data_9F0S
# 
_entry.id   9F0S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9F0S         pdb_00009f0s 10.2210/pdb9f0s/pdb 
WWPDB D_1292137931 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-30 ? 
2 'Structure model' 1 1 2025-05-07 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F0S 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-17 
_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           N 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              ec.schulz@uke.de 
_pdbx_contact_author.name_first         Eike 
_pdbx_contact_author.name_last          Schulz 
_pdbx_contact_author.name_mi            Christian 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1685-8605 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bosman, R.'   1 0000-0003-2738-7682 
'Prester, A.'  2 0000-0002-9939-602X 
'Bartels, K.'  3 0000-0002-7980-1913 
'Gulyas, K.V.' 4 ?                   
'Erdelyi, M.'  5 0000-0003-0359-5970 
'Schulz, E.C.' 6 0000-0002-1685-8605 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                119 
_citation.page_last                 119 
_citation.title                     'Dynamically chiral phosphonic acid-type metallo-beta-lactamase inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01510-5 
_citation.pdbx_database_id_PubMed   40253435 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gulyas, K.V.'            1  ?                   
primary 'Zhou, L.'                2  ?                   
primary 'Salamonsen, D.'          3  ?                   
primary 'Prester, A.'             4  0000-0003-2738-7682 
primary 'Bartels, K.'             5  ?                   
primary 'Bosman, R.'              6  ?                   
primary 'Haffke, P.'              7  ?                   
primary 'Li, J.'                  8  ?                   
primary 'Tamasi, V.'              9  ?                   
primary 'Deufel, F.'              10 0000-0003-4910-3388 
primary 'Thoma, J.'               11 0000-0003-3584-8274 
primary 'Andersson Rasmussen, A.' 12 ?                   
primary 'Csala, M.'               13 0000-0002-3829-4361 
primary 'Schroder Leiros, H.K.'   14 0000-0002-2726-6322 
primary 'Xu, Z.'                  15 0000-0002-3063-8473 
primary 'Widersten, M.'           16 0000-0002-3203-3793 
primary 'Rohde, H.'               17 0000-0001-8587-4433 
primary 'Schulz, E.C.'            18 0000-0002-1685-8605 
primary 'Zhu, W.'                 19 0000-0001-6699-5299 
primary 'Erdelyi, M.'             20 0000-0003-0359-5970 
# 
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 'Metallo-beta-lactamase type 2'                                                  27351.303 2   3.5.2.6 ? ? 
;The gene sequence coding for residues Val25 to Glu300 of VIM-2 was isolated from Pseudomonas aeruginosa strain 301 5473. Protein was purified as a construct with His6-tag (residues 1-7) and TEV protease cleavage site (residues 8-14).
;
2 non-polymer syn 'FORMIC ACID'                                                                    46.025    4   ?       ? ? ? 
3 non-polymer syn '[(~{R})-(2-hydroxyphenyl)-(2-thiophen-3-ylethanoylamino)methyl]phosphonic acid' 327.293   2   ?       ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                       65.409    6   ?       ? ? ? 
5 water       nat water                                                                            18.015    621 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'B2 metallo-beta-lactamase,Metallo-beta-lactamase type II' 
# 
_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       
;MHHHHHHENLYFQGVDSSGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNT
AALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVEL
FYPGAAHSTDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYPEAQFVIPGHGLPGGLDLLKHT
TNVVKAHTNRSVVE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHENLYFQGVDSSGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNT
AALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVEL
FYPGAAHSTDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYPEAQFVIPGHGLPGGLDLLKHT
TNVVKAHTNRSVVE
;
_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 'FORMIC ACID'                                                                    FMT   
3 '[(~{R})-(2-hydroxyphenyl)-(2-thiophen-3-ylethanoylamino)methyl]phosphonic acid' A1H8U 
4 'ZINC ION'                                                                       ZN    
5 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLU n 
1 9   ASN n 
1 10  LEU n 
1 11  TYR n 
1 12  PHE n 
1 13  GLN n 
1 14  GLY n 
1 15  VAL n 
1 16  ASP n 
1 17  SER n 
1 18  SER n 
1 19  GLY n 
1 20  GLU n 
1 21  TYR n 
1 22  PRO n 
1 23  THR n 
1 24  VAL n 
1 25  SER n 
1 26  GLU n 
1 27  ILE n 
1 28  PRO n 
1 29  VAL n 
1 30  GLY n 
1 31  GLU n 
1 32  VAL n 
1 33  ARG n 
1 34  LEU n 
1 35  TYR n 
1 36  GLN n 
1 37  ILE n 
1 38  ALA n 
1 39  ASP n 
1 40  GLY n 
1 41  VAL n 
1 42  TRP n 
1 43  SER n 
1 44  HIS n 
1 45  ILE n 
1 46  ALA n 
1 47  THR n 
1 48  GLN n 
1 49  SER n 
1 50  PHE n 
1 51  ASP n 
1 52  GLY n 
1 53  ALA n 
1 54  VAL n 
1 55  TYR n 
1 56  PRO n 
1 57  SER n 
1 58  ASN n 
1 59  GLY n 
1 60  LEU n 
1 61  ILE n 
1 62  VAL n 
1 63  ARG n 
1 64  ASP n 
1 65  GLY n 
1 66  ASP n 
1 67  GLU n 
1 68  LEU n 
1 69  LEU n 
1 70  LEU n 
1 71  ILE n 
1 72  ASP n 
1 73  THR n 
1 74  ALA n 
1 75  TRP n 
1 76  GLY n 
1 77  ALA n 
1 78  LYS n 
1 79  ASN n 
1 80  THR n 
1 81  ALA n 
1 82  ALA n 
1 83  LEU n 
1 84  LEU n 
1 85  ALA n 
1 86  GLU n 
1 87  ILE n 
1 88  GLU n 
1 89  LYS n 
1 90  GLN n 
1 91  ILE n 
1 92  GLY n 
1 93  LEU n 
1 94  PRO n 
1 95  VAL n 
1 96  THR n 
1 97  ARG n 
1 98  ALA n 
1 99  VAL n 
1 100 SER n 
1 101 THR n 
1 102 HIS n 
1 103 PHE n 
1 104 HIS n 
1 105 ASP n 
1 106 ASP n 
1 107 ARG n 
1 108 VAL n 
1 109 GLY n 
1 110 GLY n 
1 111 VAL n 
1 112 ASP n 
1 113 VAL n 
1 114 LEU n 
1 115 ARG n 
1 116 ALA n 
1 117 ALA n 
1 118 GLY n 
1 119 VAL n 
1 120 ALA n 
1 121 THR n 
1 122 TYR n 
1 123 ALA n 
1 124 SER n 
1 125 PRO n 
1 126 SER n 
1 127 THR n 
1 128 ARG n 
1 129 ARG n 
1 130 LEU n 
1 131 ALA n 
1 132 GLU n 
1 133 VAL n 
1 134 GLU n 
1 135 GLY n 
1 136 ASN n 
1 137 GLU n 
1 138 ILE n 
1 139 PRO n 
1 140 THR n 
1 141 HIS n 
1 142 SER n 
1 143 LEU n 
1 144 GLU n 
1 145 GLY n 
1 146 LEU n 
1 147 SER n 
1 148 SER n 
1 149 SER n 
1 150 GLY n 
1 151 ASP n 
1 152 ALA n 
1 153 VAL n 
1 154 ARG n 
1 155 PHE n 
1 156 GLY n 
1 157 PRO n 
1 158 VAL n 
1 159 GLU n 
1 160 LEU n 
1 161 PHE n 
1 162 TYR n 
1 163 PRO n 
1 164 GLY n 
1 165 ALA n 
1 166 ALA n 
1 167 HIS n 
1 168 SER n 
1 169 THR n 
1 170 ASP n 
1 171 ASN n 
1 172 LEU n 
1 173 VAL n 
1 174 VAL n 
1 175 TYR n 
1 176 VAL n 
1 177 PRO n 
1 178 SER n 
1 179 ALA n 
1 180 SER n 
1 181 VAL n 
1 182 LEU n 
1 183 TYR n 
1 184 GLY n 
1 185 GLY n 
1 186 CYS n 
1 187 ALA n 
1 188 ILE n 
1 189 TYR n 
1 190 GLU n 
1 191 LEU n 
1 192 SER n 
1 193 ARG n 
1 194 THR n 
1 195 SER n 
1 196 ALA n 
1 197 GLY n 
1 198 ASN n 
1 199 VAL n 
1 200 ALA n 
1 201 ASP n 
1 202 ALA n 
1 203 ASP n 
1 204 LEU n 
1 205 ALA n 
1 206 GLU n 
1 207 TRP n 
1 208 PRO n 
1 209 THR n 
1 210 SER n 
1 211 ILE n 
1 212 GLU n 
1 213 ARG n 
1 214 ILE n 
1 215 GLN n 
1 216 GLN n 
1 217 HIS n 
1 218 TYR n 
1 219 PRO n 
1 220 GLU n 
1 221 ALA n 
1 222 GLN n 
1 223 PHE n 
1 224 VAL n 
1 225 ILE n 
1 226 PRO n 
1 227 GLY n 
1 228 HIS n 
1 229 GLY n 
1 230 LEU n 
1 231 PRO n 
1 232 GLY n 
1 233 GLY n 
1 234 LEU n 
1 235 ASP n 
1 236 LEU n 
1 237 LEU n 
1 238 LYS n 
1 239 HIS n 
1 240 THR n 
1 241 THR n 
1 242 ASN n 
1 243 VAL n 
1 244 VAL n 
1 245 LYS n 
1 246 ALA n 
1 247 HIS n 
1 248 THR n 
1 249 ASN n 
1 250 ARG n 
1 251 SER n 
1 252 VAL n 
1 253 VAL n 
1 254 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   254 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 blaVIM 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    301-5473 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
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 
A1H8U non-polymer         . '[(~{R})-(2-hydroxyphenyl)-(2-thiophen-3-ylethanoylamino)methyl]phosphonic acid' ? 'C13 H14 N O5 P S' 
327.293 
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 
FMT   non-polymer         . 'FORMIC ACID'                                                                    ? 'C H2 O2'          
46.025  
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'     
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'       
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'       
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1'   
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'             
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'      
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'      
131.173 
LYS   'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1'   
147.195 
MET   'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'    
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'      
165.189 
PRO   'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'       
115.130 
SER   'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'       
105.093 
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 
ZN    non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'             
65.409  
# 
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   MET 1   13  ?   ?   ?   A . n 
A 1 2   HIS 2   14  ?   ?   ?   A . n 
A 1 3   HIS 3   15  ?   ?   ?   A . n 
A 1 4   HIS 4   16  ?   ?   ?   A . n 
A 1 5   HIS 5   17  ?   ?   ?   A . n 
A 1 6   HIS 6   18  ?   ?   ?   A . n 
A 1 7   HIS 7   19  ?   ?   ?   A . n 
A 1 8   GLU 8   20  ?   ?   ?   A . n 
A 1 9   ASN 9   21  ?   ?   ?   A . n 
A 1 10  LEU 10  22  ?   ?   ?   A . n 
A 1 11  TYR 11  23  ?   ?   ?   A . n 
A 1 12  PHE 12  24  ?   ?   ?   A . n 
A 1 13  GLN 13  25  ?   ?   ?   A . n 
A 1 14  GLY 14  26  ?   ?   ?   A . n 
A 1 15  VAL 15  27  ?   ?   ?   A . n 
A 1 16  ASP 16  28  ?   ?   ?   A . n 
A 1 17  SER 17  29  ?   ?   ?   A . n 
A 1 18  SER 18  30  ?   ?   ?   A . n 
A 1 19  GLY 19  31  ?   ?   ?   A . n 
A 1 20  GLU 20  32  32  GLU GLU A . n 
A 1 21  TYR 21  33  33  TYR TYR A . n 
A 1 22  PRO 22  34  34  PRO PRO A . n 
A 1 23  THR 23  35  35  THR THR A . n 
A 1 24  VAL 24  36  36  VAL VAL A . n 
A 1 25  SER 25  37  37  SER SER A . n 
A 1 26  GLU 26  38  38  GLU GLU A . n 
A 1 27  ILE 27  39  39  ILE ILE A . n 
A 1 28  PRO 28  40  40  PRO PRO A . n 
A 1 29  VAL 29  41  41  VAL VAL A . n 
A 1 30  GLY 30  42  42  GLY GLY A . n 
A 1 31  GLU 31  43  43  GLU GLU A . n 
A 1 32  VAL 32  44  44  VAL VAL A . n 
A 1 33  ARG 33  45  45  ARG ARG A . n 
A 1 34  LEU 34  46  46  LEU LEU A . n 
A 1 35  TYR 35  47  47  TYR TYR A . n 
A 1 36  GLN 36  48  48  GLN GLN A . n 
A 1 37  ILE 37  49  49  ILE ILE A . n 
A 1 38  ALA 38  50  50  ALA ALA A . n 
A 1 39  ASP 39  51  51  ASP ASP A . n 
A 1 40  GLY 40  52  52  GLY GLY A . n 
A 1 41  VAL 41  53  53  VAL VAL A . n 
A 1 42  TRP 42  54  54  TRP TRP A . n 
A 1 43  SER 43  55  55  SER SER A . n 
A 1 44  HIS 44  56  56  HIS HIS A . n 
A 1 45  ILE 45  57  57  ILE ILE A . n 
A 1 46  ALA 46  58  58  ALA ALA A . n 
A 1 47  THR 47  59  59  THR THR A . n 
A 1 48  GLN 48  60  60  GLN GLN A . n 
A 1 49  SER 49  61  61  SER SER A . n 
A 1 50  PHE 50  62  62  PHE PHE A . n 
A 1 51  ASP 51  63  63  ASP ASP A . n 
A 1 52  GLY 52  64  64  GLY GLY A . n 
A 1 53  ALA 53  65  65  ALA ALA A . n 
A 1 54  VAL 54  66  66  VAL VAL A . n 
A 1 55  TYR 55  67  67  TYR TYR A . n 
A 1 56  PRO 56  68  68  PRO PRO A . n 
A 1 57  SER 57  69  69  SER SER A . n 
A 1 58  ASN 58  70  70  ASN ASN A . n 
A 1 59  GLY 59  71  71  GLY GLY A . n 
A 1 60  LEU 60  72  72  LEU LEU A . n 
A 1 61  ILE 61  73  73  ILE ILE A . n 
A 1 62  VAL 62  74  74  VAL VAL A . n 
A 1 63  ARG 63  75  75  ARG ARG A . n 
A 1 64  ASP 64  76  76  ASP ASP A . n 
A 1 65  GLY 65  77  77  GLY GLY A . n 
A 1 66  ASP 66  78  78  ASP ASP A . n 
A 1 67  GLU 67  79  79  GLU GLU A . n 
A 1 68  LEU 68  80  80  LEU LEU A . n 
A 1 69  LEU 69  81  81  LEU LEU A . n 
A 1 70  LEU 70  82  82  LEU LEU A . n 
A 1 71  ILE 71  83  83  ILE ILE A . n 
A 1 72  ASP 72  84  84  ASP ASP A . n 
A 1 73  THR 73  85  85  THR THR A . n 
A 1 74  ALA 74  86  86  ALA ALA A . n 
A 1 75  TRP 75  87  87  TRP TRP A . n 
A 1 76  GLY 76  88  88  GLY GLY A . n 
A 1 77  ALA 77  89  89  ALA ALA A . n 
A 1 78  LYS 78  90  90  LYS LYS A . n 
A 1 79  ASN 79  91  91  ASN ASN A . n 
A 1 80  THR 80  92  92  THR THR A . n 
A 1 81  ALA 81  93  93  ALA ALA A . n 
A 1 82  ALA 82  94  94  ALA ALA A . n 
A 1 83  LEU 83  95  95  LEU LEU A . n 
A 1 84  LEU 84  96  96  LEU LEU A . n 
A 1 85  ALA 85  97  97  ALA ALA A . n 
A 1 86  GLU 86  98  98  GLU GLU A . n 
A 1 87  ILE 87  99  99  ILE ILE A . n 
A 1 88  GLU 88  100 100 GLU GLU A . n 
A 1 89  LYS 89  101 101 LYS LYS A . n 
A 1 90  GLN 90  102 102 GLN GLN A . n 
A 1 91  ILE 91  103 103 ILE ILE A . n 
A 1 92  GLY 92  104 104 GLY GLY A . n 
A 1 93  LEU 93  105 105 LEU LEU A . n 
A 1 94  PRO 94  106 106 PRO PRO A . n 
A 1 95  VAL 95  107 107 VAL VAL A . n 
A 1 96  THR 96  108 108 THR THR A . n 
A 1 97  ARG 97  109 109 ARG ARG A . n 
A 1 98  ALA 98  110 110 ALA ALA A . n 
A 1 99  VAL 99  111 111 VAL VAL A . n 
A 1 100 SER 100 112 112 SER SER A . n 
A 1 101 THR 101 113 113 THR THR A . n 
A 1 102 HIS 102 114 114 HIS HIS A . n 
A 1 103 PHE 103 115 115 PHE PHE A . n 
A 1 104 HIS 104 116 116 HIS HIS A . n 
A 1 105 ASP 105 117 117 ASP ASP A . n 
A 1 106 ASP 106 118 118 ASP ASP A . n 
A 1 107 ARG 107 119 119 ARG ARG A . n 
A 1 108 VAL 108 120 120 VAL VAL A . n 
A 1 109 GLY 109 121 121 GLY GLY A . n 
A 1 110 GLY 110 122 122 GLY GLY A . n 
A 1 111 VAL 111 123 123 VAL VAL A . n 
A 1 112 ASP 112 124 124 ASP ASP A . n 
A 1 113 VAL 113 125 125 VAL VAL A . n 
A 1 114 LEU 114 126 126 LEU LEU A . n 
A 1 115 ARG 115 127 127 ARG ARG A . n 
A 1 116 ALA 116 128 128 ALA ALA A . n 
A 1 117 ALA 117 129 129 ALA ALA A . n 
A 1 118 GLY 118 130 130 GLY GLY A . n 
A 1 119 VAL 119 131 131 VAL VAL A . n 
A 1 120 ALA 120 132 132 ALA ALA A . n 
A 1 121 THR 121 133 133 THR THR A . n 
A 1 122 TYR 122 134 134 TYR TYR A . n 
A 1 123 ALA 123 135 135 ALA ALA A . n 
A 1 124 SER 124 136 136 SER SER A . n 
A 1 125 PRO 125 137 137 PRO PRO A . n 
A 1 126 SER 126 138 138 SER SER A . n 
A 1 127 THR 127 139 139 THR THR A . n 
A 1 128 ARG 128 140 140 ARG ARG A . n 
A 1 129 ARG 129 141 141 ARG ARG A . n 
A 1 130 LEU 130 142 142 LEU LEU A . n 
A 1 131 ALA 131 143 143 ALA ALA A . n 
A 1 132 GLU 132 144 144 GLU GLU A . n 
A 1 133 VAL 133 145 145 VAL VAL A . n 
A 1 134 GLU 134 146 146 GLU GLU A . n 
A 1 135 GLY 135 147 147 GLY GLY A . n 
A 1 136 ASN 136 148 148 ASN ASN A . n 
A 1 137 GLU 137 149 149 GLU GLU A . n 
A 1 138 ILE 138 150 150 ILE ILE A . n 
A 1 139 PRO 139 151 151 PRO PRO A . n 
A 1 140 THR 140 152 152 THR THR A . n 
A 1 141 HIS 141 153 153 HIS HIS A . n 
A 1 142 SER 142 154 154 SER SER A . n 
A 1 143 LEU 143 155 155 LEU LEU A . n 
A 1 144 GLU 144 156 156 GLU GLU A . n 
A 1 145 GLY 145 157 157 GLY GLY A . n 
A 1 146 LEU 146 158 158 LEU LEU A . n 
A 1 147 SER 147 159 159 SER SER A . n 
A 1 148 SER 148 160 160 SER SER A . n 
A 1 149 SER 149 161 161 SER SER A . n 
A 1 150 GLY 150 162 162 GLY GLY A . n 
A 1 151 ASP 151 163 163 ASP ASP A . n 
A 1 152 ALA 152 164 164 ALA ALA A . n 
A 1 153 VAL 153 165 165 VAL VAL A . n 
A 1 154 ARG 154 166 166 ARG ARG A . n 
A 1 155 PHE 155 167 167 PHE PHE A . n 
A 1 156 GLY 156 168 168 GLY GLY A . n 
A 1 157 PRO 157 169 169 PRO PRO A . n 
A 1 158 VAL 158 170 170 VAL VAL A . n 
A 1 159 GLU 159 171 171 GLU GLU A . n 
A 1 160 LEU 160 172 172 LEU LEU A . n 
A 1 161 PHE 161 173 173 PHE PHE A . n 
A 1 162 TYR 162 174 174 TYR TYR A . n 
A 1 163 PRO 163 175 175 PRO PRO A . n 
A 1 164 GLY 164 176 176 GLY GLY A . n 
A 1 165 ALA 165 177 177 ALA ALA A . n 
A 1 166 ALA 166 178 178 ALA ALA A . n 
A 1 167 HIS 167 179 179 HIS HIS A . n 
A 1 168 SER 168 180 180 SER SER A . n 
A 1 169 THR 169 181 181 THR THR A . n 
A 1 170 ASP 170 182 182 ASP ASP A . n 
A 1 171 ASN 171 183 183 ASN ASN A . n 
A 1 172 LEU 172 184 184 LEU LEU A . n 
A 1 173 VAL 173 185 185 VAL VAL A . n 
A 1 174 VAL 174 186 186 VAL VAL A . n 
A 1 175 TYR 175 187 187 TYR TYR A . n 
A 1 176 VAL 176 188 188 VAL VAL A . n 
A 1 177 PRO 177 189 189 PRO PRO A . n 
A 1 178 SER 178 190 190 SER SER A . n 
A 1 179 ALA 179 191 191 ALA ALA A . n 
A 1 180 SER 180 192 192 SER SER A . n 
A 1 181 VAL 181 193 193 VAL VAL A . n 
A 1 182 LEU 182 194 194 LEU LEU A . n 
A 1 183 TYR 183 195 195 TYR TYR A . n 
A 1 184 GLY 184 196 196 GLY GLY A . n 
A 1 185 GLY 185 197 197 GLY GLY A . n 
A 1 186 CYS 186 198 198 CYS CYS A . n 
A 1 187 ALA 187 199 199 ALA ALA A . n 
A 1 188 ILE 188 200 200 ILE ILE A . n 
A 1 189 TYR 189 201 201 TYR TYR A . n 
A 1 190 GLU 190 202 202 GLU GLU A . n 
A 1 191 LEU 191 203 203 LEU LEU A . n 
A 1 192 SER 192 204 204 SER SER A . n 
A 1 193 ARG 193 205 205 ARG ARG A . n 
A 1 194 THR 194 206 206 THR THR A . n 
A 1 195 SER 195 207 207 SER SER A . n 
A 1 196 ALA 196 208 208 ALA ALA A . n 
A 1 197 GLY 197 209 209 GLY GLY A . n 
A 1 198 ASN 198 210 210 ASN ASN A . n 
A 1 199 VAL 199 211 211 VAL VAL A . n 
A 1 200 ALA 200 212 212 ALA ALA A . n 
A 1 201 ASP 201 213 213 ASP ASP A . n 
A 1 202 ALA 202 214 214 ALA ALA A . n 
A 1 203 ASP 203 215 215 ASP ASP A . n 
A 1 204 LEU 204 216 216 LEU LEU A . n 
A 1 205 ALA 205 217 217 ALA ALA A . n 
A 1 206 GLU 206 218 218 GLU GLU A . n 
A 1 207 TRP 207 219 219 TRP TRP A . n 
A 1 208 PRO 208 220 220 PRO PRO A . n 
A 1 209 THR 209 221 221 THR THR A . n 
A 1 210 SER 210 222 222 SER SER A . n 
A 1 211 ILE 211 223 223 ILE ILE A . n 
A 1 212 GLU 212 224 224 GLU GLU A . n 
A 1 213 ARG 213 225 225 ARG ARG A . n 
A 1 214 ILE 214 226 226 ILE ILE A . n 
A 1 215 GLN 215 227 227 GLN GLN A . n 
A 1 216 GLN 216 228 228 GLN GLN A . n 
A 1 217 HIS 217 229 229 HIS HIS A . n 
A 1 218 TYR 218 230 230 TYR TYR A . n 
A 1 219 PRO 219 231 231 PRO PRO A . n 
A 1 220 GLU 220 232 232 GLU GLU A . n 
A 1 221 ALA 221 233 233 ALA ALA A . n 
A 1 222 GLN 222 234 234 GLN GLN A . n 
A 1 223 PHE 223 235 235 PHE PHE A . n 
A 1 224 VAL 224 236 236 VAL VAL A . n 
A 1 225 ILE 225 237 237 ILE ILE A . n 
A 1 226 PRO 226 238 238 PRO PRO A . n 
A 1 227 GLY 227 239 239 GLY GLY A . n 
A 1 228 HIS 228 240 240 HIS HIS A . n 
A 1 229 GLY 229 241 241 GLY GLY A . n 
A 1 230 LEU 230 242 242 LEU LEU A . n 
A 1 231 PRO 231 243 243 PRO PRO A . n 
A 1 232 GLY 232 244 244 GLY GLY A . n 
A 1 233 GLY 233 245 245 GLY GLY A . n 
A 1 234 LEU 234 246 246 LEU LEU A . n 
A 1 235 ASP 235 247 247 ASP ASP A . n 
A 1 236 LEU 236 248 248 LEU LEU A . n 
A 1 237 LEU 237 249 249 LEU LEU A . n 
A 1 238 LYS 238 250 250 LYS LYS A . n 
A 1 239 HIS 239 251 251 HIS HIS A . n 
A 1 240 THR 240 252 252 THR THR A . n 
A 1 241 THR 241 253 253 THR THR A . n 
A 1 242 ASN 242 254 254 ASN ASN A . n 
A 1 243 VAL 243 255 255 VAL VAL A . n 
A 1 244 VAL 244 256 256 VAL VAL A . n 
A 1 245 LYS 245 257 257 LYS LYS A . n 
A 1 246 ALA 246 258 258 ALA ALA A . n 
A 1 247 HIS 247 259 259 HIS HIS A . n 
A 1 248 THR 248 260 260 THR THR A . n 
A 1 249 ASN 249 261 261 ASN ASN A . n 
A 1 250 ARG 250 262 262 ARG ARG A . n 
A 1 251 SER 251 263 ?   ?   ?   A . n 
A 1 252 VAL 252 264 ?   ?   ?   A . n 
A 1 253 VAL 253 265 ?   ?   ?   A . n 
A 1 254 GLU 254 266 ?   ?   ?   A . n 
B 1 1   MET 1   13  ?   ?   ?   B . n 
B 1 2   HIS 2   14  ?   ?   ?   B . n 
B 1 3   HIS 3   15  ?   ?   ?   B . n 
B 1 4   HIS 4   16  ?   ?   ?   B . n 
B 1 5   HIS 5   17  ?   ?   ?   B . n 
B 1 6   HIS 6   18  ?   ?   ?   B . n 
B 1 7   HIS 7   19  ?   ?   ?   B . n 
B 1 8   GLU 8   20  ?   ?   ?   B . n 
B 1 9   ASN 9   21  ?   ?   ?   B . n 
B 1 10  LEU 10  22  ?   ?   ?   B . n 
B 1 11  TYR 11  23  ?   ?   ?   B . n 
B 1 12  PHE 12  24  ?   ?   ?   B . n 
B 1 13  GLN 13  25  ?   ?   ?   B . n 
B 1 14  GLY 14  26  ?   ?   ?   B . n 
B 1 15  VAL 15  27  ?   ?   ?   B . n 
B 1 16  ASP 16  28  ?   ?   ?   B . n 
B 1 17  SER 17  29  ?   ?   ?   B . n 
B 1 18  SER 18  30  ?   ?   ?   B . n 
B 1 19  GLY 19  31  ?   ?   ?   B . n 
B 1 20  GLU 20  32  32  GLU GLU B . n 
B 1 21  TYR 21  33  33  TYR TYR B . n 
B 1 22  PRO 22  34  34  PRO PRO B . n 
B 1 23  THR 23  35  35  THR THR B . n 
B 1 24  VAL 24  36  36  VAL VAL B . n 
B 1 25  SER 25  37  37  SER SER B . n 
B 1 26  GLU 26  38  38  GLU GLU B . n 
B 1 27  ILE 27  39  39  ILE ILE B . n 
B 1 28  PRO 28  40  40  PRO PRO B . n 
B 1 29  VAL 29  41  41  VAL VAL B . n 
B 1 30  GLY 30  42  42  GLY GLY B . n 
B 1 31  GLU 31  43  43  GLU GLU B . n 
B 1 32  VAL 32  44  44  VAL VAL B . n 
B 1 33  ARG 33  45  45  ARG ARG B . n 
B 1 34  LEU 34  46  46  LEU LEU B . n 
B 1 35  TYR 35  47  47  TYR TYR B . n 
B 1 36  GLN 36  48  48  GLN GLN B . n 
B 1 37  ILE 37  49  49  ILE ILE B . n 
B 1 38  ALA 38  50  50  ALA ALA B . n 
B 1 39  ASP 39  51  51  ASP ASP B . n 
B 1 40  GLY 40  52  52  GLY GLY B . n 
B 1 41  VAL 41  53  53  VAL VAL B . n 
B 1 42  TRP 42  54  54  TRP TRP B . n 
B 1 43  SER 43  55  55  SER SER B . n 
B 1 44  HIS 44  56  56  HIS HIS B . n 
B 1 45  ILE 45  57  57  ILE ILE B . n 
B 1 46  ALA 46  58  58  ALA ALA B . n 
B 1 47  THR 47  59  59  THR THR B . n 
B 1 48  GLN 48  60  60  GLN GLN B . n 
B 1 49  SER 49  61  61  SER SER B . n 
B 1 50  PHE 50  62  62  PHE PHE B . n 
B 1 51  ASP 51  63  63  ASP ASP B . n 
B 1 52  GLY 52  64  64  GLY GLY B . n 
B 1 53  ALA 53  65  65  ALA ALA B . n 
B 1 54  VAL 54  66  66  VAL VAL B . n 
B 1 55  TYR 55  67  67  TYR TYR B . n 
B 1 56  PRO 56  68  68  PRO PRO B . n 
B 1 57  SER 57  69  69  SER SER B . n 
B 1 58  ASN 58  70  70  ASN ASN B . n 
B 1 59  GLY 59  71  71  GLY GLY B . n 
B 1 60  LEU 60  72  72  LEU LEU B . n 
B 1 61  ILE 61  73  73  ILE ILE B . n 
B 1 62  VAL 62  74  74  VAL VAL B . n 
B 1 63  ARG 63  75  75  ARG ARG B . n 
B 1 64  ASP 64  76  76  ASP ASP B . n 
B 1 65  GLY 65  77  77  GLY GLY B . n 
B 1 66  ASP 66  78  78  ASP ASP B . n 
B 1 67  GLU 67  79  79  GLU GLU B . n 
B 1 68  LEU 68  80  80  LEU LEU B . n 
B 1 69  LEU 69  81  81  LEU LEU B . n 
B 1 70  LEU 70  82  82  LEU LEU B . n 
B 1 71  ILE 71  83  83  ILE ILE B . n 
B 1 72  ASP 72  84  84  ASP ASP B . n 
B 1 73  THR 73  85  85  THR THR B . n 
B 1 74  ALA 74  86  86  ALA ALA B . n 
B 1 75  TRP 75  87  87  TRP TRP B . n 
B 1 76  GLY 76  88  88  GLY GLY B . n 
B 1 77  ALA 77  89  89  ALA ALA B . n 
B 1 78  LYS 78  90  90  LYS LYS B . n 
B 1 79  ASN 79  91  91  ASN ASN B . n 
B 1 80  THR 80  92  92  THR THR B . n 
B 1 81  ALA 81  93  93  ALA ALA B . n 
B 1 82  ALA 82  94  94  ALA ALA B . n 
B 1 83  LEU 83  95  95  LEU LEU B . n 
B 1 84  LEU 84  96  96  LEU LEU B . n 
B 1 85  ALA 85  97  97  ALA ALA B . n 
B 1 86  GLU 86  98  98  GLU GLU B . n 
B 1 87  ILE 87  99  99  ILE ILE B . n 
B 1 88  GLU 88  100 100 GLU GLU B . n 
B 1 89  LYS 89  101 101 LYS LYS B . n 
B 1 90  GLN 90  102 102 GLN GLN B . n 
B 1 91  ILE 91  103 103 ILE ILE B . n 
B 1 92  GLY 92  104 104 GLY GLY B . n 
B 1 93  LEU 93  105 105 LEU LEU B . n 
B 1 94  PRO 94  106 106 PRO PRO B . n 
B 1 95  VAL 95  107 107 VAL VAL B . n 
B 1 96  THR 96  108 108 THR THR B . n 
B 1 97  ARG 97  109 109 ARG ARG B . n 
B 1 98  ALA 98  110 110 ALA ALA B . n 
B 1 99  VAL 99  111 111 VAL VAL B . n 
B 1 100 SER 100 112 112 SER SER B . n 
B 1 101 THR 101 113 113 THR THR B . n 
B 1 102 HIS 102 114 114 HIS HIS B . n 
B 1 103 PHE 103 115 115 PHE PHE B . n 
B 1 104 HIS 104 116 116 HIS HIS B . n 
B 1 105 ASP 105 117 117 ASP ASP B . n 
B 1 106 ASP 106 118 118 ASP ASP B . n 
B 1 107 ARG 107 119 119 ARG ARG B . n 
B 1 108 VAL 108 120 120 VAL VAL B . n 
B 1 109 GLY 109 121 121 GLY GLY B . n 
B 1 110 GLY 110 122 122 GLY GLY B . n 
B 1 111 VAL 111 123 123 VAL VAL B . n 
B 1 112 ASP 112 124 124 ASP ASP B . n 
B 1 113 VAL 113 125 125 VAL VAL B . n 
B 1 114 LEU 114 126 126 LEU LEU B . n 
B 1 115 ARG 115 127 127 ARG ARG B . n 
B 1 116 ALA 116 128 128 ALA ALA B . n 
B 1 117 ALA 117 129 129 ALA ALA B . n 
B 1 118 GLY 118 130 130 GLY GLY B . n 
B 1 119 VAL 119 131 131 VAL VAL B . n 
B 1 120 ALA 120 132 132 ALA ALA B . n 
B 1 121 THR 121 133 133 THR THR B . n 
B 1 122 TYR 122 134 134 TYR TYR B . n 
B 1 123 ALA 123 135 135 ALA ALA B . n 
B 1 124 SER 124 136 136 SER SER B . n 
B 1 125 PRO 125 137 137 PRO PRO B . n 
B 1 126 SER 126 138 138 SER SER B . n 
B 1 127 THR 127 139 139 THR THR B . n 
B 1 128 ARG 128 140 140 ARG ARG B . n 
B 1 129 ARG 129 141 141 ARG ARG B . n 
B 1 130 LEU 130 142 142 LEU LEU B . n 
B 1 131 ALA 131 143 143 ALA ALA B . n 
B 1 132 GLU 132 144 144 GLU GLU B . n 
B 1 133 VAL 133 145 145 VAL VAL B . n 
B 1 134 GLU 134 146 146 GLU GLU B . n 
B 1 135 GLY 135 147 147 GLY GLY B . n 
B 1 136 ASN 136 148 148 ASN ASN B . n 
B 1 137 GLU 137 149 149 GLU GLU B . n 
B 1 138 ILE 138 150 150 ILE ILE B . n 
B 1 139 PRO 139 151 151 PRO PRO B . n 
B 1 140 THR 140 152 152 THR THR B . n 
B 1 141 HIS 141 153 153 HIS HIS B . n 
B 1 142 SER 142 154 154 SER SER B . n 
B 1 143 LEU 143 155 155 LEU LEU B . n 
B 1 144 GLU 144 156 156 GLU GLU B . n 
B 1 145 GLY 145 157 157 GLY GLY B . n 
B 1 146 LEU 146 158 158 LEU LEU B . n 
B 1 147 SER 147 159 159 SER SER B . n 
B 1 148 SER 148 160 160 SER SER B . n 
B 1 149 SER 149 161 161 SER SER B . n 
B 1 150 GLY 150 162 162 GLY GLY B . n 
B 1 151 ASP 151 163 163 ASP ASP B . n 
B 1 152 ALA 152 164 164 ALA ALA B . n 
B 1 153 VAL 153 165 165 VAL VAL B . n 
B 1 154 ARG 154 166 166 ARG ARG B . n 
B 1 155 PHE 155 167 167 PHE PHE B . n 
B 1 156 GLY 156 168 168 GLY GLY B . n 
B 1 157 PRO 157 169 169 PRO PRO B . n 
B 1 158 VAL 158 170 170 VAL VAL B . n 
B 1 159 GLU 159 171 171 GLU GLU B . n 
B 1 160 LEU 160 172 172 LEU LEU B . n 
B 1 161 PHE 161 173 173 PHE PHE B . n 
B 1 162 TYR 162 174 174 TYR TYR B . n 
B 1 163 PRO 163 175 175 PRO PRO B . n 
B 1 164 GLY 164 176 176 GLY GLY B . n 
B 1 165 ALA 165 177 177 ALA ALA B . n 
B 1 166 ALA 166 178 178 ALA ALA B . n 
B 1 167 HIS 167 179 179 HIS HIS B . n 
B 1 168 SER 168 180 180 SER SER B . n 
B 1 169 THR 169 181 181 THR THR B . n 
B 1 170 ASP 170 182 182 ASP ASP B . n 
B 1 171 ASN 171 183 183 ASN ASN B . n 
B 1 172 LEU 172 184 184 LEU LEU B . n 
B 1 173 VAL 173 185 185 VAL VAL B . n 
B 1 174 VAL 174 186 186 VAL VAL B . n 
B 1 175 TYR 175 187 187 TYR TYR B . n 
B 1 176 VAL 176 188 188 VAL VAL B . n 
B 1 177 PRO 177 189 189 PRO PRO B . n 
B 1 178 SER 178 190 190 SER SER B . n 
B 1 179 ALA 179 191 191 ALA ALA B . n 
B 1 180 SER 180 192 192 SER SER B . n 
B 1 181 VAL 181 193 193 VAL VAL B . n 
B 1 182 LEU 182 194 194 LEU LEU B . n 
B 1 183 TYR 183 195 195 TYR TYR B . n 
B 1 184 GLY 184 196 196 GLY GLY B . n 
B 1 185 GLY 185 197 197 GLY GLY B . n 
B 1 186 CYS 186 198 198 CYS CYS B . n 
B 1 187 ALA 187 199 199 ALA ALA B . n 
B 1 188 ILE 188 200 200 ILE ILE B . n 
B 1 189 TYR 189 201 201 TYR TYR B . n 
B 1 190 GLU 190 202 202 GLU GLU B . n 
B 1 191 LEU 191 203 203 LEU LEU B . n 
B 1 192 SER 192 204 204 SER SER B . n 
B 1 193 ARG 193 205 205 ARG ARG B . n 
B 1 194 THR 194 206 206 THR THR B . n 
B 1 195 SER 195 207 207 SER SER B . n 
B 1 196 ALA 196 208 208 ALA ALA B . n 
B 1 197 GLY 197 209 209 GLY GLY B . n 
B 1 198 ASN 198 210 210 ASN ASN B . n 
B 1 199 VAL 199 211 211 VAL VAL B . n 
B 1 200 ALA 200 212 212 ALA ALA B . n 
B 1 201 ASP 201 213 213 ASP ASP B . n 
B 1 202 ALA 202 214 214 ALA ALA B . n 
B 1 203 ASP 203 215 215 ASP ASP B . n 
B 1 204 LEU 204 216 216 LEU LEU B . n 
B 1 205 ALA 205 217 217 ALA ALA B . n 
B 1 206 GLU 206 218 218 GLU GLU B . n 
B 1 207 TRP 207 219 219 TRP TRP B . n 
B 1 208 PRO 208 220 220 PRO PRO B . n 
B 1 209 THR 209 221 221 THR THR B . n 
B 1 210 SER 210 222 222 SER SER B . n 
B 1 211 ILE 211 223 223 ILE ILE B . n 
B 1 212 GLU 212 224 224 GLU GLU B . n 
B 1 213 ARG 213 225 225 ARG ARG B . n 
B 1 214 ILE 214 226 226 ILE ILE B . n 
B 1 215 GLN 215 227 227 GLN GLN B . n 
B 1 216 GLN 216 228 228 GLN GLN B . n 
B 1 217 HIS 217 229 229 HIS HIS B . n 
B 1 218 TYR 218 230 230 TYR TYR B . n 
B 1 219 PRO 219 231 231 PRO PRO B . n 
B 1 220 GLU 220 232 232 GLU GLU B . n 
B 1 221 ALA 221 233 233 ALA ALA B . n 
B 1 222 GLN 222 234 234 GLN GLN B . n 
B 1 223 PHE 223 235 235 PHE PHE B . n 
B 1 224 VAL 224 236 236 VAL VAL B . n 
B 1 225 ILE 225 237 237 ILE ILE B . n 
B 1 226 PRO 226 238 238 PRO PRO B . n 
B 1 227 GLY 227 239 239 GLY GLY B . n 
B 1 228 HIS 228 240 240 HIS HIS B . n 
B 1 229 GLY 229 241 241 GLY GLY B . n 
B 1 230 LEU 230 242 242 LEU LEU B . n 
B 1 231 PRO 231 243 243 PRO PRO B . n 
B 1 232 GLY 232 244 244 GLY GLY B . n 
B 1 233 GLY 233 245 245 GLY GLY B . n 
B 1 234 LEU 234 246 246 LEU LEU B . n 
B 1 235 ASP 235 247 247 ASP ASP B . n 
B 1 236 LEU 236 248 248 LEU LEU B . n 
B 1 237 LEU 237 249 249 LEU LEU B . n 
B 1 238 LYS 238 250 250 LYS LYS B . n 
B 1 239 HIS 239 251 251 HIS HIS B . n 
B 1 240 THR 240 252 252 THR THR B . n 
B 1 241 THR 241 253 253 THR THR B . n 
B 1 242 ASN 242 254 254 ASN ASN B . n 
B 1 243 VAL 243 255 255 VAL VAL B . n 
B 1 244 VAL 244 256 256 VAL VAL B . n 
B 1 245 LYS 245 257 257 LYS LYS B . n 
B 1 246 ALA 246 258 258 ALA ALA B . n 
B 1 247 HIS 247 259 259 HIS HIS B . n 
B 1 248 THR 248 260 260 THR THR B . n 
B 1 249 ASN 249 261 261 ASN ASN B . n 
B 1 250 ARG 250 262 262 ARG ARG B . n 
B 1 251 SER 251 263 ?   ?   ?   B . n 
B 1 252 VAL 252 264 ?   ?   ?   B . n 
B 1 253 VAL 253 265 ?   ?   ?   B . n 
B 1 254 GLU 254 266 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H8U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H8U 
_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 FMT   1   301 301 FMT   FMT A . 
D 2 FMT   1   302 302 FMT   FMT A . 
E 3 A1H8U 1   303 303 A1H8U RLG A . 
F 4 ZN    1   304 1   ZN    ZN  A . 
G 4 ZN    1   305 2   ZN    ZN  A . 
H 4 ZN    1   306 6   ZN    ZN  A . 
I 3 A1H8U 1   301 301 A1H8U RLG B . 
J 2 FMT   1   302 302 FMT   FMT B . 
K 2 FMT   1   303 303 FMT   FMT B . 
L 4 ZN    1   304 3   ZN    ZN  B . 
M 4 ZN    1   305 4   ZN    ZN  B . 
N 4 ZN    1   306 5   ZN    ZN  B . 
O 5 HOH   1   401 609 HOH   HOH A . 
O 5 HOH   2   402 257 HOH   HOH A . 
O 5 HOH   3   403 173 HOH   HOH A . 
O 5 HOH   4   404 155 HOH   HOH A . 
O 5 HOH   5   405 190 HOH   HOH A . 
O 5 HOH   6   406 198 HOH   HOH A . 
O 5 HOH   7   407 551 HOH   HOH A . 
O 5 HOH   8   408 238 HOH   HOH A . 
O 5 HOH   9   409 235 HOH   HOH A . 
O 5 HOH   10  410 544 HOH   HOH A . 
O 5 HOH   11  411 498 HOH   HOH A . 
O 5 HOH   12  412 70  HOH   HOH A . 
O 5 HOH   13  413 541 HOH   HOH A . 
O 5 HOH   14  414 78  HOH   HOH A . 
O 5 HOH   15  415 176 HOH   HOH A . 
O 5 HOH   16  416 222 HOH   HOH A . 
O 5 HOH   17  417 175 HOH   HOH A . 
O 5 HOH   18  418 60  HOH   HOH A . 
O 5 HOH   19  419 326 HOH   HOH A . 
O 5 HOH   20  420 253 HOH   HOH A . 
O 5 HOH   21  421 479 HOH   HOH A . 
O 5 HOH   22  422 109 HOH   HOH A . 
O 5 HOH   23  423 288 HOH   HOH A . 
O 5 HOH   24  424 524 HOH   HOH A . 
O 5 HOH   25  425 455 HOH   HOH A . 
O 5 HOH   26  426 126 HOH   HOH A . 
O 5 HOH   27  427 123 HOH   HOH A . 
O 5 HOH   28  428 611 HOH   HOH A . 
O 5 HOH   29  429 457 HOH   HOH A . 
O 5 HOH   30  430 594 HOH   HOH A . 
O 5 HOH   31  431 209 HOH   HOH A . 
O 5 HOH   32  432 96  HOH   HOH A . 
O 5 HOH   33  433 587 HOH   HOH A . 
O 5 HOH   34  434 255 HOH   HOH A . 
O 5 HOH   35  435 105 HOH   HOH A . 
O 5 HOH   36  436 8   HOH   HOH A . 
O 5 HOH   37  437 463 HOH   HOH A . 
O 5 HOH   38  438 528 HOH   HOH A . 
O 5 HOH   39  439 143 HOH   HOH A . 
O 5 HOH   40  440 375 HOH   HOH A . 
O 5 HOH   41  441 95  HOH   HOH A . 
O 5 HOH   42  442 355 HOH   HOH A . 
O 5 HOH   43  443 37  HOH   HOH A . 
O 5 HOH   44  444 44  HOH   HOH A . 
O 5 HOH   45  445 119 HOH   HOH A . 
O 5 HOH   46  446 448 HOH   HOH A . 
O 5 HOH   47  447 406 HOH   HOH A . 
O 5 HOH   48  448 547 HOH   HOH A . 
O 5 HOH   49  449 137 HOH   HOH A . 
O 5 HOH   50  450 356 HOH   HOH A . 
O 5 HOH   51  451 147 HOH   HOH A . 
O 5 HOH   52  452 122 HOH   HOH A . 
O 5 HOH   53  453 607 HOH   HOH A . 
O 5 HOH   54  454 114 HOH   HOH A . 
O 5 HOH   55  455 207 HOH   HOH A . 
O 5 HOH   56  456 19  HOH   HOH A . 
O 5 HOH   57  457 552 HOH   HOH A . 
O 5 HOH   58  458 108 HOH   HOH A . 
O 5 HOH   59  459 606 HOH   HOH A . 
O 5 HOH   60  460 6   HOH   HOH A . 
O 5 HOH   61  461 32  HOH   HOH A . 
O 5 HOH   62  462 98  HOH   HOH A . 
O 5 HOH   63  463 107 HOH   HOH A . 
O 5 HOH   64  464 245 HOH   HOH A . 
O 5 HOH   65  465 165 HOH   HOH A . 
O 5 HOH   66  466 359 HOH   HOH A . 
O 5 HOH   67  467 254 HOH   HOH A . 
O 5 HOH   68  468 169 HOH   HOH A . 
O 5 HOH   69  469 65  HOH   HOH A . 
O 5 HOH   70  470 133 HOH   HOH A . 
O 5 HOH   71  471 204 HOH   HOH A . 
O 5 HOH   72  472 249 HOH   HOH A . 
O 5 HOH   73  473 20  HOH   HOH A . 
O 5 HOH   74  474 328 HOH   HOH A . 
O 5 HOH   75  475 183 HOH   HOH A . 
O 5 HOH   76  476 24  HOH   HOH A . 
O 5 HOH   77  477 9   HOH   HOH A . 
O 5 HOH   78  478 28  HOH   HOH A . 
O 5 HOH   79  479 55  HOH   HOH A . 
O 5 HOH   80  480 411 HOH   HOH A . 
O 5 HOH   81  481 15  HOH   HOH A . 
O 5 HOH   82  482 153 HOH   HOH A . 
O 5 HOH   83  483 1   HOH   HOH A . 
O 5 HOH   84  484 125 HOH   HOH A . 
O 5 HOH   85  485 72  HOH   HOH A . 
O 5 HOH   86  486 342 HOH   HOH A . 
O 5 HOH   87  487 491 HOH   HOH A . 
O 5 HOH   88  488 268 HOH   HOH A . 
O 5 HOH   89  489 294 HOH   HOH A . 
O 5 HOH   90  490 31  HOH   HOH A . 
O 5 HOH   91  491 502 HOH   HOH A . 
O 5 HOH   92  492 244 HOH   HOH A . 
O 5 HOH   93  493 110 HOH   HOH A . 
O 5 HOH   94  494 435 HOH   HOH A . 
O 5 HOH   95  495 613 HOH   HOH A . 
O 5 HOH   96  496 118 HOH   HOH A . 
O 5 HOH   97  497 80  HOH   HOH A . 
O 5 HOH   98  498 146 HOH   HOH A . 
O 5 HOH   99  499 101 HOH   HOH A . 
O 5 HOH   100 500 327 HOH   HOH A . 
O 5 HOH   101 501 219 HOH   HOH A . 
O 5 HOH   102 502 41  HOH   HOH A . 
O 5 HOH   103 503 181 HOH   HOH A . 
O 5 HOH   104 504 304 HOH   HOH A . 
O 5 HOH   105 505 439 HOH   HOH A . 
O 5 HOH   106 506 140 HOH   HOH A . 
O 5 HOH   107 507 33  HOH   HOH A . 
O 5 HOH   108 508 189 HOH   HOH A . 
O 5 HOH   109 509 280 HOH   HOH A . 
O 5 HOH   110 510 115 HOH   HOH A . 
O 5 HOH   111 511 370 HOH   HOH A . 
O 5 HOH   112 512 391 HOH   HOH A . 
O 5 HOH   113 513 276 HOH   HOH A . 
O 5 HOH   114 514 54  HOH   HOH A . 
O 5 HOH   115 515 462 HOH   HOH A . 
O 5 HOH   116 516 486 HOH   HOH A . 
O 5 HOH   117 517 185 HOH   HOH A . 
O 5 HOH   118 518 68  HOH   HOH A . 
O 5 HOH   119 519 53  HOH   HOH A . 
O 5 HOH   120 520 277 HOH   HOH A . 
O 5 HOH   121 521 178 HOH   HOH A . 
O 5 HOH   122 522 102 HOH   HOH A . 
O 5 HOH   123 523 39  HOH   HOH A . 
O 5 HOH   124 524 483 HOH   HOH A . 
O 5 HOH   125 525 76  HOH   HOH A . 
O 5 HOH   126 526 38  HOH   HOH A . 
O 5 HOH   127 527 214 HOH   HOH A . 
O 5 HOH   128 528 593 HOH   HOH A . 
O 5 HOH   129 529 83  HOH   HOH A . 
O 5 HOH   130 530 261 HOH   HOH A . 
O 5 HOH   131 531 256 HOH   HOH A . 
O 5 HOH   132 532 243 HOH   HOH A . 
O 5 HOH   133 533 52  HOH   HOH A . 
O 5 HOH   134 534 36  HOH   HOH A . 
O 5 HOH   135 535 309 HOH   HOH A . 
O 5 HOH   136 536 353 HOH   HOH A . 
O 5 HOH   137 537 454 HOH   HOH A . 
O 5 HOH   138 538 369 HOH   HOH A . 
O 5 HOH   139 539 195 HOH   HOH A . 
O 5 HOH   140 540 615 HOH   HOH A . 
O 5 HOH   141 541 307 HOH   HOH A . 
O 5 HOH   142 542 449 HOH   HOH A . 
O 5 HOH   143 543 291 HOH   HOH A . 
O 5 HOH   144 544 290 HOH   HOH A . 
O 5 HOH   145 545 51  HOH   HOH A . 
O 5 HOH   146 546 333 HOH   HOH A . 
O 5 HOH   147 547 111 HOH   HOH A . 
O 5 HOH   148 548 481 HOH   HOH A . 
O 5 HOH   149 549 499 HOH   HOH A . 
O 5 HOH   150 550 94  HOH   HOH A . 
O 5 HOH   151 551 113 HOH   HOH A . 
O 5 HOH   152 552 392 HOH   HOH A . 
O 5 HOH   153 553 263 HOH   HOH A . 
O 5 HOH   154 554 27  HOH   HOH A . 
O 5 HOH   155 555 497 HOH   HOH A . 
O 5 HOH   156 556 223 HOH   HOH A . 
O 5 HOH   157 557 313 HOH   HOH A . 
O 5 HOH   158 558 379 HOH   HOH A . 
O 5 HOH   159 559 297 HOH   HOH A . 
O 5 HOH   160 560 227 HOH   HOH A . 
O 5 HOH   161 561 216 HOH   HOH A . 
O 5 HOH   162 562 3   HOH   HOH A . 
O 5 HOH   163 563 619 HOH   HOH A . 
O 5 HOH   164 564 213 HOH   HOH A . 
O 5 HOH   165 565 89  HOH   HOH A . 
O 5 HOH   166 566 365 HOH   HOH A . 
O 5 HOH   167 567 576 HOH   HOH A . 
O 5 HOH   168 568 50  HOH   HOH A . 
O 5 HOH   169 569 318 HOH   HOH A . 
O 5 HOH   170 570 482 HOH   HOH A . 
O 5 HOH   171 571 324 HOH   HOH A . 
O 5 HOH   172 572 556 HOH   HOH A . 
O 5 HOH   173 573 161 HOH   HOH A . 
O 5 HOH   174 574 429 HOH   HOH A . 
O 5 HOH   175 575 389 HOH   HOH A . 
O 5 HOH   176 576 163 HOH   HOH A . 
O 5 HOH   177 577 164 HOH   HOH A . 
O 5 HOH   178 578 282 HOH   HOH A . 
O 5 HOH   179 579 432 HOH   HOH A . 
O 5 HOH   180 580 124 HOH   HOH A . 
O 5 HOH   181 581 563 HOH   HOH A . 
O 5 HOH   182 582 401 HOH   HOH A . 
O 5 HOH   183 583 292 HOH   HOH A . 
O 5 HOH   184 584 386 HOH   HOH A . 
O 5 HOH   185 585 74  HOH   HOH A . 
O 5 HOH   186 586 82  HOH   HOH A . 
O 5 HOH   187 587 605 HOH   HOH A . 
O 5 HOH   188 588 104 HOH   HOH A . 
O 5 HOH   189 589 559 HOH   HOH A . 
O 5 HOH   190 590 252 HOH   HOH A . 
O 5 HOH   191 591 240 HOH   HOH A . 
O 5 HOH   192 592 385 HOH   HOH A . 
O 5 HOH   193 593 513 HOH   HOH A . 
O 5 HOH   194 594 315 HOH   HOH A . 
O 5 HOH   195 595 270 HOH   HOH A . 
O 5 HOH   196 596 302 HOH   HOH A . 
O 5 HOH   197 597 46  HOH   HOH A . 
O 5 HOH   198 598 529 HOH   HOH A . 
O 5 HOH   199 599 201 HOH   HOH A . 
O 5 HOH   200 600 293 HOH   HOH A . 
O 5 HOH   201 601 510 HOH   HOH A . 
O 5 HOH   202 602 310 HOH   HOH A . 
O 5 HOH   203 603 493 HOH   HOH A . 
O 5 HOH   204 604 546 HOH   HOH A . 
O 5 HOH   205 605 14  HOH   HOH A . 
O 5 HOH   206 606 405 HOH   HOH A . 
O 5 HOH   207 607 496 HOH   HOH A . 
O 5 HOH   208 608 469 HOH   HOH A . 
O 5 HOH   209 609 621 HOH   HOH A . 
O 5 HOH   210 610 453 HOH   HOH A . 
O 5 HOH   211 611 470 HOH   HOH A . 
O 5 HOH   212 612 260 HOH   HOH A . 
O 5 HOH   213 613 543 HOH   HOH A . 
O 5 HOH   214 614 598 HOH   HOH A . 
O 5 HOH   215 615 503 HOH   HOH A . 
O 5 HOH   216 616 396 HOH   HOH A . 
O 5 HOH   217 617 459 HOH   HOH A . 
O 5 HOH   218 618 561 HOH   HOH A . 
O 5 HOH   219 619 413 HOH   HOH A . 
O 5 HOH   220 620 187 HOH   HOH A . 
O 5 HOH   221 621 418 HOH   HOH A . 
O 5 HOH   222 622 566 HOH   HOH A . 
O 5 HOH   223 623 530 HOH   HOH A . 
O 5 HOH   224 624 296 HOH   HOH A . 
O 5 HOH   225 625 596 HOH   HOH A . 
O 5 HOH   226 626 234 HOH   HOH A . 
O 5 HOH   227 627 578 HOH   HOH A . 
O 5 HOH   228 628 526 HOH   HOH A . 
O 5 HOH   229 629 395 HOH   HOH A . 
O 5 HOH   230 630 279 HOH   HOH A . 
O 5 HOH   231 631 451 HOH   HOH A . 
O 5 HOH   232 632 403 HOH   HOH A . 
O 5 HOH   233 633 231 HOH   HOH A . 
O 5 HOH   234 634 45  HOH   HOH A . 
O 5 HOH   235 635 562 HOH   HOH A . 
O 5 HOH   236 636 148 HOH   HOH A . 
O 5 HOH   237 637 426 HOH   HOH A . 
O 5 HOH   238 638 341 HOH   HOH A . 
O 5 HOH   239 639 542 HOH   HOH A . 
O 5 HOH   240 640 364 HOH   HOH A . 
O 5 HOH   241 641 394 HOH   HOH A . 
O 5 HOH   242 642 516 HOH   HOH A . 
O 5 HOH   243 643 445 HOH   HOH A . 
O 5 HOH   244 644 360 HOH   HOH A . 
O 5 HOH   245 645 409 HOH   HOH A . 
O 5 HOH   246 646 512 HOH   HOH A . 
O 5 HOH   247 647 408 HOH   HOH A . 
O 5 HOH   248 648 273 HOH   HOH A . 
O 5 HOH   249 649 321 HOH   HOH A . 
O 5 HOH   250 650 346 HOH   HOH A . 
O 5 HOH   251 651 399 HOH   HOH A . 
O 5 HOH   252 652 351 HOH   HOH A . 
O 5 HOH   253 653 425 HOH   HOH A . 
O 5 HOH   254 654 474 HOH   HOH A . 
O 5 HOH   255 655 414 HOH   HOH A . 
O 5 HOH   256 656 488 HOH   HOH A . 
O 5 HOH   257 657 539 HOH   HOH A . 
O 5 HOH   258 658 507 HOH   HOH A . 
O 5 HOH   259 659 322 HOH   HOH A . 
O 5 HOH   260 660 393 HOH   HOH A . 
O 5 HOH   261 661 303 HOH   HOH A . 
O 5 HOH   262 662 422 HOH   HOH A . 
O 5 HOH   263 663 383 HOH   HOH A . 
O 5 HOH   264 664 601 HOH   HOH A . 
O 5 HOH   265 665 331 HOH   HOH A . 
O 5 HOH   266 666 182 HOH   HOH A . 
O 5 HOH   267 667 128 HOH   HOH A . 
O 5 HOH   268 668 492 HOH   HOH A . 
O 5 HOH   269 669 616 HOH   HOH A . 
O 5 HOH   270 670 368 HOH   HOH A . 
O 5 HOH   271 671 437 HOH   HOH A . 
O 5 HOH   272 672 589 HOH   HOH A . 
O 5 HOH   273 673 583 HOH   HOH A . 
O 5 HOH   274 674 151 HOH   HOH A . 
O 5 HOH   275 675 267 HOH   HOH A . 
O 5 HOH   276 676 537 HOH   HOH A . 
O 5 HOH   277 677 549 HOH   HOH A . 
O 5 HOH   278 678 575 HOH   HOH A . 
O 5 HOH   279 679 390 HOH   HOH A . 
O 5 HOH   280 680 211 HOH   HOH A . 
O 5 HOH   281 681 168 HOH   HOH A . 
O 5 HOH   282 682 610 HOH   HOH A . 
O 5 HOH   283 683 237 HOH   HOH A . 
O 5 HOH   284 684 347 HOH   HOH A . 
O 5 HOH   285 685 380 HOH   HOH A . 
O 5 HOH   286 686 330 HOH   HOH A . 
O 5 HOH   287 687 283 HOH   HOH A . 
O 5 HOH   288 688 515 HOH   HOH A . 
O 5 HOH   289 689 339 HOH   HOH A . 
O 5 HOH   290 690 478 HOH   HOH A . 
O 5 HOH   291 691 278 HOH   HOH A . 
O 5 HOH   292 692 521 HOH   HOH A . 
O 5 HOH   293 693 554 HOH   HOH A . 
O 5 HOH   294 694 443 HOH   HOH A . 
O 5 HOH   295 695 371 HOH   HOH A . 
O 5 HOH   296 696 595 HOH   HOH A . 
O 5 HOH   297 697 317 HOH   HOH A . 
