE2   1 
ATOM   570  N  N     . LYS A 1 87  ? 4.082   6.867   -7.429  1.00 54.80  ? 35  LYS A N     1 
ATOM   571  C  CA    . LYS A 1 87  ? 3.243   6.888   -8.627  1.00 59.53  ? 35  LYS A CA    1 
ATOM   572  C  C     . LYS A 1 87  ? 2.050   7.817   -8.435  1.00 60.12  ? 35  LYS A C     1 
ATOM   573  O  O     . LYS A 1 87  ? 1.339   7.705   -7.434  1.00 59.78  ? 35  LYS A O     1 
ATOM   574  C  CB    . LYS A 1 87  ? 2.744   5.482   -9.001  1.00 55.54  ? 35  LYS A CB    1 
ATOM   575  C  CG    . LYS A 1 87  ? 1.935   5.471   -10.328 1.00 65.58  ? 35  LYS A CG    1 
ATOM   576  C  CD    . LYS A 1 87  ? 2.495   4.525   -11.402 1.00 56.80  ? 35  LYS A CD    1 
ATOM   577  C  CE    . LYS A 1 87  ? 1.698   4.604   -12.696 1.00 63.92  ? 35  LYS A CE    1 
ATOM   578  N  NZ    . LYS A 1 87  ? 1.966   5.855   -13.490 1.00 71.77  ? 35  LYS A NZ    1 
ATOM   579  N  N     . ARG A 1 88  ? 1.821   8.713   -9.405  1.00 61.53  ? 36  ARG A N     1 
ATOM   580  C  CA    . ARG A 1 88  ? 0.619   9.542   -9.448  1.00 61.03  ? 36  ARG A CA    1 
ATOM   581  C  C     . ARG A 1 88  ? -0.486  8.834   -10.220 1.00 59.97  ? 36  ARG A C     1 
ATOM   582  O  O     . ARG A 1 88  ? -0.224  8.176   -11.236 1.00 63.22  ? 36  ARG A O     1 
ATOM   583  C  CB    . ARG A 1 88  ? 0.929   10.902  -10.074 1.00 66.52  ? 36  ARG A CB    1 
ATOM   584  C  CG    . ARG A 1 88  ? 1.576   11.834  -9.069  1.00 67.51  ? 36  ARG A CG    1 
ATOM   585  C  CD    . ARG A 1 88  ? 2.706   12.675  -9.657  1.00 73.95  ? 36  ARG A CD    1 
ATOM   586  N  NE    . ARG A 1 88  ? 3.609   13.179  -8.616  1.00 76.32  ? 36  ARG A NE    1 
ATOM   587  C  CZ    . ARG A 1 88  ? 3.237   13.899  -7.552  1.00 81.39  ? 36  ARG A CZ    1 
ATOM   588  N  NH1   . ARG A 1 88  ? 1.964   14.235  -7.364  1.00 79.28  ? 36  ARG A NH1   1 
ATOM   589  N  NH2   . ARG A 1 88  ? 4.148   14.303  -6.670  1.00 74.90  ? 36  ARG A NH2   1 
ATOM   590  N  N     . VAL A 1 89  ? -1.722  8.972   -9.733  1.00 55.37  ? 37  VAL A N     1 
ATOM   591  C  CA    . VAL A 1 89  ? -2.819  8.096   -10.130 1.00 55.21  ? 37  VAL A CA    1 
ATOM   592  C  C     . VAL A 1 89  ? -4.137  8.827   -9.917  1.00 58.60  ? 37  VAL A C     1 
ATOM   593  O  O     . VAL A 1 89  ? -4.291  9.601   -8.965  1.00 58.22  ? 37  VAL A O     1 
ATOM   594  C  CB    . VAL A 1 89  ? -2.770  6.762   -9.337  1.00 60.83  ? 37  VAL A CB    1 
ATOM   595  C  CG1   . VAL A 1 89  ? -4.149  6.106   -9.232  1.00 56.21  ? 37  VAL A CG1   1 
ATOM   596  C  CG2   . VAL A 1 89  ? -1.784  5.787   -9.980  1.00 56.24  ? 37  VAL A CG2   1 
ATOM   597  N  N     . VAL A 1 90  ? -5.103  8.550   -10.785 1.00 59.85  ? 38  VAL A N     1 
ATOM   598  C  CA    . VAL A 1 90  ? -6.429  9.142   -10.703 1.00 65.82  ? 38  VAL A CA    1 
ATOM   599  C  C     . VAL A 1 90  ? -7.394  8.081   -10.180 1.00 68.73  ? 38  VAL A C     1 
ATOM   600  O  O     . VAL A 1 90  ? -7.787  7.175   -10.921 1.00 69.13  ? 38  VAL A O     1 
ATOM   601  C  CB    . VAL A 1 90  ? -6.873  9.694   -12.060 1.00 60.84  ? 38  VAL A CB    1 
ATOM   602  C  CG1   . VAL A 1 90  ? -8.255  10.320  -11.940 1.00 64.79  ? 38  VAL A CG1   1 
ATOM   603  C  CG2   . VAL A 1 90  ? -5.845  10.713  -12.565 1.00 59.02  ? 38  VAL A CG2   1 
ATOM   604  N  N     . TYR A 1 91  ? -7.782  8.188   -8.904  1.00 63.52  ? 39  TYR A N     1 
ATOM   605  C  CA    . TYR A 1 91  ? -8.697  7.226   -8.295  1.00 69.42  ? 39  TYR A CA    1 
ATOM   606  C  C     . TYR A 1 91  ? -10.140 7.665   -8.501  1.00 75.09  ? 39  TYR A C     1 
ATOM   607  O  O     . TYR A 1 91  ? -10.502 8.799   -8.170  1.00 77.06  ? 39  TYR A O     1 
ATOM   608  C  CB    . TYR A 1 91  ? -8.428  7.066   -6.795  1.00 72.36  ? 39  TYR A CB    1 
ATOM   609  C  CG    . TYR A 1 91  ? -9.586  6.433   -6.046  1.00 71.67  ? 39  TYR A CG    1 
ATOM   610  C  CD1   . TYR A 1 91  ? -9.877  5.084   -6.193  1.00 75.24  ? 39  TYR A CD1   1 
ATOM   611  C  CD2   . TYR A 1 91  ? -10.400 7.186   -5.211  1.00 75.38  ? 39  TYR A CD2   1 
ATOM   612  C  CE1   . TYR A 1 91  ? -10.938 4.493   -5.521  1.00 72.25  ? 39  TYR A CE1   1 
ATOM   613  C  CE2   . TYR A 1 91  ? -11.473 6.604   -4.539  1.00 81.14  ? 39  TYR A CE2   1 
ATOM   614  C  CZ    . TYR A 1 91  ? -11.732 5.253   -4.701  1.00 78.28  ? 39  TYR A CZ    1 
ATOM   615  O  OH    . TYR A 1 91  ? -12.788 4.658   -4.041  1.00 85.37  ? 39  TYR A OH    1 
ATOM   616  N  N     . ARG A 1 92  ? -10.965 6.754   -9.017  1.00 75.72  ? 40  ARG A N     1 
ATOM   617  C  CA    . ARG A 1 92  ? -12.386 7.003   -9.232  1.00 82.22  ? 40  ARG A CA    1 
ATOM   618  C  C     . ARG A 1 92  ? -13.210 6.002   -8.432  1.00 81.91  ? 40  ARG A C     1 
ATOM   619  O  O     . ARG A 1 92  ? -13.034 4.784   -8.578  1.00 75.13  ? 40  ARG A O     1 
ATOM   620  C  CB    . ARG A 1 92  ? -12.746 6.918   -10.719 1.00 86.46  ? 40  ARG A CB    1 
ATOM   621  C  CG    . ARG A 1 92  ? -11.596 7.214   -11.668 1.00 82.81  ? 40  ARG A CG    1 
ATOM   622  C  CD    . ARG A 1 92  ? -12.088 7.185   -13.093 1.00 74.94  ? 40  ARG A CD    1 
ATOM   623  N  NE    . ARG A 1 92  ? -13.160 8.156   -13.258 1.00 83.83  ? 40  ARG A NE    1 
ATOM   624  C  CZ    . ARG A 1 92  ? -14.114 8.065   -14.175 1.00 89.35  ? 40  ARG A CZ    1 
ATOM   625  N  NH1   . ARG A 1 92  ? -14.126 7.036   -15.019 1.00 84.06  ? 40  ARG A NH1   1 
ATOM   626  N  NH2   . ARG A 1 92  ? -15.052 9.005   -14.249 1.00 91.41  ? 40  ARG A NH2   1 
ATOM   627  N  N     . ALA A 1 93  ? -14.128 6.524   -7.615  1.00 86.61  ? 41  ALA A N     1 
ATOM   628  C  CA    . ALA A 1 93  ? -14.850 5.708   -6.645  1.00 91.44  ? 41  ALA A CA    1 
ATOM   629  C  C     . ALA A 1 93  ? -15.808 4.734   -7.327  1.00 90.82  ? 41  ALA A C     1 
ATOM   630  O  O     . ALA A 1 93  ? -16.418 5.050   -8.352  1.00 92.10  ? 41  ALA A O     1 
ATOM   631  C  CB    . ALA A 1 93  ? -15.617 6.610   -5.670  1.00 89.31  ? 41  ALA A CB    1 
ATOM   632  N  N     . SER A 1 94  ? -15.945 3.545   -6.742  1.00 87.04  ? 42  SER A N     1 
ATOM   633  C  CA    . SER A 1 94  ? -16.847 2.523   -7.267  1.00 89.97  ? 42  SER A CA    1 
ATOM   634  C  C     . SER A 1 94  ? -18.182 2.548   -6.524  1.00 90.07  ? 42  SER A C     1 
ATOM   635  O  O     . SER A 1 94  ? -19.207 2.953   -7.075  1.00 95.03  ? 42  SER A O     1 
ATOM   636  C  CB    . SER A 1 94  ? -16.214 1.125   -7.167  1.00 89.61  ? 42  SER A CB    1 
ATOM   637  O  OG    . SER A 1 94  ? -14.813 1.149   -7.400  1.00 84.08  ? 42  SER A OG    1 
ATOM   638  N  N     . ALA A 1 99  ? -21.058 1.993   -11.461 1.00 94.39  ? 43  ALA A N     1 
ATOM   639  C  CA    . ALA A 1 99  ? -22.050 2.765   -10.720 1.00 97.12  ? 43  ALA A CA    1 
ATOM   640  C  C     . ALA A 1 99  ? -21.825 4.282   -10.848 1.00 105.68 ? 43  ALA A C     1 
ATOM   641  O  O     . ALA A 1 99  ? -22.575 4.970   -11.551 1.00 101.47 ? 43  ALA A O     1 
ATOM   642  C  CB    . ALA A 1 99  ? -22.046 2.350   -9.251  1.00 100.13 ? 43  ALA A CB    1 
ATOM   643  N  N     . THR A 1 100 ? -20.800 4.793   -10.173 1.00 105.76 ? 44  THR A N     1 
ATOM   644  C  CA    . THR A 1 100 ? -20.545 6.233   -10.093 1.00 101.48 ? 44  THR A CA    1 
ATOM   645  C  C     . THR A 1 100 ? -19.039 6.450   -10.233 1.00 103.70 ? 44  THR A C     1 
ATOM   646  O  O     . THR A 1 100 ? -18.318 5.606   -10.778 1.00 105.49 ? 44  THR A O     1 
ATOM   647  C  CB    . THR A 1 100 ? -21.142 6.800   -8.789  1.00 102.05 ? 44  THR A CB    1 
ATOM   648  O  OG1   . THR A 1 100 ? -21.081 8.232   -8.800  1.00 104.18 ? 44  THR A OG1   1 
ATOM   649  C  CG2   . THR A 1 100 ? -20.408 6.256   -7.554  1.00 99.94  ? 44  THR A CG2   1 
ATOM   650  N  N     . GLY A 1 101 ? -18.546 7.603   -9.765  1.00 102.11 ? 45  GLY A N     1 
ATOM   651  C  CA    . GLY A 1 101 ? -17.112 7.835   -9.691  1.00 95.76  ? 45  GLY A CA    1 
ATOM   652  C  C     . GLY A 1 101 ? -16.575 9.121   -10.299 1.00 94.94  ? 45  GLY A C     1 
ATOM   653  O  O     . GLY A 1 101 ? -16.678 9.344   -11.514 1.00 94.88  ? 45  GLY A O     1 
ATOM   654  N  N     . ARG A 1 102 ? -15.974 9.961   -9.453  1.00 90.95  ? 46  ARG A N     1 
ATOM   655  C  CA    . ARG A 1 102 ? -15.309 11.195  -9.863  1.00 90.57  ? 46  ARG A CA    1 
ATOM   656  C  C     . ARG A 1 102 ? -13.820 11.095  -9.560  1.00 86.95  ? 46  ARG A C     1 
ATOM   657  O  O     . ARG A 1 102 ? -13.424 10.656  -8.474  1.00 90.64  ? 46  ARG A O     1 
ATOM   658  C  CB    . ARG A 1 102 ? -15.896 12.421  -9.152  1.00 86.65  ? 46  ARG A CB    1 
ATOM   659  N  N     . GLY A 1 103 ? -12.999 11.515  -10.521 1.00 90.81  ? 47  GLY A N     1 
ATOM   660  C  CA    . GLY A 1 103 ? -11.566 11.321  -10.434 1.00 82.97  ? 47  GLY A CA    1 
ATOM   661  C  C     . GLY A 1 103 ? -10.869 12.156  -9.382  1.00 78.12  ? 47  GLY A C     1 
ATOM   662  O  O     . GLY A 1 103 ? -10.704 13.366  -9.558  1.00 78.00  ? 47  GLY A O     1 
ATOM   663  N  N     . GLN A 1 104 ? -10.466 11.522  -8.280  1.00 80.42  ? 48  GLN A N     1 
ATOM   664  C  CA    . GLN A 1 104 ? -9.582  12.144  -7.304  1.00 82.07  ? 48  GLN A CA    1 
ATOM   665  C  C     . GLN A 1 104 ? -8.132  11.822  -7.650  1.00 72.53  ? 48  GLN A C     1 
ATOM   666  O  O     . GLN A 1 104 ? -7.819  10.723  -8.121  1.00 67.79  ? 48  GLN A O     1 
ATOM   667  C  CB    . GLN A 1 104 ? -9.908  11.686  -5.871  1.00 81.55  ? 48  GLN A CB    1 
ATOM   668  C  CG    . GLN A 1 104 ? -11.229 12.235  -5.321  1.00 83.84  ? 48  GLN A CG    1 
ATOM   669  C  CD    . GLN A 1 104 ? -11.947 11.290  -4.377  1.00 84.54  ? 48  GLN A CD    1 
ATOM   670  O  OE1   . GLN A 1 104 ? -11.918 11.482  -3.160  1.00 92.49  ? 48  GLN A OE1   1 
ATOM   671  N  NE2   . GLN A 1 104 ? -12.611 10.273  -4.934  1.00 85.26  ? 48  GLN A NE2   1 
ATOM   672  N  N     . ARG A 1 105 ? -7.255  12.796  -7.422  1.00 72.62  ? 49  ARG A N     1 
ATOM   673  C  CA    . ARG A 1 105 ? -5.834  12.671  -7.725  1.00 70.85  ? 49  ARG A CA    1 
ATOM   674  C  C     . ARG A 1 105 ? -5.126  12.125  -6.495  1.00 67.88  ? 49  ARG A C     1 
ATOM   675  O  O     . ARG A 1 105 ? -5.023  12.814  -5.480  1.00 74.44  ? 49  ARG A O     1 
ATOM   676  C  CB    . ARG A 1 105 ? -5.247  14.019  -8.133  1.00 75.93  ? 49  ARG A CB    1 
ATOM   677  C  CG    . ARG A 1 105 ? -4.339  13.973  -9.358  1.00 72.30  ? 49  ARG A CG    1 
ATOM   678  C  CD    . ARG A 1 105 ? -3.696  15.334  -9.612  1.00 78.94  ? 49  ARG A CD    1 
ATOM   679  N  NE    . ARG A 1 105 ? -4.565  16.432  -9.187  1.00 82.47  ? 49  ARG A NE    1 
ATOM   680  C  CZ    . ARG A 1 105 ? -4.179  17.699  -9.064  1.00 81.41  ? 49  ARG A CZ    1 
ATOM   681  N  NH1   . ARG A 1 105 ? -2.929  18.052  -9.339  1.00 82.50  ? 49  ARG A NH1   1 
ATOM   682  N  NH2   . ARG A 1 105 ? -5.049  18.614  -8.665  1.00 79.24  ? 49  ARG A NH2   1 
ATOM   683  N  N     . ILE A 1 106 ? -4.630  10.894  -6.589  1.00 65.32  ? 50  ILE A N     1 
ATOM   684  C  CA    . ILE A 1 106 ? -3.981  10.204  -5.482  1.00 59.84  ? 50  ILE A CA    1 
ATOM   685  C  C     . ILE A 1 106 ? -2.482  10.183  -5.739  1.00 57.28  ? 50  ILE A C     1 
ATOM   686  O  O     . ILE A 1 106 ? -2.036  9.774   -6.814  1.00 62.01  ? 50  ILE A O     1 
ATOM   687  C  CB    . ILE A 1 106 ? -4.519  8.773   -5.320  1.00 57.18  ? 50  ILE A CB    1 
ATOM   688  C  CG1   . ILE A 1 106 ? -5.942  8.781   -4.758  1.00 57.76  ? 50  ILE A CG1   1 
ATOM   689  C  CG2   . ILE A 1 106 ? -3.590  7.955   -4.426  1.00 60.53  ? 50  ILE A CG2   1 
ATOM   690  C  CD1   . ILE A 1 106 ? -6.104  9.626   -3.493  1.00 73.51  ? 50  ILE A CD1   1 
ATOM   691  N  N     . HIS A 1 107 ? -1.710  10.618  -4.759  1.00 64.90  ? 51  HIS A N     1 
ATOM   692  C  CA    . HIS A 1 107 ? -0.260  10.468  -4.770  1.00 61.84  ? 51  HIS A CA    1 
ATOM   693  C  C     . HIS A 1 107 ? 0.086   9.241   -3.933  1.00 63.50  ? 51  HIS A C     1 
ATOM   694  O  O     . HIS A 1 107 ? -0.062  9.255   -2.703  1.00 66.38  ? 51  HIS A O     1 
ATOM   695  C  CB    . HIS A 1 107 ? 0.420   11.719  -4.223  1.00 66.02  ? 51  HIS A CB    1 
ATOM   696  C  CG    . HIS A 1 107 ? 1.909   11.694  -4.337  1.00 64.69  ? 51  HIS A CG    1 
ATOM   697  N  ND1   . HIS A 1 107 ? 2.594   10.637  -4.895  1.00 64.08  ? 51  HIS A ND1   1 
ATOM   698  C  CD2   . HIS A 1 107 ? 2.846   12.600  -3.973  1.00 71.68  ? 51  HIS A CD2   1 
ATOM   699  C  CE1   . HIS A 1 107 ? 3.891   10.890  -4.867  1.00 63.80  ? 51  HIS A CE1   1 
ATOM   700  N  NE2   . HIS A 1 107 ? 4.070   12.078  -4.320  1.00 65.88  ? 51  HIS A NE2   1 
ATOM   701  N  N     . LEU A 1 108 ? 0.545   8.185   -4.598  1.00 59.00  ? 52  LEU A N     1 
ATOM   702  C  CA    . LEU A 1 108 ? 0.850   6.919   -3.942  1.00 58.49  ? 52  LEU A CA    1 
ATOM   703  C  C     . LEU A 1 108 ? 2.321   6.843   -3.551  1.00 56.98  ? 52  LEU A C     1 
ATOM   704  O  O     . LEU A 1 108 ? 3.205   7.145   -4.363  1.00 56.46  ? 52  LEU A O     1 
ATOM   705  C  CB    . LEU A 1 108 ? 0.507   5.753   -4.862  1.00 58.72  ? 52  LEU A CB    1 
ATOM   706  C  CG    . LEU A 1 108 ? -0.967  5.395   -4.938  1.00 65.01  ? 52  LEU A CG    1 
ATOM   707  C  CD1   . LEU A 1 108 ? -1.156  4.241   -5.930  1.00 52.85  ? 52  LEU A CD1   1 
ATOM   708  C  CD2   . LEU A 1 108 ? -1.492  5.067   -3.527  1.00 63.05  ? 52  LEU A CD2   1 
ATOM   709  N  N     . GLN A 1 109 ? 2.574   6.448   -2.305  1.00 57.07  ? 53  GLN A N     1 
ATOM   710  C  CA    . GLN A 1 109 ? 3.899   6.048   -1.849  1.00 54.51  ? 53  GLN A CA    1 
ATOM   711  C  C     . GLN A 1 109 ? 3.828   4.542   -1.646  1.00 51.85  ? 53  GLN A C     1 
ATOM   712  O  O     . GLN A 1 109 ? 3.021   4.067   -0.839  1.00 52.01  ? 53  GLN A O     1 
ATOM   713  C  CB    . GLN A 1 109 ? 4.302   6.778   -0.559  1.00 55.36  ? 53  GLN A CB    1 
ATOM   714  C  CG    . GLN A 1 109 ? 5.636   6.310   0.054   1.00 53.57  ? 53  GLN A CG    1 
ATOM   715  C  CD    . GLN A 1 109 ? 6.147   7.185   1.226   1.00 49.98  ? 53  GLN A CD    1 
ATOM   716  O  OE1   . GLN A 1 109 ? 5.377   7.894   1.885   1.00 48.38  ? 53  GLN A OE1   1 
ATOM   717  N  NE2   . GLN A 1 109 ? 7.463   7.150   1.458   1.00 43.01  ? 53  GLN A NE2   1 
ATOM   718  N  N     . LEU A 1 110 ? 4.633   3.797   -2.408  1.00 49.91  ? 54  LEU A N     1 
ATOM   719  C  CA    . LEU A 1 110 ? 4.598   2.329   -2.427  1.00 46.87  ? 54  LEU A CA    1 
ATOM   720  C  C     . LEU A 1 110 ? 5.796   1.801   -1.639  1.00 49.29  ? 54  LEU A C     1 
ATOM   721  O  O     . LEU A 1 110 ? 6.894   1.637   -2.176  1.00 48.63  ? 54  LEU A O     1 
ATOM   722  C  CB    . LEU A 1 110 ? 4.618   1.795   -3.854  1.00 59.13  ? 54  LEU A CB    1 
ATOM   723  C  CG    . LEU A 1 110 ? 3.781   2.510   -4.917  1.00 56.62  ? 54  LEU A CG    1 
ATOM   724  C  CD1   . LEU A 1 110 ? 3.694   1.668   -6.168  1.00 51.48  ? 54  LEU A CD1   1 
ATOM   725  C  CD2   . LEU A 1 110 ? 2.402   2.764   -4.371  1.00 56.23  ? 54  LEU A CD2   1 
ATOM   726  N  N     . TRP A 1 111 ? 5.577   1.531   -0.355  1.00 50.97  ? 55  TRP A N     1 
ATOM   727  C  CA    . TRP A 1 111 ? 6.656   1.052   0.492   1.00 49.98  ? 55  TRP A CA    1 
ATOM   728  C  C     . TRP A 1 111 ? 7.002   -0.385  0.145   1.00 44.14  ? 55  TRP A C     1 
ATOM   729  O  O     . TRP A 1 111 ? 6.117   -1.225  -0.004  1.00 45.44  ? 55  TRP A O     1 
ATOM   730  C  CB    . TRP A 1 111 ? 6.257   1.155   1.957   1.00 48.27  ? 55  TRP A CB    1 
ATOM   731  C  CG    . TRP A 1 111 ? 6.466   2.513   2.549   1.00 42.16  ? 55  TRP A CG    1 
ATOM   732  C  CD1   . TRP A 1 111 ? 5.503   3.390   2.921   1.00 44.08  ? 55  TRP A CD1   1 
ATOM   733  C  CD2   . TRP A 1 111 ? 7.720   3.133   2.859   1.00 37.68  ? 55  TRP A CD2   1 
ATOM   734  N  NE1   . TRP A 1 111 ? 6.071   4.525   3.443   1.00 45.22  ? 55  TRP A NE1   1 
ATOM   735  C  CE2   . TRP A 1 111 ? 7.434   4.396   3.409   1.00 39.58  ? 55  TRP A CE2   1 
ATOM   736  C  CE3   . TRP A 1 111 ? 9.054   2.741   2.726   1.00 39.11  ? 55  TRP A CE3   1 
ATOM   737  C  CZ2   . TRP A 1 111 ? 8.434   5.278   3.835   1.00 41.00  ? 55  TRP A CZ2   1 
ATOM   738  C  CZ3   . TRP A 1 111 ? 10.049  3.619   3.147   1.00 44.29  ? 55  TRP A CZ3   1 
ATOM   739  C  CH2   . TRP A 1 111 ? 9.730   4.873   3.696   1.00 42.06  ? 55  TRP A CH2   1 
ATOM   740  N  N     . ASP A 1 112 ? 8.300   -0.672  0.053   1.00 45.72  ? 56  ASP A N     1 
ATOM   741  C  CA    . ASP A 1 112 ? 8.824   -1.910  -0.535  1.00 51.10  ? 56  ASP A CA    1 
ATOM   742  C  C     . ASP A 1 112 ? 9.808   -2.532  0.448   1.00 51.62  ? 56  ASP A C     1 
ATOM   743  O  O     . ASP A 1 112 ? 11.013  -2.286  0.332   1.00 57.22  ? 56  ASP A O     1 
ATOM   744  C  CB    . ASP A 1 112 ? 9.500   -1.588  -1.875  1.00 54.16  ? 56  ASP A CB    1 
ATOM   745  C  CG    . ASP A 1 112 ? 10.090  -2.805  -2.555  1.00 54.54  ? 56  ASP A CG    1 
ATOM   746  O  OD1   . ASP A 1 112 ? 9.628   -3.938  -2.255  1.00 52.26  ? 56  ASP A OD1   1 
ATOM   747  O  OD2   . ASP A 1 112 ? 11.020  -2.611  -3.392  1.00 52.55  ? 56  ASP A OD2   1 
ATOM   748  N  N     . THR A 1 113 ? 9.317   -3.331  1.397   1.00 47.36  ? 57  THR A N     1 
ATOM   749  C  CA    . THR A 1 113 ? 10.190  -3.853  2.445   1.00 48.38  ? 57  THR A CA    1 
ATOM   750  C  C     . THR A 1 113 ? 11.021  -5.022  1.942   1.00 48.01  ? 57  THR A C     1 
ATOM   751  O  O     . THR A 1 113 ? 10.608  -5.772  1.047   1.00 52.48  ? 57  THR A O     1 
ATOM   752  C  CB    . THR A 1 113 ? 9.394   -4.311  3.666   1.00 48.63  ? 57  THR A CB    1 
ATOM   753  O  OG1   . THR A 1 113 ? 8.555   -5.418  3.306   1.00 50.03  ? 57  THR A OG1   1 
ATOM   754  C  CG2   . THR A 1 113 ? 8.554   -3.167  4.242   1.00 42.47  ? 57  THR A CG2   1 
ATOM   755  N  N     . ALA A 1 114 ? 12.206  -5.176  2.527   1.00 45.39  ? 58  ALA A N     1 
ATOM   756  C  CA    . ALA A 1 114 ? 12.977  -6.376  2.264   1.00 48.57  ? 58  ALA A CA    1 
ATOM   757  C  C     . ALA A 1 114 ? 12.319  -7.554  2.976   1.00 50.00  ? 58  ALA A C     1 
ATOM   758  O  O     . ALA A 1 114 ? 11.441  -7.382  3.820   1.00 49.96  ? 58  ALA A O     1 
ATOM   759  C  CB    . ALA A 1 114 ? 14.417  -6.202  2.720   1.00 49.39  ? 58  ALA A CB    1 
ATOM   760  N  N     . GLY A 1 115 ? 12.718  -8.763  2.606   1.00 48.69  ? 59  GLY A N     1 
ATOM   761  C  CA    . GLY A 1 115 ? 12.066  -9.921  3.192   1.00 49.50  ? 59  GLY A CA    1 
ATOM   762  C  C     . GLY A 1 115 ? 12.966  -10.717 4.107   1.00 45.53  ? 59  GLY A C     1 
ATOM   763  O  O     . GLY A 1 115 ? 12.496  -11.553 4.878   1.00 43.43  ? 59  GLY A O     1 
ATOM   764  N  N     . LEU A 1 116 ? 14.267  -10.463 4.017   1.00 48.47  ? 60  LEU A N     1 
ATOM   765  C  CA    . LEU A 1 116 ? 15.232  -11.156 4.854   1.00 53.09  ? 60  LEU A CA    1 
ATOM   766  C  C     . LEU A 1 116 ? 14.971  -10.826 6.320   1.00 56.55  ? 60  LEU A C     1 
ATOM   767  O  O     . LEU A 1 116 ? 14.789  -9.660  6.683   1.00 53.84  ? 60  LEU A O     1 
ATOM   768  C  CB    . LEU A 1 116 ? 16.657  -10.773 4.439   1.00 54.70  ? 60  LEU A CB    1 
ATOM   769  C  CG    . LEU A 1 116 ? 17.004  -11.245 3.013   1.00 46.75  ? 60  LEU A CG    1 
ATOM   770  C  CD1   . LEU A 1 116 ? 18.328  -10.704 2.485   1.00 40.40  ? 60  LEU A CD1   1 
ATOM   771  C  CD2   . LEU A 1 116 ? 16.996  -12.758 2.971   1.00 47.17  ? 60  LEU A CD2   1 
ATOM   772  N  N     . GLU A 1 117 ? 14.911  -11.868 7.158   1.00 62.08  ? 61  GLU A N     1 
ATOM   773  C  CA    . GLU A 1 117 ? 14.640  -11.683 8.581   1.00 60.72  ? 61  GLU A CA    1 
ATOM   774  C  C     . GLU A 1 117 ? 15.624  -10.707 9.219   1.00 61.37  ? 61  GLU A C     1 
ATOM   775  O  O     . GLU A 1 117 ? 15.292  -10.087 10.237  1.00 56.49  ? 61  GLU A O     1 
ATOM   776  C  CB    . GLU A 1 117 ? 14.657  -13.049 9.292   1.00 59.05  ? 61  GLU A CB    1 
ATOM   777  C  CG    . GLU A 1 117 ? 14.410  -13.049 10.826  1.00 77.85  ? 61  GLU A CG    1 
ATOM   778  C  CD    . GLU A 1 117 ? 13.026  -13.610 11.265  1.00 81.84  ? 61  GLU A CD    1 
ATOM   779  O  OE1   . GLU A 1 117 ? 12.503  -14.540 10.592  1.00 85.89  ? 61  GLU A OE1   1 
ATOM   780  O  OE2   . GLU A 1 117 ? 12.494  -13.152 12.322  1.00 70.93  ? 61  GLU A OE2   1 
ATOM   781  N  N     . ARG A 1 118 ? 16.794  -10.502 8.600   1.00 57.90  ? 62  ARG A N     1 
ATOM   782  C  CA    . ARG A 1 118 ? 17.823  -9.642  9.167   1.00 57.01  ? 62  ARG A CA    1 
ATOM   783  C  C     . ARG A 1 118 ? 17.528  -8.159  8.985   1.00 57.77  ? 62  ARG A C     1 
ATOM   784  O  O     . ARG A 1 118 ? 18.290  -7.327  9.489   1.00 59.51  ? 62  ARG A O     1 
ATOM   785  C  CB    . ARG A 1 118 ? 19.191  -10.007 8.579   1.00 62.93  ? 62  ARG A CB    1 
ATOM   786  C  CG    . ARG A 1 118 ? 19.732  -9.138  7.468   1.00 64.33  ? 62  ARG A CG    1 
ATOM   787  C  CD    . ARG A 1 118 ? 21.094  -9.667  7.091   1.00 71.46  ? 62  ARG A CD    1 
ATOM   788  N  NE    . ARG A 1 118 ? 21.704  -8.953  5.977   1.00 77.83  ? 62  ARG A NE    1 
ATOM   789  C  CZ    . ARG A 1 118 ? 22.489  -7.894  6.118   1.00 75.84  ? 62  ARG A CZ    1 
ATOM   790  N  NH1   . ARG A 1 118 ? 22.747  -7.417  7.331   1.00 73.51  ? 62  ARG A NH1   1 
ATOM   791  N  NH2   . ARG A 1 118 ? 23.012  -7.319  5.046   1.00 72.15  ? 62  ARG A NH2   1 
ATOM   792  N  N     . PHE A 1 119 ? 16.446  -7.815  8.286   1.00 59.85  ? 63  PHE A N     1 
ATOM   793  C  CA    . PHE A 1 119 ? 15.903  -6.462  8.259   1.00 56.02  ? 63  PHE A CA    1 
ATOM   794  C  C     . PHE A 1 119 ? 14.552  -6.371  8.951   1.00 56.81  ? 63  PHE A C     1 
ATOM   795  O  O     . PHE A 1 119 ? 13.885  -5.341  8.831   1.00 52.84  ? 63  PHE A O     1 
ATOM   796  C  CB    . PHE A 1 119 ? 15.731  -5.960  6.826   1.00 52.20  ? 63  PHE A CB    1 
ATOM   797  C  CG    . PHE A 1 119 ? 16.981  -5.987  6.000   1.00 58.11  ? 63  PHE A CG    1 
ATOM   798  C  CD1   . PHE A 1 119 ? 17.939  -4.992  6.131   1.00 55.83  ? 63  PHE A CD1   1 
ATOM   799  C  CD2   . PHE A 1 119 ? 17.181  -6.987  5.054   1.00 54.77  ? 63  PHE A CD2   1 
ATOM   800  C  CE1   . PHE A 1 119 ? 19.081  -5.001  5.345   1.00 55.30  ? 63  PHE A CE1   1 
ATOM   801  C  CE2   . PHE A 1 119 ? 18.327  -7.005  4.280   1.00 52.33  ? 63  PHE A CE2   1 
ATOM   802  C  CZ    . PHE A 1 119 ? 19.278  -6.008  4.427   1.00 52.19  ? 63  PHE A CZ    1 
ATOM   803  N  N     . ARG A 1 120 ? 14.118  -7.429  9.653   1.00 59.84  ? 64  ARG A N     1 
ATOM   804  C  CA    . ARG A 1 120 ? 12.702  -7.534  10.008  1.00 54.70  ? 64  ARG A CA    1 
ATOM   805  C  C     . ARG A 1 120 ? 12.276  -6.417  10.946  1.00 57.72  ? 64  ARG A C     1 
ATOM   806  O  O     . ARG A 1 120 ? 11.156  -5.908  10.843  1.00 57.77  ? 64  ARG A O     1 
ATOM   807  C  CB    . ARG A 1 120 ? 12.392  -8.888  10.635  1.00 54.21  ? 64  ARG A CB    1 
ATOM   808  C  CG    . ARG A 1 120 ? 10.912  -9.037  10.925  1.00 57.95  ? 64  ARG A CG    1 
ATOM   809  C  CD    . ARG A 1 120 ? 10.133  -9.356  9.667   1.00 52.38  ? 64  ARG A CD    1 
ATOM   810  N  NE    . ARG A 1 120 ? 10.176  -10.797 9.426   1.00 62.24  ? 64  ARG A NE    1 
ATOM   811  C  CZ    . ARG A 1 120 ? 10.952  -11.383 8.518   1.00 58.61  ? 64  ARG A CZ    1 
ATOM   812  N  NH1   . ARG A 1 120 ? 11.733  -10.644 7.738   1.00 56.61  ? 64  ARG A NH1   1 
ATOM   813  N  NH2   . ARG A 1 120 ? 10.933  -12.705 8.381   1.00 60.82  ? 64  ARG A NH2   1 
ATOM   814  N  N     . SER A 1 121 ? 13.146  -6.035  11.882  1.00 61.91  ? 65  SER A N     1 
ATOM   815  C  CA    . SER A 1 121 ? 12.880  -4.876  12.727  1.00 56.79  ? 65  SER A CA    1 
ATOM   816  C  C     . SER A 1 121 ? 12.644  -3.635  11.875  1.00 58.88  ? 65  SER A C     1 
ATOM   817  O  O     . SER A 1 121 ? 11.606  -2.965  11.985  1.00 56.86  ? 65  SER A O     1 
ATOM   818  C  CB    . SER A 1 121 ? 14.060  -4.646  13.661  1.00 58.84  ? 65  SER A CB    1 
ATOM   819  O  OG    . SER A 1 121 ? 15.135  -4.096  12.911  1.00 63.94  ? 65  SER A OG    1 
ATOM   820  N  N     . LEU A 1 122 ? 13.608  -3.324  11.005  1.00 59.94  ? 66  LEU A N     1 
ATOM   821  C  CA    . LEU A 1 122 ? 13.496  -2.136  10.170  1.00 57.52  ? 66  LEU A CA    1 
ATOM   822  C  C     . LEU A 1 122 ? 12.221  -2.150  9.337   1.00 55.71  ? 66  LEU A C     1 
ATOM   823  O  O     . LEU A 1 122 ? 11.505  -1.148  9.278   1.00 61.50  ? 66  LEU A O     1 
ATOM   824  C  CB    . LEU A 1 122 ? 14.722  -2.008  9.276   1.00 57.65  ? 66  LEU A CB    1 
ATOM   825  C  CG    . LEU A 1 122 ? 14.879  -0.650  8.614   1.00 59.12  ? 66  LEU A CG    1 
ATOM   826  C  CD1   . LEU A 1 122 ? 16.304  -0.142  8.811   1.00 55.54  ? 66  LEU A CD1   1 
ATOM   827  C  CD2   . LEU A 1 122 ? 14.508  -0.774  7.141   1.00 57.24  ? 66  LEU A CD2   1 
ATOM   828  N  N     . THR A 1 123 ? 11.898  -3.270  8.696   1.00 54.65  ? 67  THR A N     1 
ATOM   829  C  CA    . THR A 1 123 ? 10.685  -3.236  7.890   1.00 54.08  ? 67  THR A CA    1 
ATOM   830  C  C     . THR A 1 123 ? 9.435   -3.156  8.762   1.00 53.15  ? 67  THR A C     1 
ATOM   831  O  O     . THR A 1 123 ? 8.468   -2.481  8.379   1.00 46.20  ? 67  THR A O     1 
ATOM   832  C  CB    . THR A 1 123 ? 10.637  -4.428  6.930   1.00 54.74  ? 67  THR A CB    1 
ATOM   833  O  OG1   . THR A 1 123 ? 10.026  -5.571  7.547   1.00 56.10  ? 67  THR A OG1   1 
ATOM   834  C  CG2   . THR A 1 123 ? 12.040  -4.766  6.460   1.00 54.42  ? 67  THR A CG2   1 
ATOM   835  N  N     . THR A 1 124 ? 9.454   -3.781  9.956   1.00 57.74  ? 68  THR A N     1 
ATOM   836  C  CA    . THR A 1 124 ? 8.293   -3.704  10.841  1.00 52.34  ? 68  THR A CA    1 
ATOM   837  C  C     . THR A 1 124 ? 8.085   -2.297  11.362  1.00 53.60  ? 68  THR A C     1 
ATOM   838  O  O     . THR A 1 124 ? 6.946   -1.908  11.641  1.00 53.47  ? 68  THR A O     1 
ATOM   839  C  CB    . THR A 1 124 ? 8.410   -4.646  12.031  1.00 51.84  ? 68  THR A CB    1 
ATOM   840  O  OG1   . THR A 1 124 ? 9.061   -5.866  11.657  1.00 50.69  ? 68  THR A OG1   1 
ATOM   841  C  CG2   . THR A 1 124 ? 7.019   -4.985  12.514  1.00 55.67  ? 68  THR A CG2   1 
ATOM   842  N  N     . ALA A 1 125 ? 9.164   -1.518  11.479  1.00 54.49  ? 69  ALA A N     1 
ATOM   843  C  CA    . ALA A 1 125 ? 9.058   -0.126  11.900  1.00 50.94  ? 69  ALA A CA    1 
ATOM   844  C  C     . ALA A 1 125 ? 8.260   0.733   10.931  1.00 56.86  ? 69  ALA A C     1 
ATOM   845  O  O     . ALA A 1 125 ? 8.002   1.900   11.242  1.00 70.69  ? 69  ALA A O     1 
ATOM   846  C  CB    . ALA A 1 125 ? 10.455  0.475   12.071  1.00 50.12  ? 69  ALA A CB    1 
ATOM   847  N  N     . PHE A 1 126 ? 7.887   0.213   9.763   1.00 59.10  ? 70  PHE A N     1 
ATOM   848  C  CA    . PHE A 1 126 ? 7.200   1.005   8.760   1.00 53.02  ? 70  PHE A CA    1 
ATOM   849  C  C     . PHE A 1 126 ? 5.744   0.621   8.567   1.00 57.24  ? 70  PHE A C     1 
ATOM   850  O  O     . PHE A 1 126 ? 5.017   1.365   7.900   1.00 60.11  ? 70  PHE A O     1 
ATOM   851  C  CB    . PHE A 1 126 ? 7.963   0.924   7.433   1.00 54.13  ? 70  PHE A CB    1 
ATOM   852  C  CG    . PHE A 1 126 ? 9.119   1.876   7.387   1.00 55.24  ? 70  PHE A CG    1 
ATOM   853  C  CD1   . PHE A 1 126 ? 10.414  1.426   7.607   1.00 47.89  ? 70  PHE A CD1   1 
ATOM   854  C  CD2   . PHE A 1 126 ? 8.895   3.247   7.205   1.00 50.78  ? 70  PHE A CD2   1 
ATOM   855  C  CE1   . PHE A 1 126 ? 11.468  2.311   7.614   1.00 48.98  ? 70  PHE A CE1   1 
ATOM   856  C  CE2   . PHE A 1 126 ? 9.943   4.143   7.211   1.00 48.55  ? 70  PHE A CE2   1 
ATOM   857  C  CZ    . PHE A 1 126 ? 11.231  3.677   7.421   1.00 50.72  ? 70  PHE A CZ    1 
ATOM   858  N  N     . PHE A 1 127 ? 5.299   -0.502  9.145   1.00 57.08  ? 71  PHE A N     1 
ATOM   859  C  CA    . PHE A 1 127 ? 3.881   -0.824  9.181   1.00 52.63  ? 71  PHE A CA    1 
ATOM   860  C  C     . PHE A 1 127 ? 3.082   0.328   9.766   1.00 59.45  ? 71  PHE A C     1 
ATOM   861  O  O     . PHE A 1 127 ? 1.889   0.455   9.486   1.00 68.49  ? 71  PHE A O     1 
ATOM   862  C  CB    . PHE A 1 127 ? 3.620   -2.080  10.019  1.00 58.47  ? 71  PHE A CB    1 
ATOM   863  C  CG    . PHE A 1 127 ? 4.315   -3.346  9.526   1.00 56.98  ? 71  PHE A CG    1 
ATOM   864  C  CD1   . PHE A 1 127 ? 5.345   -3.313  8.586   1.00 57.64  ? 71  PHE A CD1   1 
ATOM   865  C  CD2   . PHE A 1 127 ? 3.921   -4.584  10.022  1.00 50.42  ? 71  PHE A CD2   1 
ATOM   866  C  CE1   . PHE A 1 127 ? 5.959   -4.495  8.169   1.00 58.63  ? 71  PHE A CE1   1 
ATOM   867  C  CE2   . PHE A 1 127 ? 4.530   -5.745  9.616   1.00 48.93  ? 71  PHE A CE2   1 
ATOM   868  C  CZ    . PHE A 1 127 ? 5.545   -5.709  8.690   1.00 56.62  ? 71  PHE A CZ    1 
ATOM   869  N  N     . ARG A 1 128 ? 3.721   1.152   10.596  1.00 60.42  ? 72  ARG A N     1 
ATOM   870  C  CA    . ARG A 1 128 ? 3.123   2.402   11.061  1.00 65.37  ? 72  ARG A CA    1 
ATOM   871  C  C     . ARG A 1 128 ? 2.707   3.280   9.899   1.00 66.38  ? 72  ARG A C     1 
ATOM   872  O  O     . ARG A 1 128 ? 1.531   3.661   9.770   1.00 68.75  ? 72  ARG A O     1 
ATOM   873  C  CB    . ARG A 1 128 ? 4.121   3.156   11.948  1.00 66.22  ? 72  ARG A CB    1 
ATOM   874  C  CG    . ARG A 1 128 ? 4.573   2.367   13.172  1.00 68.16  ? 72  ARG A CG    1 
ATOM   875  C  CD    . ARG A 1 128 ? 5.678   1.406   12.927  1.00 65.23  ? 72  ARG A CD    1 
ATOM   876  N  NE    . ARG A 1 128 ? 5.791   0.441   14.012  1.00 64.88  ? 72  ARG A NE    1 
ATOM   877  C  CZ    . ARG A 1 128 ? 5.836   0.746   15.301  1.00 65.63  ? 72  ARG A CZ    1 
ATOM   878  N  NH1   . ARG A 1 128 ? 5.928   -0.240  16.179  1.00 69.34  ? 72  ARG A NH1   1 
ATOM   879  N  NH2   . ARG A 1 128 ? 5.777   2.013   15.713  1.00 72.59  ? 72  ARG A NH2   1 
ATOM   880  N  N     . ASP A 1 129 ? 3.675   3.640   9.049   1.00 66.76  ? 73  ASP A N     1 
ATOM   881  C  CA    . ASP A 1 129 ? 3.511   4.573   7.939   1.00 68.02  ? 73  ASP A CA    1 
ATOM   882  C  C     . ASP A 1 129 ? 2.552   4.078   6.860   1.00 64.68  ? 73  ASP A C     1 
ATOM   883  O  O     . ASP A 1 129 ? 2.300   4.816   5.903   1.00 69.00  ? 73  ASP A O     1 
ATOM   884  C  CB    . ASP A 1 129 ? 4.871   4.881   7.299   1.00 60.43  ? 73  ASP A CB    1 
ATOM   885  C  CG    . ASP A 1 129 ? 4.875   6.207   6.547   1.00 62.65  ? 73  ASP A CG    1 
ATOM   886  O  OD1   . ASP A 1 129 ? 4.459   7.218   7.146   1.00 67.64  ? 73  ASP A OD1   1 
ATOM   887  O  OD2   . ASP A 1 129 ? 5.288   6.241   5.363   1.00 57.35  ? 73  ASP A OD2   1 
ATOM   888  N  N     . ALA A 1 130 ? 2.002   2.878   6.983   1.00 63.22  ? 74  ALA A N     1 
ATOM   889  C  CA    . ALA A 1 130 ? 1.195   2.270   5.937   1.00 58.89  ? 74  ALA A CA    1 
ATOM   890  C  C     . ALA A 1 130 ? -0.291  2.469   6.198   1.00 54.27  ? 74  ALA A C     1 
ATOM   891  O  O     . ALA A 1 130 ? -0.738  2.533   7.341   1.00 63.87  ? 74  ALA A O     1 
ATOM   892  C  CB    . ALA A 1 130 ? 1.500   0.777   5.835   1.00 58.63  ? 74  ALA A CB    1 
ATOM   893  N  N     . MET A 1 131 ? -1.052  2.582   5.117   1.00 50.42  ? 75  MET A N     1 
ATOM   894  C  CA    . MET A 1 131 ? -2.504  2.582   5.179   1.00 51.29  ? 75  MET A CA    1 
ATOM   895  C  C     . MET A 1 131 ? -3.094  1.269   4.722   1.00 54.07  ? 75  MET A C     1 
ATOM   896  O  O     . MET A 1 131 ? -4.275  1.012   4.974   1.00 59.46  ? 75  MET A O     1 
ATOM   897  C  CB    . MET A 1 131 ? -3.092  3.688   4.302   1.00 55.80  ? 75  MET A CB    1 
ATOM   898  C  CG    . MET A 1 131 ? -3.380  4.967   5.003   1.00 62.79  ? 75  MET A CG    1 
ATOM   899  S  SD    . MET A 1 131 ? -3.247  6.316   3.823   1.00 59.10  ? 75  MET A SD    1 
ATOM   900  C  CE    . MET A 1 131 ? -1.568  6.828   4.178   1.00 62.55  ? 75  MET A CE    1 
ATOM   901  N  N     . GLY A 1 132 ? -2.305  0.459   4.029   1.00 53.22  ? 76  GLY A N     1 
ATOM   902  C  CA    . GLY A 1 132 ? -2.746  -0.831  3.546   1.00 49.97  ? 76  GLY A CA    1 
ATOM   903  C  C     . GLY A 1 132 ? -1.520  -1.648  3.225   1.00 51.53  ? 76  GLY A C     1 
ATOM   904  O  O     . GLY A 1 132 ? -0.396  -1.141  3.166   1.00 49.46  ? 76  GLY A O     1 
ATOM   905  N  N     . PHE A 1 133 ? -1.751  -2.934  3.019   1.00 53.48  ? 77  PHE A N     1 
ATOM   906  C  CA    . PHE A 1 133 ? -0.662  -3.864  2.799   1.00 50.41  ? 77  PHE A CA    1 
ATOM   907  C  C     . PHE A 1 133 ? -0.987  -4.742  1.607   1.00 53.30  ? 77  PHE A C     1 
ATOM   908  O  O     . PHE A 1 133 ? -2.135  -5.159  1.407   1.00 55.16  ? 77  PHE A O     1 
ATOM   909  C  CB    . PHE A 1 133 ? -0.399  -4.697  4.063   1.00 53.45  ? 77  PHE A CB    1 
ATOM   910  C  CG    . PHE A 1 133 ? -0.270  -3.852  5.302   1.00 55.39  ? 77  PHE A CG    1 
ATOM   911  C  CD1   . PHE A 1 133 ? 0.942   -3.269  5.630   1.00 54.46  ? 77  PHE A CD1   1 
ATOM   912  C  CD2   . PHE A 1 133 ? -1.368  -3.584  6.094   1.00 55.53  ? 77  PHE A CD2   1 
ATOM   913  C  CE1   . PHE A 1 133 ? 1.063   -2.481  6.747   1.00 53.62  ? 77  PHE A CE1   1 
ATOM   914  C  CE2   . PHE A 1 133 ? -1.248  -2.779  7.204   1.00 56.54  ? 77  PHE A CE2   1 
ATOM   915  C  CZ    . PHE A 1 133 ? -0.034  -2.231  7.531   1.00 56.71  ? 77  PHE A CZ    1 
ATOM   916  N  N     . LEU A 1 134 ? 0.024   -4.945  0.786   1.00 48.29  ? 78  LEU A N     1 
ATOM   917  C  CA    . LEU A 1 134 ? 0.028   -5.960  -0.241  1.00 45.50  ? 78  LEU A CA    1 
ATOM   918  C  C     . LEU A 1 134 ? 0.858   -7.081  0.362   1.00 46.75  ? 78  LEU A C     1 
ATOM   919  O  O     . LEU A 1 134 ? 2.087   -6.985  0.422   1.00 43.73  ? 78  LEU A O     1 
ATOM   920  C  CB    . LEU A 1 134 ? 0.637   -5.396  -1.518  1.00 56.17  ? 78  LEU A CB    1 
ATOM   921  C  CG    . LEU A 1 134 ? 0.035   -5.571  -2.918  1.00 58.21  ? 78  LEU A CG    1 
ATOM   922  C  CD1   . LEU A 1 134 ? -1.491  -5.515  -2.930  1.00 51.25  ? 78  LEU A CD1   1 
ATOM   923  C  CD2   . LEU A 1 134 ? 0.612   -4.469  -3.814  1.00 54.73  ? 78  LEU A CD2   1 
ATOM   924  N  N     . LEU A 1 135 ? 0.189   -8.105  0.889   1.00 50.29  ? 79  LEU A N     1 
ATOM   925  C  CA    . LEU A 1 135 ? 0.891   -9.266  1.419   1.00 48.55  ? 79  LEU A CA    1 
ATOM   926  C  C     . LEU A 1 135 ? 1.120   -10.224 0.264   1.00 50.36  ? 79  LEU A C     1 
ATOM   927  O  O     . LEU A 1 135 ? 0.165   -10.630 -0.412  1.00 53.24  ? 79  LEU A O     1 
ATOM   928  C  CB    . LEU A 1 135 ? 0.114   -9.944  2.544   1.00 41.89  ? 79  LEU A CB    1 
ATOM   929  C  CG    . LEU A 1 135 ? 0.722   -11.226 3.148   1.00 46.80  ? 79  LEU A CG    1 
ATOM   930  C  CD1   . LEU A 1 135 ? 2.264   -11.287 3.200   1.00 46.55  ? 79  LEU A CD1   1 