O 5 HOH   298 698 604 HOH   HOH A . 
O 5 HOH   299 699 323 HOH   HOH A . 
O 5 HOH   300 700 597 HOH   HOH A . 
O 5 HOH   301 701 436 HOH   HOH A . 
P 5 HOH   1   401 281 HOH   HOH B . 
P 5 HOH   2   402 239 HOH   HOH B . 
P 5 HOH   3   403 229 HOH   HOH B . 
P 5 HOH   4   404 511 HOH   HOH B . 
P 5 HOH   5   405 565 HOH   HOH B . 
P 5 HOH   6   406 505 HOH   HOH B . 
P 5 HOH   7   407 490 HOH   HOH B . 
P 5 HOH   8   408 519 HOH   HOH B . 
P 5 HOH   9   409 363 HOH   HOH B . 
P 5 HOH   10  410 258 HOH   HOH B . 
P 5 HOH   11  411 66  HOH   HOH B . 
P 5 HOH   12  412 572 HOH   HOH B . 
P 5 HOH   13  413 382 HOH   HOH B . 
P 5 HOH   14  414 612 HOH   HOH B . 
P 5 HOH   15  415 250 HOH   HOH B . 
P 5 HOH   16  416 366 HOH   HOH B . 
P 5 HOH   17  417 150 HOH   HOH B . 
P 5 HOH   18  418 100 HOH   HOH B . 
P 5 HOH   19  419 188 HOH   HOH B . 
P 5 HOH   20  420 264 HOH   HOH B . 
P 5 HOH   21  421 506 HOH   HOH B . 
P 5 HOH   22  422 581 HOH   HOH B . 
P 5 HOH   23  423 42  HOH   HOH B . 
P 5 HOH   24  424 384 HOH   HOH B . 
P 5 HOH   25  425 427 HOH   HOH B . 
P 5 HOH   26  426 215 HOH   HOH B . 
P 5 HOH   27  427 11  HOH   HOH B . 
P 5 HOH   28  428 308 HOH   HOH B . 
P 5 HOH   29  429 103 HOH   HOH B . 
P 5 HOH   30  430 47  HOH   HOH B . 
P 5 HOH   31  431 361 HOH   HOH B . 
P 5 HOH   32  432 210 HOH   HOH B . 
P 5 HOH   33  433 194 HOH   HOH B . 
P 5 HOH   34  434 79  HOH   HOH B . 
P 5 HOH   35  435 377 HOH   HOH B . 
P 5 HOH   36  436 64  HOH   HOH B . 
P 5 HOH   37  437 588 HOH   HOH B . 
P 5 HOH   38  438 532 HOH   HOH B . 
P 5 HOH   39  439 156 HOH   HOH B . 
P 5 HOH   40  440 224 HOH   HOH B . 
P 5 HOH   41  441 159 HOH   HOH B . 
P 5 HOH   42  442 582 HOH   HOH B . 
P 5 HOH   43  443 218 HOH   HOH B . 
P 5 HOH   44  444 424 HOH   HOH B . 
P 5 HOH   45  445 197 HOH   HOH B . 
P 5 HOH   46  446 320 HOH   HOH B . 
P 5 HOH   47  447 367 HOH   HOH B . 
P 5 HOH   48  448 62  HOH   HOH B . 
P 5 HOH   49  449 135 HOH   HOH B . 
P 5 HOH   50  450 259 HOH   HOH B . 
P 5 HOH   51  451 450 HOH   HOH B . 
P 5 HOH   52  452 504 HOH   HOH B . 
P 5 HOH   53  453 144 HOH   HOH B . 
P 5 HOH   54  454 145 HOH   HOH B . 
P 5 HOH   55  455 136 HOH   HOH B . 
P 5 HOH   56  456 311 HOH   HOH B . 
P 5 HOH   57  457 99  HOH   HOH B . 
P 5 HOH   58  458 97  HOH   HOH B . 
P 5 HOH   59  459 298 HOH   HOH B . 
P 5 HOH   60  460 208 HOH   HOH B . 
P 5 HOH   61  461 18  HOH   HOH B . 
P 5 HOH   62  462 29  HOH   HOH B . 
P 5 HOH   63  463 332 HOH   HOH B . 
P 5 HOH   64  464 285 HOH   HOH B . 
P 5 HOH   65  465 314 HOH   HOH B . 
P 5 HOH   66  466 400 HOH   HOH B . 
P 5 HOH   67  467 484 HOH   HOH B . 
P 5 HOH   68  468 16  HOH   HOH B . 
P 5 HOH   69  469 180 HOH   HOH B . 
P 5 HOH   70  470 2   HOH   HOH B . 
P 5 HOH   71  471 61  HOH   HOH B . 
P 5 HOH   72  472 248 HOH   HOH B . 
P 5 HOH   73  473 357 HOH   HOH B . 
P 5 HOH   74  474 569 HOH   HOH B . 
P 5 HOH   75  475 142 HOH   HOH B . 
P 5 HOH   76  476 160 HOH   HOH B . 
P 5 HOH   77  477 5   HOH   HOH B . 
P 5 HOH   78  478 387 HOH   HOH B . 
P 5 HOH   79  479 520 HOH   HOH B . 
P 5 HOH   80  480 535 HOH   HOH B . 
P 5 HOH   81  481 117 HOH   HOH B . 
P 5 HOH   82  482 158 HOH   HOH B . 
P 5 HOH   83  483 86  HOH   HOH B . 
P 5 HOH   84  484 531 HOH   HOH B . 
P 5 HOH   85  485 372 HOH   HOH B . 
P 5 HOH   86  486 59  HOH   HOH B . 
P 5 HOH   87  487 232 HOH   HOH B . 
P 5 HOH   88  488 585 HOH   HOH B . 
P 5 HOH   89  489 200 HOH   HOH B . 
P 5 HOH   90  490 56  HOH   HOH B . 
P 5 HOH   91  491 23  HOH   HOH B . 
P 5 HOH   92  492 88  HOH   HOH B . 
P 5 HOH   93  493 316 HOH   HOH B . 
P 5 HOH   94  494 13  HOH   HOH B . 
P 5 HOH   95  495 120 HOH   HOH B . 
P 5 HOH   96  496 196 HOH   HOH B . 
P 5 HOH   97  497 433 HOH   HOH B . 
P 5 HOH   98  498 85  HOH   HOH B . 
P 5 HOH   99  499 289 HOH   HOH B . 
P 5 HOH   100 500 349 HOH   HOH B . 
P 5 HOH   101 501 352 HOH   HOH B . 
P 5 HOH   102 502 4   HOH   HOH B . 
P 5 HOH   103 503 472 HOH   HOH B . 
P 5 HOH   104 504 305 HOH   HOH B . 
P 5 HOH   105 505 203 HOH   HOH B . 
P 5 HOH   106 506 138 HOH   HOH B . 
P 5 HOH   107 507 34  HOH   HOH B . 
P 5 HOH   108 508 112 HOH   HOH B . 
P 5 HOH   109 509 192 HOH   HOH B . 
P 5 HOH   110 510 247 HOH   HOH B . 
P 5 HOH   111 511 167 HOH   HOH B . 
P 5 HOH   112 512 376 HOH   HOH B . 
P 5 HOH   113 513 428 HOH   HOH B . 
P 5 HOH   114 514 335 HOH   HOH B . 
P 5 HOH   115 515 30  HOH   HOH B . 
P 5 HOH   116 516 354 HOH   HOH B . 
P 5 HOH   117 517 93  HOH   HOH B . 
P 5 HOH   118 518 10  HOH   HOH B . 
P 5 HOH   119 519 92  HOH   HOH B . 
P 5 HOH   120 520 374 HOH   HOH B . 
P 5 HOH   121 521 220 HOH   HOH B . 
P 5 HOH   122 522 12  HOH   HOH B . 
P 5 HOH   123 523 586 HOH   HOH B . 
P 5 HOH   124 524 22  HOH   HOH B . 
P 5 HOH   125 525 116 HOH   HOH B . 
P 5 HOH   126 526 226 HOH   HOH B . 
P 5 HOH   127 527 7   HOH   HOH B . 
P 5 HOH   128 528 246 HOH   HOH B . 
P 5 HOH   129 529 388 HOH   HOH B . 
P 5 HOH   130 530 480 HOH   HOH B . 
P 5 HOH   131 531 57  HOH   HOH B . 
P 5 HOH   132 532 564 HOH   HOH B . 
P 5 HOH   133 533 184 HOH   HOH B . 
P 5 HOH   134 534 312 HOH   HOH B . 
P 5 HOH   135 535 404 HOH   HOH B . 
P 5 HOH   136 536 49  HOH   HOH B . 
P 5 HOH   137 537 599 HOH   HOH B . 
P 5 HOH   138 538 84  HOH   HOH B . 
P 5 HOH   139 539 417 HOH   HOH B . 
P 5 HOH   140 540 91  HOH   HOH B . 
P 5 HOH   141 541 174 HOH   HOH B . 
P 5 HOH   142 542 534 HOH   HOH B . 
P 5 HOH   143 543 48  HOH   HOH B . 
P 5 HOH   144 544 75  HOH   HOH B . 
P 5 HOH   145 545 87  HOH   HOH B . 
P 5 HOH   146 546 186 HOH   HOH B . 
P 5 HOH   147 547 69  HOH   HOH B . 
P 5 HOH   148 548 558 HOH   HOH B . 
P 5 HOH   149 549 416 HOH   HOH B . 
P 5 HOH   150 550 131 HOH   HOH B . 
P 5 HOH   151 551 602 HOH   HOH B . 
P 5 HOH   152 552 345 HOH   HOH B . 
P 5 HOH   153 553 242 HOH   HOH B . 
P 5 HOH   154 554 412 HOH   HOH B . 
P 5 HOH   155 555 58  HOH   HOH B . 
P 5 HOH   156 556 40  HOH   HOH B . 
P 5 HOH   157 557 73  HOH   HOH B . 
P 5 HOH   158 558 442 HOH   HOH B . 
P 5 HOH   159 559 344 HOH   HOH B . 
P 5 HOH   160 560 191 HOH   HOH B . 
P 5 HOH   161 561 206 HOH   HOH B . 
P 5 HOH   162 562 139 HOH   HOH B . 
P 5 HOH   163 563 21  HOH   HOH B . 
P 5 HOH   164 564 25  HOH   HOH B . 
P 5 HOH   165 565 397 HOH   HOH B . 
P 5 HOH   166 566 121 HOH   HOH B . 
P 5 HOH   167 567 171 HOH   HOH B . 
P 5 HOH   168 568 67  HOH   HOH B . 
P 5 HOH   169 569 336 HOH   HOH B . 
P 5 HOH   170 570 591 HOH   HOH B . 
P 5 HOH   171 571 590 HOH   HOH B . 
P 5 HOH   172 572 269 HOH   HOH B . 
P 5 HOH   173 573 571 HOH   HOH B . 
P 5 HOH   174 574 177 HOH   HOH B . 
P 5 HOH   175 575 362 HOH   HOH B . 
P 5 HOH   176 576 287 HOH   HOH B . 
P 5 HOH   177 577 536 HOH   HOH B . 
P 5 HOH   178 578 241 HOH   HOH B . 
P 5 HOH   179 579 329 HOH   HOH B . 
P 5 HOH   180 580 228 HOH   HOH B . 
P 5 HOH   181 581 272 HOH   HOH B . 
P 5 HOH   182 582 77  HOH   HOH B . 
P 5 HOH   183 583 179 HOH   HOH B . 
P 5 HOH   184 584 172 HOH   HOH B . 
P 5 HOH   185 585 444 HOH   HOH B . 
P 5 HOH   186 586 225 HOH   HOH B . 
P 5 HOH   187 587 350 HOH   HOH B . 
P 5 HOH   188 588 334 HOH   HOH B . 
P 5 HOH   189 589 410 HOH   HOH B . 
P 5 HOH   190 590 17  HOH   HOH B . 
P 5 HOH   191 591 233 HOH   HOH B . 
P 5 HOH   192 592 230 HOH   HOH B . 
P 5 HOH   193 593 152 HOH   HOH B . 
P 5 HOH   194 594 467 HOH   HOH B . 
P 5 HOH   195 595 193 HOH   HOH B . 
P 5 HOH   196 596 337 HOH   HOH B . 
P 5 HOH   197 597 570 HOH   HOH B . 
P 5 HOH   198 598 423 HOH   HOH B . 
P 5 HOH   199 599 275 HOH   HOH B . 
P 5 HOH   200 600 584 HOH   HOH B . 
P 5 HOH   201 601 407 HOH   HOH B . 
P 5 HOH   202 602 81  HOH   HOH B . 
P 5 HOH   203 603 465 HOH   HOH B . 
P 5 HOH   204 604 26  HOH   HOH B . 
P 5 HOH   205 605 35  HOH   HOH B . 
P 5 HOH   206 606 212 HOH   HOH B . 
P 5 HOH   207 607 553 HOH   HOH B . 
P 5 HOH   208 608 300 HOH   HOH B . 
P 5 HOH   209 609 295 HOH   HOH B . 
P 5 HOH   210 610 434 HOH   HOH B . 
P 5 HOH   211 611 577 HOH   HOH B . 
P 5 HOH   212 612 205 HOH   HOH B . 
P 5 HOH   213 613 130 HOH   HOH B . 
P 5 HOH   214 614 557 HOH   HOH B . 
P 5 HOH   215 615 199 HOH   HOH B . 
P 5 HOH   216 616 620 HOH   HOH B . 
P 5 HOH   217 617 398 HOH   HOH B . 
P 5 HOH   218 618 43  HOH   HOH B . 
P 5 HOH   219 619 217 HOH   HOH B . 
P 5 HOH   220 620 603 HOH   HOH B . 
P 5 HOH   221 621 522 HOH   HOH B . 
P 5 HOH   222 622 464 HOH   HOH B . 
P 5 HOH   223 623 550 HOH   HOH B . 
P 5 HOH   224 624 600 HOH   HOH B . 
P 5 HOH   225 625 170 HOH   HOH B . 
P 5 HOH   226 626 517 HOH   HOH B . 
P 5 HOH   227 627 477 HOH   HOH B . 
P 5 HOH   228 628 485 HOH   HOH B . 
P 5 HOH   229 629 608 HOH   HOH B . 
P 5 HOH   230 630 438 HOH   HOH B . 
P 5 HOH   231 631 402 HOH   HOH B . 
P 5 HOH   232 632 274 HOH   HOH B . 
P 5 HOH   233 633 90  HOH   HOH B . 
P 5 HOH   234 634 415 HOH   HOH B . 
P 5 HOH   235 635 533 HOH   HOH B . 
P 5 HOH   236 636 568 HOH   HOH B . 
P 5 HOH   237 637 489 HOH   HOH B . 
P 5 HOH   238 638 306 HOH   HOH B . 
P 5 HOH   239 639 538 HOH   HOH B . 
P 5 HOH   240 640 157 HOH   HOH B . 
P 5 HOH   241 641 580 HOH   HOH B . 
P 5 HOH   242 642 301 HOH   HOH B . 
P 5 HOH   243 643 446 HOH   HOH B . 
P 5 HOH   244 644 475 HOH   HOH B . 
P 5 HOH   245 645 419 HOH   HOH B . 
P 5 HOH   246 646 132 HOH   HOH B . 
P 5 HOH   247 647 456 HOH   HOH B . 
P 5 HOH   248 648 340 HOH   HOH B . 
P 5 HOH   249 649 430 HOH   HOH B . 
P 5 HOH   250 650 154 HOH   HOH B . 
P 5 HOH   251 651 265 HOH   HOH B . 
P 5 HOH   252 652 251 HOH   HOH B . 
P 5 HOH   253 653 518 HOH   HOH B . 
P 5 HOH   254 654 614 HOH   HOH B . 
P 5 HOH   255 655 166 HOH   HOH B . 
P 5 HOH   256 656 262 HOH   HOH B . 
P 5 HOH   257 657 440 HOH   HOH B . 
P 5 HOH   258 658 134 HOH   HOH B . 
P 5 HOH   259 659 555 HOH   HOH B . 
P 5 HOH   260 660 299 HOH   HOH B . 
P 5 HOH   261 661 527 HOH   HOH B . 
P 5 HOH   262 662 271 HOH   HOH B . 
P 5 HOH   263 663 573 HOH   HOH B . 
P 5 HOH   264 664 441 HOH   HOH B . 
P 5 HOH   265 665 545 HOH   HOH B . 
P 5 HOH   266 666 501 HOH   HOH B . 
P 5 HOH   267 667 420 HOH   HOH B . 
P 5 HOH   268 668 106 HOH   HOH B . 
P 5 HOH   269 669 540 HOH   HOH B . 
P 5 HOH   270 670 548 HOH   HOH B . 
P 5 HOH   271 671 509 HOH   HOH B . 
P 5 HOH   272 672 487 HOH   HOH B . 
P 5 HOH   273 673 560 HOH   HOH B . 
P 5 HOH   274 674 514 HOH   HOH B . 
P 5 HOH   275 675 63  HOH   HOH B . 
P 5 HOH   276 676 129 HOH   HOH B . 
P 5 HOH   277 677 461 HOH   HOH B . 
P 5 HOH   278 678 381 HOH   HOH B . 
P 5 HOH   279 679 319 HOH   HOH B . 
P 5 HOH   280 680 338 HOH   HOH B . 
P 5 HOH   281 681 71  HOH   HOH B . 
P 5 HOH   282 682 141 HOH   HOH B . 
P 5 HOH   283 683 149 HOH   HOH B . 
P 5 HOH   284 684 373 HOH   HOH B . 
P 5 HOH   285 685 494 HOH   HOH B . 
P 5 HOH   286 686 284 HOH   HOH B . 
P 5 HOH   287 687 266 HOH   HOH B . 
P 5 HOH   288 688 286 HOH   HOH B . 
P 5 HOH   289 689 476 HOH   HOH B . 
P 5 HOH   290 690 221 HOH   HOH B . 
P 5 HOH   291 691 162 HOH   HOH B . 
P 5 HOH   292 692 236 HOH   HOH B . 
P 5 HOH   293 693 127 HOH   HOH B . 
P 5 HOH   294 694 202 HOH   HOH B . 
P 5 HOH   295 695 574 HOH   HOH B . 
P 5 HOH   296 696 421 HOH   HOH B . 
P 5 HOH   297 697 617 HOH   HOH B . 
P 5 HOH   298 698 500 HOH   HOH B . 
P 5 HOH   299 699 358 HOH   HOH B . 
P 5 HOH   300 700 567 HOH   HOH B . 
P 5 HOH   301 701 523 HOH   HOH B . 
P 5 HOH   302 702 525 HOH   HOH B . 
P 5 HOH   303 703 508 HOH   HOH B . 
P 5 HOH   304 704 431 HOH   HOH B . 
P 5 HOH   305 705 452 HOH   HOH B . 
P 5 HOH   306 706 343 HOH   HOH B . 
P 5 HOH   307 707 468 HOH   HOH B . 
P 5 HOH   308 708 458 HOH   HOH B . 
P 5 HOH   309 709 495 HOH   HOH B . 
P 5 HOH   310 710 466 HOH   HOH B . 
P 5 HOH   311 711 592 HOH   HOH B . 
P 5 HOH   312 712 579 HOH   HOH B . 
P 5 HOH   313 713 378 HOH   HOH B . 
P 5 HOH   314 714 325 HOH   HOH B . 
P 5 HOH   315 715 460 HOH   HOH B . 
P 5 HOH   316 716 447 HOH   HOH B . 
P 5 HOH   317 717 473 HOH   HOH B . 
P 5 HOH   318 718 618 HOH   HOH B . 
P 5 HOH   319 719 471 HOH   HOH B . 
P 5 HOH   320 720 348 HOH   HOH B . 
# 
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 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   130.380 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F0S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.506 
_cell.length_a_esd                 ? 
_cell.length_b                     79.244 
_cell.length_b_esd                 ? 
_cell.length_c                     67.716 
_cell.length_c_esd                 ? 
_cell.volume                       414925.502 
_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                         9F0S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9F0S 
_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             1.90 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.14 
_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              7.2 
_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    
;protein solution: 10.3 mg/ml in 50 mM Tris/HCl, pH 7.2, 100 uM ZnCl2

crystallization agent: 20 mM inhibitor, 25% polyethylene glycol (PEG) 3350, 0.2 M magnesium formate

cryo protectant solution: (20 mM inhibitor, 25% PEG3350, 15% Ethylene glycol, 0.2 mM MgCl2, 50 mM HEPES pH 7.2)
;
_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         2023-08-19 
_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   0.8 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          13.24 
_reflns.entry_id                                       9F0S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.11 
_reflns.d_resolution_low                               55.4 
_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                                     100869 
_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                           79.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_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                                0.054 
_reflns.pdbx_Rpim_I_all                                0.02 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05 
_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                                    1.11 
_reflns_shell.d_res_low                                     1.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5044 
_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                               0.774 
_reflns_shell.pdbx_Rpim_I_all                               0.471 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.742 
_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                                  0.688 
_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                               19.33 
_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                                 9F0S 
_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                            1.40 
_refine.ls_d_res_low                             55.34 
_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                     77532 
_refine.ls_number_reflns_R_free                  3842 
_refine.ls_number_reflns_R_work                  73690 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.63 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1724 
_refine.ls_R_factor_R_free                       0.1860 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1716 
_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                          1.36 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 20.2364 
_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                            0.1420 
_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.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        55.34 
_refine_hist.number_atoms_solvent             621 
_refine_hist.number_atoms_total               4167 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3486 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0066  ? 3801 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9664  ? 5240 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0859  ? 596  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0086  ? 692  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.5010 ? 564  ? f_dihedral_angle_d ? ? 
# 
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' 1.40 1.42  . . 132 2401 85.06 . . . . 0.2338 . . . . . . . . . . . 0.2598 
'X-RAY DIFFRACTION' 1.42 1.44  . . 122 2543 90.25 . . . . 0.2452 . . . . . . . . . . . 0.2811 
'X-RAY DIFFRACTION' 1.44 1.46  . . 125 2660 93.43 . . . . 0.2280 . . . . . . . . . . . 0.2741 
'X-RAY DIFFRACTION' 1.46 1.48  . . 134 2653 95.91 . . . . 0.2202 . . . . . . . . . . . 0.2554 
'X-RAY DIFFRACTION' 1.48 1.50  . . 175 2705 97.13 . . . . 0.2174 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 1.50 1.52  . . 166 2731 97.35 . . . . 0.2146 . . . . . . . . . . . 0.2350 
'X-RAY DIFFRACTION' 1.52 1.55  . . 172 2684 96.88 . . . . 0.2129 . . . . . . . . . . . 0.2817 
'X-RAY DIFFRACTION' 1.55 1.57  . . 128 2756 96.91 . . . . 0.2085 . . . . . . . . . . . 0.2403 
'X-RAY DIFFRACTION' 1.57 1.60  . . 137 2762 97.45 . . . . 0.2026 . . . . . . . . . . . 0.2424 
'X-RAY DIFFRACTION' 1.60 1.63  . . 124 2744 97.45 . . . . 0.2034 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 1.63 1.67  . . 160 2714 97.32 . . . . 0.1956 . . . . . . . . . . . 0.2107 
'X-RAY DIFFRACTION' 1.67 1.70  . . 165 2728 97.11 . . . . 0.1918 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 1.70 1.74  . . 140 2751 97.80 . . . . 0.1799 . . . . . . . . . . . 0.2285 
'X-RAY DIFFRACTION' 1.74 1.79  . . 100 2790 97.40 . . . . 0.1915 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 1.79 1.83  . . 102 2789 97.90 . . . . 0.1839 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 1.83 1.89  . . 160 2767 97.79 . . . . 0.1825 . . . . . . . . . . . 0.2248 
'X-RAY DIFFRACTION' 1.89 1.95  . . 154 2753 98.48 . . . . 0.1773 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 1.95 2.02  . . 148 2771 98.28 . . . . 0.1662 . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 2.02 2.10  . . 140 2770 97.95 . . . . 0.1638 . . . . . . . . . . . 0.1628 
'X-RAY DIFFRACTION' 2.10 2.20  . . 132 2765 97.74 . . . . 0.1694 . . . . . . . . . . . 0.1925 
'X-RAY DIFFRACTION' 2.20 2.31  . . 121 2811 98.29 . . . . 0.1696 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 2.31 2.46  . . 100 2791 97.27 . . . . 0.1665 . . . . . . . . . . . 0.1848 
'X-RAY DIFFRACTION' 2.46 2.65  . . 127 2757 96.84 . . . . 0.1707 . . . . . . . . . . . 0.1661 
'X-RAY DIFFRACTION' 2.65 2.91  . . 128 2849 99.17 . . . . 0.1709 . . . . . . . . . . . 0.1860 
'X-RAY DIFFRACTION' 2.91 3.33  . . 184 2759 98.73 . . . . 0.1538 . . . . . . . . . . . 0.1558 
'X-RAY DIFFRACTION' 3.33 4.20  . . 176 2761 97.93 . . . . 0.1391 . . . . . . . . . . . 0.1341 
'X-RAY DIFFRACTION' 4.20 55.34 . . 190 2725 95.29 . . . . 0.1537 . . . . . . . . . . . 0.1727 
# 
_struct.entry_id                     9F0S 
_struct.title                        
'VIM-2 in complex with GKV63 (5j) - dynamically chiral phosphonic acid-type metallo-beta-lactamase inhibitors' 
_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        9F0S 
_struct_keywords.text            'beta-lactamase, metallo-beta-lactamase, inhibitor, ANTIBIOTIC' 
_struct_keywords.pdbx_keywords   ANTIBIOTIC 
# 
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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 3 ? 
J N N 2 ? 
K N N 2 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 5 ? 
P N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    B8QIQ9_PSEAI 
_struct_ref.pdbx_db_accession          B8QIQ9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VDSSGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLP
VTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTDNLVV
YVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYPEAQFVIPGHGLPGGLDLLKHTTNVVKAHTNRSVVE

;
_struct_ref.pdbx_align_begin           27 
# 
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 9F0S A 15 ? 254 ? B8QIQ9 27 ? 266 ? 27 266 
2 1 9F0S B 15 ? 254 ? B8QIQ9 27 ? 266 ? 27 266 
# 
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 9F0S MET A 1  ? UNP B8QIQ9 ? ? 'initiating methionine' 13 1  
1 9F0S HIS A 2  ? UNP B8QIQ9 ? ? 'expression tag'        14 2  
1 9F0S HIS A 3  ? UNP B8QIQ9 ? ? 'expression tag'        15 3  
1 9F0S HIS A 4  ? UNP B8QIQ9 ? ? 'expression tag'        16 4  
1 9F0S HIS A 5  ? UNP B8QIQ9 ? ? 'expression tag'        17 5  
1 9F0S HIS A 6  ? UNP B8QIQ9 ? ? 'expression tag'        18 6  
1 9F0S HIS A 7  ? UNP B8QIQ9 ? ? 'expression tag'        19 7  
1 9F0S GLU A 8  ? UNP B8QIQ9 ? ? 'expression tag'        20 8  
1 9F0S ASN A 9  ? UNP B8QIQ9 ? ? 'expression tag'        21 9  
1 9F0S LEU A 10 ? UNP B8QIQ9 ? ? 'expression tag'        22 10 
1 9F0S TYR A 11 ? UNP B8QIQ9 ? ? 'expression tag'        23 11 
1 9F0S PHE A 12 ? UNP B8QIQ9 ? ? 'expression tag'        24 12 
1 9F0S GLN A 13 ? UNP B8QIQ9 ? ? 'expression tag'        25 13 
1 9F0S GLY A 14 ? UNP B8QIQ9 ? ? 'expression tag'        26 14 
2 9F0S MET B 1  ? UNP B8QIQ9 ? ? 'initiating methionine' 13 15 
2 9F0S HIS B 2  ? UNP B8QIQ9 ? ? 'expression tag'        14 16 
2 9F0S HIS B 3  ? UNP B8QIQ9 ? ? 'expression tag'        15 17 
2 9F0S HIS B 4  ? UNP B8QIQ9 ? ? 'expression tag'        16 18 
2 9F0S HIS B 5  ? UNP B8QIQ9 ? ? 'expression tag'        17 19 
2 9F0S HIS B 6  ? UNP B8QIQ9 ? ? 'expression tag'        18 20 
2 9F0S HIS B 7  ? UNP B8QIQ9 ? ? 'expression tag'        19 21 
2 9F0S GLU B 8  ? UNP B8QIQ9 ? ? 'expression tag'        20 22 
2 9F0S ASN B 9  ? UNP B8QIQ9 ? ? 'expression tag'        21 23 
2 9F0S LEU B 10 ? UNP B8QIQ9 ? ? 'expression tag'        22 24 
2 9F0S TYR B 11 ? UNP B8QIQ9 ? ? 'expression tag'        23 25 
2 9F0S PHE B 12 ? UNP B8QIQ9 ? ? 'expression tag'        24 26 
2 9F0S GLN B 13 ? UNP B8QIQ9 ? ? 'expression tag'        25 27 
2 9F0S GLY B 14 ? UNP B8QIQ9 ? ? 'expression tag'        26 28 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,O 
2 1 B,I,J,K,L,M,N,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 23  ? ILE A 27  ? THR A 35  ILE A 39  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 76  ? ILE A 91  ? GLY A 88  ILE A 103 1 ? 16 
HELX_P HELX_P3  AA3 HIS A 104 ? GLY A 109 ? HIS A 116 GLY A 121 1 ? 6  
HELX_P HELX_P4  AA4 GLY A 110 ? ALA A 117 ? GLY A 122 ALA A 129 1 ? 8  
HELX_P HELX_P5  AA5 SER A 124 ? GLY A 135 ? SER A 136 GLY A 147 1 ? 12 
HELX_P HELX_P6  AA6 CYS A 186 ? ILE A 188 ? CYS A 198 ILE A 200 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 206 ? TYR A 218 ? GLU A 218 TYR A 230 1 ? 13 
HELX_P HELX_P8  AA8 LEU A 234 ? ASN A 249 ? LEU A 246 ASN A 261 1 ? 16 
HELX_P HELX_P9  AA9 THR B 23  ? ILE B 27  ? THR B 35  ILE B 39  5 ? 5  
HELX_P HELX_P10 AB1 GLY B 76  ? ILE B 91  ? GLY B 88  ILE B 103 1 ? 16 
HELX_P HELX_P11 AB2 HIS B 104 ? GLY B 109 ? HIS B 116 GLY B 121 1 ? 6  
HELX_P HELX_P12 AB3 GLY B 110 ? ALA B 117 ? GLY B 122 ALA B 129 1 ? 8  
HELX_P HELX_P13 AB4 SER B 124 ? GLY B 135 ? SER B 136 GLY B 147 1 ? 12 
HELX_P HELX_P14 AB5 CYS B 186 ? ILE B 188 ? CYS B 198 ILE B 200 5 ? 3  
HELX_P HELX_P15 AB6 GLU B 206 ? TYR B 218 ? GLU B 218 TYR B 230 1 ? 13 
HELX_P HELX_P16 AB7 LEU B 234 ? ASN B 249 ? LEU B 246 ASN B 261 1 ? 16 
# 
_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 
metalc1  metalc ? ? A HIS   102 NE2 ? ? ? 1_555 F ZN . ZN ? ? A HIS   114 A ZN 304 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc2  metalc ? ? A HIS   104 ND1 ? ? ? 1_555 F ZN . ZN ? ? A HIS   116 A ZN 304 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc3  metalc ? ? A ASP   106 OD2 ? ? ? 1_555 H ZN . ZN ? ? A ASP   118 A ZN 306 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc4  metalc ? ? A HIS   141 NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS   153 A ZN 305 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc5  metalc ? ? A HIS   167 NE2 ? ? ? 1_555 F ZN . ZN ? ? A HIS   179 A ZN 304 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc6  metalc ? ? A CYS   186 SG  ? ? ? 1_555 H ZN . ZN ? ? A CYS   198 A ZN 306 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc7  metalc ? ? A HIS   228 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS   240 A ZN 306 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc8  metalc ? ? A HIS   239 ND1 ? ? ? 1_555 G ZN . ZN ? ? A HIS   251 A ZN 305 4_545 ? ? ? ? ? ? ? 2.141 ? ? 
metalc9  metalc ? ? C FMT   .   O1  ? ? ? 1_555 G ZN . ZN ? ? A FMT   301 A ZN 305 1_555 ? ? ? ? ? ? ? 1.897 ? ? 
metalc10 metalc ? ? D FMT   .   O1  ? ? ? 1_555 G ZN . ZN ? ? A FMT   302 A ZN 305 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc11 metalc ? ? D FMT   .   O2  ? ? ? 1_555 G ZN . ZN ? ? A FMT   302 A ZN 305 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc12 metalc ? ? E A1H8U .   O3  ? ? ? 1_555 F ZN . ZN ? ? A A1H8U 303 A ZN 304 1_555 ? ? ? ? ? ? ? 1.856 ? ? 
metalc13 metalc ? ? E A1H8U .   O5  ? ? ? 1_555 H ZN . ZN ? ? A A1H8U 303 A ZN 306 1_555 ? ? ? ? ? ? ? 1.893 ? ? 
metalc14 metalc ? ? B HIS   102 NE2 ? ? ? 1_555 L ZN . ZN ? ? B HIS   114 B ZN 304 1_555 ? ? ? ? ? ? ? 2.155 ? ? 
metalc15 metalc ? ? B HIS   104 ND1 ? ? ? 1_555 L ZN . ZN ? ? B HIS   116 B ZN 304 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc16 metalc ? ? B ASP   106 OD2 ? ? ? 1_555 N ZN . ZN ? ? B ASP   118 B ZN 306 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc17 metalc ? ? B HIS   141 NE2 ? ? ? 1_555 M ZN . ZN ? ? B HIS   153 B ZN 305 4_546 ? ? ? ? ? ? ? 2.324 ? ? 
metalc18 metalc ? ? B HIS   167 NE2 ? ? ? 1_555 L ZN . ZN ? ? B HIS   179 B ZN 304 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc19 metalc ? ? B CYS   186 SG  ? ? ? 1_555 N ZN . ZN ? ? B CYS   198 B ZN 306 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc20 metalc ? ? B HIS   228 NE2 ? ? ? 1_555 N ZN . ZN ? ? B HIS   240 B ZN 306 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc21 metalc ? ? B HIS   239 ND1 ? ? ? 1_555 M ZN . ZN ? ? B HIS   251 B ZN 305 1_555 ? ? ? ? ? ? ? 2.135 ? ? 
metalc22 metalc ? ? I A1H8U .   O5  A ? ? 1_555 L ZN . ZN ? ? B A1H8U 301 B ZN 304 1_555 ? ? ? ? ? ? ? 1.730 ? ? 
metalc23 metalc ? ? I A1H8U .   O4  A ? ? 1_555 N ZN . ZN ? ? B A1H8U 301 B ZN 306 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc24 metalc ? ? J FMT   .   O1  ? ? ? 1_555 M ZN . ZN ? ? B FMT   302 B ZN 305 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc25 metalc ? ? J FMT   .   O2  ? ? ? 1_555 M ZN . ZN ? ? B FMT   302 B ZN 305 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  NE2 ? A HIS 102 ? A HIS 114 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 ND1 ? A HIS   104 ? A HIS   116 ? 1_555 100.3 ? 
2  NE2 ? A HIS 102 ? A HIS 114 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 NE2 ? A HIS   167 ? A HIS   179 ? 1_555 100.0 ? 
3  ND1 ? A HIS 104 ? A HIS 116 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 NE2 ? A HIS   167 ? A HIS   179 ? 1_555 114.5 ? 
4  NE2 ? A HIS 102 ? A HIS 114 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O3  ? E A1H8U .   ? A A1H8U 303 ? 1_555 117.7 ? 
5  ND1 ? A HIS 104 ? A HIS 116 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O3  ? E A1H8U .   ? A A1H8U 303 ? 1_555 111.7 ? 
6  NE2 ? A HIS 167 ? A HIS 179 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O3  ? E A1H8U .   ? A A1H8U 303 ? 1_555 111.8 ? 
7  OD2 ? A ASP 106 ? A ASP 118 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 SG  ? A CYS   186 ? A CYS   198 ? 1_555 118.9 ? 
8  OD2 ? A ASP 106 ? A ASP 118 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 NE2 ? A HIS   228 ? A HIS   240 ? 1_555 96.8  ? 
9  SG  ? A CYS 186 ? A CYS 198 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 NE2 ? A HIS   228 ? A HIS   240 ? 1_555 108.2 ? 
10 OD2 ? A ASP 106 ? A ASP 118 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O5  ? E A1H8U .   ? A A1H8U 303 ? 1_555 113.3 ? 
11 SG  ? A CYS 186 ? A CYS 198 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O5  ? E A1H8U .   ? A A1H8U 303 ? 1_555 108.7 ? 
12 NE2 ? A HIS 228 ? A HIS 240 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O5  ? E A1H8U .   ? A A1H8U 303 ? 1_555 110.3 ? 
13 NE2 ? A HIS 141 ? A HIS 153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 ND1 ? A HIS   239 ? A HIS   251 ? 1_555 47.9  ? 
14 NE2 ? A HIS 141 ? A HIS 153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? C FMT   .   ? A FMT   301 ? 1_555 135.9 ? 
15 ND1 ? A HIS 239 ? A HIS 251 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? C FMT   .   ? A FMT   301 ? 1_555 99.9  ? 
16 NE2 ? A HIS 141 ? A HIS 153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 110.8 ? 
17 ND1 ? A HIS 239 ? A HIS 251 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 72.2  ? 
18 O1  ? C FMT .   ? A FMT 301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 76.3  ? 
19 NE2 ? A HIS 141 ? A HIS 153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 75.0  ? 
20 ND1 ? A HIS 239 ? A HIS 251 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 74.2  ? 
21 O1  ? C FMT .   ? A FMT 301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 131.6 ? 
22 O1  ? D FMT .   ? A FMT 302 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 55.9  ? 
23 NE2 ? B HIS 102 ? B HIS 114 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 ND1 ? B HIS   104 ? B HIS   116 ? 1_555 101.2 ? 
24 NE2 ? B HIS 102 ? B HIS 114 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 NE2 ? B HIS   167 ? B HIS   179 ? 1_555 103.3 ? 
25 ND1 ? B HIS 104 ? B HIS 116 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 NE2 ? B HIS   167 ? B HIS   179 ? 1_555 112.1 ? 
26 NE2 ? B HIS 102 ? B HIS 114 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 O5  A I A1H8U .   ? B A1H8U 301 ? 1_555 118.5 ? 
27 ND1 ? B HIS 104 ? B HIS 116 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 O5  A I A1H8U .   ? B A1H8U 301 ? 1_555 106.1 ? 
28 NE2 ? B HIS 167 ? B HIS 179 ? 1_555 ZN ? L ZN . ? B ZN 304 ? 1_555 O5  A I A1H8U .   ? B A1H8U 301 ? 1_555 114.8 ? 
29 OD2 ? B ASP 106 ? B ASP 118 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 SG  ? B CYS   186 ? B CYS   198 ? 1_555 120.0 ? 
30 OD2 ? B ASP 106 ? B ASP 118 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 NE2 ? B HIS   228 ? B HIS   240 ? 1_555 97.8  ? 
31 SG  ? B CYS 186 ? B CYS 198 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 NE2 ? B HIS   228 ? B HIS   240 ? 1_555 109.6 ? 
32 OD2 ? B ASP 106 ? B ASP 118 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 O4  A I A1H8U .   ? B A1H8U 301 ? 1_555 113.7 ? 
33 SG  ? B CYS 186 ? B CYS 198 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 O4  A I A1H8U .   ? B A1H8U 301 ? 1_555 114.3 ? 
34 NE2 ? B HIS 228 ? B HIS 240 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 1_555 O4  A I A1H8U .   ? B A1H8U 301 ? 1_555 97.1  ? 
35 NE2 ? B HIS 141 ? B HIS 153 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 ND1 ? B HIS   239 ? B HIS   251 ? 1_555 57.9  ? 
36 NE2 ? B HIS 141 ? B HIS 153 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 O1  ? J FMT   .   ? B FMT   302 ? 1_555 56.0  ? 
37 ND1 ? B HIS 239 ? B HIS 251 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 O1  ? J FMT   .   ? B FMT   302 ? 1_555 2.1   ? 
38 NE2 ? B HIS 141 ? B HIS 153 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 O2  ? J FMT   .   ? B FMT   302 ? 1_555 58.8  ? 
39 ND1 ? B HIS 239 ? B HIS 251 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 O2  ? J FMT   .   ? B FMT   302 ? 1_555 2.2   ? 
40 O1  ? J FMT .   ? B FMT 302 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 4_546 O2  ? J FMT   .   ? B FMT   302 ? 1_555 2.9   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? 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 ARG A 33  ? ALA A 38  ? ARG A 45  ALA A 50  
AA1 2 VAL A 41  ? PHE A 50  ? VAL A 53  PHE A 62  
AA1 3 ALA A 53  ? ASP A 64  ? ALA A 65  ASP A 76  
AA1 4 GLU A 67  ? ILE A 71  ? GLU A 79  ILE A 83  
AA1 5 VAL A 95  ? VAL A 99  ? VAL A 107 VAL A 111 
AA1 6 ALA A 120 ? ALA A 123 ? ALA A 132 ALA A 135 
AA1 7 HIS A 141 ? SER A 142 ? HIS A 153 SER A 154 
AA2 1 ASP A 151 ? PHE A 155 ? ASP A 163 PHE A 167 
AA2 2 VAL A 158 ? TYR A 162 ? VAL A 170 TYR A 174 
AA2 3 VAL A 173 ? VAL A 176 ? VAL A 185 VAL A 188 
AA2 4 VAL A 181 ? GLY A 185 ? VAL A 193 GLY A 197 
AA2 5 PHE A 223 ? PRO A 226 ? PHE A 235 PRO A 238 
AA3 1 VAL B 32  ? ALA B 38  ? VAL B 44  ALA B 50  
AA3 2 VAL B 41  ? PHE B 50  ? VAL B 53  PHE B 62  
AA3 3 ALA B 53  ? ASP B 64  ? ALA B 65  ASP B 76  
AA3 4 GLU B 67  ? ILE B 71  ? GLU B 79  ILE B 83  
AA3 5 VAL B 95  ? VAL B 99  ? VAL B 107 VAL B 111 
AA3 6 ALA B 120 ? ALA B 123 ? ALA B 132 ALA B 135 
AA3 7 HIS B 141 ? SER B 142 ? HIS B 153 SER B 154 
AA4 1 ASP B 151 ? PHE B 155 ? ASP B 163 PHE B 167 
AA4 2 VAL B 158 ? TYR B 162 ? VAL B 170 TYR B 174 
AA4 3 VAL B 173 ? VAL B 176 ? VAL B 185 VAL B 188 
AA4 4 VAL B 181 ? GLY B 185 ? VAL B 193 GLY B 197 
AA4 5 PHE B 223 ? PRO B 226 ? PHE B 235 PRO B 238 
# 
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 ARG A 33  ? N ARG A 45  O ILE A 45  ? O ILE A 57  
AA1 2 3 N PHE A 50  ? N PHE A 62  O ALA A 53  ? O ALA A 65  
AA1 3 4 N LEU A 60  ? N LEU A 72  O ILE A 71  ? O ILE A 83  
AA1 4 5 N LEU A 70  ? N LEU A 82  O ARG A 97  ? O ARG A 109 
AA1 5 6 N ALA A 98  ? N ALA A 110 O ALA A 120 ? O ALA A 132 
AA1 6 7 N THR A 121 ? N THR A 133 O HIS A 141 ? O HIS A 153 
AA2 1 2 N VAL A 153 ? N VAL A 165 O LEU A 160 ? O LEU A 172 
AA2 2 3 N GLU A 159 ? N GLU A 171 O TYR A 175 ? O TYR A 187 
AA2 3 4 N VAL A 174 ? N VAL A 186 O TYR A 183 ? O TYR A 195 
AA2 4 5 N LEU A 182 ? N LEU A 194 O PHE A 223 ? O PHE A 235 
AA3 1 2 N ARG B 33  ? N ARG B 45  O ILE B 45  ? O ILE B 57  
AA3 2 3 N PHE B 50  ? N PHE B 62  O ALA B 53  ? O ALA B 65  
AA3 3 4 N ASP B 64  ? N ASP B 76  O GLU B 67  ? O GLU B 79  
AA3 4 5 N LEU B 70  ? N LEU B 82  O ARG B 97  ? O ARG B 109 
AA3 5 6 N THR B 96  ? N THR B 108 O ALA B 120 ? O ALA B 132 
AA3 6 7 N THR B 121 ? N THR B 133 O HIS B 141 ? O HIS B 153 
AA4 1 2 N VAL B 153 ? N VAL B 165 O LEU B 160 ? O LEU B 172 
AA4 2 3 N GLU B 159 ? N GLU B 171 O TYR B 175 ? O TYR B 187 
AA4 3 4 N VAL B 174 ? N VAL B 186 O TYR B 183 ? O TYR B 195 
AA4 4 5 N LEU B 182 ? N LEU B 194 O PHE B 223 ? O PHE B 235 
# 
_pdbx_entry_details.entry_id                   9F0S 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 ND2 B ASN 254 ? A O1 B FMT 303 ? ? 1.30 
2  1 O2  B FMT 303 ? ? ZN B ZN  305 ? ? 1.59 
3  1 O   A HOH 487 ? ? O  A HOH 603 ? ? 1.65 
4  1 O   B HOH 523 ? ? O  B HOH 571 ? ? 1.73 
5  1 O   B HOH 622 ? ? O  B HOH 654 ? ? 1.83 
6  1 O   B HOH 480 ? ? O  B HOH 577 ? ? 1.92 
7  1 O   A HOH 424 ? ? O  A HOH 549 ? ? 1.93 
8  1 O   B HOH 412 ? ? O  B HOH 623 ? ? 1.98 
9  1 O   B HOH 405 ? ? O  B HOH 611 ? ? 2.00 
10 1 O   B HOH 616 ? ? O  B HOH 620 ? ? 2.00 
11 1 NH1 A ARG 141 ? ? O  A HOH 401 ? ? 2.00 
12 1 O   B HOH 478 ? ? O  B HOH 548 ? ? 2.00 
13 1 O   B HOH 467 ? ? O  B HOH 627 ? ? 2.01 
14 1 O   A HOH 559 ? ? O  A HOH 595 ? ? 2.01 
15 1 OD1 A ASP 247 ? A O  A HOH 402 ? ? 2.03 
16 1 NH2 B ARG 205 ? A O  B HOH 401 ? ? 2.04 
17 1 O   A HOH 424 ? ? O  A HOH 457 ? ? 2.04 
18 1 O   A HOH 416 ? ? O  A HOH 601 ? ? 2.05 
19 1 ND2 B ASN 254 ? A C  B FMT 303 ? ? 2.06 
20 1 O   B HOH 671 ? ? O  B HOH 674 ? ? 2.07 
21 1 O   B HOH 534 ? ? O  B HOH 576 ? ? 2.08 
22 1 O   B HOH 677 ? ? O  B HOH 718 ? ? 2.10 
23 1 O   A HOH 572 ? ? O  A HOH 677 ? ? 2.10 
24 1 O   B HOH 679 ? ? O  B HOH 706 ? ? 2.11 
25 1 O   B HOH 408 ? ? O  B HOH 480 ? ? 2.11 
26 1 O   B HOH 413 ? ? O  B HOH 425 ? ? 2.12 
27 1 O   B HOH 549 ? ? O  B HOH 705 ? ? 2.12 
28 1 OD2 A ASP 247 ? B O  A HOH 403 ? ? 2.13 
29 1 NZ  B LYS 90  ? ? O  B HOH 402 ? ? 2.14 
30 1 O   A HOH 604 ? ? O  A HOH 627 ? ? 2.15 
31 1 O   B HOH 710 ? ? O  B HOH 719 ? ? 2.16 
32 1 O   A HOH 409 ? ? O  A HOH 433 ? ? 2.16 
33 1 O   A HOH 571 ? ? O  A HOH 622 ? ? 2.17 
34 1 O   B HOH 408 ? ? O  B HOH 577 ? ? 2.17 
35 1 O   B HOH 415 ? ? O  B HOH 573 ? ? 2.18 
36 1 O   B HOH 581 ? ? O  B HOH 607 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 611 ? ? 1_555 O B HOH 548 ? ? 4_546 1.98 
2 1 O A HOH 664 ? ? 1_555 O A HOH 700 ? ? 2_555 2.05 
3 1 O A HOH 611 ? ? 1_555 O B HOH 401 ? ? 4_546 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 84  ? ? 76.72   146.01  
2 1 TRP A 87  ? ? 68.14   73.03   
3 1 ALA A 178 ? ? -153.47 -106.42 
4 1 ASP B 84  ? ? 77.15   145.23  
5 1 TRP B 87  ? ? 69.74   72.16   
6 1 ALA B 178 ? ? -152.40 -107.14 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     554 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   P 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 701 ? 5.95 . 
2 1 O ? B HOH 719 ? 5.82 . 
3 1 O ? B HOH 720 ? 6.05 . 