ATOM   931  C  CD2   . LEU A 1 135 ? 0.175   -11.419 4.539   1.00 57.94  ? 79  LEU A CD2   1 
ATOM   932  N  N     . LEU A 1 136 ? 2.381   -10.571 0.029   1.00 46.00  ? 80  LEU A N     1 
ATOM   933  C  CA    . LEU A 1 136 ? 2.767   -11.383 -1.109  1.00 48.91  ? 80  LEU A CA    1 
ATOM   934  C  C     . LEU A 1 136 ? 3.371   -12.706 -0.677  1.00 48.91  ? 80  LEU A C     1 
ATOM   935  O  O     . LEU A 1 136 ? 3.996   -12.811 0.383   1.00 52.50  ? 80  LEU A O     1 
ATOM   936  C  CB    . LEU A 1 136 ? 3.779   -10.656 -1.996  1.00 51.91  ? 80  LEU A CB    1 
ATOM   937  C  CG    . LEU A 1 136 ? 3.190   -9.703  -3.027  1.00 46.72  ? 80  LEU A CG    1 
ATOM   938  C  CD1   . LEU A 1 136 ? 3.008   -8.297  -2.451  1.00 53.29  ? 80  LEU A CD1   1 
ATOM   939  C  CD2   . LEU A 1 136 ? 4.103   -9.695  -4.254  1.00 50.09  ? 80  LEU A CD2   1 
ATOM   940  N  N     . PHE A 1 137 ? 3.199   -13.703 -1.548  1.00 57.28  ? 81  PHE A N     1 
ATOM   941  C  CA    . PHE A 1 137 ? 3.921   -14.968 -1.512  1.00 50.62  ? 81  PHE A CA    1 
ATOM   942  C  C     . PHE A 1 137 ? 4.146   -15.458 -2.942  1.00 54.61  ? 81  PHE A C     1 
ATOM   943  O  O     . PHE A 1 137 ? 3.643   -14.874 -3.913  1.00 54.00  ? 81  PHE A O     1 
ATOM   944  C  CB    . PHE A 1 137 ? 3.158   -16.011 -0.705  1.00 49.01  ? 81  PHE A CB    1 
ATOM   945  C  CG    . PHE A 1 137 ? 1.863   -16.415 -1.327  1.00 50.47  ? 81  PHE A CG    1 
ATOM   946  C  CD1   . PHE A 1 137 ? 0.711   -15.682 -1.087  1.00 47.02  ? 81  PHE A CD1   1 
ATOM   947  C  CD2   . PHE A 1 137 ? 1.797   -17.528 -2.164  1.00 51.73  ? 81  PHE A CD2   1 
ATOM   948  C  CE1   . PHE A 1 137 ? -0.487  -16.062 -1.650  1.00 48.84  ? 81  PHE A CE1   1 
ATOM   949  C  CE2   . PHE A 1 137 ? 0.606   -17.908 -2.735  1.00 49.68  ? 81  PHE A CE2   1 
ATOM   950  C  CZ    . PHE A 1 137 ? -0.542  -17.169 -2.482  1.00 51.49  ? 81  PHE A CZ    1 
ATOM   951  N  N     . ASP A 1 138 ? 4.870   -16.572 -3.057  1.00 53.35  ? 82  ASP A N     1 
ATOM   952  C  CA    . ASP A 1 138 ? 5.332   -17.132 -4.323  1.00 45.92  ? 82  ASP A CA    1 
ATOM   953  C  C     . ASP A 1 138 ? 4.484   -18.342 -4.699  1.00 50.01  ? 82  ASP A C     1 
ATOM   954  O  O     . ASP A 1 138 ? 4.497   -19.355 -3.995  1.00 55.16  ? 82  ASP A O     1 
ATOM   955  C  CB    . ASP A 1 138 ? 6.802   -17.530 -4.200  1.00 48.98  ? 82  ASP A CB    1 
ATOM   956  C  CG    . ASP A 1 138 ? 7.560   -17.428 -5.505  1.00 52.06  ? 82  ASP A CG    1 
ATOM   957  O  OD1   . ASP A 1 138 ? 6.974   -17.756 -6.566  1.00 56.34  ? 82  ASP A OD1   1 
ATOM   958  O  OD2   . ASP A 1 138 ? 8.752   -17.027 -5.465  1.00 50.64  ? 82  ASP A OD2   1 
ATOM   959  N  N     . LEU A 1 139 ? 3.771   -18.252 -5.824  1.00 59.36  ? 83  LEU A N     1 
ATOM   960  C  CA    . LEU A 1 139 ? 3.039   -19.406 -6.345  1.00 53.78  ? 83  LEU A CA    1 
ATOM   961  C  C     . LEU A 1 139 ? 3.958   -20.585 -6.632  1.00 55.45  ? 83  LEU A C     1 
ATOM   962  O  O     . LEU A 1 139 ? 3.479   -21.719 -6.721  1.00 54.47  ? 83  LEU A O     1 
ATOM   963  C  CB    . LEU A 1 139 ? 2.284   -19.034 -7.630  1.00 51.62  ? 83  LEU A CB    1 
ATOM   964  C  CG    . LEU A 1 139 ? 1.002   -18.195 -7.542  1.00 52.57  ? 83  LEU A CG    1 
ATOM   965  C  CD1   . LEU A 1 139 ? 0.386   -18.009 -8.910  1.00 52.87  ? 83  LEU A CD1   1 
ATOM   966  C  CD2   . LEU A 1 139 ? -0.014  -18.812 -6.608  1.00 50.45  ? 83  LEU A CD2   1 
ATOM   967  N  N     . THR A 1 140 ? 5.260   -20.344 -6.785  1.00 57.27  ? 84  THR A N     1 
ATOM   968  C  CA    . THR A 1 140 ? 6.242   -21.391 -7.039  1.00 56.70  ? 84  THR A CA    1 
ATOM   969  C  C     . THR A 1 140 ? 7.028   -21.785 -5.786  1.00 56.04  ? 84  THR A C     1 
ATOM   970  O  O     . THR A 1 140 ? 7.939   -22.610 -5.874  1.00 57.34  ? 84  THR A O     1 
ATOM   971  C  CB    . THR A 1 140 ? 7.191   -20.935 -8.155  1.00 57.87  ? 84  THR A CB    1 
ATOM   972  O  OG1   . THR A 1 140 ? 7.966   -19.805 -7.717  1.00 55.89  ? 84  THR A OG1   1 
ATOM   973  C  CG2   . THR A 1 140 ? 6.381   -20.517 -9.378  1.00 56.74  ? 84  THR A CG2   1 
ATOM   974  N  N     . ASN A 1 141 ? 6.699   -21.213 -4.624  1.00 59.56  ? 85  ASN A N     1 
ATOM   975  C  CA    . ASN A 1 141 ? 7.370   -21.524 -3.358  1.00 63.61  ? 85  ASN A CA    1 
ATOM   976  C  C     . ASN A 1 141 ? 6.320   -21.836 -2.297  1.00 59.25  ? 85  ASN A C     1 
ATOM   977  O  O     . ASN A 1 141 ? 5.580   -20.944 -1.869  1.00 50.30  ? 85  ASN A O     1 
ATOM   978  C  CB    . ASN A 1 141 ? 8.274   -20.374 -2.903  1.00 55.74  ? 85  ASN A CB    1 
ATOM   979  C  CG    . ASN A 1 141 ? 9.235   -20.789 -1.815  1.00 56.79  ? 85  ASN A CG    1 
ATOM   980  O  OD1   . ASN A 1 141 ? 8.849   -21.445 -0.845  1.00 52.61  ? 85  ASN A OD1   1 
ATOM   981  N  ND2   . ASN A 1 141 ? 10.503  -20.421 -1.976  1.00 60.64  ? 85  ASN A ND2   1 
ATOM   982  N  N     . GLU A 1 142 ? 6.274   -23.104 -1.868  1.00 64.25  ? 86  GLU A N     1 
ATOM   983  C  CA    . GLU A 1 142 ? 5.292   -23.537 -0.876  1.00 65.06  ? 86  GLU A CA    1 
ATOM   984  C  C     . GLU A 1 142 ? 5.544   -22.865 0.475   1.00 60.07  ? 86  GLU A C     1 
ATOM   985  O  O     . GLU A 1 142 ? 4.617   -22.349 1.116   1.00 49.82  ? 86  GLU A O     1 
ATOM   986  C  CB    . GLU A 1 142 ? 5.331   -25.069 -0.761  1.00 64.62  ? 86  GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 142 ? 4.467   -25.676 0.353   1.00 65.87  ? 86  GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 142 ? 3.058   -26.000 -0.118  1.00 74.72  ? 86  GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 142 ? 2.908   -26.843 -1.038  1.00 77.57  ? 86  GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 142 ? 2.099   -25.408 0.436   1.00 71.13  ? 86  GLU A OE2   1 
ATOM   991  N  N     . GLN A 1 143 ? 6.806   -22.833 0.901   1.00 59.72  ? 87  GLN A N     1 
ATOM   992  C  CA    . GLN A 1 143 ? 7.140   -22.296 2.213   1.00 56.30  ? 87  GLN A CA    1 
ATOM   993  C  C     . GLN A 1 143 ? 6.650   -20.858 2.359   1.00 55.51  ? 87  GLN A C     1 
ATOM   994  O  O     . GLN A 1 143 ? 6.024   -20.510 3.366   1.00 65.08  ? 87  GLN A O     1 
ATOM   995  C  CB    . GLN A 1 143 ? 8.651   -22.402 2.446   1.00 55.56  ? 87  GLN A CB    1 
ATOM   996  C  CG    . GLN A 1 143 ? 9.086   -22.044 3.840   1.00 61.05  ? 87  GLN A CG    1 
ATOM   997  C  CD    . GLN A 1 143 ? 8.368   -22.862 4.891   1.00 65.51  ? 87  GLN A CD    1 
ATOM   998  O  OE1   . GLN A 1 143 ? 8.754   -24.000 5.181   1.00 69.57  ? 87  GLN A OE1   1 
ATOM   999  N  NE2   . GLN A 1 143 ? 7.301   -22.296 5.456   1.00 59.68  ? 87  GLN A NE2   1 
ATOM   1000 N  N     . SER A 1 144 ? 6.907   -20.009 1.358   1.00 50.70  ? 88  SER A N     1 
ATOM   1001 C  CA    . SER A 1 144 ? 6.434   -18.626 1.431   1.00 48.32  ? 88  SER A CA    1 
ATOM   1002 C  C     . SER A 1 144 ? 4.920   -18.544 1.510   1.00 49.33  ? 88  SER A C     1 
ATOM   1003 O  O     . SER A 1 144 ? 4.380   -17.510 1.913   1.00 47.38  ? 88  SER A O     1 
ATOM   1004 C  CB    . SER A 1 144 ? 6.888   -17.810 0.218   1.00 51.85  ? 88  SER A CB    1 
ATOM   1005 O  OG    . SER A 1 144 ? 6.159   -18.172 -0.954  1.00 52.29  ? 88  SER A OG    1 
ATOM   1006 N  N     . PHE A 1 145 ? 4.215   -19.590 1.092   1.00 55.42  ? 89  PHE A N     1 
ATOM   1007 C  CA    . PHE A 1 145 ? 2.766   -19.565 1.227   1.00 54.11  ? 89  PHE A CA    1 
ATOM   1008 C  C     . PHE A 1 145 ? 2.383   -19.729 2.685   1.00 56.60  ? 89  PHE A C     1 
ATOM   1009 O  O     . PHE A 1 145 ? 1.568   -18.968 3.221   1.00 57.60  ? 89  PHE A O     1 
ATOM   1010 C  CB    . PHE A 1 145 ? 2.132   -20.665 0.372   1.00 51.11  ? 89  PHE A CB    1 
ATOM   1011 C  CG    . PHE A 1 145 ? 0.678   -20.915 0.679   1.00 53.23  ? 89  PHE A CG    1 
ATOM   1012 C  CD1   . PHE A 1 145 ? -0.249  -19.866 0.683   1.00 53.37  ? 89  PHE A CD1   1 
ATOM   1013 C  CD2   . PHE A 1 145 ? 0.231   -22.200 0.952   1.00 50.49  ? 89  PHE A CD2   1 
ATOM   1014 C  CE1   . PHE A 1 145 ? -1.599  -20.105 0.967   1.00 52.34  ? 89  PHE A CE1   1 
ATOM   1015 C  CE2   . PHE A 1 145 ? -1.110  -22.439 1.230   1.00 56.51  ? 89  PHE A CE2   1 
ATOM   1016 C  CZ    . PHE A 1 145 ? -2.024  -21.391 1.238   1.00 53.23  ? 89  PHE A CZ    1 
ATOM   1017 N  N     . LEU A 1 146 ? 2.988   -20.716 3.345   1.00 54.41  ? 90  LEU A N     1 
ATOM   1018 C  CA    . LEU A 1 146 ? 2.657   -20.998 4.727   1.00 53.46  ? 90  LEU A CA    1 
ATOM   1019 C  C     . LEU A 1 146 ? 3.105   -19.872 5.639   1.00 59.12  ? 90  LEU A C     1 
ATOM   1020 O  O     . LEU A 1 146 ? 2.438   -19.597 6.646   1.00 66.68  ? 90  LEU A O     1 
ATOM   1021 C  CB    . LEU A 1 146 ? 3.283   -22.327 5.145   1.00 57.19  ? 90  LEU A CB    1 
ATOM   1022 C  CG    . LEU A 1 146 ? 2.769   -23.541 4.366   1.00 47.74  ? 90  LEU A CG    1 
ATOM   1023 C  CD1   . LEU A 1 146 ? 3.663   -24.755 4.582   1.00 43.56  ? 90  LEU A CD1   1 
ATOM   1024 C  CD2   . LEU A 1 146 ? 1.304   -23.844 4.701   1.00 42.95  ? 90  LEU A CD2   1 
ATOM   1025 N  N     . ASN A 1 147 ? 4.207   -19.192 5.294   1.00 53.15  ? 91  ASN A N     1 
ATOM   1026 C  CA    . ASN A 1 147 ? 4.677   -18.091 6.129   1.00 55.36  ? 91  ASN A CA    1 
ATOM   1027 C  C     . ASN A 1 147 ? 3.674   -16.948 6.181   1.00 53.93  ? 91  ASN A C     1 
ATOM   1028 O  O     . ASN A 1 147 ? 3.705   -16.161 7.130   1.00 60.25  ? 91  ASN A O     1 
ATOM   1029 C  CB    . ASN A 1 147 ? 6.028   -17.576 5.631   1.00 55.35  ? 91  ASN A CB    1 
ATOM   1030 C  CG    . ASN A 1 147 ? 7.157   -18.545 5.913   1.00 60.20  ? 91  ASN A CG    1 
ATOM   1031 O  OD1   . ASN A 1 147 ? 6.938   -19.605 6.484   1.00 58.45  ? 91  ASN A OD1   1 
ATOM   1032 N  ND2   . ASN A 1 147 ? 8.375   -18.182 5.516   1.00 63.07  ? 91  ASN A ND2   1 
ATOM   1033 N  N     . VAL A 1 148 ? 2.784   -16.853 5.193   1.00 46.64  ? 92  VAL A N     1 
ATOM   1034 C  CA    . VAL A 1 148 ? 1.808   -15.766 5.148   1.00 56.44  ? 92  VAL A CA    1 
ATOM   1035 C  C     . VAL A 1 148 ? 1.077   -15.656 6.478   1.00 61.47  ? 92  VAL A C     1 
ATOM   1036 O  O     . VAL A 1 148 ? 0.912   -14.560 7.031   1.00 57.90  ? 92  VAL A O     1 
ATOM   1037 C  CB    . VAL A 1 148 ? 0.820   -15.981 3.985   1.00 59.15  ? 92  VAL A CB    1 
ATOM   1038 C  CG1   . VAL A 1 148 ? -0.410  -15.095 4.157   1.00 58.75  ? 92  VAL A CG1   1 
ATOM   1039 C  CG2   . VAL A 1 148 ? 1.501   -15.724 2.646   1.00 49.99  ? 92  VAL A CG2   1 
ATOM   1040 N  N     . ARG A 1 149 ? 0.639   -16.803 7.011   1.00 68.43  ? 93  ARG A N     1 
ATOM   1041 C  CA    . ARG A 1 149 ? 0.005   -16.870 8.325   1.00 65.15  ? 93  ARG A CA    1 
ATOM   1042 C  C     . ARG A 1 149 ? 0.739   -15.997 9.330   1.00 61.73  ? 93  ARG A C     1 
ATOM   1043 O  O     . ARG A 1 149 ? 0.144   -15.125 9.974   1.00 61.78  ? 93  ARG A O     1 
ATOM   1044 C  CB    . ARG A 1 149 ? -0.019  -18.327 8.793   1.00 70.22  ? 93  ARG A CB    1 
ATOM   1045 C  CG    . ARG A 1 149 ? -1.407  -18.946 8.906   1.00 78.42  ? 93  ARG A CG    1 
ATOM   1046 C  CD    . ARG A 1 149 ? -1.469  -20.038 9.991   1.00 83.67  ? 93  ARG A CD    1 
ATOM   1047 N  NE    . ARG A 1 149 ? -0.190  -20.716 10.230  1.00 86.87  ? 93  ARG A NE    1 
ATOM   1048 C  CZ    . ARG A 1 149 ? 0.316   -21.679 9.459   1.00 96.03  ? 93  ARG A CZ    1 
ATOM   1049 N  NH1   . ARG A 1 149 ? -0.335  -22.091 8.370   1.00 85.10  ? 93  ARG A NH1   1 
ATOM   1050 N  NH2   . ARG A 1 149 ? 1.484   -22.229 9.775   1.00 99.01  ? 93  ARG A NH2   1 
ATOM   1051 N  N     . ASN A 1 150 ? 2.054   -16.203 9.438   1.00 60.15  ? 94  ASN A N     1 
ATOM   1052 C  CA    . ASN A 1 150 ? 2.876   -15.422 10.355  1.00 61.08  ? 94  ASN A CA    1 
ATOM   1053 C  C     . ASN A 1 150 ? 2.898   -13.944 9.955   1.00 59.52  ? 94  ASN A C     1 
ATOM   1054 O  O     . ASN A 1 150 ? 2.721   -13.063 10.806  1.00 58.61  ? 94  ASN A O     1 
ATOM   1055 C  CB    . ASN A 1 150 ? 4.277   -16.049 10.408  1.00 60.83  ? 94  ASN A CB    1 
ATOM   1056 C  CG    . ASN A 1 150 ? 5.363   -15.064 10.779  1.00 67.63  ? 94  ASN A CG    1 
ATOM   1057 O  OD1   . ASN A 1 150 ? 5.993   -14.460 9.902   1.00 68.87  ? 94  ASN A OD1   1 
ATOM   1058 N  ND2   . ASN A 1 150 ? 5.618   -14.917 12.085  1.00 68.51  ? 94  ASN A ND2   1 
ATOM   1059 N  N     . TRP A 1 151 ? 3.041   -13.658 8.654   1.00 60.90  ? 95  TRP A N     1 
ATOM   1060 C  CA    . TRP A 1 151 ? 3.068   -12.278 8.160   1.00 57.85  ? 95  TRP A CA    1 
ATOM   1061 C  C     . TRP A 1 151 ? 1.794   -11.513 8.492   1.00 56.62  ? 95  TRP A C     1 
ATOM   1062 O  O     . TRP A 1 151 ? 1.840   -10.292 8.706   1.00 56.72  ? 95  TRP A O     1 
ATOM   1063 C  CB    . TRP A 1 151 ? 3.260   -12.252 6.640   1.00 58.67  ? 95  TRP A CB    1 
ATOM   1064 C  CG    . TRP A 1 151 ? 4.650   -12.468 6.149   1.00 54.55  ? 95  TRP A CG    1 
ATOM   1065 C  CD1   . TRP A 1 151 ? 5.102   -13.518 5.383   1.00 49.02  ? 95  TRP A CD1   1 
ATOM   1066 C  CD2   . TRP A 1 151 ? 5.776   -11.609 6.358   1.00 53.54  ? 95  TRP A CD2   1 
ATOM   1067 N  NE1   . TRP A 1 151 ? 6.446   -13.363 5.113   1.00 48.16  ? 95  TRP A NE1   1 
ATOM   1068 C  CE2   . TRP A 1 151 ? 6.883   -12.198 5.695   1.00 53.15  ? 95  TRP A CE2   1 
ATOM   1069 C  CE3   . TRP A 1 151 ? 5.960   -10.402 7.037   1.00 49.90  ? 95  TRP A CE3   1 
ATOM   1070 C  CZ2   . TRP A 1 151 ? 8.155   -11.615 5.703   1.00 47.99  ? 95  TRP A CZ2   1 
ATOM   1071 C  CZ3   . TRP A 1 151 ? 7.213   -9.827  7.035   1.00 52.01  ? 95  TRP A CZ3   1 
ATOM   1072 C  CH2   . TRP A 1 151 ? 8.298   -10.433 6.370   1.00 45.67  ? 95  TRP A CH2   1 
ATOM   1073 N  N     . ILE A 1 152 ? 0.645   -12.189 8.489   1.00 57.18  ? 96  ILE A N     1 
ATOM   1074 C  CA    . ILE A 1 152 ? -0.597  -11.504 8.835   1.00 65.06  ? 96  ILE A CA    1 
ATOM   1075 C  C     . ILE A 1 152 ? -0.593  -11.099 10.303  1.00 62.94  ? 96  ILE A C     1 
ATOM   1076 O  O     . ILE A 1 152 ? -0.862  -9.942  10.637  1.00 62.36  ? 96  ILE A O     1 
ATOM   1077 C  CB    . ILE A 1 152 ? -1.821  -12.374 8.511   1.00 68.43  ? 96  ILE A CB    1 
ATOM   1078 C  CG1   . ILE A 1 152 ? -1.644  -13.100 7.192   1.00 62.81  ? 96  ILE A CG1   1 
ATOM   1079 C  CG2   . ILE A 1 152 ? -3.074  -11.503 8.457   1.00 73.88  ? 96  ILE A CG2   1 
ATOM   1080 C  CD1   . ILE A 1 152 ? -2.515  -14.324 7.091   1.00 68.09  ? 96  ILE A CD1   1 
ATOM   1081 N  N     . SER A 1 153 ? -0.306  -12.053 11.200  1.00 65.69  ? 97  SER A N     1 
ATOM   1082 C  CA    . SER A 1 153 ? -0.266  -11.742 12.627  1.00 66.42  ? 97  SER A CA    1 
ATOM   1083 C  C     . SER A 1 153 ? 0.747   -10.648 12.929  1.00 65.81  ? 97  SER A C     1 
ATOM   1084 O  O     . SER A 1 153 ? 0.533   -9.847  13.849  1.00 62.37  ? 97  SER A O     1 
ATOM   1085 C  CB    . SER A 1 153 ? 0.057   -12.992 13.438  1.00 63.84  ? 97  SER A CB    1 
ATOM   1086 O  OG    . SER A 1 153 ? 1.421   -13.331 13.273  1.00 66.41  ? 97  SER A OG    1 
ATOM   1087 N  N     . GLN A 1 154 ? 1.851   -10.596 12.170  1.00 62.47  ? 98  GLN A N     1 
ATOM   1088 C  CA    . GLN A 1 154 ? 2.778   -9.477  12.302  1.00 59.86  ? 98  GLN A CA    1 
ATOM   1089 C  C     . GLN A 1 154 ? 2.100   -8.172  11.924  1.00 58.34  ? 98  GLN A C     1 
ATOM   1090 O  O     . GLN A 1 154 ? 2.314   -7.140  12.565  1.00 64.94  ? 98  GLN A O     1 
ATOM   1091 C  CB    . GLN A 1 154 ? 4.016   -9.694  11.439  1.00 57.05  ? 98  GLN A CB    1 
ATOM   1092 C  CG    . GLN A 1 154 ? 5.124   -10.462 12.145  1.00 67.97  ? 98  GLN A CG    1 
ATOM   1093 C  CD    . GLN A 1 154 ? 6.481   -10.259 11.488  1.00 66.53  ? 98  GLN A CD    1 
ATOM   1094 O  OE1   . GLN A 1 154 ? 7.106   -9.202  11.651  1.00 67.61  ? 98  GLN A OE1   1 
ATOM   1095 N  NE2   . GLN A 1 154 ? 6.952   -11.276 10.750  1.00 51.66  ? 98  GLN A NE2   1 
ATOM   1096 N  N     . LEU A 1 155 ? 1.273   -8.195  10.889  1.00 59.73  ? 99  LEU A N     1 
ATOM   1097 C  CA    . LEU A 1 155 ? 0.513   -6.999  10.559  1.00 60.77  ? 99  LEU A CA    1 
ATOM   1098 C  C     . LEU A 1 155 ? -0.538  -6.713  11.616  1.00 58.19  ? 99  LEU A C     1 
ATOM   1099 O  O     . LEU A 1 155 ? -0.876  -5.549  11.850  1.00 65.31  ? 99  LEU A O     1 
ATOM   1100 C  CB    . LEU A 1 155 ? -0.134  -7.140  9.178   1.00 63.43  ? 99  LEU A CB    1 
ATOM   1101 C  CG    . LEU A 1 155 ? 0.900   -7.177  8.056   1.00 56.08  ? 99  LEU A CG    1 
ATOM   1102 C  CD1   . LEU A 1 155 ? 0.344   -7.867  6.826   1.00 64.89  ? 99  LEU A CD1   1 
ATOM   1103 C  CD2   . LEU A 1 155 ? 1.429   -5.799  7.729   1.00 52.56  ? 99  LEU A CD2   1 
ATOM   1104 N  N     . GLN A 1 156 ? -1.052  -7.753  12.274  1.00 62.23  ? 100 GLN A N     1 
ATOM   1105 C  CA    . GLN A 1 156 ? -1.964  -7.528  13.395  1.00 69.17  ? 100 GLN A CA    1 
ATOM   1106 C  C     . GLN A 1 156 ? -1.252  -6.829  14.558  1.00 71.47  ? 100 GLN A C     1 
ATOM   1107 O  O     . GLN A 1 156 ? -1.746  -5.828  15.094  1.00 67.84  ? 100 GLN A O     1 
ATOM   1108 C  CB    . GLN A 1 156 ? -2.599  -8.851  13.859  1.00 65.53  ? 100 GLN A CB    1 
ATOM   1109 C  CG    . GLN A 1 156 ? -3.024  -9.831  12.752  1.00 68.10  ? 100 GLN A CG    1 
ATOM   1110 C  CD    . GLN A 1 156 ? -4.515  -9.785  12.396  1.00 64.96  ? 100 GLN A CD    1 
ATOM   1111 O  OE1   . GLN A 1 156 ? -5.020  -8.755  11.933  1.00 56.16  ? 100 GLN A OE1   1 
ATOM   1112 N  NE2   . GLN A 1 156 ? -5.215  -10.924 12.572  1.00 51.93  ? 100 GLN A NE2   1 
ATOM   1113 N  N     . MET A 1 157 ? -0.070  -7.319  14.942  1.00 70.16  ? 101 MET A N     1 
ATOM   1114 C  CA    . MET A 1 157 ? 0.629   -6.741  16.081  1.00 65.95  ? 101 MET A CA    1 
ATOM   1115 C  C     . MET A 1 157 ? 1.180   -5.344  15.816  1.00 68.05  ? 101 MET A C     1 
ATOM   1116 O  O     . MET A 1 157 ? 1.502   -4.644  16.781  1.00 69.24  ? 101 MET A O     1 
ATOM   1117 C  CB    . MET A 1 157 ? 1.782   -7.637  16.515  1.00 63.17  ? 101 MET A CB    1 
ATOM   1118 C  CG    . MET A 1 157 ? 1.373   -9.022  16.926  1.00 69.74  ? 101 MET A CG    1 
ATOM   1119 S  SD    . MET A 1 157 ? 2.811   -10.107 16.944  1.00 84.93  ? 101 MET A SD    1 
ATOM   1120 C  CE    . MET A 1 157 ? 2.238   -11.402 18.054  1.00 67.46  ? 101 MET A CE    1 
ATOM   1121 N  N     . HIS A 1 158 ? 1.318   -4.911  14.557  1.00 63.52  ? 102 HIS A N     1 
ATOM   1122 C  CA    . HIS A 1 158 ? 2.091   -3.694  14.303  1.00 64.16  ? 102 HIS A CA    1 
ATOM   1123 C  C     . HIS A 1 158 ? 1.390   -2.598  13.510  1.00 59.77  ? 102 HIS A C     1 
ATOM   1124 O  O     . HIS A 1 158 ? 1.886   -1.464  13.511  1.00 59.27  ? 102 HIS A O     1 
ATOM   1125 C  CB    . HIS A 1 158 ? 3.411   -4.040  13.608  1.00 57.78  ? 102 HIS A CB    1 
ATOM   1126 C  CG    . HIS A 1 158 ? 4.367   -4.775  14.489  1.00 58.44  ? 102 HIS A CG    1 
ATOM   1127 N  ND1   . HIS A 1 158 ? 4.468   -6.150  14.491  1.00 62.28  ? 102 HIS A ND1   1 
ATOM   1128 C  CD2   . HIS A 1 158 ? 5.248   -4.331  15.417  1.00 55.86  ? 102 HIS A CD2   1 
ATOM   1129 C  CE1   . HIS A 1 158 ? 5.383   -6.523  15.370  1.00 59.87  ? 102 HIS A CE1   1 
ATOM   1130 N  NE2   . HIS A 1 158 ? 5.872   -5.438  15.944  1.00 55.93  ? 102 HIS A NE2   1 
ATOM   1131 N  N     . ALA A 1 159 ? 0.270   -2.869  12.851  1.00 61.09  ? 103 ALA A N     1 
ATOM   1132 C  CA    . ALA A 1 159 ? -0.425  -1.802  12.144  1.00 67.87  ? 103 ALA A CA    1 
ATOM   1133 C  C     . ALA A 1 159 ? -1.119  -0.891  13.152  1.00 63.48  ? 103 ALA A C     1 
ATOM   1134 O  O     . ALA A 1 159 ? -1.727  -1.367  14.111  1.00 65.59  ? 103 ALA A O     1 
ATOM   1135 C  CB    . ALA A 1 159 ? -1.428  -2.388  11.146  1.00 63.48  ? 103 ALA A CB    1 
ATOM   1136 N  N     . TYR A 1 160 ? -0.999  0.416   12.956  1.00 63.34  ? 104 TYR A N     1 
ATOM   1137 C  CA    . TYR A 1 160 ? -1.685  1.383   13.805  1.00 58.68  ? 104 TYR A CA    1 
ATOM   1138 C  C     . TYR A 1 160 ? -3.187  1.199   13.744  1.00 61.50  ? 104 TYR A C     1 
ATOM   1139 O  O     . TYR A 1 160 ? -3.936  1.954   14.357  1.00 64.24  ? 104 TYR A O     1 
ATOM   1140 C  CB    . TYR A 1 160 ? -1.354  2.806   13.387  1.00 68.05  ? 104 TYR A CB    1 
ATOM   1141 C  CG    . TYR A 1 160 ? -0.003  3.294   13.819  1.00 68.56  ? 104 TYR A CG    1 
ATOM   1142 C  CD1   . TYR A 1 160 ? 0.521   4.481   13.293  1.00 72.12  ? 104 TYR A CD1   1 
ATOM   1143 C  CD2   . TYR A 1 160 ? 0.754   2.581   14.748  1.00 62.45  ? 104 TYR A CD2   1 
ATOM   1144 C  CE1   . TYR A 1 160 ? 1.763   4.954   13.690  1.00 74.30  ? 104 TYR A CE1   1 
ATOM   1145 C  CE2   . TYR A 1 160 ? 1.996   3.036   15.153  1.00 64.71  ? 104 TYR A CE2   1 
ATOM   1146 C  CZ    . TYR A 1 160 ? 2.493   4.232   14.631  1.00 72.97  ? 104 TYR A CZ    1 
ATOM   1147 O  OH    . TYR A 1 160 ? 3.739   4.688   15.019  1.00 72.90  ? 104 TYR A OH    1 
ATOM   1148 N  N     . CYS A 1 161 ? -4.029  1.303   12.592  1.00 68.94  ? 105 CYS A N     1 
ATOM   1149 C  CA    . CYS A 1 161 ? -5.360  0.799   12.292  1.00 71.40  ? 105 CYS A CA    1 
ATOM   1150 C  C     . CYS A 1 161 ? -5.538  -0.466  13.134  1.00 71.26  ? 105 CYS A C     1 
ATOM   1151 O  O     . CYS A 1 161 ? -4.485  -1.154  13.309  1.00 70.36  ? 105 CYS A O     1 
ATOM   1152 C  CB    . CYS A 1 161 ? -5.505  0.471   10.794  1.00 73.41  ? 105 CYS A CB    1 
ATOM   1153 S  SG    . CYS A 1 161 ? -3.968  0.757   9.848   1.00 81.62  ? 105 CYS A SG    1 
ATOM   1154 N  N     . GLU A 1 162 ? -6.753  -0.882  13.776  1.00 70.78  ? 106 GLU A N     1 
ATOM   1155 C  CA    . GLU A 1 162 ? -6.483  -2.237  13.300  1.00 74.64  ? 106 GLU A CA    1 
ATOM   1156 C  C     . GLU A 1 162 ? -7.617  -2.797  12.449  1.00 80.38  ? 106 GLU A C     1 
ATOM   1157 O  O     . GLU A 1 162 ? -8.532  -2.069  12.066  1.00 85.35  ? 106 GLU A O     1 
ATOM   1158 C  CB    . GLU A 1 162 ? -6.176  -3.193  14.461  1.00 79.49  ? 106 GLU A CB    1 
ATOM   1159 C  CG    . GLU A 1 162 ? -5.126  -4.239  14.056  1.00 72.55  ? 106 GLU A CG    1 
ATOM   1160 C  CD    . GLU A 1 162 ? -5.729  -5.628  13.944  1.00 77.81  ? 106 GLU A CD    1 
ATOM   1161 O  OE1   . GLU A 1 162 ? -5.008  -6.560  13.552  1.00 74.08  ? 106 GLU A OE1   1 
ATOM   1162 O  OE2   . GLU A 1 162 ? -6.928  -5.797  14.264  1.00 82.52  ? 106 GLU A OE2   1 
ATOM   1163 N  N     . ASN A 1 163 ? -7.530  -4.100  12.164  1.00 76.72  ? 107 ASN A N     1 
ATOM   1164 C  CA    . ASN A 1 163 ? -8.099  -4.727  10.982  1.00 76.04  ? 107 ASN A CA    1 
ATOM   1165 C  C     . ASN A 1 163 ? -7.536  -4.005  9.764   1.00 77.35  ? 107 ASN A C     1 
ATOM   1166 O  O     . ASN A 1 163 ? -8.310  -3.523  8.928   1.00 78.61  ? 107 ASN A O     1 
ATOM   1167 C  CB    . ASN A 1 163 ? -9.627  -4.687  10.993  1.00 81.04  ? 107 ASN A CB    1 
ATOM   1168 C  CG    . ASN A 1 163 ? -10.233 -5.871  11.728  1.00 87.34  ? 107 ASN A CG    1 
ATOM   1169 O  OD1   . ASN A 1 163 ? -9.515  -6.722  12.261  1.00 86.19  ? 107 ASN A OD1   1 
ATOM   1170 N  ND2   . ASN A 1 163 ? -11.561 -5.936  11.754  1.00 87.80  ? 107 ASN A ND2   1 
ATOM   1171 N  N     . PRO A 1 164 ? -6.209  -3.920  9.624   1.00 73.43  ? 108 PRO A N     1 
ATOM   1172 C  CA    . PRO A 1 164 ? -5.653  -3.196  8.479   1.00 68.42  ? 108 PRO A CA    1 
ATOM   1173 C  C     . PRO A 1 164 ? -6.053  -3.887  7.194   1.00 66.29  ? 108 PRO A C     1 
ATOM   1174 O  O     . PRO A 1 164 ? -6.024  -5.115  7.103   1.00 68.78  ? 108 PRO A O     1 
ATOM   1175 C  CB    . PRO A 1 164 ? -4.146  -3.276  8.712   1.00 64.50  ? 108 PRO A CB    1 
ATOM   1176 C  CG    . PRO A 1 164 ? -3.965  -4.549  9.417   1.00 64.46  ? 108 PRO A CG    1 
ATOM   1177 C  CD    . PRO A 1 164 ? -5.160  -4.694  10.317  1.00 69.44  ? 108 PRO A CD    1 
ATOM   1178 N  N     . ASP A 1 165 ? -6.466  -3.094  6.214   1.00 70.02  ? 109 ASP A N     1 
ATOM   1179 C  CA    . ASP A 1 165 ? -6.813  -3.659  4.919   1.00 59.94  ? 109 ASP A CA    1 
ATOM   1180 C  C     . ASP A 1 165 ? -5.590  -4.316  4.307   1.00 57.38  ? 109 ASP A C     1 
ATOM   1181 O  O     . ASP A 1 165 ? -4.541  -3.681  4.156   1.00 52.88  ? 109 ASP A O     1 
ATOM   1182 C  CB    . ASP A 1 165 ? -7.359  -2.580  3.996   1.00 60.63  ? 109 ASP A CB    1 
ATOM   1183 C  CG    . ASP A 1 165 ? -8.405  -1.717  4.664   1.00 70.12  ? 109 ASP A CG    1 
ATOM   1184 O  OD1   . ASP A 1 165 ? -8.045  -0.614  5.127   1.00 74.40  ? 109 ASP A OD1   1 
ATOM   1185 O  OD2   . ASP A 1 165 ? -9.584  -2.142  4.736   1.00 72.38  ? 109 ASP A OD2   1 
ATOM   1186 N  N     . ILE A 1 166 ? -5.714  -5.598  3.987   1.00 56.88  ? 110 ILE A N     1 
ATOM   1187 C  CA    . ILE A 1 166 ? -4.646  -6.358  3.357   1.00 59.47  ? 110 ILE A CA    1 
ATOM   1188 C  C     . ILE A 1 166 ? -5.178  -6.933  2.052   1.00 61.30  ? 110 ILE A C     1 
ATOM   1189 O  O     . ILE A 1 166 ? -6.349  -7.315  1.962   1.00 66.97  ? 110 ILE A O     1 
ATOM   1190 C  CB    . ILE A 1 166 ? -4.124  -7.464  4.296   1.00 56.88  ? 110 ILE A CB    1 
ATOM   1191 C  CG1   . ILE A 1 166 ? -3.454  -6.820  5.508   1.00 61.03  ? 110 ILE A CG1   1 
ATOM   1192 C  CG2   . ILE A 1 166 ? -3.137  -8.386  3.574   1.00 55.33  ? 110 ILE A CG2   1 
ATOM   1193 C  CD1   . ILE A 1 166 ? -3.108  -7.812  6.616   1.00 62.54  ? 110 ILE A CD1   1 
ATOM   1194 N  N     . VAL A 1 167 ? -4.332  -6.943  1.029   1.00 57.34  ? 111 VAL A N     1 
ATOM   1195 C  CA    . VAL A 1 167 ? -4.615  -7.604  -0.238  1.00 52.30  ? 111 VAL A CA    1 
ATOM   1196 C  C     . VAL A 1 167 ? -3.567  -8.695  -0.427  1.00 52.35  ? 111 VAL A C     1 
ATOM   1197 O  O     . VAL A 1 167 ? -2.354  -8.422  -0.452  1.00 46.64  ? 111 VAL A O     1 
ATOM   1198 C  CB    . VAL A 1 167 ? -4.633  -6.612  -1.418  1.00 56.77  ? 111 VAL A CB    1 
ATOM   1199 C  CG1   . VAL A 1 167 ? -4.595  -7.326  -2.758  1.00 58.04  ? 111 VAL A CG1   1 
ATOM   1200 C  CG2   . VAL A 1 167 ? -5.887  -5.726  -1.352  1.00 55.34  ? 111 VAL A CG2   1 
ATOM   1201 N  N     . LEU A 1 168 ? -4.047  -9.931  -0.527  1.00 58.78  ? 112 LEU A N     1 
ATOM   1202 C  CA    . LEU A 1 168 ? -3.208  -11.117 -0.634  1.00 57.07  ? 112 LEU A CA    1 
ATOM   1203 C  C     . LEU A 1 168 ? -2.939  -11.404 -2.107  1.00 59.40  ? 112 LEU A C     1 
ATOM   1204 O  O     . LEU A 1 168 ? -3.884  -11.542 -2.896  1.00 61.30  ? 112 LEU A O     1 
ATOM   1205 C  CB    . LEU A 1 168 ? -3.905  -12.290 0.059   1.00 53.03  ? 112 LEU A CB    1 
ATOM   1206 C  CG    . LEU A 1 168 ? -3.563  -13.753 -0.247  1.00 55.12  ? 112 LEU A CG    1 
ATOM   1207 C  CD1   . LEU A 1 168 ? -2.280  -14.215 0.443   1.00 53.44  ? 112 LEU A CD1   1 
ATOM   1208 C  CD2   . LEU A 1 168 ? -4.744  -14.648 0.136   1.00 54.08  ? 112 LEU A CD2   1 
ATOM   1209 N  N     . CYS A 1 169 ? -1.656  -11.467 -2.481  1.00 52.50  ? 113 CYS A N     1 
ATOM   1210 C  CA    . CYS A 1 169 ? -1.249  -11.716 -3.858  1.00 53.11  ? 113 CYS A CA    1 
ATOM   1211 C  C     . CYS A 1 169 ? -0.383  -12.970 -3.980  1.00 55.95  ? 113 CYS A C     1 
ATOM   1212 O  O     . CYS A 1 169 ? 0.665   -13.085 -3.335  1.00 50.82  ? 113 CYS A O     1 
ATOM   1213 C  CB    . CYS A 1 169 ? -0.496  -10.533 -4.464  1.00 54.25  ? 113 CYS A CB    1 
ATOM   1214 S  SG    . CYS A 1 169 ? -1.161  -8.936  -4.241  1.00 65.10  ? 113 CYS A SG    1 
ATOM   1215 N  N     . GLY A 1 170 ? -0.834  -13.894 -4.826  1.00 56.82  ? 114 GLY A N     1 
ATOM   1216 C  CA    . GLY A 1 170 ? -0.014  -14.999 -5.295  1.00 56.01  ? 114 GLY A CA    1 
ATOM   1217 C  C     . GLY A 1 170 ? 0.791   -14.563 -6.502  1.00 55.96  ? 114 GLY A C     1 
ATOM   1218 O  O     . GLY A 1 170 ? 0.357   -14.687 -7.645  1.00 54.60  ? 114 GLY A O     1 
ATOM   1219 N  N     . ASN A 1 171 ? 1.961   -14.006 -6.248  1.00 60.09  ? 115 ASN A N     1 
ATOM   1220 C  CA    . ASN A 1 171 ? 2.805   -13.517 -7.318  1.00 48.96  ? 115 ASN A CA    1 
ATOM   1221 C  C     . ASN A 1 171 ? 3.384   -14.694 -8.095  1.00 52.70  ? 115 ASN A C     1 
ATOM   1222 O  O     . ASN A 1 171 ? 3.346   -15.847 -7.642  1.00 46.20  ? 115 ASN A O     1 
ATOM   1223 C  CB    . ASN A 1 171 ? 3.928   -12.655 -6.738  1.00 45.12  ? 115 ASN A CB    1 
ATOM   1224 C  CG    . ASN A 1 171 ? 4.719   -11.963 -7.792  1.00 50.10  ? 115 ASN A CG    1 
ATOM   1225 O  OD1   . ASN A 1 171 ? 4.146   -11.342 -8.684  1.00 54.57  ? 115 ASN A OD1   1 
ATOM   1226 N  ND2   . ASN A 1 171 ? 6.047   -12.092 -7.737  1.00 49.21  ? 115 ASN A ND2   1 
ATOM   1227 N  N     . LYS A 1 172 ? 3.919   -14.377 -9.284  1.00 48.22  ? 116 LYS A N     1 
ATOM   1228 C  CA    . LYS A 1 172 ? 4.629   -15.292 -10.174 1.00 47.15  ? 116 LYS A CA    1 
ATOM   1229 C  C     . LYS A 1 172 ? 3.682   -16.217 -10.949 1.00 50.60  ? 116 LYS A C     1 
ATOM   1230 O  O     . LYS A 1 172 ? 4.069   -17.328 -11.342 1.00 50.43  ? 116 LYS A O     1 
ATOM   1231 C  CB    . LYS A 1 172 ? 5.672   -16.094 -9.394  1.00 44.96  ? 116 LYS A CB    1 
ATOM   1232 C  CG    . LYS A 1 172 ? 6.667   -15.226 -8.655  1.00 45.19  ? 116 LYS A CG    1 
ATOM   1233 C  CD    . LYS A 1 172 ? 8.052   -15.842 -8.679  1.00 44.86  ? 116 LYS A CD    1 
ATOM   1234 C  CE    . LYS A 1 172 ? 9.041   -15.009 -7.911  1.00 42.67  ? 116 LYS A CE    1 
ATOM   1235 N  NZ    . LYS A 1 172 ? 10.201  -15.832 -7.481  1.00 46.90  ? 116 LYS A NZ    1 
ATOM   1236 N  N     . SER A 1 173 ? 2.453   -15.753 -11.219 1.00 45.85  ? 117 SER A N     1 
ATOM   1237 C  CA    . SER A 1 173 ? 1.491   -16.580 -11.944 1.00 52.83  ? 117 SER A CA    1 
ATOM   1238 C  C     . SER A 1 173 ? 1.904   -16.865 -13.388 1.00 58.66  ? 117 SER A C     1 
ATOM   1239 O  O     . SER A 1 173 ? 1.267   -17.701 -14.038 1.00 61.71  ? 117 SER A O     1 
ATOM   1240 C  CB    . SER A 1 173 ? 0.087   -15.948 -11.901 1.00 50.99  ? 117 SER A CB    1 
ATOM   1241 O  OG    . SER A 1 173 ? -0.062  -14.835 -12.766 1.00 52.39  ? 117 SER A OG    1 
ATOM   1242 N  N     . ASP A 1 174 ? 2.949   -16.216 -13.903 1.00 56.10  ? 118 ASP A N     1 
ATOM   1243 C  CA    . ASP A 1 174 ? 3.418   -16.533 -15.246 1.00 56.26  ? 118 ASP A CA    1 
ATOM   1244 C  C     . ASP A 1 174 ? 4.124   -17.884 -15.332 1.00 61.42  ? 118 ASP A C     1 
ATOM   1245 O  O     . ASP A 1 174 ? 4.370   -18.355 -16.446 1.00 65.75  ? 118 ASP A O     1 
ATOM   1246 C  CB    . ASP A 1 174 ? 4.365   -15.443 -15.749 1.00 55.22  ? 118 ASP A CB    1 
ATOM   1247 C  CG    . ASP A 1 174 ? 5.501   -15.153 -14.768 1.00 58.27  ? 118 ASP A CG    1 
ATOM   1248 O  OD1   . ASP A 1 174 ? 5.268   -14.442 -13.756 1.00 50.23  ? 118 ASP A OD1   1 
ATOM   1249 O  OD2   . ASP A 1 174 ? 6.633   -15.637 -15.020 1.00 56.90  ? 118 ASP A OD2   1 
ATOM   1250 N  N     . LEU A 1 175 ? 4.463   -18.513 -14.203 1.00 62.47  ? 119 LEU A N     1 
ATOM   1251 C  CA    . LEU A 1 175 ? 5.213   -19.769 -14.209 1.00 62.81  ? 119 LEU A CA    1 
ATOM   1252 C  C     . LEU A 1 175 ? 4.340   -20.958 -13.836 1.00 60.61  ? 119 LEU A C     1 
ATOM   1253 O  O     . LEU A 1 175 ? 4.621   -21.648 -12.856 1.00 57.63  ? 119 LEU A O     1 
ATOM   1254 C  CB    . LEU A 1 175 ? 6.388   -19.711 -13.233 1.00 61.67  ? 119 LEU A CB    1 
ATOM   1255 C  CG    . LEU A 1 175 ? 7.455   -18.668 -13.505 1.00 57.08  ? 119 LEU A CG    1 
ATOM   1256 C  CD1   . LEU A 1 175 ? 8.700   -18.954 -12.668 1.00 56.75  ? 119 LEU A CD1   1 
ATOM   1257 C  CD2   . LEU A 1 175 ? 7.760   -18.657 -14.975 1.00 58.12  ? 119 LEU A CD2   1 
ATOM   1258 N  N     . GLU A 1 176 ? 3.290   -21.207 -14.618 1.00 68.58  ? 120 GLU A N     1 
ATOM   1259 C  CA    . GLU A 1 176 ? 2.372   -22.308 -14.356 1.00 65.18  ? 120 GLU A CA    1 
ATOM   1260 C  C     . GLU A 1 176 ? 3.085   -23.658 -14.278 1.00 63.23  ? 120 GLU A C     1 
ATOM   1261 O  O     . GLU A 1 176 ? 2.565   -24.586 -13.654 1.00 58.97  ? 120 GLU A O     1 
ATOM   1262 C  CB    . GLU A 1 176 ? 1.297   -22.328 -15.447 1.00 66.78  ? 120 GLU A CB    1 
ATOM   1263 C  CG    . GLU A 1 176 ? 0.700   -20.947 -15.762 1.00 60.38  ? 120 GLU A CG    1 
ATOM   1264 C  CD    . GLU A 1 176 ? 1.400   -20.267 -16.957 1.00 78.07  ? 120 GLU A CD    1 
ATOM   1265 O  OE1   . GLU A 1 176 ? 2.481   -20.775 -17.366 1.00 75.52  ? 120 GLU A OE1   1 
ATOM   1266 O  OE2   . GLU A 1 176 ? 0.870   -19.253 -17.507 1.00 75.06  ? 120 GLU A OE2   1 
ATOM   1267 N  N     . ASP A 1 177 ? 4.271   -23.790 -14.875 1.00 67.23  ? 121 ASP A N     1 
ATOM   1268 C  CA    . ASP A 1 177 ? 4.986   -25.057 -14.780 1.00 66.54  ? 121 ASP A CA    1 
ATOM   1269 C  C     . ASP A 1 177 ? 5.620   -25.210 -13.406 1.00 62.18  ? 121 ASP A C     1 
ATOM   1270 O  O     . ASP A 1 177 ? 5.507   -26.264 -12.775 1.00 68.74  ? 121 ASP A O     1 
ATOM   1271 C  CB    . ASP A 1 177 ? 6.049   -25.161 -15.881 1.00 70.04  ? 121 ASP A CB    1 
ATOM   1272 C  CG    . ASP A 1 177 ? 5.525   -25.825 -17.156 1.00 70.88  ? 121 ASP A CG    1 
ATOM   1273 O  OD1   . ASP A 1 177 ? 6.240   -25.768 -18.189 1.00 71.70  ? 121 ASP A OD1   1 
ATOM   1274 O  OD2   . ASP A 1 177 ? 4.399   -26.382 -17.131 1.00 69.50  ? 121 ASP A OD2   1 
ATOM   1275 N  N     . GLN A 1 178 ? 6.286   -24.165 -12.923 1.00 68.93  ? 122 GLN A N     1 
ATOM   1276 C  CA    . GLN A 1 178 ? 6.955   -24.198 -11.626 1.00 62.28  ? 122 GLN A CA    1 
ATOM   1277 C  C     . GLN A 1 178 ? 5.983   -24.076 -10.454 1.00 60.25  ? 122 GLN A C     1 
ATOM   1278 O  O     . GLN A 1 178 ? 6.405   -24.235 -9.299  1.00 63.59  ? 122 GLN A O     1 
ATOM   1279 C  CB    . GLN A 1 178 ? 8.009   -23.077 -11.560 1.00 60.46  ? 122 GLN A CB    1 
ATOM   1280 C  CG    . GLN A 1 178 ? 9.287   -23.327 -12.377 1.00 60.75  ? 122 GLN A CG    1 
ATOM   1281 C  CD    . GLN A 1 178 ? 9.110   -23.096 -13.882 1.00 72.41  ? 122 GLN A CD    1 
ATOM   1282 O  OE1   . GLN A 1 178 ? 8.015   -22.749 -14.353 1.00 71.94  ? 122 GLN A OE1   1 
ATOM   1283 N  NE2   . GLN A 1 178 ? 10.195  -23.291 -14.645 1.00 66.34  ? 122 GLN A NE2   1 
ATOM   1284 N  N     . ARG A 1 179 ? 4.699   -23.825 -10.719 1.00 55.45  ? 123 ARG A N     1 
ATOM   1285 C  CA    . ARG A 1 179 ? 3.734   -23.575 -9.655  1.00 55.02  ? 123 ARG A CA    1 
ATOM   1286 C  C     . ARG A 1 179 ? 3.569   -24.792 -8.746  1.00 53.95  ? 123 ARG A C     1 
ATOM   1287 O  O     . ARG A 1 179 ? 3.610   -25.941 -9.197  1.00 59.25  ? 123 ARG A O     1 
ATOM   1288 C  CB    . ARG A 1 179 ? 2.383   -23.179 -10.255 1.00 54.40  ? 123 ARG A CB    1 
ATOM   1289 C  CG    . ARG A 1 179 ? 1.380   -22.655 -9.218  1.00 52.66  ? 123 ARG A CG    1 
ATOM   1290 C  CD    . ARG A 1 179 ? -0.047  -22.791 -9.693  1.00 49.89  ? 123 ARG A CD    1 
ATOM   1291 N  NE    . ARG A 1 179 ? -0.997  -22.214 -8.751  1.00 48.00  ? 123 ARG A NE    1 