# 
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 MET 13  ? A MET 1   
2  1 Y 1 A HIS 14  ? A HIS 2   
3  1 Y 1 A HIS 15  ? A HIS 3   
4  1 Y 1 A HIS 16  ? A HIS 4   
5  1 Y 1 A HIS 17  ? A HIS 5   
6  1 Y 1 A HIS 18  ? A HIS 6   
7  1 Y 1 A HIS 19  ? A HIS 7   
8  1 Y 1 A GLU 20  ? A GLU 8   
9  1 Y 1 A ASN 21  ? A ASN 9   
10 1 Y 1 A LEU 22  ? A LEU 10  
11 1 Y 1 A TYR 23  ? A TYR 11  
12 1 Y 1 A PHE 24  ? A PHE 12  
13 1 Y 1 A GLN 25  ? A GLN 13  
14 1 Y 1 A GLY 26  ? A GLY 14  
15 1 Y 1 A VAL 27  ? A VAL 15  
16 1 Y 1 A ASP 28  ? A ASP 16  
17 1 Y 1 A SER 29  ? A SER 17  
18 1 Y 1 A SER 30  ? A SER 18  
19 1 Y 1 A GLY 31  ? A GLY 19  
20 1 Y 1 A SER 263 ? A SER 251 
21 1 Y 1 A VAL 264 ? A VAL 252 
22 1 Y 1 A VAL 265 ? A VAL 253 
23 1 Y 1 A GLU 266 ? A GLU 254 
24 1 Y 1 B MET 13  ? B MET 1   
25 1 Y 1 B HIS 14  ? B HIS 2   
26 1 Y 1 B HIS 15  ? B HIS 3   
27 1 Y 1 B HIS 16  ? B HIS 4   
28 1 Y 1 B HIS 17  ? B HIS 5   
29 1 Y 1 B HIS 18  ? B HIS 6   
30 1 Y 1 B HIS 19  ? B HIS 7   
31 1 Y 1 B GLU 20  ? B GLU 8   
32 1 Y 1 B ASN 21  ? B ASN 9   
33 1 Y 1 B LEU 22  ? B LEU 10  
34 1 Y 1 B TYR 23  ? B TYR 11  
35 1 Y 1 B PHE 24  ? B PHE 12  
36 1 Y 1 B GLN 25  ? B GLN 13  
37 1 Y 1 B GLY 26  ? B GLY 14  
38 1 Y 1 B VAL 27  ? B VAL 15  
39 1 Y 1 B ASP 28  ? B ASP 16  
40 1 Y 1 B SER 29  ? B SER 17  
41 1 Y 1 B SER 30  ? B SER 18  
42 1 Y 1 B GLY 31  ? B GLY 19  
43 1 Y 1 B SER 263 ? B SER 251 
44 1 Y 1 B VAL 264 ? B VAL 252 
45 1 Y 1 B VAL 265 ? B VAL 253 
46 1 Y 1 B GLU 266 ? B GLU 254 
# 
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 
A1H8U C13  C  Y N 1   
A1H8U C10  C  Y N 2   
A1H8U C11  C  Y N 3   
A1H8U C1   C  N N 4   
A1H8U C12  C  Y N 5   
A1H8U C2   C  N S 6   
A1H8U C3   C  Y N 7   
A1H8U C4   C  Y N 8   
A1H8U C5   C  Y N 9   
A1H8U C6   C  Y N 10  
A1H8U C7   C  Y N 11  
A1H8U C8   C  Y N 12  
A1H8U C9   C  N N 13  
A1H8U N1   N  N N 14  
A1H8U O1   O  N N 15  
A1H8U O2   O  N N 16  
A1H8U O3   O  N N 17  
A1H8U O4   O  N N 18  
A1H8U O5   O  N N 19  
A1H8U P1   P  N N 20  
A1H8U S1   S  Y N 21  
A1H8U H12  H  N N 22  
A1H8U H10  H  N N 23  
A1H8U H11  H  N N 24  
A1H8U H2   H  N N 25  
A1H8U H3   H  N N 26  
A1H8U H4   H  N N 27  
A1H8U H5   H  N N 28  
A1H8U H6   H  N N 29  
A1H8U H8   H  N N 30  
A1H8U H9   H  N N 31  
A1H8U H1   H  N N 32  
A1H8U H7   H  N N 33  
A1H8U H13  H  N N 34  
A1H8U H14  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
FMT   C    C  N N 123 
FMT   O1   O  N N 124 
FMT   O2   O  N N 125 
FMT   H    H  N N 126 
FMT   HO2  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
HIS   N    N  N N 177 
HIS   CA   C  N S 178 
HIS   C    C  N N 179 
HIS   O    O  N N 180 
HIS   CB   C  N N 181 
HIS   CG   C  Y N 182 
HIS   ND1  N  Y N 183 
HIS   CD2  C  Y N 184 
HIS   CE1  C  Y N 185 
HIS   NE2  N  Y N 186 
HIS   OXT  O  N N 187 
HIS   H    H  N N 188 
HIS   H2   H  N N 189 
HIS   HA   H  N N 190 
HIS   HB2  H  N N 191 
HIS   HB3  H  N N 192 
HIS   HD1  H  N N 193 
HIS   HD2  H  N N 194 
HIS   HE1  H  N N 195 
HIS   HE2  H  N N 196 
HIS   HXT  H  N N 197 
HOH   O    O  N N 198 
HOH   H1   H  N N 199 
HOH   H2   H  N N 200 
ILE   N    N  N N 201 
ILE   CA   C  N S 202 
ILE   C    C  N N 203 
ILE   O    O  N N 204 
ILE   CB   C  N S 205 
ILE   CG1  C  N N 206 
ILE   CG2  C  N N 207 
ILE   CD1  C  N N 208 
ILE   OXT  O  N N 209 
ILE   H    H  N N 210 
ILE   H2   H  N N 211 
ILE   HA   H  N N 212 
ILE   HB   H  N N 213 
ILE   HG12 H  N N 214 
ILE   HG13 H  N N 215 
ILE   HG21 H  N N 216 
ILE   HG22 H  N N 217 
ILE   HG23 H  N N 218 
ILE   HD11 H  N N 219 
ILE   HD12 H  N N 220 
ILE   HD13 H  N N 221 
ILE   HXT  H  N N 222 
LEU   N    N  N N 223 
LEU   CA   C  N S 224 
LEU   C    C  N N 225 
LEU   O    O  N N 226 
LEU   CB   C  N N 227 
LEU   CG   C  N N 228 
LEU   CD1  C  N N 229 
LEU   CD2  C  N N 230 
LEU   OXT  O  N N 231 
LEU   H    H  N N 232 
LEU   H2   H  N N 233 
LEU   HA   H  N N 234 
LEU   HB2  H  N N 235 
LEU   HB3  H  N N 236 
LEU   HG   H  N N 237 
LEU   HD11 H  N N 238 
LEU   HD12 H  N N 239 
LEU   HD13 H  N N 240 
LEU   HD21 H  N N 241 
LEU   HD22 H  N N 242 
LEU   HD23 H  N N 243 
LEU   HXT  H  N N 244 
LYS   N    N  N N 245 
LYS   CA   C  N S 246 
LYS   C    C  N N 247 
LYS   O    O  N N 248 
LYS   CB   C  N N 249 
LYS   CG   C  N N 250 
LYS   CD   C  N N 251 
LYS   CE   C  N N 252 
LYS   NZ   N  N N 253 
LYS   OXT  O  N N 254 
LYS   H    H  N N 255 
LYS   H2   H  N N 256 
LYS   HA   H  N N 257 
LYS   HB2  H  N N 258 
LYS   HB3  H  N N 259 
LYS   HG2  H  N N 260 
LYS   HG3  H  N N 261 
LYS   HD2  H  N N 262 
LYS   HD3  H  N N 263 
LYS   HE2  H  N N 264 
LYS   HE3  H  N N 265 
LYS   HZ1  H  N N 266 
LYS   HZ2  H  N N 267 
LYS   HZ3  H  N N 268 
LYS   HXT  H  N N 269 
MET   N    N  N N 270 
MET   CA   C  N S 271 
MET   C    C  N N 272 
MET   O    O  N N 273 
MET   CB   C  N N 274 
MET   CG   C  N N 275 
MET   SD   S  N N 276 
MET   CE   C  N N 277 
MET   OXT  O  N N 278 
MET   H    H  N N 279 
MET   H2   H  N N 280 
MET   HA   H  N N 281 
MET   HB2  H  N N 282 
MET   HB3  H  N N 283 
MET   HG2  H  N N 284 
MET   HG3  H  N N 285 
MET   HE1  H  N N 286 
MET   HE2  H  N N 287 
MET   HE3  H  N N 288 
MET   HXT  H  N N 289 
PHE   N    N  N N 290 
PHE   CA   C  N S 291 
PHE   C    C  N N 292 
PHE   O    O  N N 293 
PHE   CB   C  N N 294 
PHE   CG   C  Y N 295 
PHE   CD1  C  Y N 296 
PHE   CD2  C  Y N 297 
PHE   CE1  C  Y N 298 
PHE   CE2  C  Y N 299 
PHE   CZ   C  Y N 300 
PHE   OXT  O  N N 301 
PHE   H    H  N N 302 
PHE   H2   H  N N 303 
PHE   HA   H  N N 304 
PHE   HB2  H  N N 305 
PHE   HB3  H  N N 306 
PHE   HD1  H  N N 307 
PHE   HD2  H  N N 308 
PHE   HE1  H  N N 309 
PHE   HE2  H  N N 310 
PHE   HZ   H  N N 311 
PHE   HXT  H  N N 312 
PRO   N    N  N N 313 
PRO   CA   C  N S 314 
PRO   C    C  N N 315 
PRO   O    O  N N 316 
PRO   CB   C  N N 317 
PRO   CG   C  N N 318 
PRO   CD   C  N N 319 
PRO   OXT  O  N N 320 
PRO   H    H  N N 321 
PRO   HA   H  N N 322 
PRO   HB2  H  N N 323 
PRO   HB3  H  N N 324 
PRO   HG2  H  N N 325 
PRO   HG3  H  N N 326 
PRO   HD2  H  N N 327 
PRO   HD3  H  N N 328 
PRO   HXT  H  N N 329 
SER   N    N  N N 330 
SER   CA   C  N S 331 
SER   C    C  N N 332 
SER   O    O  N N 333 
SER   CB   C  N N 334 
SER   OG   O  N N 335 
SER   OXT  O  N N 336 
SER   H    H  N N 337 
SER   H2   H  N N 338 
SER   HA   H  N N 339 
SER   HB2  H  N N 340 
SER   HB3  H  N N 341 
SER   HG   H  N N 342 
SER   HXT  H  N N 343 
THR   N    N  N N 344 
THR   CA   C  N S 345 
THR   C    C  N N 346 
THR   O    O  N N 347 
THR   CB   C  N R 348 
THR   OG1  O  N N 349 
THR   CG2  C  N N 350 
THR   OXT  O  N N 351 
THR   H    H  N N 352 
THR   H2   H  N N 353 
THR   HA   H  N N 354 
THR   HB   H  N N 355 
THR   HG1  H  N N 356 
THR   HG21 H  N N 357 
THR   HG22 H  N N 358 
THR   HG23 H  N N 359 
THR   HXT  H  N N 360 
TRP   N    N  N N 361 
TRP   CA   C  N S 362 
TRP   C    C  N N 363 
TRP   O    O  N N 364 
TRP   CB   C  N N 365 
TRP   CG   C  Y N 366 
TRP   CD1  C  Y N 367 
TRP   CD2  C  Y N 368 
TRP   NE1  N  Y N 369 
TRP   CE2  C  Y N 370 
TRP   CE3  C  Y N 371 
TRP   CZ2  C  Y N 372 
TRP   CZ3  C  Y N 373 
TRP   CH2  C  Y N 374 
TRP   OXT  O  N N 375 
TRP   H    H  N N 376 
TRP   H2   H  N N 377 
TRP   HA   H  N N 378 
TRP   HB2  H  N N 379 
TRP   HB3  H  N N 380 
TRP   HD1  H  N N 381 
TRP   HE1  H  N N 382 
TRP   HE3  H  N N 383 
TRP   HZ2  H  N N 384 
TRP   HZ3  H  N N 385 
TRP   HH2  H  N N 386 
TRP   HXT  H  N N 387 
TYR   N    N  N N 388 
TYR   CA   C  N S 389 
TYR   C    C  N N 390 
TYR   O    O  N N 391 
TYR   CB   C  N N 392 
TYR   CG   C  Y N 393 
TYR   CD1  C  Y N 394 
TYR   CD2  C  Y N 395 
TYR   CE1  C  Y N 396 
TYR   CE2  C  Y N 397 
TYR   CZ   C  Y N 398 
TYR   OH   O  N N 399 
TYR   OXT  O  N N 400 
TYR   H    H  N N 401 
TYR   H2   H  N N 402 
TYR   HA   H  N N 403 
TYR   HB2  H  N N 404 
TYR   HB3  H  N N 405 
TYR   HD1  H  N N 406 
TYR   HD2  H  N N 407 
TYR   HE1  H  N N 408 
TYR   HE2  H  N N 409 
TYR   HH   H  N N 410 
TYR   HXT  H  N N 411 
VAL   N    N  N N 412 
VAL   CA   C  N S 413 
VAL   C    C  N N 414 
VAL   O    O  N N 415 
VAL   CB   C  N N 416 
VAL   CG1  C  N N 417 
VAL   CG2  C  N N 418 
VAL   OXT  O  N N 419 
VAL   H    H  N N 420 
VAL   H2   H  N N 421 
VAL   HA   H  N N 422 
VAL   HB   H  N N 423 
VAL   HG11 H  N N 424 
VAL   HG12 H  N N 425 
VAL   HG13 H  N N 426 
VAL   HG21 H  N N 427 
VAL   HG22 H  N N 428 
VAL   HG23 H  N N 429 
VAL   HXT  H  N N 430 
ZN    ZN   ZN N N 431 
# 
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 
A1H8U C1  O1   doub N N 1   
A1H8U C2  N1   sing N N 2   
A1H8U C4  C3   doub Y N 3   
A1H8U C5  C4   sing Y N 4   
A1H8U C6  C5   doub Y N 5   
A1H8U C7  C6   sing Y N 6   
A1H8U C8  C7   doub Y N 7   
A1H8U O2  C8   sing N N 8   
A1H8U C3  C2   sing N N 9   
A1H8U P1  C2   sing N N 10  
A1H8U O3  P1   doub N N 11  
A1H8U O4  P1   sing N N 12  
A1H8U O5  P1   sing N N 13  
A1H8U N1  C1   sing N N 14  
A1H8U C9  C1   sing N N 15  
A1H8U C10 C9   sing N N 16  
A1H8U C11 C10  doub Y N 17  
A1H8U S1  C11  sing Y N 18  
A1H8U C12 S1   sing Y N 19  
A1H8U C13 C12  doub Y N 20  
A1H8U C3  C8   sing Y N 21  
A1H8U C10 C13  sing Y N 22  
A1H8U C13 H12  sing N N 23  
A1H8U C11 H10  sing N N 24  
A1H8U C12 H11  sing N N 25  
A1H8U C2  H2   sing N N 26  
A1H8U C4  H3   sing N N 27  
A1H8U C5  H4   sing N N 28  
A1H8U C6  H5   sing N N 29  
A1H8U C7  H6   sing N N 30  
A1H8U C9  H8   sing N N 31  
A1H8U C9  H9   sing N N 32  
A1H8U N1  H1   sing N N 33  
A1H8U O2  H7   sing N N 34  
A1H8U O4  H13  sing N N 35  
A1H8U O5  H14  sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
FMT   C   O1   doub N N 119 
FMT   C   O2   sing N N 120 
FMT   C   H    sing N N 121 
FMT   O2  HO2  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Federal Ministry for Education and Research' Germany 01KI2114  1 
'German Research Foundation (DFG)'                   Germany 458246365 2 
'Max Planck Society'                                 Germany ?         3 
'Swedish Research Council'                           Sweden  2013-8804 4 
'Uppsala Antibiotic Center'                          Sweden  ?         5 
# 
_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   5YD7 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9F0S 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009852 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008378 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012619 
_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]   0.019386 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN  ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU   A 1 20  ? 35.54537  -14.86231 13.25451  1.000 39.14218 ?  32  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 20  ? 36.40360  -13.76343 12.82662  1.000 30.77700 ?  32  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 20  ? 35.58557  -12.49719 12.57992  1.000 28.45293 ?  32  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 20  ? 35.80772  -11.48029 13.22321  1.000 31.43904 ?  32  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 20  ? 37.15444  -14.13624 11.55880  1.000 28.43729 ?  32  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 20  ? 38.49601  -13.44914 11.41646  1.000 39.93241 ?  32  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 20  ? 39.14826  -13.74704 10.08079  1.000 45.28154 ?  32  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 20  ? 39.39088  -14.93933 9.78692   1.000 51.75198 ?  32  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 20  ? 39.41949  -12.79138 9.32207   1.000 51.05425 ?  32  GLU   A OE2 1 
ATOM   10   N  N   . TYR   A 1 21  ? 34.65541  -12.55569 11.63267  1.000 32.73711 ?  33  TYR   A N   1 
ATOM   11   C  CA  . TYR   A 1 21  ? 33.76726  -11.41872 11.40944  1.000 23.96487 ?  33  TYR   A CA  1 
ATOM   12   C  C   . TYR   A 1 21  ? 32.80812  -11.28469 12.58460  1.000 22.23570 ?  33  TYR   A C   1 
ATOM   13   O  O   . TYR   A 1 21  ? 32.21065  -12.27935 13.00724  1.000 28.55593 ?  33  TYR   A O   1 
ATOM   14   C  CB  . TYR   A 1 21  ? 32.97074  -11.60003 10.12266  1.000 22.73307 ?  33  TYR   A CB  1 
ATOM   15   C  CG  . TYR   A 1 21  ? 32.42406  -10.29491 9.57937   1.000 17.10081 ?  33  TYR   A CG  1 
ATOM   16   C  CD1 . TYR   A 1 21  ? 33.22727  -9.45949  8.82300   1.000 18.09102 ?  33  TYR   A CD1 1 
ATOM   17   C  CD2 . TYR   A 1 21  ? 31.12194  -9.88853  9.85215   1.000 18.26985 ?  33  TYR   A CD2 1 
ATOM   18   C  CE1 . TYR   A 1 21  ? 32.74253  -8.25671  8.31941   1.000 17.41712 ?  33  TYR   A CE1 1 
ATOM   19   C  CE2 . TYR   A 1 21  ? 30.62333  -8.68135  9.34618   1.000 16.42283 ?  33  TYR   A CE2 1 
ATOM   20   C  CZ  . TYR   A 1 21  ? 31.44849  -7.87605  8.59903   1.000 15.88357 ?  33  TYR   A CZ  1 
ATOM   21   O  OH  . TYR   A 1 21  ? 30.97064  -6.68842  8.08968   1.000 16.67399 ?  33  TYR   A OH  1 
ATOM   22   N  N   . PRO   A 1 22  ? 32.61918  -10.08500 13.12642  1.000 21.42705 ?  34  PRO   A N   1 
ATOM   23   C  CA  . PRO   A 1 22  ? 31.78035  -9.94667  14.32042  1.000 25.02361 ?  34  PRO   A CA  1 
ATOM   24   C  C   . PRO   A 1 22  ? 30.30308  -10.11579 14.00663  1.000 32.53776 ?  34  PRO   A C   1 
ATOM   25   O  O   . PRO   A 1 22  ? 29.83369  -9.80389  12.90696  1.000 28.42845 ?  34  PRO   A O   1 
ATOM   26   C  CB  . PRO   A 1 22  ? 32.08245  -8.52692  14.80920  1.000 29.12554 ?  34  PRO   A CB  1 
ATOM   27   C  CG  . PRO   A 1 22  ? 32.57946  -7.80701  13.60486  1.000 21.11303 ?  34  PRO   A CG  1 
ATOM   28   C  CD  . PRO   A 1 22  ? 33.29508  -8.83115  12.76443  1.000 22.22120 ?  34  PRO   A CD  1 
ATOM   29   N  N   . THR   A 1 23  ? 29.57703  -10.61798 15.00344  1.000 32.17200 ?  35  THR   A N   1 
ATOM   30   C  CA  . THR   A 1 23  ? 28.14263  -10.88401 14.96492  1.000 27.04399 ?  35  THR   A CA  1 
ATOM   31   C  C   . THR   A 1 23  ? 27.45153  -10.08026 16.06592  1.000 27.85761 ?  35  THR   A C   1 
ATOM   32   O  O   . THR   A 1 23  ? 28.09943  -9.37830  16.84435  1.000 34.87263 ?  35  THR   A O   1 
ATOM   33   C  CB  . THR   A 1 23  ? 27.87361  -12.38046 15.14247  1.000 39.37588 ?  35  THR   A CB  1 
ATOM   34   O  OG1 . THR   A 1 23  ? 28.32327  -12.78987 16.43907  1.000 40.92398 ?  35  THR   A OG1 1 
ATOM   35   C  CG2 . THR   A 1 23  ? 28.61961  -13.17851 14.09569  1.000 32.27505 ?  35  THR   A CG2 1 
ATOM   36   N  N   . VAL   A 1 24  ? 26.11725  -10.20355 16.12996  1.000 34.77335 ?  36  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 24  ? 25.32168  -9.43535  17.09393  1.000 25.61167 ?  36  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 24  ? 25.83291  -9.63748  18.51457  1.000 41.33554 ?  36  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 24  ? 26.00461  -8.67675  19.27600  1.000 44.16530 ?  36  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 24  ? 23.82511  -9.78521  16.97062  1.000 38.13608 ?  36  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 24  ? 23.11373  -9.56542  18.30102  1.000 38.88713 ?  36  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 24  ? 23.15795  -8.94636  15.88422  1.000 25.34998 ?  36  VAL   A CG2 1 
ATOM   43   N  N   . SER   A 1 25  ? 26.08487  -10.89226 18.89485  1.000 41.57242 ?  37  SER   A N   1 
ATOM   44   C  CA  . SER   A 1 25  ? 26.42936  -11.18049 20.28299  1.000 39.82936 ?  37  SER   A CA  1 
ATOM   45   C  C   . SER   A 1 25  ? 27.77858  -10.60513 20.69868  1.000 45.57553 ?  37  SER   A C   1 
ATOM   46   O  O   . SER   A 1 25  ? 28.03095  -10.47437 21.90224  1.000 48.93024 ?  37  SER   A O   1 
ATOM   47   C  CB  . SER   A 1 25  ? 26.34961  -12.68386 20.55677  1.000 45.72064 ?  37  SER   A CB  1 
ATOM   48   O  OG  . SER   A 1 25  ? 25.22068  -13.24980 19.90870  1.000 50.47721 ?  37  SER   A OG  1 
ATOM   49   N  N   . GLU   A 1 26  ? 28.64650  -10.25135 19.74662  1.000 34.38234 ?  38  GLU   A N   1 
ATOM   50   C  CA  . GLU   A 1 26  ? 29.89738  -9.58520  20.08661  1.000 37.12481 ?  38  GLU   A CA  1 
ATOM   51   C  C   . GLU   A 1 26  ? 29.77031  -8.07218  20.17414  1.000 36.29808 ?  38  GLU   A C   1 
ATOM   52   O  O   . GLU   A 1 26  ? 30.74034  -7.41146  20.56022  1.000 43.77791 ?  38  GLU   A O   1 
ATOM   53   C  CB  . GLU   A 1 26  ? 31.01633  -9.91578  19.08738  1.000 42.57944 ?  38  GLU   A CB  1 
ATOM   54   C  CG  . GLU   A 1 26  ? 31.62031  -11.30398 19.21095  1.000 43.78549 ?  38  GLU   A CG  1 
ATOM   55   C  CD  . GLU   A 1 26  ? 30.73365  -12.37918 18.63118  1.000 47.20704 ?  38  GLU   A CD  1 
ATOM   56   O  OE1 . GLU   A 1 26  ? 30.32472  -12.23483 17.46014  1.000 50.81268 ?  38  GLU   A OE1 1 
ATOM   57   O  OE2 . GLU   A 1 26  ? 30.44471  -13.36473 19.34009  1.000 53.16690 ?  38  GLU   A OE2 1 
ATOM   58   N  N   . ILE   A 1 27  ? 28.62584  -7.50462  19.81685  1.000 35.43885 ?  39  ILE   A N   1 
ATOM   59   C  CA  . ILE   A 1 27  ? 28.45961  -6.06170  19.72391  1.000 37.16177 ?  39  ILE   A CA  1 
ATOM   60   C  C   . ILE   A 1 27  ? 27.30227  -5.64749  20.61875  1.000 38.19087 ?  39  ILE   A C   1 
ATOM   61   O  O   . ILE   A 1 27  ? 26.13736  -5.77232  20.24201  1.000 45.19400 ?  39  ILE   A O   1 
ATOM   62   C  CB  . ILE   A 1 27  ? 28.21559  -5.61366  18.27242  1.000 31.56577 ?  39  ILE   A CB  1 
ATOM   63   C  CG1 . ILE   A 1 27  ? 29.24847  -6.23229  17.33825  1.000 30.54753 ?  39  ILE   A CG1 1 
ATOM   64   C  CG2 . ILE   A 1 27  ? 28.23384  -4.09324  18.18688  1.000 29.19249 ?  39  ILE   A CG2 1 
ATOM   65   C  CD1 . ILE   A 1 27  ? 29.01339  -5.87603  15.90362  1.000 22.97224 ?  39  ILE   A CD1 1 
ATOM   66   N  N   . PRO   A 1 28  ? 27.58521  -5.14086  21.81400  1.000 40.80401 ?  40  PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 28  ? 26.52611  -4.50485  22.60044  1.000 45.64265 ?  40  PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 28  ? 25.96047  -3.31991  21.83233  1.000 47.38936 ?  40  PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 28  ? 26.69941  -2.55619  21.20505  1.000 37.27765 ?  40  PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 28  ? 27.25448  -4.05241  23.87022  1.000 41.91026 ?  40  PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 28  ? 28.45153  -4.94518  23.95882  1.000 47.57542 ?  40  PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 28  ? 28.86567  -5.18661  22.53729  1.000 43.63911 ?  40  PRO   A CD  1 
ATOM   73   N  N   . VAL   A 1 29  ? 24.63030  -3.19008  21.85993  1.000 50.00762 ?  41  VAL   A N   1 
ATOM   74   C  CA  . VAL   A 1 29  ? 23.98296  -2.08989  21.15665  1.000 47.29451 ?  41  VAL   A CA  1 
ATOM   75   C  C   . VAL   A 1 29  ? 24.58810  -0.76999  21.60749  1.000 43.27294 ?  41  VAL   A C   1 
ATOM   76   O  O   . VAL   A 1 29  ? 24.90149  -0.57576  22.78686  1.000 38.08594 ?  41  VAL   A O   1 
ATOM   77   C  CB  . VAL   A 1 29  ? 22.45760  -2.12811  21.35959  1.000 51.37809 ?  41  VAL   A CB  1 
ATOM   78   C  CG1 . VAL   A 1 29  ? 21.76269  -1.26047  20.31669  1.000 39.78167 ?  41  VAL   A CG1 1 
ATOM   79   C  CG2 . VAL   A 1 29  ? 21.95402  -3.55562  21.27599  1.000 44.12613 ?  41  VAL   A CG2 1 
ATOM   80   N  N   . GLY   A 1 30  ? 24.77773  0.13657   20.65134  1.000 39.43691 ?  42  GLY   A N   1 
ATOM   81   C  CA  . GLY   A 1 30  ? 25.48813  1.36660   20.88631  1.000 32.43626 ?  42  GLY   A CA  1 
ATOM   82   C  C   . GLY   A 1 30  ? 26.96193  1.31508   20.54895  1.000 25.09913 ?  42  GLY   A C   1 
ATOM   83   O  O   . GLY   A 1 30  ? 27.58612  2.37453   20.41414  1.000 30.15518 ?  42  GLY   A O   1 
ATOM   84   N  N   . GLU   A 1 31  ? 27.53782  0.12252   20.42020  1.000 25.65712 ?  43  GLU   A N   1 
ATOM   85   C  CA  A GLU   A 1 31  ? 28.93864  -0.03888  20.06073  0.547 29.66458 ?  43  GLU   A CA  1 
ATOM   86   C  CA  B GLU   A 1 31  ? 28.93748  -0.04685  20.06180  0.453 29.65974 ?  43  GLU   A CA  1 
ATOM   87   C  C   . GLU   A 1 31  ? 29.07500  -0.30123  18.56571  1.000 19.38949 ?  43  GLU   A C   1 
ATOM   88   O  O   . GLU   A 1 31  ? 28.12290  -0.69936  17.88348  1.000 22.85460 ?  43  GLU   A O   1 
ATOM   89   C  CB  A GLU   A 1 31  ? 29.59018  -1.18086  20.84941  0.547 31.00850 ?  43  GLU   A CB  1 
ATOM   90   C  CB  B GLU   A 1 31  ? 29.56559  -1.20889  20.83627  0.453 31.03407 ?  43  GLU   A CB  1 
ATOM   91   C  CG  A GLU   A 1 31  ? 29.61051  -0.97878  22.36138  0.547 34.53981 ?  43  GLU   A CG  1 
ATOM   92   C  CG  B GLU   A 1 31  ? 29.57320  -1.02473  22.34447  0.453 34.52677 ?  43  GLU   A CG  1 
ATOM   93   C  CD  A GLU   A 1 31  ? 30.38637  -2.06383  23.09137  0.547 36.97553 ?  43  GLU   A CD  1 
ATOM   94   C  CD  B GLU   A 1 31  ? 29.53998  0.43329   22.74939  0.453 32.54430 ?  43  GLU   A CD  1 
ATOM   95   O  OE1 A GLU   A 1 31  ? 31.22726  -2.73311  22.45565  0.547 36.82277 ?  43  GLU   A OE1 1 
ATOM   96   O  OE1 B GLU   A 1 31  ? 30.58863  1.10206   22.64929  0.453 30.86379 ?  43  GLU   A OE1 1 
ATOM   97   O  OE2 A GLU   A 1 31  ? 30.15685  -2.24676  24.30580  0.547 37.75314 ?  43  GLU   A OE2 1 
ATOM   98   O  OE2 B GLU   A 1 31  ? 28.46481  0.90873   23.17139  0.453 37.63977 ?  43  GLU   A OE2 1 
ATOM   99   N  N   . VAL   A 1 32  ? 30.28251  -0.06612  18.06061  1.000 18.89706 ?  44  VAL   A N   1 
ATOM   100  C  CA  . VAL   A 1 32  ? 30.60588  -0.27905  16.65581  1.000 15.83487 ?  44  VAL   A CA  1 
ATOM   101  C  C   . VAL   A 1 32  ? 31.93010  -1.02409  16.59132  1.000 19.80613 ?  44  VAL   A C   1 
ATOM   102  O  O   . VAL   A 1 32  ? 32.88567  -0.66429  17.29202  1.000 20.07218 ?  44  VAL   A O   1 
ATOM   103  C  CB  . VAL   A 1 32  ? 30.68598  1.05316   15.88121  1.000 15.54667 ?  44  VAL   A CB  1 
ATOM   104  C  CG1 . VAL   A 1 32  ? 31.22086  0.82705   14.46748  1.000 16.45647 ?  44  VAL   A CG1 1 
ATOM   105  C  CG2 . VAL   A 1 32  ? 29.32941  1.73207   15.82790  1.000 18.67991 ?  44  VAL   A CG2 1 
ATOM   106  N  N   . ARG   A 1 33  ? 31.98066  -2.07150  15.77861  1.000 14.56738 ?  45  ARG   A N   1 
ATOM   107  C  CA  . ARG   A 1 33  ? 33.20286  -2.80826  15.50467  1.000 15.66736 ?  45  ARG   A CA  1 
ATOM   108  C  C   . ARG   A 1 33  ? 33.67657  -2.49218  14.08928  1.000 15.51298 ?  45  ARG   A C   1 
ATOM   109  O  O   . ARG   A 1 33  ? 32.86948  -2.26495  13.17452  1.000 15.12575 ?  45  ARG   A O   1 
ATOM   110  C  CB  . ARG   A 1 33  ? 32.95195  -4.31977  15.55452  1.000 20.01146 ?  45  ARG   A CB  1 
ATOM   111  C  CG  . ARG   A 1 33  ? 32.94910  -5.00448  16.91884  1.000 31.70983 ?  45  ARG   A CG  1 
ATOM   112  C  CD  . ARG   A 1 33  ? 33.77025  -4.31160  17.99033  1.000 36.41478 ?  45  ARG   A CD  1 
ATOM   113  N  NE  . ARG   A 1 33  ? 33.52031  -4.92493  19.29258  1.000 47.07011 ?  45  ARG   A NE  1 
ATOM   114  C  CZ  . ARG   A 1 33  ? 33.06862  -4.28393  20.36267  1.000 47.69582 ?  45  ARG   A CZ  1 
ATOM   115  N  NH1 . ARG   A 1 33  ? 32.81403  -2.98561  20.33662  1.000 39.81061 ?  45  ARG   A NH1 1 
ATOM   116  N  NH2 . ARG   A 1 33  ? 32.86621  -4.96480  21.48814  1.000 51.21058 ?  45  ARG   A NH2 1 
ATOM   117  N  N   . LEU   A 1 34  ? 34.98654  -2.52617  13.89378  1.000 14.82624 ?  46  LEU   A N   1 
ATOM   118  C  CA  . LEU   A 1 34  ? 35.57716  -2.38664  12.57391  1.000 14.43239 ?  46  LEU   A CA  1 
ATOM   119  C  C   . LEU   A 1 34  ? 36.25164  -3.69520  12.20685  1.000 16.65181 ?  46  LEU   A C   1 
ATOM   120  O  O   . LEU   A 1 34  ? 36.80915  -4.37605  13.07162  1.000 17.94933 ?  46  LEU   A O   1 
ATOM   121  C  CB  . LEU   A 1 34  ? 36.62011  -1.26980  12.55041  1.000 15.57492 ?  46  LEU   A CB  1 
ATOM   122  C  CG  . LEU   A 1 34  ? 36.17680  0.09952   13.05404  1.000 14.85107 ?  46  LEU   A CG  1 
ATOM   123  C  CD1 . LEU   A 1 34  ? 37.37220  1.05345   12.96543  1.000 18.54996 ?  46  LEU   A CD1 1 
ATOM   124  C  CD2 . LEU   A 1 34  ? 34.98344  0.65109   12.28190  1.000 14.35262 ?  46  LEU   A CD2 1 
ATOM   125  N  N   . TYR   A 1 35  ? 36.19802  -4.05808  10.93248  1.000 15.98229 ?  47  TYR   A N   1 
ATOM   126  C  CA  . TYR   A 1 35  ? 36.78932  -5.30225  10.45645  1.000 14.65435 ?  47  TYR   A CA  1 
ATOM   127  C  C   . TYR   A 1 35  ? 37.59697  -4.99349  9.20891   1.000 16.20132 ?  47  TYR   A C   1 
ATOM   128  O  O   . TYR   A 1 35  ? 37.03353  -4.54601  8.20839   1.000 18.25002 ?  47  TYR   A O   1 
ATOM   129  C  CB  . TYR   A 1 35  ? 35.69249  -6.32219  10.13289  1.000 16.77343 ?  47  TYR   A CB  1 
ATOM   130  C  CG  . TYR   A 1 35  ? 36.21719  -7.63400  9.59047   1.000 17.99848 ?  47  TYR   A CG  1 
ATOM   131  C  CD1 . TYR   A 1 35  ? 36.61283  -8.64533  10.44861  1.000 20.21632 ?  47  TYR   A CD1 1 
ATOM   132  C  CD2 . TYR   A 1 35  ? 36.31108  -7.85943  8.22212   1.000 23.93890 ?  47  TYR   A CD2 1 
ATOM   133  C  CE1 . TYR   A 1 35  ? 37.09162  -9.84559  9.96692   1.000 28.07494 ?  47  TYR   A CE1 1 
ATOM   134  C  CE2 . TYR   A 1 35  ? 36.78929  -9.06606  7.72901   1.000 25.62137 ?  47  TYR   A CE2 1 
ATOM   135  C  CZ  . TYR   A 1 35  ? 37.17583  -10.05376 8.61030   1.000 29.82188 ?  47  TYR   A CZ  1 
ATOM   136  O  OH  . TYR   A 1 35  ? 37.65876  -11.26266 8.13846   1.000 30.16253 ?  47  TYR   A OH  1 
ATOM   137  N  N   . GLN   A 1 36  ? 38.90376  -5.24821  9.24792   1.000 14.07744 ?  48  GLN   A N   1 
ATOM   138  C  CA  . GLN   A 1 36  ? 39.75496  -4.96866  8.09782   1.000 18.37261 ?  48  GLN   A CA  1 
ATOM   139  C  C   . GLN   A 1 36  ? 39.60194  -6.05878  7.04552   1.000 22.02455 ?  48  GLN   A C   1 
ATOM   140  O  O   . GLN   A 1 36  ? 39.91426  -7.22738  7.29391   1.000 22.88252 ?  48  GLN   A O   1 
ATOM   141  C  CB  . GLN   A 1 36  ? 41.21434  -4.79902  8.50740   1.000 22.30603 ?  48  GLN   A CB  1 
ATOM   142  C  CG  . GLN   A 1 36  ? 42.06623  -4.23929  7.37301   1.000 23.82312 ?  48  GLN   A CG  1 
ATOM   143  C  CD  . GLN   A 1 36  ? 43.26167  -3.43862  7.84752   1.000 35.85055 ?  48  GLN   A CD  1 
ATOM   144  O  OE1 . GLN   A 1 36  ? 43.94419  -3.81642  8.79690   1.000 39.30860 ?  48  GLN   A OE1 1 
ATOM   145  N  NE2 . GLN   A 1 36  ? 43.51880  -2.31789  7.18272   1.000 35.74398 ?  48  GLN   A NE2 1 
ATOM   146  N  N   . ILE   A 1 37  ? 39.11333  -5.67619  5.87152   1.000 17.83279 ?  49  ILE   A N   1 
ATOM   147  C  CA  . ILE   A 1 37  ? 38.89866  -6.61883  4.77711   1.000 20.04447 ?  49  ILE   A CA  1 
ATOM   148  C  C   . ILE   A 1 37  ? 40.13986  -6.75372  3.91024   1.000 23.05890 ?  49  ILE   A C   1 
ATOM   149  O  O   . ILE   A 1 37  ? 40.47261  -7.85169  3.45133   1.000 27.47156 ?  49  ILE   A O   1 
ATOM   150  C  CB  . ILE   A 1 37  ? 37.69044  -6.14349  3.95321   1.000 19.24930 ?  49  ILE   A CB  1 
ATOM   151  C  CG1 . ILE   A 1 37  ? 36.45958  -6.11078  4.83659   1.000 20.88122 ?  49  ILE   A CG1 1 
ATOM   152  C  CG2 . ILE   A 1 37  ? 37.46685  -7.04185  2.74251   1.000 24.32292 ?  49  ILE   A CG2 1 
ATOM   153  C  CD1 . ILE   A 1 37  ? 35.45927  -5.14160  4.36430   1.000 20.00579 ?  49  ILE   A CD1 1 
ATOM   154  N  N   . ALA   A 1 38  ? 40.82323  -5.64366  3.67976   1.000 23.70673 ?  50  ALA   A N   1 
ATOM   155  C  CA  . ALA   A 1 38  ? 42.03058  -5.59985  2.87405   1.000 21.38750 ?  50  ALA   A CA  1 
ATOM   156  C  C   . ALA   A 1 38  ? 42.78496  -4.33820  3.25350   1.000 26.66340 ?  50  ALA   A C   1 
ATOM   157  O  O   . ALA   A 1 38  ? 42.33878  -3.55478  4.09751   1.000 26.68701 ?  50  ALA   A O   1 
ATOM   158  C  CB  . ALA   A 1 38  ? 41.70095  -5.63131  1.37805   1.000 25.04381 ?  50  ALA   A CB  1 
ATOM   159  N  N   . ASP   A 1 39  ? 43.94215  -4.15049  2.63205   1.000 25.78972 ?  51  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 39  ? 44.71061  -2.93372  2.83934   1.000 24.33703 ?  51  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 39  ? 43.84570  -1.71938  2.52727   1.000 23.87772 ?  51  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 39  ? 43.36416  -1.55759  1.40225   1.000 23.72462 ?  51  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 39  ? 45.94460  -2.95181  1.93672   1.000 32.39612 ?  51  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 39  ? 46.82722  -1.73138  2.13004   1.000 42.61446 ?  51  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 39  ? 46.69066  -1.04749  3.16868   1.000 44.37173 ?  51  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 39  ? 47.66552  -1.45711  1.24327   1.000 53.32861 ?  51  ASP   A OD2 1 
ATOM   167  N  N   . GLY   A 1 40  ? 43.60951  -0.89716  3.54683   1.000 22.12599 ?  52  GLY   A N   1 
ATOM   168  C  CA  . GLY   A 1 40  ? 42.85360  0.32749   3.38793   1.000 21.17630 ?  52  GLY   A CA  1 
ATOM   169  C  C   . GLY   A 1 40  ? 41.35857  0.16626   3.23536   1.000 18.76845 ?  52  GLY   A C   1 
ATOM   170  O  O   . GLY   A 1 40  ? 40.69480  1.13121   2.83350   1.000 18.30405 ?  52  GLY   A O   1 
ATOM   171  N  N   . VAL   A 1 41  ? 40.80135  -1.01186  3.51634   1.000 16.14077 ?  53  VAL   A N   1 
ATOM   172  C  CA  . VAL   A 1 41  ? 39.36759  -1.23891  3.37488   1.000 14.88011 ?  53  VAL   A CA  1 
ATOM   173  C  C   . VAL   A 1 41  ? 38.87358  -1.94304  4.62286   1.000 18.35597 ?  53  VAL   A C   1 
ATOM   174  O  O   . VAL   A 1 41  ? 39.35044  -3.03650  4.95443   1.000 17.76617 ?  53  VAL   A O   1 
ATOM   175  C  CB  . VAL   A 1 41  ? 39.01176  -2.07530  2.13493   1.000 16.21367 ?  53  VAL   A CB  1 
ATOM   176  C  CG1 . VAL   A 1 41  ? 37.50506  -2.16518  1.99448   1.000 16.85751 ?  53  VAL   A CG1 1 
ATOM   177  C  CG2 . VAL   A 1 41  ? 39.66099  -1.49848  0.88436   1.000 17.63330 ?  53  VAL   A CG2 1 
ATOM   178  N  N   . TRP   A 1 42  ? 37.90364  -1.33673  5.29793   1.000 12.40900 ?  54  TRP   A N   1 
ATOM   179  C  CA  . TRP   A 1 42  ? 37.26308  -1.93744  6.44546   1.000 14.88177 ?  54  TRP   A CA  1 
ATOM   180  C  C   . TRP   A 1 42  ? 35.76482  -1.96473  6.22175   1.000 14.81808 ?  54  TRP   A C   1 
ATOM   181  O  O   . TRP   A 1 42  ? 35.21817  -1.15820  5.46386   1.000 12.47350 ?  54  TRP   A O   1 
ATOM   182  C  CB  . TRP   A 1 42  ? 37.50219  -1.10567  7.70368   1.000 15.36843 ?  54  TRP   A CB  1 
ATOM   183  C  CG  . TRP   A 1 42  ? 38.92394  -0.87178  8.08226   1.000 14.78293 ?  54  TRP   A CG  1 
ATOM   184  C  CD1 . TRP   A 1 42  ? 39.61800  -1.51725  9.06930   1.000 16.86670 ?  54  TRP   A CD1 1 
ATOM   185  C  CD2 . TRP   A 1 42  ? 39.81570  0.09890   7.52716   1.000 13.05807 ?  54  TRP   A CD2 1 
ATOM   186  N  NE1 . TRP   A 1 42  ? 40.89159  -1.01130  9.15432   1.000 18.51503 ?  54  TRP   A NE1 1 
ATOM   187  C  CE2 . TRP   A 1 42  ? 41.04062  -0.01602  8.22341   1.000 19.17820 ?  54  TRP   A CE2 1 
ATOM   188  C  CE3 . TRP   A 1 42  ? 39.70013  1.05626   6.51692   1.000 14.83496 ?  54  TRP   A CE3 1 
ATOM   189  C  CZ2 . TRP   A 1 42  ? 42.14427  0.78998   7.93605   1.000 20.29219 ?  54  TRP   A CZ2 1 
ATOM   190  C  CZ3 . TRP   A 1 42  ? 40.79623  1.86047   6.23353   1.000 16.07998 ?  54  TRP   A CZ3 1 
ATOM   191  C  CH2 . TRP   A 1 42  ? 42.00664  1.71702   6.94172   1.000 17.92718 ?  54  TRP   A CH2 1 
ATOM   192  N  N   . SER   A 1 43  ? 35.09364  -2.88422  6.89943   1.000 12.25879 ?  55  SER   A N   1 
ATOM   193  C  CA  . SER   A 1 43  ? 33.67745  -2.70799  7.15413   1.000 12.34330 ?  55  SER   A CA  1 
ATOM   194  C  C   . SER   A 1 43  ? 33.48320  -2.18608  8.57066   1.000 13.58371 ?  55  SER   A C   1 
ATOM   195  O  O   . SER   A 1 43  ? 34.34479  -2.35626  9.43738   1.000 12.56263 ?  55  SER   A O   1 
ATOM   196  C  CB  . SER   A 1 43  ? 32.86790  -3.98401  6.90982   1.000 14.71194 ?  55  SER   A CB  1 
ATOM   197  O  OG  . SER   A 1 43  ? 33.18073  -4.97484  7.87040   1.000 16.45366 ?  55  SER   A OG  1 
ATOM   198  N  N   . HIS   A 1 44  ? 32.38246  -1.47207  8.77671   1.000 12.38692 ?  56  HIS   A N   1 
ATOM   199  C  CA  . HIS   A 1 44  ? 31.92544  -1.13104  10.10911  1.000 9.36501  ?  56  HIS   A CA  1 
ATOM   200  C  C   . HIS   A 1 44  ? 30.65560  -1.91186  10.40311  1.000 12.28342 ?  56  HIS   A C   1 
ATOM   201  O  O   . HIS   A 1 44  ? 29.81734  -2.09942  9.52025   1.000 13.20562 ?  56  HIS   A O   1 
ATOM   202  C  CB  . HIS   A 1 44  ? 31.78564  0.39671   10.33666  1.000 10.63028 ?  56  HIS   A CB  1 
ATOM   203  C  CG  . HIS   A 1 44  ? 30.79658  1.11207   9.45187   1.000 10.35053 ?  56  HIS   A CG  1 
ATOM   204  N  ND1 . HIS   A 1 44  ? 29.44606  1.20126   9.73371   1.000 11.70021 ?  56  HIS   A ND1 1 
ATOM   205  C  CD2 . HIS   A 1 44  ? 31.00340  1.90165   8.37154   1.000 10.38170 ?  56  HIS   A CD2 1 
ATOM   206  C  CE1 . HIS   A 1 44  ? 28.85561  1.96288   8.82686   1.000 9.82607  ?  56  HIS   A CE1 1 
ATOM   207  N  NE2 . HIS   A 1 44  ? 29.78301  2.40023   7.98762   1.000 10.21328 ?  56  HIS   A NE2 1 
ATOM   208  N  N   . ILE   A 1 45  ? 30.54239  -2.40967  11.62749  1.000 12.11851 ?  57  ILE   A N   1 
ATOM   209  C  CA  . ILE   A 1 45  ? 29.43139  -3.26647  12.02645  1.000 14.77320 ?  57  ILE   A CA  1 
ATOM   210  C  C   . ILE   A 1 45  ? 28.79276  -2.69641  13.28205  1.000 14.42930 ?  57  ILE   A C   1 
ATOM   211  O  O   . ILE   A 1 45  ? 29.48721  -2.43366  14.27392  1.000 13.81828 ?  57  ILE   A O   1 
ATOM   212  C  CB  . ILE   A 1 45  ? 29.86777  -4.72357  12.27225  1.000 14.27188 ?  57  ILE   A CB  1 
ATOM   213  C  CG1 . ILE   A 1 45  ? 30.68591  -5.25915  11.09412  1.000 16.96144 ?  57  ILE   A CG1 1 
ATOM   214  C  CG2 . ILE   A 1 45  ? 28.64420  -5.61471  12.47491  1.000 16.53608 ?  57  ILE   A CG2 1 
ATOM   215  C  CD1 . ILE   A 1 45  ? 32.19880  -5.08919  11.22011  1.000 19.54144 ?  57  ILE   A CD1 1 
ATOM   216  N  N   . ALA   A 1 46  ? 27.47753  -2.51013  13.24098  1.000 13.86790 ?  58  ALA   A N   1 
ATOM   217  C  CA  . ALA   A 1 46  ? 26.71484  -1.95858  14.35017  1.000 14.53510 ?  58  ALA   A CA  1 
ATOM   218  C  C   . ALA   A 1 46  ? 25.42650  -2.75628  14.48456  1.000 16.20179 ?  58  ALA   A C   1 
ATOM   219  O  O   . ALA   A 1 46  ? 25.11985  -3.60255  13.65007  1.000 15.85337 ?  58  ALA   A O   1 
ATOM   220  C  CB  . ALA   A 1 46  ? 26.42750  -0.46776  14.15336  1.000 15.47571 ?  58  ALA   A CB  1 
ATOM   221  N  N   . THR   A 1 47  ? 24.66135  -2.49366  15.54133  1.000 17.89486 ?  59  THR   A N   1 
ATOM   222  C  CA  . THR   A 1 47  ? 23.42029  -3.23099  15.75917  1.000 16.39988 ?  59  THR   A CA  1 
ATOM   223  C  C   . THR   A 1 47  ? 22.27917  -2.29015  16.10929  1.000 21.90623 ?  59  THR   A C   1 
ATOM   224  O  O   . THR   A 1 47  ? 22.48375  -1.20717  16.66125  1.000 19.21322 ?  59  THR   A O   1 
ATOM   225  C  CB  . THR   A 1 47  ? 23.54810  -4.28981  16.86334  1.000 22.14433 ?  59  THR   A CB  1 
ATOM   226  O  OG1 . THR   A 1 47  ? 23.88931  -3.65006  18.10007  1.000 31.24817 ?  59  THR   A OG1 1 
ATOM   227  C  CG2 . THR   A 1 47  ? 24.60102  -5.31575  16.51267  1.000 25.89538 ?  59  THR   A CG2 1 
ATOM   228  N  N   . GLN   A 1 48  ? 21.06426  -2.71429  15.76984  1.000 20.19065 ?  60  GLN   A N   1 
ATOM   229  C  CA  . GLN   A 1 48  ? 19.87085  -2.00782  16.19818  1.000 18.71125 ?  60  GLN   A CA  1 
ATOM   230  C  C   . GLN   A 1 48  ? 18.84798  -3.02944  16.67484  1.000 22.87387 ?  60  GLN   A C   1 
ATOM   231  O  O   . GLN   A 1 48  ? 18.75288  -4.12837  16.12032  1.000 22.55244 ?  60  GLN   A O   1 
ATOM   232  C  CB  . GLN   A 1 48  ? 19.26917  -1.15554  15.06578  1.000 25.65464 ?  60  GLN   A CB  1 
ATOM   233  C  CG  . GLN   A 1 48  ? 19.36892  0.37373   15.23483  1.000 31.37195 ?  60  GLN   A CG  1 
ATOM   234  C  CD  . GLN   A 1 48  ? 18.75697  0.94225   16.51738  1.000 37.57352 ?  60  GLN   A CD  1 
ATOM   235  O  OE1 . GLN   A 1 48  ? 18.56198  0.24727   17.51301  1.000 44.04651 ?  60  GLN   A OE1 1 
ATOM   236  N  NE2 . GLN   A 1 48  ? 18.46439  2.23593   16.48818  1.000 45.99699 ?  60  GLN   A NE2 1 
ATOM   237  N  N   . SER   A 1 49  ? 18.10519  -2.66730  17.71709  1.000 29.57547 ?  61  SER   A N   1 
ATOM   238  C  CA  . SER   A 1 49  ? 16.98353  -3.47104  18.18088  1.000 34.61888 ?  61  SER   A CA  1 
ATOM   239  C  C   . SER   A 1 49  ? 15.71214  -2.95805  17.52414  1.000 41.98483 ?  61  SER   A C   1 
ATOM   240  O  O   . SER   A 1 49  ? 15.51436  -1.74666  17.38924  1.000 45.32668 ?  61  SER   A O   1 
ATOM   241  C  CB  . SER   A 1 49  ? 16.84183  -3.37588  19.69744  1.000 35.91177 ?  61  SER   A CB  1 
ATOM   242  O  OG  . SER   A 1 49  ? 16.17614  -2.18002  20.05779  1.000 55.55689 ?  61  SER   A OG  1 
ATOM   243  N  N   . PHE   A 1 50  ? 14.85075  -3.88513  17.11389  1.000 41.33731 ?  62  PHE   A N   1 
ATOM   244  C  CA  . PHE   A 1 50  ? 13.68456  -3.51102  16.32224  1.000 45.62733 ?  62  PHE   A CA  1 
ATOM   245  C  C   . PHE   A 1 50  ? 12.68706  -4.65831  16.37105  1.000 39.65363 ?  62  PHE   A C   1 
ATOM   246  O  O   . PHE   A 1 50  ? 13.02610  -5.78713  15.99815  1.000 42.69759 ?  62  PHE   A O   1 
ATOM   247  C  CB  . PHE   A 1 50  ? 14.13867  -3.22216  14.88972  1.000 49.93539 ?  62  PHE   A CB  1 
ATOM   248  C  CG  . PHE   A 1 50  ? 13.01929  -3.05713  13.91022  1.000 54.02444 ?  62  PHE   A CG  1 
ATOM   249  C  CD1 . PHE   A 1 50  ? 12.20699  -1.93613  13.94899  1.000 54.69778 ?  62  PHE   A CD1 1 
ATOM   250  C  CD2 . PHE   A 1 50  ? 12.79454  -4.01212  12.93236  1.000 51.00128 ?  62  PHE   A CD2 1 
ATOM   251  C  CE1 . PHE   A 1 50  ? 11.17807  -1.77597  13.03687  1.000 63.12993 ?  62  PHE   A CE1 1 
ATOM   252  C  CE2 . PHE   A 1 50  ? 11.76874  -3.86026  12.01886  1.000 57.24184 ?  62  PHE   A CE2 1 
ATOM   253  C  CZ  . PHE   A 1 50  ? 10.95854  -2.74040  12.07114  1.000 64.12938 ?  62  PHE   A CZ  1 
ATOM   254  N  N   . ASP   A 1 51  ? 11.46734  -4.37627  16.83728  1.000 44.55458 ?  63  ASP   A N   1 
ATOM   255  C  CA  . ASP   A 1 51  ? 10.43182  -5.40317  16.99255  1.000 40.73757 ?  63  ASP   A CA  1 
ATOM   256  C  C   . ASP   A 1 51  ? 10.90668  -6.56622  17.85716  1.000 32.40072 ?  63  ASP   A C   1 
ATOM   257  O  O   . ASP   A 1 51  ? 10.63543  -7.73352  17.56858  1.000 38.34813 ?  63  ASP   A O   1 
ATOM   258  C  CB  . ASP   A 1 51  ? 9.89174   -5.89612  15.64644  1.000 41.00011 ?  63  ASP   A CB  1 
ATOM   259  C  CG  . ASP   A 1 51  ? 8.77852   -5.02714  15.11524  1.000 40.75823 ?  63  ASP   A CG  1 
ATOM   260  O  OD1 . ASP   A 1 51  ? 8.05248   -4.43642  15.94133  1.000 34.87451 ?  63  ASP   A OD1 1 
ATOM   261  O  OD2 . ASP   A 1 51  ? 8.61791   -4.94740  13.87821  1.000 41.65256 ?  63  ASP   A OD2 1 
ATOM   262  N  N   . GLY   A 1 52  ? 11.64090  -6.24603  18.91796  1.000 35.92188 ?  64  GLY   A N   1 
ATOM   263  C  CA  . GLY   A 1 52  ? 12.06813  -7.27129  19.84876  1.000 36.55488 ?  64  GLY   A CA  1 
ATOM   264  C  C   . GLY   A 1 52  ? 13.13766  -8.21143  19.34334  1.000 39.74252 ?  64  GLY   A C   1 
ATOM   265  O  O   . GLY   A 1 52  ? 13.34516  -9.26946  19.94148  1.000 36.90045 ?  64  GLY   A O   1 
ATOM   266  N  N   . ALA   A 1 53  ? 13.82358  -7.86085  18.25627  1.000 26.57885 ?  65  ALA   A N   1 
ATOM   267  C  CA  . ALA   A 1 53  ? 14.95000  -8.62634  17.75155  1.000 27.56829 ?  65  ALA   A CA  1 
ATOM   268  C  C   . ALA   A 1 53  ? 16.11661  -7.67564  17.53891  1.000 20.65044 ?  65  ALA   A C   1 
ATOM   269  O  O   . ALA   A 1 53  ? 15.94477  -6.45690  17.50361  1.000 28.81661 ?  65  ALA   A O   1 
ATOM   270  C  CB  . ALA   A 1 53  ? 14.61478  -9.30502  16.42390  1.000 28.55724 ?  65  ALA   A CB  1 
ATOM   271  N  N   . VAL   A 1 54  ? 17.31056  -8.24282  17.39701  1.000 18.07552 ?  66  VAL   A N   1 
ATOM   272  C  CA  . VAL   A 1 54  ? 18.51903  -7.45170  17.19744  1.000 20.96224 ?  66  VAL   A CA  1 
ATOM   273  C  C   . VAL   A 1 54  ? 19.10794  -7.78517  15.83628  1.000 18.79694 ?  66  VAL   A C   1 
ATOM   274  O  O   . VAL   A 1 54  ? 19.28690  -8.96156  15.49527  1.000 16.82314 ?  66  VAL   A O   1 
ATOM   275  C  CB  . VAL   A 1 54  ? 19.53709  -7.66898  18.32823  1.000 19.99355 ?  66  VAL   A CB  1 
ATOM   276  C  CG1 . VAL   A 1 54  ? 20.77092  -6.80262  18.10164  1.000 24.32914 ?  66  VAL   A CG1 1 
ATOM   277  C  CG2 . VAL   A 1 54  ? 18.89055  -7.32322  19.66178  1.000 25.11743 ?  66  VAL   A CG2 1 
ATOM   278  N  N   . TYR   A 1 55  ? 19.42333  -6.73902  15.06552  1.000 20.76815 ?  67  TYR   A N   1 
ATOM   279  C  CA  . TYR   A 1 55  ? 19.89896  -6.86495  13.70327  1.000 20.80933 ?  67  TYR   A CA  1 
ATOM   280  C  C   . TYR   A 1 55  ? 21.28298  -6.24015  13.58680  1.000 13.70511 ?  67  TYR   A C   1 
ATOM   281  O  O   . TYR   A 1 55  ? 21.49830  -5.14052  14.10835  1.000 19.98142 ?  67  TYR   A O   1 
ATOM   282  C  CB  . TYR   A 1 55  ? 18.94575  -6.09444  12.77682  1.000 20.45638 ?  67  TYR   A CB  1 
ATOM   283  C  CG  . TYR   A 1 55  ? 17.54871  -6.66539  12.74003  1.000 26.88171 ?  67  TYR   A CG  1 
ATOM   284  C  CD1 . TYR   A 1 55  ? 17.23100  -7.72837  11.90372  1.000 28.73667 ?  67  TYR   A CD1 1 
ATOM   285  C  CD2 . TYR   A 1 55  ? 16.55348  -6.15255  13.55926  1.000 25.85286 ?  67  TYR   A CD2 1 
ATOM   286  C  CE1 . TYR   A 1 55  ? 15.95125  -8.25538  11.87604  1.000 31.38647 ?  67  TYR   A CE1 1 
ATOM   287  C  CE2 . TYR   A 1 55  ? 15.27364  -6.67964  13.54676  1.000 32.93148 ?  67  TYR   A CE2 1 
ATOM   288  C  CZ  . TYR   A 1 55  ? 14.98088  -7.72991  12.70508  1.000 35.54097 ?  67  TYR   A CZ  1 
ATOM   289  O  OH  . TYR   A 1 55  ? 13.70717  -8.25392  12.68379  1.000 47.72765 ?  67  TYR   A OH  1 
ATOM   290  N  N   . PRO   A 1 56  ? 22.22794  -6.89681  12.91953  1.000 15.10224 ?  68  PRO   A N   1 
ATOM   291  C  CA  . PRO   A 1 56  ? 23.49206  -6.23571  12.59144  1.000 17.35774 ?  68  PRO   A CA  1 
ATOM   292  C  C   . PRO   A 1 56  ? 23.34713  -5.45136  11.29342  1.000 15.98492 ?  68  PRO   A C   1 
ATOM   293  O  O   . PRO   A 1 56  ? 22.43696  -5.67495  10.49037  1.000 15.68149 ?  68  PRO   A O   1 
ATOM   294  C  CB  . PRO   A 1 56  ? 24.44053  -7.42009  12.37966  1.000 19.16290 ?  68  PRO   A CB  1 
ATOM   295  C  CG  . PRO   A 1 56  ? 23.55632  -8.47063  11.76285  1.000 21.11279 ?  68  PRO   A CG  1 
ATOM   296  C  CD  . PRO   A 1 56  ? 22.16198  -8.25510  12.34532  1.000 17.45120 ?  68  PRO   A CD  1 
ATOM   297  N  N   . SER   A 1 57  ? 24.27309  -4.51771  11.09593  1.000 13.60245 ?  69  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 57  ? 24.27247  -3.70636  9.88300   1.000 13.43203 ?  69  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 57  ? 25.71454  -3.36437  9.54484   1.000 12.85342 ?  69  SER   A C   1 
ATOM   300  O  O   . SER   A 1 57  ? 26.50574  -3.05182  10.44357  1.000 12.50973 ?  69  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 57  ? 23.45218  -2.43150  10.08886  1.000 15.92402 ?  69  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 57  ? 23.33137  -1.69637  8.87876   1.000 19.08821 ?  69  SER   A OG  1 