ATOM   1292 C  CZ    . ARG A 1 179 ? -1.990  -21.394 -9.075  1.00 56.61  ? 123 ARG A CZ    1 
ATOM   1293 N  NH1   . ARG A 1 179 ? -2.186  -21.032 -10.332 1.00 56.72  ? 123 ARG A NH1   1 
ATOM   1294 N  NH2   . ARG A 1 179 ? -2.803  -20.944 -8.131  1.00 61.41  ? 123 ARG A NH2   1 
ATOM   1295 N  N     . VAL A 1 180 ? 3.383   -24.521 -7.455  1.00 59.48  ? 124 VAL A N     1 
ATOM   1296 C  CA    . VAL A 1 180 ? 3.170   -25.547 -6.432  1.00 58.72  ? 124 VAL A CA    1 
ATOM   1297 C  C     . VAL A 1 180 ? 1.973   -25.264 -5.543  1.00 47.58  ? 124 VAL A C     1 
ATOM   1298 O  O     . VAL A 1 180 ? 1.423   -26.202 -4.956  1.00 54.65  ? 124 VAL A O     1 
ATOM   1299 C  CB    . VAL A 1 180 ? 4.429   -25.726 -5.552  1.00 50.13  ? 124 VAL A CB    1 
ATOM   1300 C  CG1   . VAL A 1 180 ? 5.677   -26.010 -6.402  1.00 55.07  ? 124 VAL A CG1   1 
ATOM   1301 C  CG2   . VAL A 1 180 ? 4.616   -24.481 -4.708  1.00 50.84  ? 124 VAL A CG2   1 
ATOM   1302 N  N     . VAL A 1 181 ? 1.516   -24.025 -5.414  1.00 50.82  ? 125 VAL A N     1 
ATOM   1303 C  CA    . VAL A 1 181 ? 0.471   -23.665 -4.464  1.00 55.74  ? 125 VAL A CA    1 
ATOM   1304 C  C     . VAL A 1 181 ? -0.891  -23.817 -5.132  1.00 51.78  ? 125 VAL A C     1 
ATOM   1305 O  O     . VAL A 1 181 ? -1.214  -23.080 -6.067  1.00 53.07  ? 125 VAL A O     1 
ATOM   1306 C  CB    . VAL A 1 181 ? 0.678   -22.232 -3.941  1.00 55.49  ? 125 VAL A CB    1 
ATOM   1307 C  CG1   . VAL A 1 181 ? -0.558  -21.722 -3.204  1.00 54.14  ? 125 VAL A CG1   1 
ATOM   1308 C  CG2   . VAL A 1 181 ? 1.894   -22.167 -3.016  1.00 53.44  ? 125 VAL A CG2   1 
ATOM   1309 N  N     . LYS A 1 182 ? -1.696  -24.761 -4.639  1.00 55.30  ? 126 LYS A N     1 
ATOM   1310 C  CA    . LYS A 1 182 ? -3.052  -24.935 -5.146  1.00 60.52  ? 126 LYS A CA    1 
ATOM   1311 C  C     . LYS A 1 182 ? -3.823  -23.633 -5.029  1.00 56.84  ? 126 LYS A C     1 
ATOM   1312 O  O     . LYS A 1 182 ? -3.788  -22.971 -3.993  1.00 64.66  ? 126 LYS A O     1 
ATOM   1313 C  CB    . LYS A 1 182 ? -3.785  -26.043 -4.382  1.00 68.28  ? 126 LYS A CB    1 
ATOM   1314 C  CG    . LYS A 1 182 ? -3.463  -27.486 -4.802  1.00 68.39  ? 126 LYS A CG    1 
ATOM   1315 C  CD    . LYS A 1 182 ? -4.112  -28.496 -3.841  1.00 79.60  ? 126 LYS A CD    1 
ATOM   1316 C  CE    . LYS A 1 182 ? -3.759  -29.948 -4.187  1.00 79.83  ? 126 LYS A CE    1 
ATOM   1317 N  NZ    . LYS A 1 182 ? -4.076  -30.888 -3.066  1.00 72.16  ? 126 LYS A NZ    1 
ATOM   1318 N  N     . GLU A 1 183 ? -4.501  -23.252 -6.108  1.00 65.59  ? 127 GLU A N     1 
ATOM   1319 C  CA    . GLU A 1 183 ? -5.363  -22.080 -6.069  1.00 63.91  ? 127 GLU A CA    1 
ATOM   1320 C  C     . GLU A 1 183 ? -6.389  -22.203 -4.957  1.00 67.98  ? 127 GLU A C     1 
ATOM   1321 O  O     . GLU A 1 183 ? -6.696  -21.222 -4.277  1.00 69.00  ? 127 GLU A O     1 
ATOM   1322 C  CB    . GLU A 1 183 ? -6.064  -21.909 -7.413  1.00 71.56  ? 127 GLU A CB    1 
ATOM   1323 C  CG    . GLU A 1 183 ? -6.748  -23.196 -7.920  1.00 79.50  ? 127 GLU A CG    1 
ATOM   1324 C  CD    . GLU A 1 183 ? -5.806  -24.152 -8.667  1.00 84.44  ? 127 GLU A CD    1 
ATOM   1325 O  OE1   . GLU A 1 183 ? -5.162  -25.009 -8.010  1.00 78.31  ? 127 GLU A OE1   1 
ATOM   1326 O  OE2   . GLU A 1 183 ? -5.726  -24.045 -9.917  1.00 85.94  ? 127 GLU A OE2   1 
ATOM   1327 N  N     . GLU A 1 184 ? -6.895  -23.422 -4.731  1.00 78.04  ? 128 GLU A N     1 
ATOM   1328 C  CA    . GLU A 1 184 ? -7.969  -23.652 -3.764  1.00 68.51  ? 128 GLU A CA    1 
ATOM   1329 C  C     . GLU A 1 184 ? -7.540  -23.268 -2.356  1.00 65.23  ? 128 GLU A C     1 
ATOM   1330 O  O     . GLU A 1 184 ? -8.231  -22.509 -1.661  1.00 57.58  ? 128 GLU A O     1 
ATOM   1331 C  CB    . GLU A 1 184 ? -8.395  -25.121 -3.805  1.00 65.38  ? 128 GLU A CB    1 
ATOM   1332 C  CG    . GLU A 1 184 ? -9.081  -25.550 -5.102  1.00 70.94  ? 128 GLU A CG    1 
ATOM   1333 C  CD    . GLU A 1 184 ? -8.093  -25.933 -6.194  1.00 78.56  ? 128 GLU A CD    1 
ATOM   1334 O  OE1   . GLU A 1 184 ? -6.932  -26.243 -5.840  1.00 78.16  ? 128 GLU A OE1   1 
ATOM   1335 O  OE2   . GLU A 1 184 ? -8.481  -25.939 -7.393  1.00 79.46  ? 128 GLU A OE2   1 
ATOM   1336 N  N     . GLU A 1 185 ? -6.403  -23.802 -1.909  1.00 71.91  ? 129 GLU A N     1 
ATOM   1337 C  CA    . GLU A 1 185 ? -5.922  -23.490 -0.570  1.00 65.25  ? 129 GLU A CA    1 
ATOM   1338 C  C     . GLU A 1 185 ? -5.722  -22.000 -0.370  1.00 60.31  ? 129 GLU A C     1 
ATOM   1339 O  O     . GLU A 1 185 ? -5.786  -21.531 0.764   1.00 62.77  ? 129 GLU A O     1 
ATOM   1340 C  CB    . GLU A 1 185 ? -4.614  -24.229 -0.292  1.00 62.10  ? 129 GLU A CB    1 
ATOM   1341 C  CG    . GLU A 1 185 ? -4.779  -25.733 -0.178  1.00 73.37  ? 129 GLU A CG    1 
ATOM   1342 C  CD    . GLU A 1 185 ? -3.757  -26.356 0.755   1.00 86.65  ? 129 GLU A CD    1 
ATOM   1343 O  OE1   . GLU A 1 185 ? -2.651  -25.776 0.912   1.00 84.31  ? 129 GLU A OE1   1 
ATOM   1344 O  OE2   . GLU A 1 185 ? -4.064  -27.427 1.326   1.00 89.86  ? 129 GLU A OE2   1 
ATOM   1345 N  N     . ALA A 1 186 ? -5.503  -21.240 -1.442  1.00 66.48  ? 130 ALA A N     1 
ATOM   1346 C  CA    . ALA A 1 186 ? -5.201  -19.821 -1.282  1.00 63.69  ? 130 ALA A CA    1 
ATOM   1347 C  C     . ALA A 1 186 ? -6.463  -18.967 -1.159  1.00 64.26  ? 130 ALA A C     1 
ATOM   1348 O  O     . ALA A 1 186 ? -6.494  -18.023 -0.356  1.00 62.16  ? 130 ALA A O     1 
ATOM   1349 C  CB    . ALA A 1 186 ? -4.333  -19.342 -2.440  1.00 58.41  ? 130 ALA A CB    1 
ATOM   1350 N  N     . ILE A 1 187 ? -7.512  -19.266 -1.939  1.00 62.85  ? 131 ILE A N     1 
ATOM   1351 C  CA    . ILE A 1 187 ? -8.762  -18.523 -1.767  1.00 65.30  ? 131 ILE A CA    1 
ATOM   1352 C  C     . ILE A 1 187 ? -9.361  -18.791 -0.390  1.00 64.61  ? 131 ILE A C     1 
ATOM   1353 O  O     . ILE A 1 187 ? -9.936  -17.885 0.229   1.00 66.67  ? 131 ILE A O     1 
ATOM   1354 C  CB    . ILE A 1 187 ? -9.779  -18.850 -2.881  1.00 66.17  ? 131 ILE A CB    1 
ATOM   1355 C  CG1   . ILE A 1 187 ? -9.268  -18.421 -4.256  1.00 63.37  ? 131 ILE A CG1   1 
ATOM   1356 C  CG2   . ILE A 1 187 ? -11.143 -18.208 -2.597  1.00 63.92  ? 131 ILE A CG2   1 
ATOM   1357 C  CD1   . ILE A 1 187 ? -8.962  -19.582 -5.178  1.00 60.98  ? 131 ILE A CD1   1 
ATOM   1358 N  N     . ALA A 1 188 ? -9.235  -20.024 0.112   1.00 63.61  ? 132 ALA A N     1 
ATOM   1359 C  CA    . ALA A 1 188 ? -9.740  -20.376 1.434   1.00 61.58  ? 132 ALA A CA    1 
ATOM   1360 C  C     . ALA A 1 188 ? -9.162  -19.427 2.465   1.00 70.19  ? 132 ALA A C     1 
ATOM   1361 O  O     . ALA A 1 188 ? -9.902  -18.646 3.085   1.00 73.04  ? 132 ALA A O     1 
ATOM   1362 C  CB    . ALA A 1 188 ? -9.382  -21.816 1.798   1.00 66.25  ? 132 ALA A CB    1 
ATOM   1363 N  N     . LEU A 1 189 ? -7.834  -19.479 2.622   1.00 67.92  ? 133 LEU A N     1 
ATOM   1364 C  CA    . LEU A 1 189 ? -7.136  -18.568 3.524   1.00 69.62  ? 133 LEU A CA    1 
ATOM   1365 C  C     . LEU A 1 189 ? -7.685  -17.151 3.414   1.00 67.00  ? 133 LEU A C     1 
ATOM   1366 O  O     . LEU A 1 189 ? -8.005  -16.516 4.425   1.00 74.37  ? 133 LEU A O     1 
ATOM   1367 C  CB    . LEU A 1 189 ? -5.629  -18.609 3.234   1.00 63.22  ? 133 LEU A CB    1 
ATOM   1368 C  CG    . LEU A 1 189 ? -4.761  -18.184 4.423   1.00 72.46  ? 133 LEU A CG    1 
ATOM   1369 C  CD1   . LEU A 1 189 ? -3.427  -18.882 4.423   1.00 66.99  ? 133 LEU A CD1   1 
ATOM   1370 C  CD2   . LEU A 1 189 ? -4.544  -16.660 4.428   1.00 77.07  ? 133 LEU A CD2   1 
ATOM   1371 N  N     . ALA A 1 190 ? -7.859  -16.666 2.185   1.00 68.59  ? 134 ALA A N     1 
ATOM   1372 C  CA    . ALA A 1 190 ? -8.333  -15.308 1.950   1.00 72.02  ? 134 ALA A CA    1 
ATOM   1373 C  C     . ALA A 1 190 ? -9.635  -15.024 2.693   1.00 71.61  ? 134 ALA A C     1 
ATOM   1374 O  O     . ALA A 1 190 ? -9.708  -14.104 3.517   1.00 75.10  ? 134 ALA A O     1 
ATOM   1375 C  CB    . ALA A 1 190 ? -8.505  -15.069 0.444   1.00 71.76  ? 134 ALA A CB    1 
ATOM   1376 N  N     . GLU A 1 191 ? -10.683 -15.805 2.419   1.00 75.11  ? 135 GLU A N     1 
ATOM   1377 C  CA    . GLU A 1 191 ? -11.962 -15.473 3.038   1.00 78.00  ? 135 GLU A CA    1 
ATOM   1378 C  C     . GLU A 1 191 ? -12.038 -15.915 4.493   1.00 74.91  ? 135 GLU A C     1 
ATOM   1379 O  O     . GLU A 1 191 ? -12.963 -15.497 5.201   1.00 71.16  ? 135 GLU A O     1 
ATOM   1380 C  CB    . GLU A 1 191 ? -13.129 -16.061 2.233   1.00 79.71  ? 135 GLU A CB    1 
ATOM   1381 C  CG    . GLU A 1 191 ? -14.201 -15.014 1.861   1.00 84.42  ? 135 GLU A CG    1 
ATOM   1382 C  CD    . GLU A 1 191 ? -13.645 -13.840 1.039   1.00 84.80  ? 135 GLU A CD    1 
ATOM   1383 O  OE1   . GLU A 1 191 ? -13.098 -14.091 -0.067  1.00 80.42  ? 135 GLU A OE1   1 
ATOM   1384 O  OE2   . GLU A 1 191 ? -13.756 -12.675 1.500   1.00 73.05  ? 135 GLU A OE2   1 
ATOM   1385 N  N     . LYS A 1 192 ? -11.087 -16.737 4.953   1.00 72.18  ? 136 LYS A N     1 
ATOM   1386 C  CA    . LYS A 1 192 ? -10.929 -16.964 6.386   1.00 71.58  ? 136 LYS A CA    1 
ATOM   1387 C  C     . LYS A 1 192 ? -10.489 -15.684 7.086   1.00 74.77  ? 136 LYS A C     1 
ATOM   1388 O  O     . LYS A 1 192 ? -10.917 -15.404 8.212   1.00 70.19  ? 136 LYS A O     1 
ATOM   1389 C  CB    . LYS A 1 192 ? -9.925  -18.091 6.630   1.00 70.19  ? 136 LYS A CB    1 
ATOM   1390 C  CG    . LYS A 1 192 ? -9.403  -18.180 8.063   1.00 74.09  ? 136 LYS A CG    1 
ATOM   1391 C  CD    . LYS A 1 192 ? -8.807  -19.557 8.360   1.00 77.39  ? 136 LYS A CD    1 
ATOM   1392 C  CE    . LYS A 1 192 ? -7.857  -19.998 7.248   1.00 78.10  ? 136 LYS A CE    1 
ATOM   1393 N  NZ    . LYS A 1 192 ? -7.529  -21.458 7.308   1.00 91.06  ? 136 LYS A NZ    1 
ATOM   1394 N  N     . TYR A 1 193 ? -9.650  -14.890 6.425   1.00 71.61  ? 137 TYR A N     1 
ATOM   1395 C  CA    . TYR A 1 193 ? -9.253  -13.582 6.911   1.00 68.57  ? 137 TYR A CA    1 
ATOM   1396 C  C     . TYR A 1 193 ? -10.075 -12.459 6.298   1.00 72.10  ? 137 TYR A C     1 
ATOM   1397 O  O     . TYR A 1 193 ? -9.890  -11.297 6.673   1.00 75.43  ? 137 TYR A O     1 
ATOM   1398 C  CB    . TYR A 1 193 ? -7.769  -13.353 6.632   1.00 65.40  ? 137 TYR A CB    1 
ATOM   1399 C  CG    . TYR A 1 193 ? -6.873  -14.234 7.464   1.00 73.28  ? 137 TYR A CG    1 
ATOM   1400 C  CD1   . TYR A 1 193 ? -6.203  -13.731 8.580   1.00 77.32  ? 137 TYR A CD1   1 
ATOM   1401 C  CD2   . TYR A 1 193 ? -6.697  -15.569 7.147   1.00 74.04  ? 137 TYR A CD2   1 
ATOM   1402 C  CE1   . TYR A 1 193 ? -5.375  -14.541 9.347   1.00 71.40  ? 137 TYR A CE1   1 
ATOM   1403 C  CE2   . TYR A 1 193 ? -5.880  -16.383 7.910   1.00 73.29  ? 137 TYR A CE2   1 
ATOM   1404 C  CZ    . TYR A 1 193 ? -5.222  -15.868 9.002   1.00 69.79  ? 137 TYR A CZ    1 
ATOM   1405 O  OH    . TYR A 1 193 ? -4.406  -16.692 9.745   1.00 81.47  ? 137 TYR A OH    1 
ATOM   1406 N  N     . GLY A 1 194 ? -10.969 -12.775 5.364   1.00 70.48  ? 138 GLY A N     1 
ATOM   1407 C  CA    . GLY A 1 194 ? -11.774 -11.748 4.729   1.00 68.72  ? 138 GLY A CA    1 
ATOM   1408 C  C     . GLY A 1 194 ? -10.969 -10.767 3.914   1.00 68.71  ? 138 GLY A C     1 
ATOM   1409 O  O     . GLY A 1 194 ? -11.340 -9.591  3.831   1.00 74.96  ? 138 GLY A O     1 
ATOM   1410 N  N     . ILE A 1 195 ? -9.878  -11.214 3.310   1.00 67.72  ? 139 ILE A N     1 
ATOM   1411 C  CA    . ILE A 1 195 ? -8.974  -10.356 2.546   1.00 68.59  ? 139 ILE A CA    1 
ATOM   1412 C  C     . ILE A 1 195 ? -9.068  -10.728 1.072   1.00 66.77  ? 139 ILE A C     1 
ATOM   1413 O  O     . ILE A 1 195 ? -9.034  -11.919 0.736   1.00 64.95  ? 139 ILE A O     1 
ATOM   1414 C  CB    . ILE A 1 195 ? -7.515  -10.460 3.034   1.00 72.99  ? 139 ILE A CB    1 
ATOM   1415 C  CG1   . ILE A 1 195 ? -6.997  -11.893 2.893   1.00 68.60  ? 139 ILE A CG1   1 
ATOM   1416 C  CG2   . ILE A 1 195 ? -7.368  -9.896  4.474   1.00 68.46  ? 139 ILE A CG2   1 
ATOM   1417 C  CD1   . ILE A 1 195 ? -5.538  -12.028 3.203   1.00 70.66  ? 139 ILE A CD1   1 
ATOM   1418 N  N     . PRO A 1 196 ? -9.202  -9.749  0.180   1.00 66.87  ? 140 PRO A N     1 
ATOM   1419 C  CA    . PRO A 1 196 ? -9.160  -10.005 -1.262  1.00 61.26  ? 140 PRO A CA    1 
ATOM   1420 C  C     . PRO A 1 196 ? -8.010  -10.897 -1.708  1.00 67.06  ? 140 PRO A C     1 
ATOM   1421 O  O     . PRO A 1 196 ? -6.949  -10.924 -1.074  1.00 69.84  ? 140 PRO A O     1 
ATOM   1422 C  CB    . PRO A 1 196 ? -9.006  -8.595  -1.838  1.00 60.75  ? 140 PRO A CB    1 
ATOM   1423 C  CG    . PRO A 1 196 ? -9.697  -7.729  -0.886  1.00 60.17  ? 140 PRO A CG    1 
ATOM   1424 C  CD    . PRO A 1 196 ? -9.547  -8.352  0.481   1.00 68.13  ? 140 PRO A CD    1 
ATOM   1425 N  N     . TYR A 1 197 ? -8.197  -11.617 -2.810  1.00 62.15  ? 141 TYR A N     1 
ATOM   1426 C  CA    . TYR A 1 197 ? -7.157  -12.494 -3.316  1.00 57.09  ? 141 TYR A CA    1 
ATOM   1427 C  C     . TYR A 1 197 ? -7.002  -12.314 -4.818  1.00 65.90  ? 141 TYR A C     1 
ATOM   1428 O  O     . TYR A 1 197 ? -7.986  -12.136 -5.547  1.00 62.77  ? 141 TYR A O     1 
ATOM   1429 C  CB    . TYR A 1 197 ? -7.457  -13.946 -2.999  1.00 59.64  ? 141 TYR A CB    1 
ATOM   1430 C  CG    . TYR A 1 197 ? -6.438  -14.886 -3.568  1.00 56.41  ? 141 TYR A CG    1 
ATOM   1431 C  CD1   . TYR A 1 197 ? -5.083  -14.682 -3.355  1.00 53.89  ? 141 TYR A CD1   1 
ATOM   1432 C  CD2   . TYR A 1 197 ? -6.828  -15.971 -4.333  1.00 56.12  ? 141 TYR A CD2   1 
ATOM   1433 C  CE1   . TYR A 1 197 ? -4.143  -15.547 -3.887  1.00 56.82  ? 141 TYR A CE1   1 
ATOM   1434 C  CE2   . TYR A 1 197 ? -5.904  -16.829 -4.875  1.00 56.85  ? 141 TYR A CE2   1 
ATOM   1435 C  CZ    . TYR A 1 197 ? -4.562  -16.617 -4.652  1.00 55.99  ? 141 TYR A CZ    1 
ATOM   1436 O  OH    . TYR A 1 197 ? -3.643  -17.487 -5.194  1.00 54.90  ? 141 TYR A OH    1 
ATOM   1437 N  N     . PHE A 1 198 ? -5.752  -12.379 -5.268  1.00 63.65  ? 142 PHE A N     1 
ATOM   1438 C  CA    . PHE A 1 198 ? -5.360  -12.075 -6.634  1.00 53.42  ? 142 PHE A CA    1 
ATOM   1439 C  C     . PHE A 1 198 ? -4.146  -12.911 -6.976  1.00 59.57  ? 142 PHE A C     1 
ATOM   1440 O  O     . PHE A 1 198 ? -3.152  -12.905 -6.237  1.00 57.58  ? 142 PHE A O     1 
ATOM   1441 C  CB    . PHE A 1 198 ? -4.988  -10.605 -6.797  1.00 60.62  ? 142 PHE A CB    1 
ATOM   1442 C  CG    . PHE A 1 198 ? -6.146  -9.668  -6.822  1.00 64.20  ? 142 PHE A CG    1 
ATOM   1443 C  CD1   . PHE A 1 198 ? -6.642  -9.155  -5.644  1.00 66.55  ? 142 PHE A CD1   1 
ATOM   1444 C  CD2   . PHE A 1 198 ? -6.695  -9.244  -8.020  1.00 65.01  ? 142 PHE A CD2   1 
ATOM   1445 C  CE1   . PHE A 1 198 ? -7.693  -8.255  -5.655  1.00 71.97  ? 142 PHE A CE1   1 
ATOM   1446 C  CE2   . PHE A 1 198 ? -7.756  -8.355  -8.038  1.00 67.33  ? 142 PHE A CE2   1 
ATOM   1447 C  CZ    . PHE A 1 198 ? -8.247  -7.852  -6.858  1.00 67.98  ? 142 PHE A CZ    1 
ATOM   1448 N  N     . GLU A 1 199 ? -4.218  -13.624 -8.092  1.00 65.63  ? 143 GLU A N     1 
ATOM   1449 C  CA    . GLU A 1 199 ? -3.069  -14.361 -8.601  1.00 61.59  ? 143 GLU A CA    1 
ATOM   1450 C  C     . GLU A 1 199 ? -2.353  -13.440 -9.588  1.00 61.54  ? 143 GLU A C     1 
ATOM   1451 O  O     . GLU A 1 199 ? -2.727  -13.337 -10.765 1.00 64.52  ? 143 GLU A O     1 
ATOM   1452 C  CB    . GLU A 1 199 ? -3.508  -15.685 -9.219  1.00 66.52  ? 143 GLU A CB    1 
ATOM   1453 C  CG    . GLU A 1 199 ? -4.107  -16.672 -8.197  1.00 62.21  ? 143 GLU A CG    1 
ATOM   1454 C  CD    . GLU A 1 199 ? -4.161  -18.127 -8.690  1.00 64.88  ? 143 GLU A CD    1 
ATOM   1455 O  OE1   . GLU A 1 199 ? -4.589  -18.996 -7.895  1.00 63.34  ? 143 GLU A OE1   1 
ATOM   1456 O  OE2   . GLU A 1 199 ? -3.787  -18.404 -9.860  1.00 63.81  ? 143 GLU A OE2   1 
ATOM   1457 N  N     . THR A 1 200 ? -1.326  -12.748 -9.096  1.00 61.85  ? 144 THR A N     1 
ATOM   1458 C  CA    . THR A 1 200 ? -0.623  -11.740 -9.882  1.00 58.67  ? 144 THR A CA    1 
ATOM   1459 C  C     . THR A 1 200 ? 0.592   -12.340 -10.585 1.00 52.71  ? 144 THR A C     1 
ATOM   1460 O  O     . THR A 1 200 ? 0.983   -13.479 -10.337 1.00 52.34  ? 144 THR A O     1 
ATOM   1461 C  CB    . THR A 1 200 ? -0.177  -10.561 -8.997  1.00 56.83  ? 144 THR A CB    1 
ATOM   1462 O  OG1   . THR A 1 200 ? 0.778   -11.005 -8.015  1.00 60.04  ? 144 THR A OG1   1 
ATOM   1463 C  CG2   . THR A 1 200 ? -1.370  -9.911  -8.293  1.00 54.63  ? 144 THR A CG2   1 
ATOM   1464 N  N     . SER A 1 201 ? 1.200   -11.542 -11.469 1.00 53.02  ? 145 SER A N     1 
ATOM   1465 C  CA    . SER A 1 201 ? 2.506   -11.877 -12.039 1.00 52.64  ? 145 SER A CA    1 
ATOM   1466 C  C     . SER A 1 201 ? 3.207   -10.559 -12.357 1.00 55.57  ? 145 SER A C     1 
ATOM   1467 O  O     . SER A 1 201 ? 2.787   -9.841  -13.269 1.00 54.56  ? 145 SER A O     1 
ATOM   1468 C  CB    . SER A 1 201 ? 2.378   -12.753 -13.288 1.00 52.18  ? 145 SER A CB    1 
ATOM   1469 O  OG    . SER A 1 201 ? 3.476   -12.577 -14.158 1.00 51.40  ? 145 SER A OG    1 
ATOM   1470 N  N     . ALA A 1 202 ? 4.254   -10.235 -11.589 1.00 55.29  ? 146 ALA A N     1 
ATOM   1471 C  CA    . ALA A 1 202 ? 5.052   -9.065  -11.931 1.00 56.21  ? 146 ALA A CA    1 
ATOM   1472 C  C     . ALA A 1 202 ? 5.814   -9.231  -13.227 1.00 55.59  ? 146 ALA A C     1 
ATOM   1473 O  O     . ALA A 1 202 ? 6.494   -8.285  -13.639 1.00 57.05  ? 146 ALA A O     1 
ATOM   1474 C  CB    . ALA A 1 202 ? 6.022   -8.747  -10.802 1.00 52.66  ? 146 ALA A CB    1 
ATOM   1475 N  N     . ALA A 1 203 ? 5.696   -10.376 -13.897 1.00 51.88  ? 147 ALA A N     1 
ATOM   1476 C  CA    . ALA A 1 203 ? 6.409   -10.558 -15.151 1.00 49.05  ? 147 ALA A CA    1 
ATOM   1477 C  C     . ALA A 1 203 ? 5.610   -9.984  -16.318 1.00 55.10  ? 147 ALA A C     1 
ATOM   1478 O  O     . ALA A 1 203 ? 6.096   -9.101  -17.035 1.00 54.91  ? 147 ALA A O     1 
ATOM   1479 C  CB    . ALA A 1 203 ? 6.727   -12.037 -15.370 1.00 48.66  ? 147 ALA A CB    1 
ATOM   1480 N  N     . ASN A 1 204 ? 4.374   -10.456 -16.513 1.00 52.51  ? 148 ASN A N     1 
ATOM   1481 C  CA    . ASN A 1 204 ? 3.530   -9.979  -17.603 1.00 51.70  ? 148 ASN A CA    1 
ATOM   1482 C  C     . ASN A 1 204 ? 2.498   -8.959  -17.145 1.00 54.25  ? 148 ASN A C     1 
ATOM   1483 O  O     . ASN A 1 204 ? 1.672   -8.515  -17.958 1.00 53.90  ? 148 ASN A O     1 
ATOM   1484 C  CB    . ASN A 1 204 ? 2.828   -11.149 -18.304 1.00 54.73  ? 148 ASN A CB    1 
ATOM   1485 C  CG    . ASN A 1 204 ? 2.009   -12.021 -17.348 1.00 56.97  ? 148 ASN A CG    1 
ATOM   1486 O  OD1   . ASN A 1 204 ? 1.090   -11.548 -16.675 1.00 55.69  ? 148 ASN A OD1   1 
ATOM   1487 N  ND2   . ASN A 1 204 ? 2.328   -13.312 -17.312 1.00 57.12  ? 148 ASN A ND2   1 
ATOM   1488 N  N     . GLY A 1 205 ? 2.529   -8.580  -15.870 1.00 50.47  ? 149 GLY A N     1 
ATOM   1489 C  CA    . GLY A 1 205 ? 1.661   -7.553  -15.348 1.00 46.98  ? 149 GLY A CA    1 
ATOM   1490 C  C     . GLY A 1 205 ? 0.248   -7.975  -15.019 1.00 48.01  ? 149 GLY A C     1 
ATOM   1491 O  O     . GLY A 1 205 ? -0.518  -7.135  -14.532 1.00 52.56  ? 149 GLY A O     1 
ATOM   1492 N  N     . THR A 1 206 ? -0.130  -9.231  -15.272 1.00 48.87  ? 150 THR A N     1 
ATOM   1493 C  CA    . THR A 1 206 ? -1.474  -9.700  -14.939 1.00 51.11  ? 150 THR A CA    1 
ATOM   1494 C  C     . THR A 1 206 ? -1.796  -9.369  -13.493 1.00 60.66  ? 150 THR A C     1 
ATOM   1495 O  O     . THR A 1 206 ? -0.984  -9.619  -12.594 1.00 60.07  ? 150 THR A O     1 
ATOM   1496 C  CB    . THR A 1 206 ? -1.596  -11.215 -15.129 1.00 52.33  ? 150 THR A CB    1 
ATOM   1497 O  OG1   . THR A 1 206 ? -1.322  -11.576 -16.491 1.00 60.86  ? 150 THR A OG1   1 
ATOM   1498 C  CG2   . THR A 1 206 ? -3.005  -11.673 -14.762 1.00 46.58  ? 150 THR A CG2   1 
ATOM   1499 N  N     . ASN A 1 207 ? -2.970  -8.774  -13.278 1.00 62.69  ? 151 ASN A N     1 
ATOM   1500 C  CA    . ASN A 1 207 ? -3.530  -8.537  -11.946 1.00 60.37  ? 151 ASN A CA    1 
ATOM   1501 C  C     . ASN A 1 207 ? -2.730  -7.550  -11.091 1.00 60.68  ? 151 ASN A C     1 
ATOM   1502 O  O     . ASN A 1 207 ? -3.181  -7.173  -10.005 1.00 61.04  ? 151 ASN A O     1 
ATOM   1503 C  CB    . ASN A 1 207 ? -3.672  -9.859  -11.181 1.00 59.30  ? 151 ASN A CB    1 
ATOM   1504 C  CG    . ASN A 1 207 ? -4.998  -10.554 -11.443 1.00 60.27  ? 151 ASN A CG    1 
ATOM   1505 O  OD1   . ASN A 1 207 ? -5.945  -9.958  -11.978 1.00 60.54  ? 151 ASN A OD1   1 
ATOM   1506 N  ND2   . ASN A 1 207 ? -5.087  -11.816 -11.023 1.00 55.49  ? 151 ASN A ND2   1 
ATOM   1507 N  N     . ILE A 1 208 ? -1.546  -7.138  -11.550 1.00 58.02  ? 152 ILE A N     1 
ATOM   1508 C  CA    . ILE A 1 208 ? -0.740  -6.180  -10.792 1.00 56.44  ? 152 ILE A CA    1 
ATOM   1509 C  C     . ILE A 1 208 ? -1.514  -4.884  -10.584 1.00 56.93  ? 152 ILE A C     1 
ATOM   1510 O  O     . ILE A 1 208 ? -1.565  -4.344  -9.479  1.00 62.09  ? 152 ILE A O     1 
ATOM   1511 C  CB    . ILE A 1 208 ? 0.604   -5.928  -11.503 1.00 56.91  ? 152 ILE A CB    1 
ATOM   1512 C  CG1   . ILE A 1 208 ? 1.371   -7.239  -11.714 1.00 57.04  ? 152 ILE A CG1   1 
ATOM   1513 C  CG2   . ILE A 1 208 ? 1.459   -4.962  -10.719 1.00 55.94  ? 152 ILE A CG2   1 
ATOM   1514 C  CD1   . ILE A 1 208 ? 2.128   -7.709  -10.481 1.00 57.86  ? 152 ILE A CD1   1 
ATOM   1515 N  N     . SER A 1 209 ? -2.143  -4.373  -11.642 1.00 63.12  ? 153 SER A N     1 
ATOM   1516 C  CA    . SER A 1 209 ? -2.946  -3.163  -11.506 1.00 61.33  ? 153 SER A CA    1 
ATOM   1517 C  C     . SER A 1 209 ? -4.231  -3.435  -10.726 1.00 60.88  ? 153 SER A C     1 
ATOM   1518 O  O     . SER A 1 209 ? -4.655  -2.605  -9.915  1.00 63.29  ? 153 SER A O     1 
ATOM   1519 C  CB    . SER A 1 209 ? -3.254  -2.570  -12.894 1.00 65.35  ? 153 SER A CB    1 
ATOM   1520 O  OG    . SER A 1 209 ? -3.410  -3.580  -13.896 1.00 73.09  ? 153 SER A OG    1 
ATOM   1521 N  N     . GLN A 1 210 ? -4.846  -4.601  -10.927 1.00 63.38  ? 154 GLN A N     1 
ATOM   1522 C  CA    . GLN A 1 210 ? -6.182  -4.843  -10.384 1.00 64.89  ? 154 GLN A CA    1 
ATOM   1523 C  C     . GLN A 1 210 ? -6.156  -5.010  -8.859  1.00 67.09  ? 154 GLN A C     1 
ATOM   1524 O  O     . GLN A 1 210 ? -7.073  -4.560  -8.158  1.00 63.16  ? 154 GLN A O     1 
ATOM   1525 C  CB    . GLN A 1 210 ? -6.788  -6.069  -11.076 1.00 61.75  ? 154 GLN A CB    1 
ATOM   1526 C  CG    . GLN A 1 210 ? -7.211  -5.840  -12.556 1.00 63.00  ? 154 GLN A CG    1 
ATOM   1527 C  CD    . GLN A 1 210 ? -6.098  -6.113  -13.563 1.00 64.05  ? 154 GLN A CD    1 
ATOM   1528 O  OE1   . GLN A 1 210 ? -4.917  -5.931  -13.263 1.00 67.16  ? 154 GLN A OE1   1 
ATOM   1529 N  NE2   . GLN A 1 210 ? -6.474  -6.561  -14.768 1.00 74.26  ? 154 GLN A NE2   1 
ATOM   1530 N  N     . ALA A 1 211 ? -5.113  -5.648  -8.324  1.00 66.40  ? 155 ALA A N     1 
ATOM   1531 C  CA    . ALA A 1 211 ? -5.014  -5.828  -6.881  1.00 61.39  ? 155 ALA A CA    1 
ATOM   1532 C  C     . ALA A 1 211 ? -4.692  -4.515  -6.185  1.00 62.00  ? 155 ALA A C     1 
ATOM   1533 O  O     . ALA A 1 211 ? -5.311  -4.171  -5.176  1.00 65.53  ? 155 ALA A O     1 
ATOM   1534 C  CB    . ALA A 1 211 ? -3.951  -6.877  -6.554  1.00 63.91  ? 155 ALA A CB    1 
ATOM   1535 N  N     . ILE A 1 212 ? -3.734  -3.764  -6.714  1.00 60.69  ? 156 ILE A N     1 
ATOM   1536 C  CA    . ILE A 1 212 ? -3.411  -2.472  -6.125  1.00 59.22  ? 156 ILE A CA    1 
ATOM   1537 C  C     . ILE A 1 212 ? -4.629  -1.550  -6.125  1.00 62.27  ? 156 ILE A C     1 
ATOM   1538 O  O     . ILE A 1 212 ? -4.906  -0.874  -5.127  1.00 64.90  ? 156 ILE A O     1 
ATOM   1539 C  CB    . ILE A 1 212 ? -2.208  -1.858  -6.857  1.00 57.10  ? 156 ILE A CB    1 
ATOM   1540 C  CG1   . ILE A 1 212 ? -0.946  -2.638  -6.461  1.00 57.45  ? 156 ILE A CG1   1 
ATOM   1541 C  CG2   . ILE A 1 212 ? -2.106  -0.370  -6.563  1.00 57.66  ? 156 ILE A CG2   1 
ATOM   1542 C  CD1   . ILE A 1 212 ? 0.333   -2.213  -7.151  1.00 53.74  ? 156 ILE A CD1   1 
ATOM   1543 N  N     . GLU A 1 213 ? -5.394  -1.528  -7.222  1.00 66.54  ? 157 GLU A N     1 
ATOM   1544 C  CA    . GLU A 1 213 ? -6.572  -0.664  -7.269  1.00 66.87  ? 157 GLU A CA    1 
ATOM   1545 C  C     . GLU A 1 213 ? -7.615  -1.090  -6.239  1.00 67.47  ? 157 GLU A C     1 
ATOM   1546 O  O     . GLU A 1 213 ? -8.410  -0.261  -5.780  1.00 67.05  ? 157 GLU A O     1 
ATOM   1547 C  CB    . GLU A 1 213 ? -7.174  -0.655  -8.677  1.00 67.27  ? 157 GLU A CB    1 
ATOM   1548 C  CG    . GLU A 1 213 ? -6.290  0.028   -9.730  1.00 68.17  ? 157 GLU A CG    1 
ATOM   1549 C  CD    . GLU A 1 213 ? -6.744  -0.260  -11.152 1.00 75.12  ? 157 GLU A CD    1 
ATOM   1550 O  OE1   . GLU A 1 213 ? -7.843  -0.842  -11.324 1.00 76.07  ? 157 GLU A OE1   1 
ATOM   1551 O  OE2   . GLU A 1 213 ? -5.999  0.087   -12.099 1.00 79.77  ? 157 GLU A OE2   1 
ATOM   1552 N  N     . MET A 1 214 ? -7.614  -2.366  -5.846  1.00 62.05  ? 158 MET A N     1 
ATOM   1553 C  CA    . MET A 1 214 ? -8.525  -2.806  -4.791  1.00 62.92  ? 158 MET A CA    1 
ATOM   1554 C  C     . MET A 1 214 ? -8.063  -2.320  -3.431  1.00 69.41  ? 158 MET A C     1 
ATOM   1555 O  O     . MET A 1 214 ? -8.879  -1.848  -2.620  1.00 72.97  ? 158 MET A O     1 
ATOM   1556 C  CB    . MET A 1 214 ? -8.660  -4.329  -4.797  1.00 66.67  ? 158 MET A CB    1 
ATOM   1557 C  CG    . MET A 1 214 ? -9.592  -4.869  -3.724  1.00 66.68  ? 158 MET A CG    1 
ATOM   1558 S  SD    . MET A 1 214 ? -11.274 -5.061  -4.348  1.00 78.51  ? 158 MET A SD    1 
ATOM   1559 C  CE    . MET A 1 214 ? -12.262 -4.564  -2.932  1.00 73.80  ? 158 MET A CE    1 
ATOM   1560 N  N     . LEU A 1 215 ? -6.762  -2.428  -3.148  1.00 63.51  ? 159 LEU A N     1 
ATOM   1561 C  CA    . LEU A 1 215 ? -6.231  -1.830  -1.935  1.00 58.88  ? 159 LEU A CA    1 
ATOM   1562 C  C     . LEU A 1 215 ? -6.647  -0.368  -1.834  1.00 63.39  ? 159 LEU A C     1 
ATOM   1563 O  O     . LEU A 1 215 ? -7.361  0.031   -0.908  1.00 67.74  ? 159 LEU A O     1 
ATOM   1564 C  CB    . LEU A 1 215 ? -4.713  -1.968  -1.899  1.00 56.83  ? 159 LEU A CB    1 
ATOM   1565 C  CG    . LEU A 1 215 ? -4.091  -1.994  -0.488  1.00 55.74  ? 159 LEU A CG    1 
ATOM   1566 C  CD1   . LEU A 1 215 ? -4.845  -2.915  0.473   1.00 52.15  ? 159 LEU A CD1   1 
ATOM   1567 C  CD2   . LEU A 1 215 ? -2.616  -2.368  -0.539  1.00 45.87  ? 159 LEU A CD2   1 
ATOM   1568 N  N     . LEU A 1 216 ? -6.240  0.436   -2.821  1.00 70.01  ? 160 LEU A N     1 
ATOM   1569 C  CA    . LEU A 1 216 ? -6.632  1.841   -2.883  1.00 66.38  ? 160 LEU A CA    1 
ATOM   1570 C  C     . LEU A 1 216 ? -8.141  2.028   -2.760  1.00 68.53  ? 160 LEU A C     1 
ATOM   1571 O  O     . LEU A 1 216 ? -8.602  3.055   -2.244  1.00 69.49  ? 160 LEU A O     1 
ATOM   1572 C  CB    . LEU A 1 216 ? -6.120  2.436   -4.188  1.00 60.36  ? 160 LEU A CB    1 
ATOM   1573 C  CG    . LEU A 1 216 ? -6.326  3.933   -4.407  1.00 73.45  ? 160 LEU A CG    1 
ATOM   1574 C  CD1   . LEU A 1 216 ? -5.470  4.764   -3.459  1.00 64.89  ? 160 LEU A CD1   1 
ATOM   1575 C  CD2   . LEU A 1 216 ? -6.058  4.311   -5.877  1.00 67.80  ? 160 LEU A CD2   1 
ATOM   1576 N  N     . ASP A 1 217 ? -8.924  1.042   -3.206  1.00 69.24  ? 161 ASP A N     1 
ATOM   1577 C  CA    . ASP A 1 217 ? -10.376 1.119   -3.067  1.00 74.69  ? 161 ASP A CA    1 
ATOM   1578 C  C     . ASP A 1 217 ? -10.801 0.875   -1.621  1.00 76.01  ? 161 ASP A C     1 
ATOM   1579 O  O     . ASP A 1 217 ? -11.621 1.622   -1.073  1.00 80.63  ? 161 ASP A O     1 
ATOM   1580 C  CB    . ASP A 1 217 ? -11.048 0.123   -4.020  1.00 77.53  ? 161 ASP A CB    1 
ATOM   1581 C  CG    . ASP A 1 217 ? -12.513 0.453   -4.282  1.00 87.24  ? 161 ASP A CG    1 
ATOM   1582 O  OD1   . ASP A 1 217 ? -12.805 1.604   -4.695  1.00 82.24  ? 161 ASP A OD1   1 
ATOM   1583 O  OD2   . ASP A 1 217 ? -13.366 -0.448  -4.087  1.00 89.77  ? 161 ASP A OD2   1 
ATOM   1584 N  N     . LEU A 1 218 ? -10.240 -0.157  -0.978  1.00 74.13  ? 162 LEU A N     1 
ATOM   1585 C  CA    . LEU A 1 218 ? -10.488 -0.367  0.450   1.00 67.89  ? 162 LEU A CA    1 
ATOM   1586 C  C     . LEU A 1 218 ? -10.055 0.838   1.276   1.00 68.07  ? 162 LEU A C     1 
ATOM   1587 O  O     . LEU A 1 218 ? -10.691 1.175   2.279   1.00 76.98  ? 162 LEU A O     1 
ATOM   1588 C  CB    . LEU A 1 218 ? -9.752  -1.612  0.941   1.00 59.94  ? 162 LEU A CB    1 
ATOM   1589 C  CG    . LEU A 1 218 ? -10.260 -3.005  0.586   1.00 58.46  ? 162 LEU A CG    1 
ATOM   1590 C  CD1   . LEU A 1 218 ? -9.681  -3.997  1.568   1.00 60.45  ? 162 LEU A CD1   1 
ATOM   1591 C  CD2   . LEU A 1 218 ? -11.773 -3.075  0.588   1.00 55.40  ? 162 LEU A CD2   1 
ATOM   1592 N  N     . ILE A 1 219 ? -8.970  1.491   0.877   1.00 67.18  ? 163 ILE A N     1 
ATOM   1593 C  CA    . ILE A 1 219 ? -8.430  2.605   1.648   1.00 71.40  ? 163 ILE A CA    1 
ATOM   1594 C  C     . ILE A 1 219 ? -9.259  3.866   1.448   1.00 79.90  ? 163 ILE A C     1 
ATOM   1595 O  O     . ILE A 1 219 ? -9.791  4.431   2.408   1.00 87.69  ? 163 ILE A O     1 
ATOM   1596 C  CB    . ILE A 1 219 ? -6.962  2.851   1.271   1.00 70.03  ? 163 ILE A CB    1 
ATOM   1597 C  CG1   . ILE A 1 219 ? -6.150  1.590   1.546   1.00 63.68  ? 163 ILE A CG1   1 
ATOM   1598 C  CG2   . ILE A 1 219 ? -6.427  4.094   1.986   1.00 67.58  ? 163 ILE A CG2   1 
ATOM   1599 C  CD1   . ILE A 1 219 ? -6.449  0.988   2.878   1.00 63.68  ? 163 ILE A CD1   1 
ATOM   1600 N  N     . MET A 1 220 ? -9.345  4.356   0.206   1.00 84.86  ? 164 MET A N     1 
ATOM   1601 C  CA    . MET A 1 220 ? -10.092 5.587   -0.043  1.00 86.25  ? 164 MET A CA    1 
ATOM   1602 C  C     . MET A 1 220 ? -11.553 5.456   0.373   1.00 89.24  ? 164 MET A C     1 
ATOM   1603 O  O     . MET A 1 220 ? -12.208 6.476   0.623   1.00 91.29  ? 164 MET A O     1 
ATOM   1604 C  CB    . MET A 1 220 ? -9.984  5.996   -1.520  1.00 73.43  ? 164 MET A CB    1 
ATOM   1605 C  CG    . MET A 1 220 ? -9.458  7.433   -1.759  1.00 77.26  ? 164 MET A CG    1 
ATOM   1606 S  SD    . MET A 1 220 ? -10.385 8.834   -1.019  1.00 111.09 ? 164 MET A SD    1 
ATOM   1607 C  CE    . MET A 1 220 ? -12.005 8.729   -1.807  1.00 84.07  ? 164 MET A CE    1 
ATOM   1608 N  N     . LYS A 1 221 ? -12.076 4.230   0.465   1.00 82.92  ? 165 LYS A N     1 
ATOM   1609 C  CA    . LYS A 1 221 ? -13.397 4.001   1.029   1.00 87.02  ? 165 LYS A CA    1 
ATOM   1610 C  C     . LYS A 1 221 ? -13.359 3.812   2.542   1.00 88.23  ? 165 LYS A C     1 
ATOM   1611 O  O     . LYS A 1 221 ? -14.368 3.413   3.129   1.00 89.54  ? 165 LYS A O     1 
ATOM   1612 C  CB    . LYS A 1 221 ? -14.065 2.798   0.356   1.00 86.51  ? 165 LYS A CB    1 
ATOM   1613 C  CG    . LYS A 1 221 ? -14.465 3.051   -1.096  1.00 86.08  ? 165 LYS A CG    1 
ATOM   1614 C  CD    . LYS A 1 221 ? -15.443 4.212   -1.225  1.00 86.67  ? 165 LYS A CD    1 
ATOM   1615 C  CE    . LYS A 1 221 ? -15.887 4.365   -2.664  1.00 88.40  ? 165 LYS A CE    1 
ATOM   1616 N  NZ    . LYS A 1 221 ? -16.258 3.044   -3.240  1.00 88.79  ? 165 LYS A NZ    1 
ATOM   1617 N  N     . ARG A 1 222 ? -12.227 4.107   3.184   1.00 88.93  ? 166 ARG A N     1 
ATOM   1618 C  CA    . ARG A 1 222 ? -12.057 4.067   4.636   1.00 91.05  ? 166 ARG A CA    1 
ATOM   1619 C  C     . ARG A 1 222 ? -11.684 5.416   5.232   1.00 96.77  ? 166 ARG A C     1 
ATOM   1620 O  O     . ARG A 1 222 ? -12.105 5.729   6.353   1.00 101.00 ? 166 ARG A O     1 
ATOM   1621 C  CB    . ARG A 1 222 ? -10.996 3.030   5.027   1.00 84.21  ? 166 ARG A CB    1 
ATOM   1622 C  CG    . ARG A 1 222 ? -11.259 2.374   6.375   1.00 86.34  ? 166 ARG A CG    1 
ATOM   1623 C  CD    . ARG A 1 222 ? -9.987  1.785   6.980   1.00 84.87  ? 166 ARG A CD    1 
ATOM   1624 N  NE    . ARG A 1 222 ? -10.266 0.593   7.784   1.00 84.26  ? 166 ARG A NE    1 
ATOM   1625 C  CZ    . ARG A 1 222 ? -9.340  -0.156  8.374   1.00 81.01  ? 166 ARG A CZ    1 
ATOM   1626 N  NH1   . ARG A 1 222 ? -8.055  0.155   8.257   1.00 83.06  ? 166 ARG A NH1   1 
ATOM   1627 N  NH2   . ARG A 1 222 ? -9.699  -1.218  9.085   1.00 80.60  ? 166 ARG A NH2   1 
ATOM   1628 N  N     . MET A 1 223 ? -10.878 6.216   4.528   1.00 90.52  ? 167 MET A N     1 
ATOM   1629 C  CA    . MET A 1 223 ? -10.927 7.655   4.742   1.00 95.94  ? 167 MET A CA    1 
ATOM   1630 C  C     . MET A 1 223 ? -12.341 8.188   4.519   1.00 99.80  ? 167 MET A C     1 
ATOM   1631 O  O     . MET A 1 223 ? -12.713 9.218   5.094   1.00 99.64  ? 167 MET A O     1 
ATOM   1632 C  CB    . MET A 1 223 ? -9.933  8.358   3.816   1.00 99.19  ? 167 MET A CB    1 
ATOM   1633 C  CG    . MET A 1 223 ? -8.477  8.038   4.071   1.00 98.09  ? 167 MET A CG    1 
ATOM   1634 S  SD    . MET A 1 223 ? -7.416  9.309   3.358   1.00 107.06 ? 167 MET A SD    1 
ATOM   1635 C  CE    . MET A 1 223 ? -7.254  10.421  4.767   1.00 94.22  ? 167 MET A CE    1 
ATOM   1636 N  N     . GLU A 1 224 ? -13.126 7.504   3.669   1.00 101.18 ? 168 GLU A N     1 
ATOM   1637 C  CA    . GLU A 1 224 ? -14.566 7.700   3.486   1.00 104.60 ? 168 GLU A CA    1 
ATOM   1638 C  C     . GLU A 1 224 ? -15.278 7.942   4.799   1.00 108.08 ? 168 GLU A C     1 
ATOM   1639 O  O     . GLU A 1 224 ? -15.715 9.060   5.103   1.00 110.44 ? 168 GLU A O     1 
ATOM   1640 C  CB    . GLU A 1 224 ? -15.188 6.462   2.812   1.00 101.92 ? 168 GLU A CB    1 
ATOM   1641 C  CG    . GLU A 1 224 ? -16.673 6.493   2.386   1.00 105.67 ? 168 GLU A CG    1 
ATOM   1642 C  CD    . GLU A 1 224 ? -17.051 7.596   1.378   1.00 111.20 ? 168 GLU A CD    1 
ATOM   1643 O  OE1   . GLU A 1 224 ? -16.270 8.544   1.131   1.00 107.59 ? 168 GLU A OE1   1 
ATOM   1644 O  OE2   . GLU A 1 224 ? -18.156 7.495   0.805   1.00 111.90 ? 168 GLU A OE2   1 
ATOM   1645 N  N     . ARG A 1 225 ? -15.421 6.870   5.569   1.00 105.90 ? 169 ARG A N     1 
ATOM   1646 C  CA    . ARG A 1 225 ? -16.154 6.937   6.829   1.00 109.50 ? 169 ARG A CA    1 
ATOM   1647 C  C     . ARG A 1 225 ? -15.206 6.978   8.031   1.00 105.33 ? 169 ARG A C     1 
ATOM   1648 O  O     . ARG A 1 225 ? -15.283 6.183   8.970   1.00 103.79 ? 169 ARG A O     1 
ATOM   1649 C  CB    . ARG A 1 225 ? -17.144 5.780   6.918   1.00 112.10 ? 169 ARG A CB    1 
ATOM   1650 C  CG    . ARG A 1 225 ? -18.301 5.880   5.896   1.00 110.45 ? 169 ARG A CG    1 
ATOM   1651 C  CD    . ARG A 1 225 ? -18.459 7.286   5.279   1.00 106.24 ? 169 ARG A CD    1 
ATOM   1652 N  NE    . ARG A 1 225 ? -19.811 7.639   4.859   1.00 112.43 ? 169 ARG A NE    1 