ATOM   303  N  N   . ASN   A 1 58  ? 26.04840  -3.43582  8.25766   1.000 12.53565 ?  70  ASN   A N   1 
ATOM   304  C  CA  . ASN   A 1 58  ? 27.38179  -3.14711  7.74187   1.000 11.41311 ?  70  ASN   A CA  1 
ATOM   305  C  C   . ASN   A 1 58  ? 27.40391  -1.82985  6.98622   1.000 13.60787 ?  70  ASN   A C   1 
ATOM   306  O  O   . ASN   A 1 58  ? 26.45361  -1.49846  6.27293   1.000 11.34777 ?  70  ASN   A O   1 
ATOM   307  C  CB  . ASN   A 1 58  ? 27.82993  -4.21031  6.74081   1.000 11.64547 ?  70  ASN   A CB  1 
ATOM   308  C  CG  . ASN   A 1 58  ? 27.94279  -5.57427  7.34731   1.000 14.16035 ?  70  ASN   A CG  1 
ATOM   309  O  OD1 . ASN   A 1 58  ? 28.50750  -5.74932  8.43560   1.000 13.71907 ?  70  ASN   A OD1 1 
ATOM   310  N  ND2 . ASN   A 1 58  ? 27.42592  -6.56416  6.64404   1.000 11.91477 ?  70  ASN   A ND2 1 
ATOM   311  N  N   . GLY   A 1 59  ? 28.52380  -1.11512  7.10471   1.000 12.03885 ?  71  GLY   A N   1 
ATOM   312  C  CA  . GLY   A 1 59  ? 28.91563  -0.09785  6.14481   1.000 11.36680 ?  71  GLY   A CA  1 
ATOM   313  C  C   . GLY   A 1 59  ? 30.35990  -0.32021  5.74211   1.000 10.43000 ?  71  GLY   A C   1 
ATOM   314  O  O   . GLY   A 1 59  ? 30.94813  -1.35027  6.08706   1.000 11.51621 ?  71  GLY   A O   1 
ATOM   315  N  N   . LEU   A 1 60  ? 30.95896  0.62463   5.02310   1.000 10.54525 ?  72  LEU   A N   1 
ATOM   316  C  CA  . LEU   A 1 60  ? 32.30832  0.46570   4.51342   1.000 12.21321 ?  72  LEU   A CA  1 
ATOM   317  C  C   . LEU   A 1 60  ? 33.13403  1.69921   4.84920   1.000 10.28912 ?  72  LEU   A C   1 
ATOM   318  O  O   . LEU   A 1 60  ? 32.59673  2.80132   5.00255   1.000 9.72759  ?  72  LEU   A O   1 
ATOM   319  C  CB  . LEU   A 1 60  ? 32.28950  0.25708   2.98503   1.000 11.28283 ?  72  LEU   A CB  1 
ATOM   320  C  CG  . LEU   A 1 60  ? 33.44944  -0.52739  2.37310   1.000 14.03285 ?  72  LEU   A CG  1 
ATOM   321  C  CD1 . LEU   A 1 60  ? 33.38851  -1.96347  2.83035   1.000 16.06332 ?  72  LEU   A CD1 1 
ATOM   322  C  CD2 . LEU   A 1 60  ? 33.41698  -0.42020  0.84228   1.000 15.60122 ?  72  LEU   A CD2 1 
ATOM   323  N  N   . ILE   A 1 61  ? 34.44655  1.49400   5.00114   1.000 11.47091 ?  73  ILE   A N   1 
ATOM   324  C  CA  . ILE   A 1 61  ? 35.41300  2.57414   5.15497   1.000 10.80178 ?  73  ILE   A CA  1 
ATOM   325  C  C   . ILE   A 1 61  ? 36.54561  2.30403   4.18302   1.000 10.68527 ?  73  ILE   A C   1 
ATOM   326  O  O   . ILE   A 1 61  ? 37.07390  1.18580   4.14197   1.000 11.94742 ?  73  ILE   A O   1 
ATOM   327  C  CB  . ILE   A 1 61  ? 35.98046  2.64611   6.58522   1.000 11.13145 ?  73  ILE   A CB  1 
ATOM   328  C  CG1 . ILE   A 1 61  ? 34.86203  2.74779   7.63309   1.000 10.81682 ?  73  ILE   A CG1 1 
ATOM   329  C  CG2 . ILE   A 1 61  ? 37.00447  3.79277   6.69735   1.000 14.88473 ?  73  ILE   A CG2 1 
ATOM   330  C  CD1 . ILE   A 1 61  ? 35.29717  2.35836   9.02436   1.000 12.71864 ?  73  ILE   A CD1 1 
ATOM   331  N  N   . VAL   A 1 62  ? 36.91146  3.30930   3.39962   1.000 11.30709 ?  74  VAL   A N   1 
ATOM   332  C  CA  . VAL   A 1 62  ? 37.92875  3.14710   2.36793   1.000 11.34826 ?  74  VAL   A CA  1 
ATOM   333  C  C   . VAL   A 1 62  ? 38.96654  4.25918   2.49723   1.000 15.07132 ?  74  VAL   A C   1 
ATOM   334  O  O   . VAL   A 1 62  ? 38.63068  5.44491   2.42228   1.000 13.70574 ?  74  VAL   A O   1 
ATOM   335  C  CB  . VAL   A 1 62  ? 37.32224  3.11659   0.95562   1.000 10.21282 ?  74  VAL   A CB  1 
ATOM   336  C  CG1 . VAL   A 1 62  ? 38.42188  2.79567   -0.05598  1.000 14.49155 ?  74  VAL   A CG1 1 
ATOM   337  C  CG2 . VAL   A 1 62  ? 36.21154  2.07126   0.85136   1.000 14.22444 ?  74  VAL   A CG2 1 
ATOM   338  N  N   . ARG   A 1 63  ? 40.23075  3.87929   2.67550   1.000 14.49432 ?  75  ARG   A N   1 
ATOM   339  C  CA  A ARG   A 1 63  ? 41.27948  4.88363   2.75396   0.636 15.84083 ?  75  ARG   A CA  1 
ATOM   340  C  CA  B ARG   A 1 63  ? 41.30561  4.86175   2.74732   0.364 15.89468 ?  75  ARG   A CA  1 
ATOM   341  C  C   . ARG   A 1 63  ? 41.54479  5.50342   1.38381   1.000 15.89695 ?  75  ARG   A C   1 
ATOM   342  O  O   . ARG   A 1 63  ? 41.57210  4.81594   0.35895   1.000 17.55116 ?  75  ARG   A O   1 
ATOM   343  C  CB  A ARG   A 1 63  ? 42.56797  4.27539   3.30834   0.636 16.67488 ?  75  ARG   A CB  1 
ATOM   344  C  CB  B ARG   A 1 63  ? 42.59621  4.17435   3.19555   0.364 16.71809 ?  75  ARG   A CB  1 
ATOM   345  C  CG  A ARG   A 1 63  ? 43.66714  5.30624   3.51516   0.636 19.14551 ?  75  ARG   A CG  1 
ATOM   346  C  CG  B ARG   A 1 63  ? 43.77682  5.11806   3.33892   0.364 19.69250 ?  75  ARG   A CG  1 
ATOM   347  C  CD  A ARG   A 1 63  ? 44.86748  4.72417   4.24723   0.636 20.06151 ?  75  ARG   A CD  1 
ATOM   348  C  CD  B ARG   A 1 63  ? 45.07075  4.37004   3.65082   0.364 21.89387 ?  75  ARG   A CD  1 
ATOM   349  N  NE  A ARG   A 1 63  ? 45.87227  5.75186   4.49469   0.636 20.03567 ?  75  ARG   A NE  1 
ATOM   350  N  NE  B ARG   A 1 63  ? 44.94371  3.41941   4.74723   0.364 25.33076 ?  75  ARG   A NE  1 
ATOM   351  C  CZ  A ARG   A 1 63  ? 46.89946  5.61372   5.32270   0.636 22.35198 ?  75  ARG   A CZ  1 
ATOM   352  C  CZ  B ARG   A 1 63  ? 45.64592  2.29789   4.84950   0.364 22.12591 ?  75  ARG   A CZ  1 
ATOM   353  N  NH1 A ARG   A 1 63  ? 47.09214  4.49611   6.00194   0.636 25.33928 ?  75  ARG   A NH1 1 
ATOM   354  N  NH1 B ARG   A 1 63  ? 46.49669  1.92538   3.90685   0.364 28.29487 ?  75  ARG   A NH1 1 
ATOM   355  N  NH2 A ARG   A 1 63  ? 47.75725  6.62119   5.46708   0.636 26.17096 ?  75  ARG   A NH2 1 
ATOM   356  N  NH2 B ARG   A 1 63  ? 45.49067  1.53107   5.92420   0.364 23.83009 ?  75  ARG   A NH2 1 
ATOM   357  N  N   . ASP   A 1 64  ? 41.73889  6.82518   1.37780   1.000 18.29037 ?  76  ASP   A N   1 
ATOM   358  C  CA  . ASP   A 1 64  ? 42.11282  7.58971   0.18145   1.000 22.30353 ?  76  ASP   A CA  1 
ATOM   359  C  C   . ASP   A 1 64  ? 43.25465  8.52282   0.56766   1.000 19.43426 ?  76  ASP   A C   1 
ATOM   360  O  O   . ASP   A 1 64  ? 43.01193  9.63173   1.04983   1.000 18.60770 ?  76  ASP   A O   1 
ATOM   361  C  CB  . ASP   A 1 64  ? 40.94804  8.38065   -0.37255  1.000 25.79864 ?  76  ASP   A CB  1 
ATOM   362  C  CG  . ASP   A 1 64  ? 41.27679  9.04695   -1.69708  1.000 25.44868 ?  76  ASP   A CG  1 
ATOM   363  O  OD1 . ASP   A 1 64  ? 42.35155  8.75525   -2.27411  1.000 30.81894 ?  76  ASP   A OD1 1 
ATOM   364  O  OD2 . ASP   A 1 64  ? 40.47226  9.88454   -2.14341  1.000 24.77778 ?  76  ASP   A OD2 1 
ATOM   365  N  N   . GLY   A 1 65  ? 44.48459  8.07690   0.33974   1.000 30.41977 ?  77  GLY   A N   1 
ATOM   366  C  CA  . GLY   A 1 65  ? 45.62539  8.82772   0.80963   1.000 28.45044 ?  77  GLY   A CA  1 
ATOM   367  C  C   . GLY   A 1 65  ? 45.63187  8.87565   2.32003   1.000 25.66715 ?  77  GLY   A C   1 
ATOM   368  O  O   . GLY   A 1 65  ? 45.71021  7.83491   2.98106   1.000 28.79642 ?  77  GLY   A O   1 
ATOM   369  N  N   . ASP   A 1 66  ? 45.52925  10.07836  2.88082   1.000 22.41197 ?  78  ASP   A N   1 
ATOM   370  C  CA  . ASP   A 1 66  ? 45.53541  10.25621  4.32483   1.000 21.69106 ?  78  ASP   A CA  1 
ATOM   371  C  C   . ASP   A 1 66  ? 44.16411  10.64412  4.87440   1.000 18.98380 ?  78  ASP   A C   1 
ATOM   372  O  O   . ASP   A 1 66  ? 44.06916  11.18808  5.97598   1.000 20.29311 ?  78  ASP   A O   1 
ATOM   373  C  CB  . ASP   A 1 66  ? 46.61170  11.25851  4.74178   1.000 29.52786 ?  78  ASP   A CB  1 
ATOM   374  C  CG  . ASP   A 1 66  ? 48.00445  10.81064  4.33503   1.000 42.85013 ?  78  ASP   A CG  1 
ATOM   375  O  OD1 . ASP   A 1 66  ? 48.41073  9.70204   4.74122   1.000 43.19123 ?  78  ASP   A OD1 1 
ATOM   376  O  OD2 . ASP   A 1 66  ? 48.68987  11.56229  3.61057   1.000 41.92502 ?  78  ASP   A OD2 1 
ATOM   377  N  N   . GLU   A 1 67  ? 43.10124  10.36991  4.12105   1.000 18.27674 ?  79  GLU   A N   1 
ATOM   378  C  CA  . GLU   A 1 67  ? 41.72967  10.64244  4.52586   1.000 18.01343 ?  79  GLU   A CA  1 
ATOM   379  C  C   . GLU   A 1 67  ? 40.94106  9.35399   4.34710   1.000 14.37814 ?  79  GLU   A C   1 
ATOM   380  O  O   . GLU   A 1 67  ? 41.42315  8.39149   3.74870   1.000 15.42303 ?  79  GLU   A O   1 
ATOM   381  C  CB  . GLU   A 1 67  ? 41.10646  11.73785  3.64812   1.000 20.37625 ?  79  GLU   A CB  1 
ATOM   382  C  CG  . GLU   A 1 67  ? 41.92847  13.02027  3.59059   1.000 25.78258 ?  79  GLU   A CG  1 
ATOM   383  C  CD  . GLU   A 1 67  ? 41.31019  14.08249  2.69860   1.000 32.77096 ?  79  GLU   A CD  1 
ATOM   384  O  OE1 . GLU   A 1 67  ? 40.26809  13.81286  2.06036   1.000 29.34409 ?  79  GLU   A OE1 1 
ATOM   385  O  OE2 . GLU   A 1 67  ? 41.87497  15.19467  2.63335   1.000 41.58429 ?  79  GLU   A OE2 1 
ATOM   386  N  N   . LEU   A 1 68  ? 39.71614  9.33390   4.87726   1.000 14.75385 ?  80  LEU   A N   1 
ATOM   387  C  CA  . LEU   A 1 68  ? 38.84003  8.17834   4.74190   1.000 13.62483 ?  80  LEU   A CA  1 
ATOM   388  C  C   . LEU   A 1 68  ? 37.53942  8.58654   4.06262   1.000 12.33082 ?  80  LEU   A C   1 
ATOM   389  O  O   . LEU   A 1 68  ? 36.98946  9.65073   4.34631   1.000 13.73073 ?  80  LEU   A O   1 
ATOM   390  C  CB  . LEU   A 1 68  ? 38.48446  7.60628   6.11052   1.000 11.77024 ?  80  LEU   A CB  1 
ATOM   391  C  CG  . LEU   A 1 68  ? 39.66798  7.17444   6.97492   1.000 12.71149 ?  80  LEU   A CG  1 
ATOM   392  C  CD1 . LEU   A 1 68  ? 39.16058  6.68908   8.29245   1.000 14.28925 ?  80  LEU   A CD1 1 
ATOM   393  C  CD2 . LEU   A 1 68  ? 40.48136  6.09474   6.28481   1.000 15.32337 ?  80  LEU   A CD2 1 
ATOM   394  N  N   . LEU   A 1 69  ? 37.03660  7.69768   3.21681   1.000 12.63771 ?  81  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 69  ? 35.69355  7.78198   2.66731   1.000 11.88874 ?  81  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 69  ? 34.82769  6.79676   3.43686   1.000 10.69926 ?  81  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 69  ? 35.19298  5.62368   3.56380   1.000 10.36539 ?  81  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 69  ? 35.72036  7.38193   1.19847   1.000 11.92116 ?  81  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 69  ? 34.33154  7.25586   0.56962   1.000 11.04715 ?  81  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 69  ? 33.62763  8.59907   0.47325   1.000 12.08671 ?  81  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 69  ? 34.44646  6.61880   -0.81636  1.000 12.93417 ?  81  LEU   A CD2 1 
ATOM   402  N  N   . LEU   A 1 70  ? 33.70532  7.27523   3.96409   1.000 8.98465  ?  82  LEU   A N   1 
ATOM   403  C  CA  . LEU   A 1 70  ? 32.74855  6.43162   4.67335   1.000 8.56965  ?  82  LEU   A CA  1 
ATOM   404  C  C   . LEU   A 1 70  ? 31.57785  6.08748   3.75507   1.000 8.29003  ?  82  LEU   A C   1 
ATOM   405  O  O   . LEU   A 1 70  ? 31.04254  6.96864   3.06330   1.000 9.54537  ?  82  LEU   A O   1 
ATOM   406  C  CB  . LEU   A 1 70  ? 32.23420  7.19157   5.89434   1.000 10.79489 ?  82  LEU   A CB  1 
ATOM   407  C  CG  . LEU   A 1 70  ? 31.15375  6.51168   6.74936   1.000 10.94902 ?  82  LEU   A CG  1 
ATOM   408  C  CD1 . LEU   A 1 70  ? 31.74919  5.27905   7.41846   1.000 13.63836 ?  82  LEU   A CD1 1 
ATOM   409  C  CD2 . LEU   A 1 70  ? 30.58501  7.46758   7.78864   1.000 12.46557 ?  82  LEU   A CD2 1 
ATOM   410  N  N   . ILE   A 1 71  ? 31.18411  4.80805   3.73707   1.000 8.53004  ?  83  ILE   A N   1 
ATOM   411  C  CA  . ILE   A 1 71  ? 29.97073  4.37197   3.04487   1.000 9.51766  ?  83  ILE   A CA  1 
ATOM   412  C  C   . ILE   A 1 71  ? 28.93925  3.97450   4.09889   1.000 9.22369  ?  83  ILE   A C   1 
ATOM   413  O  O   . ILE   A 1 71  ? 29.12919  2.99842   4.83731   1.000 9.17874  ?  83  ILE   A O   1 
ATOM   414  C  CB  . ILE   A 1 71  ? 30.22906  3.20975   2.08644   1.000 8.50022  ?  83  ILE   A CB  1 
ATOM   415  C  CG1 . ILE   A 1 71  ? 31.41374  3.51403   1.14870   1.000 10.70842 ?  83  ILE   A CG1 1 
ATOM   416  C  CG2 . ILE   A 1 71  ? 28.94907  2.90825   1.29722   1.000 11.91305 ?  83  ILE   A CG2 1 
ATOM   417  C  CD1 . ILE   A 1 71  ? 31.21515  4.70426   0.21442   1.000 10.31096 ?  83  ILE   A CD1 1 
ATOM   418  N  N   . ASP   A 1 72  ? 27.87774  4.76695   4.18616   1.000 8.42233  ?  84  ASP   A N   1 
ATOM   419  C  CA  . ASP   A 1 72  ? 26.72113  4.53067   5.05121   1.000 8.34549  ?  84  ASP   A CA  1 
ATOM   420  C  C   . ASP   A 1 72  ? 26.97770  4.85932   6.51128   1.000 9.77773  ?  84  ASP   A C   1 
ATOM   421  O  O   . ASP   A 1 72  ? 28.08615  4.68772   7.02689   1.000 9.57416  ?  84  ASP   A O   1 
ATOM   422  C  CB  . ASP   A 1 72  ? 26.11524  3.13749   4.83477   1.000 9.17801  ?  84  ASP   A CB  1 
ATOM   423  C  CG  . ASP   A 1 72  ? 25.44859  3.01594   3.48971   1.000 9.55775  ?  84  ASP   A CG  1 
ATOM   424  O  OD1 . ASP   A 1 72  ? 24.89657  4.02506   3.02106   1.000 8.51583  ?  84  ASP   A OD1 1 
ATOM   425  O  OD2 . ASP   A 1 72  ? 25.48803  1.92829   2.88164   1.000 10.30948 ?  84  ASP   A OD2 1 
ATOM   426  N  N   . THR   A 1 73  ? 25.93776  5.34392   7.18473   1.000 8.48361  ?  85  THR   A N   1 
ATOM   427  C  CA  . THR   A 1 73  ? 26.00301  5.56537   8.61608   1.000 10.62833 ?  85  THR   A CA  1 
ATOM   428  C  C   . THR   A 1 73  ? 25.97025  4.22333   9.35073   1.000 11.02225 ?  85  THR   A C   1 
ATOM   429  O  O   . THR   A 1 73  ? 25.84368  3.14288   8.75548   1.000 10.80124 ?  85  THR   A O   1 
ATOM   430  C  CB  . THR   A 1 73  ? 24.81516  6.41173   9.06157   1.000 11.85945 ?  85  THR   A CB  1 
ATOM   431  O  OG1 . THR   A 1 73  ? 23.60547  5.65360   8.86868   1.000 13.63337 ?  85  THR   A OG1 1 
ATOM   432  C  CG2 . THR   A 1 73  ? 24.71811  7.70541   8.27455   1.000 12.28994 ?  85  THR   A CG2 1 
ATOM   433  N  N   . ALA   A 1 74  ? 26.05025  4.29127   10.68214  1.000 11.76966 ?  86  ALA   A N   1 
ATOM   434  C  CA  . ALA   A 1 74  ? 25.93440  3.09995   11.51125  1.000 12.88778 ?  86  ALA   A CA  1 
ATOM   435  C  C   . ALA   A 1 74  ? 24.52610  2.91653   12.05687  1.000 16.78664 ?  86  ALA   A C   1 
ATOM   436  O  O   . ALA   A 1 74  ? 24.35890  2.28512   13.10870  1.000 17.75064 ?  86  ALA   A O   1 
ATOM   437  C  CB  . ALA   A 1 74  ? 26.97782  3.08714   12.63458  1.000 14.29163 ?  86  ALA   A CB  1 
ATOM   438  N  N   . TRP   A 1 75  ? 23.50930  3.43401   11.35176  1.000 15.69777 ?  87  TRP   A N   1 
ATOM   439  C  CA  . TRP   A 1 75  ? 22.11465  3.25353   11.75299  1.000 17.41201 ?  87  TRP   A CA  1 
ATOM   440  C  C   . TRP   A 1 75  ? 21.77776  3.99609   13.03991  1.000 17.14189 ?  87  TRP   A C   1 
ATOM   441  O  O   . TRP   A 1 75  ? 21.61601  3.38121   14.10248  1.000 21.07027 ?  87  TRP   A O   1 
ATOM   442  C  CB  . TRP   A 1 75  ? 21.75283  1.77077   11.86613  1.000 17.80570 ?  87  TRP   A CB  1 
ATOM   443  C  CG  . TRP   A 1 75  ? 20.28600  1.43618   11.74576  1.000 16.34685 ?  87  TRP   A CG  1 
ATOM   444  C  CD1 . TRP   A 1 75  ? 19.23340  2.30309   11.73683  1.000 19.43664 ?  87  TRP   A CD1 1 
ATOM   445  C  CD2 . TRP   A 1 75  ? 19.72463  0.11799   11.70878  1.000 19.81519 ?  87  TRP   A CD2 1 
ATOM   446  N  NE1 . TRP   A 1 75  ? 18.04318  1.60204   11.65237  1.000 19.07394 ?  87  TRP   A NE1 1 
ATOM   447  C  CE2 . TRP   A 1 75  ? 18.32595  0.26046   11.62838  1.000 26.67212 ?  87  TRP   A CE2 1 
ATOM   448  C  CE3 . TRP   A 1 75  ? 20.27391  -1.16580  11.70306  1.000 26.47796 ?  87  TRP   A CE3 1 
ATOM   449  C  CZ2 . TRP   A 1 75  ? 17.46754  -0.83781  11.55767  1.000 25.19003 ?  87  TRP   A CZ2 1 
ATOM   450  C  CZ3 . TRP   A 1 75  ? 19.41536  -2.25879  11.63537  1.000 27.87196 ?  87  TRP   A CZ3 1 
ATOM   451  C  CH2 . TRP   A 1 75  ? 18.03257  -2.08162  11.56604  1.000 26.57871 ?  87  TRP   A CH2 1 
ATOM   452  N  N   . GLY   A 1 76  ? 21.68219  5.31039   12.94750  1.000 16.96216 ?  88  GLY   A N   1 
ATOM   453  C  CA  . GLY   A 1 76  ? 21.23811  6.12328   14.05765  1.000 18.16172 ?  88  GLY   A CA  1 
ATOM   454  C  C   . GLY   A 1 76  ? 22.30828  7.06896   14.56027  1.000 18.55654 ?  88  GLY   A C   1 
ATOM   455  O  O   . GLY   A 1 76  ? 23.49790  6.83802   14.34841  1.000 17.41428 ?  88  GLY   A O   1 
ATOM   456  N  N   . ALA   A 1 77  ? 21.87955  8.14408   15.22197  1.000 17.11123 ?  89  ALA   A N   1 
ATOM   457  C  CA  . ALA   A 1 77  ? 22.80632  9.15538   15.72334  1.000 17.99961 ?  89  ALA   A CA  1 
ATOM   458  C  C   . ALA   A 1 77  ? 23.79139  8.57818   16.73432  1.000 19.71456 ?  89  ALA   A C   1 
ATOM   459  O  O   . ALA   A 1 77  ? 24.99764  8.83768   16.65550  1.000 19.05090 ?  89  ALA   A O   1 
ATOM   460  C  CB  . ALA   A 1 77  ? 22.01730  10.30489  16.34774  1.000 21.83820 ?  89  ALA   A CB  1 
ATOM   461  N  N   . LYS   A 1 78  ? 23.29737  7.81330   17.71230  1.000 20.19035 ?  90  LYS   A N   1 
ATOM   462  C  CA  . LYS   A 1 78  ? 24.18005  7.29618   18.75604  1.000 23.49748 ?  90  LYS   A CA  1 
ATOM   463  C  C   . LYS   A 1 78  ? 25.23736  6.37429   18.16755  1.000 18.17115 ?  90  LYS   A C   1 
ATOM   464  O  O   . LYS   A 1 78  ? 26.43149  6.51375   18.45790  1.000 18.89885 ?  90  LYS   A O   1 
ATOM   465  C  CB  . LYS   A 1 78  ? 23.38566  6.55565   19.83865  1.000 24.70419 ?  90  LYS   A CB  1 
ATOM   466  C  CG  . LYS   A 1 78  ? 22.51954  7.41430   20.77320  1.000 36.66326 ?  90  LYS   A CG  1 
ATOM   467  C  CD  . LYS   A 1 78  ? 21.36355  8.11439   20.06609  1.000 43.84639 ?  90  LYS   A CD  1 
ATOM   468  C  CE  . LYS   A 1 78  ? 20.60094  7.15836   19.15298  1.000 35.44602 ?  90  LYS   A CE  1 
ATOM   469  N  NZ  . LYS   A 1 78  ? 19.88107  7.89017   18.08097  1.000 33.54986 ?  90  LYS   A NZ  1 
ATOM   470  N  N   . ASN   A 1 79  ? 24.80718  5.40879   17.34469  1.000 16.00128 ?  91  ASN   A N   1 
ATOM   471  C  CA  . ASN   A 1 79  ? 25.73726  4.46985   16.72957  1.000 14.82193 ?  91  ASN   A CA  1 
ATOM   472  C  C   . ASN   A 1 79  ? 26.73549  5.19548   15.83710  1.000 12.79664 ?  91  ASN   A C   1 
ATOM   473  O  O   . ASN   A 1 79  ? 27.89851  4.78962   15.74665  1.000 13.02558 ?  91  ASN   A O   1 
ATOM   474  C  CB  . ASN   A 1 79  ? 24.96686  3.48306   15.84719  1.000 17.45329 ?  91  ASN   A CB  1 
ATOM   475  C  CG  . ASN   A 1 79  ? 24.36005  2.31501   16.61813  1.000 20.81802 ?  91  ASN   A CG  1 
ATOM   476  O  OD1 . ASN   A 1 79  ? 24.62099  2.12056   17.80656  1.000 23.43612 ?  91  ASN   A OD1 1 
ATOM   477  N  ND2 . ASN   A 1 79  ? 23.53376  1.52380   15.92531  1.000 19.77691 ?  91  ASN   A ND2 1 
ATOM   478  N  N   . THR   A 1 80  ? 26.27186  6.22138   15.10987  1.000 14.90287 ?  92  THR   A N   1 
ATOM   479  C  CA  . THR   A 1 80  ? 27.15850  6.92381   14.18320  1.000 11.57011 ?  92  THR   A CA  1 
ATOM   480  C  C   . THR   A 1 80  ? 28.18699  7.75950   14.94308  1.000 14.41834 ?  92  THR   A C   1 
ATOM   481  O  O   . THR   A 1 80  ? 29.35090  7.82879   14.54029  1.000 12.47543 ?  92  THR   A O   1 
ATOM   482  C  CB  . THR   A 1 80  ? 26.34440  7.74638   13.17631  1.000 11.17773 ?  92  THR   A CB  1 
ATOM   483  O  OG1 . THR   A 1 80  ? 25.47790  6.85396   12.44456  1.000 12.37749 ?  92  THR   A OG1 1 
ATOM   484  C  CG2 . THR   A 1 80  ? 27.26781  8.47943   12.19142  1.000 11.53723 ?  92  THR   A CG2 1 
ATOM   485  N  N   . ALA   A 1 81  ? 27.78618  8.36868   16.06616  1.000 12.91194 ?  93  ALA   A N   1 
ATOM   486  C  CA  . ALA   A 1 81  ? 28.77927  8.99378   16.93284  1.000 14.85669 ?  93  ALA   A CA  1 
ATOM   487  C  C   . ALA   A 1 81  ? 29.80730  7.97171   17.39213  1.000 14.31778 ?  93  ALA   A C   1 
ATOM   488  O  O   . ALA   A 1 81  ? 31.01694  8.22367   17.34576  1.000 15.46000 ?  93  ALA   A O   1 
ATOM   489  C  CB  . ALA   A 1 81  ? 28.09316  9.65751   18.12618  1.000 17.22870 ?  93  ALA   A CB  1 
ATOM   490  N  N   . ALA   A 1 82  ? 29.35021  6.78708   17.79403  1.000 12.94573 ?  94  ALA   A N   1 
ATOM   491  C  CA  . ALA   A 1 82  ? 30.29540  5.76591   18.21688  1.000 14.83071 ?  94  ALA   A CA  1 
ATOM   492  C  C   . ALA   A 1 82  ? 31.17004  5.30526   17.05661  1.000 13.37864 ?  94  ALA   A C   1 
ATOM   493  O  O   . ALA   A 1 82  ? 32.35293  5.00600   17.24351  1.000 15.72497 ?  94  ALA   A O   1 
ATOM   494  C  CB  . ALA   A 1 82  ? 29.55141  4.58915   18.84293  1.000 14.94356 ?  94  ALA   A CB  1 
ATOM   495  N  N   . LEU   A 1 83  ? 30.59444  5.21566   15.84945  1.000 12.39413 ?  95  LEU   A N   1 
ATOM   496  C  CA  . LEU   A 1 83  ? 31.38748  4.87872   14.67136  1.000 12.73158 ?  95  LEU   A CA  1 
ATOM   497  C  C   . LEU   A 1 83  ? 32.55532  5.84965   14.49162  1.000 12.22904 ?  95  LEU   A C   1 
ATOM   498  O  O   . LEU   A 1 83  ? 33.70098  5.42933   14.28621  1.000 11.45089 ?  95  LEU   A O   1 
ATOM   499  C  CB  . LEU   A 1 83  ? 30.47442  4.86900   13.43719  1.000 13.14852 ?  95  LEU   A CB  1 
ATOM   500  C  CG  . LEU   A 1 83  ? 31.17339  4.83573   12.07322  1.000 11.79497 ?  95  LEU   A CG  1 
ATOM   501  C  CD1 . LEU   A 1 83  ? 31.95711  3.54444   11.87882  1.000 14.17811 ?  95  LEU   A CD1 1 
ATOM   502  C  CD2 . LEU   A 1 83  ? 30.13980  5.04570   10.94031  1.000 13.29816 ?  95  LEU   A CD2 1 
ATOM   503  N  N   . LEU   A 1 84  ? 32.27596  7.15426   14.53761  1.000 12.60177 ?  96  LEU   A N   1 
ATOM   504  C  CA  . LEU   A 1 84  ? 33.35142  8.13746   14.39056  1.000 12.58724 ?  96  LEU   A CA  1 
ATOM   505  C  C   . LEU   A 1 84  ? 34.40406  7.99033   15.48712  1.000 13.38512 ?  96  LEU   A C   1 
ATOM   506  O  O   . LEU   A 1 84  ? 35.60366  8.11342   15.22197  1.000 13.18082 ?  96  LEU   A O   1 
ATOM   507  C  CB  . LEU   A 1 84  ? 32.77838  9.54984   14.38802  1.000 13.31153 ?  96  LEU   A CB  1 
ATOM   508  C  CG  . LEU   A 1 84  ? 31.92326  9.89209   13.16606  1.000 12.39432 ?  96  LEU   A CG  1 
ATOM   509  C  CD1 . LEU   A 1 84  ? 31.41676  11.31326  13.27766  1.000 15.78294 ?  96  LEU   A CD1 1 
ATOM   510  C  CD2 . LEU   A 1 84  ? 32.69094  9.69953   11.87398  1.000 14.52652 ?  96  LEU   A CD2 1 
ATOM   511  N  N   . ALA   A 1 85  ? 33.97987  7.69708   16.71138  1.000 12.18889 ?  97  ALA   A N   1 
ATOM   512  C  CA  . ALA   A 1 85  ? 34.95446  7.54575   17.78650  1.000 11.94056 ?  97  ALA   A CA  1 
ATOM   513  C  C   . ALA   A 1 85  ? 35.82046  6.31395   17.57918  1.000 15.01487 ?  97  ALA   A C   1 
ATOM   514  O  O   . ALA   A 1 85  ? 37.02679  6.33637   17.85972  1.000 15.64071 ?  97  ALA   A O   1 
ATOM   515  C  CB  . ALA   A 1 85  ? 34.23273  7.49001   19.13099  1.000 14.79282 ?  97  ALA   A CB  1 
ATOM   516  N  N   . GLU   A 1 86  ? 35.22240  5.22237   17.09733  1.000 13.23599 ?  98  GLU   A N   1 
ATOM   517  C  CA  . GLU   A 1 86  ? 35.98925  4.00929   16.85494  1.000 12.43268 ?  98  GLU   A CA  1 
ATOM   518  C  C   . GLU   A 1 86  ? 36.95105  4.18302   15.68828  1.000 15.07324 ?  98  GLU   A C   1 
ATOM   519  O  O   . GLU   A 1 86  ? 38.07654  3.67875   15.72820  1.000 14.43809 ?  98  GLU   A O   1 
ATOM   520  C  CB  . GLU   A 1 86  ? 35.02778  2.85086   16.58415  1.000 19.48583 ?  98  GLU   A CB  1 
ATOM   521  C  CG  . GLU   A 1 86  ? 35.67237  1.47395   16.57478  1.000 24.52198 ?  98  GLU   A CG  1 
ATOM   522  C  CD  . GLU   A 1 86  ? 36.05971  0.98756   17.96577  1.000 22.19881 ?  98  GLU   A CD  1 
ATOM   523  O  OE1 . GLU   A 1 86  ? 35.48454  1.48704   18.95985  1.000 22.75517 ?  98  GLU   A OE1 1 
ATOM   524  O  OE2 . GLU   A 1 86  ? 36.92263  0.09199   18.05703  1.000 31.27221 ?  98  GLU   A OE2 1 
ATOM   525  N  N   . ILE   A 1 87  ? 36.51821  4.87845   14.63133  1.000 12.60739 ?  99  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 87  ? 37.42665  5.18775   13.52930  1.000 15.25318 ?  99  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 87  ? 38.63231  5.97710   14.03296  1.000 13.42548 ?  99  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 87  ? 39.78398  5.67099   13.69813  1.000 16.07663 ?  99  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 87  ? 36.68011  5.92931   12.40943  1.000 13.14183 ?  99  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 87  ? 35.70796  4.97598   11.70969  1.000 12.84403 ?  99  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 87  ? 37.67043  6.46577   11.41038  1.000 16.02833 ?  99  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 87  ? 34.82059  5.65926   10.71534  1.000 13.05413 ?  99  ILE   A CD1 1 
ATOM   533  N  N   . GLU   A 1 88  ? 38.38047  7.01728   14.83254  1.000 13.75009 ?  100 GLU   A N   1 
ATOM   534  C  CA  A GLU   A 1 88  ? 39.49757  7.80650   15.33879  0.528 14.92985 ?  100 GLU   A CA  1 
ATOM   535  C  CA  B GLU   A 1 88  ? 39.45794  7.82765   15.40105  0.472 14.95919 ?  100 GLU   A CA  1 
ATOM   536  C  C   . GLU   A 1 88  ? 40.40229  6.97668   16.24215  1.000 16.68608 ?  100 GLU   A C   1 
ATOM   537  O  O   . GLU   A 1 88  ? 41.63261  7.10551   16.16381  1.000 17.23845 ?  100 GLU   A O   1 
ATOM   538  C  CB  A GLU   A 1 88  ? 39.00849  9.08582   16.01904  0.528 17.74844 ?  100 GLU   A CB  1 
ATOM   539  C  CB  B GLU   A 1 88  ? 38.80488  8.88534   16.28395  0.472 17.29059 ?  100 GLU   A CB  1 
ATOM   540  C  CG  A GLU   A 1 88  ? 40.12345  10.06652  16.44882  0.528 17.21500 ?  100 GLU   A CG  1 
ATOM   541  C  CG  B GLU   A 1 88  ? 39.68318  10.01981  16.72746  0.472 19.65956 ?  100 GLU   A CG  1 
ATOM   542  C  CD  A GLU   A 1 88  ? 41.02533  10.56900  15.31270  0.528 19.76632 ?  100 GLU   A CD  1 
ATOM   543  C  CD  B GLU   A 1 88  ? 38.88864  11.08740  17.45869  0.472 19.02026 ?  100 GLU   A CD  1 
ATOM   544  O  OE1 A GLU   A 1 88  ? 40.66659  10.45253  14.12184  0.528 17.49329 ?  100 GLU   A OE1 1 
ATOM   545  O  OE1 B GLU   A 1 88  ? 37.89671  10.74281  18.14924  0.472 23.03258 ?  100 GLU   A OE1 1 
ATOM   546  O  OE2 A GLU   A 1 88  ? 42.10979  11.11427  15.62179  0.528 20.68864 ?  100 GLU   A OE2 1 
ATOM   547  O  OE2 B GLU   A 1 88  ? 39.25707  12.27133  17.33985  0.472 25.87422 ?  100 GLU   A OE2 1 
ATOM   548  N  N   . LYS   A 1 89  ? 39.82488  6.11017   17.07509  1.000 12.98668 ?  101 LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 89  ? 40.60807  5.24975   17.95923  1.000 14.30303 ?  101 LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 89  ? 41.48472  4.27426   17.17620  1.000 16.03099 ?  101 LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 89  ? 42.67805  4.13034   17.46579  1.000 19.24399 ?  101 LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 89  ? 39.65401  4.46698   18.86261  1.000 17.40488 ?  101 LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 89  ? 40.34337  3.55007   19.87257  1.000 19.81583 ?  101 LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 89  ? 39.34459  3.00196   20.86955  1.000 20.50217 ?  101 LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 89  ? 40.01332  2.03901   21.84923  1.000 31.63730 ?  101 LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 89  ? 39.01475  1.34196   22.71034  1.000 32.04765 ?  101 LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 90  ? 40.90500  3.56279   16.20249  1.000 15.52760 ?  102 GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 90  ? 41.62456  2.46617   15.55541  1.000 16.68097 ?  102 GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 90  ? 42.37137  2.85487   14.29115  1.000 16.75265 ?  102 GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 90  ? 43.38578  2.22687   13.97216  1.000 17.95566 ?  102 GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 90  ? 40.70010  1.28129   15.25093  1.000 22.93481 ?  102 GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 90  ? 39.67949  0.97181   16.31418  1.000 24.81199 ?  102 GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 90  ? 40.23643  0.03542   17.37477  1.000 37.28594 ?  102 GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 90  ? 39.72790  -0.03353  18.49426  1.000 40.13567 ?  102 GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 90  ? 41.30296  -0.67756  17.02927  1.000 40.37575 ?  102 GLN   A NE2 1 
ATOM   566  N  N   . ILE   A 1 91  ? 41.90294  3.85048   13.54818  1.000 15.20974 ?  103 ILE   A N   1 
ATOM   567  C  CA  . ILE   A 1 91  ? 42.51242  4.22597   12.28484  1.000 15.67918 ?  103 ILE   A CA  1 
ATOM   568  C  C   . ILE   A 1 91  ? 43.19540  5.58444   12.37312  1.000 18.31840 ?  103 ILE   A C   1 
ATOM   569  O  O   . ILE   A 1 91  ? 44.31721  5.75336   11.88365  1.000 18.70665 ?  103 ILE   A O   1 
ATOM   570  C  CB  . ILE   A 1 91  ? 41.49085  4.17009   11.12207  1.000 14.42537 ?  103 ILE   A CB  1 
ATOM   571  C  CG1 . ILE   A 1 91  ? 40.84607  2.78060   11.08260  1.000 12.95366 ?  103 ILE   A CG1 1 
ATOM   572  C  CG2 . ILE   A 1 91  ? 42.15904  4.52151   9.79501   1.000 15.02007 ?  103 ILE   A CG2 1 
ATOM   573  C  CD1 . ILE   A 1 91  ? 39.68979  2.64097   10.07677  1.000 15.14011 ?  103 ILE   A CD1 1 
ATOM   574  N  N   . GLY   A 1 92  ? 42.54014  6.55674   13.00475  1.000 17.24614 ?  104 GLY   A N   1 
ATOM   575  C  CA  . GLY   A 1 92  ? 43.16170  7.83771   13.26757  1.000 18.00487 ?  104 GLY   A CA  1 
ATOM   576  C  C   . GLY   A 1 92  ? 43.33941  8.73067   12.06557  1.000 20.93088 ?  104 GLY   A C   1 
ATOM   577  O  O   . GLY   A 1 92  ? 44.18345  9.62959   12.09754  1.000 25.28177 ?  104 GLY   A O   1 
ATOM   578  N  N   . LEU   A 1 93  ? 42.56987  8.51172   10.99797  1.000 17.45128 ?  105 LEU   A N   1 
ATOM   579  C  CA  . LEU   A 1 93  ? 42.53710  9.36868   9.82253   1.000 19.86750 ?  105 LEU   A CA  1 
ATOM   580  C  C   . LEU   A 1 93  ? 41.16282  10.02528  9.71536   1.000 19.50318 ?  105 LEU   A C   1 
ATOM   581  O  O   . LEU   A 1 93  ? 40.15688  9.43033   10.11871  1.000 18.70196 ?  105 LEU   A O   1 
ATOM   582  C  CB  . LEU   A 1 93  ? 42.80902  8.57006   8.53954   1.000 18.06350 ?  105 LEU   A CB  1 
ATOM   583  C  CG  . LEU   A 1 93  ? 44.19856  7.94859   8.38381   1.000 23.77291 ?  105 LEU   A CG  1 
ATOM   584  C  CD1 . LEU   A 1 93  ? 44.28059  7.03461   7.16000   1.000 18.69735 ?  105 LEU   A CD1 1 
ATOM   585  C  CD2 . LEU   A 1 93  ? 45.27678  9.03678   8.34169   1.000 26.50390 ?  105 LEU   A CD2 1 
ATOM   586  N  N   . PRO   A 1 94  ? 41.08023  11.24598  9.19072   1.000 18.69660 ?  106 PRO   A N   1 
ATOM   587  C  CA  . PRO   A 1 94  ? 39.79293  11.95179  9.17943   1.000 18.96630 ?  106 PRO   A CA  1 
ATOM   588  C  C   . PRO   A 1 94  ? 38.85245  11.39686  8.11830   1.000 15.29975 ?  106 PRO   A C   1 
ATOM   589  O  O   . PRO   A 1 94  ? 39.25420  11.10402  6.99060   1.000 14.67609 ?  106 PRO   A O   1 
ATOM   590  C  CB  . PRO   A 1 94  ? 40.18839  13.40114  8.87083   1.000 22.17499 ?  106 PRO   A CB  1 
ATOM   591  C  CG  . PRO   A 1 94  ? 41.44338  13.26428  8.06910   1.000 20.74058 ?  106 PRO   A CG  1 
ATOM   592  C  CD  . PRO   A 1 94  ? 42.17331  12.07226  8.63945   1.000 20.70037 ?  106 PRO   A CD  1 
ATOM   593  N  N   . VAL   A 1 95  ? 37.59066  11.23868  8.50829   1.000 15.64672 ?  107 VAL   A N   1 
ATOM   594  C  CA  . VAL   A 1 95  ? 36.51964  10.93622  7.56140   1.000 13.54844 ?  107 VAL   A CA  1 
ATOM   595  C  C   . VAL   A 1 95  ? 36.13103  12.26087  6.92067   1.000 14.97726 ?  107 VAL   A C   1 
ATOM   596  O  O   . VAL   A 1 95  ? 35.53463  13.11681  7.57402   1.000 15.86963 ?  107 VAL   A O   1 
ATOM   597  C  CB  . VAL   A 1 95  ? 35.31034  10.30232  8.26241   1.000 11.49608 ?  107 VAL   A CB  1 
ATOM   598  C  CG1 . VAL   A 1 95  ? 34.16833  10.05766  7.26858   1.000 12.47075 ?  107 VAL   A CG1 1 
ATOM   599  C  CG2 . VAL   A 1 95  ? 35.70487  9.00789   8.97433   1.000 16.46200 ?  107 VAL   A CG2 1 
ATOM   600  N  N   . THR   A 1 96  ? 36.48575  12.44481  5.65730   1.000 13.60123 ?  108 THR   A N   1 
ATOM   601  C  CA  . THR   A 1 96  ? 36.19317  13.70894  5.00035   1.000 13.48138 ?  108 THR   A CA  1 
ATOM   602  C  C   . THR   A 1 96  ? 34.92419  13.68938  4.16333   1.000 13.74166 ?  108 THR   A C   1 
ATOM   603  O  O   . THR   A 1 96  ? 34.31223  14.74335  3.98076   1.000 13.93023 ?  108 THR   A O   1 
ATOM   604  C  CB  . THR   A 1 96  ? 37.38315  14.16470  4.14720   1.000 15.88478 ?  108 THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 96  ? 37.72040  13.13615  3.21196   1.000 17.08009 ?  108 THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 96  ? 38.58839  14.44882  5.03987   1.000 20.97452 ?  108 THR   A CG2 1 
ATOM   607  N  N   . ARG   A 1 97  ? 34.50549  12.52646  3.65783   1.000 11.07463 ?  109 ARG   A N   1 
ATOM   608  C  CA  . ARG   A 1 97  ? 33.29276  12.41824  2.85015   1.000 12.03096 ?  109 ARG   A CA  1 
ATOM   609  C  C   . ARG   A 1 97  ? 32.56600  11.14313  3.23918   1.000 10.65623 ?  109 ARG   A C   1 
ATOM   610  O  O   . ARG   A 1 97  ? 33.19647  10.16058  3.64142   1.000 12.05252 ?  109 ARG   A O   1 
ATOM   611  C  CB  . ARG   A 1 97  ? 33.61329  12.39667  1.34594   1.000 13.10384 ?  109 ARG   A CB  1 
ATOM   612  C  CG  . ARG   A 1 97  ? 34.17971  13.72455  0.84546   1.000 17.21948 ?  109 ARG   A CG  1 
ATOM   613  C  CD  . ARG   A 1 97  ? 34.37725  13.75943  -0.67656  1.000 17.39180 ?  109 ARG   A CD  1 
ATOM   614  N  NE  . ARG   A 1 97  ? 35.40912  12.81720  -1.10299  1.000 17.58583 ?  109 ARG   A NE  1 
ATOM   615  C  CZ  . ARG   A 1 97  ? 35.77037  12.61513  -2.36598  1.000 19.95008 ?  109 ARG   A CZ  1 
ATOM   616  N  NH1 . ARG   A 1 97  ? 35.20559  13.27901  -3.36248  1.000 20.53170 ?  109 ARG   A NH1 1 
ATOM   617  N  NH2 . ARG   A 1 97  ? 36.72943  11.73209  -2.63354  1.000 22.96301 ?  109 ARG   A NH2 1 
ATOM   618  N  N   . ALA   A 1 98  ? 31.24027  11.15576  3.07650   1.000 10.76734 ?  110 ALA   A N   1 
ATOM   619  C  CA  . ALA   A 1 98  ? 30.42473  9.97194   3.30390   1.000 10.34722 ?  110 ALA   A CA  1 
ATOM   620  C  C   . ALA   A 1 98  ? 29.39300  9.86404   2.19914   1.000 9.49984  ?  110 ALA   A C   1 
ATOM   621  O  O   . ALA   A 1 98  ? 28.85156  10.87732  1.75634   1.000 11.11446 ?  110 ALA   A O   1 
ATOM   622  C  CB  . ALA   A 1 98  ? 29.67999  10.05757  4.63810   1.000 11.43829 ?  110 ALA   A CB  1 
ATOM   623  N  N   . VAL   A 1 99  ? 29.09579  8.63756   1.78052   1.000 8.72362  ?  111 VAL   A N   1 
ATOM   624  C  CA  . VAL   A 1 99  ? 28.05074  8.36457   0.80103   1.000 8.46254  ?  111 VAL   A CA  1 
ATOM   625  C  C   . VAL   A 1 99  ? 27.01750  7.45648   1.45247   1.000 9.04735  ?  111 VAL   A C   1 
ATOM   626  O  O   . VAL   A 1 99  ? 27.38200  6.43491   2.04152   1.000 9.88730  ?  111 VAL   A O   1 
ATOM   627  C  CB  . VAL   A 1 99  ? 28.64448  7.64898   -0.42051  1.000 8.84429  ?  111 VAL   A CB  1 
ATOM   628  C  CG1 . VAL   A 1 99  ? 27.54519  7.16441   -1.33629  1.000 11.62321 ?  111 VAL   A CG1 1 
ATOM   629  C  CG2 . VAL   A 1 99  ? 29.58699  8.58003   -1.15779  1.000 11.77528 ?  111 VAL   A CG2 1 
ATOM   630  N  N   . SER   A 1 100 ? 25.73587  7.79486   1.29817   1.000 9.04351  ?  112 SER   A N   1 
ATOM   631  C  CA  . SER   A 1 100 ? 24.64469  6.91957   1.72165   1.000 7.36821  ?  112 SER   A CA  1 
ATOM   632  C  C   . SER   A 1 100 ? 24.09646  6.20958   0.49949   1.000 8.85576  ?  112 SER   A C   1 
ATOM   633  O  O   . SER   A 1 100 ? 23.79070  6.85821   -0.51168  1.000 9.85152  ?  112 SER   A O   1 
ATOM   634  C  CB  . SER   A 1 100 ? 23.52312  7.70365   2.40511   1.000 8.95199  ?  112 SER   A CB  1 
ATOM   635  O  OG  . SER   A 1 100 ? 23.97275  8.18900   3.67596   1.000 10.14812 ?  112 SER   A OG  1 
ATOM   636  N  N   . THR   A 1 101 ? 23.94725  4.87847   0.60593   1.000 8.60917  ?  113 THR   A N   1 
ATOM   637  C  CA  . THR   A 1 101 ? 23.62194  4.06771   -0.56102  1.000 8.01591  ?  113 THR   A CA  1 
ATOM   638  C  C   . THR   A 1 101 ? 22.12804  3.89886   -0.83061  1.000 8.32999  ?  113 THR   A C   1 
ATOM   639  O  O   . THR   A 1 101 ? 21.76254  3.45299   -1.92956  1.000 9.49429  ?  113 THR   A O   1 
ATOM   640  C  CB  . THR   A 1 101 ? 24.29136  2.68485   -0.48733  1.000 9.90902  ?  113 THR   A CB  1 
ATOM   641  O  OG1 . THR   A 1 101 ? 23.89431  2.00635   0.70846   1.000 9.64147  ?  113 THR   A OG1 1 
ATOM   642  C  CG2 . THR   A 1 101 ? 25.80625  2.81567   -0.51388  1.000 9.54622  ?  113 THR   A CG2 1 
ATOM   643  N  N   . HIS   A 1 102 ? 21.25283  4.21504   0.12456   1.000 8.30311  ?  114 HIS   A N   1 
ATOM   644  C  CA  . HIS   A 1 102 ? 19.84811  4.45690   -0.18562  1.000 7.44224  ?  114 HIS   A CA  1 
ATOM   645  C  C   . HIS   A 1 102 ? 19.22117  5.24412   0.95910   1.000 9.90477  ?  114 HIS   A C   1 
ATOM   646  O  O   . HIS   A 1 102 ? 19.90011  5.60213   1.92165   1.000 8.86661  ?  114 HIS   A O   1 
ATOM   647  C  CB  . HIS   A 1 102 ? 19.07839  3.18127   -0.58540  1.000 8.62070  ?  114 HIS   A CB  1 
ATOM   648  C  CG  . HIS   A 1 102 ? 18.79941  2.22897   0.53752   1.000 8.90832  ?  114 HIS   A CG  1 
ATOM   649  N  ND1 . HIS   A 1 102 ? 19.73134  1.32894   1.01428   1.000 8.53887  ?  114 HIS   A ND1 1 
ATOM   650  C  CD2 . HIS   A 1 102 ? 17.67437  2.01559   1.25949   1.000 9.16041  ?  114 HIS   A CD2 1 
ATOM   651  C  CE1 . HIS   A 1 102 ? 19.19476  0.59996   1.97356   1.000 10.96934 ?  114 HIS   A CE1 1 
ATOM   652  N  NE2 . HIS   A 1 102 ? 17.95847  1.01348   2.15069   1.000 9.89428  ?  114 HIS   A NE2 1 
ATOM   653  N  N   . PHE   A 1 103 ? 17.91997  5.52900   0.83050   1.000 9.92297  ?  115 PHE   A N   1 
ATOM   654  C  CA  . PHE   A 1 103 ? 17.28044  6.57921   1.63137   1.000 8.92378  ?  115 PHE   A CA  1 
ATOM   655  C  C   . PHE   A 1 103 ? 16.79534  6.11187   2.99267   1.000 11.59040 ?  115 PHE   A C   1 
ATOM   656  O  O   . PHE   A 1 103 ? 16.34544  6.94771   3.78874   1.000 10.78555 ?  115 PHE   A O   1 
ATOM   657  C  CB  . PHE   A 1 103 ? 16.10254  7.21545   0.86704   1.000 11.27545 ?  115 PHE   A CB  1 
ATOM   658  C  CG  . PHE   A 1 103 ? 14.86358  6.34270   0.77539   1.000 9.96250  ?  115 PHE   A CG  1 
ATOM   659  C  CD1 . PHE   A 1 103 ? 14.73480  5.38642   -0.22425  1.000 10.61681 ?  115 PHE   A CD1 1 
ATOM   660  C  CD2 . PHE   A 1 103 ? 13.80224  6.51591   1.66330   1.000 11.01792 ?  115 PHE   A CD2 1 
ATOM   661  C  CE1 . PHE   A 1 103 ? 13.58616  4.60483   -0.32767  1.000 13.21946 ?  115 PHE   A CE1 1 
ATOM   662  C  CE2 . PHE   A 1 103 ? 12.66080  5.73059   1.57176   1.000 13.01537 ?  115 PHE   A CE2 1 
ATOM   663  C  CZ  . PHE   A 1 103 ? 12.54361  4.78624   0.57937   1.000 11.62946 ?  115 PHE   A CZ  1 
ATOM   664  N  N   . HIS   A 1 104 ? 16.84741  4.81774   3.28502   1.000 9.70421  ?  116 HIS   A N   1 
ATOM   665  C  CA  . HIS   A 1 104 ? 16.28357  4.35046   4.54278   1.000 11.35733 ?  116 HIS   A CA  1 
ATOM   666  C  C   . HIS   A 1 104 ? 17.17989  4.71833   5.72719   1.000 12.69891 ?  116 HIS   A C   1 
ATOM   667  O  O   . HIS   A 1 104 ? 18.36461  5.00832   5.58626   1.000 10.52677 ?  116 HIS   A O   1 
ATOM   668  C  CB  . HIS   A 1 104 ? 16.05983  2.84652   4.48188   1.000 10.48631 ?  116 HIS   A CB  1 
ATOM   669  C  CG  . HIS   A 1 104 ? 14.89680  2.44383   3.63129   1.000 10.88119 ?  116 HIS   A CG  1 
ATOM   670  N  ND1 . HIS   A 1 104 ? 14.81809  1.21501   3.02925   1.000 13.11307 ?  116 HIS   A ND1 1 
ATOM   671  C  CD2 . HIS   A 1 104 ? 13.76077  3.09042   3.28864   1.000 13.43114 ?  116 HIS   A CD2 1 
ATOM   672  C  CE1 . HIS   A 1 104 ? 13.69619  1.10706   2.35108   1.000 12.83614 ?  116 HIS   A CE1 1 
ATOM   673  N  NE2 . HIS   A 1 104 ? 13.03220  2.23643   2.49185   1.000 12.79181 ?  116 HIS   A NE2 1 
ATOM   674  N  N   . ASP   A 1 105 ? 16.58811  4.63286   6.92173   1.000 15.23520 ?  117 ASP   A N   1 
ATOM   675  C  CA  A ASP   A 1 105 ? 17.23260  5.10990   8.14395   0.709 15.12483 ?  117 ASP   A CA  1 
ATOM   676  C  CA  B ASP   A 1 105 ? 17.25338  5.14262   8.11555   0.291 15.15628 ?  117 ASP   A CA  1 
ATOM   677  C  C   . ASP   A 1 105 ? 18.52925  4.37990   8.45632   1.000 15.08291 ?  117 ASP   A C   1 
ATOM   678  O  O   . ASP   A 1 105 ? 19.42948  4.94986   9.07802   1.000 17.71968 ?  117 ASP   A O   1 
ATOM   679  C  CB  A ASP   A 1 105 ? 16.24736  4.92775   9.29494   0.709 17.68292 ?  117 ASP   A CB  1 
ATOM   680  C  CB  B ASP   A 1 105 ? 16.28150  5.15892   9.29241   0.291 18.02516 ?  117 ASP   A CB  1 
ATOM   681  C  CG  A ASP   A 1 105 ? 16.61012  5.73567   10.50573  0.709 21.59011 ?  117 ASP   A CG  1 
ATOM   682  C  CG  B ASP   A 1 105 ? 16.11383  6.54097   9.87941   0.291 20.30911 ?  117 ASP   A CG  1 
ATOM   683  O  OD1 A ASP   A 1 105 ? 16.98791  6.91498   10.35455  0.709 23.82663 ?  117 ASP   A OD1 1 
ATOM   684  O  OD1 B ASP   A 1 105 ? 17.03834  7.00661   10.57681  0.291 24.18846 ?  117 ASP   A OD1 1 
ATOM   685  O  OD2 A ASP   A 1 105 ? 16.49073  5.18119   11.61336  0.709 21.55428 ?  117 ASP   A OD2 1 
ATOM   686  O  OD2 B ASP   A 1 105 ? 15.06677  7.16885   9.62813   0.291 23.96595 ?  117 ASP   A OD2 1 
ATOM   687  N  N   . ASP   A 1 106 ? 18.64772  3.11051   8.05904   1.000 14.10049 ?  118 ASP   A N   1 
ATOM   688  C  CA  . ASP   A 1 106 ? 19.89381  2.41826   8.36364   1.000 16.26644 ?  118 ASP   A CA  1 
ATOM   689  C  C   . ASP   A 1 106 ? 21.06206  2.89737   7.51126   1.000 17.42571 ?  118 ASP   A C   1 
ATOM   690  O  O   . ASP   A 1 106 ? 22.19992  2.48454   7.75846   1.000 17.59911 ?  118 ASP   A O   1 
ATOM   691  C  CB  . ASP   A 1 106 ? 19.74582  0.88503   8.33693   1.000 19.57112 ?  118 ASP   A CB  1 
ATOM   692  C  CG  . ASP   A 1 106 ? 19.50537  0.31398   6.94629   1.000 14.75050 ?  118 ASP   A CG  1 
ATOM   693  O  OD1 . ASP   A 1 106 ? 19.19614  1.06813   6.00203   1.000 17.41837 ?  118 ASP   A OD1 1 
ATOM   694  O  OD2 . ASP   A 1 106 ? 19.60551  -0.92909  6.81516   1.000 15.75292 ?  118 ASP   A OD2 1 
ATOM   695  N  N   . ARG   A 1 107 ? 20.81060  3.74842   6.51752   1.000 11.67020 ?  119 ARG   A N   1 
ATOM   696  C  CA  A ARG   A 1 107 ? 21.85318  4.30288   5.65936   0.505 11.99545 ?  119 ARG   A CA  1 
ATOM   697  C  CA  B ARG   A 1 107 ? 21.87675  4.29380   5.69712   0.495 11.96001 ?  119 ARG   A CA  1 
ATOM   698  C  C   . ARG   A 1 107 ? 22.05464  5.79795   5.83569   1.000 10.09745 ?  119 ARG   A C   1 
ATOM   699  O  O   . ARG   A 1 107 ? 23.16366  6.28295   5.61554   1.000 10.73600 ?  119 ARG   A O   1 
ATOM   700  C  CB  A ARG   A 1 107 ? 21.51812  4.06666   4.17819   0.505 10.11003 ?  119 ARG   A CB  1 
ATOM   701  C  CB  B ARG   A 1 107 ? 21.66575  3.92944   4.21771   0.495 10.32859 ?  119 ARG   A CB  1 
ATOM   702  C  CG  A ARG   A 1 107 ? 21.11891  2.65367   3.81782   0.505 11.85946 ?  119 ARG   A CG  1 
ATOM   703  C  CG  B ARG   A 1 107 ? 21.46519  2.43610   3.98455   0.495 11.42831 ?  119 ARG   A CG  1 
ATOM   704  C  CD  A ARG   A 1 107 ? 22.28830  1.70304   3.80331   0.505 10.09026 ?  119 ARG   A CD  1 
ATOM   705  C  CD  B ARG   A 1 107 ? 22.59626  1.66251   4.64907   0.495 14.26405 ?  119 ARG   A CD  1 
ATOM   706  N  NE  A ARG   A 1 107 ? 22.07924  0.64665   4.78411   0.505 12.03570 ?  119 ARG   A NE  1 
ATOM   707  N  NE  B ARG   A 1 107 ? 22.41402  0.21683   4.65024   0.495 13.31955 ?  119 ARG   A NE  1 
ATOM   708  C  CZ  A ARG   A 1 107 ? 23.05144  -0.08820  5.30112   0.505 12.43230 ?  119 ARG   A CZ  1 
ATOM   709  C  CZ  B ARG   A 1 107 ? 23.24607  -0.62011  5.25261   0.495 12.57151 ?  119 ARG   A CZ  1 
ATOM   710  N  NH1 A ARG   A 1 107 ? 24.30929  0.04941   4.90012   0.505 11.29358 ?  119 ARG   A NH1 1 
ATOM   711  N  NH1 B ARG   A 1 107 ? 24.25050  -0.17801  5.99976   0.495 10.69627 ?  119 ARG   A NH1 1 
ATOM   712  N  NH2 A ARG   A 1 107 ? 22.75256  -0.99726  6.22586   0.505 12.18064 ?  119 ARG   A NH2 1 
ATOM   713  N  NH2 B ARG   A 1 107 ? 23.07152  -1.92807  5.10193   0.495 15.97020 ?  119 ARG   A NH2 1 
ATOM   714  N  N   . VAL   A 1 108 ? 20.98863  6.53673   6.16488   1.000 12.25691 ?  120 VAL   A N   1 
ATOM   715  C  CA  . VAL   A 1 108 ? 21.05405  7.98135   6.36278   1.000 10.44134 ?  120 VAL   A CA  1 
ATOM   716  C  C   . VAL   A 1 108 ? 20.86782  8.38915   7.81401   1.000 11.64221 ?  120 VAL   A C   1 
ATOM   717  O  O   . VAL   A 1 108 ? 21.13210  9.55060   8.14030   1.000 11.17883 ?  120 VAL   A O   1 
ATOM   718  C  CB  . VAL   A 1 108 ? 20.05504  8.74904   5.46991   1.000 9.48619  ?  120 VAL   A CB  1 
ATOM   719  C  CG1 . VAL   A 1 108 ? 20.31558  8.48627   3.99259   1.000 11.60482 ?  120 VAL   A CG1 1 
ATOM   720  C  CG2 . VAL   A 1 108 ? 18.59715  8.44775   5.86900   1.000 12.07208 ?  120 VAL   A CG2 1 
ATOM   721  N  N   . GLY   A 1 109 ? 20.41799  7.49620   8.68933   1.000 11.40574 ?  121 GLY   A N   1 
ATOM   722  C  CA  . GLY   A 1 109 ? 20.25787  7.87852   10.08237  1.000 13.67206 ?  121 GLY   A CA  1 
ATOM   723  C  C   . GLY   A 1 109 ? 21.62101  8.02741   10.71804  1.000 11.77262 ?  121 GLY   A C   1 
ATOM   724  O  O   . GLY   A 1 109 ? 22.36059  7.04471   10.82414  1.000 13.44013 ?  121 GLY   A O   1 
ATOM   725  N  N   . GLY   A 1 110 ? 21.97999  9.24395   11.11904  1.000 13.27160 ?  122 GLY   A N   1 
ATOM   726  C  CA  . GLY   A 1 110 ? 23.35156  9.55403   11.49701  1.000 13.78809 ?  122 GLY   A CA  1 
ATOM   727  C  C   . GLY   A 1 110 ? 24.01123  10.58201  10.60248  1.000 11.13676 ?  122 GLY   A C   1 
ATOM   728  O  O   . GLY   A 1 110 ? 25.09782  11.08640  10.94007  1.000 12.10906 ?  122 GLY   A O   1 
ATOM   729  N  N   . VAL   A 1 111 ? 23.37273  10.93313  9.48436   1.000 11.68183 ?  123 VAL   A N   1 
ATOM   730  C  CA  . VAL   A 1 111 ? 23.90142  11.96237  8.59609   1.000 11.38679 ?  123 VAL   A CA  1 
ATOM   731  C  C   . VAL   A 1 111 ? 24.05854  13.28950  9.33365   1.000 12.46464 ?  123 VAL   A C   1 
ATOM   732  O  O   . VAL   A 1 111 ? 25.03151  14.02068  9.11169   1.000 12.80892 ?  123 VAL   A O   1 
ATOM   733  C  CB  . VAL   A 1 111 ? 23.02784  12.08072  7.32957   1.000 10.81665 ?  123 VAL   A CB  1 
ATOM   734  C  CG1 . VAL   A 1 111 ? 23.13695  13.47211  6.70640   1.000 13.89833 ?  123 VAL   A CG1 1 
ATOM   735  C  CG2 . VAL   A 1 111 ? 23.42846  11.01131  6.31923   1.000 12.14061 ?  123 VAL   A CG2 1 
ATOM   736  N  N   . ASP   A 1 112 ? 23.12657  13.61628  10.23868  1.000 14.31305 ?  124 ASP   A N   1 
ATOM   737  C  CA  . ASP   A 1 112 ? 23.24685  14.88573  10.95634  1.000 13.47217 ?  124 ASP   A CA  1 
ATOM   738  C  C   . ASP   A 1 112 ? 24.46080  14.87820  11.87980  1.000 11.72305 ?  124 ASP   A C   1 
ATOM   739  O  O   . ASP   A 1 112 ? 25.15035  15.89638  12.01326  1.000 15.02191 ?  124 ASP   A O   1 
ATOM   740  C  CB  . ASP   A 1 112 ? 21.96510  15.17230  11.74712  1.000 15.80920 ?  124 ASP   A CB  1 
ATOM   741  C  CG  . ASP   A 1 112 ? 20.82016  15.65378  10.86985  1.000 19.53890 ?  124 ASP   A CG  1 
ATOM   742  O  OD1 . ASP   A 1 112 ? 20.99931  15.78191  9.64148   1.000 22.00498 ?  124 ASP   A OD1 1 
ATOM   743  O  OD2 . ASP   A 1 112 ? 19.71880  15.90475  11.41139  1.000 24.14573 ?  124 ASP   A OD2 1 
ATOM   744  N  N   . VAL   A 1 113 ? 24.74716  13.73100  12.50369  1.000 12.94491 ?  125 VAL   A N   1 
ATOM   745  C  CA  . VAL   A 1 113 ? 25.95580  13.58677  13.31884  1.000 12.64194 ?  125 VAL   A CA  1 
ATOM   746  C  C   . VAL   A 1 113 ? 27.20547  13.74849  12.45637  1.000 13.92745 ?  125 VAL   A C   1 
ATOM   747  O  O   . VAL   A 1 113 ? 28.15975  14.43964  12.83275  1.000 15.77620 ?  125 VAL   A O   1 
ATOM   748  C  CB  . VAL   A 1 113 ? 25.94263  12.23789  14.06403  1.000 13.95791 ?  125 VAL   A CB  1 
ATOM   749  C  CG1 . VAL   A 1 113 ? 27.33248  11.83364  14.51669  1.000 16.70226 ?  125 VAL   A CG1 1 
ATOM   750  C  CG2 . VAL   A 1 113 ? 24.97002  12.29152  15.26657  1.000 15.65540 ?  125 VAL   A CG2 1 
ATOM   751  N  N   . LEU   A 1 114 ? 27.23269  13.09981  11.29046  1.000 12.98802 ?  126 LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 114 ? 28.36799  13.26246  10.39342  1.000 13.30821 ?  126 LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 114 ? 28.54362  14.71801  9.99862   1.000 12.61231 ?  126 LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 114 ? 29.65779  15.24513  10.01702  1.000 13.74315 ?  126 LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 114 ? 28.16575  12.42574  9.13161   1.000 13.48189 ?  126 LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 114 ? 28.11476  10.91522  9.29127   1.000 12.34490 ?  126 LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 114 ? 27.83178  10.27041  7.94522   1.000 14.60977 ?  126 LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 114 ? 29.43188  10.41397  9.88122   1.000 12.60861 ?  126 LEU   A CD2 1 
ATOM   759  N  N   . ARG   A 1 115 ? 27.45178  15.36705  9.58469   1.000 12.44294 ?  127 ARG   A N   1 
ATOM   760  C  CA  . ARG   A 1 115 ? 27.50665  16.76701  9.18207   1.000 14.59443 ?  127 ARG   A CA  1 
ATOM   761  C  C   . ARG   A 1 115 ? 28.03481  17.65142  10.30537  1.000 14.92504 ?  127 ARG   A C   1 
ATOM   762  O  O   . ARG   A 1 115 ? 28.89874  18.51124  10.08225  1.000 14.04414 ?  127 ARG   A O   1 
ATOM   763  C  CB  . ARG   A 1 115 ? 26.11367  17.21248  8.74280   1.000 14.33239 ?  127 ARG   A CB  1 
ATOM   764  C  CG  . ARG   A 1 115 ? 26.01397  18.63932  8.20859   1.000 13.75346 ?  127 ARG   A CG  1 
ATOM   765  C  CD  . ARG   A 1 115 ? 24.86033  18.75066  7.19211   1.000 17.73283 ?  127 ARG   A CD  1 
ATOM   766  N  NE  . ARG   A 1 115 ? 23.65406  18.06974  7.64801   1.000 18.88041 ?  127 ARG   A NE  1 
ATOM   767  C  CZ  . ARG   A 1 115 ? 22.86166  17.35287  6.86921   1.000 18.60312 ?  127 ARG   A CZ  1 
ATOM   768  N  NH1 . ARG   A 1 115 ? 23.14010  17.16734  5.58889   1.000 15.11138 ?  127 ARG   A NH1 1 
ATOM   769  N  NH2 . ARG   A 1 115 ? 21.76797  16.80095  7.38951   1.000 18.24187 ?  127 ARG   A NH2 1 
ATOM   770  N  N   . ALA   A 1 116 ? 27.52783  17.45303  11.52347  1.000 14.59835 ?  128 ALA   A N   1 
ATOM   771  C  CA  . ALA   A 1 116 ? 27.99323  18.26054  12.64763  1.000 18.01336 ?  128 ALA   A CA  1 
ATOM   772  C  C   . ALA   A 1 116 ? 29.47871  18.06544  12.91379  1.000 15.68898 ?  128 ALA   A C   1 
ATOM   773  O  O   . ALA   A 1 116 ? 30.15708  19.00562  13.35453  1.000 21.61537 ?  128 ALA   A O   1 
ATOM   774  C  CB  . ALA   A 1 116 ? 27.16525  17.94521  13.89099  1.000 17.50425 ?  128 ALA   A CB  1 
ATOM   775  N  N   . ALA   A 1 117 ? 30.00547  16.87011  12.64578  1.000 14.94774 ?  129 ALA   A N   1 
ATOM   776  C  CA  . ALA   A 1 117 ? 31.41879  16.56839  12.82700  1.000 14.83563 ?  129 ALA   A CA  1 
ATOM   777  C  C   . ALA   A 1 117 ? 32.29568  17.05077  11.66962  1.000 14.99816 ?  129 ALA   A C   1 
ATOM   778  O  O   . ALA   A 1 117 ? 33.50731  16.78749  11.67694  1.000 19.60244 ?  129 ALA   A O   1 
ATOM   779  C  CB  . ALA   A 1 117 ? 31.61289  15.06480  13.05490  1.000 19.61656 ?  129 ALA   A CB  1 
ATOM   780  N  N   . GLY   A 1 118 ? 31.72593  17.73723  10.67485  1.000 14.09783 ?  130 GLY   A N   1 
ATOM   781  C  CA  . GLY   A 1 118 ? 32.48764  18.24668  9.55378   1.000 15.82642 ?  130 GLY   A CA  1 
ATOM   782  C  C   . GLY   A 1 118 ? 32.65661  17.30478  8.37999   1.000 15.27219 ?  130 GLY   A C   1 
ATOM   783  O  O   . GLY   A 1 118 ? 33.48720  17.57803  7.50454   1.000 16.16036 ?  130 GLY   A O   1 
ATOM   784  N  N   . VAL   A 1 119 ? 31.91367  16.20223  8.33386   1.000 14.10800 ?  131 VAL   A N   1 
ATOM   785  C  CA  . VAL   A 1 119 ? 31.98990  15.28216  7.20258   1.000 12.26859 ?  131 VAL   A CA  1 
ATOM   786  C  C   . VAL   A 1 119 ? 31.05471  15.78551  6.11682   1.000 10.16653 ?  131 VAL   A C   1 
ATOM   787  O  O   . VAL   A 1 119 ? 29.89510  16.09203  6.39636   1.000 11.59285 ?  131 VAL   A O   1 
ATOM   788  C  CB  . VAL   A 1 119 ? 31.57345  13.86534  7.63692   1.000 10.88501 ?  131 VAL   A CB  1 
ATOM   789  C  CG1 . VAL   A 1 119 ? 31.58854  12.90324  6.44508   1.000 12.53937 ?  131 VAL   A CG1 1 
ATOM   790  C  CG2 . VAL   A 1 119 ? 32.43549  13.36662  8.77253   1.000 13.07825 ?  131 VAL   A CG2 1 
ATOM   791  N  N   . ALA   A 1 120 ? 31.56016  15.86241  4.88487   1.000 10.53895 ?  132 ALA   A N   1 
ATOM   792  C  CA  . ALA   A 1 120 ? 30.71584  16.18611  3.73538   1.000 8.22983  ?  132 ALA   A CA  1 
ATOM   793  C  C   . ALA   A 1 120 ? 29.89756  14.95207  3.34835   1.000 12.17396 ?  132 ALA   A C   1 
ATOM   794  O  O   . ALA   A 1 120 ? 30.46248  13.91578  2.96999   1.000 12.99755 ?  132 ALA   A O   1 
ATOM   795  C  CB  . ALA   A 1 120 ? 31.59539  16.64419  2.57588   1.000 12.27799 ?  132 ALA   A CB  1 
ATOM   796  N  N   . THR   A 1 121 ? 28.57839  15.06203  3.42394   1.000 10.30456 ?  133 THR   A N   1 
ATOM   797  C  CA  . THR   A 1 121 ? 27.68611  13.93705  3.15731   1.000 8.06325  ?  133 THR   A CA  1 
ATOM   798  C  C   . THR   A 1 121 ? 27.10552  14.01241  1.74687   1.000 10.64512 ?  133 THR   A C   1 
ATOM   799  O  O   . THR   A 1 121 ? 26.76740  15.09224  1.25108   1.000 11.44002 ?  133 THR   A O   1 
ATOM   800  C  CB  . THR   A 1 121 ? 26.56448  13.88085  4.19198   1.000 10.46757 ?  133 THR   A CB  1 
ATOM   801  O  OG1 . THR   A 1 121 ? 25.87095  15.13867  4.23862   1.000 9.57472  ?  133 THR   A OG1 1 
ATOM   802  C  CG2 . THR   A 1 121 ? 27.15863  13.54113  5.54981   1.000 10.84766 ?  133 THR   A CG2 1 
ATOM   803  N  N   . TYR   A 1 122 ? 26.97764  12.83946  1.11611   1.000 9.74867  ?  134 TYR   A N   1 
ATOM   804  C  CA  . TYR   A 1 122 ? 26.58979  12.70326  -0.28416  1.000 10.01351 ?  134 TYR   A CA  1 
ATOM   805  C  C   . TYR   A 1 122 ? 25.56449  11.59651  -0.43380  1.000 9.24390  ?  134 TYR   A C   1 
ATOM   806  O  O   . TYR   A 1 122 ? 25.61679  10.58290  0.26679   1.000 9.76036  ?  134 TYR   A O   1 
ATOM   807  C  CB  . TYR   A 1 122 ? 27.77757  12.28498  -1.16612  1.000 11.67006 ?  134 TYR   A CB  1 
ATOM   808  C  CG  . TYR   A 1 122 ? 28.83985  13.34719  -1.32552  1.000 11.31801 ?  134 TYR   A CG  1 
ATOM   809  C  CD1 . TYR   A 1 122 ? 29.72739  13.63045  -0.29753  1.000 11.42338 ?  134 TYR   A CD1 1 
ATOM   810  C  CD2 . TYR   A 1 122 ? 28.95374  14.06070  -2.50297  1.000 11.49492 ?  134 TYR   A CD2 1 
ATOM   811  C  CE1 . TYR   A 1 122 ? 30.69385  14.61680  -0.43233  1.000 14.52891 ?  134 TYR   A CE1 1 
ATOM   812  C  CE2 . TYR   A 1 122 ? 29.92745  15.04480  -2.65289  1.000 12.47204 ?  134 TYR   A CE2 1 
ATOM   813  C  CZ  . TYR   A 1 122 ? 30.78693  15.30878  -1.61141  1.000 14.59117 ?  134 TYR   A CZ  1 
ATOM   814  O  OH  . TYR   A 1 122 ? 31.75086  16.28989  -1.77173  1.000 20.55363 ?  134 TYR   A OH  1 
ATOM   815  N  N   . ALA   A 1 123 ? 24.66711  11.77493  -1.39472  1.000 8.56145  ?  135 ALA   A N   1 
ATOM   816  C  CA  . ALA   A 1 123 ? 23.81298  10.70165  -1.88965  1.000 8.54234  ?  135 ALA   A CA  1 
ATOM   817  C  C   . ALA   A 1 123 ? 23.34507  11.11260  -3.27371  1.000 10.59497 ?  135 ALA   A C   1 
ATOM   818  O  O   . ALA   A 1 123 ? 23.52404  12.25567  -3.68924  1.000 10.81782 ?  135 ALA   A O   1 
ATOM   819  C  CB  . ALA   A 1 123 ? 22.61900  10.45306  -0.97321  1.000 9.19468  ?  135 ALA   A CB  1 
ATOM   820  N  N   . SER   A 1 124 ? 22.76277  10.17337  -3.99863  1.000 9.34416  ?  136 SER   A N   1 
ATOM   821  C  CA  . SER   A 1 124 ? 22.19995  10.54763  -5.29207  1.000 9.98026  ?  136 SER   A CA  1 
ATOM   822  C  C   . SER   A 1 124 ? 21.02520  11.49456  -5.07453  1.000 10.45030 ?  136 SER   A C   1 
ATOM   823  O  O   . SER   A 1 124 ? 20.44809  11.53087  -3.98497  1.000 10.54831 ?  136 SER   A O   1 
ATOM   824  C  CB  . SER   A 1 124 ? 21.69000  9.31183   -6.03807  1.000 10.62496 ?  136 SER   A CB  1 
ATOM   825  O  OG  . SER   A 1 124 ? 20.45691  8.87853   -5.48073  1.000 10.80730 ?  136 SER   A OG  1 
ATOM   826  N  N   . PRO   A 1 125 ? 20.63460  12.25986  -6.10356  1.000 9.86513  ?  137 PRO   A N   1 
ATOM   827  C  CA  . PRO   A 1 125 ? 19.45728  13.13004  -5.94065  1.000 11.95492 ?  137 PRO   A CA  1 
ATOM   828  C  C   . PRO   A 1 125 ? 18.18524  12.34352  -5.70698  1.000 10.85404 ?  137 PRO   A C   1 
ATOM   829  O  O   . PRO   A 1 125 ? 17.29093  12.81173  -4.99326  1.000 10.45174 ?  137 PRO   A O   1 
ATOM   830  C  CB  . PRO   A 1 125 ? 19.43162  13.96565  -7.22999  1.000 14.26824 ?  137 PRO   A CB  1 
ATOM   831  C  CG  . PRO   A 1 125 ? 20.30283  13.23277  -8.19762  1.000 14.67261 ?  137 PRO   A CG  1 
ATOM   832  C  CD  . PRO   A 1 125 ? 21.32057  12.46431  -7.39482  1.000 9.86457  ?  137 PRO   A CD  1 
ATOM   833  N  N   . SER   A 1 126 ? 18.10034  11.12409  -6.24291  1.000 9.79298  ?  138 SER   A N   1 
ATOM   834  C  CA  A SER   A 1 126 ? 16.93822  10.28970  -5.97274  0.765 12.53137 ?  138 SER   A CA  1 
ATOM   835  C  CA  B SER   A 1 126 ? 16.93944  10.28550  -5.97331  0.235 12.49235 ?  138 SER   A CA  1 
ATOM   836  C  C   . SER   A 1 126 ? 16.88215  9.90299   -4.50300  1.000 8.77702  ?  138 SER   A C   1 
ATOM   837  O  O   . SER   A 1 126 ? 15.82113  9.99406   -3.87128  1.000 11.26682 ?  138 SER   A O   1 
ATOM   838  C  CB  A SER   A 1 126 ? 16.97740  9.04862   -6.85810  0.765 11.72639 ?  138 SER   A CB  1 
ATOM   839  C  CB  B SER   A 1 126 ? 16.97878  9.03865   -6.85335  0.235 11.82003 ?  138 SER   A CB  1 
ATOM   840  O  OG  A SER   A 1 126 ? 15.83044  8.24272   -6.66383  0.765 15.96579 ?  138 SER   A OG  1 
ATOM   841  O  OG  B SER   A 1 126 ? 18.08054  8.21689   -6.51377  0.235 10.50914 ?  138 SER   A OG  1 
ATOM   842  N  N   . THR   A 1 127 ? 18.02285  9.50699   -3.93377  1.000 10.11510 ?  139 THR   A N   1 
ATOM   843  C  CA  . THR   A 1 127 ? 18.07800  9.18381   -2.50993  1.000 10.05833 ?  139 THR   A CA  1 
ATOM   844  C  C   . THR   A 1 127 ? 17.71129  10.38567  -1.64794  1.000 8.56143  ?  139 THR   A C   1 
ATOM   845  O  O   . THR   A 1 127 ? 16.95494  10.24857  -0.68332  1.000 10.51750 ?  139 THR   A O   1 
ATOM   846  C  CB  . THR   A 1 127 ? 19.47407  8.68187   -2.14536  1.000 9.90576  ?  139 THR   A CB  1 
ATOM   847  O  OG1 . THR   A 1 127 ? 19.70226  7.42393   -2.78656  1.000 8.73511  ?  139 THR   A OG1 1 
ATOM   848  C  CG2 . THR   A 1 127 ? 19.63731  8.49808   -0.63061  1.000 9.41788  ?  139 THR   A CG2 1 
ATOM   849  N  N   . ARG   A 1 128 ? 18.25283  11.56555  -1.96198  1.000 8.75928  ?  140 ARG   A N   1 
ATOM   850  C  CA  . ARG   A 1 128 ? 17.94331  12.74069  -1.15223  1.000 10.88958 ?  140 ARG   A CA  1 
ATOM   851  C  C   . ARG   A 1 128 ? 16.45473  13.04370  -1.16732  1.000 10.98849 ?  140 ARG   A C   1 
ATOM   852  O  O   . ARG   A 1 128 ? 15.86843  13.37446  -0.12628  1.000 11.14013 ?  140 ARG   A O   1 
ATOM   853  C  CB  . ARG   A 1 128 ? 18.72256  13.93697  -1.67926  1.000 9.73721  ?  140 ARG   A CB  1 
ATOM   854  C  CG  . ARG   A 1 128 ? 20.22764  13.83649  -1.40881  1.000 10.98760 ?  140 ARG   A CG  1 
ATOM   855  C  CD  . ARG   A 1 128 ? 20.97480  15.07052  -1.92330  1.000 12.28683 ?  140 ARG   A CD  1 
ATOM   856  N  NE  . ARG   A 1 128 ? 20.66696  16.27389  -1.14971  1.000 14.40968 ?  140 ARG   A NE  1 
ATOM   857  C  CZ  . ARG   A 1 128 ? 19.86889  17.26016  -1.54508  1.000 17.00946 ?  140 ARG   A CZ  1 
ATOM   858  N  NH1 . ARG   A 1 128 ? 19.23060  17.21602  -2.70341  1.000 16.79440 ?  140 ARG   A NH1 1 
ATOM   859  N  NH2 . ARG   A 1 128 ? 19.71937  18.32817  -0.76337  1.000 19.09297 ?  140 ARG   A NH2 1 
ATOM   860  N  N   . ARG   A 1 129 ? 15.82221  12.93271  -2.33586  1.000 10.72091 ?  141 ARG   A N   1 
ATOM   861  C  CA  . ARG   A 1 129 ? 14.39502  13.21438  -2.42059  1.000 12.16607 ?  141 ARG   A CA  1 
ATOM   862  C  C   . ARG   A 1 129 ? 13.58743  12.20949  -1.61740  1.000 11.22087 ?  141 ARG   A C   1 
ATOM   863  O  O   . ARG   A 1 129 ? 12.67264  12.58287  -0.87811  1.000 12.82642 ?  141 ARG   A O   1 
ATOM   864  C  CB  . ARG   A 1 129 ? 13.94483  13.20365  -3.87678  1.000 12.39206 ?  141 ARG   A CB  1 
ATOM   865  C  CG  . ARG   A 1 129 ? 12.46089  13.49666  -4.03697  1.000 16.56627 ?  141 ARG   A CG  1 
ATOM   866  C  CD  . ARG   A 1 129 ? 12.04747  13.48215  -5.50444  1.000 18.51676 ?  141 ARG   A CD  1 
ATOM   867  N  NE  . ARG   A 1 129 ? 12.75158  14.49858  -6.27883  1.000 20.13567 ?  141 ARG   A NE  1 
ATOM   868  C  CZ  . ARG   A 1 129 ? 13.73070  14.24197  -7.13240  1.000 26.61864 ?  141 ARG   A CZ  1 
ATOM   869  N  NH1 . ARG   A 1 129 ? 14.18591  13.01291  -7.30820  1.000 22.01060 ?  141 ARG   A NH1 1 
ATOM   870  N  NH2 . ARG   A 1 129 ? 14.27025  15.24400  -7.82235  1.000 28.63394 ?  141 ARG   A NH2 1 
ATOM   871  N  N   . LEU   A 1 130 ? 13.89527  10.91787  -1.76240  1.000 9.91004  ?  142 LEU   A N   1 
ATOM   872  C  CA  . LEU   A 1 130 ? 13.15806  9.89534   -1.03059  1.000 9.48338  ?  142 LEU   A CA  1 
ATOM   873  C  C   . LEU   A 1 130 ? 13.36671  10.03898  0.47032   1.000 10.15104 ?  142 LEU   A C   1 
ATOM   874  O  O   . LEU   A 1 130 ? 12.42791  9.82591   1.25466   1.000 11.53755 ?  142 LEU   A O   1 
ATOM   875  C  CB  . LEU   A 1 130 ? 13.59597  8.50813   -1.51093  1.000 11.22629 ?  142 LEU   A CB  1 
ATOM   876  C  CG  . LEU   A 1 130 ? 13.07249  8.13731   -2.90616  1.000 10.47307 ?  142 LEU   A CG  1 
ATOM   877  C  CD1 . LEU   A 1 130 ? 13.89631  7.01598   -3.52431  1.000 11.60994 ?  142 LEU   A CD1 1 
ATOM   878  C  CD2 . LEU   A 1 130 ? 11.61536  7.71589   -2.81514  1.000 14.75660 ?  142 LEU   A CD2 1 
ATOM   879  N  N   . ALA   A 1 131 ? 14.58456  10.40757  0.89323   1.000 10.28615 ?  143 ALA   A N   1 
ATOM   880  C  CA  . ALA   A 1 131 ? 14.84583  10.62991  2.31319   1.000 11.28966 ?  143 ALA   A CA  1 
ATOM   881  C  C   . ALA   A 1 131 ? 13.97451  11.75889  2.83315   1.000 11.26771 ?  143 ALA   A C   1 
ATOM   882  O  O   . ALA   A 1 131 ? 13.35843  11.64055  3.89866   1.000 12.31800 ?  143 ALA   A O   1 
ATOM   883  C  CB  . ALA   A 1 131 ? 16.33354  10.92436  2.54320   1.000 12.03192 ?  143 ALA   A CB  1 
ATOM   884  N  N   . GLU   A 1 132 ? 13.86724  12.83031  2.05958   1.000 11.57671 ?  144 GLU   A N   1 
ATOM   885  C  CA  . GLU   A 1 132 ? 13.04298  13.95826  2.47379   1.000 15.07276 ?  144 GLU   A CA  1 
ATOM   886  C  C   . GLU   A 1 132 ? 11.58546  13.55402  2.60065   1.000 15.10715 ?  144 GLU   A C   1 
ATOM   887  O  O   . GLU   A 1 132 ? 10.92191  13.89320  3.58878   1.000 16.58222 ?  144 GLU   A O   1 
ATOM   888  C  CB  . GLU   A 1 132 ? 13.21578  15.10337  1.48851   1.000 16.23257 ?  144 GLU   A CB  1 
ATOM   889  C  CG  . GLU   A 1 132 ? 12.50811  16.39155  1.92115   1.000 15.31281 ?  144 GLU   A CG  1 
ATOM   890  C  CD  . GLU   A 1 132 ? 12.85655  17.55795  1.01402   1.000 25.70673 ?  144 GLU   A CD  1 
ATOM   891  O  OE1 . GLU   A 1 132 ? 12.56368  17.47587  -0.19822  1.000 29.91512 ?  144 GLU   A OE1 1 
ATOM   892  O  OE2 . GLU   A 1 132 ? 13.42067  18.55860  1.50891   1.000 36.64178 ?  144 GLU   A OE2 1 
ATOM   893  N  N   . VAL   A 1 133 ? 11.06637  12.82400  1.61194   1.000 13.70331 ?  145 VAL   A N   1 
ATOM   894  C  CA  . VAL   A 1 133 ? 9.68192   12.36466  1.67274   1.000 18.62789 ?  145 VAL   A CA  1 
ATOM   895  C  C   . VAL   A 1 133 ? 9.44128   11.52761  2.92375   1.000 16.31334 ?  145 VAL   A C   1 
ATOM   896  O  O   . VAL   A 1 133 ? 8.39206   11.63639  3.57772   1.000 19.31625 ?  145 VAL   A O   1 
ATOM   897  C  CB  . VAL   A 1 133 ? 9.33192   11.59947  0.38630   1.000 17.12409 ?  145 VAL   A CB  1 
ATOM   898  C  CG1 . VAL   A 1 133 ? 7.99125   10.87206  0.53991   1.000 23.41387 ?  145 VAL   A CG1 1 
ATOM   899  C  CG2 . VAL   A 1 133 ? 9.30198   12.56547  -0.79558  1.000 17.64899 ?  145 VAL   A CG2 1 
ATOM   900  N  N   . GLU   A 1 134 ? 10.41401  10.69441  3.29280   1.000 13.53629 ?  146 GLU   A N   1 
ATOM   901  C  CA  . GLU   A 1 134 ? 10.27552  9.82311   4.45247   1.000 14.21741 ?  146 GLU   A CA  1 
ATOM   902  C  C   . GLU   A 1 134 ? 10.47039  10.56182  5.77114   1.000 12.89897 ?  146 GLU   A C   1 
ATOM   903  O  O   . GLU   A 1 134 ? 10.25208  9.96342   6.83509   1.000 16.43321 ?  146 GLU   A O   1 
ATOM   904  C  CB  . GLU   A 1 134 ? 11.30351  8.68510   4.34593   1.000 14.84613 ?  146 GLU   A CB  1 
ATOM   905  C  CG  . GLU   A 1 134 ? 10.93825  7.41714   5.10379   1.000 20.06172 ?  146 GLU   A CG  1 
ATOM   906  C  CD  . GLU   A 1 134 ? 9.81594   6.65489   4.43418   1.000 31.44431 ?  146 GLU   A CD  1 
ATOM   907  O  OE1 . GLU   A 1 134 ? 9.48342   6.98554   3.27692   1.000 22.74311 ?  146 GLU   A OE1 1 
ATOM   908  O  OE2 . GLU   A 1 134 ? 9.25337   5.74067   5.07191   1.000 41.25332 ?  146 GLU   A OE2 1 
ATOM   909  N  N   . GLY   A 1 135 ? 10.85810  11.83578  5.73246   1.000 13.50093 ?  147 GLY   A N   1 
ATOM   910  C  CA  . GLY   A 1 135 ? 11.21014  12.55200  6.94994   1.000 14.73645 ?  147 GLY   A CA  1 
ATOM   911  C  C   . GLY   A 1 135 ? 12.52222  12.12464  7.56220   1.000 15.23801 ?  147 GLY   A C   1 
ATOM   912  O  O   . GLY   A 1 135 ? 12.76024  12.37894  8.74781   1.000 15.08497 ?  147 GLY   A O   1 
ATOM   913  N  N   . ASN   A 1 136 ? 13.39243  11.48656  6.78104   1.000 11.90510 ?  148 ASN   A N   1 
ATOM   914  C  CA  . ASN   A 1 136 ? 14.68939  11.04092  7.24988   1.000 11.63866 ?  148 ASN   A CA  1 
ATOM   915  C  C   . ASN   A 1 136 ? 15.72271  12.15557  7.07724   1.000 11.33847 ?  148 ASN   A C   1 
ATOM   916  O  O   . ASN   A 1 136 ? 15.47211  13.19717  6.47061   1.000 13.74884 ?  148 ASN   A O   1 
ATOM   917  C  CB  . ASN   A 1 136 ? 15.13291  9.81762   6.44001   1.000 11.72887 ?  148 ASN   A CB  1 
ATOM   918  C  CG  . ASN   A 1 136 ? 14.30737  8.57695   6.74268   1.000 15.88073 ?  148 ASN   A CG  1 
ATOM   919  O  OD1 . ASN   A 1 136 ? 13.46687  8.57478   7.64746   1.000 15.13729 ?  148 ASN   A OD1 1 
ATOM   920  N  ND2 . ASN   A 1 136 ? 14.55101  7.49732   5.99079   1.000 14.07942 ?  148 ASN   A ND2 1 
ATOM   921  N  N   . GLU   A 1 137 ? 16.91443  11.91533  7.61287   1.000 12.32630 ?  149 GLU   A N   1 
ATOM   922  C  CA  . GLU   A 1 137 ? 18.00476  12.85944  7.44001   1.000 12.10731 ?  149 GLU   A CA  1 
ATOM   923  C  C   . GLU   A 1 137 ? 18.47816  12.86072  5.98631   1.000 11.62628 ?  149 GLU   A C   1 
ATOM   924  O  O   . GLU   A 1 137 ? 18.46248  11.82954  5.30541   1.000 12.90680 ?  149 GLU   A O   1 
ATOM   925  C  CB  . GLU   A 1 137 ? 19.14432  12.50117  8.38393   1.000 12.34209 ?  149 GLU   A CB  1 
ATOM   926  C  CG  . GLU   A 1 137 ? 18.71626  12.60084  9.85965   1.000 13.62822 ?  149 GLU   A CG  1 
ATOM   927  C  CD  . GLU   A 1 137 ? 19.56072  11.73263  10.74945  1.000 19.85722 ?  149 GLU   A CD  1 
ATOM   928  O  OE1 . GLU   A 1 137 ? 20.76173  12.02595  10.87106  1.000 15.88755 ?  149 GLU   A OE1 1 
ATOM   929  O  OE2 . GLU   A 1 137 ? 19.02765  10.74889  11.31679  1.000 25.80575 ?  149 GLU   A OE2 1 
ATOM   930  N  N   . ILE   A 1 138 ? 18.90640  14.03216  5.51654   1.000 12.00361 ?  150 ILE   A N   1 
ATOM   931  C  CA  . ILE   A 1 138 ? 19.15881  14.27099  4.09219   1.000 11.40500 ?  150 ILE   A CA  1 
ATOM   932  C  C   . ILE   A 1 138 ? 20.62390  14.62615  3.86657   1.000 12.29171 ?  150 ILE   A C   1 
ATOM   933  O  O   . ILE   A 1 138 ? 21.07770  15.67840  4.32939   1.000 13.31882 ?  150 ILE   A O   1 
ATOM   934  C  CB  . ILE   A 1 138 ? 18.26743  15.39319  3.54075   1.000 12.44269 ?  150 ILE   A CB  1 
ATOM   935  C  CG1 . ILE   A 1 138 ? 16.79222  15.08511  3.82058   1.000 13.12915 ?  150 ILE   A CG1 1 
ATOM   936  C  CG2 . ILE   A 1 138 ? 18.50993  15.55300  2.04146   1.000 12.25002 ?  150 ILE   A CG2 1 
ATOM   937  C  CD1 . ILE   A 1 138 ? 15.91170  16.33376  3.78929   1.000 16.75181 ?  150 ILE   A CD1 1 
ATOM   938  N  N   . PRO   A 1 139 ? 21.40085  13.78599  3.18801   1.000 10.05898 ?  151 PRO   A N   1 
ATOM   939  C  CA  . PRO   A 1 139 ? 22.77847  14.14987  2.85622   1.000 12.70699 ?  151 PRO   A CA  1 
ATOM   940  C  C   . PRO   A 1 139 ? 22.84970  15.47432  2.11058   1.000 12.24158 ?  151 PRO   A C   1 
ATOM   941  O  O   . PRO   A 1 139 ? 21.95754  15.82549  1.33543   1.000 12.78794 ?  151 PRO   A O   1 
ATOM   942  C  CB  . PRO   A 1 139 ? 23.23956  12.98647  1.97024   1.000 10.38090 ?  151 PRO   A CB  1 
ATOM   943  C  CG  . PRO   A 1 139 ? 22.42625  11.82004  2.46897   1.000 11.73984 ?  151 PRO   A CG  1 
ATOM   944  C  CD  . PRO   A 1 139 ? 21.06649  12.40406  2.78344   1.000 10.60762 ?  151 PRO   A CD  1 
ATOM   945  N  N   . THR   A 1 140 ? 23.95216  16.19127  2.32400   1.000 11.18468 ?  152 THR   A N   1 
ATOM   946  C  CA  . THR   A 1 140 ? 24.07609  17.54288  1.77899   1.000 10.87042 ?  152 THR   A CA  1 
ATOM   947  C  C   . THR   A 1 140 ? 24.20353  17.53563  0.25919   1.000 11.44729 ?  152 THR   A C   1 
ATOM   948  O  O   . THR   A 1 140 ? 23.49098  18.26975  -0.43797  1.000 11.80649 ?  152 THR   A O   1 
ATOM   949  C  CB  . THR   A 1 140 ? 25.27698  18.22909  2.41991   1.000 11.42946 ?  152 THR   A CB  1 
ATOM   950  O  OG1 . THR   A 1 140 ? 24.98551  18.49715  3.80013   1.000 14.82223 ?  152 THR   A OG1 1 
ATOM   951  C  CG2 . THR   A 1 140 ? 25.57279  19.55119  1.72777   1.000 12.70686 ?  152 THR   A CG2 1 
ATOM   952  N  N   . HIS   A 1 141 ? 25.11334  16.73582  -0.27077  1.000 11.52570 ?  153 HIS   A N   1 
ATOM   953  C  CA  . HIS   A 1 141 ? 25.49409  16.83607  -1.66518  1.000 11.93449 ?  153 HIS   A CA  1 
ATOM   954  C  C   . HIS   A 1 141 ? 24.80409  15.78181  -2.51388  1.000 12.61876 ?  153 HIS   A C   1 
ATOM   955  O  O   . HIS   A 1 141 ? 24.48259  14.68980  -2.04676  1.000 11.52798 ?  153 HIS   A O   1 
ATOM   956  C  CB  . HIS   A 1 141 ? 26.99128  16.64869  -1.80536  1.000 12.84310 ?  153 HIS   A CB  1 
ATOM   957  C  CG  . HIS   A 1 141 ? 27.77126  17.82032  -1.33517  1.000 10.85850 ?  153 HIS   A CG  1 
ATOM   958  N  ND1 . HIS   A 1 141 ? 27.90293  18.96316  -2.09101  1.000 12.27445 ?  153 HIS   A ND1 1 
ATOM   959  C  CD2 . HIS   A 1 141 ? 28.46634  18.02892  -0.20105  1.000 9.47643  ?  153 HIS   A CD2 1 
ATOM   960  C  CE1 . HIS   A 1 141 ? 28.64482  19.83306  -1.44104  1.000 14.70189 ?  153 HIS   A CE1 1 
ATOM   961  N  NE2 . HIS   A 1 141 ? 28.99215  19.29243  -0.29118  1.000 13.63398 ?  153 HIS   A NE2 1 
ATOM   962  N  N   . SER   A 1 142 ? 24.64191  16.10870  -3.78469  1.000 10.96780 ?  154 SER   A N   1 
ATOM   963  C  CA  . SER   A 1 142 ? 23.99069  15.25998  -4.76995  1.000 10.98506 ?  154 SER   A CA  1 
ATOM   964  C  C   . SER   A 1 142 ? 25.02773  14.67124  -5.70590  1.000 12.94127 ?  154 SER   A C   1 
ATOM   965  O  O   . SER   A 1 142 ? 25.82525  15.40167  -6.30890  1.000 14.60260 ?  154 SER   A O   1 
ATOM   966  C  CB  . SER   A 1 142 ? 22.99679  16.07397  -5.59363  1.000 12.97234 ?  154 SER   A CB  1 
ATOM   967  O  OG  . SER   A 1 142 ? 21.93969  16.54699  -4.78623  1.000 14.78634 ?  154 SER   A OG  1 
ATOM   968  N  N   . LEU   A 1 143 ? 24.99545  13.35126  -5.85314  1.000 11.25489 ?  155 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 143 ? 25.89180  12.63856  -6.75762  1.000 13.17730 ?  155 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 143 ? 25.25904  12.57124  -8.14093  1.000 13.15316 ?  155 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 143 ? 24.23310  11.90986  -8.32912  1.000 16.72054 ?  155 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 143 ? 26.11976  11.22856  -6.22200  1.000 12.55237 ?  155 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 143 ? 26.85033  11.13209  -4.87508  1.000 12.10204 ?  155 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 143 ? 26.61116  9.76535   -4.24075  1.000 12.17107 ?  155 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 143 ? 28.34256  11.41079  -5.02072  1.000 15.79174 ?  155 LEU   A CD2 1 
ATOM   976  N  N   . GLU   A 1 144 ? 25.88134  13.23327  -9.11236  1.000 17.29111 ?  156 GLU   A N   1 
ATOM   977  C  CA  . GLU   A 1 144 ? 25.39439  13.17480  -10.48142 1.000 17.20524 ?  156 GLU   A CA  1 
ATOM   978  C  C   . GLU   A 1 144 ? 25.87060  11.89791  -11.16957 1.000 15.00286 ?  156 GLU   A C   1 
ATOM   979  O  O   . GLU   A 1 144 ? 26.79963  11.22323  -10.72154 1.000 15.79465 ?  156 GLU   A O   1 
ATOM   980  C  CB  . GLU   A 1 144 ? 25.89287  14.37751  -11.28774 1.000 25.67571 ?  156 GLU   A CB  1 
ATOM   981  C  CG  . GLU   A 1 144 ? 25.73704  15.72119  -10.59750 1.000 35.45285 ?  156 GLU   A CG  1 
ATOM   982  C  CD  . GLU   A 1 144 ? 24.32881  16.27823  -10.69023 1.000 41.30283 ?  156 GLU   A CD  1 
ATOM   983  O  OE1 . GLU   A 1 144 ? 24.19533  17.51088  -10.84908 1.000 50.61165 ?  156 GLU   A OE1 1 
ATOM   984  O  OE2 . GLU   A 1 144 ? 23.35685  15.49603  -10.60889 1.000 43.08390 ?  156 GLU   A OE2 1 
ATOM   985  N  N   . GLY   A 1 145 ? 25.21703  11.57789  -12.28222 1.000 15.75278 ?  157 GLY   A N   1 
ATOM   986  C  CA  . GLY   A 1 145 ? 25.68807  10.51287  -13.14441 1.000 14.10591 ?  157 GLY   A CA  1 
ATOM   987  C  C   . GLY   A 1 145 ? 25.29302  9.12214   -12.71719 1.000 12.10232 ?  157 GLY   A C   1 
ATOM   988  O  O   . GLY   A 1 145 ? 25.90823  8.15339   -13.17474 1.000 14.71188 ?  157 GLY   A O   1 
ATOM   989  N  N   . LEU   A 1 146 ? 24.27420  8.99105   -11.85831 1.000 12.31400 ?  158 LEU   A N   1 
ATOM   990  C  CA  . LEU   A 1 146 ? 23.85516  7.68421   -11.37179 1.000 11.92796 ?  158 LEU   A CA  1 
ATOM   991  C  C   . LEU   A 1 146 ? 22.36155  7.44806   -11.56166 1.000 10.47411 ?  158 LEU   A C   1 
ATOM   992  O  O   . LEU   A 1 146 ? 21.78698  6.59856   -10.88622 1.000 13.19706 ?  158 LEU   A O   1 
ATOM   993  C  CB  . LEU   A 1 146 ? 24.24144  7.51495   -9.90061  1.000 12.62100 ?  158 LEU   A CB  1 
ATOM   994  C  CG  . LEU   A 1 146 ? 25.74203  7.45949   -9.61254  1.000 11.45071 ?  158 LEU   A CG  1 
ATOM   995  C  CD1 . LEU   A 1 146 ? 26.05350  7.71322   -8.12945  1.000 11.73222 ?  158 LEU   A CD1 1 
ATOM   996  C  CD2 . LEU   A 1 146 ? 26.30820  6.11262   -10.11390 1.000 12.97418 ?  158 LEU   A CD2 1 
ATOM   997  N  N   . SER   A 1 147 ? 21.71444  8.18015   -12.47240 1.000 13.69415 ?  159 SER   A N   1 
ATOM   998  C  CA  . SER   A 1 147 ? 20.25766  8.14293   -12.53707 1.000 14.88305 ?  159 SER   A CA  1 
ATOM   999  C  C   . SER   A 1 147 ? 19.71194  6.99927   -13.37775 1.000 16.08026 ?  159 SER   A C   1 
ATOM   1000 O  O   . SER   A 1 147 ? 18.52739  6.67425   -13.24298 1.000 16.77645 ?  159 SER   A O   1 
ATOM   1001 C  CB  . SER   A 1 147 ? 19.70164  9.46316   -13.07827 1.000 20.81176 ?  159 SER   A CB  1 
ATOM   1002 O  OG  . SER   A 1 147 ? 20.07231  9.63721   -14.42697 1.000 21.44868 ?  159 SER   A OG  1 
ATOM   1003 N  N   . SER   A 1 148 ? 20.53124  6.38121   -14.22699 1.000 13.18094 ?  160 SER   A N   1 
ATOM   1004 C  CA  . SER   A 1 148 ? 20.06635  5.32553   -15.12275 1.000 15.46473 ?  160 SER   A CA  1 
ATOM   1005 C  C   . SER   A 1 148 ? 20.75559  4.01934   -14.76973 1.000 12.30301 ?  160 SER   A C   1 
ATOM   1006 O  O   . SER   A 1 148 ? 21.95744  4.00621   -14.48500 1.000 11.94873 ?  160 SER   A O   1 
ATOM   1007 C  CB  . SER   A 1 148 ? 20.37026  5.66355   -16.58896 1.000 17.15970 ?  160 SER   A CB  1 
ATOM   1008 O  OG  . SER   A 1 148 ? 19.80734  6.91707   -16.95691 1.000 22.80061 ?  160 SER   A OG  1 
ATOM   1009 N  N   . SER   A 1 149 ? 19.99825  2.92131   -14.80365 1.000 13.45471 ?  161 SER   A N   1 
ATOM   1010 C  CA  A SER   A 1 149 ? 20.57318  1.62304   -14.47115 0.470 12.58362 ?  161 SER   A CA  1 
ATOM   1011 C  CA  B SER   A 1 149 ? 20.56039  1.61445   -14.48484 0.530 12.56430 ?  161 SER   A CA  1 
ATOM   1012 C  C   . SER   A 1 149 ? 21.79823  1.34554   -15.32984 1.000 12.52569 ?  161 SER   A C   1 
ATOM   1013 O  O   . SER   A 1 149 ? 21.79128  1.56428   -16.54876 1.000 14.45358 ?  161 SER   A O   1 
ATOM   1014 C  CB  A SER   A 1 149 ? 19.55140  0.50291   -14.65941 0.470 13.72709 ?  161 SER   A CB  1 
ATOM   1015 C  CB  B SER   A 1 149 ? 19.51843  0.52828   -14.73953 0.530 13.76950 ?  161 SER   A CB  1 
ATOM   1016 O  OG  A SER   A 1 149 ? 19.01958  0.50994   -15.96718 0.470 17.37339 ?  161 SER   A OG  1 
ATOM   1017 O  OG  B SER   A 1 149 ? 18.31876  0.81571   -14.04104 0.530 12.01714 ?  161 SER   A OG  1 
ATOM   1018 N  N   . GLY   A 1 150 ? 22.85214  0.86488   -14.67610 1.000 12.52733 ?  162 GLY   A N   1 
ATOM   1019 C  CA  . GLY   A 1 150 ? 24.11648  0.61009   -15.32633 1.000 11.99051 ?  162 GLY   A CA  1 
ATOM   1020 C  C   . GLY   A 1 150 ? 25.09548  1.76114   -15.25372 1.000 14.46273 ?  162 GLY   A C   1 
ATOM   1021 O  O   . GLY   A 1 150 ? 26.24816  1.60299   -15.67089 1.000 15.05181 ?  162 GLY   A O   1 
ATOM   1022 N  N   . ASP   A 1 151 ? 24.67369  2.91560   -14.73879 1.000 12.51879 ?  163 ASP   A N   1 
ATOM   1023 C  CA  . ASP   A 1 151 ? 25.57588  4.05655   -14.62768 1.000 11.66851 ?  163 ASP   A CA  1 
ATOM   1024 C  C   . ASP   A 1 151 ? 26.60312  3.83146   -13.52669 1.000 12.51958 ?  163 ASP   A C   1 
ATOM   1025 O  O   . ASP   A 1 151 ? 26.28788  3.29977   -12.46143 1.000 11.17237 ?  163 ASP   A O   1 
ATOM   1026 C  CB  . ASP   A 1 151 ? 24.80059  5.32173   -14.25654 1.000 12.56243 ?  163 ASP   A CB  1 
ATOM   1027 C  CG  . ASP   A 1 151 ? 24.08099  5.95511   -15.42959 1.000 13.77448 ?  163 ASP   A CG  1 
ATOM   1028 O  OD1 . ASP   A 1 151 ? 24.32096  5.56954   -16.59913 1.000 18.00994 ?  163 ASP   A OD1 1 
ATOM   1029 O  OD2 . ASP   A 1 151 ? 23.27180  6.86116   -15.15104 1.000 16.64094 ?  163 ASP   A OD2 1 
ATOM   1030 N  N   . ALA   A 1 152 ? 27.82569  4.28672   -13.76727 1.000 13.50897 ?  164 ALA   A N   1 
ATOM   1031 C  CA  . ALA   A 1 152 ? 28.89154  4.20095   -12.78352 1.000 12.53182 ?  164 ALA   A CA  1 
ATOM   1032 C  C   . ALA   A 1 152 ? 29.65900  5.50945   -12.77900 1.000 14.79363 ?  164 ALA   A C   1 
ATOM   1033 O  O   . ALA   A 1 152 ? 29.81822  6.15028   -13.82368 1.000 16.25856 ?  164 ALA   A O   1 
ATOM   1034 C  CB  . ALA   A 1 152 ? 29.85275  3.05448   -13.12303 1.000 15.66530 ?  164 ALA   A CB  1 
ATOM   1035 N  N   . VAL   A 1 153 ? 30.14125  5.90667   -11.59696 1.000 12.72614 ?  165 VAL   A N   1 
ATOM   1036 C  CA  . VAL   A 1 153 ? 31.02985  7.05460   -11.45481 1.000 13.50526 ?  165 VAL   A CA  1 
ATOM   1037 C  C   . VAL   A 1 153 ? 32.11375  6.73137   -10.43710 1.000 15.28961 ?  165 VAL   A C   1 
ATOM   1038 O  O   . VAL   A 1 153 ? 31.91021  5.96149   -9.49286  1.000 15.59112 ?  165 VAL   A O   1 
ATOM   1039 C  CB  . VAL   A 1 153 ? 30.31047  8.35618   -11.04916 1.000 15.35167 ?  165 VAL   A CB  1 
ATOM   1040 C  CG1 . VAL   A 1 153 ? 29.22153  8.72767   -12.04791 1.000 18.93941 ?  165 VAL   A CG1 1 
ATOM   1041 C  CG2 . VAL   A 1 153 ? 29.72895  8.22264   -9.65185  1.000 14.81598 ?  165 VAL   A CG2 1 
ATOM   1042 N  N   . ARG   A 1 154 ? 33.28486  7.31400   -10.64089 1.000 13.32065 ?  166 ARG   A N   1 
ATOM   1043 C  CA  . ARG   A 1 154 ? 34.34461  7.22570   -9.65750  1.000 11.56267 ?  166 ARG   A CA  1 
ATOM   1044 C  C   . ARG   A 1 154 ? 34.12139  8.29134   -8.59150  1.000 13.27395 ?  166 ARG   A C   1 
ATOM   1045 O  O   . ARG   A 1 154 ? 33.69024  9.40611   -8.88935  1.000 14.90677 ?  166 ARG   A O   1 
ATOM   1046 C  CB  . ARG   A 1 154 ? 35.70674  7.42790   -10.33635 1.000 14.85994 ?  166 ARG   A CB  1 
ATOM   1047 C  CG  . ARG   A 1 154 ? 36.88621  7.16385   -9.42332  1.000 15.66257 ?  166 ARG   A CG  1 
ATOM   1048 C  CD  . ARG   A 1 154 ? 37.18041  5.67357   -9.30693  1.000 22.85411 ?  166 ARG   A CD  1 
ATOM   1049 N  NE  . ARG   A 1 154 ? 38.21180  5.43187   -8.30800  1.000 22.69079 ?  166 ARG   A NE  1 
ATOM   1050 C  CZ  . ARG   A 1 154 ? 39.21819  4.58754   -8.46435  1.000 18.24636 ?  166 ARG   A CZ  1 
ATOM   1051 N  NH1 . ARG   A 1 154 ? 39.27852  3.77361   -9.50816  1.000 21.27543 ?  166 ARG   A NH1 1 
ATOM   1052 N  NH2 . ARG   A 1 154 ? 40.20357  4.58353   -7.57499  1.000 23.27673 ?  166 ARG   A NH2 1 
ATOM   1053 N  N   . PHE   A 1 155 ? 34.37608  7.92412   -7.33710  1.000 12.77225 ?  167 PHE   A N   1 
ATOM   1054 C  CA  . PHE   A 1 155 ? 34.23661  8.84333   -6.20839  1.000 10.52898 ?  167 PHE   A CA  1 
ATOM   1055 C  C   . PHE   A 1 155 ? 35.41599  8.52898   -5.29740  1.000 11.96797 ?  167 PHE   A C   1 
ATOM   1056 O  O   . PHE   A 1 155 ? 35.38369  7.56398   -4.53310  1.000 12.30885 ?  167 PHE   A O   1 
ATOM   1057 C  CB  . PHE   A 1 155 ? 32.90058  8.64809   -5.48807  1.000 11.43005 ?  167 PHE   A CB  1 
ATOM   1058 C  CG  . PHE   A 1 155 ? 32.54093  9.78084   -4.56345  1.000 10.88241 ?  167 PHE   A CG  1 
ATOM   1059 C  CD1 . PHE   A 1 155 ? 32.00330  10.95573  -5.05052  1.000 11.70343 ?  167 PHE   A CD1 1 
ATOM   1060 C  CD2 . PHE   A 1 155 ? 32.77560  9.67908   -3.20363  1.000 12.11484 ?  167 PHE   A CD2 1 
ATOM   1061 C  CE1 . PHE   A 1 155 ? 31.71063  11.99846  -4.20039  1.000 14.43986 ?  167 PHE   A CE1 1 
ATOM   1062 C  CE2 . PHE   A 1 155 ? 32.46948  10.72021  -2.34140  1.000 12.33510 ?  167 PHE   A CE2 1 
ATOM   1063 C  CZ  . PHE   A 1 155 ? 31.93373  11.87362  -2.83798  1.000 12.81420 ?  167 PHE   A CZ  1 
ATOM   1064 N  N   . GLY   A 1 156 ? 36.49052  9.30253   -5.42579  1.000 13.77916 ?  168 GLY   A N   1 
ATOM   1065 C  CA  . GLY   A 1 156 ? 37.69755  8.99790   -4.69677  1.000 13.42185 ?  168 GLY   A CA  1 
ATOM   1066 C  C   . GLY   A 1 156 ? 38.19704  7.59397   -4.99194  1.000 13.60972 ?  168 GLY   A C   1 
ATOM   1067 O  O   . GLY   A 1 156 ? 38.38666  7.20441   -6.15527  1.000 17.14497 ?  168 GLY   A O   1 
ATOM   1068 N  N   . PRO   A 1 157 ? 38.41891  6.80101   -3.94188  1.000 13.08098 ?  169 PRO   A N   1 
ATOM   1069 C  CA  . PRO   A 1 157 ? 38.99094  5.46757   -4.12289  1.000 12.96191 ?  169 PRO   A CA  1 
ATOM   1070 C  C   . PRO   A 1 157 ? 37.98309  4.39618   -4.50078  1.000 13.23548 ?  169 PRO   A C   1 
ATOM   1071 O  O   . PRO   A 1 157 ? 38.36560  3.22656   -4.56683  1.000 14.97853 ?  169 PRO   A O   1 
ATOM   1072 C  CB  . PRO   A 1 157 ? 39.59443  5.17267   -2.74065  1.000 13.77700 ?  169 PRO   A CB  1 
ATOM   1073 C  CG  . PRO   A 1 157 ? 38.60536  5.86435   -1.78897  1.000 14.84605 ?  169 PRO   A CG  1 
ATOM   1074 C  CD  . PRO   A 1 157 ? 38.21044  7.13516   -2.51501  1.000 14.22298 ?  169 PRO   A CD  1 
ATOM   1075 N  N   . VAL   A 1 158 ? 36.71513  4.74299   -4.75018  1.000 11.58675 ?  170 VAL   A N   1 
ATOM   1076 C  CA  . VAL   A 1 158 ? 35.71413  3.74260   -5.10540  1.000 11.00589 ?  170 VAL   A CA  1 
ATOM   1077 C  C   . VAL   A 1 158 ? 35.03969  4.09643   -6.41740  1.000 10.16637 ?  170 VAL   A C   1 
ATOM   1078 O  O   . VAL   A 1 158 ? 35.08520  5.23452   -6.89762  1.000 10.97965 ?  170 VAL   A O   1 
ATOM   1079 C  CB  . VAL   A 1 158 ? 34.63224  3.53775   -4.01658  1.000 9.08012  ?  170 VAL   A CB  1 
ATOM   1080 C  CG1 . VAL   A 1 158 ? 35.28066  3.25723   -2.68500  1.000 12.72073 ?  170 VAL   A CG1 1 
ATOM   1081 C  CG2 . VAL   A 1 158 ? 33.69535  4.75239   -3.93714  1.000 10.79128 ?  170 VAL   A CG2 1 
ATOM   1082 N  N   . GLU   A 1 159 ? 34.36628  3.09722   -6.96867  1.000 11.50475 ?  171 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 159 ? 33.37207  3.28756   -8.00716  1.000 10.63555 ?  171 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 159 ? 31.99017  3.10621   -7.39008  1.000 10.54529 ?  171 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 159 ? 31.74543  2.12873   -6.66525  1.000 9.95123  ?  171 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 159 ? 33.57563  2.30078   -9.15724  1.000 12.49906 ?  171 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 159 ? 32.66098  2.57566   -10.32363 1.000 12.08593 ?  171 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 159 ? 33.03335  1.75259   -11.54755 1.000 14.79314 ?  171 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 159 ? 32.78230  0.53054   -11.54733 1.000 15.40545 ?  171 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 159 ? 33.56683  2.34819   -12.50187 1.000 18.28674 ?  171 GLU   A OE2 1 
ATOM   1091 N  N   . LEU   A 1 160 ? 31.10983  4.05528   -7.66581  1.000 10.37887 ?  172 LEU   A N   1 
ATOM   1092 C  CA  . LEU   A 1 160 ? 29.70041  3.95628   -7.30676  1.000 10.27220 ?  172 LEU   A CA  1 
ATOM   1093 C  C   . LEU   A 1 160 ? 28.93090  3.47693   -8.52628  1.000 12.63118 ?  172 LEU   A C   1 
ATOM   1094 O  O   . LEU   A 1 160 ? 29.21227  3.90578   -9.65001  1.000 12.01722 ?  172 LEU   A O   1 
ATOM   1095 C  CB  . LEU   A 1 160 ? 29.16571  5.32499   -6.88185  1.000 8.64082  ?  172 LEU   A CB  1 
ATOM   1096 C  CG  . LEU   A 1 160 ? 29.94440  6.05282   -5.79888  1.000 9.65354  ?  172 LEU   A CG  1 
ATOM   1097 C  CD1 . LEU   A 1 160 ? 29.35886  7.44014   -5.58141  1.000 11.23943 ?  172 LEU   A CD1 1 
ATOM   1098 C  CD2 . LEU   A 1 160 ? 29.94654  5.23725   -4.52606  1.000 11.06843 ?  172 LEU   A CD2 1 
ATOM   1099 N  N   . PHE   A 1 161 ? 27.97969  2.57076   -8.30932  1.000 9.30380  ?  173 PHE   A N   1 
ATOM   1100 C  CA  . PHE   A 1 161 ? 27.23829  1.95744   -9.40798  1.000 9.66281  ?  173 PHE   A CA  1 
ATOM   1101 C  C   . PHE   A 1 161 ? 25.75993  1.92767   -9.05943  1.000 9.79311  ?  173 PHE   A C   1 
ATOM   1102 O  O   . PHE   A 1 161 ? 25.38627  1.49161   -7.96372  1.000 9.28729  ?  173 PHE   A O   1 
ATOM   1103 C  CB  . PHE   A 1 161 ? 27.76685  0.52346   -9.59829  1.000 9.52590  ?  173 PHE   A CB  1 
ATOM   1104 C  CG  . PHE   A 1 161 ? 27.17073  -0.23145  -10.76355 1.000 9.01720  ?  173 PHE   A CG  1 
ATOM   1105 C  CD1 . PHE   A 1 161 ? 27.38394  0.17909   -12.06281 1.000 11.87456 ?  173 PHE   A CD1 1 