ATOM   1653 C  CZ    . ARG A 1 225 ? -20.096 8.722   4.138   1.00 116.20 ? 169 ARG A CZ    1 
ATOM   1654 N  NH1   . ARG A 1 225 ? -19.123 9.547   3.768   1.00 114.39 ? 169 ARG A NH1   1 
ATOM   1655 N  NH2   . ARG A 1 225 ? -21.349 8.995   3.798   1.00 111.18 ? 169 ARG A NH2   1 
ATOM   1656 N  N     . SER A 1 226 ? -14.268 7.919   7.963   1.00 104.10 ? 170 SER A N     1 
ATOM   1657 C  CA    . SER A 1 226 ? -13.334 8.252   9.031   1.00 103.95 ? 170 SER A CA    1 
ATOM   1658 C  C     . SER A 1 226 ? -13.986 9.093   10.128  1.00 104.48 ? 170 SER A C     1 
ATOM   1659 O  O     . SER A 1 226 ? -15.174 9.415   10.054  1.00 106.36 ? 170 SER A O     1 
ATOM   1660 C  CB    . SER A 1 226 ? -12.142 8.994   8.427   1.00 101.16 ? 170 SER A CB    1 
ATOM   1661 O  OG    . SER A 1 226 ? -11.603 9.930   9.335   1.00 105.85 ? 170 SER A OG    1 
ATOM   1662 N  N     . SER B 1 4   ? 22.007  -14.038 10.535  1.00 91.05  ? -35 SER B N     1 
ATOM   1663 C  CA    . SER B 1 4   ? 22.194  -13.703 11.942  1.00 97.38  ? -35 SER B CA    1 
ATOM   1664 C  C     . SER B 1 4   ? 22.983  -12.387 12.095  1.00 98.68  ? -35 SER B C     1 
ATOM   1665 O  O     . SER B 1 4   ? 22.486  -11.337 11.663  1.00 90.91  ? -35 SER B O     1 
ATOM   1666 C  CB    . SER B 1 4   ? 22.883  -14.862 12.680  1.00 95.04  ? -35 SER B CB    1 
ATOM   1667 O  OG    . SER B 1 4   ? 22.352  -16.123 12.289  1.00 86.38  ? -35 SER B OG    1 
ATOM   1668 N  N     . PHE B 1 5   ? 24.171  -12.463 12.730  1.00 101.39 ? -34 PHE B N     1 
ATOM   1669 C  CA    . PHE B 1 5   ? 24.940  -11.312 13.219  1.00 100.18 ? -34 PHE B CA    1 
ATOM   1670 C  C     . PHE B 1 5   ? 23.986  -10.215 13.672  1.00 100.49 ? -34 PHE B C     1 
ATOM   1671 O  O     . PHE B 1 5   ? 23.949  -9.121  13.097  1.00 94.30  ? -34 PHE B O     1 
ATOM   1672 C  CB    . PHE B 1 5   ? 25.920  -10.772 12.163  1.00 97.49  ? -34 PHE B CB    1 
ATOM   1673 C  CG    . PHE B 1 5   ? 27.052  -9.910  12.731  1.00 99.38  ? -34 PHE B CG    1 
ATOM   1674 C  CD1   . PHE B 1 5   ? 26.863  -9.123  13.868  1.00 99.38  ? -34 PHE B CD1   1 
ATOM   1675 C  CD2   . PHE B 1 5   ? 28.300  -9.895  12.122  1.00 100.29 ? -34 PHE B CD2   1 
ATOM   1676 C  CE1   . PHE B 1 5   ? 27.883  -8.345  14.383  1.00 95.79  ? -34 PHE B CE1   1 
ATOM   1677 C  CE2   . PHE B 1 5   ? 29.325  -9.124  12.636  1.00 102.28 ? -34 PHE B CE2   1 
ATOM   1678 C  CZ    . PHE B 1 5   ? 29.115  -8.347  13.769  1.00 97.67  ? -34 PHE B CZ    1 
ATOM   1679 N  N     . LEU B 1 6   ? 23.246  -10.524 14.731  1.00 104.84 ? -33 LEU B N     1 
ATOM   1680 C  CA    . LEU B 1 6   ? 22.181  -9.734  15.326  1.00 98.03  ? -33 LEU B CA    1 
ATOM   1681 C  C     . LEU B 1 6   ? 21.405  -10.704 16.190  1.00 92.10  ? -33 LEU B C     1 
ATOM   1682 O  O     . LEU B 1 6   ? 20.610  -11.499 15.674  1.00 92.59  ? -33 LEU B O     1 
ATOM   1683 C  CB    . LEU B 1 6   ? 21.278  -9.091  14.277  1.00 96.75  ? -33 LEU B CB    1 
ATOM   1684 C  CG    . LEU B 1 6   ? 20.024  -8.427  14.842  1.00 95.43  ? -33 LEU B CG    1 
ATOM   1685 C  CD1   . LEU B 1 6   ? 20.391  -7.072  15.456  1.00 96.50  ? -33 LEU B CD1   1 
ATOM   1686 C  CD2   . LEU B 1 6   ? 18.935  -8.307  13.768  1.00 89.15  ? -33 LEU B CD2   1 
ATOM   1687 N  N     . THR B 1 7   ? 21.670  -10.679 17.492  1.00 89.00  ? -32 THR B N     1 
ATOM   1688 C  CA    . THR B 1 7   ? 21.052  -11.626 18.404  1.00 86.76  ? -32 THR B CA    1 
ATOM   1689 C  C     . THR B 1 7   ? 19.547  -11.674 18.188  1.00 87.01  ? -32 THR B C     1 
ATOM   1690 O  O     . THR B 1 7   ? 18.920  -10.656 17.874  1.00 87.36  ? -32 THR B O     1 
ATOM   1691 C  CB    . THR B 1 7   ? 21.375  -11.222 19.842  1.00 86.77  ? -32 THR B CB    1 
ATOM   1692 O  OG1   . THR B 1 7   ? 22.781  -10.951 19.953  1.00 96.52  ? -32 THR B OG1   1 
ATOM   1693 C  CG2   . THR B 1 7   ? 21.012  -12.337 20.817  1.00 85.84  ? -32 THR B CG2   1 
ATOM   1694 N  N     . GLU B 1 8   ? 18.970  -12.876 18.298  1.00 91.38  ? -31 GLU B N     1 
ATOM   1695 C  CA    . GLU B 1 8   ? 17.516  -12.961 18.344  1.00 88.45  ? -31 GLU B CA    1 
ATOM   1696 C  C     . GLU B 1 8   ? 16.993  -12.298 19.616  1.00 81.04  ? -31 GLU B C     1 
ATOM   1697 O  O     . GLU B 1 8   ? 15.953  -11.628 19.595  1.00 79.52  ? -31 GLU B O     1 
ATOM   1698 C  CB    . GLU B 1 8   ? 17.061  -14.418 18.228  1.00 73.16  ? -31 GLU B CB    1 
ATOM   1699 N  N     . GLU B 1 9   ? 17.731  -12.429 20.723  1.00 77.25  ? -30 GLU B N     1 
ATOM   1700 C  CA    . GLU B 1 9   ? 17.400  -11.663 21.921  1.00 80.93  ? -30 GLU B CA    1 
ATOM   1701 C  C     . GLU B 1 9   ? 17.527  -10.167 21.676  1.00 79.58  ? -30 GLU B C     1 
ATOM   1702 O  O     . GLU B 1 9   ? 16.800  -9.377  22.287  1.00 72.68  ? -30 GLU B O     1 
ATOM   1703 C  CB    . GLU B 1 9   ? 18.292  -12.083 23.089  1.00 79.73  ? -30 GLU B CB    1 
ATOM   1704 N  N     . GLU B 1 10  ? 18.429  -9.752  20.782  1.00 82.32  ? -29 GLU B N     1 
ATOM   1705 C  CA    . GLU B 1 10  ? 18.503  -8.335  20.435  1.00 76.33  ? -29 GLU B CA    1 
ATOM   1706 C  C     . GLU B 1 10  ? 17.308  -7.913  19.582  1.00 69.56  ? -29 GLU B C     1 
ATOM   1707 O  O     . GLU B 1 10  ? 16.740  -6.833  19.785  1.00 63.08  ? -29 GLU B O     1 
ATOM   1708 C  CB    . GLU B 1 10  ? 19.820  -8.030  19.712  1.00 76.78  ? -29 GLU B CB    1 
ATOM   1709 C  CG    . GLU B 1 10  ? 20.920  -7.398  20.585  1.00 80.62  ? -29 GLU B CG    1 
ATOM   1710 C  CD    . GLU B 1 10  ? 21.896  -6.543  19.771  1.00 81.69  ? -29 GLU B CD    1 
ATOM   1711 O  OE1   . GLU B 1 10  ? 21.980  -6.754  18.534  1.00 86.65  ? -29 GLU B OE1   1 
ATOM   1712 O  OE2   . GLU B 1 10  ? 22.575  -5.662  20.359  1.00 67.80  ? -29 GLU B OE2   1 
ATOM   1713 N  N     . GLN B 1 11  ? 16.890  -8.758  18.640  1.00 75.22  ? -28 GLN B N     1 
ATOM   1714 C  CA    . GLN B 1 11  ? 15.871  -8.317  17.692  1.00 74.09  ? -28 GLN B CA    1 
ATOM   1715 C  C     . GLN B 1 11  ? 14.477  -8.339  18.308  1.00 63.69  ? -28 GLN B C     1 
ATOM   1716 O  O     . GLN B 1 11  ? 13.696  -7.405  18.098  1.00 62.01  ? -28 GLN B O     1 
ATOM   1717 C  CB    . GLN B 1 11  ? 15.908  -9.169  16.413  1.00 74.81  ? -28 GLN B CB    1 
ATOM   1718 C  CG    . GLN B 1 11  ? 14.932  -8.679  15.332  1.00 67.14  ? -28 GLN B CG    1 
ATOM   1719 C  CD    . GLN B 1 11  ? 15.482  -8.798  13.910  1.00 72.34  ? -28 GLN B CD    1 
ATOM   1720 O  OE1   . GLN B 1 11  ? 15.425  -7.841  13.126  1.00 66.72  ? -28 GLN B OE1   1 
ATOM   1721 N  NE2   . GLN B 1 11  ? 15.991  -9.984  13.562  1.00 74.37  ? -28 GLN B NE2   1 
ATOM   1722 N  N     . GLU B 1 12  ? 14.130  -9.388  19.055  1.00 64.25  ? -27 GLU B N     1 
ATOM   1723 C  CA    . GLU B 1 12  ? 12.760  -9.457  19.554  1.00 66.33  ? -27 GLU B CA    1 
ATOM   1724 C  C     . GLU B 1 12  ? 12.504  -8.403  20.626  1.00 64.16  ? -27 GLU B C     1 
ATOM   1725 O  O     . GLU B 1 12  ? 11.349  -8.002  20.829  1.00 64.13  ? -27 GLU B O     1 
ATOM   1726 C  CB    . GLU B 1 12  ? 12.432  -10.879 20.054  1.00 67.44  ? -27 GLU B CB    1 
ATOM   1727 C  CG    . GLU B 1 12  ? 10.939  -11.291 19.875  1.00 66.17  ? -27 GLU B CG    1 
ATOM   1728 C  CD    . GLU B 1 12  ? 10.484  -11.342 18.404  1.00 85.18  ? -27 GLU B CD    1 
ATOM   1729 O  OE1   . GLU B 1 12  ? 11.316  -11.645 17.520  1.00 90.68  ? -27 GLU B OE1   1 
ATOM   1730 O  OE2   . GLU B 1 12  ? 9.286   -11.075 18.122  1.00 89.32  ? -27 GLU B OE2   1 
ATOM   1731 N  N     . ALA B 1 13  ? 13.555  -7.920  21.289  1.00 60.77  ? -26 ALA B N     1 
ATOM   1732 C  CA    . ALA B 1 13  ? 13.420  -6.732  22.128  1.00 57.42  ? -26 ALA B CA    1 
ATOM   1733 C  C     . ALA B 1 13  ? 12.927  -5.532  21.316  1.00 54.72  ? -26 ALA B C     1 
ATOM   1734 O  O     . ALA B 1 13  ? 11.999  -4.823  21.730  1.00 52.51  ? -26 ALA B O     1 
ATOM   1735 C  CB    . ALA B 1 13  ? 14.756  -6.415  22.804  1.00 55.03  ? -26 ALA B CB    1 
ATOM   1736 N  N     . ILE B 1 14  ? 13.542  -5.285  20.154  1.00 53.78  ? -25 ILE B N     1 
ATOM   1737 C  CA    . ILE B 1 14  ? 13.106  -4.189  19.291  1.00 51.03  ? -25 ILE B CA    1 
ATOM   1738 C  C     . ILE B 1 14  ? 11.684  -4.421  18.796  1.00 50.95  ? -25 ILE B C     1 
ATOM   1739 O  O     . ILE B 1 14  ? 10.870  -3.489  18.742  1.00 47.58  ? -25 ILE B O     1 
ATOM   1740 C  CB    . ILE B 1 14  ? 14.089  -4.017  18.123  1.00 51.15  ? -25 ILE B CB    1 
ATOM   1741 C  CG1   . ILE B 1 14  ? 15.523  -4.130  18.637  1.00 56.51  ? -25 ILE B CG1   1 
ATOM   1742 C  CG2   . ILE B 1 14  ? 13.865  -2.693  17.434  1.00 52.89  ? -25 ILE B CG2   1 
ATOM   1743 C  CD1   . ILE B 1 14  ? 16.567  -3.706  17.635  1.00 55.50  ? -25 ILE B CD1   1 
ATOM   1744 N  N     . MET B 1 15  ? 11.356  -5.661  18.429  1.00 47.54  ? -24 MET B N     1 
ATOM   1745 C  CA    . MET B 1 15  ? 9.985   -5.945  18.040  1.00 49.03  ? -24 MET B CA    1 
ATOM   1746 C  C     . MET B 1 15  ? 9.043   -5.799  19.214  1.00 52.04  ? -24 MET B C     1 
ATOM   1747 O  O     . MET B 1 15  ? 7.864   -5.472  19.015  1.00 49.85  ? -24 MET B O     1 
ATOM   1748 C  CB    . MET B 1 15  ? 9.864   -7.346  17.442  1.00 61.69  ? -24 MET B CB    1 
ATOM   1749 C  CG    . MET B 1 15  ? 10.942  -7.703  16.432  1.00 69.27  ? -24 MET B CG    1 
ATOM   1750 S  SD    . MET B 1 15  ? 10.584  -6.934  14.846  1.00 66.93  ? -24 MET B SD    1 
ATOM   1751 C  CE    . MET B 1 15  ? 8.969   -7.659  14.486  1.00 61.38  ? -24 MET B CE    1 
ATOM   1752 N  N     . LYS B 1 16  ? 9.538   -6.048  20.438  1.00 54.93  ? -23 LYS B N     1 
ATOM   1753 C  CA    . LYS B 1 16  ? 8.752   -5.732  21.629  1.00 51.07  ? -23 LYS B CA    1 
ATOM   1754 C  C     . LYS B 1 16  ? 8.479   -4.234  21.709  1.00 48.88  ? -23 LYS B C     1 
ATOM   1755 O  O     . LYS B 1 16  ? 7.328   -3.810  21.876  1.00 46.01  ? -23 LYS B O     1 
ATOM   1756 C  CB    . LYS B 1 16  ? 9.472   -6.220  22.882  1.00 56.32  ? -23 LYS B CB    1 
ATOM   1757 C  CG    . LYS B 1 16  ? 8.735   -7.306  23.674  1.00 66.22  ? -23 LYS B CG    1 
ATOM   1758 C  CD    . LYS B 1 16  ? 9.564   -7.757  24.885  1.00 71.74  ? -23 LYS B CD    1 
ATOM   1759 C  CE    . LYS B 1 16  ? 10.495  -8.900  24.498  1.00 70.80  ? -23 LYS B CE    1 
ATOM   1760 N  NZ    . LYS B 1 16  ? 11.636  -9.067  25.432  1.00 63.05  ? -23 LYS B NZ    1 
ATOM   1761 N  N     . VAL B 1 17  ? 9.533   -3.417  21.557  1.00 50.23  ? -22 VAL B N     1 
ATOM   1762 C  CA    . VAL B 1 17  ? 9.389   -1.962  21.461  1.00 46.70  ? -22 VAL B CA    1 
ATOM   1763 C  C     . VAL B 1 17  ? 8.426   -1.588  20.343  1.00 50.10  ? -22 VAL B C     1 
ATOM   1764 O  O     . VAL B 1 17  ? 7.581   -0.692  20.497  1.00 49.47  ? -22 VAL B O     1 
ATOM   1765 C  CB    . VAL B 1 17  ? 10.768  -1.304  21.250  1.00 50.60  ? -22 VAL B CB    1 
ATOM   1766 C  CG1   . VAL B 1 17  ? 10.644  0.223   21.183  1.00 48.12  ? -22 VAL B CG1   1 
ATOM   1767 C  CG2   . VAL B 1 17  ? 11.739  -1.722  22.347  1.00 43.27  ? -22 VAL B CG2   1 
ATOM   1768 N  N     . LEU B 1 18  ? 8.536   -2.275  19.199  1.00 52.23  ? -21 LEU B N     1 
ATOM   1769 C  CA    . LEU B 1 18  ? 7.661   -2.001  18.069  1.00 39.73  ? -21 LEU B CA    1 
ATOM   1770 C  C     . LEU B 1 18  ? 6.223   -2.407  18.362  1.00 43.70  ? -21 LEU B C     1 
ATOM   1771 O  O     . LEU B 1 18  ? 5.290   -1.676  18.024  1.00 48.79  ? -21 LEU B O     1 
ATOM   1772 C  CB    . LEU B 1 18  ? 8.194   -2.714  16.836  1.00 51.50  ? -21 LEU B CB    1 
ATOM   1773 C  CG    . LEU B 1 18  ? 9.398   -2.017  16.179  1.00 54.66  ? -21 LEU B CG    1 
ATOM   1774 C  CD1   . LEU B 1 18  ? 10.020  -2.891  15.099  1.00 50.13  ? -21 LEU B CD1   1 
ATOM   1775 C  CD2   . LEU B 1 18  ? 9.003   -0.676  15.608  1.00 53.55  ? -21 LEU B CD2   1 
ATOM   1776 N  N     . GLN B 1 19  ? 6.018   -3.556  19.008  1.00 50.61  ? -20 GLN B N     1 
ATOM   1777 C  CA    . GLN B 1 19  ? 4.661   -3.987  19.331  1.00 53.34  ? -20 GLN B CA    1 
ATOM   1778 C  C     . GLN B 1 19  ? 4.005   -3.060  20.356  1.00 56.88  ? -20 GLN B C     1 
ATOM   1779 O  O     . GLN B 1 19  ? 2.829   -2.702  20.207  1.00 56.42  ? -20 GLN B O     1 
ATOM   1780 C  CB    . GLN B 1 19  ? 4.683   -5.435  19.825  1.00 59.20  ? -20 GLN B CB    1 
ATOM   1781 C  CG    . GLN B 1 19  ? 3.358   -5.925  20.401  1.00 70.06  ? -20 GLN B CG    1 
ATOM   1782 C  CD    . GLN B 1 19  ? 3.514   -7.150  21.300  1.00 80.31  ? -20 GLN B CD    1 
ATOM   1783 O  OE1   . GLN B 1 19  ? 4.463   -7.933  21.160  1.00 82.32  ? -20 GLN B OE1   1 
ATOM   1784 N  NE2   . GLN B 1 19  ? 2.582   -7.310  22.240  1.00 85.82  ? -20 GLN B NE2   1 
ATOM   1785 N  N     . ARG B 1 20  ? 4.748   -2.654  21.394  1.00 47.25  ? -19 ARG B N     1 
ATOM   1786 C  CA    . ARG B 1 20  ? 4.200   -1.729  22.384  1.00 50.81  ? -19 ARG B CA    1 
ATOM   1787 C  C     . ARG B 1 20  ? 3.662   -0.466  21.718  1.00 53.98  ? -19 ARG B C     1 
ATOM   1788 O  O     . ARG B 1 20  ? 2.527   -0.039  21.983  1.00 51.59  ? -19 ARG B O     1 
ATOM   1789 C  CB    . ARG B 1 20  ? 5.270   -1.363  23.421  1.00 53.91  ? -19 ARG B CB    1 
ATOM   1790 C  CG    . ARG B 1 20  ? 5.776   -2.515  24.279  1.00 46.80  ? -19 ARG B CG    1 
ATOM   1791 C  CD    . ARG B 1 20  ? 6.448   -1.993  25.544  1.00 48.22  ? -19 ARG B CD    1 
ATOM   1792 N  NE    . ARG B 1 20  ? 7.770   -1.411  25.323  1.00 47.03  ? -19 ARG B NE    1 
ATOM   1793 C  CZ    . ARG B 1 20  ? 8.121   -0.175  25.695  1.00 56.45  ? -19 ARG B CZ    1 
ATOM   1794 N  NH1   . ARG B 1 20  ? 7.237   0.627   26.314  1.00 50.88  ? -19 ARG B NH1   1 
ATOM   1795 N  NH2   . ARG B 1 20  ? 9.363   0.267   25.455  1.00 45.21  ? -19 ARG B NH2   1 
ATOM   1796 N  N     . ASP B 1 21  ? 4.473   0.134   20.833  1.00 53.21  ? -18 ASP B N     1 
ATOM   1797 C  CA    . ASP B 1 21  ? 4.094   1.376   20.163  1.00 54.76  ? -18 ASP B CA    1 
ATOM   1798 C  C     . ASP B 1 21  ? 2.849   1.208   19.299  1.00 55.50  ? -18 ASP B C     1 
ATOM   1799 O  O     . ASP B 1 21  ? 2.036   2.131   19.185  1.00 52.69  ? -18 ASP B O     1 
ATOM   1800 C  CB    . ASP B 1 21  ? 5.259   1.879   19.314  1.00 59.16  ? -18 ASP B CB    1 
ATOM   1801 C  CG    . ASP B 1 21  ? 4.926   3.168   18.560  1.00 62.93  ? -18 ASP B CG    1 
ATOM   1802 O  OD1   . ASP B 1 21  ? 4.735   4.223   19.217  1.00 61.63  ? -18 ASP B OD1   1 
ATOM   1803 O  OD2   . ASP B 1 21  ? 4.863   3.125   17.307  1.00 67.20  ? -18 ASP B OD2   1 
ATOM   1804 N  N     . ALA B 1 22  ? 2.681   0.047   18.669  1.00 54.74  ? -17 ALA B N     1 
ATOM   1805 C  CA    . ALA B 1 22  ? 1.483   -0.154  17.865  1.00 59.51  ? -17 ALA B CA    1 
ATOM   1806 C  C     . ALA B 1 22  ? 0.242   -0.162  18.746  1.00 57.66  ? -17 ALA B C     1 
ATOM   1807 O  O     . ALA B 1 22  ? -0.717  0.575   18.492  1.00 61.06  ? -17 ALA B O     1 
ATOM   1808 C  CB    . ALA B 1 22  ? 1.592   -1.443  17.053  1.00 62.23  ? -17 ALA B CB    1 
ATOM   1809 N  N     . ALA B 1 23  ? 0.255   -0.976  19.803  1.00 59.77  ? -16 ALA B N     1 
ATOM   1810 C  CA    . ALA B 1 23  ? -0.852  -0.988  20.755  1.00 61.98  ? -16 ALA B CA    1 
ATOM   1811 C  C     . ALA B 1 23  ? -1.158  0.414   21.272  1.00 65.57  ? -16 ALA B C     1 
ATOM   1812 O  O     . ALA B 1 23  ? -2.314  0.860   21.237  1.00 66.56  ? -16 ALA B O     1 
ATOM   1813 C  CB    . ALA B 1 23  ? -0.527  -1.925  21.918  1.00 59.04  ? -16 ALA B CB    1 
ATOM   1814 N  N     . LEU B 1 24  ? -0.128  1.122   21.758  1.00 59.16  ? -15 LEU B N     1 
ATOM   1815 C  CA    . LEU B 1 24  ? -0.317  2.476   22.269  1.00 55.82  ? -15 LEU B CA    1 
ATOM   1816 C  C     . LEU B 1 24  ? -1.099  3.340   21.287  1.00 63.24  ? -15 LEU B C     1 
ATOM   1817 O  O     . LEU B 1 24  ? -2.037  4.041   21.675  1.00 65.56  ? -15 LEU B O     1 
ATOM   1818 C  CB    . LEU B 1 24  ? 1.036   3.117   22.577  1.00 56.64  ? -15 LEU B CB    1 
ATOM   1819 C  CG    . LEU B 1 24  ? 1.050   4.612   22.970  1.00 68.92  ? -15 LEU B CG    1 
ATOM   1820 C  CD1   . LEU B 1 24  ? -0.051  4.976   23.984  1.00 74.40  ? -15 LEU B CD1   1 
ATOM   1821 C  CD2   . LEU B 1 24  ? 2.418   5.048   23.524  1.00 64.16  ? -15 LEU B CD2   1 
ATOM   1822 N  N     . LYS B 1 25  ? -0.733  3.290   20.002  1.00 68.13  ? -14 LYS B N     1 
ATOM   1823 C  CA    . LYS B 1 25  ? -1.389  4.128   19.001  1.00 61.10  ? -14 LYS B CA    1 
ATOM   1824 C  C     . LYS B 1 25  ? -2.803  3.640   18.709  1.00 66.74  ? -14 LYS B C     1 
ATOM   1825 O  O     . LYS B 1 25  ? -3.745  4.437   18.662  1.00 71.07  ? -14 LYS B O     1 
ATOM   1826 C  CB    . LYS B 1 25  ? -0.554  4.164   17.723  1.00 60.54  ? -14 LYS B CB    1 
ATOM   1827 C  CG    . LYS B 1 25  ? 0.904   4.548   17.947  1.00 62.08  ? -14 LYS B CG    1 
ATOM   1828 C  CD    . LYS B 1 25  ? 1.113   6.045   17.934  1.00 63.26  ? -14 LYS B CD    1 
ATOM   1829 C  CE    . LYS B 1 25  ? 2.421   6.450   17.256  1.00 66.62  ? -14 LYS B CE    1 
ATOM   1830 N  NZ    . LYS B 1 25  ? 3.659   6.208   18.040  1.00 59.28  ? -14 LYS B NZ    1 
ATOM   1831 N  N     . ARG B 1 26  ? -2.973  2.330   18.508  1.00 68.94  ? -13 ARG B N     1 
ATOM   1832 C  CA    . ARG B 1 26  ? -4.314  1.781   18.323  1.00 70.24  ? -13 ARG B CA    1 
ATOM   1833 C  C     . ARG B 1 26  ? -5.232  2.129   19.487  1.00 71.81  ? -13 ARG B C     1 
ATOM   1834 O  O     . ARG B 1 26  ? -6.444  2.265   19.296  1.00 76.14  ? -13 ARG B O     1 
ATOM   1835 C  CB    . ARG B 1 26  ? -4.254  0.264   18.146  1.00 67.61  ? -13 ARG B CB    1 
ATOM   1836 C  CG    . ARG B 1 26  ? -3.640  -0.198  16.848  1.00 59.49  ? -13 ARG B CG    1 
ATOM   1837 C  CD    . ARG B 1 26  ? -3.847  -1.692  16.686  1.00 64.44  ? -13 ARG B CD    1 
ATOM   1838 N  NE    . ARG B 1 26  ? -3.551  -2.429  17.914  1.00 65.30  ? -13 ARG B NE    1 
ATOM   1839 C  CZ    . ARG B 1 26  ? -2.480  -3.200  18.073  1.00 68.28  ? -13 ARG B CZ    1 
ATOM   1840 N  NH1   . ARG B 1 26  ? -1.611  -3.323  17.071  1.00 62.31  ? -13 ARG B NH1   1 
ATOM   1841 N  NH2   . ARG B 1 26  ? -2.274  -3.841  19.226  1.00 68.10  ? -13 ARG B NH2   1 
ATOM   1842 N  N     . ALA B 1 27  ? -4.683  2.271   20.695  1.00 72.45  ? -12 ALA B N     1 
ATOM   1843 C  CA    . ALA B 1 27  ? -5.500  2.703   21.828  1.00 77.07  ? -12 ALA B CA    1 
ATOM   1844 C  C     . ALA B 1 27  ? -5.908  4.167   21.683  1.00 80.68  ? -12 ALA B C     1 
ATOM   1845 O  O     . ALA B 1 27  ? -7.102  4.498   21.677  1.00 81.89  ? -12 ALA B O     1 
ATOM   1846 C  CB    . ALA B 1 27  ? -4.745  2.482   23.138  1.00 61.09  ? -12 ALA B CB    1 
ATOM   1847 N  N     . GLU B 1 28  ? -4.924  5.063   21.538  1.00 76.89  ? -11 GLU B N     1 
ATOM   1848 C  CA    . GLU B 1 28  ? -5.196  6.493   21.534  1.00 80.38  ? -11 GLU B CA    1 
ATOM   1849 C  C     . GLU B 1 28  ? -5.923  6.972   20.264  1.00 86.06  ? -11 GLU B C     1 
ATOM   1850 O  O     . GLU B 1 28  ? -6.097  8.193   20.149  1.00 91.36  ? -11 GLU B O     1 
ATOM   1851 C  CB    . GLU B 1 28  ? -3.898  7.282   21.725  1.00 74.82  ? -11 GLU B CB    1 
ATOM   1852 C  CG    . GLU B 1 28  ? -3.353  7.235   23.150  1.00 79.56  ? -11 GLU B CG    1 
ATOM   1853 C  CD    . GLU B 1 28  ? -4.194  8.036   24.158  1.00 94.07  ? -11 GLU B CD    1 
ATOM   1854 O  OE1   . GLU B 1 28  ? -4.771  9.083   23.770  1.00 91.76  ? -11 GLU B OE1   1 
ATOM   1855 O  OE2   . GLU B 1 28  ? -4.280  7.610   25.344  1.00 96.76  ? -11 GLU B OE2   1 
ATOM   1856 N  N     . GLU B 1 29  ? -6.325  6.109   19.327  1.00 89.13  ? -10 GLU B N     1 
ATOM   1857 C  CA    . GLU B 1 29  ? -7.254  6.482   18.260  1.00 94.07  ? -10 GLU B CA    1 
ATOM   1858 C  C     . GLU B 1 29  ? -8.478  5.564   18.253  1.00 94.66  ? -10 GLU B C     1 
ATOM   1859 O  O     . GLU B 1 29  ? -9.222  5.510   17.264  1.00 93.38  ? -10 GLU B O     1 
ATOM   1860 C  CB    . GLU B 1 29  ? -6.549  6.519   16.890  1.00 83.28  ? -10 GLU B CB    1 
ATOM   1861 C  CG    . GLU B 1 29  ? -6.459  5.210   16.079  1.00 85.32  ? -10 GLU B CG    1 
ATOM   1862 C  CD    . GLU B 1 29  ? -5.527  5.331   14.849  1.00 95.68  ? -10 GLU B CD    1 
ATOM   1863 O  OE1   . GLU B 1 29  ? -5.431  4.360   14.064  1.00 89.98  ? -10 GLU B OE1   1 
ATOM   1864 O  OE2   . GLU B 1 29  ? -4.887  6.394   14.662  1.00 95.00  ? -10 GLU B OE2   1 
ATOM   1865 N  N     . GLU B 1 30  ? -8.695  4.852   19.359  1.00 91.45  ? -9  GLU B N     1 
ATOM   1866 C  CA    . GLU B 1 30  ? -9.882  4.033   19.582  1.00 95.86  ? -9  GLU B CA    1 
ATOM   1867 C  C     . GLU B 1 30  ? -10.860 4.751   20.520  1.00 93.71  ? -9  GLU B C     1 
ATOM   1868 O  O     . GLU B 1 30  ? -10.454 5.561   21.357  1.00 89.26  ? -9  GLU B O     1 
ATOM   1869 C  CB    . GLU B 1 30  ? -9.493  2.671   20.171  1.00 87.76  ? -9  GLU B CB    1 
ATOM   1870 N  N     . TYR B 1 44  ? -7.129  9.800   27.913  1.00 108.72 ? -8  TYR B N     1 
ATOM   1871 C  CA    . TYR B 1 44  ? -6.682  11.192  27.923  1.00 102.83 ? -8  TYR B CA    1 
ATOM   1872 C  C     . TYR B 1 44  ? -6.947  11.859  26.582  1.00 108.06 ? -8  TYR B C     1 
ATOM   1873 O  O     . TYR B 1 44  ? -7.353  11.204  25.615  1.00 112.22 ? -8  TYR B O     1 
ATOM   1874 C  CB    . TYR B 1 44  ? -5.196  11.280  28.269  1.00 97.36  ? -8  TYR B CB    1 
ATOM   1875 C  CG    . TYR B 1 44  ? -4.791  10.299  29.343  1.00 108.25 ? -8  TYR B CG    1 
ATOM   1876 C  CD1   . TYR B 1 44  ? -3.728  9.421   29.151  1.00 103.80 ? -8  TYR B CD1   1 
ATOM   1877 C  CD2   . TYR B 1 44  ? -5.490  10.235  30.550  1.00 109.85 ? -8  TYR B CD2   1 
ATOM   1878 C  CE1   . TYR B 1 44  ? -3.369  8.507   30.143  1.00 102.01 ? -8  TYR B CE1   1 
ATOM   1879 C  CE2   . TYR B 1 44  ? -5.138  9.331   31.539  1.00 105.69 ? -8  TYR B CE2   1 
ATOM   1880 C  CZ    . TYR B 1 44  ? -4.079  8.472   31.331  1.00 102.10 ? -8  TYR B CZ    1 
ATOM   1881 O  OH    . TYR B 1 44  ? -3.733  7.576   32.315  1.00 107.85 ? -8  TYR B OH    1 
ATOM   1882 N  N     . ASP B 1 45  ? -6.711  13.170  26.527  1.00 104.21 ? -7  ASP B N     1 
ATOM   1883 C  CA    . ASP B 1 45  ? -7.046  13.955  25.342  1.00 105.81 ? -7  ASP B CA    1 
ATOM   1884 C  C     . ASP B 1 45  ? -5.961  13.832  24.277  1.00 103.27 ? -7  ASP B C     1 
ATOM   1885 O  O     . ASP B 1 45  ? -6.101  13.053  23.327  1.00 101.71 ? -7  ASP B O     1 
ATOM   1886 C  CB    . ASP B 1 45  ? -7.271  15.427  25.718  1.00 104.19 ? -7  ASP B CB    1 
ATOM   1887 C  CG    . ASP B 1 45  ? -8.630  15.667  26.380  1.00 114.08 ? -7  ASP B CG    1 
ATOM   1888 O  OD1   . ASP B 1 45  ? -9.544  16.174  25.690  1.00 111.10 ? -7  ASP B OD1   1 
ATOM   1889 O  OD2   . ASP B 1 45  ? -8.783  15.349  27.586  1.00 108.34 ? -7  ASP B OD2   1 
ATOM   1890 N  N     . TYR B 1 46  ? -4.874  14.583  24.433  1.00 99.96  ? -6  TYR B N     1 
ATOM   1891 C  CA    . TYR B 1 46  ? -3.795  14.560  23.458  1.00 91.75  ? -6  TYR B CA    1 
ATOM   1892 C  C     . TYR B 1 46  ? -2.829  13.403  23.731  1.00 87.16  ? -6  TYR B C     1 
ATOM   1893 O  O     . TYR B 1 46  ? -2.757  12.855  24.838  1.00 85.04  ? -6  TYR B O     1 
ATOM   1894 C  CB    . TYR B 1 46  ? -3.019  15.879  23.473  1.00 87.55  ? -6  TYR B CB    1 
ATOM   1895 C  CG    . TYR B 1 46  ? -3.744  17.083  22.898  1.00 93.70  ? -6  TYR B CG    1 
ATOM   1896 C  CD1   . TYR B 1 46  ? -3.042  18.240  22.576  1.00 95.08  ? -6  TYR B CD1   1 
ATOM   1897 C  CD2   . TYR B 1 46  ? -5.124  17.075  22.688  1.00 97.18  ? -6  TYR B CD2   1 
ATOM   1898 C  CE1   . TYR B 1 46  ? -3.689  19.355  22.054  1.00 98.39  ? -6  TYR B CE1   1 
ATOM   1899 C  CE2   . TYR B 1 46  ? -5.782  18.191  22.166  1.00 92.89  ? -6  TYR B CE2   1 
ATOM   1900 C  CZ    . TYR B 1 46  ? -5.055  19.324  21.851  1.00 95.94  ? -6  TYR B CZ    1 
ATOM   1901 O  OH    . TYR B 1 46  ? -5.686  20.433  21.335  1.00 96.85  ? -6  TYR B OH    1 
ATOM   1902 N  N     . LEU B 1 47  ? -2.096  13.026  22.684  1.00 78.66  ? -5  LEU B N     1 
ATOM   1903 C  CA    . LEU B 1 47  ? -0.934  12.150  22.783  1.00 71.04  ? -5  LEU B CA    1 
ATOM   1904 C  C     . LEU B 1 47  ? 0.210   12.858  22.077  1.00 70.96  ? -5  LEU B C     1 
ATOM   1905 O  O     . LEU B 1 47  ? 0.097   13.181  20.889  1.00 71.40  ? -5  LEU B O     1 
ATOM   1906 C  CB    . LEU B 1 47  ? -1.206  10.783  22.152  1.00 63.62  ? -5  LEU B CB    1 
ATOM   1907 C  CG    . LEU B 1 47  ? -0.072  9.748   22.103  1.00 69.63  ? -5  LEU B CG    1 
ATOM   1908 C  CD1   . LEU B 1 47  ? 0.793   9.888   20.859  1.00 64.69  ? -5  LEU B CD1   1 
ATOM   1909 C  CD2   . LEU B 1 47  ? 0.807   9.763   23.340  1.00 71.75  ? -5  LEU B CD2   1 
ATOM   1910 N  N     . ILE B 1 48  ? 1.296   13.125  22.798  1.00 69.14  ? -4  ILE B N     1 
ATOM   1911 C  CA    . ILE B 1 48  ? 2.405   13.916  22.272  1.00 66.38  ? -4  ILE B CA    1 
ATOM   1912 C  C     . ILE B 1 48  ? 3.657   13.050  22.269  1.00 66.10  ? -4  ILE B C     1 
ATOM   1913 O  O     . ILE B 1 48  ? 3.894   12.284  23.214  1.00 66.08  ? -4  ILE B O     1 
ATOM   1914 C  CB    . ILE B 1 48  ? 2.627   15.210  23.086  1.00 61.85  ? -4  ILE B CB    1 
ATOM   1915 C  CG1   . ILE B 1 48  ? 1.317   15.993  23.217  1.00 61.29  ? -4  ILE B CG1   1 
ATOM   1916 C  CG2   . ILE B 1 48  ? 3.722   16.057  22.469  1.00 54.69  ? -4  ILE B CG2   1 
ATOM   1917 C  CD1   . ILE B 1 48  ? 0.565   16.190  21.933  1.00 65.91  ? -4  ILE B CD1   1 
ATOM   1918 N  N     . LYS B 1 49  ? 4.455   13.177  21.205  1.00 59.10  ? -3  LYS B N     1 
ATOM   1919 C  CA    . LYS B 1 49  ? 5.551   12.257  20.916  1.00 55.19  ? -3  LYS B CA    1 
ATOM   1920 C  C     . LYS B 1 49  ? 6.880   13.001  20.926  1.00 53.54  ? -3  LYS B C     1 
ATOM   1921 O  O     . LYS B 1 49  ? 7.179   13.784  20.021  1.00 55.33  ? -3  LYS B O     1 
ATOM   1922 C  CB    . LYS B 1 49  ? 5.327   11.562  19.576  1.00 59.47  ? -3  LYS B CB    1 
ATOM   1923 C  CG    . LYS B 1 49  ? 4.106   10.678  19.550  1.00 61.64  ? -3  LYS B CG    1 
ATOM   1924 C  CD    . LYS B 1 49  ? 3.945   10.006  18.198  1.00 69.74  ? -3  LYS B CD    1 
ATOM   1925 C  CE    . LYS B 1 49  ? 3.222   10.890  17.189  1.00 69.79  ? -3  LYS B CE    1 
ATOM   1926 N  NZ    . LYS B 1 49  ? 2.808   10.085  15.996  1.00 70.24  ? -3  LYS B NZ    1 
ATOM   1927 N  N     . PHE B 1 50  ? 7.686   12.737  21.931  1.00 56.06  ? -2  PHE B N     1 
ATOM   1928 C  CA    . PHE B 1 50  ? 9.038   13.262  21.996  1.00 56.32  ? -2  PHE B CA    1 
ATOM   1929 C  C     . PHE B 1 50  ? 10.014  12.170  21.581  1.00 51.60  ? -2  PHE B C     1 
ATOM   1930 O  O     . PHE B 1 50  ? 9.740   10.970  21.706  1.00 49.24  ? -2  PHE B O     1 
ATOM   1931 C  CB    . PHE B 1 50  ? 9.388   13.743  23.416  1.00 65.16  ? -2  PHE B CB    1 
ATOM   1932 C  CG    . PHE B 1 50  ? 8.658   14.990  23.863  1.00 68.13  ? -2  PHE B CG    1 
ATOM   1933 C  CD1   . PHE B 1 50  ? 7.449   15.366  23.304  1.00 71.56  ? -2  PHE B CD1   1 
ATOM   1934 C  CD2   . PHE B 1 50  ? 9.195   15.786  24.856  1.00 71.61  ? -2  PHE B CD2   1 
ATOM   1935 C  CE1   . PHE B 1 50  ? 6.796   16.508  23.729  1.00 70.84  ? -2  PHE B CE1   1 
ATOM   1936 C  CE2   . PHE B 1 50  ? 8.550   16.939  25.273  1.00 70.26  ? -2  PHE B CE2   1 
ATOM   1937 C  CZ    . PHE B 1 50  ? 7.348   17.299  24.705  1.00 67.63  ? -2  PHE B CZ    1 
ATOM   1938 N  N     . LEU B 1 51  ? 11.170  12.596  21.099  1.00 48.73  ? -1  LEU B N     1 
ATOM   1939 C  CA    . LEU B 1 51  ? 12.238  11.673  20.754  1.00 48.56  ? -1  LEU B CA    1 
ATOM   1940 C  C     . LEU B 1 51  ? 13.531  12.286  21.240  1.00 46.07  ? -1  LEU B C     1 
ATOM   1941 O  O     . LEU B 1 51  ? 13.732  13.494  21.111  1.00 44.29  ? -1  LEU B O     1 
ATOM   1942 C  CB    . LEU B 1 51  ? 12.316  11.402  19.232  1.00 55.23  ? -1  LEU B CB    1 
ATOM   1943 C  CG    . LEU B 1 51  ? 13.358  10.396  18.704  1.00 51.41  ? -1  LEU B CG    1 
ATOM   1944 C  CD1   . LEU B 1 51  ? 12.726  9.410   17.750  1.00 46.80  ? -1  LEU B CD1   1 
ATOM   1945 C  CD2   . LEU B 1 51  ? 14.555  11.094  18.061  1.00 48.60  ? -1  LEU B CD2   1 
ATOM   1946 N  N     . ALA B 1 52  ? 14.400  11.462  21.804  1.00 46.83  ? 0   ALA B N     1 
ATOM   1947 C  CA    . ALA B 1 52  ? 15.664  11.942  22.342  1.00 48.53  ? 0   ALA B CA    1 
ATOM   1948 C  C     . ALA B 1 52  ? 16.806  11.395  21.504  1.00 46.52  ? 0   ALA B C     1 
ATOM   1949 O  O     . ALA B 1 52  ? 16.814  10.208  21.144  1.00 48.00  ? 0   ALA B O     1 
ATOM   1950 C  CB    . ALA B 1 52  ? 15.846  11.537  23.815  1.00 44.60  ? 0   ALA B CB    1 
ATOM   1951 N  N     . LEU B 1 53  ? 17.770  12.262  21.205  1.00 45.54  ? 1   LEU B N     1 
ATOM   1952 C  CA    . LEU B 1 53  ? 18.880  11.857  20.358  1.00 50.32  ? 1   LEU B CA    1 
ATOM   1953 C  C     . LEU B 1 53  ? 20.153  12.561  20.808  1.00 44.47  ? 1   LEU B C     1 
ATOM   1954 O  O     . LEU B 1 53  ? 20.118  13.573  21.505  1.00 49.69  ? 1   LEU B O     1 
ATOM   1955 C  CB    . LEU B 1 53  ? 18.580  12.143  18.886  1.00 48.66  ? 1   LEU B CB    1 
ATOM   1956 C  CG    . LEU B 1 53  ? 18.352  13.597  18.512  1.00 49.24  ? 1   LEU B CG    1 
ATOM   1957 C  CD1   . LEU B 1 53  ? 18.864  13.751  17.111  1.00 52.82  ? 1   LEU B CD1   1 
ATOM   1958 C  CD2   . LEU B 1 53  ? 16.869  13.987  18.615  1.00 52.91  ? 1   LEU B CD2   1 
ATOM   1959 N  N     . GLY B 1 54  ? 21.270  12.007  20.384  1.00 39.13  ? 2   GLY B N     1 
ATOM   1960 C  CA    . GLY B 1 54  ? 22.587  12.366  20.861  1.00 38.26  ? 2   GLY B CA    1 
ATOM   1961 C  C     . GLY B 1 54  ? 23.522  11.195  20.651  1.00 47.12  ? 2   GLY B C     1 
ATOM   1962 O  O     . GLY B 1 54  ? 23.106  10.079  20.326  1.00 43.18  ? 2   GLY B O     1 
ATOM   1963 N  N     . ASP B 1 55  ? 24.814  11.470  20.813  1.00 49.12  ? 3   ASP B N     1 
ATOM   1964 C  CA    . ASP B 1 55  ? 25.798  10.401  20.747  1.00 50.68  ? 3   ASP B CA    1 
ATOM   1965 C  C     . ASP B 1 55  ? 25.474  9.363   21.812  1.00 52.44  ? 3   ASP B C     1 
ATOM   1966 O  O     . ASP B 1 55  ? 24.972  9.688   22.892  1.00 55.03  ? 3   ASP B O     1 
ATOM   1967 C  CB    . ASP B 1 55  ? 27.216  10.947  20.969  1.00 57.13  ? 3   ASP B CB    1 
ATOM   1968 C  CG    . ASP B 1 55  ? 27.779  11.706  19.752  1.00 66.95  ? 3   ASP B CG    1 
ATOM   1969 O  OD1   . ASP B 1 55  ? 27.244  11.577  18.616  1.00 60.10  ? 3   ASP B OD1   1 
ATOM   1970 O  OD2   . ASP B 1 55  ? 28.777  12.436  19.947  1.00 68.11  ? 3   ASP B OD2   1 
ATOM   1971 N  N     . SER B 1 56  ? 25.745  8.101   21.503  1.00 53.41  ? 4   SER B N     1 
ATOM   1972 C  CA    . SER B 1 56  ? 25.617  7.058   22.514  1.00 50.48  ? 4   SER B CA    1 
ATOM   1973 C  C     . SER B 1 56  ? 26.410  7.427   23.755  1.00 52.57  ? 4   SER B C     1 
ATOM   1974 O  O     . SER B 1 56  ? 27.575  7.833   23.666  1.00 52.63  ? 4   SER B O     1 
ATOM   1975 C  CB    . SER B 1 56  ? 26.108  5.719   21.976  1.00 50.47  ? 4   SER B CB    1 
ATOM   1976 O  OG    . SER B 1 56  ? 26.239  4.789   23.035  1.00 53.43  ? 4   SER B OG    1 
ATOM   1977 N  N     . GLY B 1 57  ? 25.755  7.302   24.912  1.00 51.86  ? 5   GLY B N     1 
ATOM   1978 C  CA    . GLY B 1 57  ? 26.371  7.550   26.202  1.00 51.17  ? 5   GLY B CA    1 
ATOM   1979 C  C     . GLY B 1 57  ? 26.178  8.940   26.780  1.00 46.43  ? 5   GLY B C     1 
ATOM   1980 O  O     . GLY B 1 57  ? 26.637  9.195   27.897  1.00 51.62  ? 5   GLY B O     1 
ATOM   1981 N  N     . VAL B 1 58  ? 25.515  9.848   26.077  1.00 48.76  ? 6   VAL B N     1 
ATOM   1982 C  CA    . VAL B 1 58  ? 25.356  11.205  26.592  1.00 49.07  ? 6   VAL B CA    1 
ATOM   1983 C  C     . VAL B 1 58  ? 24.217  11.252  27.606  1.00 49.48  ? 6   VAL B C     1 
ATOM   1984 O  O     . VAL B 1 58  ? 23.883  12.317  28.149  1.00 45.55  ? 6   VAL B O     1 
ATOM   1985 C  CB    . VAL B 1 58  ? 25.118  12.194  25.440  1.00 50.33  ? 6   VAL B CB    1 
ATOM   1986 C  CG1   . VAL B 1 58  ? 26.279  12.140  24.485  1.00 48.11  ? 6   VAL B CG1   1 
ATOM   1987 C  CG2   . VAL B 1 58  ? 23.790  11.883  24.743  1.00 46.65  ? 6   VAL B CG2   1 
ATOM   1988 N  N     . GLY B 1 59  ? 23.598  10.105  27.855  1.00 49.77  ? 7   GLY B N     1 
ATOM   1989 C  CA    . GLY B 1 59  ? 22.568  9.987   28.856  1.00 47.35  ? 7   GLY B CA    1 
ATOM   1990 C  C     . GLY B 1 59  ? 21.148  10.158  28.373  1.00 48.67  ? 7   GLY B C     1 
ATOM   1991 O  O     . GLY B 1 59  ? 20.313  10.662  29.128  1.00 51.00  ? 7   GLY B O     1 
ATOM   1992 N  N     . LYS B 1 60  ? 20.843  9.763   27.144  1.00 48.95  ? 8   LYS B N     1 
ATOM   1993 C  CA    . LYS B 1 60  ? 19.470  9.872   26.672  1.00 47.15  ? 8   LYS B CA    1 
ATOM   1994 C  C     . LYS B 1 60  ? 18.535  9.002   27.514  1.00 51.54  ? 8   LYS B C     1 
ATOM   1995 O  O     . LYS B 1 60  ? 17.485  9.467   27.984  1.00 46.41  ? 8   LYS B O     1 
ATOM   1996 C  CB    . LYS B 1 60  ? 19.419  9.494   25.193  1.00 44.85  ? 8   LYS B CB    1 
ATOM   1997 C  CG    . LYS B 1 60  ? 20.590  10.088  24.394  1.00 48.65  ? 8   LYS B CG    1 
ATOM   1998 C  CD    . LYS B 1 60  ? 20.476  9.819   22.915  1.00 44.10  ? 8   LYS B CD    1 
ATOM   1999 C  CE    . LYS B 1 60  ? 21.108  8.481   22.554  1.00 45.13  ? 8   LYS B CE    1 
ATOM   2000 N  NZ    . LYS B 1 60  ? 22.594  8.482   22.691  1.00 44.81  ? 8   LYS B NZ    1 
ATOM   2001 N  N     . THR B 1 61  ? 18.912  7.739   27.739  1.00 43.67  ? 9   THR B N     1 
ATOM   2002 C  CA    . THR B 1 61  ? 18.086  6.866   28.561  1.00 44.52  ? 9   THR B CA    1 
ATOM   2003 C  C     . THR B 1 61  ? 18.074  7.347   30.011  1.00 50.88  ? 9   THR B C     1 
ATOM   2004 O  O     . THR B 1 61  ? 17.013  7.487   30.634  1.00 44.87  ? 9   THR B O     1 
ATOM   2005 C  CB    . THR B 1 61  ? 18.612  5.433   28.465  1.00 44.97  ? 9   THR B CB    1 
ATOM   2006 O  OG1   . THR B 1 61  ? 18.782  5.089   27.092  1.00 48.44  ? 9   THR B OG1   1 
ATOM   2007 C  CG2   . THR B 1 61  ? 17.639  4.467   29.074  1.00 47.60  ? 9   THR B CG2   1 
ATOM   2008 N  N     . SER B 1 62  ? 19.256  7.617   30.562  1.00 47.74  ? 10  SER B N     1 
ATOM   2009 C  CA    . SER B 1 62  ? 19.351  8.095   31.930  1.00 42.48  ? 10  SER B CA    1 
ATOM   2010 C  C     . SER B 1 62  ? 18.516  9.340   32.171  1.00 52.16  ? 10  SER B C     1 
ATOM   2011 O  O     . SER B 1 62  ? 18.072  9.564   33.302  1.00 56.90  ? 10  SER B O     1 
ATOM   2012 C  CB    . SER B 1 62  ? 20.806  8.367   32.283  1.00 45.91  ? 10  SER B CB    1 
ATOM   2013 O  OG    . SER B 1 62  ? 21.554  7.179   32.074  1.00 55.25  ? 10  SER B OG    1 
ATOM   2014 N  N     . VAL B 1 63  ? 18.276  10.150  31.142  1.00 53.70  ? 11  VAL B N     1 