ATOM   1106 C  CD2 . PHE   A 1 161 ? 26.45801  -1.41023  -10.54477 1.000 10.13798 ?  173 PHE   A CD2 1 
ATOM   1107 C  CE1 . PHE   A 1 161 ? 26.86435  -0.54823  -13.13456 1.000 12.75343 ?  173 PHE   A CE1 1 
ATOM   1108 C  CE2 . PHE   A 1 161 ? 25.94467  -2.14107  -11.60451 1.000 10.47578 ?  173 PHE   A CE2 1 
ATOM   1109 C  CZ  . PHE   A 1 161 ? 26.15114  -1.70215  -12.90577 1.000 12.37880 ?  173 PHE   A CZ  1 
ATOM   1110 N  N   . TYR   A 1 162 ? 24.91982  2.34341   -10.01173 1.000 10.17846 ?  174 TYR   A N   1 
ATOM   1111 C  CA  . TYR   A 1 162 ? 23.48287  2.21795   -9.84451  1.000 9.73954  ?  174 TYR   A CA  1 
ATOM   1112 C  C   . TYR   A 1 162 ? 23.05283  1.01708   -10.66782 1.000 10.05901 ?  174 TYR   A C   1 
ATOM   1113 O  O   . TYR   A 1 162 ? 23.03864  1.10109   -11.90834 1.000 10.48749 ?  174 TYR   A O   1 
ATOM   1114 C  CB  . TYR   A 1 162 ? 22.74645  3.47192   -10.31290 1.000 10.95316 ?  174 TYR   A CB  1 
ATOM   1115 C  CG  . TYR   A 1 162 ? 21.25815  3.29161   -10.27461 1.000 8.35851  ?  174 TYR   A CG  1 
ATOM   1116 C  CD1 . TYR   A 1 162 ? 20.62132  2.79358   -9.13548  1.000 9.66986  ?  174 TYR   A CD1 1 
ATOM   1117 C  CD2 . TYR   A 1 162 ? 20.47439  3.60611   -11.38254 1.000 10.95456 ?  174 TYR   A CD2 1 
ATOM   1118 C  CE1 . TYR   A 1 162 ? 19.25772  2.62169   -9.10170  1.000 10.28244 ?  174 TYR   A CE1 1 
ATOM   1119 C  CE2 . TYR   A 1 162 ? 19.08951  3.43687   -11.35229 1.000 11.88259 ?  174 TYR   A CE2 1 
ATOM   1120 C  CZ  . TYR   A 1 162 ? 18.49089  2.94624   -10.20478 1.000 9.46573  ?  174 TYR   A CZ  1 
ATOM   1121 O  OH  . TYR   A 1 162 ? 17.12744  2.75587   -10.14959 1.000 11.57491 ?  174 TYR   A OH  1 
ATOM   1122 N  N   . PRO   A 1 163 ? 22.70945  -0.11636  -10.04636 1.000 7.37161  ?  175 PRO   A N   1 
ATOM   1123 C  CA  . PRO   A 1 163 ? 22.41668  -1.32386  -10.82717 1.000 8.36660  ?  175 PRO   A CA  1 
ATOM   1124 C  C   . PRO   A 1 163 ? 21.00111  -1.35887  -11.35773 1.000 10.23367 ?  175 PRO   A C   1 
ATOM   1125 O  O   . PRO   A 1 163 ? 20.66191  -2.28185  -12.11880 1.000 10.58712 ?  175 PRO   A O   1 
ATOM   1126 C  CB  . PRO   A 1 163 ? 22.64292  -2.44977  -9.80942  1.000 10.86480 ?  175 PRO   A CB  1 
ATOM   1127 C  CG  . PRO   A 1 163 ? 22.22108  -1.80140  -8.47888  1.000 9.97638  ?  175 PRO   A CG  1 
ATOM   1128 C  CD  . PRO   A 1 163 ? 22.72044  -0.37906  -8.59350  1.000 8.24455  ?  175 PRO   A CD  1 
ATOM   1129 N  N   . GLY   A 1 164 ? 20.17073  -0.39448  -10.98408 1.000 10.36745 ?  176 GLY   A N   1 
ATOM   1130 C  CA  . GLY   A 1 164 ? 18.73594  -0.49244  -11.15153 1.000 9.73521  ?  176 GLY   A CA  1 
ATOM   1131 C  C   . GLY   A 1 164 ? 18.03884  -0.72495  -9.82019  1.000 9.38254  ?  176 GLY   A C   1 
ATOM   1132 O  O   . GLY   A 1 164 ? 18.65597  -1.00589  -8.79327  1.000 8.96792  ?  176 GLY   A O   1 
ATOM   1133 N  N   . ALA   A 1 165 ? 16.72307  -0.58452  -9.85203  1.000 10.40632 ?  177 ALA   A N   1 
ATOM   1134 C  CA  . ALA   A 1 165 ? 15.91701  -0.76381  -8.64897  1.000 8.96478  ?  177 ALA   A CA  1 
ATOM   1135 C  C   . ALA   A 1 165 ? 16.02996  -2.19111  -8.10993  1.000 9.49073  ?  177 ALA   A C   1 
ATOM   1136 O  O   . ALA   A 1 165 ? 16.09773  -3.15920  -8.86754  1.000 9.88126  ?  177 ALA   A O   1 
ATOM   1137 C  CB  . ALA   A 1 165 ? 14.46060  -0.41106  -8.95671  1.000 10.62011 ?  177 ALA   A CB  1 
ATOM   1138 N  N   . ALA   A 1 166 ? 16.05306  -2.32868  -6.78022  1.000 9.88946  ?  178 ALA   A N   1 
ATOM   1139 C  CA  . ALA   A 1 166 ? 16.17806  -3.65227  -6.18466  1.000 9.51719  ?  178 ALA   A CA  1 
ATOM   1140 C  C   . ALA   A 1 166 ? 15.53370  -3.59683  -4.80899  1.000 10.60461 ?  178 ALA   A C   1 
ATOM   1141 O  O   . ALA   A 1 166 ? 14.30409  -3.52816  -4.70926  1.000 11.07550 ?  178 ALA   A O   1 
ATOM   1142 C  CB  . ALA   A 1 166 ? 17.64725  -4.09220  -6.14082  1.000 10.81366 ?  178 ALA   A CB  1 
ATOM   1143 N  N   . HIS   A 1 167 ? 16.35075  -3.59840  -3.74908  1.000 10.10910 ?  179 HIS   A N   1 
ATOM   1144 C  CA  . HIS   A 1 167 ? 15.81452  -3.39026  -2.41063  1.000 7.42933  ?  179 HIS   A CA  1 
ATOM   1145 C  C   . HIS   A 1 167 ? 15.04822  -2.07516  -2.32074  1.000 10.33733 ?  179 HIS   A C   1 
ATOM   1146 O  O   . HIS   A 1 167 ? 14.04755  -1.97523  -1.60040  1.000 9.32788  ?  179 HIS   A O   1 
ATOM   1147 C  CB  . HIS   A 1 167 ? 16.97361  -3.41071  -1.42398  1.000 10.61100 ?  179 HIS   A CB  1 
ATOM   1148 C  CG  . HIS   A 1 167 ? 16.62435  -2.89161  -0.07555  1.000 9.15503  ?  179 HIS   A CG  1 
ATOM   1149 N  ND1 . HIS   A 1 167 ? 16.07173  -3.68570  0.90828   1.000 10.97668 ?  179 HIS   A ND1 1 
ATOM   1150 C  CD2 . HIS   A 1 167 ? 16.77692  -1.66408  0.46455   1.000 10.02069 ?  179 HIS   A CD2 1 
ATOM   1151 C  CE1 . HIS   A 1 167 ? 15.89206  -2.96676  1.99827   1.000 11.66223 ?  179 HIS   A CE1 1 
ATOM   1152 N  NE2 . HIS   A 1 167 ? 16.31665  -1.74103  1.75232   1.000 9.89746  ?  179 HIS   A NE2 1 
ATOM   1153 N  N   . SER   A 1 168 ? 15.52354  -1.04574  -3.01682  1.000 9.93250  ?  180 SER   A N   1 
ATOM   1154 C  CA  . SER   A 1 168 ? 14.83314  0.23233   -3.15207  1.000 9.66202  ?  180 SER   A CA  1 
ATOM   1155 C  C   . SER   A 1 168 ? 15.11317  0.74208   -4.55527  1.000 9.99839  ?  180 SER   A C   1 
ATOM   1156 O  O   . SER   A 1 168 ? 15.96839  0.21128   -5.26086  1.000 9.86094  ?  180 SER   A O   1 
ATOM   1157 C  CB  . SER   A 1 168 ? 15.32140  1.22257   -2.09037  1.000 9.63633  ?  180 SER   A CB  1 
ATOM   1158 O  OG  . SER   A 1 168 ? 16.71261  1.48936   -2.25546  1.000 10.30993 ?  180 SER   A OG  1 
ATOM   1159 N  N   . THR   A 1 169 ? 14.36672  1.76492   -4.99031  1.000 10.48647 ?  181 THR   A N   1 
ATOM   1160 C  CA  . THR   A 1 169 ? 14.56137  2.24523   -6.35801  1.000 10.61090 ?  181 THR   A CA  1 
ATOM   1161 C  C   . THR   A 1 169 ? 15.87594  2.99229   -6.53060  1.000 9.96969  ?  181 THR   A C   1 
ATOM   1162 O  O   . THR   A 1 169 ? 16.39838  3.06308   -7.64865  1.000 10.53482 ?  181 THR   A O   1 
ATOM   1163 C  CB  . THR   A 1 169 ? 13.39771  3.12801   -6.83636  1.000 12.40065 ?  181 THR   A CB  1 
ATOM   1164 O  OG1 . THR   A 1 169 ? 13.26355  4.26774   -5.98264  1.000 14.57204 ?  181 THR   A OG1 1 
ATOM   1165 C  CG2 . THR   A 1 169 ? 12.08128  2.35605   -6.84929  1.000 13.45751 ?  181 THR   A CG2 1 
ATOM   1166 N  N   . ASP   A 1 170 ? 16.44205  3.51509   -5.44031  1.000 8.72892  ?  182 ASP   A N   1 
ATOM   1167 C  CA  . ASP   A 1 170 ? 17.60599  4.38580   -5.49078  1.000 8.95745  ?  182 ASP   A CA  1 
ATOM   1168 C  C   . ASP   A 1 170 ? 18.90052  3.67306   -5.11334  1.000 8.68873  ?  182 ASP   A C   1 
ATOM   1169 O  O   . ASP   A 1 170 ? 19.94844  4.30694   -5.08434  1.000 9.38746  ?  182 ASP   A O   1 
ATOM   1170 C  CB  . ASP   A 1 170 ? 17.38661  5.56333   -4.52890  1.000 9.17596  ?  182 ASP   A CB  1 
ATOM   1171 C  CG  . ASP   A 1 170 ? 17.15560  5.11190   -3.08441  1.000 9.88198  ?  182 ASP   A CG  1 
ATOM   1172 O  OD1 . ASP   A 1 170 ? 16.47772  4.08552   -2.86053  1.000 9.49212  ?  182 ASP   A OD1 1 
ATOM   1173 O  OD2 . ASP   A 1 170 ? 17.66100  5.78813   -2.15212  1.000 8.93341  ?  182 ASP   A OD2 1 
ATOM   1174 N  N   . ASN   A 1 171 ? 18.85568  2.38573   -4.79827  1.000 8.45968  ?  183 ASN   A N   1 
ATOM   1175 C  CA  . ASN   A 1 171 ? 20.00260  1.74386   -4.16778  1.000 7.56279  ?  183 ASN   A CA  1 
ATOM   1176 C  C   . ASN   A 1 171 ? 21.26075  1.73362   -5.02941  1.000 7.56566  ?  183 ASN   A C   1 
ATOM   1177 O  O   . ASN   A 1 171 ? 21.21873  1.43552   -6.22446  1.000 8.77403  ?  183 ASN   A O   1 
ATOM   1178 C  CB  . ASN   A 1 171 ? 19.57896  0.37869   -3.60048  1.000 7.84770  ?  183 ASN   A CB  1 
ATOM   1179 C  CG  . ASN   A 1 171 ? 19.11026  -0.62916  -4.64555  1.000 9.36324  ?  183 ASN   A CG  1 
ATOM   1180 O  OD1 . ASN   A 1 171 ? 19.21374  -0.45108  -5.87800  1.000 12.04025 ?  183 ASN   A OD1 1 
ATOM   1181 N  ND2 . ASN   A 1 171 ? 18.38335  -1.59015  -4.13824  1.000 6.99451  ?  183 ASN   A ND2 1 
ATOM   1182 N  N   . LEU   A 1 172 ? 22.37929  2.11000   -4.39419  1.000 8.45405  ?  184 LEU   A N   1 
ATOM   1183 C  CA  . LEU   A 1 172 ? 23.70171  2.09858   -5.00309  1.000 7.63064  ?  184 LEU   A CA  1 
ATOM   1184 C  C   . LEU   A 1 172 ? 24.52650  0.95404   -4.44262  1.000 8.56624  ?  184 LEU   A C   1 
ATOM   1185 O  O   . LEU   A 1 172 ? 24.34021  0.53459   -3.29638  1.000 9.11298  ?  184 LEU   A O   1 
ATOM   1186 C  CB  . LEU   A 1 172 ? 24.46896  3.38643   -4.67885  1.000 8.53859  ?  184 LEU   A CB  1 
ATOM   1187 C  CG  . LEU   A 1 172 ? 23.87445  4.71801   -5.13106  1.000 6.91002  ?  184 LEU   A CG  1 
ATOM   1188 C  CD1 . LEU   A 1 172 ? 24.82694  5.87271   -4.79598  1.000 10.76776 ?  184 LEU   A CD1 1 
ATOM   1189 C  CD2 . LEU   A 1 172 ? 23.51216  4.68855   -6.61547  1.000 11.51560 ?  184 LEU   A CD2 1 
ATOM   1190 N  N   . VAL   A 1 173 ? 25.45821  0.45691   -5.25833  1.000 8.28439  ?  185 VAL   A N   1 
ATOM   1191 C  CA  . VAL   A 1 173 ? 26.50683  -0.41353  -4.74616  1.000 9.33793  ?  185 VAL   A CA  1 
ATOM   1192 C  C   . VAL   A 1 173 ? 27.85615  0.27081   -4.95061  1.000 8.14172  ?  185 VAL   A C   1 
ATOM   1193 O  O   . VAL   A 1 173 ? 27.98841  1.24419   -5.69865  1.000 8.79054  ?  185 VAL   A O   1 
ATOM   1194 C  CB  . VAL   A 1 173 ? 26.47640  -1.82234  -5.36601  1.000 11.75040 ?  185 VAL   A CB  1 
ATOM   1195 C  CG1 . VAL   A 1 173 ? 25.10116  -2.47471  -5.13493  1.000 11.39339 ?  185 VAL   A CG1 1 
ATOM   1196 C  CG2 . VAL   A 1 173 ? 26.84743  -1.78636  -6.84432  1.000 12.72489 ?  185 VAL   A CG2 1 
ATOM   1197 N  N   . VAL   A 1 174 ? 28.86752  -0.23677  -4.24528  1.000 9.08274  ?  186 VAL   A N   1 
ATOM   1198 C  CA  . VAL   A 1 174 ? 30.17157  0.41544   -4.16858  1.000 9.71462  ?  186 VAL   A CA  1 
ATOM   1199 C  C   . VAL   A 1 174 ? 31.23999  -0.63591  -4.41665  1.000 9.58477  ?  186 VAL   A C   1 
ATOM   1200 O  O   . VAL   A 1 174 ? 31.21674  -1.70467  -3.80026  1.000 11.26858 ?  186 VAL   A O   1 
ATOM   1201 C  CB  . VAL   A 1 174 ? 30.36505  1.07723   -2.79242  1.000 9.77775  ?  186 VAL   A CB  1 
ATOM   1202 C  CG1 . VAL   A 1 174 ? 31.71868  1.75508   -2.68741  1.000 10.80161 ?  186 VAL   A CG1 1 
ATOM   1203 C  CG2 . VAL   A 1 174 ? 29.24543  2.10075   -2.52613  1.000 10.90724 ?  186 VAL   A CG2 1 
ATOM   1204 N  N   . TYR   A 1 175 ? 32.18548  -0.33378  -5.30516  1.000 9.39501  ?  187 TYR   A N   1 
ATOM   1205 C  CA  . TYR   A 1 175 ? 33.28977  -1.24951  -5.57327  1.000 10.38145 ?  187 TYR   A CA  1 
ATOM   1206 C  C   . TYR   A 1 175 ? 34.61097  -0.55730  -5.28144  1.000 11.18216 ?  187 TYR   A C   1 
ATOM   1207 O  O   . TYR   A 1 175 ? 34.79831  0.60145   -5.64124  1.000 11.37819 ?  187 TYR   A O   1 
ATOM   1208 C  CB  . TYR   A 1 175 ? 33.27835  -1.66062  -7.03171  1.000 12.27880 ?  187 TYR   A CB  1 
ATOM   1209 C  CG  . TYR   A 1 175 ? 34.26694  -2.74572  -7.36504  1.000 10.98453 ?  187 TYR   A CG  1 
ATOM   1210 C  CD1 . TYR   A 1 175 ? 34.15938  -4.00072  -6.80301  1.000 11.35323 ?  187 TYR   A CD1 1 
ATOM   1211 C  CD2 . TYR   A 1 175 ? 35.30467  -2.51216  -8.26474  1.000 12.68277 ?  187 TYR   A CD2 1 
ATOM   1212 C  CE1 . TYR   A 1 175 ? 35.05813  -5.00692  -7.11461  1.000 12.33027 ?  187 TYR   A CE1 1 
ATOM   1213 C  CE2 . TYR   A 1 175 ? 36.20411  -3.51778  -8.58355  1.000 12.18761 ?  187 TYR   A CE2 1 
ATOM   1214 C  CZ  . TYR   A 1 175 ? 36.06147  -4.74681  -8.00066  1.000 13.15031 ?  187 TYR   A CZ  1 
ATOM   1215 O  OH  . TYR   A 1 175 ? 36.93207  -5.77066  -8.29014  1.000 16.21549 ?  187 TYR   A OH  1 
ATOM   1216 N  N   . VAL   A 1 176 ? 35.50654  -1.26731  -4.59951  1.000 11.50420 ?  188 VAL   A N   1 
ATOM   1217 C  CA  . VAL   A 1 176 ? 36.86523  -0.79038  -4.32915  1.000 12.87577 ?  188 VAL   A CA  1 
ATOM   1218 C  C   . VAL   A 1 176 ? 37.83857  -1.50423  -5.26152  1.000 13.96152 ?  188 VAL   A C   1 
ATOM   1219 O  O   . VAL   A 1 176 ? 38.22200  -2.65384  -4.98496  1.000 13.83379 ?  188 VAL   A O   1 
ATOM   1220 C  CB  . VAL   A 1 176 ? 37.28050  -1.01087  -2.86821  1.000 11.28416 ?  188 VAL   A CB  1 
ATOM   1221 C  CG1 . VAL   A 1 176 ? 38.59132  -0.25142  -2.58277  1.000 14.05734 ?  188 VAL   A CG1 1 
ATOM   1222 C  CG2 . VAL   A 1 176 ? 36.17235  -0.57472  -1.90208  1.000 10.95727 ?  188 VAL   A CG2 1 
ATOM   1223 N  N   . PRO   A 1 177 ? 38.26092  -0.88273  -6.35999  1.000 15.18629 ?  189 PRO   A N   1 
ATOM   1224 C  CA  . PRO   A 1 177 ? 39.04246  -1.63865  -7.35439  1.000 16.06896 ?  189 PRO   A CA  1 
ATOM   1225 C  C   . PRO   A 1 177 ? 40.38859  -2.12314  -6.84320  1.000 17.83948 ?  189 PRO   A C   1 
ATOM   1226 O  O   . PRO   A 1 177 ? 40.79648  -3.24343  -7.17539  1.000 19.83338 ?  189 PRO   A O   1 
ATOM   1227 C  CB  . PRO   A 1 177 ? 39.15642  -0.66557  -8.53839  1.000 19.87504 ?  189 PRO   A CB  1 
ATOM   1228 C  CG  . PRO   A 1 177 ? 38.80552  0.67245   -8.00349  1.000 25.59684 ?  189 PRO   A CG  1 
ATOM   1229 C  CD  . PRO   A 1 177 ? 37.87615  0.45285   -6.84083  1.000 15.99371 ?  189 PRO   A CD  1 
ATOM   1230 N  N   . SER   A 1 178 ? 41.05444  -1.34155  -5.99114  1.000 17.59311 ?  190 SER   A N   1 
ATOM   1231 C  CA  . SER   A 1 178 ? 42.36751  -1.73863  -5.48582  1.000 24.10006 ?  190 SER   A CA  1 
ATOM   1232 C  C   . SER   A 1 178 ? 42.30156  -3.01976  -4.66664  1.000 26.05114 ?  190 SER   A C   1 
ATOM   1233 O  O   . SER   A 1 178 ? 43.28331  -3.76903  -4.60825  1.000 21.43512 ?  190 SER   A O   1 
ATOM   1234 C  CB  . SER   A 1 178 ? 42.96497  -0.60861  -4.64536  1.000 24.27413 ?  190 SER   A CB  1 
ATOM   1235 O  OG  . SER   A 1 178 ? 42.20074  -0.39258  -3.46476  1.000 27.26614 ?  190 SER   A OG  1 
ATOM   1236 N  N   . ALA   A 1 179 ? 41.16077  -3.29251  -4.03485  1.000 16.35247 ?  191 ALA   A N   1 
ATOM   1237 C  CA  . ALA   A 1 179 ? 41.00828  -4.42103  -3.13106  1.000 17.39067 ?  191 ALA   A CA  1 
ATOM   1238 C  C   . ALA   A 1 179 ? 40.03608  -5.48734  -3.62619  1.000 14.84299 ?  191 ALA   A C   1 
ATOM   1239 O  O   . ALA   A 1 179 ? 39.88202  -6.52145  -2.96239  1.000 18.05872 ?  191 ALA   A O   1 
ATOM   1240 C  CB  . ALA   A 1 179 ? 40.57530  -3.91470  -1.74948  1.000 20.60514 ?  191 ALA   A CB  1 
ATOM   1241 N  N   . SER   A 1 180 ? 39.36171  -5.26310  -4.75687  1.000 16.12845 ?  192 SER   A N   1 
ATOM   1242 C  CA  A SER   A 1 180 ? 38.36754  -6.20202  -5.28856  0.688 15.51978 ?  192 SER   A CA  1 
ATOM   1243 C  CA  B SER   A 1 180 ? 38.38088  -6.21856  -5.27886  0.312 15.58512 ?  192 SER   A CA  1 
ATOM   1244 C  C   . SER   A 1 180 ? 37.23692  -6.45343  -4.29210  1.000 13.85858 ?  192 SER   A C   1 
ATOM   1245 O  O   . SER   A 1 180 ? 36.73326  -7.56864  -4.15004  1.000 15.89382 ?  192 SER   A O   1 
ATOM   1246 C  CB  A SER   A 1 180 ? 39.00359  -7.50764  -5.77750  0.688 19.90903 ?  192 SER   A CB  1 
ATOM   1247 C  CB  B SER   A 1 180 ? 39.04000  -7.53800  -5.69468  0.312 19.82676 ?  192 SER   A CB  1 
ATOM   1248 O  OG  A SER   A 1 180 ? 40.04749  -7.23829  -6.70492  0.688 22.35016 ?  192 SER   A OG  1 
ATOM   1249 O  OG  B SER   A 1 180 ? 38.14220  -8.35870  -6.41378  0.312 19.13337 ?  192 SER   A OG  1 
ATOM   1250 N  N   . VAL   A 1 181 ? 36.81665  -5.39368  -3.60784  1.000 12.88938 ?  193 VAL   A N   1 
ATOM   1251 C  CA  . VAL   A 1 181 ? 35.77157  -5.46565  -2.59127  1.000 12.58024 ?  193 VAL   A CA  1 
ATOM   1252 C  C   . VAL   A 1 181 ? 34.51107  -4.84015  -3.16164  1.000 11.27843 ?  193 VAL   A C   1 
ATOM   1253 O  O   . VAL   A 1 181 ? 34.52613  -3.67563  -3.58998  1.000 11.07813 ?  193 VAL   A O   1 
ATOM   1254 C  CB  . VAL   A 1 181 ? 36.18260  -4.74968  -1.29350  1.000 13.06595 ?  193 VAL   A CB  1 
ATOM   1255 C  CG1 . VAL   A 1 181 ? 34.98099  -4.63633  -0.36020  1.000 12.35436 ?  193 VAL   A CG1 1 
ATOM   1256 C  CG2 . VAL   A 1 181 ? 37.30972  -5.48958  -0.59230  1.000 14.81626 ?  193 VAL   A CG2 1 
ATOM   1257 N  N   . LEU   A 1 182 ? 33.42158  -5.59922  -3.13327  1.000 11.38961 ?  194 LEU   A N   1 
ATOM   1258 C  CA  . LEU   A 1 182 ? 32.11321  -5.14134  -3.58512  1.000 11.07400 ?  194 LEU   A CA  1 
ATOM   1259 C  C   . LEU   A 1 182 ? 31.19951  -5.02620  -2.37242  1.000 10.51790 ?  194 LEU   A C   1 
ATOM   1260 O  O   . LEU   A 1 182 ? 30.95349  -6.01842  -1.67997  1.000 12.65588 ?  194 LEU   A O   1 
ATOM   1261 C  CB  . LEU   A 1 182 ? 31.53469  -6.13722  -4.58361  1.000 12.66172 ?  194 LEU   A CB  1 
ATOM   1262 C  CG  . LEU   A 1 182 ? 30.11917  -5.82976  -5.06390  1.000 12.42593 ?  194 LEU   A CG  1 
ATOM   1263 C  CD1 . LEU   A 1 182 ? 30.04211  -4.49346  -5.81322  1.000 15.06720 ?  194 LEU   A CD1 1 
ATOM   1264 C  CD2 . LEU   A 1 182 ? 29.61808  -6.95029  -5.94255  1.000 14.16079 ?  194 LEU   A CD2 1 
ATOM   1265 N  N   . TYR   A 1 183 ? 30.71214  -3.81896  -2.10602  1.000 11.21800 ?  195 TYR   A N   1 
ATOM   1266 C  CA  . TYR   A 1 183 ? 29.75303  -3.57646  -1.03368  1.000 9.77384  ?  195 TYR   A CA  1 
ATOM   1267 C  C   . TYR   A 1 183 ? 28.37607  -3.43809  -1.66644  1.000 9.38271  ?  195 TYR   A C   1 
ATOM   1268 O  O   . TYR   A 1 183 ? 28.12521  -2.49318  -2.43137  1.000 9.74592  ?  195 TYR   A O   1 
ATOM   1269 C  CB  . TYR   A 1 183 ? 30.13774  -2.31408  -0.27687  1.000 10.78023 ?  195 TYR   A CB  1 
ATOM   1270 C  CG  . TYR   A 1 183 ? 29.09247  -1.85903  0.69192   1.000 9.45552  ?  195 TYR   A CG  1 
ATOM   1271 C  CD1 . TYR   A 1 183 ? 28.84073  -2.57122  1.85525   1.000 16.76740 ?  195 TYR   A CD1 1 
ATOM   1272 C  CD2 . TYR   A 1 183 ? 28.32610  -0.73727  0.42633   1.000 10.36826 ?  195 TYR   A CD2 1 
ATOM   1273 C  CE1 . TYR   A 1 183 ? 27.86354  -2.15542  2.75101   1.000 16.08715 ?  195 TYR   A CE1 1 
ATOM   1274 C  CE2 . TYR   A 1 183 ? 27.36914  -0.29621  1.31768   1.000 11.29085 ?  195 TYR   A CE2 1 
ATOM   1275 C  CZ  . TYR   A 1 183 ? 27.13899  -1.00973  2.47149   1.000 13.79109 ?  195 TYR   A CZ  1 
ATOM   1276 O  OH  . TYR   A 1 183 ? 26.16643  -0.60434  3.35903   1.000 18.49931 ?  195 TYR   A OH  1 
ATOM   1277 N  N   . GLY   A 1 184 ? 27.49400  -4.39134  -1.35980  1.000 9.04762  ?  196 GLY   A N   1 
ATOM   1278 C  CA  . GLY   A 1 184 ? 26.19323  -4.42292  -2.00001  1.000 8.31008  ?  196 GLY   A CA  1 
ATOM   1279 C  C   . GLY   A 1 184 ? 25.10291  -3.66663  -1.27151  1.000 8.62248  ?  196 GLY   A C   1 
ATOM   1280 O  O   . GLY   A 1 184 ? 24.01992  -3.46849  -1.83806  1.000 9.54589  ?  196 GLY   A O   1 
ATOM   1281 N  N   . GLY   A 1 185 ? 25.36484  -3.21379  -0.05183  1.000 8.36451  ?  197 GLY   A N   1 
ATOM   1282 C  CA  . GLY   A 1 185 ? 24.29471  -2.64165  0.75148   1.000 9.11766  ?  197 GLY   A CA  1 
ATOM   1283 C  C   . GLY   A 1 185 ? 23.11078  -3.57919  0.81186   1.000 9.59020  ?  197 GLY   A C   1 
ATOM   1284 O  O   . GLY   A 1 185 ? 23.23909  -4.80560  0.68701   1.000 9.86264  ?  197 GLY   A O   1 
ATOM   1285 N  N   . CYS   A 1 186 ? 21.92208  -3.00315  0.98581   1.000 9.61596  ?  198 CYS   A N   1 
ATOM   1286 C  CA  . CYS   A 1 186 ? 20.76087  -3.82581  1.28837   1.000 9.81361  ?  198 CYS   A CA  1 
ATOM   1287 C  C   . CYS   A 1 186 ? 20.17098  -4.51493  0.06389   1.000 8.36895  ?  198 CYS   A C   1 
ATOM   1288 O  O   . CYS   A 1 186 ? 19.24330  -5.31922  0.21475   1.000 10.11179 ?  198 CYS   A O   1 
ATOM   1289 C  CB  . CYS   A 1 186 ? 19.74038  -2.99214  2.05410   1.000 10.96591 ?  198 CYS   A CB  1 
ATOM   1290 S  SG  . CYS   A 1 186 ? 20.49894  -2.26181  3.54114   1.000 14.15930 ?  198 CYS   A SG  1 
ATOM   1291 N  N   . ALA   A 1 187 ? 20.74832  -4.28202  -1.11528  1.000 9.29418  ?  199 ALA   A N   1 
ATOM   1292 C  CA  . ALA   A 1 187 ? 20.35601  -5.01012  -2.31241  1.000 10.46108 ?  199 ALA   A CA  1 
ATOM   1293 C  C   . ALA   A 1 187 ? 20.92920  -6.41792  -2.34944  1.000 8.93840  ?  199 ALA   A C   1 
ATOM   1294 O  O   . ALA   A 1 187 ? 20.51557  -7.21714  -3.19784  1.000 10.33786 ?  199 ALA   A O   1 
ATOM   1295 C  CB  . ALA   A 1 187 ? 20.84233  -4.24703  -3.54662  1.000 10.95128 ?  199 ALA   A CB  1 
ATOM   1296 N  N   . ILE   A 1 188 ? 21.90140  -6.73376  -1.49058  1.000 9.10724  ?  200 ILE   A N   1 
ATOM   1297 C  CA  . ILE   A 1 188 ? 22.53887  -8.04735  -1.47334  1.000 9.53955  ?  200 ILE   A CA  1 
ATOM   1298 C  C   . ILE   A 1 188 ? 22.36058  -8.63754  -0.08104  1.000 10.63883 ?  200 ILE   A C   1 
ATOM   1299 O  O   . ILE   A 1 188 ? 22.69080  -7.98607  0.91516   1.000 10.16127 ?  200 ILE   A O   1 
ATOM   1300 C  CB  . ILE   A 1 188 ? 24.03391  -7.95691  -1.84021  1.000 8.99356  ?  200 ILE   A CB  1 
ATOM   1301 C  CG1 . ILE   A 1 188 ? 24.23036  -7.37502  -3.24420  1.000 10.22330 ?  200 ILE   A CG1 1 
ATOM   1302 C  CG2 . ILE   A 1 188 ? 24.70495  -9.33247  -1.70702  1.000 10.60020 ?  200 ILE   A CG2 1 
ATOM   1303 C  CD1 . ILE   A 1 188 ? 23.64528  -8.24115  -4.33394  1.000 16.61238 ?  200 ILE   A CD1 1 
ATOM   1304 N  N   . TYR   A 1 189 ? 21.84278  -9.86632  -0.01860  1.000 11.19394 ?  201 TYR   A N   1 
ATOM   1305 C  CA  . TYR   A 1 189 ? 21.56074  -10.55585 1.23654   1.000 10.19790 ?  201 TYR   A CA  1 
ATOM   1306 C  C   . TYR   A 1 189 ? 22.72495  -11.46412 1.62412   1.000 9.06379  ?  201 TYR   A C   1 
ATOM   1307 O  O   . TYR   A 1 189 ? 23.35819  -12.08317 0.76257   1.000 10.36626 ?  201 TYR   A O   1 
ATOM   1308 C  CB  . TYR   A 1 189 ? 20.31053  -11.42570 1.06934   1.000 13.47974 ?  201 TYR   A CB  1 
ATOM   1309 C  CG  . TYR   A 1 189 ? 18.98413  -10.69523 1.11267   1.000 12.55173 ?  201 TYR   A CG  1 
ATOM   1310 C  CD1 . TYR   A 1 189 ? 18.91198  -9.31290  1.07540   1.000 17.92137 ?  201 TYR   A CD1 1 
ATOM   1311 C  CD2 . TYR   A 1 189 ? 17.79401  -11.40576 1.19705   1.000 27.37664 ?  201 TYR   A CD2 1 
ATOM   1312 C  CE1 . TYR   A 1 189 ? 17.68508  -8.65587  1.12263   1.000 16.31662 ?  201 TYR   A CE1 1 
ATOM   1313 C  CE2 . TYR   A 1 189 ? 16.57079  -10.76149 1.24182   1.000 24.92414 ?  201 TYR   A CE2 1 
ATOM   1314 C  CZ  . TYR   A 1 189 ? 16.52464  -9.38734  1.19874   1.000 16.83446 ?  201 TYR   A CZ  1 
ATOM   1315 O  OH  . TYR   A 1 189 ? 15.31521  -8.74044  1.24362   1.000 16.87598 ?  201 TYR   A OH  1 
ATOM   1316 N  N   . GLU   A 1 190 ? 22.98514  -11.57296 2.93089   1.000 11.21954 ?  202 GLU   A N   1 
ATOM   1317 C  CA  . GLU   A 1 190 ? 23.89474  -12.60662 3.40885   1.000 12.80089 ?  202 GLU   A CA  1 
ATOM   1318 C  C   . GLU   A 1 190 ? 23.27458  -13.99159 3.20548   1.000 12.26482 ?  202 GLU   A C   1 
ATOM   1319 O  O   . GLU   A 1 190 ? 22.06023  -14.14652 3.07552   1.000 11.00588 ?  202 GLU   A O   1 
ATOM   1320 C  CB  . GLU   A 1 190 ? 24.23001  -12.40010 4.89123   1.000 12.25845 ?  202 GLU   A CB  1 
ATOM   1321 C  CG  . GLU   A 1 190 ? 23.08263  -12.67999 5.86514   1.000 11.39294 ?  202 GLU   A CG  1 
ATOM   1322 C  CD  . GLU   A 1 190 ? 23.57658  -12.72443 7.30919   1.000 14.35596 ?  202 GLU   A CD  1 
ATOM   1323 O  OE1 . GLU   A 1 190 ? 24.69955  -13.23508 7.54682   1.000 16.56901 ?  202 GLU   A OE1 1 
ATOM   1324 O  OE2 . GLU   A 1 190 ? 22.84538  -12.23744 8.18768   1.000 18.68457 ?  202 GLU   A OE2 1 
ATOM   1325 N  N   . LEU   A 1 191 ? 24.14504  -15.00588 3.18462   1.000 13.16712 ?  203 LEU   A N   1 
ATOM   1326 C  CA  . LEU   A 1 191 ? 23.70922  -16.37167 2.88651   1.000 13.35122 ?  203 LEU   A CA  1 
ATOM   1327 C  C   . LEU   A 1 191 ? 22.73718  -16.91233 3.92663   1.000 14.39161 ?  203 LEU   A C   1 
ATOM   1328 O  O   . LEU   A 1 191 ? 21.81208  -17.65799 3.58466   1.000 14.43975 ?  203 LEU   A O   1 
ATOM   1329 C  CB  . LEU   A 1 191 ? 24.92203  -17.29361 2.77819   1.000 14.59231 ?  203 LEU   A CB  1 
ATOM   1330 C  CG  . LEU   A 1 191 ? 25.82984  -17.00950 1.58531   1.000 13.21158 ?  203 LEU   A CG  1 
ATOM   1331 C  CD1 . LEU   A 1 191 ? 26.93939  -18.04389 1.51248   1.000 15.05118 ?  203 LEU   A CD1 1 
ATOM   1332 C  CD2 . LEU   A 1 191 ? 25.00978  -16.98727 0.27482   1.000 14.21579 ?  203 LEU   A CD2 1 
ATOM   1333 N  N   . SER   A 1 192 ? 22.91096  -16.54496 5.19221   1.000 15.50508 ?  204 SER   A N   1 
ATOM   1334 C  CA  A SER   A 1 192 ? 22.03921  -17.08811 6.22693   0.572 15.86131 ?  204 SER   A CA  1 
ATOM   1335 C  CA  B SER   A 1 192 ? 22.04725  -17.06393 6.24692   0.428 15.91818 ?  204 SER   A CA  1 
ATOM   1336 C  C   . SER   A 1 192 ? 20.61579  -16.55162 6.15989   1.000 17.71856 ?  204 SER   A C   1 
ATOM   1337 O  O   . SER   A 1 192 ? 19.73587  -17.09399 6.84255   1.000 21.12506 ?  204 SER   A O   1 
ATOM   1338 C  CB  A SER   A 1 192 ? 22.63903  -16.81818 7.60730   0.572 17.74019 ?  204 SER   A CB  1 
ATOM   1339 C  CB  B SER   A 1 192 ? 22.63846  -16.71374 7.61351   0.428 17.75145 ?  204 SER   A CB  1 
ATOM   1340 O  OG  A SER   A 1 192 ? 22.39371  -15.48325 7.99973   0.572 19.21707 ?  204 SER   A OG  1 
ATOM   1341 O  OG  B SER   A 1 192 ? 23.92065  -17.29274 7.76935   0.428 18.95220 ?  204 SER   A OG  1 
ATOM   1342 N  N   . ARG   A 1 193 ? 20.35587  -15.51618 5.36146   1.000 15.63337 ?  205 ARG   A N   1 
ATOM   1343 C  CA  . ARG   A 1 193 ? 19.00686  -14.98581 5.20836   1.000 16.21021 ?  205 ARG   A CA  1 
ATOM   1344 C  C   . ARG   A 1 193 ? 18.35588  -15.67763 4.01999   1.000 19.76636 ?  205 ARG   A C   1 
ATOM   1345 O  O   . ARG   A 1 193 ? 18.78907  -15.49635 2.87947   1.000 16.71301 ?  205 ARG   A O   1 
ATOM   1346 C  CB  . ARG   A 1 193 ? 19.05387  -13.48104 4.98547   1.000 18.68248 ?  205 ARG   A CB  1 
ATOM   1347 C  CG  . ARG   A 1 193 ? 19.30958  -12.70516 6.25127   1.000 26.58707 ?  205 ARG   A CG  1 
ATOM   1348 C  CD  . ARG   A 1 193 ? 19.29634  -11.21849 5.97729   1.000 28.46493 ?  205 ARG   A CD  1 
ATOM   1349 N  NE  . ARG   A 1 193 ? 17.98120  -10.71585 5.60565   1.000 25.79991 ?  205 ARG   A NE  1 
ATOM   1350 C  CZ  . ARG   A 1 193 ? 17.78209  -9.56588  4.97714   1.000 28.25742 ?  205 ARG   A CZ  1 
ATOM   1351 N  NH1 . ARG   A 1 193 ? 18.79385  -8.83480  4.53593   1.000 24.69551 ?  205 ARG   A NH1 1 
ATOM   1352 N  NH2 . ARG   A 1 193 ? 16.54082  -9.13835  4.78492   1.000 27.68465 ?  205 ARG   A NH2 1 
ATOM   1353 N  N   . THR   A 1 194 ? 17.31498  -16.46822 4.28250   1.000 18.85824 ?  206 THR   A N   1 
ATOM   1354 C  CA  . THR   A 1 194 ? 16.64685  -17.23687 3.23977   1.000 23.81493 ?  206 THR   A CA  1 
ATOM   1355 C  C   . THR   A 1 194 ? 15.21789  -16.78063 2.99040   1.000 23.16056 ?  206 THR   A C   1 
ATOM   1356 O  O   . THR   A 1 194 ? 14.51675  -17.39163 2.17496   1.000 26.10588 ?  206 THR   A O   1 
ATOM   1357 C  CB  . THR   A 1 194 ? 16.66613  -18.73364 3.57473   1.000 28.52704 ?  206 THR   A CB  1 
ATOM   1358 O  OG1 . THR   A 1 194 ? 16.16882  -18.92793 4.90321   1.000 32.57378 ?  206 THR   A OG1 1 
ATOM   1359 C  CG2 . THR   A 1 194 ? 18.09208  -19.27735 3.49674   1.000 30.93423 ?  206 THR   A CG2 1 
ATOM   1360 N  N   . SER   A 1 195 ? 14.76428  -15.73238 3.66513   1.000 21.79157 ?  207 SER   A N   1 
ATOM   1361 C  CA  . SER   A 1 195 ? 13.47068  -15.13090 3.39487   1.000 19.27790 ?  207 SER   A CA  1 
ATOM   1362 C  C   . SER   A 1 195 ? 13.68166  -13.64676 3.15185   1.000 18.52521 ?  207 SER   A C   1 
ATOM   1363 O  O   . SER   A 1 195 ? 14.66063  -13.05956 3.61433   1.000 22.18175 ?  207 SER   A O   1 
ATOM   1364 C  CB  . SER   A 1 195 ? 12.50384  -15.32232 4.56780   1.000 22.98330 ?  207 SER   A CB  1 
ATOM   1365 O  OG  . SER   A 1 195 ? 12.90396  -14.52439 5.66699   1.000 30.97007 ?  207 SER   A OG  1 
ATOM   1366 N  N   . ALA   A 1 196 ? 12.76069  -13.03570 2.41583   1.000 18.43392 ?  208 ALA   A N   1 
ATOM   1367 C  CA  . ALA   A 1 196 ? 12.93973  -11.63554 2.07347   1.000 21.49755 ?  208 ALA   A CA  1 
ATOM   1368 C  C   . ALA   A 1 196 ? 12.83455  -10.77230 3.32387   1.000 18.61521 ?  208 ALA   A C   1 
ATOM   1369 O  O   . ALA   A 1 196 ? 12.11244  -11.08853 4.27517   1.000 25.96640 ?  208 ALA   A O   1 
ATOM   1370 C  CB  . ALA   A 1 196 ? 11.91548  -11.19472 1.02662   1.000 24.29106 ?  208 ALA   A CB  1 
ATOM   1371 N  N   . GLY   A 1 197 ? 13.58397  -9.68426  3.33188   1.000 18.22323 ?  209 GLY   A N   1 
ATOM   1372 C  CA  . GLY   A 1 197 ? 13.53715  -8.82304  4.49287   1.000 27.77914 ?  209 GLY   A CA  1 
ATOM   1373 C  C   . GLY   A 1 197 ? 12.34278  -7.90283  4.43567   1.000 38.32401 ?  209 GLY   A C   1 
ATOM   1374 O  O   . GLY   A 1 197 ? 11.22951  -8.32355  4.10066   1.000 36.38362 ?  209 GLY   A O   1 
ATOM   1375 N  N   . ASN   A 1 198 ? 12.56586  -6.64063  4.77252   1.000 29.27049 ?  210 ASN   A N   1 
ATOM   1376 C  CA  . ASN   A 1 198 ? 11.57105  -5.61630  4.52368   1.000 29.16705 ?  210 ASN   A CA  1 
ATOM   1377 C  C   . ASN   A 1 198 ? 11.68882  -5.22493  3.06129   1.000 32.01902 ?  210 ASN   A C   1 
ATOM   1378 O  O   . ASN   A 1 198 ? 12.73791  -4.73817  2.62146   1.000 33.64222 ?  210 ASN   A O   1 
ATOM   1379 C  CB  . ASN   A 1 198 ? 11.81790  -4.41864  5.43600   1.000 35.40947 ?  210 ASN   A CB  1 
ATOM   1380 C  CG  . ASN   A 1 198 ? 10.64948  -3.45123  5.45667   1.000 43.25082 ?  210 ASN   A CG  1 
ATOM   1381 O  OD1 . ASN   A 1 198 ? 10.11944  -3.07036  4.40813   1.000 37.15263 ?  210 ASN   A OD1 1 
ATOM   1382 N  ND2 . ASN   A 1 198 ? 10.22798  -3.05945  6.65686   1.000 41.35608 ?  210 ASN   A ND2 1 
ATOM   1383 N  N   . VAL   A 1 199 ? 10.63652  -5.48563  2.29368   1.000 20.53824 ?  211 VAL   A N   1 
ATOM   1384 C  CA  . VAL   A 1 199 ? 10.64013  -5.17137  0.87494   1.000 19.61821 ?  211 VAL   A CA  1 
ATOM   1385 C  C   . VAL   A 1 199 ? 9.56441   -4.15464  0.51533   1.000 18.16835 ?  211 VAL   A C   1 
ATOM   1386 O  O   . VAL   A 1 199 ? 9.15485   -4.06358  -0.63519  1.000 19.80850 ?  211 VAL   A O   1 
ATOM   1387 C  CB  . VAL   A 1 199 ? 10.57245  -6.44169  0.00568   1.000 21.14186 ?  211 VAL   A CB  1 
ATOM   1388 C  CG1 . VAL   A 1 199 ? 11.83561  -7.26936  0.19032   1.000 22.23984 ?  211 VAL   A CG1 1 
ATOM   1389 C  CG2 . VAL   A 1 199 ? 9.33569   -7.24898  0.35842   1.000 22.41998 ?  211 VAL   A CG2 1 
ATOM   1390 N  N   . ALA   A 1 200 ? 9.11763   -3.37140  1.50126   1.000 21.92701 ?  212 ALA   A N   1 
ATOM   1391 C  CA  . ALA   A 1 200 ? 8.01516   -2.44414  1.27224   1.000 24.78876 ?  212 ALA   A CA  1 
ATOM   1392 C  C   . ALA   A 1 200 ? 8.32350   -1.44149  0.16647   1.000 16.56170 ?  212 ALA   A C   1 
ATOM   1393 O  O   . ALA   A 1 200 ? 7.41811   -1.01428  -0.55548  1.000 20.02822 ?  212 ALA   A O   1 
ATOM   1394 C  CB  . ALA   A 1 200 ? 7.66520   -1.72657  2.57525   1.000 22.19462 ?  212 ALA   A CB  1 
ATOM   1395 N  N   . ASP   A 1 201 ? 9.59477   -1.07887  -0.01699  1.000 15.64223 ?  213 ASP   A N   1 
ATOM   1396 C  CA  . ASP   A 1 201 ? 9.98128   -0.10978  -1.03394  1.000 14.10679 ?  213 ASP   A CA  1 
ATOM   1397 C  C   . ASP   A 1 201 ? 10.75494  -0.74078  -2.18537  1.000 12.64072 ?  213 ASP   A C   1 
ATOM   1398 O  O   . ASP   A 1 201 ? 11.35882  -0.02023  -2.98860  1.000 13.64876 ?  213 ASP   A O   1 
ATOM   1399 C  CB  . ASP   A 1 201 ? 10.77638  1.02612   -0.39211  1.000 16.74323 ?  213 ASP   A CB  1 
ATOM   1400 C  CG  . ASP   A 1 201 ? 9.95895   1.77635   0.64025   1.000 16.82429 ?  213 ASP   A CG  1 
ATOM   1401 O  OD1 . ASP   A 1 201 ? 8.72990   1.91871   0.41987   1.000 23.76497 ?  213 ASP   A OD1 1 
ATOM   1402 O  OD2 . ASP   A 1 201 ? 10.52200  2.18038   1.67259   1.000 17.00844 ?  213 ASP   A OD2 1 
ATOM   1403 N  N   . ALA   A 1 202 ? 10.73798  -2.06663  -2.28585  1.000 13.16705 ?  214 ALA   A N   1 
ATOM   1404 C  CA  . ALA   A 1 202 ? 11.54053  -2.76902  -3.27148  1.000 12.52110 ?  214 ALA   A CA  1 
ATOM   1405 C  C   . ALA   A 1 202 ? 10.84503  -2.81070  -4.62681  1.000 12.33855 ?  214 ALA   A C   1 
ATOM   1406 O  O   . ALA   A 1 202 ? 9.61911   -2.68140  -4.74144  1.000 17.23657 ?  214 ALA   A O   1 
ATOM   1407 C  CB  . ALA   A 1 202 ? 11.78413  -4.20545  -2.81257  1.000 13.38692 ?  214 ALA   A CB  1 
ATOM   1408 N  N   . ASP   A 1 203 ? 11.64931  -2.99678  -5.66161  1.000 10.42973 ?  215 ASP   A N   1 
ATOM   1409 C  CA  . ASP   A 1 203 ? 11.16203  -3.36456  -6.99270  1.000 11.87153 ?  215 ASP   A CA  1 
ATOM   1410 C  C   . ASP   A 1 203 ? 11.51739  -4.84306  -7.16072  1.000 10.56188 ?  215 ASP   A C   1 
ATOM   1411 O  O   . ASP   A 1 203 ? 12.58405  -5.19395  -7.66052  1.000 11.19187 ?  215 ASP   A O   1 
ATOM   1412 C  CB  . ASP   A 1 203 ? 11.78680  -2.47669  -8.07340  1.000 13.12869 ?  215 ASP   A CB  1 
ATOM   1413 C  CG  . ASP   A 1 203 ? 11.10977  -2.64029  -9.42764  1.000 13.80203 ?  215 ASP   A CG  1 
ATOM   1414 O  OD1 . ASP   A 1 203 ? 10.72812  -3.77922  -9.76664  1.000 14.08660 ?  215 ASP   A OD1 1 
ATOM   1415 O  OD2 . ASP   A 1 203 ? 10.96589  -1.63264  -10.15330 1.000 20.61704 ?  215 ASP   A OD2 1 
ATOM   1416 N  N   . LEU   A 1 204 ? 10.60507  -5.71706  -6.72598  1.000 12.42443 ?  216 LEU   A N   1 
ATOM   1417 C  CA  . LEU   A 1 204 ? 10.84251  -7.14930  -6.84153  1.000 10.99475 ?  216 LEU   A CA  1 
ATOM   1418 C  C   . LEU   A 1 204 ? 10.97362  -7.58872  -8.28761  1.000 12.18292 ?  216 LEU   A C   1 
ATOM   1419 O  O   . LEU   A 1 204 ? 11.77371  -8.48049  -8.59845  1.000 12.70729 ?  216 LEU   A O   1 
ATOM   1420 C  CB  . LEU   A 1 204 ? 9.70669   -7.92123  -6.17833  1.000 12.83092 ?  216 LEU   A CB  1 
ATOM   1421 C  CG  . LEU   A 1 204 ? 9.60637   -7.69991  -4.66874  1.000 14.50653 ?  216 LEU   A CG  1 
ATOM   1422 C  CD1 . LEU   A 1 204 ? 8.26440   -8.18282  -4.16725  1.000 20.34023 ?  216 LEU   A CD1 1 
ATOM   1423 C  CD2 . LEU   A 1 204 ? 10.73607  -8.39343  -3.92647  1.000 16.38512 ?  216 LEU   A CD2 1 
ATOM   1424 N  N   . ALA   A 1 205 ? 10.22868  -6.94725  -9.19237  1.000 13.54404 ?  217 ALA   A N   1 
ATOM   1425 C  CA  . ALA   A 1 205 ? 10.25644  -7.36062  -10.58868 1.000 14.42911 ?  217 ALA   A CA  1 
ATOM   1426 C  C   . ALA   A 1 205 ? 11.60151  -7.08493  -11.22691 1.000 13.32110 ?  217 ALA   A C   1 
ATOM   1427 O  O   . ALA   A 1 205 ? 12.03629  -7.83746  -12.10149 1.000 14.86398 ?  217 ALA   A O   1 
ATOM   1428 C  CB  . ALA   A 1 205 ? 9.15462   -6.66032  -11.38787 1.000 15.39931 ?  217 ALA   A CB  1 
ATOM   1429 N  N   . GLU   A 1 206 ? 12.27089  -6.01575  -10.80483 1.000 11.78519 ?  218 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 206 ? 13.53582  -5.61640  -11.39943 1.000 11.33776 ?  218 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 206 ? 14.75315  -6.11204  -10.63499 1.000 10.47464 ?  218 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 206 ? 15.84946  -6.12849  -11.19817 1.000 10.66418 ?  218 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 206 ? 13.60735  -4.08959  -11.50107 1.000 12.64072 ?  218 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 206 ? 12.67837  -3.54037  -12.57713 1.000 16.25533 ?  218 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 206 ? 12.97188  -4.15992  -13.92461 1.000 20.51189 ?  218 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 206 ? 14.16329  -4.40768  -14.23106 1.000 16.17453 ?  218 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 206 ? 11.99743  -4.40597  -14.68349 1.000 23.63421 ?  218 GLU   A OE2 1 
ATOM   1438 N  N   . TRP   A 1 207 ? 14.56886  -6.53729  -9.39094  1.000 10.74750 ?  219 TRP   A N   1 
ATOM   1439 C  CA  . TRP   A 1 207 ? 15.70574  -6.87998  -8.53324  1.000 10.64425 ?  219 TRP   A CA  1 
ATOM   1440 C  C   . TRP   A 1 207 ? 16.63036  -7.93037  -9.14594  1.000 11.58640 ?  219 TRP   A C   1 
ATOM   1441 O  O   . TRP   A 1 207 ? 17.85520  -7.71754  -9.13875  1.000 10.19829 ?  219 TRP   A O   1 
ATOM   1442 C  CB  . TRP   A 1 207 ? 15.16221  -7.22527  -7.14644  1.000 8.88320  ?  219 TRP   A CB  1 
ATOM   1443 C  CG  . TRP   A 1 207 ? 16.10215  -7.27815  -5.98216  1.000 9.00373  ?  219 TRP   A CG  1 
ATOM   1444 C  CD1 . TRP   A 1 207 ? 17.45026  -7.47858  -6.00639  1.000 9.54294  ?  219 TRP   A CD1 1 
ATOM   1445 C  CD2 . TRP   A 1 207 ? 15.73124  -7.14666  -4.60909  1.000 8.64012  ?  219 TRP   A CD2 1 
ATOM   1446 N  NE1 . TRP   A 1 207 ? 17.94803  -7.47215  -4.72011  1.000 9.95927  ?  219 TRP   A NE1 1 
ATOM   1447 C  CE2 . TRP   A 1 207 ? 16.91135  -7.26508  -3.84342  1.000 8.29342  ?  219 TRP   A CE2 1 
ATOM   1448 C  CE3 . TRP   A 1 207 ? 14.51537  -6.93396  -3.94949  1.000 11.10019 ?  219 TRP   A CE3 1 
ATOM   1449 C  CZ2 . TRP   A 1 207 ? 16.90158  -7.18604  -2.45066  1.000 11.51021 ?  219 TRP   A CZ2 1 
ATOM   1450 C  CZ3 . TRP   A 1 207 ? 14.50697  -6.85166  -2.56884  1.000 11.97753 ?  219 TRP   A CZ3 1 
ATOM   1451 C  CH2 . TRP   A 1 207 ? 15.69110  -6.98133  -1.83388  1.000 10.57636 ?  219 TRP   A CH2 1 
ATOM   1452 N  N   . PRO   A 1 208 ? 16.14369  -9.05988  -9.68746  1.000 10.81001 ?  220 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 208 ? 17.09068  -10.00209 -10.31517 1.000 9.17673  ?  220 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 208 ? 17.86830  -9.39762  -11.46948 1.000 10.57666 ?  220 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 208 ? 19.06276  -9.67961  -11.62379 1.000 11.80656 ?  220 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 208 ? 16.18886  -11.15413 -10.76922 1.000 10.20630 ?  220 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 208 ? 15.05888  -11.11547 -9.83808  1.000 11.26648 ?  220 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 208 ? 14.79523  -9.65514  -9.57240  1.000 12.87189 ?  220 PRO   A CD  1 
ATOM   1459 N  N   . THR   A 1 209 ? 17.21150  -8.57806  -12.30627 1.000 10.41753 ?  221 THR   A N   1 
ATOM   1460 C  CA  . THR   A 1 209 ? 17.91636  -7.91844  -13.39962 1.000 12.04262 ?  221 THR   A CA  1 
ATOM   1461 C  C   . THR   A 1 209 ? 19.00222  -6.97973  -12.87975 1.000 11.72464 ?  221 THR   A C   1 
ATOM   1462 O  O   . THR   A 1 209 ? 20.10679  -6.92580  -13.43833 1.000 12.56856 ?  221 THR   A O   1 
ATOM   1463 C  CB  . THR   A 1 209 ? 16.91917  -7.15824  -14.27465 1.000 12.56617 ?  221 THR   A CB  1 
ATOM   1464 O  OG1 . THR   A 1 209 ? 15.97654  -8.08732  -14.83900 1.000 14.50472 ?  221 THR   A OG1 1 
ATOM   1465 C  CG2 . THR   A 1 209 ? 17.66923  -6.41188  -15.39818 1.000 16.15173 ?  221 THR   A CG2 1 
ATOM   1466 N  N   . SER   A 1 210 ? 18.69759  -6.22648  -11.81368 1.000 10.82504 ?  222 SER   A N   1 
ATOM   1467 C  CA  A SER   A 1 210 ? 19.68834  -5.33911  -11.21479 0.903 10.93178 ?  222 SER   A CA  1 
ATOM   1468 C  CA  B SER   A 1 210 ? 19.69896  -5.33983  -11.22624 0.097 10.97681 ?  222 SER   A CA  1 
ATOM   1469 C  C   . SER   A 1 210 ? 20.88256  -6.12579  -10.67364 1.000 11.31940 ?  222 SER   A C   1 
ATOM   1470 O  O   . SER   A 1 210 ? 22.03661  -5.72344  -10.85368 1.000 9.73146  ?  222 SER   A O   1 
ATOM   1471 C  CB  A SER   A 1 210 ? 18.99567  -4.50038  -10.13535 0.903 10.49613 ?  222 SER   A CB  1 
ATOM   1472 C  CB  B SER   A 1 210 ? 19.07195  -4.46943  -10.13829 0.097 10.61672 ?  222 SER   A CB  1 
ATOM   1473 O  OG  A SER   A 1 210 ? 17.97270  -3.73093  -10.75843 0.903 9.15540  ?  222 SER   A OG  1 
ATOM   1474 O  OG  B SER   A 1 210 ? 18.20903  -5.23315  -9.32448  0.097 10.58271 ?  222 SER   A OG  1 
ATOM   1475 N  N   . ILE   A 1 211 ? 20.62118  -7.27152  -10.02948 1.000 10.77093 ?  223 ILE   A N   1 
ATOM   1476 C  CA  A ILE   A 1 211 ? 21.71490  -8.12158  -9.55908  0.885 9.60989  ?  223 ILE   A CA  1 
ATOM   1477 C  CA  B ILE   A 1 211 ? 21.70081  -8.14269  -9.55949  0.115 9.83130  ?  223 ILE   A CA  1 
ATOM   1478 C  C   . ILE   A 1 211 ? 22.57066  -8.59657  -10.72864 1.000 10.81203 ?  223 ILE   A C   1 
ATOM   1479 O  O   . ILE   A 1 211 ? 23.80812  -8.61226  -10.64577 1.000 12.46590 ?  223 ILE   A O   1 
ATOM   1480 C  CB  A ILE   A 1 211 ? 21.16871  -9.28656  -8.70833  0.885 9.28877  ?  223 ILE   A CB  1 
ATOM   1481 C  CB  B ILE   A 1 211 ? 21.11258  -9.34565  -8.79678  0.115 9.63784  ?  223 ILE   A CB  1 
ATOM   1482 C  CG1 A ILE   A 1 211 ? 20.72079  -8.76599  -7.33275  0.885 12.82450 ?  223 ILE   A CG1 1 
ATOM   1483 C  CG1 B ILE   A 1 211 ? 20.26166  -8.87110  -7.61706  0.115 12.39713 ?  223 ILE   A CG1 1 
ATOM   1484 C  CG2 A ILE   A 1 211 ? 22.20963  -10.41826 -8.59184  0.885 12.60266 ?  223 ILE   A CG2 1 
ATOM   1485 C  CG2 B ILE   A 1 211 ? 22.22166  -10.28190 -8.33365  0.115 12.74658 ?  223 ILE   A CG2 1 
ATOM   1486 C  CD1 A ILE   A 1 211 ? 19.93525  -9.77002  -6.51274  0.885 14.48074 ?  223 ILE   A CD1 1 
ATOM   1487 C  CD1 B ILE   A 1 211 ? 21.02806  -8.17012  -6.55277  0.115 13.47909 ?  223 ILE   A CD1 1 
ATOM   1488 N  N   . GLU   A 1 212 ? 21.94090  -8.96633  -11.84363 1.000 11.76372 ?  224 GLU   A N   1 
ATOM   1489 C  CA  A GLU   A 1 212 ? 22.74577  -9.38425  -12.98628 0.525 13.71150 ?  224 GLU   A CA  1 
ATOM   1490 C  CA  B GLU   A 1 212 ? 22.70268  -9.36708  -13.02663 0.475 13.76228 ?  224 GLU   A CA  1 
ATOM   1491 C  C   . GLU   A 1 212 ? 23.62987  -8.24929  -13.49008 1.000 12.41751 ?  224 GLU   A C   1 
ATOM   1492 O  O   . GLU   A 1 212 ? 24.75910  -8.49572  -13.93422 1.000 13.64447 ?  224 GLU   A O   1 
ATOM   1493 C  CB  A GLU   A 1 212 ? 21.86228  -9.95361  -14.09800 0.525 17.15814 ?  224 GLU   A CB  1 
ATOM   1494 C  CB  B GLU   A 1 212 ? 21.74356  -9.72227  -14.16582 0.475 16.18404 ?  224 GLU   A CB  1 
ATOM   1495 C  CG  A GLU   A 1 212 ? 22.63099  -10.61371 -15.25938 0.525 13.37933 ?  224 GLU   A CG  1 
ATOM   1496 C  CG  B GLU   A 1 212 ? 20.99337  -11.03513 -14.01731 0.475 17.10211 ?  224 GLU   A CG  1 
ATOM   1497 C  CD  A GLU   A 1 212 ? 23.70482  -11.59494 -14.80677 0.525 22.75869 ?  224 GLU   A CD  1 
ATOM   1498 C  CD  B GLU   A 1 212 ? 20.06973  -11.30695 -15.19898 0.475 23.68649 ?  224 GLU   A CD  1 
ATOM   1499 O  OE1 A GLU   A 1 212 ? 23.45364  -12.41412 -13.89340 0.525 22.38850 ?  224 GLU   A OE1 1 
ATOM   1500 O  OE1 B GLU   A 1 212 ? 19.87797  -10.39154 -16.02887 0.475 24.99909 ?  224 GLU   A OE1 1 
ATOM   1501 O  OE2 A GLU   A 1 212 ? 24.80686  -11.55490 -15.39035 0.525 25.41076 ?  224 GLU   A OE2 1 
ATOM   1502 O  OE2 B GLU   A 1 212 ? 19.52923  -12.42995 -15.29573 0.475 28.72783 ?  224 GLU   A OE2 1 
ATOM   1503 N  N   . ARG   A 1 213 ? 23.16141  -6.99629  -13.41415 1.000 11.67670 ?  225 ARG   A N   1 
ATOM   1504 C  CA  . ARG   A 1 213 ? 24.03832  -5.89883  -13.81641 1.000 10.84906 ?  225 ARG   A CA  1 
ATOM   1505 C  C   . ARG   A 1 213 ? 25.26296  -5.81885  -12.90746 1.000 9.13047  ?  225 ARG   A C   1 
ATOM   1506 O  O   . ARG   A 1 213 ? 26.37518  -5.51747  -13.37076 1.000 11.42444 ?  225 ARG   A O   1 
ATOM   1507 C  CB  . ARG   A 1 213 ? 23.28891  -4.55805  -13.81867 1.000 11.13785 ?  225 ARG   A CB  1 
ATOM   1508 C  CG  . ARG   A 1 213 ? 22.16340  -4.45449  -14.85432 1.000 11.64963 ?  225 ARG   A CG  1 