ATOM   2015 C  CA    . VAL B 1 63  ? 17.449  11.344  31.312  1.00 52.03  ? 11  VAL B CA    1 
ATOM   2016 C  C     . VAL B 1 63  ? 15.969  10.973  31.381  1.00 48.99  ? 11  VAL B C     1 
ATOM   2017 O  O     . VAL B 1 63  ? 15.272  11.300  32.348  1.00 54.89  ? 11  VAL B O     1 
ATOM   2018 C  CB    . VAL B 1 63  ? 17.736  12.357  30.188  1.00 47.92  ? 11  VAL B CB    1 
ATOM   2019 C  CG1   . VAL B 1 63  ? 16.521  13.268  29.922  1.00 44.81  ? 11  VAL B CG1   1 
ATOM   2020 C  CG2   . VAL B 1 63  ? 18.991  13.160  30.524  1.00 43.67  ? 11  VAL B CG2   1 
ATOM   2021 N  N     . LEU B 1 64  ? 15.478  10.252  30.378  1.00 49.72  ? 12  LEU B N     1 
ATOM   2022 C  CA    . LEU B 1 64  ? 14.060  9.903   30.347  1.00 52.68  ? 12  LEU B CA    1 
ATOM   2023 C  C     . LEU B 1 64  ? 13.664  9.069   31.565  1.00 56.37  ? 12  LEU B C     1 
ATOM   2024 O  O     . LEU B 1 64  ? 12.542  9.190   32.077  1.00 54.93  ? 12  LEU B O     1 
ATOM   2025 C  CB    . LEU B 1 64  ? 13.738  9.151   29.053  1.00 51.48  ? 12  LEU B CB    1 
ATOM   2026 C  CG    . LEU B 1 64  ? 14.143  9.776   27.714  1.00 44.67  ? 12  LEU B CG    1 
ATOM   2027 C  CD1   . LEU B 1 64  ? 13.416  9.060   26.595  1.00 53.11  ? 12  LEU B CD1   1 
ATOM   2028 C  CD2   . LEU B 1 64  ? 13.817  11.246  27.667  1.00 43.66  ? 12  LEU B CD2   1 
ATOM   2029 N  N     . TYR B 1 65  ? 14.570  8.204   32.030  1.00 54.93  ? 13  TYR B N     1 
ATOM   2030 C  CA    . TYR B 1 65  ? 14.321  7.440   33.248  1.00 54.60  ? 13  TYR B CA    1 
ATOM   2031 C  C     . TYR B 1 65  ? 14.205  8.380   34.433  1.00 54.22  ? 13  TYR B C     1 
ATOM   2032 O  O     . TYR B 1 65  ? 13.208  8.360   35.164  1.00 53.16  ? 13  TYR B O     1 
ATOM   2033 C  CB    . TYR B 1 65  ? 15.454  6.426   33.449  1.00 56.60  ? 13  TYR B CB    1 
ATOM   2034 C  CG    . TYR B 1 65  ? 15.228  5.381   34.512  1.00 57.37  ? 13  TYR B CG    1 
ATOM   2035 C  CD1   . TYR B 1 65  ? 14.091  4.585   34.508  1.00 58.38  ? 13  TYR B CD1   1 
ATOM   2036 C  CD2   . TYR B 1 65  ? 16.178  5.168   35.513  1.00 57.93  ? 13  TYR B CD2   1 
ATOM   2037 C  CE1   . TYR B 1 65  ? 13.895  3.616   35.492  1.00 61.24  ? 13  TYR B CE1   1 
ATOM   2038 C  CE2   . TYR B 1 65  ? 15.993  4.204   36.496  1.00 53.72  ? 13  TYR B CE2   1 
ATOM   2039 C  CZ    . TYR B 1 65  ? 14.847  3.430   36.482  1.00 57.50  ? 13  TYR B CZ    1 
ATOM   2040 O  OH    . TYR B 1 65  ? 14.645  2.464   37.453  1.00 64.59  ? 13  TYR B OH    1 
ATOM   2041 N  N     . GLN B 1 66  ? 15.208  9.248   34.598  1.00 54.19  ? 14  GLN B N     1 
ATOM   2042 C  CA    . GLN B 1 66  ? 15.188  10.276  35.634  1.00 52.70  ? 14  GLN B CA    1 
ATOM   2043 C  C     . GLN B 1 66  ? 13.946  11.163  35.541  1.00 51.86  ? 14  GLN B C     1 
ATOM   2044 O  O     . GLN B 1 66  ? 13.399  11.575  36.565  1.00 54.45  ? 14  GLN B O     1 
ATOM   2045 C  CB    . GLN B 1 66  ? 16.460  11.119  35.531  1.00 53.40  ? 14  GLN B CB    1 
ATOM   2046 C  CG    . GLN B 1 66  ? 16.505  12.299  36.456  1.00 50.38  ? 14  GLN B CG    1 
ATOM   2047 C  CD    . GLN B 1 66  ? 16.473  11.884  37.923  1.00 56.89  ? 14  GLN B CD    1 
ATOM   2048 O  OE1   . GLN B 1 66  ? 15.576  12.291  38.667  1.00 52.41  ? 14  GLN B OE1   1 
ATOM   2049 N  NE2   . GLN B 1 66  ? 17.458  11.080  38.349  1.00 51.59  ? 14  GLN B NE2   1 
ATOM   2050 N  N     . TYR B 1 67  ? 13.484  11.478  34.330  1.00 57.25  ? 15  TYR B N     1 
ATOM   2051 C  CA    . TYR B 1 67  ? 12.320  12.357  34.210  1.00 54.11  ? 15  TYR B CA    1 
ATOM   2052 C  C     . TYR B 1 67  ? 11.024  11.632  34.554  1.00 56.01  ? 15  TYR B C     1 
ATOM   2053 O  O     . TYR B 1 67  ? 10.140  12.213  35.197  1.00 54.58  ? 15  TYR B O     1 
ATOM   2054 C  CB    . TYR B 1 67  ? 12.218  12.940  32.803  1.00 52.08  ? 15  TYR B CB    1 
ATOM   2055 C  CG    . TYR B 1 67  ? 10.889  13.653  32.540  1.00 60.02  ? 15  TYR B CG    1 
ATOM   2056 C  CD1   . TYR B 1 67  ? 10.643  14.924  33.049  1.00 57.94  ? 15  TYR B CD1   1 
ATOM   2057 C  CD2   . TYR B 1 67  ? 9.884   13.054  31.782  1.00 61.29  ? 15  TYR B CD2   1 
ATOM   2058 C  CE1   . TYR B 1 67  ? 9.452   15.571  32.820  1.00 54.47  ? 15  TYR B CE1   1 
ATOM   2059 C  CE2   . TYR B 1 67  ? 8.680   13.707  31.544  1.00 58.88  ? 15  TYR B CE2   1 
ATOM   2060 C  CZ    . TYR B 1 67  ? 8.470   14.964  32.071  1.00 56.72  ? 15  TYR B CZ    1 
ATOM   2061 O  OH    . TYR B 1 67  ? 7.273   15.622  31.842  1.00 62.02  ? 15  TYR B OH    1 
ATOM   2062 N  N     . THR B 1 68  ? 10.874  10.378  34.106  1.00 58.31  ? 16  THR B N     1 
ATOM   2063 C  CA    . THR B 1 68  ? 9.611   9.659   34.274  1.00 59.45  ? 16  THR B CA    1 
ATOM   2064 C  C     . THR B 1 68  ? 9.516   8.902   35.595  1.00 58.83  ? 16  THR B C     1 
ATOM   2065 O  O     . THR B 1 68  ? 8.402   8.703   36.098  1.00 58.02  ? 16  THR B O     1 
ATOM   2066 C  CB    . THR B 1 68  ? 9.373   8.667   33.120  1.00 57.92  ? 16  THR B CB    1 
ATOM   2067 O  OG1   . THR B 1 68  ? 10.424  7.691   33.083  1.00 62.54  ? 16  THR B OG1   1 
ATOM   2068 C  CG2   . THR B 1 68  ? 9.314   9.383   31.795  1.00 60.61  ? 16  THR B CG2   1 
ATOM   2069 N  N     . ASP B 1 69  ? 10.645  8.475   36.168  1.00 54.31  ? 17  ASP B N     1 
ATOM   2070 C  CA    . ASP B 1 69  ? 10.639  7.684   37.392  1.00 56.45  ? 17  ASP B CA    1 
ATOM   2071 C  C     . ASP B 1 69  ? 11.441  8.282   38.536  1.00 52.09  ? 17  ASP B C     1 
ATOM   2072 O  O     . ASP B 1 69  ? 11.481  7.678   39.611  1.00 51.00  ? 17  ASP B O     1 
ATOM   2073 C  CB    . ASP B 1 69  ? 11.180  6.276   37.120  1.00 58.31  ? 17  ASP B CB    1 
ATOM   2074 C  CG    . ASP B 1 69  ? 10.173  5.399   36.436  1.00 64.03  ? 17  ASP B CG    1 
ATOM   2075 O  OD1   . ASP B 1 69  ? 8.957   5.602   36.660  1.00 68.17  ? 17  ASP B OD1   1 
ATOM   2076 O  OD2   . ASP B 1 69  ? 10.595  4.509   35.671  1.00 73.90  ? 17  ASP B OD2   1 
ATOM   2077 N  N     . GLY B 1 70  ? 12.098  9.424   38.334  1.00 51.57  ? 18  GLY B N     1 
ATOM   2078 C  CA    . GLY B 1 70  ? 12.987  9.985   39.333  1.00 47.56  ? 18  GLY B CA    1 
ATOM   2079 C  C     . GLY B 1 70  ? 14.061  9.041   39.833  1.00 55.98  ? 18  GLY B C     1 
ATOM   2080 O  O     . GLY B 1 70  ? 14.552  9.201   40.962  1.00 57.40  ? 18  GLY B O     1 
ATOM   2081 N  N     . LYS B 1 71  ? 14.423  8.038   39.043  1.00 52.64  ? 19  LYS B N     1 
ATOM   2082 C  CA    . LYS B 1 71  ? 15.477  7.110   39.413  1.00 50.66  ? 19  LYS B CA    1 
ATOM   2083 C  C     . LYS B 1 71  ? 16.621  7.269   38.420  1.00 49.16  ? 19  LYS B C     1 
ATOM   2084 O  O     . LYS B 1 71  ? 16.424  7.762   37.304  1.00 56.89  ? 19  LYS B O     1 
ATOM   2085 C  CB    . LYS B 1 71  ? 14.959  5.658   39.425  1.00 54.08  ? 19  LYS B CB    1 
ATOM   2086 C  CG    . LYS B 1 71  ? 13.777  5.350   40.372  1.00 49.39  ? 19  LYS B CG    1 
ATOM   2087 C  CD    . LYS B 1 71  ? 13.490  3.837   40.339  1.00 56.54  ? 19  LYS B CD    1 
ATOM   2088 C  CE    . LYS B 1 71  ? 12.559  3.347   41.444  1.00 56.93  ? 19  LYS B CE    1 
ATOM   2089 N  NZ    . LYS B 1 71  ? 12.857  1.906   41.749  1.00 58.88  ? 19  LYS B NZ    1 
ATOM   2090 N  N     . PHE B 1 72  ? 17.819  6.854   38.832  1.00 45.78  ? 20  PHE B N     1 
ATOM   2091 C  CA    . PHE B 1 72  ? 19.015  6.922   38.003  1.00 46.78  ? 20  PHE B CA    1 
ATOM   2092 C  C     . PHE B 1 72  ? 19.866  5.690   38.257  1.00 46.85  ? 20  PHE B C     1 
ATOM   2093 O  O     . PHE B 1 72  ? 20.049  5.306   39.411  1.00 45.86  ? 20  PHE B O     1 
ATOM   2094 C  CB    . PHE B 1 72  ? 19.842  8.184   38.296  1.00 45.46  ? 20  PHE B CB    1 
ATOM   2095 C  CG    . PHE B 1 72  ? 21.193  8.185   37.620  1.00 51.58  ? 20  PHE B CG    1 
ATOM   2096 C  CD1   . PHE B 1 72  ? 21.320  8.566   36.282  1.00 50.33  ? 20  PHE B CD1   1 
ATOM   2097 C  CD2   . PHE B 1 72  ? 22.329  7.757   38.303  1.00 50.48  ? 20  PHE B CD2   1 
ATOM   2098 C  CE1   . PHE B 1 72  ? 22.558  8.539   35.648  1.00 48.80  ? 20  PHE B CE1   1 
ATOM   2099 C  CE2   . PHE B 1 72  ? 23.569  7.736   37.674  1.00 53.50  ? 20  PHE B CE2   1 
ATOM   2100 C  CZ    . PHE B 1 72  ? 23.682  8.129   36.342  1.00 49.76  ? 20  PHE B CZ    1 
ATOM   2101 N  N     . ASN B 1 73  ? 20.398  5.083   37.191  1.00 51.28  ? 21  ASN B N     1 
ATOM   2102 C  CA    . ASN B 1 73  ? 21.304  3.947   37.315  1.00 48.28  ? 21  ASN B CA    1 
ATOM   2103 C  C     . ASN B 1 73  ? 22.679  4.370   36.827  1.00 48.20  ? 21  ASN B C     1 
ATOM   2104 O  O     . ASN B 1 73  ? 22.842  4.759   35.674  1.00 50.76  ? 21  ASN B O     1 
ATOM   2105 C  CB    . ASN B 1 73  ? 20.818  2.725   36.536  1.00 48.12  ? 21  ASN B CB    1 
ATOM   2106 C  CG    . ASN B 1 73  ? 21.770  1.502   36.688  1.00 62.66  ? 21  ASN B CG    1 
ATOM   2107 O  OD1   . ASN B 1 73  ? 22.758  1.509   37.450  1.00 63.16  ? 21  ASN B OD1   1 
ATOM   2108 N  ND2   . ASN B 1 73  ? 21.434  0.434   35.989  1.00 69.29  ? 21  ASN B ND2   1 
ATOM   2109 N  N     . SER B 1 74  ? 23.668  4.287   37.702  1.00 54.24  ? 22  SER B N     1 
ATOM   2110 C  CA    . SER B 1 74  ? 25.036  4.605   37.318  1.00 57.74  ? 22  SER B CA    1 
ATOM   2111 C  C     . SER B 1 74  ? 25.618  3.676   36.248  1.00 52.57  ? 22  SER B C     1 
ATOM   2112 O  O     . SER B 1 74  ? 26.483  4.124   35.497  1.00 50.95  ? 22  SER B O     1 
ATOM   2113 C  CB    . SER B 1 74  ? 25.899  4.625   38.582  1.00 56.10  ? 22  SER B CB    1 
ATOM   2114 O  OG    . SER B 1 74  ? 27.222  4.185   38.382  1.00 63.41  ? 22  SER B OG    1 
ATOM   2115 N  N     . LYS B 1 75  ? 25.149  2.436   36.115  1.00 54.78  ? 23  LYS B N     1 
ATOM   2116 C  CA    . LYS B 1 75  ? 25.824  1.438   35.287  1.00 56.55  ? 23  LYS B CA    1 
ATOM   2117 C  C     . LYS B 1 75  ? 25.389  1.561   33.844  1.00 61.11  ? 23  LYS B C     1 
ATOM   2118 O  O     . LYS B 1 75  ? 24.194  1.425   33.536  1.00 63.34  ? 23  LYS B O     1 
ATOM   2119 C  CB    . LYS B 1 75  ? 25.509  0.037   35.791  1.00 61.10  ? 23  LYS B CB    1 
ATOM   2120 C  CG    . LYS B 1 75  ? 25.393  -0.035  37.342  1.00 71.27  ? 23  LYS B CG    1 
ATOM   2121 C  CD    . LYS B 1 75  ? 24.467  -1.149  37.856  1.00 70.69  ? 23  LYS B CD    1 
ATOM   2122 C  CE    . LYS B 1 75  ? 24.843  -1.609  39.218  1.00 68.25  ? 23  LYS B CE    1 
ATOM   2123 N  NZ    . LYS B 1 75  ? 26.159  -2.120  39.319  1.00 75.91  ? 23  LYS B NZ    1 
ATOM   2124 N  N     . PHE B 1 76  ? 26.368  1.690   32.955  1.00 52.12  ? 24  PHE B N     1 
ATOM   2125 C  CA    . PHE B 1 76  ? 26.076  1.962   31.561  1.00 54.06  ? 24  PHE B CA    1 
ATOM   2126 C  C     . PHE B 1 76  ? 25.514  0.726   30.866  1.00 52.75  ? 24  PHE B C     1 
ATOM   2127 O  O     . PHE B 1 76  ? 26.189  -0.302  30.769  1.00 56.99  ? 24  PHE B O     1 
ATOM   2128 C  CB    . PHE B 1 76  ? 27.331  2.451   30.848  1.00 57.40  ? 24  PHE B CB    1 
ATOM   2129 C  CG    . PHE B 1 76  ? 27.076  2.905   29.446  1.00 49.36  ? 24  PHE B CG    1 
ATOM   2130 C  CD1   . PHE B 1 76  ? 25.821  3.353   29.075  1.00 54.18  ? 24  PHE B CD1   1 
ATOM   2131 C  CD2   . PHE B 1 76  ? 28.075  2.879   28.495  1.00 54.44  ? 24  PHE B CD2   1 
ATOM   2132 C  CE1   . PHE B 1 76  ? 25.563  3.755   27.767  1.00 54.93  ? 24  PHE B CE1   1 
ATOM   2133 C  CE2   . PHE B 1 76  ? 27.824  3.291   27.190  1.00 48.49  ? 24  PHE B CE2   1 
ATOM   2134 C  CZ    . PHE B 1 76  ? 26.573  3.726   26.829  1.00 46.53  ? 24  PHE B CZ    1 
ATOM   2135 N  N     . ILE B 1 77  ? 24.286  0.847   30.360  1.00 50.68  ? 25  ILE B N     1 
ATOM   2136 C  CA    . ILE B 1 77  ? 23.597  -0.203  29.608  1.00 51.54  ? 25  ILE B CA    1 
ATOM   2137 C  C     . ILE B 1 77  ? 23.125  0.431   28.305  1.00 48.06  ? 25  ILE B C     1 
ATOM   2138 O  O     . ILE B 1 77  ? 22.075  1.085   28.267  1.00 42.63  ? 25  ILE B O     1 
ATOM   2139 C  CB    . ILE B 1 77  ? 22.407  -0.786  30.376  1.00 57.17  ? 25  ILE B CB    1 
ATOM   2140 C  CG1   . ILE B 1 77  ? 22.840  -1.360  31.732  1.00 54.34  ? 25  ILE B CG1   1 
ATOM   2141 C  CG2   . ILE B 1 77  ? 21.673  -1.802  29.503  1.00 48.26  ? 25  ILE B CG2   1 
ATOM   2142 C  CD1   . ILE B 1 77  ? 23.956  -2.387  31.641  1.00 51.93  ? 25  ILE B CD1   1 
ATOM   2143 N  N     . THR B 1 78  ? 23.883  0.235   27.231  1.00 50.66  ? 26  THR B N     1 
ATOM   2144 C  CA    . THR B 1 78  ? 23.557  0.912   25.981  1.00 50.23  ? 26  THR B CA    1 
ATOM   2145 C  C     . THR B 1 78  ? 22.186  0.486   25.446  1.00 46.81  ? 26  THR B C     1 
ATOM   2146 O  O     . THR B 1 78  ? 21.792  -0.682  25.540  1.00 52.01  ? 26  THR B O     1 
ATOM   2147 C  CB    . THR B 1 78  ? 24.636  0.654   24.936  1.00 48.56  ? 26  THR B CB    1 
ATOM   2148 O  OG1   . THR B 1 78  ? 24.291  1.371   23.750  1.00 54.41  ? 26  THR B OG1   1 
ATOM   2149 C  CG2   . THR B 1 78  ? 24.774  -0.839  24.615  1.00 44.99  ? 26  THR B CG2   1 
ATOM   2150 N  N     . THR B 1 79  ? 21.439  1.455   24.918  1.00 42.60  ? 27  THR B N     1 
ATOM   2151 C  CA    . THR B 1 79  ? 20.081  1.204   24.450  1.00 45.43  ? 27  THR B CA    1 
ATOM   2152 C  C     . THR B 1 79  ? 20.125  0.435   23.129  1.00 56.61  ? 27  THR B C     1 
ATOM   2153 O  O     . THR B 1 79  ? 20.725  0.889   22.146  1.00 48.44  ? 27  THR B O     1 
ATOM   2154 C  CB    . THR B 1 79  ? 19.330  2.519   24.293  1.00 49.20  ? 27  THR B CB    1 
ATOM   2155 O  OG1   . THR B 1 79  ? 18.971  3.011   25.590  1.00 51.26  ? 27  THR B OG1   1 
ATOM   2156 C  CG2   . THR B 1 79  ? 18.077  2.340   23.440  1.00 52.56  ? 27  THR B CG2   1 
ATOM   2157 N  N     . VAL B 1 80  ? 19.515  -0.746  23.115  1.00 59.36  ? 28  VAL B N     1 
ATOM   2158 C  CA    . VAL B 1 80  ? 19.577  -1.606  21.944  1.00 52.27  ? 28  VAL B CA    1 
ATOM   2159 C  C     . VAL B 1 80  ? 18.528  -1.148  20.947  1.00 56.86  ? 28  VAL B C     1 
ATOM   2160 O  O     . VAL B 1 80  ? 17.356  -1.533  21.041  1.00 55.35  ? 28  VAL B O     1 
ATOM   2161 C  CB    . VAL B 1 80  ? 19.381  -3.091  22.305  1.00 61.44  ? 28  VAL B CB    1 
ATOM   2162 C  CG1   . VAL B 1 80  ? 19.892  -3.985  21.153  1.00 63.50  ? 28  VAL B CG1   1 
ATOM   2163 C  CG2   . VAL B 1 80  ? 20.067  -3.423  23.646  1.00 58.94  ? 28  VAL B CG2   1 
ATOM   2164 N  N     . GLY B 1 81  ? 18.950  -0.325  19.988  1.00 62.67  ? 29  GLY B N     1 
ATOM   2165 C  CA    . GLY B 1 81  ? 18.098  0.131   18.905  1.00 60.86  ? 29  GLY B CA    1 
ATOM   2166 C  C     . GLY B 1 81  ? 17.219  1.307   19.269  1.00 57.63  ? 29  GLY B C     1 
ATOM   2167 O  O     . GLY B 1 81  ? 17.534  2.455   18.946  1.00 53.85  ? 29  GLY B O     1 
ATOM   2168 N  N     . ILE B 1 82  ? 16.123  1.031   19.967  1.00 56.79  ? 30  ILE B N     1 
ATOM   2169 C  CA    . ILE B 1 82  ? 15.116  2.042   20.232  1.00 52.44  ? 30  ILE B CA    1 
ATOM   2170 C  C     . ILE B 1 82  ? 14.277  1.574   21.408  1.00 53.74  ? 30  ILE B C     1 
ATOM   2171 O  O     . ILE B 1 82  ? 13.929  0.394   21.515  1.00 49.00  ? 30  ILE B O     1 
ATOM   2172 C  CB    . ILE B 1 82  ? 14.246  2.296   18.980  1.00 50.57  ? 30  ILE B CB    1 
ATOM   2173 C  CG1   . ILE B 1 82  ? 13.289  3.474   19.219  1.00 51.71  ? 30  ILE B CG1   1 
ATOM   2174 C  CG2   . ILE B 1 82  ? 13.504  1.019   18.594  1.00 49.52  ? 30  ILE B CG2   1 
ATOM   2175 C  CD1   . ILE B 1 82  ? 13.825  4.820   18.742  1.00 54.10  ? 30  ILE B CD1   1 
ATOM   2176 N  N     . ASP B 1 83  ? 13.962  2.509   22.297  1.00 54.16  ? 31  ASP B N     1 
ATOM   2177 C  CA    . ASP B 1 83  ? 12.963  2.248   23.316  1.00 50.66  ? 31  ASP B CA    1 
ATOM   2178 C  C     . ASP B 1 83  ? 12.182  3.533   23.560  1.00 51.06  ? 31  ASP B C     1 
ATOM   2179 O  O     . ASP B 1 83  ? 12.573  4.617   23.118  1.00 52.00  ? 31  ASP B O     1 
ATOM   2180 C  CB    . ASP B 1 83  ? 13.611  1.695   24.587  1.00 49.60  ? 31  ASP B CB    1 
ATOM   2181 C  CG    . ASP B 1 83  ? 12.596  1.216   25.587  1.00 51.51  ? 31  ASP B CG    1 
ATOM   2182 O  OD1   . ASP B 1 83  ? 12.208  2.056   26.432  1.00 61.77  ? 31  ASP B OD1   1 
ATOM   2183 O  OD2   . ASP B 1 83  ? 12.165  0.029   25.512  1.00 44.57  ? 31  ASP B OD2   1 
ATOM   2184 N  N     . PHE B 1 84  ? 11.048  3.407   24.237  1.00 52.41  ? 32  PHE B N     1 
ATOM   2185 C  CA    . PHE B 1 84  ? 10.332  4.601   24.648  1.00 57.47  ? 32  PHE B CA    1 
ATOM   2186 C  C     . PHE B 1 84  ? 9.807   4.426   26.073  1.00 54.79  ? 32  PHE B C     1 
ATOM   2187 O  O     . PHE B 1 84  ? 9.586   3.304   26.540  1.00 54.34  ? 32  PHE B O     1 
ATOM   2188 C  CB    . PHE B 1 84  ? 9.226   4.960   23.625  1.00 47.44  ? 32  PHE B CB    1 
ATOM   2189 C  CG    . PHE B 1 84  ? 8.109   3.949   23.510  1.00 48.98  ? 32  PHE B CG    1 
ATOM   2190 C  CD1   . PHE B 1 84  ? 7.001   4.009   24.346  1.00 56.90  ? 32  PHE B CD1   1 
ATOM   2191 C  CD2   . PHE B 1 84  ? 8.134   2.975   22.530  1.00 50.15  ? 32  PHE B CD2   1 
ATOM   2192 C  CE1   . PHE B 1 84  ? 5.951   3.087   24.224  1.00 53.93  ? 32  PHE B CE1   1 
ATOM   2193 C  CE2   . PHE B 1 84  ? 7.097   2.063   22.402  1.00 53.59  ? 32  PHE B CE2   1 
ATOM   2194 C  CZ    . PHE B 1 84  ? 6.003   2.122   23.255  1.00 52.68  ? 32  PHE B CZ    1 
ATOM   2195 N  N     . ARG B 1 85  ? 9.675   5.548   26.775  1.00 49.14  ? 33  ARG B N     1 
ATOM   2196 C  CA    . ARG B 1 85  ? 9.001   5.629   28.060  1.00 55.84  ? 33  ARG B CA    1 
ATOM   2197 C  C     . ARG B 1 85  ? 7.696   6.395   27.888  1.00 58.53  ? 33  ARG B C     1 
ATOM   2198 O  O     . ARG B 1 85  ? 7.514   7.127   26.914  1.00 64.17  ? 33  ARG B O     1 
ATOM   2199 C  CB    . ARG B 1 85  ? 9.882   6.318   29.115  1.00 58.28  ? 33  ARG B CB    1 
ATOM   2200 C  CG    . ARG B 1 85  ? 11.321  5.781   29.212  1.00 55.77  ? 33  ARG B CG    1 
ATOM   2201 C  CD    . ARG B 1 85  ? 11.829  5.756   30.648  1.00 56.99  ? 33  ARG B CD    1 
ATOM   2202 N  NE    . ARG B 1 85  ? 11.213  4.696   31.451  1.00 64.38  ? 33  ARG B NE    1 
ATOM   2203 C  CZ    . ARG B 1 85  ? 11.782  3.519   31.704  1.00 63.64  ? 33  ARG B CZ    1 
ATOM   2204 N  NH1   . ARG B 1 85  ? 12.992  3.235   31.224  1.00 60.73  ? 33  ARG B NH1   1 
ATOM   2205 N  NH2   . ARG B 1 85  ? 11.138  2.623   32.439  1.00 64.86  ? 33  ARG B NH2   1 
ATOM   2206 N  N     . GLU B 1 86  ? 6.776   6.206   28.829  1.00 58.76  ? 34  GLU B N     1 
ATOM   2207 C  CA    . GLU B 1 86  ? 5.524   6.949   28.843  1.00 58.29  ? 34  GLU B CA    1 
ATOM   2208 C  C     . GLU B 1 86  ? 5.412   7.724   30.150  1.00 67.61  ? 34  GLU B C     1 
ATOM   2209 O  O     . GLU B 1 86  ? 6.186   7.525   31.094  1.00 70.03  ? 34  GLU B O     1 
ATOM   2210 C  CB    . GLU B 1 86  ? 4.302   6.034   28.658  1.00 59.74  ? 34  GLU B CB    1 
ATOM   2211 C  CG    . GLU B 1 86  ? 4.412   5.040   27.507  1.00 65.56  ? 34  GLU B CG    1 
ATOM   2212 C  CD    . GLU B 1 86  ? 4.783   3.632   27.978  1.00 74.35  ? 34  GLU B CD    1 
ATOM   2213 O  OE1   . GLU B 1 86  ? 5.295   3.490   29.128  1.00 75.65  ? 34  GLU B OE1   1 
ATOM   2214 O  OE2   . GLU B 1 86  ? 4.571   2.670   27.195  1.00 71.95  ? 34  GLU B OE2   1 
ATOM   2215 N  N     . LYS B 1 87  ? 4.435   8.631   30.188  1.00 69.16  ? 35  LYS B N     1 
ATOM   2216 C  CA    . LYS B 1 87  ? 4.195   9.475   31.352  1.00 74.84  ? 35  LYS B CA    1 
ATOM   2217 C  C     . LYS B 1 87  ? 2.950   10.324  31.139  1.00 75.49  ? 35  LYS B C     1 
ATOM   2218 O  O     . LYS B 1 87  ? 2.803   10.973  30.100  1.00 73.01  ? 35  LYS B O     1 
ATOM   2219 C  CB    . LYS B 1 87  ? 5.398   10.380  31.643  1.00 71.71  ? 35  LYS B CB    1 
ATOM   2220 C  CG    . LYS B 1 87  ? 5.190   11.331  32.823  1.00 70.56  ? 35  LYS B CG    1 
ATOM   2221 C  CD    . LYS B 1 87  ? 5.602   10.694  34.155  1.00 72.16  ? 35  LYS B CD    1 
ATOM   2222 C  CE    . LYS B 1 87  ? 5.981   11.755  35.175  1.00 69.65  ? 35  LYS B CE    1 
ATOM   2223 N  NZ    . LYS B 1 87  ? 7.007   12.707  34.647  1.00 57.67  ? 35  LYS B NZ    1 
ATOM   2224 N  N     . ARG B 1 88  ? 2.048   10.324  32.115  1.00 78.39  ? 36  ARG B N     1 
ATOM   2225 C  CA    . ARG B 1 88  ? 0.867   11.172  32.076  1.00 77.62  ? 36  ARG B CA    1 
ATOM   2226 C  C     . ARG B 1 88  ? 1.218   12.536  32.672  1.00 82.14  ? 36  ARG B C     1 
ATOM   2227 O  O     . ARG B 1 88  ? 1.780   12.613  33.771  1.00 84.09  ? 36  ARG B O     1 
ATOM   2228 C  CB    . ARG B 1 88  ? -0.279  10.510  32.845  1.00 81.60  ? 36  ARG B CB    1 
ATOM   2229 C  CG    . ARG B 1 88  ? -0.754  9.175   32.267  1.00 86.76  ? 36  ARG B CG    1 
ATOM   2230 C  CD    . ARG B 1 88  ? -0.551  7.980   33.231  1.00 90.28  ? 36  ARG B CD    1 
ATOM   2231 N  NE    . ARG B 1 88  ? 0.867   7.718   33.495  1.00 86.99  ? 36  ARG B NE    1 
ATOM   2232 C  CZ    . ARG B 1 88  ? 1.592   6.777   32.883  1.00 85.65  ? 36  ARG B CZ    1 
ATOM   2233 N  NH1   . ARG B 1 88  ? 2.878   6.625   33.184  1.00 81.55  ? 36  ARG B NH1   1 
ATOM   2234 N  NH2   . ARG B 1 88  ? 1.044   5.988   31.961  1.00 76.30  ? 36  ARG B NH2   1 
ATOM   2235 N  N     . VAL B 1 89  ? 0.914   13.608  31.938  1.00 81.35  ? 37  VAL B N     1 
ATOM   2236 C  CA    . VAL B 1 89  ? 1.252   14.967  32.358  1.00 82.52  ? 37  VAL B CA    1 
ATOM   2237 C  C     . VAL B 1 89  ? 0.058   15.883  32.117  1.00 85.48  ? 37  VAL B C     1 
ATOM   2238 O  O     . VAL B 1 89  ? -0.684  15.709  31.145  1.00 88.98  ? 37  VAL B O     1 
ATOM   2239 C  CB    . VAL B 1 89  ? 2.497   15.508  31.618  1.00 84.36  ? 37  VAL B CB    1 
ATOM   2240 C  CG1   . VAL B 1 89  ? 2.952   16.830  32.221  1.00 88.63  ? 37  VAL B CG1   1 
ATOM   2241 C  CG2   . VAL B 1 89  ? 3.637   14.497  31.651  1.00 83.01  ? 37  VAL B CG2   1 
ATOM   2242 N  N     . VAL B 1 90  ? -0.126  16.861  33.005  1.00 92.65  ? 38  VAL B N     1 
ATOM   2243 C  CA    . VAL B 1 90  ? -1.124  17.920  32.848  1.00 93.54  ? 38  VAL B CA    1 
ATOM   2244 C  C     . VAL B 1 90  ? -0.405  19.185  32.377  1.00 89.89  ? 38  VAL B C     1 
ATOM   2245 O  O     . VAL B 1 90  ? 0.595   19.600  32.980  1.00 93.87  ? 38  VAL B O     1 
ATOM   2246 C  CB    . VAL B 1 90  ? -1.892  18.151  34.168  1.00 87.05  ? 38  VAL B CB    1 
ATOM   2247 C  CG1   . VAL B 1 90  ? -2.392  19.577  34.282  1.00 89.29  ? 38  VAL B CG1   1 
ATOM   2248 C  CG2   . VAL B 1 90  ? -3.062  17.179  34.277  1.00 85.83  ? 38  VAL B CG2   1 
ATOM   2249 N  N     . TYR B 1 91  ? -0.889  19.788  31.293  1.00 83.93  ? 39  TYR B N     1 
ATOM   2250 C  CA    . TYR B 1 91  ? -0.207  20.924  30.685  1.00 89.39  ? 39  TYR B CA    1 
ATOM   2251 C  C     . TYR B 1 91  ? -0.874  22.246  31.062  1.00 92.69  ? 39  TYR B C     1 
ATOM   2252 O  O     . TYR B 1 91  ? -2.095  22.322  31.237  1.00 92.09  ? 39  TYR B O     1 
ATOM   2253 C  CB    . TYR B 1 91  ? -0.163  20.784  29.161  1.00 87.69  ? 39  TYR B CB    1 
ATOM   2254 C  CG    . TYR B 1 91  ? 0.565   21.927  28.488  1.00 90.14  ? 39  TYR B CG    1 
ATOM   2255 C  CD1   . TYR B 1 91  ? 1.952   21.987  28.497  1.00 88.28  ? 39  TYR B CD1   1 
ATOM   2256 C  CD2   . TYR B 1 91  ? -0.130  22.958  27.867  1.00 87.00  ? 39  TYR B CD2   1 
ATOM   2257 C  CE1   . TYR B 1 91  ? 2.631   23.030  27.894  1.00 82.24  ? 39  TYR B CE1   1 
ATOM   2258 C  CE2   . TYR B 1 91  ? 0.541   24.008  27.267  1.00 83.36  ? 39  TYR B CE2   1 
ATOM   2259 C  CZ    . TYR B 1 91  ? 1.924   24.040  27.282  1.00 82.51  ? 39  TYR B CZ    1 
ATOM   2260 O  OH    . TYR B 1 91  ? 2.612   25.079  26.684  1.00 81.22  ? 39  TYR B OH    1 
ATOM   2261 N  N     . ARG B 1 92  ? -0.053  23.295  31.180  1.00 88.44  ? 40  ARG B N     1 
ATOM   2262 C  CA    . ARG B 1 92  ? -0.514  24.632  31.549  1.00 93.10  ? 40  ARG B CA    1 
ATOM   2263 C  C     . ARG B 1 92  ? 0.398   25.685  30.932  1.00 93.48  ? 40  ARG B C     1 
ATOM   2264 O  O     . ARG B 1 92  ? 1.625   25.561  31.001  1.00 94.52  ? 40  ARG B O     1 
ATOM   2265 C  CB    . ARG B 1 92  ? -0.544  24.811  33.078  1.00 92.22  ? 40  ARG B CB    1 
ATOM   2266 C  CG    . ARG B 1 92  ? -1.578  23.966  33.820  1.00 90.40  ? 40  ARG B CG    1 
ATOM   2267 C  CD    . ARG B 1 92  ? -1.477  24.175  35.308  1.00 90.78  ? 40  ARG B CD    1 
ATOM   2268 N  NE    . ARG B 1 92  ? -1.557  22.910  36.033  1.00 96.28  ? 40  ARG B NE    1 
ATOM   2269 C  CZ    . ARG B 1 92  ? -0.504  22.151  36.342  1.00 100.34 ? 40  ARG B CZ    1 
ATOM   2270 N  NH1   . ARG B 1 92  ? -0.672  21.012  37.011  1.00 100.00 ? 40  ARG B NH1   1 
ATOM   2271 N  NH2   . ARG B 1 92  ? 0.718   22.526  35.978  1.00 99.41  ? 40  ARG B NH2   1 
ATOM   2272 N  N     . ALA B 1 93  ? -0.192  26.730  30.354  1.00 87.24  ? 41  ALA B N     1 
ATOM   2273 C  CA    . ALA B 1 93  ? 0.577   27.894  29.923  1.00 82.50  ? 41  ALA B CA    1 
ATOM   2274 C  C     . ALA B 1 93  ? -0.001  29.179  30.532  1.00 88.47  ? 41  ALA B C     1 
ATOM   2275 O  O     . ALA B 1 93  ? 0.737   30.074  30.951  1.00 92.28  ? 41  ALA B O     1 
ATOM   2276 C  CB    . ALA B 1 93  ? 0.597   27.983  28.414  1.00 83.11  ? 41  ALA B CB    1 
ATOM   2277 N  N     . GLY B 1 101 ? -5.364  28.879  33.843  1.00 88.11  ? 42  GLY B N     1 
ATOM   2278 C  CA    . GLY B 1 101 ? -6.257  29.011  32.704  1.00 97.80  ? 42  GLY B CA    1 
ATOM   2279 C  C     . GLY B 1 101 ? -7.172  27.821  32.425  1.00 103.62 ? 42  GLY B C     1 
ATOM   2280 O  O     . GLY B 1 101 ? -8.385  27.999  32.247  1.00 100.13 ? 42  GLY B O     1 
ATOM   2281 N  N     . ARG B 1 102 ? -6.589  26.614  32.381  1.00 102.99 ? 43  ARG B N     1 
ATOM   2282 C  CA    . ARG B 1 102 ? -7.303  25.372  32.080  1.00 103.95 ? 43  ARG B CA    1 
ATOM   2283 C  C     . ARG B 1 102 ? -6.339  24.187  32.119  1.00 106.34 ? 43  ARG B C     1 
ATOM   2284 O  O     . ARG B 1 102 ? -5.150  24.345  31.826  1.00 107.66 ? 43  ARG B O     1 
ATOM   2285 C  CB    . ARG B 1 102 ? -7.985  25.454  30.707  1.00 103.32 ? 43  ARG B CB    1 
ATOM   2286 C  CG    . ARG B 1 102 ? -8.481  24.127  30.136  1.00 101.86 ? 43  ARG B CG    1 
ATOM   2287 C  CD    . ARG B 1 102 ? -9.567  24.332  29.084  1.00 104.07 ? 43  ARG B CD    1 
ATOM   2288 N  NE    . ARG B 1 102 ? -9.077  25.008  27.880  1.00 109.54 ? 43  ARG B NE    1 
ATOM   2289 C  CZ    . ARG B 1 102 ? -9.151  26.321  27.667  1.00 109.22 ? 43  ARG B CZ    1 
ATOM   2290 N  NH1   . ARG B 1 102 ? -8.680  26.841  26.539  1.00 103.13 ? 43  ARG B NH1   1 
ATOM   2291 N  NH2   . ARG B 1 102 ? -9.689  27.118  28.583  1.00 108.36 ? 43  ARG B NH2   1 
ATOM   2292 N  N     . GLY B 1 103 ? -6.828  22.999  32.480  1.00 101.22 ? 44  GLY B N     1 
ATOM   2293 C  CA    . GLY B 1 103 ? -6.007  21.809  32.525  1.00 101.46 ? 44  GLY B CA    1 
ATOM   2294 C  C     . GLY B 1 103 ? -6.223  20.902  31.314  1.00 102.19 ? 44  GLY B C     1 
ATOM   2295 O  O     . GLY B 1 103 ? -7.321  20.392  31.112  1.00 102.84 ? 44  GLY B O     1 
ATOM   2296 N  N     . GLN B 1 104 ? -5.161  20.720  30.538  1.00 99.30  ? 45  GLN B N     1 
ATOM   2297 C  CA    . GLN B 1 104 ? -5.167  19.821  29.380  1.00 100.68 ? 45  GLN B CA    1 
ATOM   2298 C  C     . GLN B 1 104 ? -4.336  18.581  29.714  1.00 98.14  ? 45  GLN B C     1 
ATOM   2299 O  O     . GLN B 1 104 ? -3.153  18.698  30.058  1.00 95.78  ? 45  GLN B O     1 
ATOM   2300 C  CB    . GLN B 1 104 ? -4.616  20.511  28.124  1.00 97.49  ? 45  GLN B CB    1 
ATOM   2301 C  CG    . GLN B 1 104 ? -5.229  21.879  27.758  1.00 100.32 ? 45  GLN B CG    1 
ATOM   2302 C  CD    . GLN B 1 104 ? -4.571  23.077  28.465  1.00 111.53 ? 45  GLN B CD    1 
ATOM   2303 O  OE1   . GLN B 1 104 ? -3.959  22.942  29.534  1.00 103.89 ? 45  GLN B OE1   1 
ATOM   2304 N  NE2   . GLN B 1 104 ? -4.699  24.258  27.857  1.00 110.85 ? 45  GLN B NE2   1 
ATOM   2305 N  N     . ARG B 1 105 ? -4.948  17.399  29.601  1.00 96.09  ? 46  ARG B N     1 
ATOM   2306 C  CA    . ARG B 1 105 ? -4.303  16.151  30.000  1.00 93.36  ? 46  ARG B CA    1 
ATOM   2307 C  C     . ARG B 1 105 ? -3.573  15.526  28.812  1.00 92.66  ? 46  ARG B C     1 
ATOM   2308 O  O     . ARG B 1 105 ? -4.064  15.562  27.680  1.00 96.14  ? 46  ARG B O     1 
ATOM   2309 C  CB    . ARG B 1 105 ? -5.337  15.180  30.582  1.00 90.43  ? 46  ARG B CB    1 
ATOM   2310 C  CG    . ARG B 1 105 ? -5.417  15.233  32.109  1.00 89.80  ? 46  ARG B CG    1 
ATOM   2311 C  CD    . ARG B 1 105 ? -6.805  14.909  32.669  1.00 92.63  ? 46  ARG B CD    1 
ATOM   2312 N  NE    . ARG B 1 105 ? -6.715  14.325  34.011  1.00 95.90  ? 46  ARG B NE    1 
ATOM   2313 C  CZ    . ARG B 1 105 ? -6.904  14.990  35.156  1.00 98.06  ? 46  ARG B CZ    1 
ATOM   2314 N  NH1   . ARG B 1 105 ? -7.204  16.287  35.150  1.00 88.39  ? 46  ARG B NH1   1 
ATOM   2315 N  NH2   . ARG B 1 105 ? -6.786  14.352  36.321  1.00 92.88  ? 46  ARG B NH2   1 
ATOM   2316 N  N     . ILE B 1 106 ? -2.386  14.970  29.072  1.00 87.28  ? 47  ILE B N     1 
ATOM   2317 C  CA    . ILE B 1 106 ? -1.478  14.523  28.017  1.00 78.28  ? 47  ILE B CA    1 
ATOM   2318 C  C     . ILE B 1 106 ? -0.857  13.182  28.371  1.00 77.86  ? 47  ILE B C     1 
ATOM   2319 O  O     . ILE B 1 106 ? -0.411  12.971  29.503  1.00 86.04  ? 47  ILE B O     1 
ATOM   2320 C  CB    . ILE B 1 106 ? -0.346  15.533  27.761  1.00 80.67  ? 47  ILE B CB    1 
ATOM   2321 C  CG1   . ILE B 1 106 ? -0.885  16.956  27.632  1.00 87.75  ? 47  ILE B CG1   1 
ATOM   2322 C  CG2   . ILE B 1 106 ? 0.396   15.148  26.516  1.00 83.18  ? 47  ILE B CG2   1 
ATOM   2323 C  CD1   . ILE B 1 106 ? 0.097   17.905  26.974  1.00 83.68  ? 47  ILE B CD1   1 
ATOM   2324 N  N     . HIS B 1 107 ? -0.801  12.288  27.390  1.00 79.30  ? 48  HIS B N     1 
ATOM   2325 C  CA    . HIS B 1 107 ? 0.034   11.095  27.450  1.00 77.55  ? 48  HIS B CA    1 
ATOM   2326 C  C     . HIS B 1 107 ? 1.299   11.381  26.655  1.00 69.91  ? 48  HIS B C     1 
ATOM   2327 O  O     . HIS B 1 107 ? 1.227   11.870  25.528  1.00 75.01  ? 48  HIS B O     1 
ATOM   2328 C  CB    . HIS B 1 107 ? -0.700  9.873   26.888  1.00 79.72  ? 48  HIS B CB    1 
ATOM   2329 C  CG    . HIS B 1 107 ? 0.023   8.577   27.100  1.00 79.75  ? 48  HIS B CG    1 
ATOM   2330 N  ND1   . HIS B 1 107 ? -0.548  7.505   27.751  1.00 89.62  ? 48  HIS B ND1   1 
ATOM   2331 C  CD2   . HIS B 1 107 ? 1.267   8.177   26.740  1.00 74.63  ? 48  HIS B CD2   1 
ATOM   2332 C  CE1   . HIS B 1 107 ? 0.312   6.501   27.790  1.00 85.88  ? 48  HIS B CE1   1 
ATOM   2333 N  NE2   . HIS B 1 107 ? 1.422   6.883   27.182  1.00 80.11  ? 48  HIS B NE2   1 
ATOM   2334 N  N     . LEU B 1 108 ? 2.452   11.119  27.248  1.00 68.61  ? 49  LEU B N     1 
ATOM   2335 C  CA    . LEU B 1 108 ? 3.722   11.412  26.606  1.00 65.62  ? 49  LEU B CA    1 
ATOM   2336 C  C     . LEU B 1 108 ? 4.390   10.129  26.149  1.00 68.22  ? 49  LEU B C     1 
ATOM   2337 O  O     . LEU B 1 108 ? 4.430   9.138   26.888  1.00 60.92  ? 49  LEU B O     1 
ATOM   2338 C  CB    . LEU B 1 108 ? 4.661   12.157  27.540  1.00 66.61  ? 49  LEU B CB    1 
ATOM   2339 C  CG    . LEU B 1 108 ? 4.887   13.609  27.170  1.00 64.48  ? 49  LEU B CG    1 
ATOM   2340 C  CD1   . LEU B 1 108 ? 3.556   14.300  27.110  1.00 72.20  ? 49  LEU B CD1   1 
ATOM   2341 C  CD2   . LEU B 1 108 ? 5.799   14.268  28.200  1.00 64.76  ? 49  LEU B CD2   1 
ATOM   2342 N  N     . GLN B 1 109 ? 4.901   10.157  24.919  1.00 66.04  ? 50  GLN B N     1 
ATOM   2343 C  CA    . GLN B 1 109 ? 5.682   9.069   24.342  1.00 59.28  ? 50  GLN B CA    1 
ATOM   2344 C  C     . GLN B 1 109 ? 7.090   9.614   24.132  1.00 57.04  ? 50  GLN B C     1 
ATOM   2345 O  O     . GLN B 1 109 ? 7.319   10.415  23.217  1.00 58.04  ? 50  GLN B O     1 
ATOM   2346 C  CB    . GLN B 1 109 ? 5.060   8.588   23.038  1.00 63.59  ? 50  GLN B CB    1 
ATOM   2347 C  CG    . GLN B 1 109 ? 5.947   7.655   22.228  1.00 57.66  ? 50  GLN B CG    1 
ATOM   2348 C  CD    . GLN B 1 109 ? 5.142   6.580   21.545  1.00 55.45  ? 50  GLN B CD    1 
ATOM   2349 O  OE1   . GLN B 1 109 ? 4.078   6.847   20.997  1.00 54.43  ? 50  GLN B OE1   1 
ATOM   2350 N  NE2   . GLN B 1 109 ? 5.630   5.346   21.602  1.00 57.45  ? 50  GLN B NE2   1 
ATOM   2351 N  N     . LEU B 1 110 ? 8.039   9.191   24.966  1.00 49.13  ? 51  LEU B N     1 
ATOM   2352 C  CA    . LEU B 1 110 ? 9.396   9.735   24.905  1.00 53.56  ? 51  LEU B CA    1 
ATOM   2353 C  C     . LEU B 1 110 ? 10.298  8.682   24.258  1.00 56.13  ? 51  LEU B C     1 
ATOM   2354 O  O     . LEU B 1 110 ? 10.802  7.770   24.918  1.00 54.18  ? 51  LEU B O     1 
ATOM   2355 C  CB    . LEU B 1 110 ? 9.875   10.166  26.292  1.00 60.22  ? 51  LEU B CB    1 
ATOM   2356 C  CG    . LEU B 1 110 ? 8.866   10.988  27.119  1.00 55.52  ? 51  LEU B CG    1 
ATOM   2357 C  CD1   . LEU B 1 110 ? 8.241   10.142  28.189  1.00 55.16  ? 51  LEU B CD1   1 
ATOM   2358 C  CD2   . LEU B 1 110 ? 9.513   12.219  27.733  1.00 61.70  ? 51  LEU B CD2   1 
ATOM   2359 N  N     . TRP B 1 111 ? 10.490  8.819   22.940  1.00 54.96  ? 52  TRP B N     1 
ATOM   2360 C  CA    . TRP B 1 111 ? 11.316  7.892   22.176  1.00 52.02  ? 52  TRP B CA    1 
ATOM   2361 C  C     . TRP B 1 111 ? 12.780  8.027   22.574  1.00 49.05  ? 52  TRP B C     1 
ATOM   2362 O  O     . TRP B 1 111 ? 13.359  9.118   22.492  1.00 50.01  ? 52  TRP B O     1 
ATOM   2363 C  CB    . TRP B 1 111 ? 11.179  8.167   20.673  1.00 53.62  ? 52  TRP B CB    1 
ATOM   2364 C  CG    . TRP B 1 111 ? 9.938   7.659   20.001  1.00 51.21  ? 52  TRP B CG    1 
ATOM   2365 C  CD1   . TRP B 1 111 ? 8.889   8.408   19.528  1.00 52.41  ? 52  TRP B CD1   1 
ATOM   2366 C  CD2   . TRP B 1 111 ? 9.632   6.297   19.685  1.00 51.80  ? 52  TRP B CD2   1 
ATOM   2367 N  NE1   . TRP B 1 111 ? 7.942   7.591   18.955  1.00 52.75  ? 52  TRP B NE1   1 
ATOM   2368 C  CE2   . TRP B 1 111 ? 8.371   6.291   19.041  1.00 53.66  ? 52  TRP B CE2   1 
ATOM   2369 C  CE3   . TRP B 1 111 ? 10.296  5.080   19.891  1.00 48.11  ? 52  TRP B CE3   1 
ATOM   2370 C  CZ2   . TRP B 1 111 ? 7.759   5.114   18.611  1.00 55.58  ? 52  TRP B CZ2   1 
ATOM   2371 C  CZ3   . TRP B 1 111 ? 9.694   3.914   19.458  1.00 48.34  ? 52  TRP B CZ3   1 
ATOM   2372 C  CH2   . TRP B 1 111 ? 8.434   3.939   18.823  1.00 56.70  ? 52  TRP B CH2   1 
ATOM   2373 N  N     . ASP B 1 112 ? 13.393  6.909   22.950  1.00 45.15  ? 53  ASP B N     1 
ATOM   2374 C  CA    . ASP B 1 112 ? 14.789  6.871   23.387  1.00 50.81  ? 53  ASP B CA    1 
ATOM   2375 C  C     . ASP B 1 112 ? 15.620  6.148   22.327  1.00 52.62  ? 53  ASP B C     1 