ATOM   1509 C  CD  . ARG   A 1 213 ? 21.80618  -2.99494  -15.13034 1.000 10.68586 ?  225 ARG   A CD  1 
ATOM   1510 N  NE  . ARG   A 1 213 ? 20.66292  -2.87924  -16.02826 1.000 12.18831 ?  225 ARG   A NE  1 
ATOM   1511 C  CZ  . ARG   A 1 213 ? 19.40073  -2.99022  -15.64614 1.000 13.88587 ?  225 ARG   A CZ  1 
ATOM   1512 N  NH1 . ARG   A 1 213 ? 19.06740  -3.06731  -14.36763 1.000 13.68839 ?  225 ARG   A NH1 1 
ATOM   1513 N  NH2 . ARG   A 1 213 ? 18.44288  -3.04655  -16.57107 1.000 16.84248 ?  225 ARG   A NH2 1 
ATOM   1514 N  N   . ILE   A 1 214 ? 25.06903  -6.05011  -11.59995 1.000 10.74806 ?  226 ILE   A N   1 
ATOM   1515 C  CA  . ILE   A 1 214 ? 26.20420  -6.07454  -10.67281 1.000 10.13683 ?  226 ILE   A CA  1 
ATOM   1516 C  C   . ILE   A 1 214 ? 27.20018  -7.15374  -11.07754 1.000 10.86309 ?  226 ILE   A C   1 
ATOM   1517 O  O   . ILE   A 1 214 ? 28.40552  -6.90512  -11.16863 1.000 12.34984 ?  226 ILE   A O   1 
ATOM   1518 C  CB  . ILE   A 1 214 ? 25.71809  -6.27818  -9.22985  1.000 9.77894  ?  226 ILE   A CB  1 
ATOM   1519 C  CG1 . ILE   A 1 214 ? 24.73543  -5.16183  -8.84657  1.000 10.58906 ?  226 ILE   A CG1 1 
ATOM   1520 C  CG2 . ILE   A 1 214 ? 26.90477  -6.25253  -8.27726  1.000 10.10755 ?  226 ILE   A CG2 1 
ATOM   1521 C  CD1 . ILE   A 1 214 ? 24.08511  -5.37641  -7.48842  1.000 12.19535 ?  226 ILE   A CD1 1 
ATOM   1522 N  N   . GLN   A 1 215 ? 26.70885  -8.37199  -11.30685 1.000 11.27308 ?  227 GLN   A N   1 
ATOM   1523 C  CA  . GLN   A 1 215 ? 27.58271  -9.47068  -11.72353 1.000 11.84273 ?  227 GLN   A CA  1 
ATOM   1524 C  C   . GLN   A 1 215 ? 28.33155  -9.12133  -13.00601 1.000 13.15872 ?  227 GLN   A C   1 
ATOM   1525 O  O   . GLN   A 1 215 ? 29.54677  -9.34908  -13.10995 1.000 16.60095 ?  227 GLN   A O   1 
ATOM   1526 C  CB  . GLN   A 1 215 ? 26.73974  -10.73727 -11.88486 1.000 13.88032 ?  227 GLN   A CB  1 
ATOM   1527 C  CG  . GLN   A 1 215 ? 27.42153  -11.92682 -12.60672 1.000 16.26887 ?  227 GLN   A CG  1 
ATOM   1528 C  CD  . GLN   A 1 215 ? 28.58603  -12.51947 -11.83027 1.000 20.97849 ?  227 GLN   A CD  1 
ATOM   1529 O  OE1 . GLN   A 1 215 ? 28.44381  -12.90722 -10.67103 1.000 20.25830 ?  227 GLN   A OE1 1 
ATOM   1530 N  NE2 . GLN   A 1 215 ? 29.75032  -12.60263 -12.48122 1.000 18.68021 ?  227 GLN   A NE2 1 
ATOM   1531 N  N   . GLN   A 1 216 ? 27.62880  -8.53381  -13.97735 1.000 12.88632 ?  228 GLN   A N   1 
ATOM   1532 C  CA  . GLN   A 1 216 ? 28.25386  -8.16958  -15.24811 1.000 16.19576 ?  228 GLN   A CA  1 
ATOM   1533 C  C   . GLN   A 1 216 ? 29.33991  -7.11672  -15.06730 1.000 15.15985 ?  228 GLN   A C   1 
ATOM   1534 O  O   . GLN   A 1 216 ? 30.36313  -7.13196  -15.76629 1.000 16.08240 ?  228 GLN   A O   1 
ATOM   1535 C  CB  . GLN   A 1 216 ? 27.18930  -7.64997  -16.21047 1.000 18.25456 ?  228 GLN   A CB  1 
ATOM   1536 C  CG  . GLN   A 1 216 ? 26.26627  -8.71337  -16.74910 1.000 26.94233 ?  228 GLN   A CG  1 
ATOM   1537 C  CD  . GLN   A 1 216 ? 27.00232  -9.74046  -17.58097 1.000 41.98853 ?  228 GLN   A CD  1 
ATOM   1538 O  OE1 . GLN   A 1 216 ? 26.95888  -10.93795 -17.29649 1.000 43.85136 ?  228 GLN   A OE1 1 
ATOM   1539 N  NE2 . GLN   A 1 216 ? 27.69250  -9.27213  -18.62054 1.000 34.56775 ?  228 GLN   A NE2 1 
ATOM   1540 N  N   . HIS   A 1 217 ? 29.13671  -6.17719  -14.14675 1.000 12.78168 ?  229 HIS   A N   1 
ATOM   1541 C  CA  . HIS   A 1 217 ? 30.07857  -5.08020  -13.99997 1.000 12.11805 ?  229 HIS   A CA  1 
ATOM   1542 C  C   . HIS   A 1 217 ? 31.25755  -5.43221  -13.10125 1.000 12.51848 ?  229 HIS   A C   1 
ATOM   1543 O  O   . HIS   A 1 217 ? 32.36146  -4.91183  -13.31510 1.000 14.42129 ?  229 HIS   A O   1 
ATOM   1544 C  CB  . HIS   A 1 217 ? 29.35990  -3.84157  -13.44904 1.000 14.43786 ?  229 HIS   A CB  1 
ATOM   1545 C  CG  . HIS   A 1 217 ? 29.92495  -2.55229  -13.94456 1.000 17.60318 ?  229 HIS   A CG  1 
ATOM   1546 N  ND1 . HIS   A 1 217 ? 29.62215  -2.04098  -15.18721 1.000 24.65155 ?  229 HIS   A ND1 1 
ATOM   1547 C  CD2 . HIS   A 1 217 ? 30.79984  -1.68533  -13.38268 1.000 16.97188 ?  229 HIS   A CD2 1 
ATOM   1548 C  CE1 . HIS   A 1 217 ? 30.27621  -0.90719  -15.36503 1.000 25.36346 ?  229 HIS   A CE1 1 
ATOM   1549 N  NE2 . HIS   A 1 217 ? 31.00798  -0.67590  -14.29096 1.000 21.69471 ?  229 HIS   A NE2 1 
ATOM   1550 N  N   . TYR   A 1 218 ? 31.05476  -6.32398  -12.12720 1.000 12.59181 ?  230 TYR   A N   1 
ATOM   1551 C  CA  . TYR   A 1 218 ? 32.09511  -6.66930  -11.15212 1.000 11.88739 ?  230 TYR   A CA  1 
ATOM   1552 C  C   . TYR   A 1 218 ? 32.33591  -8.17807  -11.06247 1.000 14.48290 ?  230 TYR   A C   1 
ATOM   1553 O  O   . TYR   A 1 218 ? 32.40423  -8.74459  -9.97115  1.000 14.24029 ?  230 TYR   A O   1 
ATOM   1554 C  CB  . TYR   A 1 218 ? 31.73384  -6.09275  -9.78215  1.000 10.66824 ?  230 TYR   A CB  1 
ATOM   1555 C  CG  . TYR   A 1 218 ? 31.52619  -4.59349  -9.83616  1.000 12.94228 ?  230 TYR   A CG  1 
ATOM   1556 C  CD1 . TYR   A 1 218 ? 32.58184  -3.72548  -10.11631 1.000 11.37414 ?  230 TYR   A CD1 1 
ATOM   1557 C  CD2 . TYR   A 1 218 ? 30.26114  -4.04184  -9.61828  1.000 11.98015 ?  230 TYR   A CD2 1 
ATOM   1558 C  CE1 . TYR   A 1 218 ? 32.38481  -2.37223  -10.19495 1.000 13.21896 ?  230 TYR   A CE1 1 
ATOM   1559 C  CE2 . TYR   A 1 218 ? 30.06173  -2.67459  -9.68269  1.000 13.21304 ?  230 TYR   A CE2 1 
ATOM   1560 C  CZ  . TYR   A 1 218 ? 31.12027  -1.84654  -9.96389  1.000 14.69753 ?  230 TYR   A CZ  1 
ATOM   1561 O  OH  . TYR   A 1 218 ? 30.93291  -0.48830  -10.03829 1.000 16.35806 ?  230 TYR   A OH  1 
ATOM   1562 N  N   . PRO   A 1 219 ? 32.53938  -8.85460  -12.20092 1.000 13.95238 ?  231 PRO   A N   1 
ATOM   1563 C  CA  . PRO   A 1 219 ? 32.76788  -10.30949 -12.15393 1.000 14.42521 ?  231 PRO   A CA  1 
ATOM   1564 C  C   . PRO   A 1 219 ? 34.04576  -10.70123 -11.44710 1.000 13.62015 ?  231 PRO   A C   1 
ATOM   1565 O  O   . PRO   A 1 219 ? 34.17507  -11.86746 -11.05544 1.000 15.36725 ?  231 PRO   A O   1 
ATOM   1566 C  CB  . PRO   A 1 219 ? 32.84131  -10.69794 -13.63545 1.000 14.49338 ?  231 PRO   A CB  1 
ATOM   1567 C  CG  . PRO   A 1 219 ? 33.38175  -9.50219  -14.27583 1.000 11.88276 ?  231 PRO   A CG  1 
ATOM   1568 C  CD  . PRO   A 1 219 ? 32.71159  -8.33753  -13.56691 1.000 14.00958 ?  231 PRO   A CD  1 
ATOM   1569 N  N   . GLU   A 1 220 ? 34.98231  -9.77157  -11.28558 1.000 15.16049 ?  232 GLU   A N   1 
ATOM   1570 C  CA  . GLU   A 1 220 ? 36.25714  -10.02494 -10.63614 1.000 18.09417 ?  232 GLU   A CA  1 
ATOM   1571 C  C   . GLU   A 1 220 ? 36.22029  -9.81608  -9.12669  1.000 15.80013 ?  232 GLU   A C   1 
ATOM   1572 O  O   . GLU   A 1 220 ? 37.23961  -10.02243 -8.46457  1.000 15.56596 ?  232 GLU   A O   1 
ATOM   1573 C  CB  . GLU   A 1 220 ? 37.35239  -9.16044  -11.28301 1.000 17.55661 ?  232 GLU   A CB  1 
ATOM   1574 C  CG  . GLU   A 1 220 ? 37.41178  -7.69412  -10.82017 1.000 17.58979 ?  232 GLU   A CG  1 
ATOM   1575 C  CD  . GLU   A 1 220 ? 36.40695  -6.74692  -11.49260 1.000 21.34146 ?  232 GLU   A CD  1 
ATOM   1576 O  OE1 . GLU   A 1 220 ? 35.37374  -7.20357  -12.02604 1.000 17.60884 ?  232 GLU   A OE1 1 
ATOM   1577 O  OE2 . GLU   A 1 220 ? 36.65231  -5.51513  -11.47988 1.000 20.70874 ?  232 GLU   A OE2 1 
ATOM   1578 N  N   . ALA   A 1 221 ? 35.07570  -9.42550  -8.56565  1.000 13.59190 ?  233 ALA   A N   1 
ATOM   1579 C  CA  . ALA   A 1 221 ? 35.01334  -9.15120  -7.13317  1.000 14.15993 ?  233 ALA   A CA  1 
ATOM   1580 C  C   . ALA   A 1 221 ? 35.37098  -10.39028 -6.31826  1.000 13.49775 ?  233 ALA   A C   1 
ATOM   1581 O  O   . ALA   A 1 221 ? 34.88498  -11.49130 -6.59102  1.000 15.54841 ?  233 ALA   A O   1 
ATOM   1582 C  CB  . ALA   A 1 221 ? 33.61879  -8.63448  -6.75104  1.000 12.09651 ?  233 ALA   A CB  1 
ATOM   1583 N  N   . GLN   A 1 222 ? 36.22110  -10.19934 -5.30953  1.000 14.87927 ?  234 GLN   A N   1 
ATOM   1584 C  CA  . GLN   A 1 222 ? 36.68411  -11.27737 -4.43994  1.000 18.48252 ?  234 GLN   A CA  1 
ATOM   1585 C  C   . GLN   A 1 222 ? 35.99419  -11.29717 -3.08589  1.000 19.37030 ?  234 GLN   A C   1 
ATOM   1586 O  O   . GLN   A 1 222 ? 35.90621  -12.36102 -2.46523  1.000 18.68106 ?  234 GLN   A O   1 
ATOM   1587 C  CB  . GLN   A 1 222 ? 38.20427  -11.18735 -4.21213  1.000 19.32202 ?  234 GLN   A CB  1 
ATOM   1588 C  CG  . GLN   A 1 222 ? 39.07448  -11.36904 -5.46386  1.000 21.72390 ?  234 GLN   A CG  1 
ATOM   1589 C  CD  . GLN   A 1 222 ? 38.77781  -12.66033 -6.19631  1.000 30.97225 ?  234 GLN   A CD  1 
ATOM   1590 O  OE1 . GLN   A 1 222 ? 39.02596  -13.74868 -5.67301  1.000 35.69619 ?  234 GLN   A OE1 1 
ATOM   1591 N  NE2 . GLN   A 1 222 ? 38.24627  -12.55283 -7.40651  1.000 29.33820 ?  234 GLN   A NE2 1 
ATOM   1592 N  N   . PHE   A 1 223 ? 35.53194  -10.14692 -2.60285  1.000 16.04222 ?  235 PHE   A N   1 
ATOM   1593 C  CA  . PHE   A 1 223 ? 34.85657  -10.04619 -1.31839  1.000 15.68446 ?  235 PHE   A CA  1 
ATOM   1594 C  C   . PHE   A 1 223 ? 33.56546  -9.29090  -1.56493  1.000 12.53093 ?  235 PHE   A C   1 
ATOM   1595 O  O   . PHE   A 1 223 ? 33.59173  -8.22811  -2.19217  1.000 17.45728 ?  235 PHE   A O   1 
ATOM   1596 C  CB  . PHE   A 1 223 ? 35.69943  -9.24293  -0.32176  1.000 18.40113 ?  235 PHE   A CB  1 
ATOM   1597 C  CG  . PHE   A 1 223 ? 37.10234  -9.74138  -0.15833  1.000 26.36203 ?  235 PHE   A CG  1 
ATOM   1598 C  CD1 . PHE   A 1 223 ? 38.12883  -9.23961  -0.94870  1.000 26.36587 ?  235 PHE   A CD1 1 
ATOM   1599 C  CD2 . PHE   A 1 223 ? 37.40838  -10.67292 0.82048   1.000 31.31195 ?  235 PHE   A CD2 1 
ATOM   1600 C  CE1 . PHE   A 1 223 ? 39.43212  -9.68800  -0.78992  1.000 29.67977 ?  235 PHE   A CE1 1 
ATOM   1601 C  CE2 . PHE   A 1 223 ? 38.71074  -11.12283 0.98769   1.000 31.51475 ?  235 PHE   A CE2 1 
ATOM   1602 C  CZ  . PHE   A 1 223 ? 39.71992  -10.62940 0.18490   1.000 27.41117 ?  235 PHE   A CZ  1 
ATOM   1603 N  N   . VAL   A 1 224 ? 32.44502  -9.84659  -1.11842  1.000 13.20507 ?  236 VAL   A N   1 
ATOM   1604 C  CA  . VAL   A 1 224 ? 31.13895  -9.22044  -1.31019  1.000 11.41522 ?  236 VAL   A CA  1 
ATOM   1605 C  C   . VAL   A 1 224 ? 30.54353  -8.98775  0.07069   1.000 11.63398 ?  236 VAL   A C   1 
ATOM   1606 O  O   . VAL   A 1 224 ? 30.37232  -9.93952  0.84140   1.000 13.71785 ?  236 VAL   A O   1 
ATOM   1607 C  CB  . VAL   A 1 224 ? 30.21916  -10.08930 -2.18269  1.000 12.08894 ?  236 VAL   A CB  1 
ATOM   1608 C  CG1 . VAL   A 1 224 ? 28.86581  -9.40344  -2.35474  1.000 12.55906 ?  236 VAL   A CG1 1 
ATOM   1609 C  CG2 . VAL   A 1 224 ? 30.87972  -10.34355 -3.53972  1.000 15.41502 ?  236 VAL   A CG2 1 
ATOM   1610 N  N   . ILE   A 1 225 ? 30.23788  -7.73454  0.38099   1.000 10.25532 ?  237 ILE   A N   1 
ATOM   1611 C  CA  A ILE   A 1 225 ? 29.72869  -7.32775  1.69066   0.477 10.92886 ?  237 ILE   A CA  1 
ATOM   1612 C  CA  B ILE   A 1 225 ? 29.71987  -7.35037  1.69350   0.523 10.91021 ?  237 ILE   A CA  1 
ATOM   1613 C  C   . ILE   A 1 225 ? 28.23367  -7.05764  1.55976   1.000 10.66745 ?  237 ILE   A C   1 
ATOM   1614 O  O   . ILE   A 1 225 ? 27.84829  -6.12048  0.83744   1.000 10.57980 ?  237 ILE   A O   1 
ATOM   1615 C  CB  A ILE   A 1 225 ? 30.45856  -6.07049  2.18638   0.477 11.76564 ?  237 ILE   A CB  1 
ATOM   1616 C  CB  B ILE   A 1 225 ? 30.45598  -6.13406  2.26242   0.523 11.78626 ?  237 ILE   A CB  1 
ATOM   1617 C  CG1 A ILE   A 1 225 ? 31.97388  -6.17015  1.93359   0.477 13.58634 ?  237 ILE   A CG1 1 
ATOM   1618 C  CG1 B ILE   A 1 225 ? 31.92319  -6.46941  2.46903   0.523 12.50922 ?  237 ILE   A CG1 1 
ATOM   1619 C  CG2 A ILE   A 1 225 ? 30.15755  -5.82151  3.65820   0.477 13.19506 ?  237 ILE   A CG2 1 
ATOM   1620 C  CG2 B ILE   A 1 225 ? 29.81410  -5.68151  3.57217   0.523 12.59489 ?  237 ILE   A CG2 1 
ATOM   1621 C  CD1 A ILE   A 1 225 ? 32.63648  -7.38764  2.55117   0.477 15.61857 ?  237 ILE   A CD1 1 
ATOM   1622 C  CD1 B ILE   A 1 225 ? 32.74382  -5.27763  2.44365   0.523 12.55640 ?  237 ILE   A CD1 1 
ATOM   1623 N  N   . PRO   A 1 226 ? 27.37227  -7.80268  2.24307   1.000 10.69745 ?  238 PRO   A N   1 
ATOM   1624 C  CA  . PRO   A 1 226 ? 25.93793  -7.51002  2.22416   1.000 10.04969 ?  238 PRO   A CA  1 
ATOM   1625 C  C   . PRO   A 1 226 ? 25.64410  -6.35581  3.17103   1.000 11.20740 ?  238 PRO   A C   1 
ATOM   1626 O  O   . PRO   A 1 226 ? 26.46085  -5.97498  4.00849   1.000 10.68935 ?  238 PRO   A O   1 
ATOM   1627 C  CB  . PRO   A 1 226 ? 25.31514  -8.80812  2.76141   1.000 12.26822 ?  238 PRO   A CB  1 
ATOM   1628 C  CG  . PRO   A 1 226 ? 26.35628  -9.32579  3.74129   1.000 12.48050 ?  238 PRO   A CG  1 
ATOM   1629 C  CD  . PRO   A 1 226 ? 27.70622  -8.93209  3.13693   1.000 10.96542 ?  238 PRO   A CD  1 
ATOM   1630 N  N   . GLY   A 1 227 ? 24.43535  -5.80869  3.05213   1.000 10.97600 ?  239 GLY   A N   1 
ATOM   1631 C  CA  . GLY   A 1 227 ? 24.05840  -4.72278  3.94004   1.000 10.45451 ?  239 GLY   A CA  1 
ATOM   1632 C  C   . GLY   A 1 227 ? 23.97317  -5.15513  5.38902   1.000 9.99615  ?  239 GLY   A C   1 
ATOM   1633 O  O   . GLY   A 1 227 ? 24.17505  -4.34163  6.29328   1.000 10.40853 ?  239 GLY   A O   1 
ATOM   1634 N  N   . HIS   A 1 228 ? 23.67969  -6.43763  5.62168   1.000 10.20066 ?  240 HIS   A N   1 
ATOM   1635 C  CA  . HIS   A 1 228 ? 23.54622  -7.01738  6.95217   1.000 11.02908 ?  240 HIS   A CA  1 
ATOM   1636 C  C   . HIS   A 1 228 ? 24.17219  -8.39959  6.96487   1.000 11.78528 ?  240 HIS   A C   1 
ATOM   1637 O  O   . HIS   A 1 228 ? 23.84842  -9.23476  6.12347   1.000 12.46254 ?  240 HIS   A O   1 
ATOM   1638 C  CB  . HIS   A 1 228 ? 22.06286  -7.11650  7.32697   1.000 11.20179 ?  240 HIS   A CB  1 
ATOM   1639 C  CG  . HIS   A 1 228 ? 21.35327  -5.81377  7.22276   1.000 11.61217 ?  240 HIS   A CG  1 
ATOM   1640 N  ND1 . HIS   A 1 228 ? 21.32190  -4.90639  8.25893   1.000 12.37746 ?  240 HIS   A ND1 1 
ATOM   1641 C  CD2 . HIS   A 1 228 ? 20.68501  -5.24215  6.19335   1.000 14.78387 ?  240 HIS   A CD2 1 
ATOM   1642 C  CE1 . HIS   A 1 228 ? 20.64801  -3.83722  7.88138   1.000 12.16056 ?  240 HIS   A CE1 1 
ATOM   1643 N  NE2 . HIS   A 1 228 ? 20.24945  -4.01696  6.63227   1.000 12.88312 ?  240 HIS   A NE2 1 
ATOM   1644 N  N   . GLY   A 1 229 ? 25.08008  -8.63528  7.89900   1.000 11.69554 ?  241 GLY   A N   1 
ATOM   1645 C  CA  . GLY   A 1 229 ? 25.59343  -9.97127  8.12036   1.000 14.95798 ?  241 GLY   A CA  1 
ATOM   1646 C  C   . GLY   A 1 229 ? 26.91283  -10.26217 7.43576   1.000 14.11672 ?  241 GLY   A C   1 
ATOM   1647 O  O   . GLY   A 1 229 ? 27.70251  -9.37481  7.10915   1.000 12.92188 ?  241 GLY   A O   1 
ATOM   1648 N  N   . LEU   A 1 230 ? 27.14875  -11.55378 7.21166   1.000 14.96220 ?  242 LEU   A N   1 
ATOM   1649 C  CA  . LEU   A 1 230 ? 28.49821  -12.02141 6.93881   1.000 15.15643 ?  242 LEU   A CA  1 
ATOM   1650 C  C   . LEU   A 1 230 ? 28.88199  -11.77682 5.48444   1.000 15.57396 ?  242 LEU   A C   1 
ATOM   1651 O  O   . LEU   A 1 230 ? 28.09573  -12.06437 4.57975   1.000 14.14696 ?  242 LEU   A O   1 
ATOM   1652 C  CB  . LEU   A 1 230 ? 28.59886  -13.51437 7.21782   1.000 16.57637 ?  242 LEU   A CB  1 
ATOM   1653 C  CG  . LEU   A 1 230 ? 28.46051  -13.89296 8.68983   1.000 21.94084 ?  242 LEU   A CG  1 
ATOM   1654 C  CD1 . LEU   A 1 230 ? 28.53124  -15.40526 8.84072   1.000 26.25192 ?  242 LEU   A CD1 1 
ATOM   1655 C  CD2 . LEU   A 1 230 ? 29.51492  -13.20136 9.54322   1.000 30.02918 ?  242 LEU   A CD2 1 
ATOM   1656 N  N   . PRO   A 1 231 ? 30.09226  -11.27629 5.24584   1.000 14.03583 ?  243 PRO   A N   1 
ATOM   1657 C  CA  . PRO   A 1 231 ? 30.63414  -11.21339 3.88511   1.000 14.78653 ?  243 PRO   A CA  1 
ATOM   1658 C  C   . PRO   A 1 231 ? 30.78346  -12.59802 3.27450   1.000 15.06579 ?  243 PRO   A C   1 
ATOM   1659 O  O   . PRO   A 1 231 ? 30.84387  -13.61934 3.96482   1.000 16.34171 ?  243 PRO   A O   1 
ATOM   1660 C  CB  . PRO   A 1 231 ? 32.00889  -10.57213 4.09438   1.000 18.55947 ?  243 PRO   A CB  1 
ATOM   1661 C  CG  . PRO   A 1 231 ? 31.87407  -9.78983  5.35234   1.000 18.35170 ?  243 PRO   A CG  1 
ATOM   1662 C  CD  . PRO   A 1 231 ? 31.02092  -10.68093 6.22518   1.000 15.69075 ?  243 PRO   A CD  1 
ATOM   1663 N  N   . GLY   A 1 232 ? 30.83469  -12.61548 1.95893   1.000 15.28595 ?  244 GLY   A N   1 
ATOM   1664 C  CA  . GLY   A 1 232 ? 31.12496  -13.82255 1.20507   1.000 16.32181 ?  244 GLY   A CA  1 
ATOM   1665 C  C   . GLY   A 1 232 ? 31.71341  -13.46119 -0.13178  1.000 14.13511 ?  244 GLY   A C   1 
ATOM   1666 O  O   . GLY   A 1 232 ? 32.41553  -12.45647 -0.27941  1.000 14.06027 ?  244 GLY   A O   1 
ATOM   1667 N  N   . GLY   A 1 233 ? 31.43750  -14.30217 -1.12493  1.000 17.01339 ?  245 GLY   A N   1 
ATOM   1668 C  CA  . GLY   A 1 233 ? 31.86252  -14.06267 -2.47254  1.000 13.81728 ?  245 GLY   A CA  1 
ATOM   1669 C  C   . GLY   A 1 233 ? 30.69458  -13.68804 -3.35671  1.000 14.63584 ?  245 GLY   A C   1 
ATOM   1670 O  O   . GLY   A 1 233 ? 29.60346  -13.35016 -2.87872  1.000 14.48528 ?  245 GLY   A O   1 
ATOM   1671 N  N   . LEU   A 1 234 ? 30.91962  -13.76591 -4.66966  1.000 13.20561 ?  246 LEU   A N   1 
ATOM   1672 C  CA  . LEU   A 1 234 ? 29.85582  -13.42432 -5.60650  1.000 11.85752 ?  246 LEU   A CA  1 
ATOM   1673 C  C   . LEU   A 1 234 ? 28.66474  -14.36279 -5.49824  1.000 13.26765 ?  246 LEU   A C   1 
ATOM   1674 O  O   . LEU   A 1 234 ? 27.59089  -14.03363 -6.01949  1.000 14.14413 ?  246 LEU   A O   1 
ATOM   1675 C  CB  . LEU   A 1 234 ? 30.40158  -13.34713 -7.03813  1.000 13.53568 ?  246 LEU   A CB  1 
ATOM   1676 C  CG  . LEU   A 1 234 ? 31.18678  -12.07220 -7.37184  1.000 13.85336 ?  246 LEU   A CG  1 
ATOM   1677 C  CD1 . LEU   A 1 234 ? 32.03972  -12.26976 -8.62718  1.000 15.35506 ?  246 LEU   A CD1 1 
ATOM   1678 C  CD2 . LEU   A 1 234 ? 30.26254  -10.88998 -7.54229  1.000 14.67274 ?  246 LEU   A CD2 1 
ATOM   1679 N  N   . ASP   A 1 235 ? 28.82313  -15.50425 -4.82147  1.000 14.52634 ?  247 ASP   A N   1 
ATOM   1680 C  CA  A ASP   A 1 235 ? 27.69228  -16.38876 -4.57008  0.564 16.88101 ?  247 ASP   A CA  1 
ATOM   1681 C  CA  B ASP   A 1 235 ? 27.69380  -16.38852 -4.56291  0.436 16.88875 ?  247 ASP   A CA  1 
ATOM   1682 C  C   . ASP   A 1 235 ? 26.54750  -15.67048 -3.86640  1.000 14.19936 ?  247 ASP   A C   1 
ATOM   1683 O  O   . ASP   A 1 235 ? 25.40113  -16.10985 -3.96974  1.000 15.23400 ?  247 ASP   A O   1 
ATOM   1684 C  CB  A ASP   A 1 235 ? 28.13661  -17.59741 -3.73070  0.564 18.53731 ?  247 ASP   A CB  1 
ATOM   1685 C  CB  B ASP   A 1 235 ? 28.14247  -17.56041 -3.68742  0.436 18.51082 ?  247 ASP   A CB  1 
ATOM   1686 C  CG  A ASP   A 1 235 ? 29.02573  -17.20872 -2.55685  0.564 16.57867 ?  247 ASP   A CG  1 
ATOM   1687 C  CG  B ASP   A 1 235 ? 28.56864  -18.76285 -4.49521  0.436 19.54027 ?  247 ASP   A CG  1 
ATOM   1688 O  OD1 A ASP   A 1 235 ? 30.09653  -16.60341 -2.77094  0.564 17.28171 ?  247 ASP   A OD1 1 
ATOM   1689 O  OD1 B ASP   A 1 235 ? 28.54625  -18.69410 -5.74275  0.436 15.12021 ?  247 ASP   A OD1 1 
ATOM   1690 O  OD2 A ASP   A 1 235 ? 28.65890  -17.52555 -1.40724  0.564 23.35337 ?  247 ASP   A OD2 1 
ATOM   1691 O  OD2 B ASP   A 1 235 ? 28.92592  -19.78450 -3.87684  0.436 20.94900 ?  247 ASP   A OD2 1 
ATOM   1692 N  N   . LEU   A 1 236 ? 26.82724  -14.57204 -3.15757  1.000 12.26935 ?  248 LEU   A N   1 
ATOM   1693 C  CA  . LEU   A 1 236 ? 25.74089  -13.85688 -2.48980  1.000 11.32816 ?  248 LEU   A CA  1 
ATOM   1694 C  C   . LEU   A 1 236 ? 24.74485  -13.28801 -3.49391  1.000 10.47666 ?  248 LEU   A C   1 
ATOM   1695 O  O   . LEU   A 1 236 ? 23.57280  -13.10338 -3.16464  1.000 12.06064 ?  248 LEU   A O   1 
ATOM   1696 C  CB  . LEU   A 1 236 ? 26.29662  -12.75706 -1.59009  1.000 11.57936 ?  248 LEU   A CB  1 
ATOM   1697 C  CG  . LEU   A 1 236 ? 26.66593  -13.15635 -0.15400  1.000 13.72048 ?  248 LEU   A CG  1 
ATOM   1698 C  CD1 . LEU   A 1 236 ? 27.70361  -14.28211 -0.10682  1.000 16.57789 ?  248 LEU   A CD1 1 
ATOM   1699 C  CD2 . LEU   A 1 236 ? 27.18281  -11.92846 0.59845   1.000 12.32832 ?  248 LEU   A CD2 1 
ATOM   1700 N  N   . LEU   A 1 237 ? 25.19373  -13.01203 -4.71854  1.000 11.17221 ?  249 LEU   A N   1 
ATOM   1701 C  CA  . LEU   A 1 237 ? 24.30613  -12.39965 -5.70490  1.000 12.10833 ?  249 LEU   A CA  1 
ATOM   1702 C  C   . LEU   A 1 237 ? 23.21025  -13.37434 -6.13247  1.000 11.88942 ?  249 LEU   A C   1 
ATOM   1703 O  O   . LEU   A 1 237 ? 22.02144  -13.06371 -6.03602  1.000 12.58112 ?  249 LEU   A O   1 
ATOM   1704 C  CB  . LEU   A 1 237 ? 25.11712  -11.89898 -6.89834  1.000 12.18622 ?  249 LEU   A CB  1 
ATOM   1705 C  CG  . LEU   A 1 237 ? 25.70285  -10.48036 -6.81548  1.000 13.03998 ?  249 LEU   A CG  1 
ATOM   1706 C  CD1 . LEU   A 1 237 ? 26.64146  -10.32355 -5.63840  1.000 13.83707 ?  249 LEU   A CD1 1 
ATOM   1707 C  CD2 . LEU   A 1 237 ? 26.43061  -10.14526 -8.09990  1.000 15.88725 ?  249 LEU   A CD2 1 
ATOM   1708 N  N   . LYS   A 1 238 ? 23.59341  -14.58269 -6.55460  1.000 12.83274 ?  250 LYS   A N   1 
ATOM   1709 C  CA  . LYS   A 1 238 ? 22.59603  -15.55459 -6.97734  1.000 14.60492 ?  250 LYS   A CA  1 
ATOM   1710 C  C   . LYS   A 1 238 ? 21.74034  -16.00890 -5.80371  1.000 13.35510 ?  250 LYS   A C   1 
ATOM   1711 O  O   . LYS   A 1 238 ? 20.54821  -16.27406 -5.97260  1.000 14.04579 ?  250 LYS   A O   1 
ATOM   1712 C  CB  . LYS   A 1 238 ? 23.28900  -16.74856 -7.63693  1.000 16.84764 ?  250 LYS   A CB  1 
ATOM   1713 C  CG  . LYS   A 1 238 ? 23.40892  -16.59860 -9.14528  1.000 24.88909 ?  250 LYS   A CG  1 
ATOM   1714 C  CD  . LYS   A 1 238 ? 24.37907  -17.61664 -9.73584  1.000 31.56020 ?  250 LYS   A CD  1 
ATOM   1715 C  CE  . LYS   A 1 238 ? 24.52126  -17.44938 -11.24289 1.000 34.19621 ?  250 LYS   A CE  1 
ATOM   1716 N  NZ  . LYS   A 1 238 ? 25.09684  -16.12263 -11.58871 1.000 34.93819 ?  250 LYS   A NZ  1 
ATOM   1717 N  N   . HIS   A 1 239 ? 22.32514  -16.07503 -4.60227  1.000 13.12805 ?  251 HIS   A N   1 
ATOM   1718 C  CA  . HIS   A 1 239 ? 21.53284  -16.36540 -3.41874  1.000 10.40087 ?  251 HIS   A CA  1 
ATOM   1719 C  C   . HIS   A 1 239 ? 20.43857  -15.31474 -3.24187  1.000 11.25526 ?  251 HIS   A C   1 
ATOM   1720 O  O   . HIS   A 1 239 ? 19.28444  -15.64920 -2.94816  1.000 12.59902 ?  251 HIS   A O   1 
ATOM   1721 C  CB  . HIS   A 1 239 ? 22.43636  -16.38237 -2.18070  1.000 9.41090  ?  251 HIS   A CB  1 
ATOM   1722 C  CG  . HIS   A 1 239 ? 21.67130  -16.21991 -0.91314  1.000 9.94855  ?  251 HIS   A CG  1 
ATOM   1723 N  ND1 . HIS   A 1 239 ? 20.85125  -17.20248 -0.40865  1.000 9.76228  ?  251 HIS   A ND1 1 
ATOM   1724 C  CD2 . HIS   A 1 239 ? 21.56439  -15.17521 -0.06197  1.000 12.62907 ?  251 HIS   A CD2 1 
ATOM   1725 C  CE1 . HIS   A 1 239 ? 20.26478  -16.77556 0.69166   1.000 12.00249 ?  251 HIS   A CE1 1 
ATOM   1726 N  NE2 . HIS   A 1 239 ? 20.68111  -15.54121 0.92315   1.000 12.93633 ?  251 HIS   A NE2 1 
ATOM   1727 N  N   . THR   A 1 240 ? 20.78613  -14.03019 -3.40676  1.000 11.55737 ?  252 THR   A N   1 
ATOM   1728 C  CA  . THR   A 1 240 ? 19.78813  -12.98635 -3.22815  1.000 11.46836 ?  252 THR   A CA  1 
ATOM   1729 C  C   . THR   A 1 240 ? 18.69064  -13.10324 -4.27862  1.000 11.67636 ?  252 THR   A C   1 
ATOM   1730 O  O   . THR   A 1 240 ? 17.50209  -12.98032 -3.96260  1.000 10.14406 ?  252 THR   A O   1 
ATOM   1731 C  CB  . THR   A 1 240 ? 20.45967  -11.61131 -3.27012  1.000 10.96375 ?  252 THR   A CB  1 
ATOM   1732 O  OG1 . THR   A 1 240 ? 21.47868  -11.55166 -2.25446  1.000 10.71749 ?  252 THR   A OG1 1 
ATOM   1733 C  CG2 . THR   A 1 240 ? 19.42374  -10.53437 -2.98251  1.000 11.32197 ?  252 THR   A CG2 1 
ATOM   1734 N  N   . THR   A 1 241 ? 19.07328  -13.36072 -5.53074  1.000 11.05468 ?  253 THR   A N   1 
ATOM   1735 C  CA  . THR   A 1 241 ? 18.07687  -13.58502 -6.57463  1.000 10.40849 ?  253 THR   A CA  1 
ATOM   1736 C  C   . THR   A 1 241 ? 17.14193  -14.73907 -6.23113  1.000 11.84390 ?  253 THR   A C   1 
ATOM   1737 O  O   . THR   A 1 241 ? 15.92654  -14.62632 -6.42433  1.000 12.20619 ?  253 THR   A O   1 
ATOM   1738 C  CB  . THR   A 1 241 ? 18.77862  -13.80388 -7.90650  1.000 11.71071 ?  253 THR   A CB  1 
ATOM   1739 O  OG1 . THR   A 1 241 ? 19.40923  -12.56743 -8.28184  1.000 14.71784 ?  253 THR   A OG1 1 
ATOM   1740 C  CG2 . THR   A 1 241 ? 17.76550  -14.17134 -8.98619  1.000 13.34987 ?  253 THR   A CG2 1 
ATOM   1741 N  N   . ASN   A 1 242 ? 17.68232  -15.84531 -5.70873  1.000 11.47241 ?  254 ASN   A N   1 
ATOM   1742 C  CA  A ASN   A 1 242 ? 16.83010  -16.96588 -5.32243  0.570 14.59562 ?  254 ASN   A CA  1 
ATOM   1743 C  CA  B ASN   A 1 242 ? 16.82676  -16.96648 -5.32449  0.430 14.58508 ?  254 ASN   A CA  1 
ATOM   1744 C  C   . ASN   A 1 242 ? 15.81686  -16.54989 -4.26185  1.000 13.55663 ?  254 ASN   A C   1 
ATOM   1745 O  O   . ASN   A 1 242 ? 14.63020  -16.86260 -4.36596  1.000 14.38683 ?  254 ASN   A O   1 
ATOM   1746 C  CB  A ASN   A 1 242 ? 17.69774  -18.11372 -4.82423  0.570 13.31222 ?  254 ASN   A CB  1 
ATOM   1747 C  CB  B ASN   A 1 242 ? 17.66673  -18.14585 -4.83883  0.430 13.36916 ?  254 ASN   A CB  1 
ATOM   1748 C  CG  A ASN   A 1 242 ? 18.41756  -18.82402 -5.94677  0.570 15.06264 ?  254 ASN   A CG  1 
ATOM   1749 C  CG  B ASN   A 1 242 ? 16.81583  -19.36530 -4.50147  0.430 13.71325 ?  254 ASN   A CG  1 
ATOM   1750 O  OD1 A ASN   A 1 242 ? 18.12986  -18.60945 -7.12746  0.570 16.61202 ?  254 ASN   A OD1 1 
ATOM   1751 O  OD1 B ASN   A 1 242 ? 16.30068  -20.04165 -5.39111  0.430 24.71417 ?  254 ASN   A OD1 1 
ATOM   1752 N  ND2 A ASN   A 1 242 ? 19.38706  -19.64549 -5.59002  0.570 18.04343 ?  254 ASN   A ND2 1 
ATOM   1753 N  ND2 B ASN   A 1 242 ? 16.64104  -19.62954 -3.21166  0.430 20.01167 ?  254 ASN   A ND2 1 
ATOM   1754 N  N   . VAL   A 1 243 ? 16.27357  -15.83505 -3.22662  1.000 12.21389 ?  255 VAL   A N   1 
ATOM   1755 C  CA  . VAL   A 1 243 ? 15.37053  -15.37949 -2.16689  1.000 12.00186 ?  255 VAL   A CA  1 
ATOM   1756 C  C   . VAL   A 1 243 ? 14.28946  -14.45215 -2.72955  1.000 12.13788 ?  255 VAL   A C   1 
ATOM   1757 O  O   . VAL   A 1 243 ? 13.10777  -14.56236 -2.38412  1.000 13.22534 ?  255 VAL   A O   1 
ATOM   1758 C  CB  . VAL   A 1 243 ? 16.19122  -14.70847 -1.04952  1.000 11.79540 ?  255 VAL   A CB  1 
ATOM   1759 C  CG1 . VAL   A 1 243 ? 15.28691  -14.03034 -0.02603  1.000 15.00177 ?  255 VAL   A CG1 1 
ATOM   1760 C  CG2 . VAL   A 1 243 ? 17.10760  -15.73899 -0.37208  1.000 13.83021 ?  255 VAL   A CG2 1 
ATOM   1761 N  N   . VAL   A 1 244 ? 14.68828  -13.50280 -3.58293  1.000 11.51939 ?  256 VAL   A N   1 
ATOM   1762 C  CA  . VAL   A 1 244 ? 13.73938  -12.54255 -4.14159  1.000 12.81742 ?  256 VAL   A CA  1 
ATOM   1763 C  C   . VAL   A 1 244 ? 12.70183  -13.24836 -5.00464  1.000 12.51334 ?  256 VAL   A C   1 
ATOM   1764 O  O   . VAL   A 1 244 ? 11.50593  -12.94756 -4.93014  1.000 12.28172 ?  256 VAL   A O   1 
ATOM   1765 C  CB  . VAL   A 1 244 ? 14.51020  -11.46704 -4.93529  1.000 15.09870 ?  256 VAL   A CB  1 
ATOM   1766 C  CG1 . VAL   A 1 244 ? 13.55214  -10.64760 -5.80261  1.000 18.58716 ?  256 VAL   A CG1 1 
ATOM   1767 C  CG2 . VAL   A 1 244 ? 15.29706  -10.55131 -3.98657  1.000 15.26003 ?  256 VAL   A CG2 1 
ATOM   1768 N  N   . LYS   A 1 245 ? 13.14823  -14.18205 -5.84489  1.000 12.08708 ?  257 LYS   A N   1 
ATOM   1769 C  CA  . LYS   A 1 245 ? 12.21977  -14.90305 -6.71291  1.000 12.31943 ?  257 LYS   A CA  1 
ATOM   1770 C  C   . LYS   A 1 245 ? 11.27328  -15.77707 -5.90142  1.000 12.21881 ?  257 LYS   A C   1 
ATOM   1771 O  O   . LYS   A 1 245 ? 10.07326  -15.83960 -6.20059  1.000 13.94944 ?  257 LYS   A O   1 
ATOM   1772 C  CB  . LYS   A 1 245 ? 13.00596  -15.70542 -7.75176  1.000 12.70035 ?  257 LYS   A CB  1 
ATOM   1773 C  CG  . LYS   A 1 245 ? 13.55521  -14.85474 -8.88171  1.000 14.43013 ?  257 LYS   A CG  1 
ATOM   1774 C  CD  . LYS   A 1 245 ? 14.23523  -15.72515 -9.92455  1.000 16.46023 ?  257 LYS   A CD  1 
ATOM   1775 C  CE  . LYS   A 1 245 ? 14.78912  -14.90686 -11.06390 1.000 20.27004 ?  257 LYS   A CE  1 
ATOM   1776 N  NZ  . LYS   A 1 245 ? 14.95256  -15.74357 -12.29628 1.000 25.27245 ?  257 LYS   A NZ  1 
ATOM   1777 N  N   . ALA   A 1 246 ? 11.78724  -16.44945 -4.86839  1.000 13.36654 ?  258 ALA   A N   1 
ATOM   1778 C  CA  . ALA   A 1 246 ? 10.90359  -17.21916 -3.99709  1.000 13.34599 ?  258 ALA   A CA  1 
ATOM   1779 C  C   . ALA   A 1 246 ? 9.84996   -16.32300 -3.36058  1.000 15.41455 ?  258 ALA   A C   1 
ATOM   1780 O  O   . ALA   A 1 246 ? 8.66355   -16.67176 -3.32033  1.000 15.75563 ?  258 ALA   A O   1 
ATOM   1781 C  CB  . ALA   A 1 246 ? 11.73219  -17.95306 -2.93782  1.000 15.49792 ?  258 ALA   A CB  1 
ATOM   1782 N  N   . HIS   A 1 247 ? 10.25507  -15.14243 -2.89496  1.000 13.44904 ?  259 HIS   A N   1 
ATOM   1783 C  CA  . HIS   A 1 247 ? 9.29678   -14.21131 -2.32549  1.000 13.61252 ?  259 HIS   A CA  1 
ATOM   1784 C  C   . HIS   A 1 247 ? 8.28042   -13.75295 -3.36159  1.000 15.34496 ?  259 HIS   A C   1 
ATOM   1785 O  O   . HIS   A 1 247 ? 7.09539   -13.59994 -3.05243  1.000 16.50353 ?  259 HIS   A O   1 
ATOM   1786 C  CB  . HIS   A 1 247 ? 10.02655  -12.99433 -1.75364  1.000 17.06187 ?  259 HIS   A CB  1 
ATOM   1787 C  CG  . HIS   A 1 247 ? 9.09859   -11.99140 -1.15435  1.000 16.82351 ?  259 HIS   A CG  1 
ATOM   1788 N  ND1 . HIS   A 1 247 ? 8.52676   -12.15825 0.08943   1.000 23.73771 ?  259 HIS   A ND1 1 
ATOM   1789 C  CD2 . HIS   A 1 247 ? 8.59122   -10.84016 -1.65136  1.000 22.23158 ?  259 HIS   A CD2 1 
ATOM   1790 C  CE1 . HIS   A 1 247 ? 7.73232   -11.13463 0.34342   1.000 21.81269 ?  259 HIS   A CE1 1 
ATOM   1791 N  NE2 . HIS   A 1 247 ? 7.74580   -10.32669 -0.69922  1.000 21.43469 ?  259 HIS   A NE2 1 
ATOM   1792 N  N   . THR   A 1 248 ? 8.72874   -13.47235 -4.58030  1.000 13.08825 ?  260 THR   A N   1 
ATOM   1793 C  CA  A THR   A 1 248 ? 7.82696   -13.06145 -5.65315  0.862 13.58292 ?  260 THR   A CA  1 
ATOM   1794 C  CA  B THR   A 1 248 ? 7.74028   -13.00947 -5.54191  0.138 13.83654 ?  260 THR   A CA  1 
ATOM   1795 C  C   . THR   A 1 248 ? 6.72255   -14.08933 -5.87028  1.000 18.28559 ?  260 THR   A C   1 
ATOM   1796 O  O   . THR   A 1 248 ? 5.55665   -13.74703 -6.10354  1.000 18.61597 ?  260 THR   A O   1 
ATOM   1797 C  CB  A THR   A 1 248 ? 8.67841   -12.90288 -6.91554  0.862 12.48081 ?  260 THR   A CB  1 
ATOM   1798 C  CB  B THR   A 1 248 ? 8.33416   -12.34318 -6.78745  0.138 15.06582 ?  260 THR   A CB  1 
ATOM   1799 O  OG1 A THR   A 1 248 ? 9.56997   -11.78456 -6.75701  0.862 15.95691 ?  260 THR   A OG1 1 
ATOM   1800 O  OG1 B THR   A 1 248 ? 7.28910   -12.12550 -7.74508  0.138 17.35780 ?  260 THR   A OG1 1 
ATOM   1801 C  CG2 A THR   A 1 248 ? 7.82514   -12.70534 -8.15076  0.862 15.10536 ?  260 THR   A CG2 1 
ATOM   1802 C  CG2 B THR   A 1 248 ? 9.36253   -13.20187 -7.42256  0.138 13.42239 ?  260 THR   A CG2 1 
ATOM   1803 N  N   . ASN   A 1 249 ? 7.09286   -15.36839 -5.81774  1.000 16.09485 ?  261 ASN   A N   1 
ATOM   1804 C  CA  . ASN   A 1 249 ? 6.13247   -16.44126 -6.06158  1.000 15.32507 ?  261 ASN   A CA  1 
ATOM   1805 C  C   . ASN   A 1 249 ? 5.33320   -16.83853 -4.82395  1.000 22.59630 ?  261 ASN   A C   1 
ATOM   1806 O  O   . ASN   A 1 249 ? 4.48002   -17.72720 -4.92318  1.000 25.89026 ?  261 ASN   A O   1 
ATOM   1807 C  CB  . ASN   A 1 249 ? 6.83555   -17.65030 -6.67896  1.000 16.06369 ?  261 ASN   A CB  1 
ATOM   1808 C  CG  . ASN   A 1 249 ? 7.21175   -17.42170 -8.12619  1.000 16.27615 ?  261 ASN   A CG  1 
ATOM   1809 O  OD1 . ASN   A 1 249 ? 6.77515   -16.44936 -8.73587  1.000 21.05382 ?  261 ASN   A OD1 1 
ATOM   1810 N  ND2 . ASN   A 1 249 ? 8.00598   -18.31085 -8.68512  1.000 18.33132 ?  261 ASN   A ND2 1 
ATOM   1811 N  N   . ARG   A 1 250 ? 5.56573   -16.20066 -3.67900  1.000 18.41497 ?  262 ARG   A N   1 
ATOM   1812 C  CA  . ARG   A 1 250 ? 4.80669   -16.47918 -2.45455  1.000 24.16012 ?  262 ARG   A CA  1 
ATOM   1813 C  C   . ARG   A 1 250 ? 3.29645   -16.45368 -2.68862  1.000 33.66697 ?  262 ARG   A C   1 
ATOM   1814 O  O   . ARG   A 1 250 ? 2.56550   -17.27978 -2.13974  1.000 42.92632 ?  262 ARG   A O   1 
ATOM   1815 C  CB  . ARG   A 1 250 ? 5.15876   -15.45242 -1.37444  1.000 28.72770 ?  262 ARG   A CB  1 
ATOM   1816 C  CG  . ARG   A 1 250 ? 4.39336   -14.13385 -1.51229  1.000 27.16277 ?  262 ARG   A CG  1 
ATOM   1817 C  CD  . ARG   A 1 250 ? 5.06168   -12.99002 -0.75390  1.000 20.57937 ?  262 ARG   A CD  1 
ATOM   1818 N  NE  . ARG   A 1 250 ? 4.38505   -11.71657 -0.97711  1.000 28.72884 ?  262 ARG   A NE  1 
ATOM   1819 C  CZ  . ARG   A 1 250 ? 4.50640   -10.98065 -2.07428  1.000 31.87627 ?  262 ARG   A CZ  1 
ATOM   1820 N  NH1 . ARG   A 1 250 ? 5.31670   -11.33597 -3.05935  1.000 23.12073 ?  262 ARG   A NH1 1 
ATOM   1821 N  NH2 . ARG   A 1 250 ? 3.80334   -9.85465  -2.18318  1.000 24.88629 ?  262 ARG   A NH2 1 
ATOM   1822 N  N   . GLU   B 1 20  ? -8.63088  34.22203  16.97743  1.000 36.45814 ?  32  GLU   B N   1 
ATOM   1823 C  CA  . GLU   B 1 20  ? -9.14668  33.00752  16.35029  1.000 36.81461 ?  32  GLU   B CA  1 
ATOM   1824 C  C   . GLU   B 1 20  ? -8.94695  31.75890  17.21284  1.000 33.94708 ?  32  GLU   B C   1 
ATOM   1825 O  O   . GLU   B 1 20  ? -9.72602  30.80687  17.12538  1.000 24.27378 ?  32  GLU   B O   1 
ATOM   1826 C  CB  . GLU   B 1 20  ? -8.53469  32.81068  14.95763  1.000 43.56847 ?  32  GLU   B CB  1 
ATOM   1827 C  CG  . GLU   B 1 20  ? -7.02271  32.63531  14.95230  1.000 41.36642 ?  32  GLU   B CG  1 
ATOM   1828 C  CD  . GLU   B 1 20  ? -6.42556  32.74950  13.55873  1.000 57.05031 ?  32  GLU   B CD  1 
ATOM   1829 O  OE1 . GLU   B 1 20  ? -6.98603  33.49343  12.72318  1.000 58.42895 ?  32  GLU   B OE1 1 
ATOM   1830 O  OE2 . GLU   B 1 20  ? -5.38485  32.10471  13.30186  1.000 61.63723 ?  32  GLU   B OE2 1 
ATOM   1831 N  N   . TYR   B 1 21  ? -7.90754  31.76093  18.04441  1.000 26.59002 ?  33  TYR   B N   1 
ATOM   1832 C  CA  . TYR   B 1 21  ? -7.67022  30.61947  18.92049  1.000 26.08494 ?  33  TYR   B CA  1 
ATOM   1833 C  C   . TYR   B 1 21  ? -8.78635  30.50656  19.95053  1.000 24.94337 ?  33  TYR   B C   1 
ATOM   1834 O  O   . TYR   B 1 21  ? -9.14430  31.50580  20.58137  1.000 29.56269 ?  33  TYR   B O   1 
ATOM   1835 C  CB  . TYR   B 1 21  ? -6.33508  30.74459  19.64913  1.000 22.36538 ?  33  TYR   B CB  1 
ATOM   1836 C  CG  . TYR   B 1 21  ? -5.79232  29.39599  20.06655  1.000 18.81643 ?  33  TYR   B CG  1 
ATOM   1837 C  CD1 . TYR   B 1 21  ? -5.22285  28.54504  19.13465  1.000 19.29466 ?  33  TYR   B CD1 1 
ATOM   1838 C  CD2 . TYR   B 1 21  ? -5.87781  28.96833  21.38489  1.000 21.89019 ?  33  TYR   B CD2 1 
ATOM   1839 C  CE1 . TYR   B 1 21  ? -4.73603  27.30203  19.50127  1.000 23.23795 ?  33  TYR   B CE1 1 
ATOM   1840 C  CE2 . TYR   B 1 21  ? -5.38819  27.72502  21.76603  1.000 15.00597 ?  33  TYR   B CE2 1 
ATOM   1841 C  CZ  . TYR   B 1 21  ? -4.82229  26.90416  20.81600  1.000 16.22525 ?  33  TYR   B CZ  1 
ATOM   1842 O  OH  . TYR   B 1 21  ? -4.34449  25.66624  21.19145  1.000 16.37036 ?  33  TYR   B OH  1 
ATOM   1843 N  N   . PRO   B 1 22  ? -9.32972  29.31403  20.17498  1.000 22.71726 ?  34  PRO   B N   1 
ATOM   1844 C  CA  . PRO   B 1 22  ? -10.43311 29.17141  21.13299  1.000 27.46042 ?  34  PRO   B CA  1 
ATOM   1845 C  C   . PRO   B 1 22  ? -9.97369  29.43125  22.55989  1.000 33.22796 ?  34  PRO   B C   1 
ATOM   1846 O  O   . PRO   B 1 22  ? -8.88953  29.00800  22.97128  1.000 29.32838 ?  34  PRO   B O   1 
ATOM   1847 C  CB  . PRO   B 1 22  ? -10.86692 27.71029  20.95727  1.000 25.19350 ?  34  PRO   B CB  1 
ATOM   1848 C  CG  . PRO   B 1 22  ? -10.29640 27.28433  19.63280  1.000 31.52199 ?  34  PRO   B CG  1 
ATOM   1849 C  CD  . PRO   B 1 22  ? -9.02605  28.05427  19.47799  1.000 21.93055 ?  34  PRO   B CD  1 
ATOM   1850 N  N   . THR   B 1 23  ? -10.82125 30.12387  23.31625  1.000 33.91025 ?  35  THR   B N   1 
ATOM   1851 C  CA  . THR   B 1 23  ? -10.58037 30.46277  24.71364  1.000 28.28219 ?  35  THR   B CA  1 
ATOM   1852 C  C   . THR   B 1 23  ? -11.63117 29.79706  25.60190  1.000 32.20030 ?  35  THR   B C   1 
ATOM   1853 O  O   . THR   B 1 23  ? -12.56674 29.15551  25.12037  1.000 31.18971 ?  35  THR   B O   1 
ATOM   1854 C  CB  . THR   B 1 23  ? -10.54503 31.98381  24.90645  1.000 35.39392 ?  35  THR   B CB  1 
ATOM   1855 O  OG1 . THR   B 1 23  ? -11.88181 32.49832  24.90012  1.000 41.80022 ?  35  THR   B OG1 1 
ATOM   1856 C  CG2 . THR   B 1 23  ? -9.73427  32.64869  23.80209  1.000 34.38183 ?  35  THR   B CG2 1 
ATOM   1857 N  N   . VAL   B 1 24  ? -11.46013 29.95684  26.91986  1.000 37.87297 ?  36  VAL   B N   1 
ATOM   1858 C  CA  . VAL   B 1 24  ? -12.32859 29.28525  27.89130  1.000 34.67410 ?  36  VAL   B CA  1 
ATOM   1859 C  C   . VAL   B 1 24  ? -13.79647 29.59892  27.63881  1.000 42.57896 ?  36  VAL   B C   1 
ATOM   1860 O  O   . VAL   B 1 24  ? -14.63239 28.69308  27.53365  1.000 47.14733 ?  36  VAL   B O   1 
ATOM   1861 C  CB  . VAL   B 1 24  ? -11.92500 29.65053  29.32997  1.000 38.01486 ?  36  VAL   B CB  1 
ATOM   1862 C  CG1 . VAL   B 1 24  ? -12.95868 29.11543  30.30250  1.000 38.02105 ?  36  VAL   B CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 24  ? -10.58901 29.07273  29.65577  1.000 28.91765 ?  36  VAL   B CG2 1 
ATOM   1864 N  N   . SER   B 1 25  ? -14.13652 30.88964  27.55949  1.000 44.31552 ?  37  SER   B N   1 
ATOM   1865 C  CA  . SER   B 1 25  ? -15.53740 31.29711  27.49445  1.000 50.81968 ?  37  SER   B CA  1 
ATOM   1866 C  C   . SER   B 1 25  ? -16.26203 30.76492  26.26852  1.000 50.11421 ?  37  SER   B C   1 
ATOM   1867 O  O   . SER   B 1 25  ? -17.49328 30.86521  26.20537  1.000 57.22455 ?  37  SER   B O   1 
ATOM   1868 C  CB  . SER   B 1 25  ? -15.65641 32.81980  27.53046  1.000 53.69220 ?  37  SER   B CB  1 
ATOM   1869 O  OG  . SER   B 1 25  ? -15.37636 33.31287  28.82529  1.000 60.34854 ?  37  SER   B OG  1 
ATOM   1870 N  N   . GLU   B 1 26  ? -15.54122 30.21194  25.29836  1.000 43.46845 ?  38  GLU   B N   1 
ATOM   1871 C  CA  . GLU   B 1 26  ? -16.15120 29.66068  24.10229  1.000 38.92480 ?  38  GLU   B CA  1 
ATOM   1872 C  C   . GLU   B 1 26  ? -16.18053 28.13942  24.09058  1.000 39.43277 ?  38  GLU   B C   1 
ATOM   1873 O  O   . GLU   B 1 26  ? -16.65174 27.55203  23.11188  1.000 38.66425 ?  38  GLU   B O   1 
ATOM   1874 C  CB  . GLU   B 1 26  ? -15.45170 30.20582  22.85210  1.000 43.06811 ?  38  GLU   B CB  1 
ATOM   1875 C  CG  . GLU   B 1 26  ? -14.89024 31.61643  23.02796  1.000 50.32691 ?  38  GLU   B CG  1 
ATOM   1876 C  CD  . GLU   B 1 26  ? -13.77748 31.93798  22.04361  1.000 52.88145 ?  38  GLU   B CD  1 
ATOM   1877 O  OE1 . GLU   B 1 26  ? -12.67219 31.36933  22.17371  1.000 51.60618 ?  38  GLU   B OE1 1 
ATOM   1878 O  OE2 . GLU   B 1 26  ? -14.01122 32.76352  21.13624  1.000 56.36752 ?  38  GLU   B OE2 1 
ATOM   1879 N  N   . ILE   B 1 27  ? -15.70397 27.48534  25.14739  1.000 32.05214 ?  39  ILE   B N   1 
ATOM   1880 C  CA  . ILE   B 1 27  ? -15.70746 26.02492  25.20721  1.000 32.01603 ?  39  ILE   B CA  1 
ATOM   1881 C  C   . ILE   B 1 27  ? -16.39523 25.55542  26.48319  1.000 35.28963 ?  39  ILE   B C   1 
ATOM   1882 O  O   . ILE   B 1 27  ? -15.76757 25.53819  27.55295  1.000 33.15560 ?  39  ILE   B O   1 
ATOM   1883 C  CB  . ILE   B 1 27  ? -14.28637 25.44065  25.11641  1.000 25.58437 ?  39  ILE   B CB  1 
ATOM   1884 C  CG1 . ILE   B 1 27  ? -13.51588 26.06144  23.95416  1.000 31.55641 ?  39  ILE   B CG1 1 
ATOM   1885 C  CG2 . ILE   B 1 27  ? -14.35377 23.93679  24.93494  1.000 24.62610 ?  39  ILE   B CG2 1 
ATOM   1886 C  CD1 . ILE   B 1 27  ? -12.03341 25.74186  23.97402  1.000 25.14857 ?  39  ILE   B CD1 1 
ATOM   1887 N  N   . PRO   B 1 28  ? -17.66638 25.16626  26.42262  1.000 31.16421 ?  40  PRO   B N   1 
ATOM   1888 C  CA  . PRO   B 1 28  ? -18.29728 24.54053  27.58917  1.000 36.77751 ?  40  PRO   B CA  1 
ATOM   1889 C  C   . PRO   B 1 28  ? -17.53774 23.28262  27.97751  1.000 35.68232 ?  40  PRO   B C   1 
ATOM   1890 O  O   . PRO   B 1 28  ? -17.04594 22.54607  27.11971  1.000 28.81553 ?  40  PRO   B O   1 
ATOM   1891 C  CB  . PRO   B 1 28  ? -19.70142 24.20080  27.07828  1.000 39.34911 ?  40  PRO   B CB  1 
ATOM   1892 C  CG  . PRO   B 1 28  ? -19.95847 25.25152  26.03466  1.000 39.85266 ?  40  PRO   B CG  1 
ATOM   1893 C  CD  . PRO   B 1 28  ? -18.63017 25.37193  25.32671  1.000 32.87897 ?  40  PRO   B CD  1 
ATOM   1894 N  N   . VAL   B 1 29  ? -17.42585 23.04991  29.28762  1.000 36.12599 ?  41  VAL   B N   1 
ATOM   1895 C  CA  . VAL   B 1 29  ? -16.74339 21.85262  29.76054  1.000 32.12600 ?  41  VAL   B CA  1 
ATOM   1896 C  C   . VAL   B 1 29  ? -17.45292 20.62274  29.21369  1.000 33.12618 ?  41  VAL   B C   1 
ATOM   1897 O  O   . VAL   B 1 29  ? -18.68227 20.50408  29.29226  1.000 29.74342 ?  41  VAL   B O   1 
ATOM   1898 C  CB  . VAL   B 1 29  ? -16.65431 21.85078  31.29421  1.000 31.77744 ?  41  VAL   B CB  1 
ATOM   1899 C  CG1 . VAL   B 1 29  ? -16.06565 20.54401  31.78631  1.000 27.19696 ?  41  VAL   B CG1 1 
ATOM   1900 C  CG2 . VAL   B 1 29  ? -15.81109 23.01857  31.77297  1.000 29.61643 ?  41  VAL   B CG2 1 
ATOM   1901 N  N   . GLY   B 1 30  ? -16.67717 19.70742  28.63539  1.000 26.70017 ?  42  GLY   B N   1 
ATOM   1902 C  CA  . GLY   B 1 30  ? -17.19555 18.56889  27.91071  1.000 30.74639 ?  42  GLY   B CA  1 
ATOM   1903 C  C   . GLY   B 1 30  ? -17.05430 18.68415  26.40721  1.000 25.57549 ?  42  GLY   B C   1 
ATOM   1904 O  O   . GLY   B 1 30  ? -17.15921 17.66728  25.70993  1.000 31.58981 ?  42  GLY   B O   1 
ATOM   1905 N  N   . GLU   B 1 31  ? -16.83135 19.89028  25.89097  1.000 26.66567 ?  43  GLU   B N   1 
ATOM   1906 C  CA  A GLU   B 1 31  ? -16.63264 20.11124  24.46694  0.672 25.84298 ?  43  GLU   B CA  1 
ATOM   1907 C  CA  B GLU   B 1 31  ? -16.63077 20.13079  24.47078  0.328 25.96751 ?  43  GLU   B CA  1 
ATOM   1908 C  C   . GLU   B 1 31  ? -15.14393 20.26115  24.16253  1.000 26.70828 ?  43  GLU   B C   1 
ATOM   1909 O  O   . GLU   B 1 31  ? -14.34201 20.62592  25.02613  1.000 23.54208 ?  43  GLU   B O   1 
ATOM   1910 C  CB  A GLU   B 1 31  ? -17.39009 21.35631  23.99304  0.672 30.13076 ?  43  GLU   B CB  1 
ATOM   1911 C  CB  B GLU   B 1 31  ? -17.36157 21.40484  24.03761  0.328 30.15244 ?  43  GLU   B CB  1 
ATOM   1912 C  CG  A GLU   B 1 31  ? -18.91279 21.22808  24.05975  0.672 31.74452 ?  43  GLU   B CG  1 
ATOM   1913 C  CG  B GLU   B 1 31  ? -18.36259 21.19355  22.91516  0.328 33.92232 ?  43  GLU   B CG  1 