ATOM   2376 O  O     . ASP B 1 112 ? 15.681  4.913   22.316  1.00 59.75  ? 53  ASP B O     1 
ATOM   2377 C  CB    . ASP B 1 112 ? 14.887  6.177   24.744  1.00 49.17  ? 53  ASP B CB    1 
ATOM   2378 C  CG    . ASP B 1 112 ? 16.309  6.113   25.278  1.00 54.52  ? 53  ASP B CG    1 
ATOM   2379 O  OD1   . ASP B 1 112 ? 16.539  5.336   26.239  1.00 60.16  ? 53  ASP B OD1   1 
ATOM   2380 O  OD2   . ASP B 1 112 ? 17.187  6.848   24.761  1.00 52.48  ? 53  ASP B OD2   1 
ATOM   2381 N  N     . THR B 1 113 ? 16.289  6.906   21.457  1.00 47.86  ? 54  THR B N     1 
ATOM   2382 C  CA    . THR B 1 113 ? 17.040  6.279   20.374  1.00 47.68  ? 54  THR B CA    1 
ATOM   2383 C  C     . THR B 1 113 ? 18.423  5.849   20.834  1.00 50.51  ? 54  THR B C     1 
ATOM   2384 O  O     . THR B 1 113 ? 19.067  6.517   21.652  1.00 48.81  ? 54  THR B O     1 
ATOM   2385 C  CB    . THR B 1 113 ? 17.210  7.211   19.177  1.00 43.90  ? 54  THR B CB    1 
ATOM   2386 O  OG1   . THR B 1 113 ? 18.247  8.163   19.443  1.00 47.38  ? 54  THR B OG1   1 
ATOM   2387 C  CG2   . THR B 1 113 ? 15.925  7.911   18.833  1.00 44.75  ? 54  THR B CG2   1 
ATOM   2388 N  N     . ALA B 1 114 ? 18.876  4.717   20.294  1.00 52.32  ? 55  ALA B N     1 
ATOM   2389 C  CA    . ALA B 1 114 ? 20.259  4.306   20.483  1.00 49.15  ? 55  ALA B CA    1 
ATOM   2390 C  C     . ALA B 1 114 ? 21.185  5.321   19.837  1.00 46.34  ? 55  ALA B C     1 
ATOM   2391 O  O     . ALA B 1 114 ? 20.885  5.867   18.775  1.00 51.54  ? 55  ALA B O     1 
ATOM   2392 C  CB    . ALA B 1 114 ? 20.489  2.935   19.874  1.00 54.60  ? 55  ALA B CB    1 
ATOM   2393 N  N     . GLY B 1 115 ? 22.302  5.592   20.486  1.00 49.51  ? 56  GLY B N     1 
ATOM   2394 C  CA    . GLY B 1 115 ? 23.191  6.600   19.961  1.00 50.04  ? 56  GLY B CA    1 
ATOM   2395 C  C     . GLY B 1 115 ? 24.291  6.052   19.107  1.00 49.41  ? 56  GLY B C     1 
ATOM   2396 O  O     . GLY B 1 115 ? 25.123  6.809   18.601  1.00 52.75  ? 56  GLY B O     1 
ATOM   2397 N  N     . LEU B 1 116 ? 24.302  4.743   18.907  1.00 56.42  ? 57  LEU B N     1 
ATOM   2398 C  CA    . LEU B 1 116 ? 25.379  4.070   18.203  1.00 63.07  ? 57  LEU B CA    1 
ATOM   2399 C  C     . LEU B 1 116 ? 25.205  4.125   16.679  1.00 64.18  ? 57  LEU B C     1 
ATOM   2400 O  O     . LEU B 1 116 ? 24.140  4.465   16.142  1.00 58.61  ? 57  LEU B O     1 
ATOM   2401 C  CB    . LEU B 1 116 ? 25.465  2.621   18.662  1.00 60.62  ? 57  LEU B CB    1 
ATOM   2402 C  CG    . LEU B 1 116 ? 25.690  2.501   20.161  1.00 56.10  ? 57  LEU B CG    1 
ATOM   2403 C  CD1   . LEU B 1 116 ? 24.312  2.462   20.910  1.00 53.54  ? 57  LEU B CD1   1 
ATOM   2404 C  CD2   . LEU B 1 116 ? 26.555  1.284   20.449  1.00 50.36  ? 57  LEU B CD2   1 
ATOM   2405 N  N     . GLU B 1 117 ? 26.299  3.797   15.986  1.00 63.89  ? 58  GLU B N     1 
ATOM   2406 C  CA    . GLU B 1 117 ? 26.276  3.708   14.533  1.00 66.71  ? 58  GLU B CA    1 
ATOM   2407 C  C     . GLU B 1 117 ? 25.516  2.465   14.067  1.00 67.30  ? 58  GLU B C     1 
ATOM   2408 O  O     . GLU B 1 117 ? 24.712  2.549   13.129  1.00 64.61  ? 58  GLU B O     1 
ATOM   2409 C  CB    . GLU B 1 117 ? 27.719  3.736   13.999  1.00 73.03  ? 58  GLU B CB    1 
ATOM   2410 C  CG    . GLU B 1 117 ? 28.522  2.383   14.046  1.00 82.96  ? 58  GLU B CG    1 
ATOM   2411 C  CD    . GLU B 1 117 ? 28.883  1.870   15.471  1.00 74.82  ? 58  GLU B CD    1 
ATOM   2412 O  OE1   . GLU B 1 117 ? 29.995  1.323   15.688  1.00 68.52  ? 58  GLU B OE1   1 
ATOM   2413 O  OE2   . GLU B 1 117 ? 28.039  1.969   16.384  1.00 66.33  ? 58  GLU B OE2   1 
ATOM   2414 N  N     . ARG B 1 118 ? 25.721  1.314   14.737  1.00 65.36  ? 59  ARG B N     1 
ATOM   2415 C  CA    . ARG B 1 118 ? 25.057  0.070   14.336  1.00 67.44  ? 59  ARG B CA    1 
ATOM   2416 C  C     . ARG B 1 118 ? 23.552  0.254   14.187  1.00 66.55  ? 59  ARG B C     1 
ATOM   2417 O  O     . ARG B 1 118 ? 22.920  -0.401  13.346  1.00 69.44  ? 59  ARG B O     1 
ATOM   2418 C  CB    . ARG B 1 118 ? 25.280  -1.063  15.354  1.00 70.56  ? 59  ARG B CB    1 
ATOM   2419 C  CG    . ARG B 1 118 ? 26.641  -1.212  16.019  1.00 75.98  ? 59  ARG B CG    1 
ATOM   2420 C  CD    . ARG B 1 118 ? 26.469  -1.805  17.438  1.00 67.94  ? 59  ARG B CD    1 
ATOM   2421 N  NE    . ARG B 1 118 ? 27.618  -1.611  18.328  1.00 68.37  ? 59  ARG B NE    1 
ATOM   2422 C  CZ    . ARG B 1 118 ? 28.226  -0.442  18.560  1.00 77.95  ? 59  ARG B CZ    1 
ATOM   2423 N  NH1   . ARG B 1 118 ? 27.829  0.688   17.983  1.00 77.04  ? 59  ARG B NH1   1 
ATOM   2424 N  NH2   . ARG B 1 118 ? 29.243  -0.385  19.403  1.00 85.38  ? 59  ARG B NH2   1 
ATOM   2425 N  N     . PHE B 1 119 ? 22.960  1.110   15.023  1.00 66.48  ? 60  PHE B N     1 
ATOM   2426 C  CA    . PHE B 1 119 ? 21.522  1.337   15.067  1.00 64.55  ? 60  PHE B CA    1 
ATOM   2427 C  C     . PHE B 1 119 ? 21.139  2.647   14.407  1.00 62.19  ? 60  PHE B C     1 
ATOM   2428 O  O     . PHE B 1 119 ? 19.987  3.086   14.553  1.00 58.23  ? 60  PHE B O     1 
ATOM   2429 C  CB    . PHE B 1 119 ? 21.010  1.335   16.513  1.00 62.44  ? 60  PHE B CB    1 
ATOM   2430 C  CG    . PHE B 1 119 ? 21.547  0.214   17.355  1.00 62.77  ? 60  PHE B CG    1 
ATOM   2431 C  CD1   . PHE B 1 119 ? 20.944  -1.034  17.344  1.00 63.29  ? 60  PHE B CD1   1 
ATOM   2432 C  CD2   . PHE B 1 119 ? 22.648  0.410   18.174  1.00 65.31  ? 60  PHE B CD2   1 
ATOM   2433 C  CE1   . PHE B 1 119 ? 21.431  -2.071  18.139  1.00 65.12  ? 60  PHE B CE1   1 
ATOM   2434 C  CE2   . PHE B 1 119 ? 23.145  -0.629  18.972  1.00 66.23  ? 60  PHE B CE2   1 
ATOM   2435 C  CZ    . PHE B 1 119 ? 22.533  -1.867  18.952  1.00 64.84  ? 60  PHE B CZ    1 
ATOM   2436 N  N     . ARG B 1 120 ? 22.077  3.282   13.688  1.00 58.35  ? 61  ARG B N     1 
ATOM   2437 C  CA    . ARG B 1 120 ? 21.837  4.647   13.238  1.00 58.55  ? 61  ARG B CA    1 
ATOM   2438 C  C     . ARG B 1 120 ? 20.661  4.721   12.283  1.00 57.47  ? 61  ARG B C     1 
ATOM   2439 O  O     . ARG B 1 120 ? 19.951  5.730   12.262  1.00 59.61  ? 61  ARG B O     1 
ATOM   2440 C  CB    . ARG B 1 120 ? 23.084  5.236   12.586  1.00 59.41  ? 61  ARG B CB    1 
ATOM   2441 C  CG    . ARG B 1 120 ? 22.989  6.741   12.410  1.00 59.16  ? 61  ARG B CG    1 
ATOM   2442 C  CD    . ARG B 1 120 ? 22.669  7.424   13.735  1.00 61.34  ? 61  ARG B CD    1 
ATOM   2443 N  NE    . ARG B 1 120 ? 23.618  7.062   14.794  1.00 63.23  ? 61  ARG B NE    1 
ATOM   2444 C  CZ    . ARG B 1 120 ? 24.773  7.694   14.990  1.00 64.02  ? 61  ARG B CZ    1 
ATOM   2445 N  NH1   . ARG B 1 120 ? 25.117  8.701   14.187  1.00 60.32  ? 61  ARG B NH1   1 
ATOM   2446 N  NH2   . ARG B 1 120 ? 25.588  7.319   15.968  1.00 58.98  ? 61  ARG B NH2   1 
ATOM   2447 N  N     . SER B 1 121 ? 20.434  3.663   11.500  1.00 58.22  ? 62  SER B N     1 
ATOM   2448 C  CA    . SER B 1 121 ? 19.326  3.656   10.550  1.00 57.34  ? 62  SER B CA    1 
ATOM   2449 C  C     . SER B 1 121 ? 17.991  3.461   11.257  1.00 56.55  ? 62  SER B C     1 
ATOM   2450 O  O     . SER B 1 121 ? 17.013  4.165   10.966  1.00 48.40  ? 62  SER B O     1 
ATOM   2451 C  CB    . SER B 1 121 ? 19.548  2.559   9.508   1.00 65.36  ? 62  SER B CB    1 
ATOM   2452 O  OG    . SER B 1 121 ? 20.922  2.437   9.177   1.00 69.22  ? 62  SER B OG    1 
ATOM   2453 N  N     . LEU B 1 122 ? 17.938  2.514   12.197  1.00 61.98  ? 63  LEU B N     1 
ATOM   2454 C  CA    . LEU B 1 122 ? 16.724  2.289   12.980  1.00 61.41  ? 63  LEU B CA    1 
ATOM   2455 C  C     . LEU B 1 122 ? 16.329  3.531   13.794  1.00 60.01  ? 63  LEU B C     1 
ATOM   2456 O  O     . LEU B 1 122 ? 15.147  3.904   13.864  1.00 54.32  ? 63  LEU B O     1 
ATOM   2457 C  CB    . LEU B 1 122 ? 16.940  1.078   13.888  1.00 56.44  ? 63  LEU B CB    1 
ATOM   2458 C  CG    . LEU B 1 122 ? 15.807  0.581   14.789  1.00 57.79  ? 63  LEU B CG    1 
ATOM   2459 C  CD1   . LEU B 1 122 ? 14.467  0.523   14.068  1.00 54.05  ? 63  LEU B CD1   1 
ATOM   2460 C  CD2   . LEU B 1 122 ? 16.172  -0.788  15.349  1.00 60.93  ? 63  LEU B CD2   1 
ATOM   2461 N  N     . THR B 1 123 ? 17.301  4.196   14.413  1.00 54.15  ? 64  THR B N     1 
ATOM   2462 C  CA    . THR B 1 123 ? 16.939  5.382   15.179  1.00 57.76  ? 64  THR B CA    1 
ATOM   2463 C  C     . THR B 1 123 ? 16.466  6.491   14.248  1.00 53.94  ? 64  THR B C     1 
ATOM   2464 O  O     . THR B 1 123 ? 15.322  6.960   14.355  1.00 53.32  ? 64  THR B O     1 
ATOM   2465 C  CB    . THR B 1 123 ? 18.110  5.821   16.064  1.00 58.09  ? 64  THR B CB    1 
ATOM   2466 O  OG1   . THR B 1 123 ? 19.311  5.915   15.298  1.00 65.12  ? 64  THR B OG1   1 
ATOM   2467 C  CG2   . THR B 1 123 ? 18.333  4.773   17.171  1.00 48.15  ? 64  THR B CG2   1 
ATOM   2468 N  N     . THR B 1 124 ? 17.311  6.866   13.277  1.00 58.09  ? 65  THR B N     1 
ATOM   2469 C  CA    . THR B 1 124 ? 16.948  7.828   12.233  1.00 57.65  ? 65  THR B CA    1 
ATOM   2470 C  C     . THR B 1 124 ? 15.563  7.573   11.640  1.00 57.34  ? 65  THR B C     1 
ATOM   2471 O  O     . THR B 1 124 ? 14.910  8.505   11.160  1.00 59.03  ? 65  THR B O     1 
ATOM   2472 C  CB    . THR B 1 124 ? 17.994  7.787   11.115  1.00 61.08  ? 65  THR B CB    1 
ATOM   2473 O  OG1   . THR B 1 124 ? 19.311  7.922   11.675  1.00 67.27  ? 65  THR B OG1   1 
ATOM   2474 C  CG2   . THR B 1 124 ? 17.765  8.886   10.094  1.00 61.35  ? 65  THR B CG2   1 
ATOM   2475 N  N     . ALA B 1 125 ? 15.105  6.320   11.652  1.00 57.36  ? 66  ALA B N     1 
ATOM   2476 C  CA    . ALA B 1 125 ? 13.788  6.007   11.110  1.00 54.62  ? 66  ALA B CA    1 
ATOM   2477 C  C     . ALA B 1 125 ? 12.685  6.666   11.925  1.00 59.37  ? 66  ALA B C     1 
ATOM   2478 O  O     . ALA B 1 125 ? 11.731  7.219   11.365  1.00 52.86  ? 66  ALA B O     1 
ATOM   2479 C  CB    . ALA B 1 125 ? 13.586  4.494   11.082  1.00 55.27  ? 66  ALA B CB    1 
ATOM   2480 N  N     . PHE B 1 126 ? 12.798  6.605   13.257  1.00 58.93  ? 67  PHE B N     1 
ATOM   2481 C  CA    . PHE B 1 126 ? 11.760  7.137   14.125  1.00 55.82  ? 67  PHE B CA    1 
ATOM   2482 C  C     . PHE B 1 126 ? 11.842  8.642   14.298  1.00 61.11  ? 67  PHE B C     1 
ATOM   2483 O  O     . PHE B 1 126 ? 10.963  9.215   14.947  1.00 68.11  ? 67  PHE B O     1 
ATOM   2484 C  CB    . PHE B 1 126 ? 11.810  6.434   15.479  1.00 54.96  ? 67  PHE B CB    1 
ATOM   2485 C  CG    . PHE B 1 126 ? 11.283  5.037   15.420  1.00 58.43  ? 67  PHE B CG    1 
ATOM   2486 C  CD1   . PHE B 1 126 ? 12.094  3.998   14.970  1.00 55.98  ? 67  PHE B CD1   1 
ATOM   2487 C  CD2   . PHE B 1 126 ? 9.958   4.769   15.741  1.00 55.46  ? 67  PHE B CD2   1 
ATOM   2488 C  CE1   . PHE B 1 126 ? 11.606  2.714   14.879  1.00 52.40  ? 67  PHE B CE1   1 
ATOM   2489 C  CE2   . PHE B 1 126 ? 9.462   3.492   15.646  1.00 56.73  ? 67  PHE B CE2   1 
ATOM   2490 C  CZ    . PHE B 1 126 ? 10.287  2.463   15.217  1.00 59.25  ? 67  PHE B CZ    1 
ATOM   2491 N  N     . PHE B 1 127 ? 12.848  9.297   13.715  1.00 57.39  ? 68  PHE B N     1 
ATOM   2492 C  CA    . PHE B 1 127 ? 12.848  10.752  13.645  1.00 59.15  ? 68  PHE B CA    1 
ATOM   2493 C  C     . PHE B 1 127 ? 11.566  11.301  13.038  1.00 65.40  ? 68  PHE B C     1 
ATOM   2494 O  O     . PHE B 1 127 ? 11.249  12.479  13.238  1.00 71.01  ? 68  PHE B O     1 
ATOM   2495 C  CB    . PHE B 1 127 ? 14.019  11.260  12.798  1.00 62.53  ? 68  PHE B CB    1 
ATOM   2496 C  CG    . PHE B 1 127 ? 15.366  11.088  13.434  1.00 57.17  ? 68  PHE B CG    1 
ATOM   2497 C  CD1   . PHE B 1 127 ? 15.532  10.287  14.549  1.00 51.38  ? 68  PHE B CD1   1 
ATOM   2498 C  CD2   . PHE B 1 127 ? 16.474  11.720  12.890  1.00 52.81  ? 68  PHE B CD2   1 
ATOM   2499 C  CE1   . PHE B 1 127 ? 16.778  10.127  15.119  1.00 55.20  ? 68  PHE B CE1   1 
ATOM   2500 C  CE2   . PHE B 1 127 ? 17.724  11.560  13.449  1.00 56.28  ? 68  PHE B CE2   1 
ATOM   2501 C  CZ    . PHE B 1 127 ? 17.881  10.763  14.567  1.00 56.90  ? 68  PHE B CZ    1 
ATOM   2502 N  N     . ARG B 1 128 ? 10.838  10.496  12.276  1.00 64.45  ? 69  ARG B N     1 
ATOM   2503 C  CA    . ARG B 1 128 ? 9.661   10.988  11.580  1.00 66.04  ? 69  ARG B CA    1 
ATOM   2504 C  C     . ARG B 1 128 ? 8.379   10.830  12.381  1.00 67.35  ? 69  ARG B C     1 
ATOM   2505 O  O     . ARG B 1 128 ? 7.321   11.235  11.893  1.00 71.55  ? 69  ARG B O     1 
ATOM   2506 C  CB    . ARG B 1 128 ? 9.511   10.276  10.237  1.00 64.97  ? 69  ARG B CB    1 
ATOM   2507 C  CG    . ARG B 1 128 ? 8.932   8.866   10.301  1.00 63.32  ? 69  ARG B CG    1 
ATOM   2508 C  CD    . ARG B 1 128 ? 9.601   7.967   9.263   1.00 60.25  ? 69  ARG B CD    1 
ATOM   2509 N  NE    . ARG B 1 128 ? 11.055  8.118   9.317   1.00 62.52  ? 69  ARG B NE    1 
ATOM   2510 C  CZ    . ARG B 1 128 ? 11.798  8.708   8.380   1.00 62.26  ? 69  ARG B CZ    1 
ATOM   2511 N  NH1   . ARG B 1 128 ? 11.235  9.209   7.275   1.00 59.97  ? 69  ARG B NH1   1 
ATOM   2512 N  NH2   . ARG B 1 128 ? 13.115  8.792   8.555   1.00 59.34  ? 69  ARG B NH2   1 
ATOM   2513 N  N     . ASP B 1 129 ? 8.443   10.246  13.579  1.00 65.24  ? 70  ASP B N     1 
ATOM   2514 C  CA    . ASP B 1 129 ? 7.279   10.073  14.441  1.00 68.69  ? 70  ASP B CA    1 
ATOM   2515 C  C     . ASP B 1 129 ? 7.259   11.061  15.603  1.00 68.27  ? 70  ASP B C     1 
ATOM   2516 O  O     . ASP B 1 129 ? 6.262   11.126  16.335  1.00 67.16  ? 70  ASP B O     1 
ATOM   2517 C  CB    . ASP B 1 129 ? 7.231   8.628   14.970  1.00 66.87  ? 70  ASP B CB    1 
ATOM   2518 C  CG    . ASP B 1 129 ? 5.885   8.261   15.608  1.00 70.98  ? 70  ASP B CG    1 
ATOM   2519 O  OD1   . ASP B 1 129 ? 5.886   7.783   16.767  1.00 69.37  ? 70  ASP B OD1   1 
ATOM   2520 O  OD2   . ASP B 1 129 ? 4.828   8.441   14.960  1.00 72.93  ? 70  ASP B OD2   1 
ATOM   2521 N  N     . ALA B 1 130 ? 8.309   11.854  15.770  1.00 61.16  ? 71  ALA B N     1 
ATOM   2522 C  CA    . ALA B 1 130 ? 8.378   12.773  16.891  1.00 62.93  ? 71  ALA B CA    1 
ATOM   2523 C  C     . ALA B 1 130 ? 7.892   14.165  16.499  1.00 60.20  ? 71  ALA B C     1 
ATOM   2524 O  O     . ALA B 1 130 ? 8.127   14.638  15.390  1.00 58.97  ? 71  ALA B O     1 
ATOM   2525 C  CB    . ALA B 1 130 ? 9.806   12.854  17.424  1.00 60.09  ? 71  ALA B CB    1 
ATOM   2526 N  N     . MET B 1 131 ? 7.216   14.824  17.439  1.00 61.56  ? 72  MET B N     1 
ATOM   2527 C  CA    . MET B 1 131 ? 6.836   16.223  17.287  1.00 57.61  ? 72  MET B CA    1 
ATOM   2528 C  C     . MET B 1 131 ? 7.910   17.178  17.784  1.00 52.65  ? 72  MET B C     1 
ATOM   2529 O  O     . MET B 1 131 ? 7.999   18.313  17.303  1.00 57.45  ? 72  MET B O     1 
ATOM   2530 C  CB    . MET B 1 131 ? 5.535   16.498  18.042  1.00 51.67  ? 72  MET B CB    1 
ATOM   2531 C  CG    . MET B 1 131 ? 4.646   15.286  18.136  1.00 54.18  ? 72  MET B CG    1 
ATOM   2532 S  SD    . MET B 1 131 ? 2.983   15.726  18.637  1.00 54.82  ? 72  MET B SD    1 
ATOM   2533 C  CE    . MET B 1 131 ? 2.110   14.179  18.308  1.00 55.57  ? 72  MET B CE    1 
ATOM   2534 N  N     . GLY B 1 132 ? 8.712   16.747  18.741  1.00 53.44  ? 73  GLY B N     1 
ATOM   2535 C  CA    . GLY B 1 132 ? 9.810   17.556  19.232  1.00 54.57  ? 73  GLY B CA    1 
ATOM   2536 C  C     . GLY B 1 132 ? 10.933  16.651  19.669  1.00 55.02  ? 73  GLY B C     1 
ATOM   2537 O  O     . GLY B 1 132 ? 10.711  15.506  20.078  1.00 58.41  ? 73  GLY B O     1 
ATOM   2538 N  N     . PHE B 1 133 ? 12.150  17.169  19.578  1.00 52.65  ? 74  PHE B N     1 
ATOM   2539 C  CA    . PHE B 1 133 ? 13.346  16.384  19.817  1.00 52.79  ? 74  PHE B CA    1 
ATOM   2540 C  C     . PHE B 1 133 ? 14.143  16.982  20.965  1.00 55.76  ? 74  PHE B C     1 
ATOM   2541 O  O     . PHE B 1 133 ? 14.323  18.203  21.043  1.00 59.09  ? 74  PHE B O     1 
ATOM   2542 C  CB    . PHE B 1 133 ? 14.217  16.316  18.551  1.00 57.33  ? 74  PHE B CB    1 
ATOM   2543 C  CG    . PHE B 1 133 ? 13.491  15.775  17.340  1.00 60.81  ? 74  PHE B CG    1 
ATOM   2544 C  CD1   . PHE B 1 133 ? 13.336  14.411  17.167  1.00 58.85  ? 74  PHE B CD1   1 
ATOM   2545 C  CD2   . PHE B 1 133 ? 12.964  16.633  16.382  1.00 62.47  ? 74  PHE B CD2   1 
ATOM   2546 C  CE1   . PHE B 1 133 ? 12.686  13.920  16.072  1.00 64.34  ? 74  PHE B CE1   1 
ATOM   2547 C  CE2   . PHE B 1 133 ? 12.305  16.149  15.287  1.00 60.38  ? 74  PHE B CE2   1 
ATOM   2548 C  CZ    . PHE B 1 133 ? 12.166  14.789  15.126  1.00 70.98  ? 74  PHE B CZ    1 
ATOM   2549 N  N     . LEU B 1 134 ? 14.628  16.121  21.853  1.00 46.49  ? 75  LEU B N     1 
ATOM   2550 C  CA    . LEU B 1 134 ? 15.576  16.540  22.870  1.00 47.99  ? 75  LEU B CA    1 
ATOM   2551 C  C     . LEU B 1 134 ? 16.954  16.077  22.420  1.00 46.38  ? 75  LEU B C     1 
ATOM   2552 O  O     . LEU B 1 134 ? 17.220  14.874  22.350  1.00 44.12  ? 75  LEU B O     1 
ATOM   2553 C  CB    . LEU B 1 134 ? 15.223  15.987  24.248  1.00 53.09  ? 75  LEU B CB    1 
ATOM   2554 C  CG    . LEU B 1 134 ? 15.829  16.867  25.359  1.00 56.73  ? 75  LEU B CG    1 
ATOM   2555 C  CD1   . LEU B 1 134 ? 15.058  18.195  25.489  1.00 57.48  ? 75  LEU B CD1   1 
ATOM   2556 C  CD2   . LEU B 1 134 ? 15.884  16.144  26.686  1.00 50.41  ? 75  LEU B CD2   1 
ATOM   2557 N  N     . LEU B 1 135 ? 17.824  17.026  22.102  1.00 47.31  ? 76  LEU B N     1 
ATOM   2558 C  CA    . LEU B 1 135 ? 19.129  16.695  21.548  1.00 49.86  ? 76  LEU B CA    1 
ATOM   2559 C  C     . LEU B 1 135 ? 20.172  16.842  22.639  1.00 45.43  ? 76  LEU B C     1 
ATOM   2560 O  O     . LEU B 1 135 ? 20.385  17.943  23.151  1.00 48.30  ? 76  LEU B O     1 
ATOM   2561 C  CB    . LEU B 1 135 ? 19.465  17.578  20.348  1.00 53.31  ? 76  LEU B CB    1 
ATOM   2562 C  CG    . LEU B 1 135 ? 20.811  17.245  19.719  1.00 49.40  ? 76  LEU B CG    1 
ATOM   2563 C  CD1   . LEU B 1 135 ? 20.530  16.348  18.555  1.00 54.72  ? 76  LEU B CD1   1 
ATOM   2564 C  CD2   . LEU B 1 135 ? 21.531  18.463  19.238  1.00 55.43  ? 76  LEU B CD2   1 
ATOM   2565 N  N     . LEU B 1 136 ? 20.810  15.734  22.983  1.00 46.04  ? 77  LEU B N     1 
ATOM   2566 C  CA    . LEU B 1 136 ? 21.708  15.683  24.130  1.00 50.97  ? 77  LEU B CA    1 
ATOM   2567 C  C     . LEU B 1 136 ? 23.163  15.633  23.692  1.00 52.34  ? 77  LEU B C     1 
ATOM   2568 O  O     . LEU B 1 136 ? 23.528  14.917  22.749  1.00 49.85  ? 77  LEU B O     1 
ATOM   2569 C  CB    . LEU B 1 136 ? 21.414  14.463  25.007  1.00 42.68  ? 77  LEU B CB    1 
ATOM   2570 C  CG    . LEU B 1 136 ? 20.580  14.648  26.267  1.00 45.50  ? 77  LEU B CG    1 
ATOM   2571 C  CD1   . LEU B 1 136 ? 19.127  14.808  25.886  1.00 40.30  ? 77  LEU B CD1   1 
ATOM   2572 C  CD2   . LEU B 1 136 ? 20.784  13.492  27.281  1.00 48.72  ? 77  LEU B CD2   1 
ATOM   2573 N  N     . PHE B 1 137 ? 23.985  16.409  24.386  1.00 54.98  ? 78  PHE B N     1 
ATOM   2574 C  CA    . PHE B 1 137 ? 25.413  16.173  24.455  1.00 55.26  ? 78  PHE B CA    1 
ATOM   2575 C  C     . PHE B 1 137 ? 25.795  16.038  25.922  1.00 58.10  ? 78  PHE B C     1 
ATOM   2576 O  O     . PHE B 1 137 ? 25.106  16.547  26.812  1.00 58.98  ? 78  PHE B O     1 
ATOM   2577 C  CB    . PHE B 1 137 ? 26.206  17.285  23.766  1.00 53.44  ? 78  PHE B CB    1 
ATOM   2578 C  CG    . PHE B 1 137 ? 26.055  18.634  24.390  1.00 54.89  ? 78  PHE B CG    1 
ATOM   2579 C  CD1   . PHE B 1 137 ? 24.948  19.421  24.103  1.00 52.76  ? 78  PHE B CD1   1 
ATOM   2580 C  CD2   . PHE B 1 137 ? 27.043  19.139  25.237  1.00 56.79  ? 78  PHE B CD2   1 
ATOM   2581 C  CE1   . PHE B 1 137 ? 24.815  20.677  24.665  1.00 56.74  ? 78  PHE B CE1   1 
ATOM   2582 C  CE2   . PHE B 1 137 ? 26.916  20.393  25.803  1.00 57.28  ? 78  PHE B CE2   1 
ATOM   2583 C  CZ    . PHE B 1 137 ? 25.803  21.167  25.516  1.00 56.77  ? 78  PHE B CZ    1 
ATOM   2584 N  N     . ASP B 1 138 ? 26.876  15.305  26.164  1.00 61.66  ? 79  ASP B N     1 
ATOM   2585 C  CA    . ASP B 1 138 ? 27.490  15.183  27.483  1.00 56.28  ? 79  ASP B CA    1 
ATOM   2586 C  C     . ASP B 1 138 ? 28.412  16.386  27.695  1.00 62.56  ? 79  ASP B C     1 
ATOM   2587 O  O     . ASP B 1 138 ? 29.317  16.630  26.884  1.00 67.81  ? 79  ASP B O     1 
ATOM   2588 C  CB    . ASP B 1 138 ? 28.240  13.844  27.548  1.00 54.44  ? 79  ASP B CB    1 
ATOM   2589 C  CG    . ASP B 1 138 ? 29.067  13.643  28.828  1.00 57.00  ? 79  ASP B CG    1 
ATOM   2590 O  OD1   . ASP B 1 138 ? 29.174  14.546  29.674  1.00 57.99  ? 79  ASP B OD1   1 
ATOM   2591 O  OD2   . ASP B 1 138 ? 29.644  12.539  28.992  1.00 60.65  ? 79  ASP B OD2   1 
ATOM   2592 N  N     . LEU B 1 139 ? 28.170  17.153  28.768  1.00 61.42  ? 80  LEU B N     1 
ATOM   2593 C  CA    . LEU B 1 139 ? 29.000  18.325  29.060  1.00 60.68  ? 80  LEU B CA    1 
ATOM   2594 C  C     . LEU B 1 139 ? 30.471  17.969  29.249  1.00 59.29  ? 80  LEU B C     1 
ATOM   2595 O  O     . LEU B 1 139 ? 31.331  18.837  29.079  1.00 61.41  ? 80  LEU B O     1 
ATOM   2596 C  CB    . LEU B 1 139 ? 28.476  19.060  30.305  1.00 55.56  ? 80  LEU B CB    1 
ATOM   2597 C  CG    . LEU B 1 139 ? 27.245  19.969  30.152  1.00 53.24  ? 80  LEU B CG    1 
ATOM   2598 C  CD1   . LEU B 1 139 ? 26.434  20.005  31.412  1.00 54.82  ? 80  LEU B CD1   1 
ATOM   2599 C  CD2   . LEU B 1 139 ? 27.639  21.367  29.761  1.00 55.27  ? 80  LEU B CD2   1 
ATOM   2600 N  N     . THR B 1 140 ? 30.778  16.710  29.562  1.00 65.04  ? 81  THR B N     1 
ATOM   2601 C  CA    . THR B 1 140 ? 32.123  16.247  29.889  1.00 67.73  ? 81  THR B CA    1 
ATOM   2602 C  C     . THR B 1 140 ? 32.875  15.701  28.687  1.00 64.89  ? 81  THR B C     1 
ATOM   2603 O  O     . THR B 1 140 ? 33.903  15.035  28.858  1.00 66.46  ? 81  THR B O     1 
ATOM   2604 C  CB    . THR B 1 140 ? 32.063  15.143  30.948  1.00 66.81  ? 81  THR B CB    1 
ATOM   2605 O  OG1   . THR B 1 140 ? 31.394  13.997  30.388  1.00 59.82  ? 81  THR B OG1   1 
ATOM   2606 C  CG2   . THR B 1 140 ? 31.345  15.628  32.215  1.00 64.63  ? 81  THR B CG2   1 
ATOM   2607 N  N     . ASN B 1 141 ? 32.382  15.936  27.484  1.00 68.12  ? 82  ASN B N     1 
ATOM   2608 C  CA    . ASN B 1 141 ? 32.907  15.229  26.320  1.00 75.12  ? 82  ASN B CA    1 
ATOM   2609 C  C     . ASN B 1 141 ? 32.771  16.162  25.128  1.00 71.36  ? 82  ASN B C     1 
ATOM   2610 O  O     . ASN B 1 141 ? 31.649  16.484  24.719  1.00 67.13  ? 82  ASN B O     1 
ATOM   2611 C  CB    . ASN B 1 141 ? 32.154  13.917  26.110  1.00 68.63  ? 82  ASN B CB    1 
ATOM   2612 C  CG    . ASN B 1 141 ? 32.809  13.012  25.100  1.00 72.80  ? 82  ASN B CG    1 
ATOM   2613 O  OD1   . ASN B 1 141 ? 33.901  12.496  25.331  1.00 79.83  ? 82  ASN B OD1   1 
ATOM   2614 N  ND2   . ASN B 1 141 ? 32.132  12.788  23.979  1.00 71.39  ? 82  ASN B ND2   1 
ATOM   2615 N  N     . GLU B 1 142 ? 33.910  16.634  24.613  1.00 73.08  ? 83  GLU B N     1 
ATOM   2616 C  CA    . GLU B 1 142 ? 33.869  17.594  23.516  1.00 77.47  ? 83  GLU B CA    1 
ATOM   2617 C  C     . GLU B 1 142 ? 33.010  17.063  22.379  1.00 69.63  ? 83  GLU B C     1 
ATOM   2618 O  O     . GLU B 1 142 ? 32.064  17.726  21.940  1.00 66.47  ? 83  GLU B O     1 
ATOM   2619 C  CB    . GLU B 1 142 ? 35.280  17.917  23.011  1.00 79.66  ? 83  GLU B CB    1 
ATOM   2620 C  CG    . GLU B 1 142 ? 35.341  19.212  22.193  1.00 74.38  ? 83  GLU B CG    1 
ATOM   2621 C  CD    . GLU B 1 142 ? 35.292  20.443  23.075  1.00 82.88  ? 83  GLU B CD    1 
ATOM   2622 O  OE1   . GLU B 1 142 ? 34.540  21.401  22.761  1.00 85.12  ? 83  GLU B OE1   1 
ATOM   2623 O  OE2   . GLU B 1 142 ? 36.000  20.436  24.103  1.00 85.08  ? 83  GLU B OE2   1 
ATOM   2624 N  N     . GLN B 1 143 ? 33.289  15.829  21.946  1.00 67.74  ? 84  GLN B N     1 
ATOM   2625 C  CA    . GLN B 1 143 ? 32.638  15.264  20.766  1.00 68.64  ? 84  GLN B CA    1 
ATOM   2626 C  C     . GLN B 1 143 ? 31.122  15.371  20.843  1.00 66.65  ? 84  GLN B C     1 
ATOM   2627 O  O     . GLN B 1 143 ? 30.471  15.745  19.856  1.00 66.77  ? 84  GLN B O     1 
ATOM   2628 C  CB    . GLN B 1 143 ? 33.077  13.809  20.578  1.00 66.91  ? 84  GLN B CB    1 
ATOM   2629 C  CG    . GLN B 1 143 ? 34.263  13.649  19.633  1.00 66.42  ? 84  GLN B CG    1 
ATOM   2630 C  CD    . GLN B 1 143 ? 33.955  14.121  18.206  1.00 73.15  ? 84  GLN B CD    1 
ATOM   2631 O  OE1   . GLN B 1 143 ? 33.777  15.312  17.959  1.00 70.65  ? 84  GLN B OE1   1 
ATOM   2632 N  NE2   . GLN B 1 143 ? 33.874  13.177  17.268  1.00 66.28  ? 84  GLN B NE2   1 
ATOM   2633 N  N     . SER B 1 144 ? 30.546  15.047  22.007  1.00 63.16  ? 85  SER B N     1 
ATOM   2634 C  CA    . SER B 1 144 ? 29.122  15.247  22.249  1.00 64.49  ? 85  SER B CA    1 
ATOM   2635 C  C     . SER B 1 144 ? 28.663  16.576  21.666  1.00 62.02  ? 85  SER B C     1 
ATOM   2636 O  O     . SER B 1 144 ? 27.798  16.638  20.792  1.00 59.42  ? 85  SER B O     1 
ATOM   2637 C  CB    . SER B 1 144 ? 28.845  15.249  23.750  1.00 68.46  ? 85  SER B CB    1 
ATOM   2638 O  OG    . SER B 1 144 ? 29.657  14.329  24.451  1.00 71.02  ? 85  SER B OG    1 
ATOM   2639 N  N     . PHE B 1 145 ? 29.303  17.638  22.141  1.00 64.61  ? 86  PHE B N     1 
ATOM   2640 C  CA    . PHE B 1 145 ? 29.023  18.981  21.659  1.00 59.66  ? 86  PHE B CA    1 
ATOM   2641 C  C     . PHE B 1 145 ? 29.316  19.091  20.165  1.00 66.01  ? 86  PHE B C     1 
ATOM   2642 O  O     . PHE B 1 145 ? 28.483  19.582  19.390  1.00 59.38  ? 86  PHE B O     1 
ATOM   2643 C  CB    . PHE B 1 145 ? 29.861  19.966  22.470  1.00 52.40  ? 86  PHE B CB    1 
ATOM   2644 C  CG    . PHE B 1 145 ? 29.525  21.403  22.204  1.00 61.44  ? 86  PHE B CG    1 
ATOM   2645 C  CD1   . PHE B 1 145 ? 28.225  21.889  22.366  1.00 57.64  ? 86  PHE B CD1   1 
ATOM   2646 C  CD2   . PHE B 1 145 ? 30.513  22.278  21.801  1.00 64.68  ? 86  PHE B CD2   1 
ATOM   2647 C  CE1   . PHE B 1 145 ? 27.950  23.230  22.130  1.00 61.16  ? 86  PHE B CE1   1 
ATOM   2648 C  CE2   . PHE B 1 145 ? 30.241  23.592  21.566  1.00 68.73  ? 86  PHE B CE2   1 
ATOM   2649 C  CZ    . PHE B 1 145 ? 28.962  24.078  21.739  1.00 68.69  ? 86  PHE B CZ    1 
ATOM   2650 N  N     . LEU B 1 146 ? 30.504  18.638  19.748  1.00 66.44  ? 87  LEU B N     1 
ATOM   2651 C  CA    . LEU B 1 146 ? 30.951  18.812  18.370  1.00 64.08  ? 87  LEU B CA    1 
ATOM   2652 C  C     . LEU B 1 146 ? 29.923  18.257  17.395  1.00 63.93  ? 87  LEU B C     1 
ATOM   2653 O  O     . LEU B 1 146 ? 29.440  18.972  16.511  1.00 64.53  ? 87  LEU B O     1 
ATOM   2654 C  CB    . LEU B 1 146 ? 32.316  18.136  18.178  1.00 64.38  ? 87  LEU B CB    1 
ATOM   2655 C  CG    . LEU B 1 146 ? 33.496  18.836  18.884  1.00 61.21  ? 87  LEU B CG    1 
ATOM   2656 C  CD1   . LEU B 1 146 ? 34.846  18.159  18.701  1.00 55.73  ? 87  LEU B CD1   1 
ATOM   2657 C  CD2   . LEU B 1 146 ? 33.575  20.287  18.450  1.00 58.87  ? 87  LEU B CD2   1 
ATOM   2658 N  N     . ASN B 1 147 ? 29.545  16.989  17.581  1.00 60.02  ? 88  ASN B N     1 
ATOM   2659 C  CA    . ASN B 1 147 ? 28.535  16.323  16.772  1.00 55.27  ? 88  ASN B CA    1 
ATOM   2660 C  C     . ASN B 1 147 ? 27.140  16.921  16.932  1.00 52.87  ? 88  ASN B C     1 
ATOM   2661 O  O     . ASN B 1 147 ? 26.217  16.482  16.247  1.00 55.87  ? 88  ASN B O     1 
ATOM   2662 C  CB    . ASN B 1 147 ? 28.487  14.832  17.122  1.00 56.14  ? 88  ASN B CB    1 
ATOM   2663 C  CG    . ASN B 1 147 ? 29.861  14.186  17.125  1.00 61.58  ? 88  ASN B CG    1 
ATOM   2664 O  OD1   . ASN B 1 147 ? 30.835  14.785  16.694  1.00 65.77  ? 88  ASN B OD1   1 
ATOM   2665 N  ND2   . ASN B 1 147 ? 29.944  12.958  17.629  1.00 68.09  ? 88  ASN B ND2   1 
ATOM   2666 N  N     . VAL B 1 148 ? 26.934  17.887  17.817  1.00 57.88  ? 89  VAL B N     1 
ATOM   2667 C  CA    . VAL B 1 148 ? 25.611  18.508  17.856  1.00 61.62  ? 89  VAL B CA    1 
ATOM   2668 C  C     . VAL B 1 148 ? 25.263  19.091  16.491  1.00 64.91  ? 89  VAL B C     1 
ATOM   2669 O  O     . VAL B 1 148 ? 24.141  18.916  15.997  1.00 57.78  ? 89  VAL B O     1 
ATOM   2670 C  CB    . VAL B 1 148 ? 25.531  19.560  18.978  1.00 54.68  ? 89  VAL B CB    1 
ATOM   2671 C  CG1   . VAL B 1 148 ? 24.305  20.440  18.797  1.00 49.06  ? 89  VAL B CG1   1 
ATOM   2672 C  CG2   . VAL B 1 148 ? 25.500  18.847  20.332  1.00 54.44  ? 89  VAL B CG2   1 
ATOM   2673 N  N     . ARG B 1 149 ? 26.234  19.757  15.849  1.00 67.34  ? 90  ARG B N     1 
ATOM   2674 C  CA    . ARG B 1 149 ? 26.033  20.356  14.530  1.00 64.13  ? 90  ARG B CA    1 
ATOM   2675 C  C     . ARG B 1 149 ? 25.403  19.359  13.550  1.00 65.82  ? 90  ARG B C     1 
ATOM   2676 O  O     . ARG B 1 149 ? 24.329  19.616  12.985  1.00 63.45  ? 90  ARG B O     1 
ATOM   2677 C  CB    . ARG B 1 149 ? 27.376  20.885  13.999  1.00 69.54  ? 90  ARG B CB    1 
ATOM   2678 C  CG    . ARG B 1 149 ? 28.033  21.960  14.882  1.00 75.65  ? 90  ARG B CG    1 
ATOM   2679 C  CD    . ARG B 1 149 ? 29.300  22.590  14.249  1.00 79.19  ? 90  ARG B CD    1 
ATOM   2680 N  NE    . ARG B 1 149 ? 29.187  24.044  14.084  1.00 87.11  ? 90  ARG B NE    1 
ATOM   2681 C  CZ    . ARG B 1 149 ? 30.215  24.870  13.884  1.00 90.79  ? 90  ARG B CZ    1 
ATOM   2682 N  NH1   . ARG B 1 149 ? 30.006  26.182  13.736  1.00 82.98  ? 90  ARG B NH1   1 
ATOM   2683 N  NH2   . ARG B 1 149 ? 31.453  24.384  13.835  1.00 83.48  ? 90  ARG B NH2   1 
ATOM   2684 N  N     . ASN B 1 150 ? 26.048  18.199  13.359  1.00 60.50  ? 91  ASN B N     1 
ATOM   2685 C  CA    . ASN B 1 150 ? 25.530  17.188  12.434  1.00 57.33  ? 91  ASN B CA    1 
ATOM   2686 C  C     . ASN B 1 150 ? 24.138  16.699  12.844  1.00 61.89  ? 91  ASN B C     1 
ATOM   2687 O  O     . ASN B 1 150 ? 23.213  16.683  12.018  1.00 59.39  ? 91  ASN B O     1 
ATOM   2688 C  CB    . ASN B 1 150 ? 26.504  16.013  12.342  1.00 60.17  ? 91  ASN B CB    1 
ATOM   2689 C  CG    . ASN B 1 150 ? 27.958  16.460  12.238  1.00 67.23  ? 91  ASN B CG    1 
ATOM   2690 O  OD1   . ASN B 1 150 ? 28.692  16.487  13.237  1.00 63.92  ? 91  ASN B OD1   1 
ATOM   2691 N  ND2   . ASN B 1 150 ? 28.380  16.824  11.024  1.00 69.42  ? 91  ASN B ND2   1 
ATOM   2692 N  N     . TRP B 1 151 ? 23.974  16.287  14.123  1.00 60.28  ? 92  TRP B N     1 
ATOM   2693 C  CA    . TRP B 1 151 ? 22.695  15.743  14.598  1.00 56.62  ? 92  TRP B CA    1 
ATOM   2694 C  C     . TRP B 1 151 ? 21.541  16.679  14.286  1.00 58.36  ? 92  TRP B C     1 
ATOM   2695 O  O     . TRP B 1 151 ? 20.439  16.228  13.956  1.00 56.78  ? 92  TRP B O     1 
ATOM   2696 C  CB    . TRP B 1 151 ? 22.701  15.468  16.122  1.00 58.49  ? 92  TRP B CB    1 
ATOM   2697 C  CG    . TRP B 1 151 ? 23.348  14.174  16.617  1.00 52.77  ? 92  TRP B CG    1 
ATOM   2698 C  CD1   . TRP B 1 151 ? 24.522  14.051  17.327  1.00 47.72  ? 92  TRP B CD1   1 
ATOM   2699 C  CD2   . TRP B 1 151 ? 22.872  12.834  16.399  1.00 57.03  ? 92  TRP B CD2   1 
ATOM   2700 N  NE1   . TRP B 1 151 ? 24.784  12.723  17.586  1.00 52.67  ? 92  TRP B NE1   1 
ATOM   2701 C  CE2   . TRP B 1 151 ? 23.797  11.955  17.013  1.00 57.14  ? 92  TRP B CE2   1 
ATOM   2702 C  CE3   . TRP B 1 151 ? 21.752  12.292  15.752  1.00 58.40  ? 92  TRP B CE3   1 
ATOM   2703 C  CZ2   . TRP B 1 151 ? 23.633  10.568  16.992  1.00 53.24  ? 92  TRP B CZ2   1 
ATOM   2704 C  CZ3   . TRP B 1 151 ? 21.591  10.911  15.743  1.00 54.06  ? 92  TRP B CZ3   1 
ATOM   2705 C  CH2   . TRP B 1 151 ? 22.529  10.070  16.353  1.00 47.33  ? 92  TRP B CH2   1 
ATOM   2706 N  N     . ILE B 1 152 ? 21.778  17.988  14.370  1.00 65.81  ? 93  ILE B N     1 
ATOM   2707 C  CA    . ILE B 1 152 ? 20.721  18.961  14.106  1.00 65.87  ? 93  ILE B CA    1 
ATOM   2708 C  C     . ILE B 1 152 ? 20.340  18.974  12.636  1.00 60.51  ? 93  ILE B C     1 
ATOM   2709 O  O     . ILE B 1 152 ? 19.154  19.078  12.281  1.00 64.31  ? 93  ILE B O     1 
ATOM   2710 C  CB    . ILE B 1 152 ? 21.161  20.361  14.564  1.00 64.39  ? 93  ILE B CB    1 
ATOM   2711 C  CG1   . ILE B 1 152 ? 21.525  20.380  16.048  1.00 59.75  ? 93  ILE B CG1   1 
ATOM   2712 C  CG2   . ILE B 1 152 ? 20.100  21.405  14.162  1.00 69.39  ? 93  ILE B CG2   1 
ATOM   2713 C  CD1   . ILE B 1 152 ? 21.405  21.752  16.686  1.00 60.63  ? 93  ILE B CD1   1 
ATOM   2714 N  N     . SER B 1 153 ? 21.320  18.909  11.745  1.00 58.86  ? 94  SER B N     1 
ATOM   2715 C  CA    . SER B 1 153 ? 20.963  18.943  10.339  1.00 65.19  ? 94  SER B CA    1 
ATOM   2716 C  C     . SER B 1 153 ? 20.487  17.585  9.863   1.00 67.05  ? 94  SER B C     1 
ATOM   2717 O  O     . SER B 1 153 ? 19.777  17.506  8.852   1.00 76.85  ? 94  SER B O     1 
ATOM   2718 C  CB    . SER B 1 153 ? 22.131  19.433  9.481   1.00 65.25  ? 94  SER B CB    1 
ATOM   2719 O  OG    . SER B 1 153 ? 23.080  18.402  9.291   1.00 62.36  ? 94  SER B OG    1 
ATOM   2720 N  N     . GLN B 1 154 ? 20.850  16.512  10.573  1.00 67.92  ? 95  GLN B N     1 
ATOM   2721 C  CA    . GLN B 1 154 ? 20.169  15.246  10.335  1.00 66.15  ? 95  GLN B CA    1 
ATOM   2722 C  C     . GLN B 1 154 ? 18.777  15.241  10.937  1.00 62.72  ? 95  GLN B C     1 
ATOM   2723 O  O     . GLN B 1 154 ? 17.901  14.517  10.456  1.00 67.03  ? 95  GLN B O     1 
ATOM   2724 C  CB    . GLN B 1 154 ? 20.974  14.070  10.873  1.00 55.88  ? 95  GLN B CB    1 
ATOM   2725 C  CG    . GLN B 1 154 ? 20.339  12.737  10.498  1.00 64.62  ? 95  GLN B CG    1 
ATOM   2726 C  CD    . GLN B 1 154 ? 21.330  11.735  9.966   1.00 68.04  ? 95  GLN B CD    1 
ATOM   2727 O  OE1   . GLN B 1 154 ? 21.997  11.033  10.733  1.00 68.19  ? 95  GLN B OE1   1 
ATOM   2728 N  NE2   . GLN B 1 154 ? 21.430  11.652  8.643   1.00 70.96  ? 95  GLN B NE2   1 
ATOM   2729 N  N     . LEU B 1 155 ? 18.539  16.068  11.945  1.00 66.67  ? 96  LEU B N     1 
ATOM   2730 C  CA    . LEU B 1 155 ? 17.190  16.186  12.472  1.00 64.55  ? 96  LEU B CA    1 
ATOM   2731 C  C     . LEU B 1 155 ? 16.250  16.765  11.429  1.00 62.03  ? 96  LEU B C     1 
ATOM   2732 O  O     . LEU B 1 155 ? 15.155  16.235  11.209  1.00 57.63  ? 96  LEU B O     1 
ATOM   2733 C  CB    . LEU B 1 155 ? 17.188  17.046  13.728  1.00 63.43  ? 96  LEU B CB    1 
ATOM   2734 C  CG    . LEU B 1 155 ? 16.984  16.224  14.994  1.00 63.46  ? 96  LEU B CG    1 
ATOM   2735 C  CD1   . LEU B 1 155 ? 16.796  17.124  16.212  1.00 64.17  ? 96  LEU B CD1   1 
ATOM   2736 C  CD2   . LEU B 1 155 ? 15.801  15.287  14.818  1.00 63.48  ? 96  LEU B CD2   1 
ATOM   2737 N  N     . GLN B 1 156 ? 16.670  17.847  10.762  1.00 68.91  ? 97  GLN B N     1 
ATOM   2738 C  CA    . GLN B 1 156 ? 15.818  18.525  9.784   1.00 74.25  ? 97  GLN B CA    1 
ATOM   2739 C  C     . GLN B 1 156 ? 15.906  17.920  8.392   1.00 70.66  ? 97  GLN B C     1 
ATOM   2740 O  O     . GLN B 1 156 ? 15.078  18.254  7.538   1.00 72.81  ? 97  GLN B O     1 
ATOM   2741 C  CB    . GLN B 1 156 ? 16.146  20.026  9.713   1.00 76.73  ? 97  GLN B CB    1 
ATOM   2742 C  CG    . GLN B 1 156 ? 16.205  20.708  11.079  1.00 78.80  ? 97  GLN B CG    1 
ATOM   2743 C  CD    . GLN B 1 156 ? 16.790  22.098  10.994  1.00 84.42  ? 97  GLN B CD    1 
ATOM   2744 O  OE1   . GLN B 1 156 ? 17.781  22.330  10.280  1.00 78.44  ? 97  GLN B OE1   1 
ATOM   2745 N  NE2   . GLN B 1 156 ? 16.192  23.037  11.733  1.00 83.50  ? 97  GLN B NE2   1 
ATOM   2746 N  N     . MET B 1 157 ? 16.900  17.068  8.140   1.00 68.48  ? 98  MET B N     1 
ATOM   2747 C  CA    . MET B 1 157 ? 16.871  16.215  6.961   1.00 62.61  ? 98  MET B CA    1 
ATOM   2748 C  C     . MET B 1 157 ? 15.722  15.208  7.037   1.00 65.87  ? 98  MET B C     1 
ATOM   2749 O  O     . MET B 1 157 ? 14.988  15.014  6.060   1.00 58.19  ? 98  MET B O     1 
ATOM   2750 C  CB    . MET B 1 157 ? 18.207  15.485  6.827   1.00 69.57  ? 98  MET B CB    1 
ATOM   2751 C  CG    . MET B 1 157 ? 18.983  15.769  5.551   1.00 76.34  ? 98  MET B CG    1 
ATOM   2752 S  SD    . MET B 1 157 ? 20.570  14.892  5.487   1.00 83.84  ? 98  MET B SD    1 
ATOM   2753 C  CE    . MET B 1 157 ? 21.591  16.001  6.470   1.00 79.37  ? 98  MET B CE    1 
ATOM   2754 N  N     . HIS B 1 158 ? 15.551  14.550  8.192   1.00 64.07  ? 99  HIS B N     1 
ATOM   2755 C  CA    . HIS B 1 158 ? 14.660  13.396  8.319   1.00 64.12  ? 99  HIS B CA    1 
ATOM   2756 C  C     . HIS B 1 158 ? 13.362  13.692  9.082   1.00 61.38  ? 99  HIS B C     1 
ATOM   2757 O  O     . HIS B 1 158 ? 12.757  12.767  9.634   1.00 67.72  ? 99  HIS B O     1 
ATOM   2758 C  CB    . HIS B 1 158 ? 15.373  12.233  9.015   1.00 62.57  ? 99  HIS B CB    1 
ATOM   2759 C  CG    . HIS B 1 158 ? 16.476  11.591  8.222   1.00 62.94  ? 99  HIS B CG    1 
ATOM   2760 N  ND1   . HIS B 1 158 ? 17.777  12.053  8.244   1.00 66.02  ? 99  HIS B ND1   1 
ATOM   2761 C  CD2   . HIS B 1 158 ? 16.487  10.482  7.444   1.00 58.41  ? 99  HIS B CD2   1 
ATOM   2762 C  CE1   . HIS B 1 158 ? 18.535  11.276  7.490   1.00 62.61  ? 99  HIS B CE1   1 
ATOM   2763 N  NE2   . HIS B 1 158 ? 17.779  10.308  7.004   1.00 58.83  ? 99  HIS B NE2   1 
ATOM   2764 N  N     . ALA B 1 159 ? 12.904  14.939  9.126   1.00 61.71  ? 100 ALA B N     1 
ATOM   2765 C  CA    . ALA B 1 159 ? 11.710  15.285  9.889   1.00 59.01  ? 100 ALA B CA    1 
ATOM   2766 C  C     . ALA B 1 159 ? 10.500  15.424  8.974   1.00 60.21  ? 100 ALA B C     1 
ATOM   2767 O  O     . ALA B 1 159 ? 10.615  15.875  7.831   1.00 63.45  ? 100 ALA B O     1 
ATOM   2768 C  CB    . ALA B 1 159 ? 11.913  16.578  10.681  1.00 64.32  ? 100 ALA B CB    1 
ATOM   2769 N  N     . TYR B 1 160 ? 9.341   15.026  9.483   1.00 64.61  ? 101 TYR B N     1 
ATOM   2770 C  CA    . TYR B 1 160 ? 8.105   15.090  8.711   1.00 64.26  ? 101 TYR B CA    1 
ATOM   2771 C  C     . TYR B 1 160 ? 7.482   16.469  8.850   1.00 66.88  ? 101 TYR B C     1 
ATOM   2772 O  O     . TYR B 1 160 ? 7.213   17.132  7.854   1.00 71.38  ? 101 TYR B O     1 
ATOM   2773 C  CB    . TYR B 1 160 ? 7.113   14.010  9.161   1.00 63.35  ? 101 TYR B CB    1 
ATOM   2774 C  CG    . TYR B 1 160 ? 7.354   12.648  8.542   1.00 63.83  ? 101 TYR B CG    1 
ATOM   2775 C  CD1   . TYR B 1 160 ? 8.463   12.417  7.725   1.00 62.14  ? 101 TYR B CD1   1 
ATOM   2776 C  CD2   . TYR B 1 160 ? 6.471   11.592  8.772   1.00 63.98  ? 101 TYR B CD2   1 
ATOM   2777 C  CE1   . TYR B 1 160 ? 8.688   11.172  7.154   1.00 58.54  ? 101 TYR B CE1   1 
ATOM   2778 C  CE2   . TYR B 1 160 ? 6.678   10.348  8.206   1.00 60.74  ? 101 TYR B CE2   1 
ATOM   2779 C  CZ    . TYR B 1 160 ? 7.789   10.141  7.397   1.00 59.70  ? 101 TYR B CZ    1 
ATOM   2780 O  OH    . TYR B 1 160 ? 8.011   8.904   6.833   1.00 54.80  ? 101 TYR B OH    1 
ATOM   2781 N  N     . CYS B 1 161 ? 8.083   17.741  9.110   1.00 68.52  ? 102 CYS B N     1 
ATOM   2782 C  CA    . CYS B 1 161 ? 7.642   19.125  9.189   1.00 73.89  ? 102 CYS B CA    1 
ATOM   2783 C  C     . CYS B 1 161 ? 8.864   20.014  9.401   0.95 77.13  ? 102 CYS B C     1 
ATOM   2784 O  O     . CYS B 1 161 ? 10.011  19.492  9.432   0.98 72.89  ? 102 CYS B O     1 
ATOM   2785 C  CB    . CYS B 1 161 ? 6.662   19.285  10.355  0.86 77.04  ? 102 CYS B CB    1 
ATOM   2786 S  SG    . CYS B 1 161 ? 7.495   19.123  11.966  0.76 79.46  ? 102 CYS B SG    1 
ATOM   2787 N  N     . GLU B 1 162 ? 9.031   21.172  8.579   1.00 82.83  ? 103 GLU B N     1 
ATOM   2788 C  CA    . GLU B 1 162 ? 10.338  21.544  8.038   1.00 88.35  ? 103 GLU B CA    1 
ATOM   2789 C  C     . GLU B 1 162 ? 11.185  22.210  9.133   1.00 85.73  ? 103 GLU B C     1 
ATOM   2790 O  O     . GLU B 1 162 ? 12.419  22.172  9.101   1.00 84.72  ? 103 GLU B O     1 
ATOM   2791 C  CB    . GLU B 1 162 ? 10.187  22.474  6.818   1.00 87.08  ? 103 GLU B CB    1 
ATOM   2792 C  CG    . GLU B 1 162 ? 11.469  22.659  6.005   1.00 87.46  ? 103 GLU B CG    1 
ATOM   2793 C  CD    . GLU B 1 162 ? 11.527  23.997  5.276   1.00 100.01 ? 103 GLU B CD    1 
ATOM   2794 O  OE1   . GLU B 1 162 ? 10.697  24.884  5.577   1.00 106.05 ? 103 GLU B OE1   1 
ATOM   2795 O  OE2   . GLU B 1 162 ? 12.412  24.164  4.405   1.00 107.33 ? 103 GLU B OE2   1 
ATOM   2796 N  N     . ASN B 1 163 ? 10.515  22.819  10.107  1.00 80.68  ? 104 ASN B N     1 
ATOM   2797 C  CA    . ASN B 1 163 ? 11.228  23.389  11.240  1.00 81.79  ? 104 ASN B CA    1 
ATOM   2798 C  C     . ASN B 1 163 ? 10.795  22.645  12.497  1.00 80.66  ? 104 ASN B C     1 
ATOM   2799 O  O     . ASN B 1 163 ? 9.893   23.106  13.211  1.00 76.25  ? 104 ASN B O     1 
ATOM   2800 C  CB    . ASN B 1 163 ? 10.960  24.891  11.362  1.00 84.13  ? 104 ASN B CB    1 
ATOM   2801 C  CG    . ASN B 1 163 ? 12.087  25.633  12.064  1.00 86.43  ? 104 ASN B CG    1 
ATOM   2802 O  OD1   . ASN B 1 163 ? 13.188  25.096  12.248  1.00 87.18  ? 104 ASN B OD1   1 
ATOM   2803 N  ND2   . ASN B 1 163 ? 11.816  26.879  12.457  1.00 81.14  ? 104 ASN B ND2   1 
ATOM   2804 N  N     . PRO B 1 164 ? 11.386  21.483  12.778  1.00 83.36  ? 105 PRO B N     1 
ATOM   2805 C  CA    . PRO B 1 164 ? 11.023  20.736  13.983  1.00 76.47  ? 105 PRO B CA    1 
ATOM   2806 C  C     . PRO B 1 164 ? 11.632  21.377  15.213  1.00 75.05  ? 105 PRO B C     1 
ATOM   2807 O  O     . PRO B 1 164 ? 12.712  21.975  15.167  1.00 76.66  ? 105 PRO B O     1 
ATOM   2808 C  CB    . PRO B 1 164 ? 11.631  19.354  13.733  1.00 77.32  ? 105 PRO B CB    1 
ATOM   2809 C  CG    . PRO B 1 164 ? 12.865  19.661  12.929  1.00 73.43  ? 105 PRO B CG    1 
ATOM   2810 C  CD    . PRO B 1 164 ? 12.499  20.837  12.052  1.00 81.03  ? 105 PRO B CD    1 
ATOM   2811 N  N     . ASP B 1 165 ? 10.921  21.249  16.326  1.00 73.33  ? 106 ASP B N     1 
ATOM   2812 C  CA    . ASP B 1 165 ? 11.355  21.882  17.563  1.00 70.44  ? 106 ASP B CA    1 
ATOM   2813 C  C     . ASP B 1 165 ? 12.411  21.028  18.270  1.00 62.78  ? 106 ASP B C     1 
ATOM   2814 O  O     . ASP B 1 165 ? 12.259  19.807  18.403  1.00 61.03  ? 106 ASP B O     1 
ATOM   2815 C  CB    . ASP B 1 165 ? 10.148  22.142  18.464  1.00 71.90  ? 106 ASP B CB    1 
ATOM   2816 C  CG    . ASP B 1 165 ? 9.207   23.173  17.871  1.00 76.21  ? 106 ASP B CG    1 
ATOM   2817 O  OD1   . ASP B 1 165 ? 9.647   23.902  16.959  1.00 78.88  ? 106 ASP B OD1   1 
ATOM   2818 O  OD2   . ASP B 1 165 ? 8.039   23.256  18.305  1.00 82.67  ? 106 ASP B OD2   1 
ATOM   2819 N  N     . ILE B 1 166 ? 13.497  21.676  18.689  1.00 56.24  ? 107 ILE B N     1 
ATOM   2820 C  CA    . ILE B 1 166 ? 14.622  21.031  19.352  1.00 57.11  ? 107 ILE B CA    1 
ATOM   2821 C  C     . ILE B 1 166 ? 14.928  21.797  20.633  1.00 59.58  ? 107 ILE B C     1 
ATOM   2822 O  O     . ILE B 1 166 ? 14.904  23.033  20.648  1.00 56.99  ? 107 ILE B O     1 
ATOM   2823 C  CB    . ILE B 1 166 ? 15.871  20.982  18.445  1.00 54.67  ? 107 ILE B CB    1 
ATOM   2824 C  CG1   . ILE B 1 166 ? 15.499  20.500  17.032  1.00 65.22  ? 107 ILE B CG1   1 
ATOM   2825 C  CG2   . ILE B 1 166 ? 16.973  20.108  19.064  1.00 50.48  ? 107 ILE B CG2   1 
ATOM   2826 C  CD1   . ILE B 1 166 ? 16.652  20.587  15.989  1.00 54.78  ? 107 ILE B CD1   1 
ATOM   2827 N  N     . VAL B 1 167 ? 15.202  21.065  21.712  1.00 58.73  ? 108 VAL B N     1 
ATOM   2828 C  CA    . VAL B 1 167 ? 15.731  21.640  22.941  1.00 52.32  ? 108 VAL B CA    1 
ATOM   2829 C  C     . VAL B 1 167 ? 17.109  21.044  23.192  1.00 51.50  ? 108 VAL B C     1 
ATOM   2830 O  O     . VAL B 1 167 ? 17.285  19.819  23.176  1.00 52.00  ? 108 VAL B O     1 
ATOM   2831 C  CB    . VAL B 1 167 ? 14.804  21.398  24.137  1.00 51.94  ? 108 VAL B CB    1 
ATOM   2832 C  CG1   . VAL B 1 167 ? 15.390  22.049  25.386  1.00 60.52  ? 108 VAL B CG1   1 
ATOM   2833 C  CG2   . VAL B 1 167 ? 13.408  21.897  23.834  1.00 53.71  ? 108 VAL B CG2   1 
ATOM   2834 N  N     . LEU B 1 168 ? 18.081  21.911  23.407  1.00 50.40  ? 109 LEU B N     1 
ATOM   2835 C  CA    . LEU B 1 168 ? 19.455  21.491  23.613  1.00 50.85  ? 109 LEU B CA    1 
ATOM   2836 C  C     . LEU B 1 168 ? 19.682  21.218  25.099  1.00 53.48  ? 109 LEU B C     1 
ATOM   2837 O  O     . LEU B 1 168 ? 19.197  21.948  25.965  1.00 52.81  ? 109 LEU B O     1 
ATOM   2838 C  CB    . LEU B 1 168 ? 20.425  22.563  23.104  1.00 52.47  ? 109 LEU B CB    1 
ATOM   2839 C  CG    . LEU B 1 168 ? 21.857  22.134  22.762  1.00 58.30  ? 109 LEU B CG    1 
ATOM   2840 C  CD1   . LEU B 1 168 ? 21.911  20.827  21.948  1.00 47.64  ? 109 LEU B CD1   1 
ATOM   2841 C  CD2   . LEU B 1 168 ? 22.581  23.287  22.064  1.00 53.43  ? 109 LEU B CD2   1 
ATOM   2842 N  N     . CYS B 1 169 ? 20.393  20.135  25.378  1.00 50.48  ? 110 CYS B N     1 
ATOM   2843 C  CA    . CYS B 1 169 ? 20.579  19.656  26.739  1.00 47.47  ? 110 CYS B CA    1 
ATOM   2844 C  C     . CYS B 1 169 ? 22.058  19.393  26.931  1.00 48.80  ? 110 CYS B C     1 
ATOM   2845 O  O     . CYS B 1 169 ? 22.593  18.428  26.391  1.00 52.92  ? 110 CYS B O     1 
ATOM   2846 C  CB    . CYS B 1 169 ? 19.812  18.375  26.986  1.00 46.45  ? 110 CYS B CB    1 
ATOM   2847 S  SG    . CYS B 1 169 ? 18.127  18.647  27.287  1.00 57.89  ? 110 CYS B SG    1 
ATOM   2848 N  N     . GLY B 1 170 ? 22.704  20.268  27.668  1.00 50.82  ? 111 GLY B N     1 
ATOM   2849 C  CA    . GLY B 1 170 ? 24.034  19.921  28.087  1.00 54.95  ? 111 GLY B CA    1 
ATOM   2850 C  C     . GLY B 1 170 ? 23.854  18.998  29.264  1.00 52.29  ? 111 GLY B C     1 
ATOM   2851 O  O     . GLY B 1 170 ? 23.596  19.465  30.367  1.00 54.07  ? 111 GLY B O     1 
ATOM   2852 N  N     . ASN B 1 171 ? 23.968  17.700  29.055  1.00 48.80  ? 112 ASN B N     1 
ATOM   2853 C  CA    . ASN B 1 171 ? 23.703  16.770  30.134  1.00 51.26  ? 112 ASN B CA    1 
ATOM   2854 C  C     . ASN B 1 171 ? 24.969  16.538  30.943  1.00 57.56  ? 112 ASN B C     1 
ATOM   2855 O  O     . ASN B 1 171 ? 26.080  16.828  30.489  1.00 54.51  ? 112 ASN B O     1 
ATOM   2856 C  CB    . ASN B 1 171 ? 23.162  15.437  29.609  1.00 51.34  ? 112 ASN B CB    1 
ATOM   2857 C  CG    . ASN B 1 171 ? 22.601  14.559  30.723  1.00 54.24  ? 112 ASN B CG    1 
ATOM   2858 O  OD1   . ASN B 1 171 ? 23.178  13.514  31.066  1.00 55.78  ? 112 ASN B OD1   1 
ATOM   2859 N  ND2   . ASN B 1 171 ? 21.491  14.996  31.318  1.00 48.88  ? 112 ASN B ND2   1 
ATOM   2860 N  N     . LYS B 1 172 ? 24.767  16.015  32.168  1.00 58.15  ? 113 LYS B N     1 
ATOM   2861 C  CA    . LYS B 1 172 ? 25.779  15.710  33.182  1.00 52.40  ? 113 LYS B CA    1 
ATOM   2862 C  C     . LYS B 1 172 ? 26.341  16.978  33.814  1.00 57.67  ? 113 LYS B C     1 
ATOM   2863 O  O     . LYS B 1 172 ? 27.537  17.048  34.123  1.00 61.80  ? 113 LYS B O     1 
ATOM   2864 C  CB    . LYS B 1 172 ? 26.902  14.845  32.605  1.00 55.34  ? 113 LYS B CB    1 
ATOM   2865 C  CG    . LYS B 1 172 ? 26.381  13.615  31.843  1.00 53.40  ? 113 LYS B CG    1 
ATOM   2866 C  CD    . LYS B 1 172 ? 27.478  12.648  31.517  1.00 45.51  ? 113 LYS B CD    1 
ATOM   2867 C  CE    . LYS B 1 172 ? 26.907  11.426  30.833  1.00 42.23  ? 113 LYS B CE    1 
ATOM   2868 N  NZ    . LYS B 1 172 ? 27.997  10.450  30.494  1.00 40.94  ? 113 LYS B NZ    1 
ATOM   2869 N  N     . SER B 1 173 ? 25.468  17.970  34.040  1.00 54.21  ? 114 SER B N     1 
ATOM   2870 C  CA    . SER B 1 173 ? 25.849  19.169  34.777  1.00 59.65  ? 114 SER B CA    1 
ATOM   2871 C  C     . SER B 1 173 ? 26.287  18.852  36.207  1.00 66.63  ? 114 SER B C     1 
ATOM   2872 O  O     . SER B 1 173 ? 26.957  19.681  36.840  1.00 71.33  ? 114 SER B O     1 
ATOM   2873 C  CB    . SER B 1 173 ? 24.685  20.177  34.762  1.00 62.16  ? 114 SER B CB    1 
ATOM   2874 O  OG    . SER B 1 173 ? 23.793  20.023  35.860  1.00 59.04  ? 114 SER B OG    1 
ATOM   2875 N  N     . ASP B 1 174 ? 25.948  17.668  36.727  1.00 60.53  ? 115 ASP B N     1 
ATOM   2876 C  CA    . ASP B 1 174 ? 26.383  17.282  38.064  1.00 62.74  ? 115 ASP B CA    1 
ATOM   2877 C  C     . ASP B 1 174 ? 27.849  16.889  38.113  1.00 65.58  ? 115 ASP B C     1 
ATOM   2878 O  O     . ASP B 1 174 ? 28.359  16.569  39.193  1.00 60.06  ? 115 ASP B O     1 
ATOM   2879 C  CB    . ASP B 1 174 ? 25.537  16.125  38.597  1.00 58.09  ? 115 ASP B CB    1 
ATOM   2880 C  CG    . ASP B 1 174 ? 25.892  14.794  37.963  1.00 57.42  ? 115 ASP B CG    1 
ATOM   2881 O  OD1   . ASP B 1 174 ? 25.505  14.560  36.796  1.00 56.02  ? 115 ASP B OD1   1 
ATOM   2882 O  OD2   . ASP B 1 174 ? 26.544  13.970  38.635  1.00 59.54  ? 115 ASP B OD2   1 
ATOM   2883 N  N     . LEU B 1 175 ? 28.535  16.868  36.981  1.00 66.55  ? 116 LEU B N     1 
ATOM   2884 C  CA    . LEU B 1 175 ? 29.960  16.548  37.008  1.00 68.83  ? 116 LEU B CA    1 
ATOM   2885 C  C     . LEU B 1 175 ? 30.782  17.812  36.833  1.00 71.21  ? 116 LEU B C     1 
ATOM   2886 O  O     . LEU B 1 175 ? 31.721  17.853  36.038  1.00 72.01  ? 116 LEU B O     1 
ATOM   2887 C  CB    . LEU B 1 175 ? 30.295  15.497  35.950  1.00 63.04  ? 116 LEU B CB    1 
ATOM   2888 C  CG    . LEU B 1 175 ? 29.558  14.160  36.142  1.00 63.05  ? 116 LEU B CG    1 
ATOM   2889 C  CD1   . LEU B 1 175 ? 30.238  12.992  35.443  1.00 56.81  ? 116 LEU B CD1   1 
ATOM   2890 C  CD2   . LEU B 1 175 ? 29.425  13.850  37.625  1.00 67.54  ? 116 LEU B CD2   1 
ATOM   2891 N  N     . GLU B 1 176 ? 30.440  18.855  37.609  1.00 74.13  ? 117 GLU B N     1 
ATOM   2892 C  CA    . GLU B 1 176 ? 31.089  20.159  37.472  1.00 79.35  ? 117 GLU B CA    1 
ATOM   2893 C  C     . GLU B 1 176 ? 32.596  20.012  37.635  1.00 77.94  ? 117 GLU B C     1 
ATOM   2894 O  O     . GLU B 1 176 ? 33.358  20.921  37.292  1.00 86.59  ? 117 GLU B O     1 
ATOM   2895 C  CB    . GLU B 1 176 ? 30.544  21.188  38.483  1.00 70.14  ? 117 GLU B CB    1 
ATOM   2896 C  CG    . GLU B 1 176 ? 29.146  21.760  38.149  1.00 79.29  ? 117 GLU B CG    1 
ATOM   2897 C  CD    . GLU B 1 176 ? 29.149  23.226  37.669  1.00 86.25  ? 117 GLU B CD    1 
ATOM   2898 O  OE1   . GLU B 1 176 ? 28.186  23.968  37.985  1.00 82.18  ? 117 GLU B OE1   1 
ATOM   2899 O  OE2   . GLU B 1 176 ? 30.095  23.631  36.955  1.00 87.90  ? 117 GLU B OE2   1 
ATOM   2900 N  N     . ASP B 1 177 ? 33.028  18.866  38.149  1.00 77.50  ? 118 ASP B N     1 
ATOM   2901 C  CA    . ASP B 1 177 ? 34.434  18.543  38.315  1.00 78.80  ? 118 ASP B CA    1 
ATOM   2902 C  C     . ASP B 1 177 ? 35.059  17.934  37.066  1.00 77.54  ? 118 ASP B C     1 
ATOM   2903 O  O     . ASP B 1 177 ? 36.260  17.652  37.072  1.00 82.79  ? 118 ASP B O     1 
ATOM   2904 C  CB    . ASP B 1 177 ? 34.602  17.586  39.501  1.00 87.31  ? 118 ASP B CB    1 
ATOM   2905 C  CG    . ASP B 1 177 ? 35.786  17.941  40.372  1.00 87.89  ? 118 ASP B CG    1 
ATOM   2906 O  OD1   . ASP B 1 177 ? 35.669  17.835  41.615  1.00 91.03  ? 118 ASP B OD1   1 
ATOM   2907 O  OD2   . ASP B 1 177 ? 36.832  18.322  39.804  1.00 89.80  ? 118 ASP B OD2   1 
ATOM   2908 N  N     . GLN B 1 178 ? 34.276  17.694  36.006  1.00 79.25  ? 119 GLN B N     1 
ATOM   2909 C  CA    . GLN B 1 178 ? 34.823  17.150  34.763  1.00 74.32  ? 119 GLN B CA    1 
ATOM   2910 C  C     . GLN B 1 178 ? 34.178  17.755  33.522  1.00 73.08  ? 119 GLN B C     1 
ATOM   2911 O  O     . GLN B 1 178 ? 34.459  17.290  32.407  1.00 72.40  ? 119 GLN B O     1 
ATOM   2912 C  CB    . GLN B 1 178 ? 34.683  15.631  34.712  1.00 71.12  ? 119 GLN B CB    1 
ATOM   2913 C  CG    . GLN B 1 178 ? 35.759  14.919  35.506  1.00 87.51  ? 119 GLN B CG    1 
ATOM   2914 C  CD    . GLN B 1 178 ? 35.236  13.712  36.245  1.00 88.59  ? 119 GLN B CD    1 
ATOM   2915 O  OE1   . GLN B 1 178 ? 36.005  12.959  36.845  1.00 89.18  ? 119 GLN B OE1   1 
ATOM   2916 N  NE2   . GLN B 1 178 ? 33.923  13.512  36.200  1.00 84.42  ? 119 GLN B NE2   1 
ATOM   2917 N  N     . ARG B 1 179 ? 33.323  18.762  33.680  1.00 69.96  ? 120 ARG B N     1 
ATOM   2918 C  CA    . ARG B 1 179 ? 32.780  19.489  32.548  1.00 61.83  ? 120 ARG B CA    1 
ATOM   2919 C  C     . ARG B 1 179 ? 33.896  19.973  31.623  1.00 66.37  ? 120 ARG B C     1 
ATOM   2920 O  O     . ARG B 1 179 ? 35.037  20.180  32.051  1.00 66.09  ? 120 ARG B O     1 
ATOM   2921 C  CB    . ARG B 1 179 ? 31.959  20.655  33.068  1.00 59.43  ? 120 ARG B CB    1 
ATOM   2922 C  CG    . ARG B 1 179 ? 31.201  21.376  32.021  1.00 51.61  ? 120 ARG B CG    1 
ATOM   2923 C  CD    . ARG B 1 179 ? 30.817  22.720  32.494  1.00 49.47  ? 120 ARG B CD    1 
ATOM   2924 N  NE    . ARG B 1 179 ? 30.106  23.416  31.448  1.00 65.53  ? 120 ARG B NE    1 
ATOM   2925 C  CZ    . ARG B 1 179 ? 28.883  23.904  31.581  1.00 69.94  ? 120 ARG B CZ    1 
ATOM   2926 N  NH1   . ARG B 1 179 ? 28.249  23.761  32.740  1.00 67.66  ? 120 ARG B NH1   1 
ATOM   2927 N  NH2   . ARG B 1 179 ? 28.305  24.532  30.553  1.00 65.95  ? 120 ARG B NH2   1 
ATOM   2928 N  N     . VAL B 1 180 ? 33.555  20.131  30.333  1.00 68.26  ? 121 VAL B N     1 
ATOM   2929 C  CA    . VAL B 1 180 ? 34.499  20.485  29.269  1.00 62.72  ? 121 VAL B CA    1 
ATOM   2930 C  C     . VAL B 1 180 ? 33.916  21.541  28.328  1.00 61.09  ? 121 VAL B C     1 
ATOM   2931 O  O     . VAL B 1 180 ? 34.635  22.428  27.859  1.00 61.29  ? 121 VAL B O     1 
ATOM   2932 C  CB    . VAL B 1 180 ? 34.933  19.239  28.476  1.00 62.22  ? 121 VAL B CB    1 
ATOM   2933 C  CG1   . VAL B 1 180 ? 35.433  19.628  27.113  1.00 65.44  ? 121 VAL B CG1   1 
ATOM   2934 C  CG2   . VAL B 1 180 ? 36.014  18.481  29.224  1.00 66.92  ? 121 VAL B CG2   1 
ATOM   2935 N  N     . VAL B 1 181 ? 32.619  21.480  28.049  1.00 57.32  ? 122 VAL B N     1 
ATOM   2936 C  CA    . VAL B 1 181 ? 31.999  22.480  27.182  1.00 65.15  ? 122 VAL B CA    1 
ATOM   2937 C  C     . VAL B 1 181 ? 31.804  23.785  27.950  1.00 64.71  ? 122 VAL B C     1 
ATOM   2938 O  O     . VAL B 1 181 ? 31.167  23.806  29.010  1.00 63.03  ? 122 VAL B O     1 
ATOM   2939 C  CB    . VAL B 1 181 ? 30.660  21.970  26.626  1.00 65.16  ? 122 VAL B CB    1 
ATOM   2940 C  CG1   . VAL B 1 181 ? 30.054  23.003  25.663  1.00 61.95  ? 122 VAL B CG1   1 
ATOM   2941 C  CG2   . VAL B 1 181 ? 30.831  20.609  25.966  1.00 61.97  ? 122 VAL B CG2   1 
ATOM   2942 N  N     . LYS B 1 182 ? 32.333  24.883  27.407  1.00 65.70  ? 123 LYS B N     1 
ATOM   2943 C  CA    . LYS B 1 182 ? 32.012  26.211  27.924  1.00 69.45  ? 123 LYS B CA    1 
ATOM   2944 C  C     . LYS B 1 182 ? 30.514  26.476  27.782  1.00 70.02  ? 123 LYS B C     1 
ATOM   2945 O  O     . LYS B 1 182 ? 29.907  26.144  26.757  1.00 67.97  ? 123 LYS B O     1 
ATOM   2946 C  CB    . LYS B 1 182 ? 32.831  27.279  27.170  1.00 74.51  ? 123 LYS B CB    1 
ATOM   2947 C  CG    . LYS B 1 182 ? 32.678  28.755  27.632  1.00 79.87  ? 123 LYS B CG    1 
ATOM   2948 C  CD    . LYS B 1 182 ? 32.758  28.906  29.147  1.00 77.51  ? 123 LYS B CD    1 
ATOM   2949 C  CE    . LYS B 1 182 ? 34.156  28.656  29.649  1.00 76.04  ? 123 LYS B CE    1 
ATOM   2950 N  NZ    . LYS B 1 182 ? 34.120  28.175  31.033  1.00 74.84  ? 123 LYS B NZ    1 
ATOM   2951 N  N     . GLU B 1 183 ? 29.910  27.074  28.818  1.00 68.91  ? 124 GLU B N     1 
ATOM   2952 C  CA    . GLU B 1 183 ? 28.479  27.374  28.748  1.00 72.55  ? 124 GLU B CA    1 
ATOM   2953 C  C     . GLU B 1 183 ? 28.163  28.369  27.629  1.00 75.30  ? 124 GLU B C     1 
ATOM   2954 O  O     . GLU B 1 183 ? 27.245  28.146  26.831  1.00 70.23  ? 124 GLU B O     1 
ATOM   2955 C  CB    . GLU B 1 183 ? 27.954  27.902  30.086  1.00 70.66  ? 124 GLU B CB    1 
ATOM   2956 C  CG    . GLU B 1 183 ? 26.417  27.950  30.115  1.00 74.22  ? 124 GLU B CG    1 
ATOM   2957 C  CD    . GLU B 1 183 ? 25.832  28.680  31.312  1.00 76.48  ? 124 GLU B CD    1 
ATOM   2958 O  OE1   . GLU B 1 183 ? 26.526  29.551  31.883  1.00 81.64  ? 124 GLU B OE1   1 
ATOM   2959 O  OE2   . GLU B 1 183 ? 24.669  28.373  31.674  1.00 76.94  ? 124 GLU B OE2   1 
ATOM   2960 N  N     . GLU B 1 184 ? 28.892  29.492  27.565  1.00 75.94  ? 125 GLU B N     1 
ATOM   2961 C  CA    . GLU B 1 184 ? 28.619  30.452  26.497  1.00 82.54  ? 125 GLU B CA    1 
ATOM   2962 C  C     . GLU B 1 184 ? 28.865  29.825  25.132  1.00 76.15  ? 125 GLU B C     1 
ATOM   2963 O  O     . GLU B 1 184 ? 28.071  30.014  24.202  1.00 76.14  ? 125 GLU B O     1 
ATOM   2964 C  CB    . GLU B 1 184 ? 29.457  31.724  26.664  1.00 85.45  ? 125 GLU B CB    1 
ATOM   2965 C  CG    . GLU B 1 184 ? 28.810  32.983  26.033  1.00 90.34  ? 125 GLU B CG    1 
ATOM   2966 C  CD    . GLU B 1 184 ? 29.092  33.154  24.523  1.00 92.65  ? 125 GLU B CD    1 
ATOM   2967 O  OE1   . GLU B 1 184 ? 28.252  33.769  23.819  1.00 89.79  ? 125 GLU B OE1   1 
ATOM   2968 O  OE2   . GLU B 1 184 ? 30.146  32.680  24.036  1.00 93.24  ? 125 GLU B OE2   1 
ATOM   2969 N  N     . GLU B 1 185 ? 29.950  29.059  25.000  1.00 72.73  ? 126 GLU B N     1 
ATOM   2970 C  CA    . GLU B 1 185 ? 30.173  28.307  23.772  1.00 78.21  ? 126 GLU B CA    1 
ATOM   2971 C  C     . GLU B 1 185 ? 28.935  27.516  23.366  1.00 74.38  ? 126 GLU B C     1 
ATOM   2972 O  O     . GLU B 1 185 ? 28.596  27.447  22.180  1.00 74.28  ? 126 GLU B O     1 
ATOM   2973 C  CB    . GLU B 1 185 ? 31.356  27.369  23.956  1.00 76.52  ? 126 GLU B CB    1 
ATOM   2974 C  CG    . GLU B 1 185 ? 31.607  26.469  22.792  1.00 81.55  ? 126 GLU B CG    1 
ATOM   2975 C  CD    . GLU B 1 185 ? 33.021  25.929  22.800  1.00 92.76  ? 126 GLU B CD    1 
ATOM   2976 O  OE1   . GLU B 1 185 ? 33.315  25.055  23.657  1.00 84.85  ? 126 GLU B OE1   1 
ATOM   2977 O  OE2   . GLU B 1 185 ? 33.835  26.402  21.964  1.00 88.70  ? 126 GLU B OE2   1 
ATOM   2978 N  N     . ALA B 1 186 ? 28.232  26.934  24.346  1.00 77.11  ? 127 ALA B N     1 
ATOM   2979 C  CA    . ALA B 1 186 ? 27.031  26.147  24.075  1.00 71.08  ? 127 ALA B CA    1 
ATOM   2980 C  C     . ALA B 1 186 ? 25.807  27.025  23.843  1.00 74.79  ? 127 ALA B C     1 
ATOM   2981 O  O     . ALA B 1 186 ? 24.976  26.707  22.984  1.00 75.68  ? 127 ALA B O     1 
ATOM   2982 C  CB    . ALA B 1 186 ? 26.761  25.173  25.220  1.00 68.11  ? 127 ALA B CB    1 
ATOM   2983 N  N     . ILE B 1 187 ? 25.661  28.122  24.594  1.00 75.25  ? 128 ILE B N     1 
ATOM   2984 C  CA    . ILE B 1 187 ? 24.559  29.039  24.305  1.00 76.68  ? 128 ILE B CA    1 
ATOM   2985 C  C     . ILE B 1 187 ? 24.842  29.874  23.061  1.00 77.13  ? 128 ILE B C     1 
ATOM   2986 O  O     . ILE B 1 187 ? 23.903  30.354  22.413  1.00 75.33  ? 128 ILE B O     1 
ATOM   2987 C  CB    . ILE B 1 187 ? 24.244  29.963  25.495  1.00 78.28  ? 128 ILE B CB    1 
ATOM   2988 C  CG1   . ILE B 1 187 ? 24.319  29.190  26.811  1.00 72.36  ? 128 ILE B CG1   1 
ATOM   2989 C  CG2   . ILE B 1 187 ? 22.861  30.595  25.325  1.00 75.89  ? 128 ILE B CG2   1 
ATOM   2990 C  CD1   . ILE B 1 187 ? 23.913  30.011  27.996  1.00 72.09  ? 128 ILE B CD1   1 
ATOM   2991 N  N     . ALA B 1 188 ? 26.113  30.064  22.700  1.00 75.29  ? 129 ALA B N     1 
ATOM   2992 C  CA    . ALA B 1 188 ? 26.404  30.649  21.397  1.00 78.38  ? 129 ALA B CA    1 
ATOM   2993 C  C     . ALA B 1 188 ? 25.968  29.706  20.290  1.00 73.97  ? 129 ALA B C     1 
ATOM   2994 O  O     . ALA B 1 188 ? 25.290  30.114  19.342  1.00 72.82  ? 129 ALA B O     1 
ATOM   2995 C  CB    . ALA B 1 188 ? 27.892  30.977  21.272  1.00 84.43  ? 129 ALA B CB    1 
ATOM   2996 N  N     . LEU B 1 189 ? 26.336  28.428  20.408  1.00 75.43  ? 130 LEU B N     1 
ATOM   2997 C  CA    . LEU B 1 189 ? 25.798  27.416  19.504  1.00 77.24  ? 130 LEU B CA    1 
ATOM   2998 C  C     . LEU B 1 189 ? 24.274  27.342  19.602  1.00 73.08  ? 130 LEU B C     1 
ATOM   2999 O  O     . LEU B 1 189 ? 23.586  27.119  18.596  1.00 68.46  ? 130 LEU B O     1 
ATOM   3000 C  CB    . LEU B 1 189 ? 26.435  26.055  19.808  1.00 69.40  ? 130 LEU B CB    1 
ATOM   3001 C  CG    . LEU B 1 189 ? 26.434  25.074  18.633  1.00 69.27  ? 130 LEU B CG    1 
ATOM   3002 C  CD1   . LEU B 1 189 ? 27.612  24.105  18.693  1.00 68.96  ? 130 LEU B CD1   1 
ATOM   3003 C  CD2   . LEU B 1 189 ? 25.122  24.318  18.599  1.00 65.84  ? 130 LEU B CD2   1 
ATOM   3004 N  N     . ALA B 1 190 ? 23.726  27.539  20.802  1.00 71.50  ? 131 ALA B N     1 
ATOM   3005 C  CA    . ALA B 1 190 ? 22.277  27.492  20.963  1.00 73.30  ? 131 ALA B CA    1 
ATOM   3006 C  C     . ALA B 1 190 ? 21.610  28.716  20.345  1.00 73.02  ? 131 ALA B C     1 
ATOM   3007 O  O     . ALA B 1 190 ? 20.573  28.594  19.679  1.00 70.22  ? 131 ALA B O     1 
ATOM   3008 C  CB    . ALA B 1 190 ? 21.916  27.367  22.445  1.00 65.83  ? 131 ALA B CB    1 
ATOM   3009 N  N     . GLU B 1 191 ? 22.187  29.907  20.556  1.00 72.18  ? 132 GLU B N     1 
ATOM   3010 C  CA    . GLU B 1 191 ? 21.586  31.130  20.021  1.00 75.07  ? 132 GLU B CA    1 
ATOM   3011 C  C     . GLU B 1 191 ? 21.636  31.166  18.492  1.00 73.21  ? 132 GLU B C     1 
ATOM   3012 O  O     . GLU B 1 191 ? 20.710  31.682  17.851  1.00 72.00  ? 132 GLU B O     1 
ATOM   3013 C  CB    . GLU B 1 191 ? 22.278  32.360  20.615  1.00 78.14  ? 132 GLU B CB    1 
ATOM   3014 N  N     . LYS B 1 192 ? 22.702  30.624  17.892  1.00 70.33  ? 133 LYS B N     1 
ATOM   3015 C  CA    . LYS B 1 192 ? 22.790  30.536  16.438  1.00 61.27  ? 133 LYS B CA    1 
ATOM   3016 C  C     . LYS B 1 192 ? 21.546  29.865  15.851  1.00 65.86  ? 133 LYS B C     1 
ATOM   3017 O  O     . LYS B 1 192 ? 20.808  30.472  15.068  1.00 71.42  ? 133 LYS B O     1 
ATOM   3018 C  CB    . LYS B 1 192 ? 24.068  29.788  16.034  1.00 55.92  ? 133 LYS B CB    1 
ATOM   3019 N  N     . TYR B 1 193 ? 21.273  28.621  16.246  1.00 65.76  ? 134 TYR B N     1 
ATOM   3020 C  CA    . TYR B 1 193 ? 20.171  27.874  15.642  1.00 63.88  ? 134 TYR B CA    1 
ATOM   3021 C  C     . TYR B 1 193 ? 18.788  28.285  16.149  1.00 64.59  ? 134 TYR B C     1 
ATOM   3022 O  O     . TYR B 1 193 ? 17.790  27.719  15.688  1.00 62.05  ? 134 TYR B O     1 
ATOM   3023 C  CB    . TYR B 1 193 ? 20.355  26.376  15.880  1.00 61.30  ? 134 TYR B CB    1 
ATOM   3024 C  CG    . TYR B 1 193 ? 21.547  25.753  15.187  1.00 61.96  ? 134 TYR B CG    1 
ATOM   3025 C  CD1   . TYR B 1 193 ? 21.425  25.184  13.928  1.00 62.16  ? 134 TYR B CD1   1 
ATOM   3026 C  CD2   . TYR B 1 193 ? 22.790  25.707  15.806  1.00 62.38  ? 134 TYR B CD2   1 
ATOM   3027 C  CE1   . TYR B 1 193 ? 22.517  24.599  13.297  1.00 60.73  ? 134 TYR B CE1   1 
ATOM   3028 C  CE2   . TYR B 1 193 ? 23.888  25.122  15.184  1.00 58.98  ? 134 TYR B CE2   1 
ATOM   3029 C  CZ    . TYR B 1 193 ? 23.745  24.572  13.929  1.00 60.54  ? 134 TYR B CZ    1 
ATOM   3030 O  OH    . TYR B 1 193 ? 24.824  23.982  13.296  1.00 67.27  ? 134 TYR B OH    1 
ATOM   3031 N  N     . GLY B 1 194 ? 18.696  29.223  17.088  1.00 69.11  ? 135 GLY B N     1 
ATOM   3032 C  CA    . GLY B 1 194 ? 17.407  29.607  17.653  1.00 65.21  ? 135 GLY B CA    1 
ATOM   3033 C  C     . GLY B 1 194 ? 16.785  28.578  18.577  1.00 64.76  ? 135 GLY B C     1 
ATOM   3034 O  O     . GLY B 1 194 ? 15.552  28.425  18.592  1.00 61.36  ? 135 GLY B O     1 
ATOM   3035 N  N     . ILE B 1 195 ? 17.602  27.867  19.356  1.00 59.24  ? 136 ILE B N     1 
ATOM   3036 C  CA    . ILE B 1 195 ? 17.110  26.745  20.157  1.00 58.18  ? 136 ILE B CA    1 
ATOM   3037 C  C     . ILE B 1 195 ? 17.378  26.978  21.640  1.00 61.22  ? 136 ILE B C     1 
ATOM   3038 O  O     . ILE B 1 195 ? 18.451  27.479  22.015  1.00 60.39  ? 136 ILE B O     1 
ATOM   3039 C  CB    . ILE B 1 195 ? 17.730  25.411  19.700  1.00 60.08  ? 136 ILE B CB    1 
ATOM   3040 C  CG1   . ILE B 1 195 ? 19.260  25.505  19.658  1.00 61.79  ? 136 ILE B CG1   1 
ATOM   3041 C  CG2   . ILE B 1 195 ? 17.156  24.975  18.343  1.00 58.32  ? 136 ILE B CG2   1 
ATOM   3042 C  CD1   . ILE B 1 195 ? 19.944  24.193  19.334  1.00 55.95  ? 136 ILE B CD1   1 
ATOM   3043 N  N     . PRO B 1 196 ? 16.435  26.616  22.510  1.00 60.06  ? 137 PRO B N     1 
ATOM   3044 C  CA    . PRO B 1 196 ? 16.667  26.718  23.956  1.00 53.15  ? 137 PRO B CA    1 
ATOM   3045 C  C     . PRO B 1 196 ? 17.762  25.778  24.432  1.00 53.24  ? 137 PRO B C     1 
ATOM   3046 O  O     . PRO B 1 196 ? 17.945  24.678  23.909  1.00 52.84  ? 137 PRO B O     1 
ATOM   3047 C  CB    . PRO B 1 196 ? 15.323  26.311  24.558  1.00 51.63  ? 137 PRO B CB    1 
ATOM   3048 C  CG    . PRO B 1 196 ? 14.352  26.256  23.409  1.00 54.83  ? 137 PRO B CG    1 
ATOM   3049 C  CD    . PRO B 1 196 ? 15.134  26.009  22.189  1.00 58.22  ? 137 PRO B CD    1 
ATOM   3050 N  N     . TYR B 1 197 ? 18.472  26.209  25.472  1.00 52.23  ? 138 TYR B N     1 
ATOM   3051 C  CA    . TYR B 1 197 ? 19.571  25.432  26.023  1.00 54.20  ? 138 TYR B CA    1 
ATOM   3052 C  C     . TYR B 1 197 ? 19.398  25.251  27.522  1.00 56.74  ? 138 TYR B C     1 
ATOM   3053 O  O     . TYR B 1 197 ? 19.149  26.223  28.243  1.00 51.23  ? 138 TYR B O     1 
ATOM   3054 C  CB    . TYR B 1 197 ? 20.902  26.104  25.755  1.00 55.84  ? 138 TYR B CB    1 
ATOM   3055 C  CG    . TYR B 1 197 ? 22.051  25.397  26.405  1.00 59.36  ? 138 TYR B CG    1 
ATOM   3056 C  CD1   . TYR B 1 197 ? 22.358  24.090  26.059  1.00 57.94  ? 138 TYR B CD1   1 
ATOM   3057 C  CD2   . TYR B 1 197 ? 22.839  26.037  27.353  1.00 63.91  ? 138 TYR B CD2   1 
ATOM   3058 C  CE1   . TYR B 1 197 ? 23.419  23.435  26.631  1.00 59.68  ? 138 TYR B CE1   1 
ATOM   3059 C  CE2   . TYR B 1 197 ? 23.905  25.396  27.933  1.00 64.88  ? 138 TYR B CE2   1 
ATOM   3060 C  CZ    . TYR B 1 197 ? 24.189  24.088  27.571  1.00 65.19  ? 138 TYR B CZ    1 
ATOM   3061 O  OH    . TYR B 1 197 ? 25.250  23.429  28.149  1.00 66.13  ? 138 TYR B OH    1 
ATOM   3062 N  N     . PHE B 1 198 ? 19.564  24.006  27.978  1.00 59.93  ? 139 PHE B N     1 
ATOM   3063 C  CA    . PHE B 1 198 ? 19.504  23.624  29.382  1.00 52.88  ? 139 PHE B CA    1 
ATOM   3064 C  C     . PHE B 1 198 ? 20.717  22.776  29.714  1.00 52.53  ? 139 PHE B C     1 
ATOM   3065 O  O     . PHE B 1 198 ? 21.072  21.873  28.954  1.00 51.39  ? 139 PHE B O     1 
ATOM   3066 C  CB    . PHE B 1 198 ? 18.245  22.821  29.691  1.00 46.26  ? 139 PHE B CB    1 
ATOM   3067 C  CG    . PHE B 1 198 ? 16.973  23.597  29.551  1.00 54.28  ? 139 PHE B CG    1 
ATOM   3068 C  CD1   . PHE B 1 198 ? 16.463  23.918  28.295  1.00 59.78  ? 139 PHE B CD1   1 
ATOM   3069 C  CD2   . PHE B 1 198 ? 16.267  23.983  30.665  1.00 55.39  ? 139 PHE B CD2   1 
ATOM   3070 C  CE1   . PHE B 1 198 ? 15.270  24.618  28.171  1.00 60.06  ? 139 PHE B CE1   1 
ATOM   3071 C  CE2   . PHE B 1 198 ? 15.075  24.690  30.546  1.00 60.81  ? 139 PHE B CE2   1 
ATOM   3072 C  CZ    . PHE B 1 198 ? 14.575  25.003  29.312  1.00 59.58  ? 139 PHE B CZ    1 
ATOM   3073 N  N     . GLU B 1 199 ? 21.342  23.049  30.848  1.00 60.02  ? 140 GLU B N     1 
ATOM   3074 C  CA    . GLU B 1 199 ? 22.342  22.147  31.403  1.00 59.39  ? 140 GLU B CA    1 
ATOM   3075 C  C     . GLU B 1 199 ? 21.633  21.224  32.394  1.00 56.54  ? 140 GLU B C     1 
ATOM   3076 O  O     . GLU B 1 199 ? 21.133  21.675  33.433  1.00 60.10  ? 140 GLU B O     1 
ATOM   3077 C  CB    . GLU B 1 199 ? 23.476  22.933  32.051  1.00 62.42  ? 140 GLU B CB    1 
ATOM   3078 C  CG    . GLU B 1 199 ? 23.870  24.181  31.255  1.00 65.34  ? 140 GLU B CG    1 
ATOM   3079 C  CD    . GLU B 1 199 ? 25.363  24.369  31.202  1.00 66.26  ? 140 GLU B CD    1 
ATOM   3080 O  OE1   . GLU B 1 199 ? 26.023  24.087  32.222  1.00 75.89  ? 140 GLU B OE1   1 
ATOM   3081 O  OE2   . GLU B 1 199 ? 25.883  24.778  30.149  1.00 66.47  ? 140 GLU B OE2   1 
ATOM   3082 N  N     . THR B 1 200 ? 21.550  19.944  32.052  1.00 55.86  ? 141 THR B N     1 
ATOM   3083 C  CA    . THR B 1 200 ? 20.851  18.961  32.862  1.00 54.70  ? 141 THR B CA    1 
ATOM   3084 C  C     . THR B 1 200 ? 21.843  18.066  33.583  1.00 52.85  ? 141 THR B C     1 
ATOM   3085 O  O     . THR B 1 200 ? 23.031  18.010  33.249  1.00 50.56  ? 141 THR B O     1 
ATOM   3086 C  CB    . THR B 1 200 ? 19.928  18.078  32.007  1.00 55.02  ? 141 THR B CB    1 
ATOM   3087 O  OG1   . THR B 1 200 ? 20.604  17.709  30.793  1.00 53.87  ? 141 THR B OG1   1 
ATOM   3088 C  CG2   . THR B 1 200 ? 18.595  18.787  31.699  1.00 53.76  ? 141 THR B CG2   1 
ATOM   3089 N  N     . SER B 1 201 ? 21.314  17.333  34.562  1.00 56.18  ? 142 SER B N     1 
ATOM   3090 C  CA    . SER B 1 201 ? 21.969  16.154  35.114  1.00 55.69  ? 142 SER B CA    1 
ATOM   3091 C  C     . SER B 1 201 ? 20.917  15.072  35.294  1.00 53.31  ? 142 SER B C     1 
ATOM   3092 O  O     . SER B 1 201 ? 19.985  15.241  36.082  1.00 53.48  ? 142 SER B O     1 
ATOM   3093 C  CB    . SER B 1 201 ? 22.640  16.432  36.453  1.00 52.26  ? 142 SER B CB    1 
ATOM   3094 O  OG    . SER B 1 201 ? 23.168  15.211  36.923  1.00 47.10  ? 142 SER B OG    1 
ATOM   3095 N  N     . ALA B 1 202 ? 21.077  13.967  34.567  1.00 49.79  ? 143 ALA B N     1 
ATOM   3096 C  CA    . ALA B 1 202 ? 20.266  12.783  34.835  1.00 53.21  ? 143 ALA B CA    1 
ATOM   3097 C  C     . ALA B 1 202 ? 20.517  12.196  36.222  1.00 56.71  ? 143 ALA B C     1 
ATOM   3098 O  O     . ALA B 1 202 ? 19.699  11.395  36.695  1.00 52.75  ? 143 ALA B O     1 
ATOM   3099 C  CB    . ALA B 1 202 ? 20.536  11.709  33.788  1.00 56.23  ? 143 ALA B CB    1 
ATOM   3100 N  N     . ALA B 1 203 ? 21.627  12.563  36.877  1.00 53.75  ? 144 ALA B N     1 
ATOM   3101 C  CA    . ALA B 1 203 ? 21.906  12.027  38.205  1.00 53.20  ? 144 ALA B CA    1 
ATOM   3102 C  C     . ALA B 1 203 ? 20.931  12.588  39.232  1.00 58.47  ? 144 ALA B C     1 
ATOM   3103 O  O     . ALA B 1 203 ? 20.376  11.835  40.046  1.00 57.17  ? 144 ALA B O     1 
ATOM   3104 C  CB    . ALA B 1 203 ? 23.352  12.317  38.622  1.00 52.80  ? 144 ALA B CB    1 
ATOM   3105 N  N     . ASN B 1 204 ? 20.691  13.907  39.201  1.00 57.39  ? 145 ASN B N     1 
ATOM   3106 C  CA    . ASN B 1 204 ? 19.855  14.550  40.206  1.00 49.07  ? 145 ASN B CA    1 
ATOM   3107 C  C     . ASN B 1 204 ? 18.628  15.261  39.652  1.00 50.00  ? 145 ASN B C     1 
ATOM   3108 O  O     . ASN B 1 204 ? 17.906  15.899  40.427  1.00 55.34  ? 145 ASN B O     1 
ATOM   3109 C  CB    . ASN B 1 204 ? 20.685  15.530  41.052  1.00 52.38  ? 145 ASN B CB    1 
ATOM   3110 C  CG    . ASN B 1 204 ? 21.401  16.573  40.232  1.00 47.88  ? 145 ASN B CG    1 
ATOM   3111 O  OD1   . ASN B 1 204 ? 20.793  17.259  39.416  1.00 55.20  ? 145 ASN B OD1   1 
ATOM   3112 N  ND2   . ASN B 1 204 ? 22.708  16.717  40.464  1.00 46.96  ? 145 ASN B ND2   1 
ATOM   3113 N  N     . GLY B 1 205 ? 18.354  15.164  38.354  1.00 55.29  ? 146 GLY B N     1 
ATOM   3114 C  CA    . GLY B 1 205 ? 17.150  15.745  37.787  1.00 53.08  ? 146 GLY B CA    1 
ATOM   3115 C  C     . GLY B 1 205 ? 17.213  17.227  37.470  1.00 53.68  ? 146 GLY B C     1 
ATOM   3116 O  O     . GLY B 1 205 ? 16.189  17.791  37.040  1.00 54.47  ? 146 GLY B O     1 
ATOM   3117 N  N     . THR B 1 206 ? 18.368  17.874  37.666  1.00 49.66  ? 147 THR B N     1 
ATOM   3118 C  CA    . THR B 1 206 ? 18.507  19.299  37.392  1.00 54.38  ? 147 THR B CA    1 
ATOM   3119 C  C     . THR B 1 206 ? 17.962  19.626  36.010  1.00 57.34  ? 147 THR B C     1 
ATOM   3120 O  O     . THR B 1 206 ? 18.412  19.056  35.007  1.00 53.68  ? 147 THR B O     1 
ATOM   3121 C  CB    . THR B 1 206 ? 19.981  19.720  37.479  1.00 56.61  ? 147 THR B CB    1 
ATOM   3122 O  OG1   . THR B 1 206 ? 20.504  19.486  38.794  1.00 57.88  ? 147 THR B OG1   1 
ATOM   3123 C  CG2   . THR B 1 206 ? 20.145  21.200  37.146  1.00 55.93  ? 147 THR B CG2   1 
ATOM   3124 N  N     . ASN B 1 207 ? 16.948  20.499  35.975  1.00 56.38  ? 148 ASN B N     1 
ATOM   3125 C  CA    . ASN B 1 207 ? 16.433  21.093  34.740  1.00 60.47  ? 148 ASN B CA    1 
ATOM   3126 C  C     . ASN B 1 207 ? 15.785  20.086  33.795  1.00 62.14  ? 148 ASN B C     1 
ATOM   3127 O  O     . ASN B 1 207 ? 15.294  20.452  32.723  1.00 57.74  ? 148 ASN B O     1 
ATOM   3128 C  CB    . ASN B 1 207 ? 17.549  21.825  33.998  1.00 60.20  ? 148 ASN B CB    1 
ATOM   3129 C  CG    . ASN B 1 207 ? 17.761  23.209  34.520  1.00 58.84  ? 148 ASN B CG    1 
ATOM   3130 O  OD1   . ASN B 1 207 ? 18.824  23.525  35.058  1.00 60.42  ? 148 ASN B OD1   1 
ATOM   3131 N  ND2   . ASN B 1 207 ? 16.734  24.046  34.398  1.00 61.10  ? 148 ASN B ND2   1 
ATOM   3132 N  N     . ILE B 1 208 ? 15.768  18.816  34.181  1.00 62.68  ? 149 ILE B N     1 
ATOM   3133 C  CA    . ILE B 1 208 ? 15.249  17.788  33.289  1.00 52.74  ? 149 ILE B CA    1 
ATOM   3134 C  C     . ILE B 1 208 ? 13.757  17.990  33.043  1.00 55.14  ? 149 ILE B C     1 
ATOM   3135 O  O     . ILE B 1 208 ? 13.304  18.016  31.898  1.00 66.66  ? 149 ILE B O     1 
ATOM   3136 C  CB    . ILE B 1 208 ? 15.569  16.398  33.853  1.00 46.45  ? 149 ILE B CB    1 
ATOM   3137 C  CG1   . ILE B 1 208 ? 17.085  16.265  33.961  1.00 48.99  ? 149 ILE B CG1   1 
ATOM   3138 C  CG2   . ILE B 1 208 ? 14.966  15.332  32.988  1.00 50.45  ? 149 ILE B CG2   1 
ATOM   3139 C  CD1   . ILE B 1 208 ? 17.604  14.864  33.876  1.00 52.36  ? 149 ILE B CD1   1 
ATOM   3140 N  N     . SER B 1 209 ? 12.972  18.166  34.103  1.00 63.86  ? 150 SER B N     1 
ATOM   3141 C  CA    . SER B 1 209 ? 11.557  18.464  33.905  1.00 64.59  ? 150 SER B CA    1 
ATOM   3142 C  C     . SER B 1 209 ? 11.376  19.789  33.173  1.00 66.26  ? 150 SER B C     1 
ATOM   3143 O  O     . SER B 1 209 ? 10.522  19.910  32.281  1.00 60.11  ? 150 SER B O     1 
ATOM   3144 C  CB    . SER B 1 209 ? 10.816  18.476  35.248  1.00 60.11  ? 150 SER B CB    1 
ATOM   3145 O  OG    . SER B 1 209 ? 11.267  17.418  36.089  1.00 72.01  ? 150 SER B OG    1 
ATOM   3146 N  N     . GLN B 1 210 ? 12.184  20.792  33.520  1.00 65.27  ? 151 GLN B N     1 
ATOM   3147 C  CA    . GLN B 1 210 ? 11.988  22.108  32.925  1.00 63.86  ? 151 GLN B CA    1 
ATOM   3148 C  C     . GLN B 1 210 ? 12.308  22.090  31.443  1.00 63.97  ? 151 GLN B C     1 
ATOM   3149 O  O     . GLN B 1 210 ? 11.589  22.703  30.641  1.00 61.81  ? 151 GLN B O     1 
ATOM   3150 C  CB    . GLN B 1 210 ? 12.829  23.143  33.664  1.00 65.58  ? 151 GLN B CB    1 
ATOM   3151 C  CG    . GLN B 1 210 ? 12.437  23.265  35.143  1.00 74.26  ? 151 GLN B CG    1 
ATOM   3152 C  CD    . GLN B 1 210 ? 13.304  22.421  36.094  1.00 75.61  ? 151 GLN B CD    1 
ATOM   3153 O  OE1   . GLN B 1 210 ? 13.111  21.203  36.216  1.00 73.95  ? 151 GLN B OE1   1 
ATOM   3154 N  NE2   . GLN B 1 210 ? 14.264  23.066  36.764  1.00 70.74  ? 151 GLN B NE2   1 
ATOM   3155 N  N     . ALA B 1 211 ? 13.366  21.363  31.062  1.00 64.25  ? 152 ALA B N     1 
ATOM   3156 C  CA    . ALA B 1 211 ? 13.737  21.255  29.658  1.00 62.46  ? 152 ALA B CA    1 
ATOM   3157 C  C     . ALA B 1 211 ? 12.671  20.516  28.858  1.00 62.12  ? 152 ALA B C     1 
ATOM   3158 O  O     . ALA B 1 211 ? 12.346  20.906  27.730  1.00 63.99  ? 152 ALA B O     1 
ATOM   3159 C  CB    . ALA B 1 211 ? 15.087  20.555  29.528  1.00 57.10  ? 152 ALA B CB    1 
ATOM   3160 N  N     . ILE B 1 212 ? 12.109  19.451  29.424  1.00 55.85  ? 153 ILE B N     1 
ATOM   3161 C  CA    . ILE B 1 212 ? 11.115  18.677  28.686  1.00 60.98  ? 153 ILE B CA    1 
ATOM   3162 C  C     . ILE B 1 212 ? 9.817   19.467  28.534  1.00 62.09  ? 153 ILE B C     1 
ATOM   3163 O  O     . ILE B 1 212 ? 9.263   19.579  27.433  1.00 62.57  ? 153 ILE B O     1 
ATOM   3164 C  CB    . ILE B 1 212 ? 10.885  17.317  29.368  1.00 60.39  ? 153 ILE B CB    1 
ATOM   3165 C  CG1   . ILE B 1 212 ? 12.002  16.342  28.950  1.00 58.27  ? 153 ILE B CG1   1 
ATOM   3166 C  CG2   . ILE B 1 212 ? 9.477   16.798  29.065  1.00 59.12  ? 153 ILE B CG2   1 
ATOM   3167 C  CD1   . ILE B 1 212 ? 11.791  14.896  29.382  1.00 57.27  ? 153 ILE B CD1   1 
ATOM   3168 N  N     . GLU B 1 213 ? 9.316   20.027  29.639  1.00 68.58  ? 154 GLU B N     1 
ATOM   3169 C  CA    . GLU B 1 213 ? 8.115   20.856  29.585  1.00 68.90  ? 154 GLU B CA    1 
ATOM   3170 C  C     . GLU B 1 213 ? 8.285   21.997  28.595  1.00 66.71  ? 154 GLU B C     1 
ATOM   3171 O  O     . GLU B 1 213 ? 7.330   22.406  27.922  1.00 62.64  ? 154 GLU B O     1 
ATOM   3172 C  CB    . GLU B 1 213 ? 7.798   21.404  30.975  1.00 65.80  ? 154 GLU B CB    1 
ATOM   3173 C  CG    . GLU B 1 213 ? 7.223   20.366  31.921  1.00 68.63  ? 154 GLU B CG    1 
ATOM   3174 C  CD    . GLU B 1 213 ? 7.766   20.508  33.322  1.00 77.02  ? 154 GLU B CD    1 
ATOM   3175 O  OE1   . GLU B 1 213 ? 7.852   19.477  34.034  1.00 84.60  ? 154 GLU B OE1   1 
ATOM   3176 O  OE2   . GLU B 1 213 ? 8.107   21.653  33.710  1.00 70.16  ? 154 GLU B OE2   1 
ATOM   3177 N  N     . MET B 1 214 ? 9.502   22.520  28.498  1.00 61.72  ? 155 MET B N     1 
ATOM   3178 C  CA    . MET B 1 214 ? 9.762   23.590  27.555  1.00 60.06  ? 155 MET B CA    1 
ATOM   3179 C  C     . MET B 1 214 ? 9.618   23.096  26.128  1.00 68.63  ? 155 MET B C     1 
ATOM   3180 O  O     . MET B 1 214 ? 9.047   23.783  25.276  1.00 69.81  ? 155 MET B O     1 
ATOM   3181 C  CB    . MET B 1 214 ? 11.154  24.137  27.800  1.00 67.08  ? 155 MET B CB    1 
ATOM   3182 C  CG    . MET B 1 214 ? 11.138  25.485  28.451  1.00 82.81  ? 155 MET B CG    1 
ATOM   3183 S  SD    . MET B 1 214 ? 11.012  26.631  27.098  1.00 74.79  ? 155 MET B SD    1 
ATOM   3184 C  CE    . MET B 1 214 ? 12.606  26.239  26.452  1.00 53.69  ? 155 MET B CE    1 
ATOM   3185 N  N     . LEU B 1 215 ? 10.093  21.886  25.854  1.00 67.94  ? 156 LEU B N     1 
ATOM   3186 C  CA    . LEU B 1 215 ? 9.807   21.266  24.570  1.00 62.88  ? 156 LEU B CA    1 
ATOM   3187 C  C     . LEU B 1 215 ? 8.303   21.094  24.377  1.00 68.54  ? 156 LEU B C     1 
ATOM   3188 O  O     . LEU B 1 215 ? 7.783   21.349  23.287  1.00 68.49  ? 156 LEU B O     1 
ATOM   3189 C  CB    . LEU B 1 215 ? 10.531  19.923  24.465  1.00 65.14  ? 156 LEU B CB    1 
ATOM   3190 C  CG    . LEU B 1 215 ? 10.388  19.221  23.116  1.00 62.72  ? 156 LEU B CG    1 
ATOM   3191 C  CD1   . LEU B 1 215 ? 10.799  20.145  21.989  1.00 61.89  ? 156 LEU B CD1   1 
ATOM   3192 C  CD2   . LEU B 1 215 ? 11.227  17.960  23.091  1.00 64.73  ? 156 LEU B CD2   1 
ATOM   3193 N  N     . LEU B 1 216 ? 7.580   20.676  25.426  1.00 71.73  ? 157 LEU B N     1 
ATOM   3194 C  CA    . LEU B 1 216 ? 6.128   20.553  25.282  1.00 74.93  ? 157 LEU B CA    1 
ATOM   3195 C  C     . LEU B 1 216 ? 5.484   21.912  25.059  1.00 74.23  ? 157 LEU B C     1 
ATOM   3196 O  O     . LEU B 1 216 ? 4.543   22.035  24.260  1.00 75.27  ? 157 LEU B O     1 
ATOM   3197 C  CB    . LEU B 1 216 ? 5.510   19.853  26.496  1.00 70.38  ? 157 LEU B CB    1 
ATOM   3198 C  CG    . LEU B 1 216 ? 4.190   19.104  26.213  1.00 76.22  ? 157 LEU B CG    1 
ATOM   3199 C  CD1   . LEU B 1 216 ? 3.831   18.179  27.384  1.00 78.48  ? 157 LEU B CD1   1 
ATOM   3200 C  CD2   . LEU B 1 216 ? 2.985   20.015  25.858  1.00 81.63  ? 157 LEU B CD2   1 
ATOM   3201 N  N     . ASP B 1 217 ? 5.971   22.943  25.755  1.00 70.83  ? 158 ASP B N     1 
ATOM   3202 C  CA    . ASP B 1 217 ? 5.552   24.303  25.446  1.00 73.01  ? 158 ASP B CA    1 
ATOM   3203 C  C     . ASP B 1 217 ? 5.687   24.561  23.950  1.00 77.83  ? 158 ASP B C     1 
ATOM   3204 O  O     . ASP B 1 217 ? 4.687   24.715  23.242  1.00 80.06  ? 158 ASP B O     1 
ATOM   3205 C  CB    . ASP B 1 217 ? 6.379   25.312  26.249  1.00 74.74  ? 158 ASP B CB    1 
ATOM   3206 C  CG    . ASP B 1 217 ? 5.651   26.626  26.455  1.00 77.18  ? 158 ASP B CG    1 
ATOM   3207 O  OD1   . ASP B 1 217 ? 4.405   26.603  26.513  1.00 76.89  ? 158 ASP B OD1   1 
ATOM   3208 O  OD2   . ASP B 1 217 ? 6.317   27.678  26.573  1.00 80.99  ? 158 ASP B OD2   1 
ATOM   3209 N  N     . LEU B 1 218 ? 6.927   24.530  23.445  1.00 75.11  ? 159 LEU B N     1 
ATOM   3210 C  CA    . LEU B 1 218 ? 7.207   24.739  22.021  1.00 76.47  ? 159 LEU B CA    1 
ATOM   3211 C  C     . LEU B 1 218 ? 6.250   23.957  21.113  1.00 79.10  ? 159 LEU B C     1 
ATOM   3212 O  O     . LEU B 1 218 ? 5.743   24.493  20.118  1.00 78.87  ? 159 LEU B O     1 
ATOM   3213 C  CB    . LEU B 1 218 ? 8.663   24.351  21.726  1.00 69.67  ? 159 LEU B CB    1 
ATOM   3214 C  CG    . LEU B 1 218 ? 9.722   25.457  21.807  1.00 73.42  ? 159 LEU B CG    1 
ATOM   3215 C  CD1   . LEU B 1 218 ? 11.128  24.872  21.940  1.00 69.81  ? 159 LEU B CD1   1 
ATOM   3216 C  CD2   . LEU B 1 218 ? 9.656   26.407  20.602  1.00 80.72  ? 159 LEU B CD2   1 
ATOM   3217 N  N     . ILE B 1 219 ? 5.981   22.692  21.450  1.00 74.20  ? 160 ILE B N     1 
ATOM   3218 C  CA    . ILE B 1 219 ? 5.140   21.851  20.599  1.00 76.17  ? 160 ILE B CA    1 
ATOM   3219 C  C     . ILE B 1 219 ? 3.696   22.338  20.620  1.00 79.45  ? 160 ILE B C     1 
ATOM   3220 O  O     . ILE B 1 219 ? 3.110   22.644  19.577  1.00 86.55  ? 160 ILE B O     1 
ATOM   3221 C  CB    . ILE B 1 219 ? 5.244   20.373  21.020  1.00 70.20  ? 160 ILE B CB    1 
ATOM   3222 C  CG1   . ILE B 1 219 ? 6.459   19.727  20.364  1.00 66.06  ? 160 ILE B CG1   1 
ATOM   3223 C  CG2   . ILE B 1 219 ? 3.995   19.585  20.639  1.00 64.61  ? 160 ILE B CG2   1 
ATOM   3224 C  CD1   . ILE B 1 219 ? 7.137   18.721  21.256  1.00 62.89  ? 160 ILE B CD1   1 
ATOM   3225 N  N     . MET B 1 220 ? 3.099   22.427  21.804  1.00 83.76  ? 161 MET B N     1 
ATOM   3226 C  CA    . MET B 1 220 ? 1.696   22.810  21.856  1.00 86.50  ? 161 MET B CA    1 
ATOM   3227 C  C     . MET B 1 220 ? 1.450   24.272  21.491  1.00 88.74  ? 161 MET B C     1 
ATOM   3228 O  O     . MET B 1 220 ? 0.285   24.660  21.351  1.00 92.45  ? 161 MET B O     1 
ATOM   3229 C  CB    . MET B 1 220 ? 1.128   22.497  23.236  1.00 85.79  ? 161 MET B CB    1 
ATOM   3230 C  CG    . MET B 1 220 ? 0.652   21.072  23.328  1.00 85.92  ? 161 MET B CG    1 
ATOM   3231 S  SD    . MET B 1 220 ? -0.705  20.874  24.485  1.00 113.13 ? 161 MET B SD    1 
ATOM   3232 C  CE    . MET B 1 220 ? -1.471  22.493  24.433  1.00 94.61  ? 161 MET B CE    1 
ATOM   3233 N  N     . LYS B 1 221 ? 2.493   25.093  21.322  1.00 84.71  ? 162 LYS B N     1 
ATOM   3234 C  CA    . LYS B 1 221 ? 2.279   26.393  20.696  1.00 85.35  ? 162 LYS B CA    1 
ATOM   3235 C  C     . LYS B 1 221 ? 2.360   26.320  19.177  1.00 90.24  ? 162 LYS B C     1 
ATOM   3236 O  O     . LYS B 1 221 ? 1.893   27.246  18.505  1.00 95.37  ? 162 LYS B O     1 
ATOM   3237 C  CB    . LYS B 1 221 ? 3.274   27.464  21.188  1.00 84.01  ? 162 LYS B CB    1 
ATOM   3238 C  CG    . LYS B 1 221 ? 3.713   27.486  22.682  1.00 90.03  ? 162 LYS B CG    1 
ATOM   3239 C  CD    . LYS B 1 221 ? 2.727   26.910  23.745  1.00 86.89  ? 162 LYS B CD    1 
ATOM   3240 C  CE    . LYS B 1 221 ? 1.373   27.572  23.854  1.00 81.22  ? 162 LYS B CE    1 
ATOM   3241 N  NZ    . LYS B 1 221 ? 0.452   26.602  24.515  1.00 81.39  ? 162 LYS B NZ    1 
ATOM   3242 N  N     . ARG B 1 222 ? 2.930   25.240  18.622  1.00 91.21  ? 163 ARG B N     1 
ATOM   3243 C  CA    . ARG B 1 222 ? 2.960   25.055  17.171  1.00 92.72  ? 163 ARG B CA    1 
ATOM   3244 C  C     . ARG B 1 222 ? 1.573   24.785  16.598  1.00 95.52  ? 163 ARG B C     1 
ATOM   3245 O  O     . ARG B 1 222 ? 1.358   25.007  15.399  1.00 102.26 ? 163 ARG B O     1 
ATOM   3246 C  CB    . ARG B 1 222 ? 3.917   23.918  16.793  1.00 86.47  ? 163 ARG B CB    1 
ATOM   3247 C  CG    . ARG B 1 222 ? 4.444   23.958  15.360  1.00 88.55  ? 163 ARG B CG    1 
ATOM   3248 C  CD    . ARG B 1 222 ? 4.712   22.535  14.862  1.00 92.09  ? 163 ARG B CD    1 
ATOM   3249 N  NE    . ARG B 1 222 ? 5.453   22.471  13.602  1.00 84.44  ? 163 ARG B NE    1 
ATOM   3250 C  CZ    . ARG B 1 222 ? 6.745   22.764  13.463  1.00 83.78  ? 163 ARG B CZ    1 
ATOM   3251 N  NH1   . ARG B 1 222 ? 7.463   23.162  14.507  1.00 84.13  ? 163 ARG B NH1   1 
ATOM   3252 N  NH2   . ARG B 1 222 ? 7.322   22.661  12.271  1.00 87.85  ? 163 ARG B NH2   1 
ATOM   3253 N  N     . MET B 1 223 ? 0.631   24.317  17.420  1.00 95.61  ? 164 MET B N     1 
ATOM   3254 C  CA    . MET B 1 223 ? -0.784  24.380  17.066  1.00 100.88 ? 164 MET B CA    1 
ATOM   3255 C  C     . MET B 1 223 ? -1.191  25.843  16.905  1.00 105.44 ? 164 MET B C     1 
ATOM   3256 O  O     . MET B 1 223 ? -1.881  26.404  17.765  1.00 104.18 ? 164 MET B O     1 
ATOM   3257 C  CB    . MET B 1 223 ? -1.650  23.692  18.124  1.00 94.67  ? 164 MET B CB    1 
ATOM   3258 C  CG    . MET B 1 223 ? -1.693  22.166  18.027  1.00 98.11  ? 164 MET B CG    1 
ATOM   3259 S  SD    . MET B 1 223 ? -0.140  21.358  18.483  1.00 100.24 ? 164 MET B SD    1 
ATOM   3260 C  CE    . MET B 1 223 ? -0.692  19.675  18.784  1.00 82.20  ? 164 MET B CE    1 
ATOM   3261 N  N     . GLU B 1 224 ? -0.751  26.465  15.806  1.00 105.60 ? 165 GLU B N     1 
ATOM   3262 C  CA    . GLU B 1 224 ? -0.907  27.898  15.569  1.00 103.38 ? 165 GLU B CA    1 
ATOM   3263 C  C     . GLU B 1 224 ? -2.044  28.093  14.570  1.00 108.99 ? 165 GLU B C     1 
ATOM   3264 O  O     . GLU B 1 224 ? -1.851  27.975  13.355  1.00 100.16 ? 165 GLU B O     1 
ATOM   3265 C  CB    . GLU B 1 224 ? 0.402   28.503  15.070  1.00 95.51  ? 165 GLU B CB    1 
ATOM   3266 N  N     . ARG B 1 225 ? -3.234  28.384  15.095  1.00 113.96 ? 166 ARG B N     1 
ATOM   3267 C  CA    . ARG B 1 225 ? -4.406  28.614  14.264  1.00 110.39 ? 166 ARG B CA    1 
ATOM   3268 C  C     . ARG B 1 225 ? -4.175  29.796  13.327  1.00 99.98  ? 166 ARG B C     1 
ATOM   3269 O  O     . ARG B 1 225 ? -3.351  30.683  13.583  1.00 85.45  ? 166 ARG B O     1 
ATOM   3270 C  CB    . ARG B 1 225 ? -5.639  28.865  15.139  1.00 109.81 ? 166 ARG B CB    1 
ATOM   3271 N  N     . SER B 1 226 ? -4.913  29.795  12.222  1.00 102.88 ? 167 SER B N     1 
ATOM   3272 C  CA    . SER B 1 226 ? -4.801  30.861  11.232  1.00 102.34 ? 167 SER B CA    1 
ATOM   3273 C  C     . SER B 1 226 ? -6.182  31.335  10.788  1.00 98.90  ? 167 SER B C     1 
ATOM   3274 O  O     . SER B 1 226 ? -6.358  31.803  9.662   1.00 100.65 ? 167 SER B O     1 
ATOM   3275 C  CB    . SER B 1 226 ? -3.980  30.391  10.023  1.00 98.76  ? 167 SER B CB    1 
ATOM   3276 O  OG    . SER B 1 226 ? -2.919  29.531  10.413  1.00 99.44  ? 167 SER B OG    1 
HETATM 3277 P  PG    . GNP C 2 .   ? 13.403  -9.234  -1.413  1.00 48.55  ? 201 GNP A PG    1 
HETATM 3278 O  O1G   . GNP C 2 .   ? 14.599  -10.058 -1.018  1.00 48.35  ? 201 GNP A O1G   1 
HETATM 3279 O  O2G   . GNP C 2 .   ? 12.434  -9.252  -0.210  1.00 48.66  ? 201 GNP A O2G   1 
HETATM 3280 O  O3G   . GNP C 2 .   ? 13.873  -7.823  -1.900  1.00 39.13  ? 201 GNP A O3G   1 
HETATM 3281 N  N3B   . GNP C 2 .   ? 12.699  -10.058 -2.709  1.00 49.05  ? 201 GNP A N3B   1 
HETATM 3282 P  PB    . GNP C 2 .   ? 11.326  -9.521  -3.386  1.00 43.13  ? 201 GNP A PB    1 
HETATM 3283 O  O1B   . GNP C 2 .   ? 11.314  -8.021  -3.366  1.00 44.42  ? 201 GNP A O1B   1 
HETATM 3284 O  O2B   . GNP C 2 .   ? 10.105  -10.107 -2.735  1.00 43.88  ? 201 GNP A O2B   1 
HETATM 3285 O  O3A   . GNP C 2 .   ? 11.357  -10.180 -4.902  1.00 55.57  ? 201 GNP A O3A   1 
HETATM 3286 P  PA    . GNP C 2 .   ? 11.956  -9.506  -6.199  1.00 47.56  ? 201 GNP A PA    1 
HETATM 3287 O  O1A   . GNP C 2 .   ? 13.076  -8.586  -5.727  1.00 52.60  ? 201 GNP A O1A   1 
HETATM 3288 O  O2A   . GNP C 2 .   ? 10.882  -8.956  -6.999  1.00 50.92  ? 201 GNP A O2A   1 
HETATM 3289 O  "O5'" . GNP C 2 .   ? 12.649  -10.655 -6.988  1.00 52.92  ? 201 GNP A "O5'" 1 
HETATM 3290 C  "C5'" . GNP C 2 .   ? 12.170  -12.012 -6.912  1.00 50.62  ? 201 GNP A "C5'" 1 
HETATM 3291 C  "C4'" . GNP C 2 .   ? 12.901  -12.823 -7.955  1.00 54.36  ? 201 GNP A "C4'" 1 
HETATM 3292 O  "O4'" . GNP C 2 .   ? 11.944  -13.564 -8.738  1.00 48.32  ? 201 GNP A "O4'" 1 
HETATM 3293 C  "C3'" . GNP C 2 .   ? 13.681  -12.018 -8.986  1.00 53.26  ? 201 GNP A "C3'" 1 
HETATM 3294 O  "O3'" . GNP C 2 .   ? 14.676  -12.822 -9.607  1.00 52.05  ? 201 GNP A "O3'" 1 
HETATM 3295 C  "C2'" . GNP C 2 .   ? 12.586  -11.640 -9.983  1.00 50.99  ? 201 GNP A "C2'" 1 
HETATM 3296 O  "O2'" . GNP C 2 .   ? 13.083  -11.485 -11.306 1.00 54.76  ? 201 GNP A "O2'" 1 
HETATM 3297 C  "C1'" . GNP C 2 .   ? 11.673  -12.871 -9.936  1.00 48.61  ? 201 GNP A "C1'" 1 
HETATM 3298 N  N9    . GNP C 2 .   ? 10.244  -12.539 -9.967  1.00 49.11  ? 201 GNP A N9    1 
HETATM 3299 C  C8    . GNP C 2 .   ? 9.560   -11.667 -9.169  1.00 47.63  ? 201 GNP A C8    1 
HETATM 3300 N  N7    . GNP C 2 .   ? 8.286   -11.581 -9.477  1.00 50.56  ? 201 GNP A N7    1 
HETATM 3301 C  C5    . GNP C 2 .   ? 8.129   -12.453 -10.547 1.00 50.19  ? 201 GNP A C5    1 
HETATM 3302 C  C6    . GNP C 2 .   ? 6.964   -12.810 -11.328 1.00 48.03  ? 201 GNP A C6    1 
HETATM 3303 O  O6    . GNP C 2 .   ? 5.804   -12.382 -11.208 1.00 48.28  ? 201 GNP A O6    1 
HETATM 3304 N  N1    . GNP C 2 .   ? 7.261   -13.739 -12.301 1.00 49.16  ? 201 GNP A N1    1 
HETATM 3305 C  C2    . GNP C 2 .   ? 8.502   -14.265 -12.536 1.00 52.82  ? 201 GNP A C2    1 
HETATM 3306 N  N2    . GNP C 2 .   ? 8.607   -15.139 -13.544 1.00 57.96  ? 201 GNP A N2    1 
HETATM 3307 N  N3    . GNP C 2 .   ? 9.581   -13.946 -11.824 1.00 46.73  ? 201 GNP A N3    1 
HETATM 3308 C  C4    . GNP C 2 .   ? 9.326   -13.042 -10.860 1.00 51.89  ? 201 GNP A C4    1 
HETATM 3309 C  C1    . GOL D 3 .   ? 15.248  -7.098  -10.007 1.00 59.92  ? 202 GOL A C1    1 
HETATM 3310 O  O1    . GOL D 3 .   ? 15.812  -5.969  -9.410  1.00 60.50  ? 202 GOL A O1    1 
HETATM 3311 C  C2    . GOL D 3 .   ? 14.002  -7.482  -9.166  1.00 63.46  ? 202 GOL A C2    1 
HETATM 3312 O  O2    . GOL D 3 .   ? 14.310  -7.999  -7.870  1.00 53.35  ? 202 GOL A O2    1 
HETATM 3313 C  C3    . GOL D 3 .   ? 13.187  -6.152  -9.152  1.00 58.67  ? 202 GOL A C3    1 
HETATM 3314 O  O3    . GOL D 3 .   ? 13.131  -5.691  -10.482 1.00 49.30  ? 202 GOL A O3    1 
HETATM 3315 C  C1    . GOL E 3 .   ? 13.591  -14.879 5.256   1.00 60.05  ? 203 GOL A C1    1 
HETATM 3316 O  O1    . GOL E 3 .   ? 13.472  -13.850 4.366   1.00 60.01  ? 203 GOL A O1    1 
HETATM 3317 C  C2    . GOL E 3 .   ? 12.679  -16.003 4.753   1.00 62.93  ? 203 GOL A C2    1 
HETATM 3318 O  O2    . GOL E 3 .   ? 13.403  -17.166 4.494   1.00 76.20  ? 203 GOL A O2    1 
HETATM 3319 C  C3    . GOL E 3 .   ? 11.646  -16.215 5.901   1.00 65.28  ? 203 GOL A C3    1 
HETATM 3320 O  O3    . GOL E 3 .   ? 10.921  -15.003 6.047   1.00 65.55  ? 203 GOL A O3    1 
HETATM 3321 C  C1    . GOL F 3 .   ? 12.528  -16.179 -11.011 1.00 61.70  ? 204 GOL A C1    1 
HETATM 3322 O  O1    . GOL F 3 .   ? 13.035  -15.856 -9.693  1.00 51.55  ? 204 GOL A O1    1 
HETATM 3323 C  C2    . GOL F 3 .   ? 13.301  -15.318 -12.133 1.00 51.43  ? 204 GOL A C2    1 
HETATM 3324 O  O2    . GOL F 3 .   ? 14.236  -16.063 -12.867 1.00 50.32  ? 204 GOL A O2    1 
HETATM 3325 C  C3    . GOL F 3 .   ? 12.172  -14.738 -13.037 1.00 54.45  ? 204 GOL A C3    1 
HETATM 3326 O  O3    . GOL F 3 .   ? 11.955  -15.550 -14.180 1.00 51.00  ? 204 GOL A O3    1 
HETATM 3327 C  C08   . WTO G 4 .   ? -3.831  2.481   9.251   1.00 70.85  ? 205 WTO A C08   1 
HETATM 3328 C  C09   . WTO G 4 .   ? -2.737  3.248   10.029  1.00 76.52  ? 205 WTO A C09   1 
HETATM 3329 C  C10   . WTO G 4 .   ? -2.363  4.646   9.475   0.97 80.21  ? 205 WTO A C10   1 
HETATM 3330 C  C12   . WTO G 4 .   ? -0.758  6.553   9.212   1.00 74.84  ? 205 WTO A C12   1 
HETATM 3331 C  C13   . WTO G 4 .   ? -0.498  7.679   9.991   1.00 83.15  ? 205 WTO A C13   1 
HETATM 3332 C  C14   . WTO G 4 .   ? -0.227  8.912   9.384   1.00 84.10  ? 205 WTO A C14   1 
HETATM 3333 C  C15   . WTO G 4 .   ? -0.742  6.675   7.840   1.00 75.56  ? 205 WTO A C15   1 
HETATM 3334 C  C16   . WTO G 4 .   ? -0.483  7.893   7.244   1.00 78.63  ? 205 WTO A C16   1 
HETATM 3335 C  C17   . WTO G 4 .   ? -0.196  9.023   7.991   0.99 85.06  ? 205 WTO A C17   1 
HETATM 3336 C  C21   . WTO G 4 .   ? -2.180  11.985  8.448   0.48 96.29  ? 205 WTO A C21   1 
HETATM 3337 C  C22   . WTO G 4 .   ? -3.159  10.968  7.778   0.86 97.16  ? 205 WTO A C22   1 
HETATM 3338 C  C24   . WTO G 4 .   ? -4.618  10.529  9.581   1.00 96.92  ? 205 WTO A C24   1 
HETATM 3339 C  C26   . WTO G 4 .   ? -2.478  13.213  8.154   0.91 98.37  ? 205 WTO A C26   1 
HETATM 3340 C  C27   . WTO G 4 .   ? -1.184  13.998  8.544   1.00 96.84  ? 205 WTO A C27   1 
HETATM 3341 C  C28   . WTO G 4 .   ? -0.040  12.955  8.452   0.97 96.01  ? 205 WTO A C28   1 
HETATM 3342 N  N11   . WTO G 4 .   ? -1.058  5.243   9.764   1.00 70.50  ? 205 WTO A N11   1 
HETATM 3343 N  N20   . WTO G 4 .   ? -0.600  11.858  8.011   0.42 93.61  ? 205 WTO A N20   1 
HETATM 3344 O  O19   . WTO G 4 .   ? 1.550   10.895  6.783   1.00 82.64  ? 205 WTO A O19   1 
HETATM 3345 O  O23   . WTO G 4 .   ? -4.483  10.910  8.237   0.74 100.69 ? 205 WTO A O23   1 
HETATM 3346 O  O25   . WTO G 4 .   ? -2.826  10.234  6.904   1.00 92.34  ? 205 WTO A O25   1 
HETATM 3347 O  O29   . WTO G 4 .   ? -0.372  10.576  5.746   1.00 84.40  ? 205 WTO A O29   1 
HETATM 3348 O  O30   . WTO G 4 .   ? -3.139  5.258   8.805   1.00 79.09  ? 205 WTO A O30   1 
HETATM 3349 S  S18   . WTO G 4 .   ? 0.143   10.602  7.119   0.24 88.83  ? 205 WTO A S18   1 
HETATM 3350 MG MG    . MG  H 5 .   ? 12.775  -6.387  -3.089  1.00 47.17  ? 206 MG  A MG    1 
HETATM 3351 P  PG    . GNP I 2 .   ? 22.958  4.864   24.492  1.00 46.83  ? 201 GNP B PG    1 
HETATM 3352 O  O1G   . GNP I 2 .   ? 22.504  5.782   23.379  1.00 49.20  ? 201 GNP B O1G   1 
HETATM 3353 O  O2G   . GNP I 2 .   ? 21.775  4.119   25.103  1.00 44.53  ? 201 GNP B O2G   1 
HETATM 3354 O  O3G   . GNP I 2 .   ? 24.007  3.821   24.009  1.00 49.21  ? 201 GNP B O3G   1 
HETATM 3355 N  N3B   . GNP I 2 .   ? 23.675  5.799   25.688  1.00 47.75  ? 201 GNP B N3B   1 
HETATM 3356 P  PB    . GNP I 2 .   ? 22.716  6.899   26.403  1.00 47.24  ? 201 GNP B PB    1 
HETATM 3357 O  O1B   . GNP I 2 .   ? 21.289  6.396   26.480  1.00 46.72  ? 201 GNP B O1B   1 
HETATM 3358 O  O2B   . GNP I 2 .   ? 22.779  8.224   25.686  1.00 44.24  ? 201 GNP B O2B   1 
HETATM 3359 O  O3A   . GNP I 2 .   ? 23.406  7.061   27.885  1.00 56.22  ? 201 GNP B O3A   1 
HETATM 3360 P  PA    . GNP I 2 .   ? 22.867  6.532   29.287  1.00 46.59  ? 201 GNP B PA    1 
HETATM 3361 O  O1A   . GNP I 2 .   ? 23.060  5.019   29.286  1.00 51.29  ? 201 GNP B O1A   1 
HETATM 3362 O  O2A   . GNP I 2 .   ? 21.498  7.045   29.534  1.00 43.19  ? 201 GNP B O2A   1 
HETATM 3363 O  "O5'" . GNP I 2 .   ? 24.029  7.110   30.157  1.00 48.48  ? 201 GNP B "O5'" 1 
HETATM 3364 C  "C5'" . GNP I 2 .   ? 25.403  6.808   29.834  1.00 48.25  ? 201 GNP B "C5'" 1 
HETATM 3365 C  "C4'" . GNP I 2 .   ? 26.200  6.572   31.091  1.00 53.59  ? 201 GNP B "C4'" 1 
HETATM 3366 O  "O4'" . GNP I 2 .   ? 26.409  7.825   31.774  1.00 53.57  ? 201 GNP B "O4'" 1 
HETATM 3367 C  "C3'" . GNP I 2 .   ? 25.580  5.629   32.119  1.00 51.22  ? 201 GNP B "C3'" 1 
HETATM 3368 O  "O3'" . GNP I 2 .   ? 26.628  4.916   32.763  1.00 47.95  ? 201 GNP B "O3'" 1 
HETATM 3369 C  "C2'" . GNP I 2 .   ? 24.835  6.587   33.053  1.00 48.45  ? 201 GNP B "C2'" 1 
HETATM 3370 O  "O2'" . GNP I 2 .   ? 24.807  6.097   34.387  1.00 59.27  ? 201 GNP B "O2'" 1 
HETATM 3371 C  "C1'" . GNP I 2 .   ? 25.730  7.830   33.019  1.00 52.99  ? 201 GNP B "C1'" 1 
HETATM 3372 N  N9    . GNP I 2 .   ? 24.987  9.093   33.114  1.00 52.75  ? 201 GNP B N9    1 
HETATM 3373 C  C8    . GNP I 2 .   ? 23.904  9.459   32.360  1.00 47.76  ? 201 GNP B C8    1 
HETATM 3374 N  N7    . GNP I 2 .   ? 23.457  10.660  32.642  1.00 49.35  ? 201 GNP B N7    1 
HETATM 3375 C  C5    . GNP I 2 .   ? 24.308  11.117  33.642  1.00 53.24  ? 201 GNP B C5    1 
HETATM 3376 C  C6    . GNP I 2 .   ? 24.329  12.357  34.385  1.00 51.00  ? 201 GNP B C6    1 
HETATM 3377 O  O6    . GNP I 2 .   ? 23.564  13.320  34.259  1.00 49.04  ? 201 GNP B O6    1 
HETATM 3378 N  N1    . GNP I 2 .   ? 25.354  12.387  35.313  1.00 51.82  ? 201 GNP B N1    1 
HETATM 3379 C  C2    . GNP I 2 .   ? 26.250  11.376  35.534  1.00 51.63  ? 201 GNP B C2    1 
HETATM 3380 N  N2    . GNP I 2 .   ? 27.184  11.590  36.465  1.00 55.43  ? 201 GNP B N2    1 
HETATM 3381 N  N3    . GNP I 2 .   ? 26.238  10.221  34.864  1.00 53.51  ? 201 GNP B N3    1 
HETATM 3382 C  C4    . GNP I 2 .   ? 25.256  10.159  33.943  1.00 54.10  ? 201 GNP B C4    1 
HETATM 3383 C  C1    . GOL J 3 .   ? 22.373  3.584   31.956  1.00 53.12  ? 202 GOL B C1    1 
HETATM 3384 O  O1    . GOL J 3 .   ? 22.226  2.894   30.759  1.00 48.01  ? 202 GOL B O1    1 
HETATM 3385 C  C2    . GOL J 3 .   ? 21.280  3.022   32.913  1.00 58.64  ? 202 GOL B C2    1 
HETATM 3386 O  O2    . GOL J 3 .   ? 21.314  1.619   32.997  1.00 61.61  ? 202 GOL B O2    1 
HETATM 3387 C  C3    . GOL J 3 .   ? 19.949  3.573   32.331  1.00 53.67  ? 202 GOL B C3    1 
HETATM 3388 O  O3    . GOL J 3 .   ? 18.915  2.796   32.844  1.00 55.27  ? 202 GOL B O3    1 
HETATM 3389 C  C08   . WTO K 4 .   ? 6.214   18.958  13.260  0.92 77.55  ? 203 WTO B C08   1 
HETATM 3390 C  C09   . WTO K 4 .   ? 5.513   17.596  13.158  0.57 73.29  ? 203 WTO B C09   1 
HETATM 3391 C  C10   . WTO K 4 .   ? 6.440   16.556  13.754  0.43 67.19  ? 203 WTO B C10   1 
HETATM 3392 C  C12   . WTO K 4 .   ? 5.089   14.144  13.683  0.87 65.45  ? 203 WTO B C12   1 
HETATM 3393 C  C13   . WTO K 4 .   ? 3.817   14.137  14.267  0.87 68.02  ? 203 WTO B C13   1 
HETATM 3394 C  C14   . WTO K 4 .   ? 2.891   13.108  14.000  1.00 70.98  ? 203 WTO B C14   1 
HETATM 3395 C  C15   . WTO K 4 .   ? 5.407   13.074  12.876  1.00 65.74  ? 203 WTO B C15   1 
HETATM 3396 C  C16   . WTO K 4 .   ? 4.506   12.054  12.603  0.91 71.50  ? 203 WTO B C16   1 
HETATM 3397 C  C17   . WTO K 4 .   ? 3.234   12.044  13.153  0.75 76.04  ? 203 WTO B C17   1 
HETATM 3398 C  C21   . WTO K 4 .   ? 3.201   8.099   11.484  0.73 78.84  ? 203 WTO B C21   1 
HETATM 3399 C  C22   . WTO K 4 .   ? 4.692   7.894   11.867  0.45 77.39  ? 203 WTO B C22   1 
HETATM 3400 C  C24   . WTO K 4 .   ? 5.810   6.057   12.923  1.00 67.62  ? 203 WTO B C24   1 
HETATM 3401 C  C26   . WTO K 4 .   ? 2.987   7.628   10.294  1.00 74.79  ? 203 WTO B C26   1 
HETATM 3402 C  C27   . WTO K 4 .   ? 3.110   8.851   9.336   0.99 76.81  ? 203 WTO B C27   1 
HETATM 3403 C  C28   . WTO K 4 .   ? 3.001   10.110  10.223  0.79 81.75  ? 203 WTO B C28   1 
HETATM 3404 N  N11   . WTO K 4 .   ? 6.172   15.119  13.930  0.27 66.72  ? 203 WTO B N11   1 
HETATM 3405 N  N20   . WTO K 4 .   ? 2.806   9.701   11.453  0.78 78.13  ? 203 WTO B N20   1 
HETATM 3406 O  O19   . WTO K 4 .   ? 0.745   11.048  12.419  1.00 81.05  ? 203 WTO B O19   1 
HETATM 3407 O  O23   . WTO K 4 .   ? 5.317   6.632   11.736  0.92 81.23  ? 203 WTO B O23   1 
HETATM 3408 O  O25   . WTO K 4 .   ? 5.304   8.829   12.266  0.78 72.64  ? 203 WTO B O25   1 
HETATM 3409 O  O29   . WTO K 4 .   ? 1.833   9.770   13.861  0.94 81.07  ? 203 WTO B O29   1 
HETATM 3410 O  O30   . WTO K 4 .   ? 7.492   16.991  14.098  0.85 62.89  ? 203 WTO B O30   1 
HETATM 3411 S  S18   . WTO K 4 .   ? 2.123   10.640  12.720  0.43 75.22  ? 203 WTO B S18   1 
HETATM 3412 MG MG    . MG  L 5 .   ? 20.203  4.550   25.773  1.00 43.54  ? 204 MG  B MG    1 
HETATM 3413 O  O     . HOH M 6 .   ? -1.866  -4.266  13.576  1.00 71.61  ? 301 HOH A O     1 
HETATM 3414 O  O     . HOH M 6 .   ? 10.357  12.027  -3.553  1.00 59.68  ? 302 HOH A O     1 
HETATM 3415 O  O     . HOH M 6 .   ? 7.568   -14.848 8.070   1.00 55.54  ? 303 HOH A O     1 
HETATM 3416 O  O     . HOH M 6 .   ? 9.445   -14.328 9.545   1.00 61.89  ? 304 HOH A O     1 
HETATM 3417 O  O     . HOH M 6 .   ? 14.247  -6.547  -4.180  1.00 39.88  ? 305 HOH A O     1 
HETATM 3418 O  O     . HOH M 6 .   ? 9.420   -24.558 -16.779 1.00 65.72  ? 306 HOH A O     1 
HETATM 3419 O  O     . HOH M 6 .   ? 8.895   5.533   -8.302  1.00 52.79  ? 307 HOH A O     1 
HETATM 3420 O  O     . HOH M 6 .   ? 11.388  -5.898  -1.676  1.00 45.25  ? 308 HOH A O     1 
HETATM 3421 O  O     . HOH M 6 .   ? 10.734  -6.492  -11.827 1.00 43.44  ? 309 HOH A O     1 
HETATM 3422 O  O     . HOH M 6 .   ? 17.523  -1.341  -1.894  1.00 40.00  ? 310 HOH A O     1 
HETATM 3423 O  O     . HOH M 6 .   ? 6.062   11.344  -9.334  1.00 61.25  ? 311 HOH A O     1 
HETATM 3424 O  O     . HOH M 6 .   ? 11.043  -17.490 -3.314  1.00 53.87  ? 312 HOH A O     1 
HETATM 3425 O  O     . HOH M 6 .   ? -14.995 7.362   -1.729  1.00 80.98  ? 313 HOH A O     1 
HETATM 3426 O  O     . HOH M 6 .   ? 1.118   -3.068  -15.318 1.00 50.98  ? 314 HOH A O     1 
HETATM 3427 O  O     . HOH M 6 .   ? -9.084  -6.366  3.944   1.00 66.81  ? 315 HOH A O     1 
HETATM 3428 O  O     . HOH M 6 .   ? -8.472  -7.517  8.073   1.00 68.68  ? 316 HOH A O     1 
HETATM 3429 O  O     . HOH M 6 .   ? 14.460  3.528   -6.003  1.00 48.92  ? 317 HOH A O     1 
HETATM 3430 O  O     . HOH M 6 .   ? 6.415   -8.911  16.838  1.00 57.96  ? 318 HOH A O     1 
HETATM 3431 O  O     . HOH M 6 .   ? 14.377  -0.595  -10.389 1.00 56.84  ? 319 HOH A O     1 
HETATM 3432 O  O     . HOH M 6 .   ? -9.898  -6.791  6.313   1.00 68.89  ? 320 HOH A O     1 
HETATM 3433 O  O     . HOH M 6 .   ? 24.127  13.933  3.120   1.00 53.90  ? 321 HOH A O     1 
HETATM 3434 O  O     . HOH M 6 .   ? 17.161  7.156   -7.800  1.00 56.27  ? 322 HOH A O     1 
HETATM 3435 O  O     . HOH M 6 .   ? 20.605  19.212  -4.189  1.00 61.27  ? 323 HOH A O     1 
HETATM 3436 O  O     . HOH N 6 .   ? 26.848  25.757  37.686  1.00 72.39  ? 301 HOH B O     1 
HETATM 3437 O  O     . HOH N 6 .   ? 5.407   1.415   30.161  1.00 79.93  ? 302 HOH B O     1 
HETATM 3438 O  O     . HOH N 6 .   ? 21.412  3.792   27.586  1.00 42.78  ? 303 HOH B O     1 
HETATM 3439 O  O     . HOH N 6 .   ? 19.819  5.945   24.452  1.00 45.94  ? 304 HOH B O     1 
HETATM 3440 O  O     . HOH N 6 .   ? 9.393   -3.398  25.536  1.00 44.83  ? 305 HOH B O     1 
HETATM 3441 O  O     . HOH N 6 .   ? 15.997  25.107  13.320  1.00 76.04  ? 306 HOH B O     1 
HETATM 3442 O  O     . HOH N 6 .   ? 27.648  -2.656  41.420  1.00 51.32  ? 307 HOH B O     1 
HETATM 3443 O  O     . HOH N 6 .   ? 0.095   8.511   15.533  1.00 65.93  ? 308 HOH B O     1 
HETATM 3444 O  O     . HOH N 6 .   ? -3.459  30.727  33.159  1.00 68.67  ? 309 HOH B O     1 
HETATM 3445 O  O     . HOH N 6 .   ? 27.187  23.308  35.261  1.00 72.31  ? 310 HOH B O     1 
HETATM 3446 O  O     . HOH N 6 .   ? -4.342  -2.988  20.943  1.00 55.62  ? 311 HOH B O     1 
HETATM 3447 O  O     . HOH N 6 .   ? 16.177  2.116   32.623  1.00 63.30  ? 312 HOH B O     1 
HETATM 3448 O  O     . HOH N 6 .   ? 28.883  4.107   23.840  1.00 44.65  ? 313 HOH B O     1 
HETATM 3449 O  O     . HOH N 6 .   ? 14.538  0.155   39.878  1.00 56.46  ? 314 HOH B O     1 
HETATM 3450 O  O     . HOH N 6 .   ? 25.923  11.712  13.731  1.00 61.77  ? 315 HOH B O     1 
HETATM 3451 O  O     . HOH N 6 .   ? -0.544  13.962  11.935  1.00 69.89  ? 316 HOH B O     1 
HETATM 3452 O  O     . HOH N 6 .   ? 28.055  8.358   36.827  1.00 57.14  ? 317 HOH B O     1 
HETATM 3453 O  O     . HOH N 6 .   ? 14.948  26.854  33.654  1.00 56.53  ? 318 HOH B O     1 
HETATM 3454 O  O     . HOH N 6 .   ? 21.328  26.396  31.577  1.00 46.20  ? 319 HOH B O     1 
HETATM 3455 O  O     . HOH N 6 .   ? 23.132  26.369  34.068  1.00 73.66  ? 320 HOH B O     1 
HETATM 3456 O  O     . HOH N 6 .   ? 28.672  8.646   17.076  1.00 55.45  ? 321 HOH B O     1 
HETATM 3457 O  O     . HOH N 6 .   ? 27.098  -1.695  27.170  1.00 47.66  ? 322 HOH B O     1 
HETATM 3458 O  O     . HOH N 6 .   ? 19.535  -4.312  26.852  1.00 54.09  ? 323 HOH B O     1 
HETATM 3459 O  O     . HOH N 6 .   ? 2.983   18.485  14.441  1.00 52.50  ? 324 HOH B O     1 
# 