ATOM   1914 C  CD  A GLU   B 1 31  ? -19.63596 22.37701  23.36689  0.672 32.91699 ?  43  GLU   B CD  1 
ATOM   1915 C  CD  B GLU   B 1 31  ? -19.75279 21.68566  23.26586  0.328 31.92975 ?  43  GLU   B CD  1 
ATOM   1916 O  OE1 A GLU   B 1 31  ? -19.21612 22.76428  22.25445  0.672 33.45413 ?  43  GLU   B OE1 1 
ATOM   1917 O  OE1 B GLU   B 1 31  ? -19.88166 22.82749  23.75516  0.328 33.77446 ?  43  GLU   B OE1 1 
ATOM   1918 O  OE2 A GLU   B 1 31  ? -20.62427 22.89463  23.93459  0.672 28.98357 ?  43  GLU   B OE2 1 
ATOM   1919 O  OE2 B GLU   B 1 31  ? -20.72093 20.92475  23.05788  0.328 32.29814 ?  43  GLU   B OE2 1 
ATOM   1920 N  N   . VAL   B 1 32  ? -14.78257 19.96297  22.91655  1.000 22.42996 ?  44  VAL   B N   1 
ATOM   1921 C  CA  . VAL   B 1 32  ? -13.40051 20.04888  22.45453  1.000 20.16517 ?  44  VAL   B CA  1 
ATOM   1922 C  C   . VAL   B 1 32  ? -13.37394 20.80122  21.13667  1.000 20.57966 ?  44  VAL   B C   1 
ATOM   1923 O  O   . VAL   B 1 32  ? -14.19684 20.54599  20.24750  1.000 20.96670 ?  44  VAL   B O   1 
ATOM   1924 C  CB  . VAL   B 1 32  ? -12.76796 18.65360  22.27329  1.000 15.68994 ?  44  VAL   B CB  1 
ATOM   1925 C  CG1 . VAL   B 1 32  ? -11.36641 18.76856  21.60803  1.000 16.38221 ?  44  VAL   B CG1 1 
ATOM   1926 C  CG2 . VAL   B 1 32  ? -12.68921 17.92839  23.58750  1.000 19.43471 ?  44  VAL   B CG2 1 
ATOM   1927 N  N   . ARG   B 1 33  ? -12.42283 21.71777  21.00267  1.000 17.17555 ?  45  ARG   B N   1 
ATOM   1928 C  CA  . ARG   B 1 33  ? -12.18977 22.42012  19.75520  1.000 15.97109 ?  45  ARG   B CA  1 
ATOM   1929 C  C   . ARG   B 1 33  ? -10.85828 21.98794  19.17034  1.000 15.76957 ?  45  ARG   B C   1 
ATOM   1930 O  O   . ARG   B 1 33  ? -9.92038  21.64709  19.90125  1.000 15.67860 ?  45  ARG   B O   1 
ATOM   1931 C  CB  . ARG   B 1 33  ? -12.13063 23.93060  19.96141  1.000 19.31911 ?  45  ARG   B CB  1 
ATOM   1932 C  CG  . ARG   B 1 33  ? -13.32589 24.48608  20.69024  1.000 29.18303 ?  45  ARG   B CG  1 
ATOM   1933 C  CD  . ARG   B 1 33  ? -14.39549 24.95121  19.71569  1.000 32.20445 ?  45  ARG   B CD  1 
ATOM   1934 N  NE  . ARG   B 1 33  ? -15.51081 25.55282  20.42964  1.000 39.09276 ?  45  ARG   B NE  1 
ATOM   1935 C  CZ  . ARG   B 1 33  ? -16.56712 24.88781  20.87856  1.000 38.36428 ?  45  ARG   B CZ  1 
ATOM   1936 N  NH1 . ARG   B 1 33  ? -16.72651 23.59421  20.64147  1.000 31.40428 ?  45  ARG   B NH1 1 
ATOM   1937 N  NH2 . ARG   B 1 33  ? -17.48616 25.53684  21.59006  1.000 36.29935 ?  45  ARG   B NH2 1 
ATOM   1938 N  N   . LEU   B 1 34  ? -10.78451 21.99313  17.84863  1.000 16.17806 ?  46  LEU   B N   1 
ATOM   1939 C  CA  . LEU   B 1 34  ? -9.53150  21.81042  17.14105  1.000 15.68278 ?  46  LEU   B CA  1 
ATOM   1940 C  C   . LEU   B 1 34  ? -9.14668  23.12439  16.48417  1.000 18.91196 ?  46  LEU   B C   1 
ATOM   1941 O  O   . LEU   B 1 34  ? -10.00225 23.91447  16.07483  1.000 20.70487 ?  46  LEU   B O   1 
ATOM   1942 C  CB  . LEU   B 1 34  ? -9.65116  20.72694  16.07041  1.000 16.57842 ?  46  LEU   B CB  1 
ATOM   1943 C  CG  . LEU   B 1 34  ? -10.25340 19.41790  16.56545  1.000 14.57566 ?  46  LEU   B CG  1 
ATOM   1944 C  CD1 . LEU   B 1 34  ? -10.27338 18.41502  15.43649  1.000 20.37911 ?  46  LEU   B CD1 1 
ATOM   1945 C  CD2 . LEU   B 1 34  ? -9.49008  18.88138  17.76914  1.000 16.17651 ?  46  LEU   B CD2 1 
ATOM   1946 N  N   . TYR   B 1 35  ? -7.84294  23.34733  16.36663  1.000 16.19913 ?  47  TYR   B N   1 
ATOM   1947 C  CA  . TYR   B 1 35  ? -7.31364  24.54099  15.72868  1.000 15.24253 ?  47  TYR   B CA  1 
ATOM   1948 C  C   . TYR   B 1 35  ? -6.20327  24.09315  14.79828  1.000 16.59557 ?  47  TYR   B C   1 
ATOM   1949 O  O   . TYR   B 1 35  ? -5.20294  23.52464  15.24920  1.000 16.84026 ?  47  TYR   B O   1 
ATOM   1950 C  CB  . TYR   B 1 35  ? -6.77098  25.51392  16.77697  1.000 17.55750 ?  47  TYR   B CB  1 
ATOM   1951 C  CG  . TYR   B 1 35  ? -6.18067  26.76907  16.17641  1.000 20.45433 ?  47  TYR   B CG  1 
ATOM   1952 C  CD1 . TYR   B 1 35  ? -6.98948  27.84616  15.82750  1.000 19.29919 ?  47  TYR   B CD1 1 
ATOM   1953 C  CD2 . TYR   B 1 35  ? -4.81893  26.86301  15.92717  1.000 20.23779 ?  47  TYR   B CD2 1 
ATOM   1954 C  CE1 . TYR   B 1 35  ? -6.44868  28.98874  15.27782  1.000 21.18017 ?  47  TYR   B CE1 1 
ATOM   1955 C  CE2 . TYR   B 1 35  ? -4.27089  28.00354  15.37274  1.000 28.88702 ?  47  TYR   B CE2 1 
ATOM   1956 C  CZ  . TYR   B 1 35  ? -5.09372  29.06034  15.04915  1.000 28.21776 ?  47  TYR   B CZ  1 
ATOM   1957 O  OH  . TYR   B 1 35  ? -4.55804  30.19975  14.49721  1.000 33.10628 ?  47  TYR   B OH  1 
ATOM   1958 N  N   . GLN   B 1 36  ? -6.37480  24.32009  13.50368  1.000 17.38434 ?  48  GLN   B N   1 
ATOM   1959 C  CA  . GLN   B 1 36  ? -5.33178  23.93520  12.56355  1.000 16.27703 ?  48  GLN   B CA  1 
ATOM   1960 C  C   . GLN   B 1 36  ? -4.21472  24.96819  12.61939  1.000 21.92460 ?  48  GLN   B C   1 
ATOM   1961 O  O   . GLN   B 1 36  ? -4.45840  26.16846  12.46534  1.000 23.61239 ?  48  GLN   B O   1 
ATOM   1962 C  CB  . GLN   B 1 36  ? -5.87595  23.76757  11.14658  1.000 22.53989 ?  48  GLN   B CB  1 
ATOM   1963 C  CG  . GLN   B 1 36  ? -4.85831  23.16967  10.19211  1.000 26.30205 ?  48  GLN   B CG  1 
ATOM   1964 C  CD  . GLN   B 1 36  ? -5.49305  22.37153  9.06715   1.000 29.92926 ?  48  GLN   B CD  1 
ATOM   1965 O  OE1 . GLN   B 1 36  ? -6.66496  22.56467  8.72994   1.000 36.73522 ?  48  GLN   B OE1 1 
ATOM   1966 N  NE2 . GLN   B 1 36  ? -4.71463  21.47007  8.47314   1.000 32.51016 ?  48  GLN   B NE2 1 
ATOM   1967 N  N   . ILE   B 1 37  ? -3.00087  24.49721  12.89355  1.000 20.31434 ?  49  ILE   B N   1 
ATOM   1968 C  CA  . ILE   B 1 37  ? -1.82523  25.35155  13.02123  1.000 24.51645 ?  49  ILE   B CA  1 
ATOM   1969 C  C   . ILE   B 1 37  ? -1.05847  25.43731  11.71831  1.000 24.67338 ?  49  ILE   B C   1 
ATOM   1970 O  O   . ILE   B 1 37  ? -0.58899  26.50917  11.33085  1.000 32.00181 ?  49  ILE   B O   1 
ATOM   1971 C  CB  . ILE   B 1 37  ? -0.94007  24.74479  14.11938  1.000 25.80317 ?  49  ILE   B CB  1 
ATOM   1972 C  CG1 . ILE   B 1 37  ? -1.69925  24.74190  15.43653  1.000 22.06687 ?  49  ILE   B CG1 1 
ATOM   1973 C  CG2 . ILE   B 1 37  ? 0.40080   25.46317  14.16068  1.000 22.80631 ?  49  ILE   B CG2 1 
ATOM   1974 C  CD1 . ILE   B 1 37  ? -1.03086  23.97255  16.49297  1.000 23.84602 ?  49  ILE   B CD1 1 
ATOM   1975 N  N   . ALA   B 1 38  ? -0.88470  24.29815  11.07260  1.000 20.07166 ?  50  ALA   B N   1 
ATOM   1976 C  CA  . ALA   B 1 38  ? -0.16778  24.18957  9.81443   1.000 22.87464 ?  50  ALA   B CA  1 
ATOM   1977 C  C   . ALA   B 1 38  ? -0.70207  22.95075  9.11775   1.000 26.84187 ?  50  ALA   B C   1 
ATOM   1978 O  O   . ALA   B 1 38  ? -1.58749  22.26085  9.63618   1.000 24.25308 ?  50  ALA   B O   1 
ATOM   1979 C  CB  . ALA   B 1 38  ? 1.34094   24.09689  10.04912  1.000 27.97394 ?  50  ALA   B CB  1 
ATOM   1980 N  N   . ASP   B 1 39  ? -0.15483  22.66606  7.94096   1.000 29.75824 ?  51  ASP   B N   1 
ATOM   1981 C  CA  . ASP   B 1 39  ? -0.54169  21.47345  7.20150   1.000 26.17191 ?  51  ASP   B CA  1 
ATOM   1982 C  C   . ASP   B 1 39  ? -0.33920  20.22864  8.06192   1.000 26.08530 ?  51  ASP   B C   1 
ATOM   1983 O  O   . ASP   B 1 39  ? 0.78176   19.92822  8.48190   1.000 25.15828 ?  51  ASP   B O   1 
ATOM   1984 C  CB  . ASP   B 1 39  ? 0.29845   21.37480  5.93162   1.000 29.36080 ?  51  ASP   B CB  1 
ATOM   1985 C  CG  . ASP   B 1 39  ? -0.51670  20.95418  4.73603   1.000 46.04824 ?  51  ASP   B CG  1 
ATOM   1986 O  OD1 . ASP   B 1 39  ? -1.43481  20.12746  4.91229   1.000 45.82456 ?  51  ASP   B OD1 1 
ATOM   1987 O  OD2 . ASP   B 1 39  ? -0.24913  21.45582  3.62472   1.000 62.46983 ?  51  ASP   B OD2 1 
ATOM   1988 N  N   . GLY   B 1 40  ? -1.43265  19.51933  8.33454   1.000 25.44265 ?  52  GLY   B N   1 
ATOM   1989 C  CA  . GLY   B 1 40  ? -1.35232  18.26145  9.05306   1.000 23.18354 ?  52  GLY   B CA  1 
ATOM   1990 C  C   . GLY   B 1 40  ? -1.02953  18.38163  10.52408  1.000 16.15686 ?  52  GLY   B C   1 
ATOM   1991 O  O   . GLY   B 1 40  ? -0.63457  17.38516  11.14338  1.000 17.04563 ?  52  GLY   B O   1 
ATOM   1992 N  N   . VAL   B 1 41  ? -1.17685  19.56868  11.10822  1.000 16.13148 ?  53  VAL   B N   1 
ATOM   1993 C  CA  . VAL   B 1 41  ? -0.88907  19.77527  12.52490  1.000 15.96405 ?  53  VAL   B CA  1 
ATOM   1994 C  C   . VAL   B 1 41  ? -2.00410  20.61656  13.11815  1.000 16.42451 ?  53  VAL   B C   1 
ATOM   1995 O  O   . VAL   B 1 41  ? -2.31330  21.70087  12.60894  1.000 16.72347 ?  53  VAL   B O   1 
ATOM   1996 C  CB  . VAL   B 1 41  ? 0.47812   20.45411  12.77318  1.000 17.72059 ?  53  VAL   B CB  1 
ATOM   1997 C  CG1 . VAL   B 1 41  ? 0.74136   20.56596  14.25502  1.000 17.16091 ?  53  VAL   B CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 41  ? 1.61530   19.69145  12.09019  1.000 18.33300 ?  53  VAL   B CG2 1 
ATOM   1999 N  N   . TRP   B 1 42  ? -2.60628  20.11691  14.19276  1.000 14.01728 ?  54  TRP   B N   1 
ATOM   2000 C  CA  . TRP   B 1 42  ? -3.66718  20.79416  14.91228  1.000 14.27365 ?  54  TRP   B CA  1 
ATOM   2001 C  C   . TRP   B 1 42  ? -3.33816  20.77709  16.39419  1.000 14.03032 ?  54  TRP   B C   1 
ATOM   2002 O  O   . TRP   B 1 42  ? -2.64512  19.87642  16.88598  1.000 13.16474 ?  54  TRP   B O   1 
ATOM   2003 C  CB  . TRP   B 1 42  ? -5.01295  20.05132  14.78680  1.000 13.48330 ?  54  TRP   B CB  1 
ATOM   2004 C  CG  . TRP   B 1 42  ? -5.54743  19.82971  13.38686  1.000 14.64412 ?  54  TRP   B CG  1 
ATOM   2005 C  CD1 . TRP   B 1 42  ? -6.56379  20.52680  12.78638  1.000 19.81609 ?  54  TRP   B CD1 1 
ATOM   2006 C  CD2 . TRP   B 1 42  ? -5.14768  18.81657  12.44609  1.000 14.90759 ?  54  TRP   B CD2 1 
ATOM   2007 N  NE1 . TRP   B 1 42  ? -6.79889  20.02890  11.53387  1.000 17.33298 ?  54  TRP   B NE1 1 
ATOM   2008 C  CE2 . TRP   B 1 42  ? -5.95184  18.98100  11.29261  1.000 14.85052 ?  54  TRP   B CE2 1 
ATOM   2009 C  CE3 . TRP   B 1 42  ? -4.19497  17.79096  12.46087  1.000 14.61235 ?  54  TRP   B CE3 1 
ATOM   2010 C  CZ2 . TRP   B 1 42  ? -5.82123  18.16195  10.16268  1.000 15.23793 ?  54  TRP   B CZ2 1 
ATOM   2011 C  CZ3 . TRP   B 1 42  ? -4.06537  16.98239  11.32910  1.000 17.38799 ?  54  TRP   B CZ3 1 
ATOM   2012 C  CH2 . TRP   B 1 42  ? -4.88193  17.17090  10.20192  1.000 16.64439 ?  54  TRP   B CH2 1 
ATOM   2013 N  N   . SER   B 1 43  ? -3.84850  21.76296  17.11321  1.000 13.14247 ?  55  SER   B N   1 
ATOM   2014 C  CA  . SER   B 1 43  ? -3.98857  21.58889  18.54483  1.000 12.22056 ?  55  SER   B CA  1 
ATOM   2015 C  C   . SER   B 1 43  ? -5.42413  21.19737  18.85070  1.000 12.75580 ?  55  SER   B C   1 
ATOM   2016 O  O   . SER   B 1 43  ? -6.34588  21.42558  18.05183  1.000 11.94959 ?  55  SER   B O   1 
ATOM   2017 C  CB  . SER   B 1 43  ? -3.58987  22.84104  19.32400  1.000 13.72109 ?  55  SER   B CB  1 
ATOM   2018 O  OG  . SER   B 1 43  ? -4.40498  23.94699  18.97825  1.000 14.88156 ?  55  SER   B OG  1 
ATOM   2019 N  N   . HIS   B 1 44  ? -5.58783  20.53208  19.98204  1.000 12.77241 ?  56  HIS   B N   1 
ATOM   2020 C  CA  . HIS   B 1 44  ? -6.89721  20.30550  20.55920  1.000 12.21287 ?  56  HIS   B CA  1 
ATOM   2021 C  C   . HIS   B 1 44  ? -7.01044  21.09489  21.84670  1.000 11.86036 ?  56  HIS   B C   1 
ATOM   2022 O  O   . HIS   B 1 44  ? -6.03734  21.21031  22.60014  1.000 12.13189 ?  56  HIS   B O   1 
ATOM   2023 C  CB  . HIS   B 1 44  ? -7.24847  18.81314  20.71750  1.000 12.52004 ?  56  HIS   B CB  1 
ATOM   2024 C  CG  . HIS   B 1 44  ? -6.35302  18.00903  21.62185  1.000 12.70550 ?  56  HIS   B CG  1 
ATOM   2025 N  ND1 . HIS   B 1 44  ? -6.54324  17.94503  22.98773  1.000 12.60191 ?  56  HIS   B ND1 1 
ATOM   2026 C  CD2 . HIS   B 1 44  ? -5.38482  17.10283  21.34026  1.000 10.61531 ?  56  HIS   B CD2 1 
ATOM   2027 C  CE1 . HIS   B 1 44  ? -5.67967  17.09201  23.51442  1.000 12.47971 ?  56  HIS   B CE1 1 
ATOM   2028 N  NE2 . HIS   B 1 44  ? -4.96007  16.57002  22.53668  1.000 10.74914 ?  56  HIS   B NE2 1 
ATOM   2029 N  N   . ILE   B 1 45  ? -8.18284  21.67860  22.07460  1.000 14.50268 ?  57  ILE   B N   1 
ATOM   2030 C  CA  . ILE   B 1 45  ? -8.40936  22.55697  23.21513  1.000 14.62773 ?  57  ILE   B CA  1 
ATOM   2031 C  C   . ILE   B 1 45  ? -9.66010  22.08880  23.93215  1.000 17.28804 ?  57  ILE   B C   1 
ATOM   2032 O  O   . ILE   B 1 45  ? -10.72556 21.95953  23.31599  1.000 15.71427 ?  57  ILE   B O   1 
ATOM   2033 C  CB  . ILE   B 1 45  ? -8.54596  24.03205  22.79878  1.000 15.55514 ?  57  ILE   B CB  1 
ATOM   2034 C  CG1 . ILE   B 1 45  ? -7.40343  24.45242  21.86661  1.000 15.47389 ?  57  ILE   B CG1 1 
ATOM   2035 C  CG2 . ILE   B 1 45  ? -8.57585  24.90792  24.05179  1.000 17.11790 ?  57  ILE   B CG2 1 
ATOM   2036 C  CD1 . ILE   B 1 45  ? -7.73846  24.33761  20.36700  1.000 17.94683 ?  57  ILE   B CD1 1 
ATOM   2037 N  N   . ALA   B 1 46  ? -9.53198  21.83434  25.22542  1.000 16.75933 ?  58  ALA   B N   1 
ATOM   2038 C  CA  . ALA   B 1 46  ? -10.63940 21.43056  26.07386  1.000 15.07808 ?  58  ALA   B CA  1 
ATOM   2039 C  C   . ALA   B 1 46  ? -10.58561 22.25828  27.35048  1.000 16.62588 ?  58  ALA   B C   1 
ATOM   2040 O  O   . ALA   B 1 46  ? -9.63584  23.00461  27.58869  1.000 16.63470 ?  58  ALA   B O   1 
ATOM   2041 C  CB  . ALA   B 1 46  ? -10.57216 19.93091  26.38599  1.000 17.18633 ?  58  ALA   B CB  1 
ATOM   2042 N  N   . THR   B 1 47  ? -11.63185 22.15003  28.16337  1.000 19.74241 ?  59  THR   B N   1 
ATOM   2043 C  CA  . THR   B 1 47  ? -11.71373 22.89565  29.41160  1.000 20.81357 ?  59  THR   B CA  1 
ATOM   2044 C  C   . THR   B 1 47  ? -12.02336 21.94148  30.55325  1.000 20.11831 ?  59  THR   B C   1 
ATOM   2045 O  O   . THR   B 1 47  ? -12.56162 20.85190  30.35551  1.000 20.48325 ?  59  THR   B O   1 
ATOM   2046 C  CB  . THR   B 1 47  ? -12.75784 24.02844  29.36016  1.000 21.76460 ?  59  THR   B CB  1 
ATOM   2047 O  OG1 . THR   B 1 47  ? -14.00307 23.52860  28.84928  1.000 25.80432 ?  59  THR   B OG1 1 
ATOM   2048 C  CG2 . THR   B 1 47  ? -12.27644 25.16300  28.48983  1.000 22.18199 ?  59  THR   B CG2 1 
ATOM   2049 N  N   . GLN   B 1 48  ? -11.64995 22.35810  31.76043  1.000 18.46559 ?  60  GLN   B N   1 
ATOM   2050 C  CA  . GLN   B 1 48  ? -11.89765 21.56254  32.94818  1.000 22.19249 ?  60  GLN   B CA  1 
ATOM   2051 C  C   . GLN   B 1 48  ? -12.05714 22.49206  34.13752  1.000 23.37145 ?  60  GLN   B C   1 
ATOM   2052 O  O   . GLN   B 1 48  ? -11.37463 23.51519  34.23372  1.000 21.32851 ?  60  GLN   B O   1 
ATOM   2053 C  CB  . GLN   B 1 48  ? -10.76052 20.57250  33.21889  1.000 26.42534 ?  60  GLN   B CB  1 
ATOM   2054 C  CG  . GLN   B 1 48  ? -11.15246 19.37553  34.07390  1.000 23.56082 ?  60  GLN   B CG  1 
ATOM   2055 C  CD  . GLN   B 1 48  ? -12.51452 18.80500  33.71624  1.000 33.31330 ?  60  GLN   B CD  1 
ATOM   2056 O  OE1 . GLN   B 1 48  ? -13.54267 19.24716  34.23919  1.000 34.44097 ?  60  GLN   B OE1 1 
ATOM   2057 N  NE2 . GLN   B 1 48  ? -12.53183 17.83083  32.81113  1.000 28.93717 ?  60  GLN   B NE2 1 
ATOM   2058 N  N   . SER   B 1 49  ? -12.98157 22.13211  35.02353  1.000 30.81238 ?  61  SER   B N   1 
ATOM   2059 C  CA  . SER   B 1 49  ? -13.14423 22.82392  36.29141  1.000 32.56676 ?  61  SER   B CA  1 
ATOM   2060 C  C   . SER   B 1 49  ? -12.13875 22.26192  37.28481  1.000 31.27200 ?  61  SER   B C   1 
ATOM   2061 O  O   . SER   B 1 49  ? -11.99247 21.04251  37.41040  1.000 35.36504 ?  61  SER   B O   1 
ATOM   2062 C  CB  . SER   B 1 49  ? -14.56265 22.61229  36.81308  1.000 32.66627 ?  61  SER   B CB  1 
ATOM   2063 O  OG  . SER   B 1 49  ? -15.40713 23.67695  36.41466  1.000 44.42026 ?  61  SER   B OG  1 
ATOM   2064 N  N   . PHE   B 1 50  ? -11.43749 23.14714  37.98361  1.000 25.13752 ?  62  PHE   B N   1 
ATOM   2065 C  CA  . PHE   B 1 50  ? -10.41625 22.72075  38.93234  1.000 26.87661 ?  62  PHE   B CA  1 
ATOM   2066 C  C   . PHE   B 1 50  ? -10.31514 23.79037  40.00726  1.000 34.30984 ?  62  PHE   B C   1 
ATOM   2067 O  O   . PHE   B 1 50  ? -10.01323 24.94549  39.69576  1.000 28.57998 ?  62  PHE   B O   1 
ATOM   2068 C  CB  . PHE   B 1 50  ? -9.07104  22.53370  38.21429  1.000 31.59382 ?  62  PHE   B CB  1 
ATOM   2069 C  CG  . PHE   B 1 50  ? -7.95702  22.07864  39.11233  1.000 34.27600 ?  62  PHE   B CG  1 
ATOM   2070 C  CD1 . PHE   B 1 50  ? -7.07860  22.99305  39.67021  1.000 39.37593 ?  62  PHE   B CD1 1 
ATOM   2071 C  CD2 . PHE   B 1 50  ? -7.79539  20.73525  39.40756  1.000 39.54685 ?  62  PHE   B CD2 1 
ATOM   2072 C  CE1 . PHE   B 1 50  ? -6.05441  22.57430  40.50260  1.000 43.44071 ?  62  PHE   B CE1 1 
ATOM   2073 C  CE2 . PHE   B 1 50  ? -6.77505  20.31017  40.23854  1.000 42.96448 ?  62  PHE   B CE2 1 
ATOM   2074 C  CZ  . PHE   B 1 50  ? -5.90339  21.23053  40.78604  1.000 40.58062 ?  62  PHE   B CZ  1 
ATOM   2075 N  N   . ASP   B 1 51  ? -10.58933 23.40947  41.25789  1.000 29.92202 ?  63  ASP   B N   1 
ATOM   2076 C  CA  . ASP   B 1 51  ? -10.48119 24.31946  42.40419  1.000 31.33915 ?  63  ASP   B CA  1 
ATOM   2077 C  C   . ASP   B 1 51  ? -11.30931 25.58961  42.21201  1.000 31.44952 ?  63  ASP   B C   1 
ATOM   2078 O  O   . ASP   B 1 51  ? -10.86747 26.69484  42.52885  1.000 34.97869 ?  63  ASP   B O   1 
ATOM   2079 C  CB  . ASP   B 1 51  ? -9.02515  24.66374  42.71925  1.000 36.88517 ?  63  ASP   B CB  1 
ATOM   2080 C  CG  . ASP   B 1 51  ? -8.53199  24.00499  43.98609  1.000 38.27954 ?  63  ASP   B CG  1 
ATOM   2081 O  OD1 . ASP   B 1 51  ? -9.36251  23.73843  44.87702  1.000 39.05045 ?  63  ASP   B OD1 1 
ATOM   2082 O  OD2 . ASP   B 1 51  ? -7.30875  23.77733  44.10188  1.000 40.53311 ?  63  ASP   B OD2 1 
ATOM   2083 N  N   . GLY   B 1 52  ? -12.51503 25.43624  41.66738  1.000 29.00323 ?  64  GLY   B N   1 
ATOM   2084 C  CA  . GLY   B 1 52  ? -13.43511 26.54866  41.52875  1.000 35.52955 ?  64  GLY   B CA  1 
ATOM   2085 C  C   . GLY   B 1 52  ? -13.26087 27.41700  40.29815  1.000 39.66877 ?  64  GLY   B C   1 
ATOM   2086 O  O   . GLY   B 1 52  ? -14.12000 28.27347  40.04198  1.000 36.55236 ?  64  GLY   B O   1 
ATOM   2087 N  N   . ALA   B 1 53  ? -12.18857 27.24102  39.53127  1.000 27.68654 ?  65  ALA   B N   1 
ATOM   2088 C  CA  . ALA   B 1 53  ? -11.96359 27.99404  38.30640  1.000 20.59003 ?  65  ALA   B CA  1 
ATOM   2089 C  C   . ALA   B 1 53  ? -12.01770 27.05587  37.10987  1.000 27.02709 ?  65  ALA   B C   1 
ATOM   2090 O  O   . ALA   B 1 53  ? -11.92488 25.83601  37.25014  1.000 24.93851 ?  65  ALA   B O   1 
ATOM   2091 C  CB  . ALA   B 1 53  ? -10.60331 28.68821  38.33375  1.000 21.01658 ?  65  ALA   B CB  1 
ATOM   2092 N  N   . VAL   B 1 54  ? -12.17247 27.63972  35.92463  1.000 21.17389 ?  66  VAL   B N   1 
ATOM   2093 C  CA  . VAL   B 1 54  ? -12.16002 26.88478  34.67867  1.000 21.56329 ?  66  VAL   B CA  1 
ATOM   2094 C  C   . VAL   B 1 54  ? -10.87417 27.20451  33.93364  1.000 17.52376 ?  66  VAL   B C   1 
ATOM   2095 O  O   . VAL   B 1 54  ? -10.50397 28.37558  33.78413  1.000 17.54134 ?  66  VAL   B O   1 
ATOM   2096 C  CB  . VAL   B 1 54  ? -13.39948 27.16878  33.81557  1.000 18.70344 ?  66  VAL   B CB  1 
ATOM   2097 C  CG1 . VAL   B 1 54  ? -13.32162 26.37487  32.51848  1.000 25.16635 ?  66  VAL   B CG1 1 
ATOM   2098 C  CG2 . VAL   B 1 54  ? -14.66920 26.82299  34.58104  1.000 28.47842 ?  66  VAL   B CG2 1 
ATOM   2099 N  N   . TYR   B 1 55  ? -10.18908 26.15529  33.47351  1.000 18.39808 ?  67  TYR   B N   1 
ATOM   2100 C  CA  . TYR   B 1 55  ? -8.92623  26.28079  32.77021  1.000 17.56325 ?  67  TYR   B CA  1 
ATOM   2101 C  C   . TYR   B 1 55  ? -9.03107  25.63707  31.39657  1.000 15.26392 ?  67  TYR   B C   1 
ATOM   2102 O  O   . TYR   B 1 55  ? -9.65543  24.57981  31.26395  1.000 16.67043 ?  67  TYR   B O   1 
ATOM   2103 C  CB  . TYR   B 1 55  ? -7.82163  25.54312  33.54134  1.000 17.99249 ?  67  TYR   B CB  1 
ATOM   2104 C  CG  . TYR   B 1 55  ? -7.53116  26.10512  34.91474  1.000 21.36900 ?  67  TYR   B CG  1 
ATOM   2105 C  CD1 . TYR   B 1 55  ? -8.28757  25.73494  36.01849  1.000 24.16605 ?  67  TYR   B CD1 1 
ATOM   2106 C  CD2 . TYR   B 1 55  ? -6.48881  27.00087  35.10255  1.000 26.55110 ?  67  TYR   B CD2 1 
ATOM   2107 C  CE1 . TYR   B 1 55  ? -8.01222  26.25586  37.27765  1.000 22.23164 ?  67  TYR   B CE1 1 
ATOM   2108 C  CE2 . TYR   B 1 55  ? -6.20681  27.52075  36.34802  1.000 28.74913 ?  67  TYR   B CE2 1 
ATOM   2109 C  CZ  . TYR   B 1 55  ? -6.97370  27.15238  37.42684  1.000 27.45650 ?  67  TYR   B CZ  1 
ATOM   2110 O  OH  . TYR   B 1 55  ? -6.68393  27.68174  38.66608  1.000 31.19138 ?  67  TYR   B OH  1 
ATOM   2111 N  N   . PRO   B 1 56  ? -8.40775  26.22435  30.37694  1.000 15.53258 ?  68  PRO   B N   1 
ATOM   2112 C  CA  . PRO   B 1 56  ? -8.25773  25.53861  29.09536  1.000 16.45503 ?  68  PRO   B CA  1 
ATOM   2113 C  C   . PRO   B 1 56  ? -6.99987  24.68149  29.12307  1.000 19.21483 ?  68  PRO   B C   1 
ATOM   2114 O  O   . PRO   B 1 56  ? -6.12235  24.82274  29.98068  1.000 15.01363 ?  68  PRO   B O   1 
ATOM   2115 C  CB  . PRO   B 1 56  ? -8.06610  26.70795  28.12576  1.000 19.55009 ?  68  PRO   B CB  1 
ATOM   2116 C  CG  . PRO   B 1 56  ? -7.24361  27.69103  28.94034  1.000 20.78382 ?  68  PRO   B CG  1 
ATOM   2117 C  CD  . PRO   B 1 56  ? -7.61886  27.46598  30.40916  1.000 17.13528 ?  68  PRO   B CD  1 
ATOM   2118 N  N   . SER   B 1 57  ? -6.93281  23.76153  28.17350  1.000 16.73591 ?  69  SER   B N   1 
ATOM   2119 C  CA  . SER   B 1 57  ? -5.79568  22.86037  28.10183  1.000 15.93724 ?  69  SER   B CA  1 
ATOM   2120 C  C   . SER   B 1 57  ? -5.60797  22.47241  26.64909  1.000 14.00434 ?  69  SER   B C   1 
ATOM   2121 O  O   . SER   B 1 57  ? -6.58734  22.19965  25.95002  1.000 13.20932 ?  69  SER   B O   1 
ATOM   2122 C  CB  . SER   B 1 57  ? -6.06874  21.61368  28.94293  1.000 16.63632 ?  69  SER   B CB  1 
ATOM   2123 O  OG  . SER   B 1 57  ? -4.91235  20.81827  29.10074  1.000 18.37066 ?  69  SER   B OG  1 
ATOM   2124 N  N   . ASN   B 1 58  ? -4.35563  22.46536  26.20046  1.000 14.10384 ?  70  ASN   B N   1 
ATOM   2125 C  CA  . ASN   B 1 58  ? -3.98561  22.10877  24.83651  1.000 12.86935 ?  70  ASN   B CA  1 
ATOM   2126 C  C   . ASN   B 1 58  ? -3.34500  20.73068  24.76403  1.000 12.26625 ?  70  ASN   B C   1 
ATOM   2127 O  O   . ASN   B 1 58  ? -2.60209  20.31574  25.65597  1.000 12.96375 ?  70  ASN   B O   1 
ATOM   2128 C  CB  . ASN   B 1 58  ? -2.93962  23.06897  24.28430  1.000 13.18438 ?  70  ASN   B CB  1 
ATOM   2129 C  CG  . ASN   B 1 58  ? -3.42748  24.48431  24.20163  1.000 12.60316 ?  70  ASN   B CG  1 
ATOM   2130 O  OD1 . ASN   B 1 58  ? -4.56566  24.74648  23.78131  1.000 14.73134 ?  70  ASN   B OD1 1 
ATOM   2131 N  ND2 . ASN   B 1 58  ? -2.56528  25.42060  24.58468  1.000 10.51672 ?  70  ASN   B ND2 1 
ATOM   2132 N  N   . GLY   B 1 59  ? -3.61181  20.05111  23.66310  1.000 10.79359 ?  71  GLY   B N   1 
ATOM   2133 C  CA  . GLY   B 1 59  ? -2.79929  18.95059  23.18508  1.000 12.10839 ?  71  GLY   B CA  1 
ATOM   2134 C  C   . GLY   B 1 59  ? -2.52369  19.13574  21.70564  1.000 8.54892  ?  71  GLY   B C   1 
ATOM   2135 O  O   . GLY   B 1 59  ? -2.82677  20.20196  21.15027  1.000 10.75140 ?  71  GLY   B O   1 
ATOM   2136 N  N   . LEU   B 1 60  ? -1.96731  18.12534  21.04778  1.000 10.86939 ?  72  LEU   B N   1 
ATOM   2137 C  CA  . LEU   B 1 60  ? -1.56944  18.24395  19.65625  1.000 11.83466 ?  72  LEU   B CA  1 
ATOM   2138 C  C   . LEU   B 1 60  ? -2.03894  17.02773  18.86871  1.000 9.75590  ?  72  LEU   B C   1 
ATOM   2139 O  O   . LEU   B 1 60  ? -2.18943  15.93213  19.41261  1.000 10.18755 ?  72  LEU   B O   1 
ATOM   2140 C  CB  . LEU   B 1 60  ? -0.05010  18.33671  19.54181  1.000 12.54708 ?  72  LEU   B CB  1 
ATOM   2141 C  CG  . LEU   B 1 60  ? 0.49098   19.03193  18.29776  1.000 11.17605 ?  72  LEU   B CG  1 
ATOM   2142 C  CD1 . LEU   B 1 60  ? 0.24009   20.49608  18.42111  1.000 13.10505 ?  72  LEU   B CD1 1 
ATOM   2143 C  CD2 . LEU   B 1 60  ? 1.98612   18.74993  18.13399  1.000 13.03641 ?  72  LEU   B CD2 1 
ATOM   2144 N  N   . ILE   B 1 61  ? -2.28359  17.23556  17.57575  1.000 11.50901 ?  73  ILE   B N   1 
ATOM   2145 C  CA  . ILE   B 1 61  ? -2.61227  16.16303  16.64080  1.000 11.21132 ?  73  ILE   B CA  1 
ATOM   2146 C  C   . ILE   B 1 61  ? -1.72778  16.33416  15.41805  1.000 11.53202 ?  73  ILE   B C   1 
ATOM   2147 O  O   . ILE   B 1 61  ? -1.65673  17.43427  14.85641  1.000 11.02526 ?  73  ILE   B O   1 
ATOM   2148 C  CB  . ILE   B 1 61  ? -4.08696  16.23623  16.20154  1.000 11.15218 ?  73  ILE   B CB  1 
ATOM   2149 C  CG1 . ILE   B 1 61  ? -5.03966  16.16661  17.39133  1.000 11.09332 ?  73  ILE   B CG1 1 
ATOM   2150 C  CG2 . ILE   B 1 61  ? -4.39648  15.13195  15.18146  1.000 13.70701 ?  73  ILE   B CG2 1 
ATOM   2151 C  CD1 . ILE   B 1 61  ? -6.42215  16.70207  17.07022  1.000 13.61001 ?  73  ILE   B CD1 1 
ATOM   2152 N  N   . VAL   B 1 62  ? -1.07078  15.25647  14.99748  1.000 9.85282  ?  74  VAL   B N   1 
ATOM   2153 C  CA  . VAL   B 1 62  ? -0.12440  15.32091  13.88440  1.000 10.73049 ?  74  VAL   B CA  1 
ATOM   2154 C  C   . VAL   B 1 62  ? -0.46524  14.22261  12.88980  1.000 13.14820 ?  74  VAL   B C   1 
ATOM   2155 O  O   . VAL   B 1 62  ? -0.50879  13.04009  13.25158  1.000 12.44097 ?  74  VAL   B O   1 
ATOM   2156 C  CB  . VAL   B 1 62  ? 1.34073   15.21098  14.35030  1.000 10.17076 ?  74  VAL   B CB  1 
ATOM   2157 C  CG1 . VAL   B 1 62  ? 2.29036   15.40784  13.17839  1.000 11.86750 ?  74  VAL   B CG1 1 
ATOM   2158 C  CG2 . VAL   B 1 62  ? 1.64849   16.22034  15.44112  1.000 13.42419 ?  74  VAL   B CG2 1 
ATOM   2159 N  N   . ARG   B 1 63  ? -0.69196  14.60726  11.63641  1.000 13.63289 ?  75  ARG   B N   1 
ATOM   2160 C  CA  . ARG   B 1 63  ? -0.98308  13.61862  10.60918  1.000 15.57681 ?  75  ARG   B CA  1 
ATOM   2161 C  C   . ARG   B 1 63  ? 0.23966   12.76303  10.31853  1.000 16.66472 ?  75  ARG   B C   1 
ATOM   2162 O  O   . ARG   B 1 63  ? 1.35871   13.27029  10.17367  1.000 16.57806 ?  75  ARG   B O   1 
ATOM   2163 C  CB  . ARG   B 1 63  ? -1.44442  14.28940  9.32026   1.000 18.42932 ?  75  ARG   B CB  1 
ATOM   2164 C  CG  . ARG   B 1 63  ? -1.90863  13.27036  8.29588   1.000 20.19670 ?  75  ARG   B CG  1 
ATOM   2165 C  CD  . ARG   B 1 63  ? -2.49782  13.91782  7.05625   1.000 26.87214 ?  75  ARG   B CD  1 
ATOM   2166 N  NE  . ARG   B 1 63  ? -2.88606  12.89734  6.09036   1.000 27.93340 ?  75  ARG   B NE  1 
ATOM   2167 C  CZ  . ARG   B 1 63  ? -3.88167  13.02252  5.22255   1.000 32.02482 ?  75  ARG   B CZ  1 
ATOM   2168 N  NH1 . ARG   B 1 63  ? -4.59370  14.13495  5.14229   1.000 31.31033 ?  75  ARG   B NH1 1 
ATOM   2169 N  NH2 . ARG   B 1 63  ? -4.16467  12.00761  4.41069   1.000 29.65762 ?  75  ARG   B NH2 1 
ATOM   2170 N  N   . ASP   B 1 64  ? -0.00224  11.45047  10.21251  1.000 18.79912 ?  76  ASP   B N   1 
ATOM   2171 C  CA  . ASP   B 1 64  ? 1.01966   10.40781  10.14425  1.000 21.88033 ?  76  ASP   B CA  1 
ATOM   2172 C  C   . ASP   B 1 64  ? 0.62650   9.51048   8.96455   1.000 28.74205 ?  76  ASP   B C   1 
ATOM   2173 O  O   . ASP   B 1 64  ? 0.09192   8.41476   9.14157   1.000 23.51123 ?  76  ASP   B O   1 
ATOM   2174 C  CB  . ASP   B 1 64  ? 1.03505   9.64103   11.48391  1.000 29.94390 ?  76  ASP   B CB  1 
ATOM   2175 C  CG  . ASP   B 1 64  ? 2.10175   8.54929   11.56111  1.000 28.14204 ?  76  ASP   B CG  1 
ATOM   2176 O  OD1 . ASP   B 1 64  ? 3.02293   8.52143   10.71169  1.000 25.99327 ?  76  ASP   B OD1 1 
ATOM   2177 O  OD2 . ASP   B 1 64  ? 2.02075   7.72536   12.51849  1.000 25.09607 ?  76  ASP   B OD2 1 
ATOM   2178 N  N   . GLY   B 1 65  ? 0.85529   10.00832  7.74995   1.000 26.27739 ?  77  GLY   B N   1 
ATOM   2179 C  CA  . GLY   B 1 65  ? 0.38157   9.33513   6.55323   1.000 30.18244 ?  77  GLY   B CA  1 
ATOM   2180 C  C   . GLY   B 1 65  ? -1.12963  9.39156   6.45123   1.000 24.09597 ?  77  GLY   B C   1 
ATOM   2181 O  O   . GLY   B 1 65  ? -1.70922  10.47202  6.30511   1.000 28.67462 ?  77  GLY   B O   1 
ATOM   2182 N  N   . ASP   B 1 66  ? -1.78617  8.23554   6.53608   1.000 21.30616 ?  78  ASP   B N   1 
ATOM   2183 C  CA  . ASP   B 1 66  ? -3.24132  8.17454   6.59430   1.000 18.65618 ?  78  ASP   B CA  1 
ATOM   2184 C  C   . ASP   B 1 66  ? -3.77863  7.96127   8.00286   1.000 25.90898 ?  78  ASP   B C   1 
ATOM   2185 O  O   . ASP   B 1 66  ? -4.97655  7.71789   8.16319   1.000 22.59049 ?  78  ASP   B O   1 
ATOM   2186 C  CB  . ASP   B 1 66  ? -3.78110  7.11405   5.63126   1.000 25.92082 ?  78  ASP   B CB  1 
ATOM   2187 C  CG  . ASP   B 1 66  ? -3.42196  7.41598   4.19394   1.000 40.96155 ?  78  ASP   B CG  1 
ATOM   2188 O  OD1 . ASP   B 1 66  ? -3.29906  8.61823   3.87081   1.000 35.88330 ?  78  ASP   B OD1 1 
ATOM   2189 O  OD2 . ASP   B 1 66  ? -3.25548  6.46816   3.39579   1.000 44.93087 ?  78  ASP   B OD2 1 
ATOM   2190 N  N   . GLU   B 1 67  ? -2.93093  8.06736   9.02075   1.000 17.64712 ?  79  GLU   B N   1 
ATOM   2191 C  CA  . GLU   B 1 67  ? -3.33195  7.95870   10.41539  1.000 18.83267 ?  79  GLU   B CA  1 
ATOM   2192 C  C   . GLU   B 1 67  ? -2.99064  9.26065   11.14144  1.000 17.58920 ?  79  GLU   B C   1 
ATOM   2193 O  O   . GLU   B 1 67  ? -2.39473  10.18226  10.57195  1.000 16.43543 ?  79  GLU   B O   1 
ATOM   2194 C  CB  . GLU   B 1 67  ? -2.66156  6.76072   11.09505  1.000 19.24516 ?  79  GLU   B CB  1 
ATOM   2195 C  CG  . GLU   B 1 67  ? -2.71641  5.45106   10.30552  1.000 27.36689 ?  79  GLU   B CG  1 
ATOM   2196 C  CD  . GLU   B 1 67  ? -1.59270  4.50290   10.68722  1.000 30.23198 ?  79  GLU   B CD  1 
ATOM   2197 O  OE1 . GLU   B 1 67  ? -1.10058  4.57998   11.83220  1.000 26.20529 ?  79  GLU   B OE1 1 
ATOM   2198 O  OE2 . GLU   B 1 67  ? -1.19867  3.67579   9.84365   1.000 40.12295 ?  79  GLU   B OE2 1 
ATOM   2199 N  N   . LEU   B 1 68  ? -3.37648  9.33166   12.41491  1.000 15.08199 ?  80  LEU   B N   1 
ATOM   2200 C  CA  . LEU   B 1 68  ? -3.07099  10.48098  13.25861  1.000 13.54231 ?  80  LEU   B CA  1 
ATOM   2201 C  C   . LEU   B 1 68  ? -2.30610  10.03849  14.49072  1.000 13.86975 ?  80  LEU   B C   1 
ATOM   2202 O  O   . LEU   B 1 68  ? -2.61743  9.00616   15.09739  1.000 13.96127 ?  80  LEU   B O   1 
ATOM   2203 C  CB  . LEU   B 1 68  ? -4.33083  11.20254  13.72258  1.000 12.57763 ?  80  LEU   B CB  1 
ATOM   2204 C  CG  . LEU   B 1 68  ? -5.23813  11.73524  12.61586  1.000 14.66222 ?  80  LEU   B CG  1 
ATOM   2205 C  CD1 . LEU   B 1 68  ? -6.46655  12.35656  13.20365  1.000 14.98145 ?  80  LEU   B CD1 1 
ATOM   2206 C  CD2 . LEU   B 1 68  ? -4.49020  12.74682  11.76145  1.000 18.26347 ?  80  LEU   B CD2 1 
ATOM   2207 N  N   . LEU   B 1 69  ? -1.33272  10.85620  14.86663  1.000 11.91220 ?  81  LEU   B N   1 
ATOM   2208 C  CA  . LEU   B 1 69  ? -0.63519  10.73423  16.13553  1.000 11.70147 ?  81  LEU   B CA  1 
ATOM   2209 C  C   . LEU   B 1 69  ? -1.20481  11.78574  17.07495  1.000 10.31526 ?  81  LEU   B C   1 
ATOM   2210 O  O   . LEU   B 1 69  ? -1.27790  12.96718  16.71850  1.000 10.22536 ?  81  LEU   B O   1 
ATOM   2211 C  CB  . LEU   B 1 69  ? 0.85342   10.99583  15.93786  1.000 11.75323 ?  81  LEU   B CB  1 
ATOM   2212 C  CG  . LEU   B 1 69  ? 1.68429   11.10217  17.21950  1.000 12.04806 ?  81  LEU   B CG  1 
ATOM   2213 C  CD1 . LEU   B 1 69  ? 1.70688   9.79250   17.98896  1.000 12.21532 ?  81  LEU   B CD1 1 
ATOM   2214 C  CD2 . LEU   B 1 69  ? 3.09760   11.53356  16.86022  1.000 14.53508 ?  81  LEU   B CD2 1 
ATOM   2215 N  N   . LEU   B 1 70  ? -1.65540  11.35195  18.25084  1.000 10.77207 ?  82  LEU   B N   1 
ATOM   2216 C  CA  . LEU   B 1 70  ? -2.20584  12.25819  19.24859  1.000 8.93006  ?  82  LEU   B CA  1 
ATOM   2217 C  C   . LEU   B 1 70  ? -1.16569  12.53869  20.32557  1.000 9.75979  ?  82  LEU   B C   1 
ATOM   2218 O  O   . LEU   B 1 70  ? -0.50869  11.61923  20.81866  1.000 10.11642 ?  82  LEU   B O   1 
ATOM   2219 C  CB  . LEU   B 1 70  ? -3.42307  11.58805  19.88696  1.000 10.37096 ?  82  LEU   B CB  1 
ATOM   2220 C  CG  . LEU   B 1 70  ? -4.13301  12.36782  20.98607  1.000 9.94711  ?  82  LEU   B CG  1 
ATOM   2221 C  CD1 . LEU   B 1 70  ? -4.70687  13.67718  20.47514  1.000 11.63190 ?  82  LEU   B CD1 1 
ATOM   2222 C  CD2 . LEU   B 1 70  ? -5.19408  11.50156  21.64608  1.000 13.08938 ?  82  LEU   B CD2 1 
ATOM   2223 N  N   . ILE   B 1 71  ? -1.02620  13.80779  20.70894  1.000 8.90351  ?  83  ILE   B N   1 
ATOM   2224 C  CA  . ILE   B 1 71  ? -0.18060  14.18539  21.84215  1.000 8.62502  ?  83  ILE   B CA  1 
ATOM   2225 C  C   . ILE   B 1 71  ? -1.10100  14.68131  22.94769  1.000 9.18075  ?  83  ILE   B C   1 
ATOM   2226 O  O   . ILE   B 1 71  ? -1.73889  15.73550  22.81371  1.000 9.89504  ?  83  ILE   B O   1 
ATOM   2227 C  CB  . ILE   B 1 71  ? 0.83921   15.26904  21.46747  1.000 9.84354  ?  83  ILE   B CB  1 
ATOM   2228 C  CG1 . ILE   B 1 71  ? 1.60957   14.89503  20.18665  1.000 11.12909 ?  83  ILE   B CG1 1 
ATOM   2229 C  CG2 . ILE   B 1 71  ? 1.78645   15.51978  22.64508  1.000 11.99869 ?  83  ILE   B CG2 1 
ATOM   2230 C  CD1 . ILE   B 1 71  ? 2.47973   13.65989  20.28752  1.000 11.90789 ?  83  ILE   B CD1 1 
ATOM   2231 N  N   . ASP   B 1 72  ? -1.17762  13.89632  24.02948  1.000 8.03021  ?  84  ASP   B N   1 
ATOM   2232 C  CA  . ASP   B 1 72  ? -1.91999  14.21249  25.25078  1.000 8.24787  ?  84  ASP   B CA  1 
ATOM   2233 C  C   . ASP   B 1 72  ? -3.42344  14.01748  25.13816  1.000 11.33612 ?  84  ASP   B C   1 
ATOM   2234 O  O   . ASP   B 1 72  ? -4.02477  14.24667  24.08515  1.000 9.26029  ?  84  ASP   B O   1 
ATOM   2235 C  CB  . ASP   B 1 72  ? -1.53546  15.58586  25.81650  1.000 9.34737  ?  84  ASP   B CB  1 
ATOM   2236 C  CG  . ASP   B 1 72  ? -0.13199  15.58797  26.37375  1.000 10.25430 ?  84  ASP   B CG  1 
ATOM   2237 O  OD1 . ASP   B 1 72  ? 0.29506   14.53925  26.89149  1.000 9.47505  ?  84  ASP   B OD1 1 
ATOM   2238 O  OD2 . ASP   B 1 72  ? 0.55910   16.61246  26.27533  1.000 10.77286 ?  84  ASP   B OD2 1 
ATOM   2239 N  N   . THR   B 1 73  ? -4.02686  13.58758  26.24007  1.000 10.72168 ?  85  THR   B N   1 
ATOM   2240 C  CA  . THR   B 1 73  ? -5.47109  13.48107  26.32233  1.000 11.05960 ?  85  THR   B CA  1 
ATOM   2241 C  C   . THR   B 1 73  ? -6.08716  14.86946  26.45201  1.000 11.77445 ?  85  THR   B C   1 
ATOM   2242 O  O   . THR   B 1 73  ? -5.39656  15.89525  26.48821  1.000 12.50918 ?  85  THR   B O   1 
ATOM   2243 C  CB  . THR   B 1 73  ? -5.86890  12.65300  27.53331  1.000 12.24792 ?  85  THR   B CB  1 
ATOM   2244 O  OG1 . THR   B 1 73  ? -5.56508  13.40018  28.71840  1.000 12.74884 ?  85  THR   B OG1 1 
ATOM   2245 C  CG2 . THR   B 1 73  ? -5.16928  11.29228  27.55453  1.000 12.67771 ?  85  THR   B CG2 1 
ATOM   2246 N  N   . ALA   B 1 74  ? -7.42171  14.90551  26.50632  1.000 12.87076 ?  86  ALA   B N   1 
ATOM   2247 C  CA  . ALA   B 1 74  ? -8.15764  16.15047  26.66492  1.000 12.06881 ?  86  ALA   B CA  1 
ATOM   2248 C  C   . ALA   B 1 74  ? -8.58047  16.39028  28.10816  1.000 17.03755 ?  86  ALA   B C   1 
ATOM   2249 O  O   . ALA   B 1 74  ? -9.55618  17.10429  28.35069  1.000 16.77749 ?  86  ALA   B O   1 
ATOM   2250 C  CB  . ALA   B 1 74  ? -9.35320  16.19160  25.71422  1.000 13.72555 ?  86  ALA   B CB  1 
ATOM   2251 N  N   . TRP   B 1 75  ? -7.83733  15.82155  29.06497  1.000 15.63862 ?  87  TRP   B N   1 
ATOM   2252 C  CA  . TRP   B 1 75  ? -8.02666  16.01700  30.49817  1.000 19.06071 ?  87  TRP   B CA  1 
ATOM   2253 C  C   . TRP   B 1 75  ? -9.31397  15.35044  30.97172  1.000 18.34635 ?  87  TRP   B C   1 
ATOM   2254 O  O   . TRP   B 1 75  ? -10.29410 16.03087  31.29587  1.000 20.53644 ?  87  TRP   B O   1 
ATOM   2255 C  CB  . TRP   B 1 75  ? -7.95853  17.50689  30.85709  1.000 18.63944 ?  87  TRP   B CB  1 
ATOM   2256 C  CG  . TRP   B 1 75  ? -7.77740  17.81600  32.31943  1.000 18.96627 ?  87  TRP   B CG  1 
ATOM   2257 C  CD1 . TRP   B 1 75  ? -7.75270  16.93069  33.35782  1.000 22.05331 ?  87  TRP   B CD1 1 
ATOM   2258 C  CD2 . TRP   B 1 75  ? -7.58618  19.11646  32.89009  1.000 18.30616 ?  87  TRP   B CD2 1 
ATOM   2259 N  NE1 . TRP   B 1 75  ? -7.55970  17.60748  34.54754  1.000 21.10218 ?  87  TRP   B NE1 1 
ATOM   2260 C  CE2 . TRP   B 1 75  ? -7.45273  18.94828  34.28077  1.000 20.72806 ?  87  TRP   B CE2 1 
ATOM   2261 C  CE3 . TRP   B 1 75  ? -7.50364  20.40726  32.35397  1.000 26.93177 ?  87  TRP   B CE3 1 
ATOM   2262 C  CZ2 . TRP   B 1 75  ? -7.25623  20.02733  35.14787  1.000 22.86173 ?  87  TRP   B CZ2 1 
ATOM   2263 C  CZ3 . TRP   B 1 75  ? -7.31280  21.47521  33.21266  1.000 25.91872 ?  87  TRP   B CZ3 1 
ATOM   2264 C  CH2 . TRP   B 1 75  ? -7.19538  21.27731  34.59446  1.000 27.63784 ?  87  TRP   B CH2 1 
ATOM   2265 N  N   . GLY   B 1 76  ? -9.31328  14.02611  31.02253  1.000 16.40526 ?  88  GLY   B N   1 
ATOM   2266 C  CA  . GLY   B 1 76  ? -10.44474 13.27731  31.53212  1.000 17.80217 ?  88  GLY   B CA  1 
ATOM   2267 C  C   . GLY   B 1 76  ? -11.13526 12.45607  30.44614  1.000 19.42318 ?  88  GLY   B C   1 
ATOM   2268 O  O   . GLY   B 1 76  ? -11.00129 12.70690  29.24663  1.000 18.40379 ?  88  GLY   B O   1 
ATOM   2269 N  N   . ALA   B 1 77  ? -11.90515 11.46048  30.89868  1.000 21.82556 ?  89  ALA   B N   1 
ATOM   2270 C  CA  . ALA   B 1 77  ? -12.53401 10.50261  29.98621  1.000 20.96774 ?  89  ALA   B CA  1 
ATOM   2271 C  C   . ALA   B 1 77  ? -13.60746 11.15631  29.11747  1.000 21.53913 ?  89  ALA   B C   1 
ATOM   2272 O  O   . ALA   B 1 77  ? -13.67080 10.91294  27.90672  1.000 21.08667 ?  89  ALA   B O   1 
ATOM   2273 C  CB  . ALA   B 1 77  ? -13.10870 9.32669   30.78271  1.000 23.63055 ?  89  ALA   B CB  1 
ATOM   2274 N  N   . LYS   B 1 78  ? -14.46710 11.97904  29.72356  1.000 18.62512 ?  90  LYS   B N   1 
ATOM   2275 C  CA  . LYS   B 1 78  ? -15.53370 12.66330  28.99252  1.000 21.82188 ?  90  LYS   B CA  1 
ATOM   2276 C  C   . LYS   B 1 78  ? -14.96692 13.54771  27.88713  1.000 18.80040 ?  90  LYS   B C   1 
ATOM   2277 O  O   . LYS   B 1 78  ? -15.37655 13.44880  26.72223  1.000 20.22059 ?  90  LYS   B O   1 
ATOM   2278 C  CB  . LYS   B 1 78  ? -16.33719 13.48833  30.00501  1.000 28.79286 ?  90  LYS   B CB  1 
ATOM   2279 C  CG  . LYS   B 1 78  ? -17.37022 14.51275  29.52174  1.000 36.68205 ?  90  LYS   B CG  1 
ATOM   2280 C  CD  . LYS   B 1 78  ? -18.42708 13.98091  28.57880  1.000 39.02558 ?  90  LYS   B CD  1 
ATOM   2281 C  CE  . LYS   B 1 78  ? -18.92312 15.10502  27.66453  1.000 43.85488 ?  90  LYS   B CE  1 
ATOM   2282 N  NZ  . LYS   B 1 78  ? -18.58135 14.95671  26.22456  1.000 37.90629 ?  90  LYS   B NZ  1 
ATOM   2283 N  N   . ASN   B 1 79  ? -14.01912 14.42121  28.23744  1.000 18.37276 ?  91  ASN   B N   1 
ATOM   2284 C  CA  . ASN   B 1 79  ? -13.39511 15.28988  27.24639  1.000 19.83499 ?  91  ASN   B CA  1 
ATOM   2285 C  C   . ASN   B 1 79  ? -12.67361 14.47879  26.17873  1.000 15.16652 ?  91  ASN   B C   1 
ATOM   2286 O  O   . ASN   B 1 79  ? -12.66647 14.86055  25.00366  1.000 16.52491 ?  91  ASN   B O   1 
ATOM   2287 C  CB  . ASN   B 1 79  ? -12.39831 16.22580  27.93119  1.000 17.70278 ?  91  ASN   B CB  1 
ATOM   2288 C  CG  . ASN   B 1 79  ? -13.06201 17.37012  28.67314  1.000 27.15003 ?  91  ASN   B CG  1 
ATOM   2289 O  OD1 . ASN   B 1 79  ? -14.28168 17.50090  28.67422  1.000 23.03678 ?  91  ASN   B OD1 1 
ATOM   2290 N  ND2 . ASN   B 1 79  ? -12.25282 18.20137  29.32446  1.000 21.33966 ?  91  ASN   B ND2 1 
ATOM   2291 N  N   . THR   B 1 80  ? -12.04175 13.36565  26.56767  1.000 17.65171 ?  92  THR   B N   1 
ATOM   2292 C  CA  . THR   B 1 80  ? -11.24888 12.61020  25.60040  1.000 16.00303 ?  92  THR   B CA  1 
ATOM   2293 C  C   . THR   B 1 80  ? -12.14605 11.86400  24.62430  1.000 17.28644 ?  92  THR   B C   1 
ATOM   2294 O  O   . THR   B 1 80  ? -11.82594 11.75843  23.43880  1.000 15.79603 ?  92  THR   B O   1 
ATOM   2295 C  CB  . THR   B 1 80  ? -10.26666 11.68625  26.32530  1.000 14.21112 ?  92  THR   B CB  1 
ATOM   2296 O  OG1 . THR   B 1 80  ? -9.37251  12.49655  27.10927  1.000 14.12137 ?  92  THR   B OG1 1 
ATOM   2297 C  CG2 . THR   B 1 80  ? -9.44280  10.85913  25.35072  1.000 17.55273 ?  92  THR   B CG2 1 
ATOM   2298 N  N   . ALA   B 1 81  ? -13.28781 11.35645  25.09623  1.000 18.92907 ?  93  ALA   B N   1 
ATOM   2299 C  CA  . ALA   B 1 81  ? -14.26172 10.80944  24.15796  1.000 21.20516 ?  93  ALA   B CA  1 
ATOM   2300 C  C   . ALA   B 1 81  ? -14.74223 11.88177  23.18952  1.000 17.58158 ?  93  ALA   B C   1 
ATOM   2301 O  O   . ALA   B 1 81  ? -14.86048 11.63413  21.97894  1.000 19.28799 ?  93  ALA   B O   1 
ATOM   2302 C  CB  . ALA   B 1 81  ? -15.43291 10.18225  24.91823  1.000 21.60619 ?  93  ALA   B CB  1 
ATOM   2303 N  N   . ALA   B 1 82  ? -15.00120 13.08802  23.69847  1.000 16.05345 ?  94  ALA   B N   1 
ATOM   2304 C  CA  . ALA   B 1 82  ? -15.39749 14.18671  22.82980  1.000 18.91649 ?  94  ALA   B CA  1 
ATOM   2305 C  C   . ALA   B 1 82  ? -14.27227 14.55242  21.87104  1.000 20.56908 ?  94  ALA   B C   1 
ATOM   2306 O  O   . ALA   B 1 82  ? -14.51957 14.86585  20.70204  1.000 19.35942 ?  94  ALA   B O   1 
ATOM   2307 C  CB  . ALA   B 1 82  ? -15.82741 15.38832  23.66926  1.000 19.32930 ?  94  ALA   B CB  1 
ATOM   2308 N  N   . LEU   B 1 83  ? -13.02344 14.49267  22.34476  1.000 17.46743 ?  95  LEU   B N   1 
ATOM   2309 C  CA  . LEU   B 1 83  ? -11.88518 14.72068  21.45886  1.000 14.92632 ?  95  LEU   B CA  1 
ATOM   2310 C  C   . LEU   B 1 83  ? -11.90759 13.76681  20.27138  1.000 17.34101 ?  95  LEU   B C   1 
ATOM   2311 O  O   . LEU   B 1 83  ? -11.74626 14.18900  19.11979  1.000 15.57774 ?  95  LEU   B O   1 
ATOM   2312 C  CB  . LEU   B 1 83  ? -10.58100 14.58025  22.25078  1.000 13.87246 ?  95  LEU   B CB  1 
ATOM   2313 C  CG  . LEU   B 1 83  ? -9.26562  14.48861  21.46825  1.000 13.01294 ?  95  LEU   B CG  1 
ATOM   2314 C  CD1 . LEU   B 1 83  ? -9.01184  15.74622  20.68241  1.000 15.99283 ?  95  LEU   B CD1 1 
ATOM   2315 C  CD2 . LEU   B 1 83  ? -8.11672  14.21879  22.44534  1.000 13.77957 ?  95  LEU   B CD2 1 
ATOM   2316 N  N   . LEU   B 1 84  ? -12.10537 12.46939  20.52842  1.000 15.06085 ?  96  LEU   B N   1 
ATOM   2317 C  CA  . LEU   B 1 84  ? -12.09534 11.51021  19.43078  1.000 16.08971 ?  96  LEU   B CA  1 
ATOM   2318 C  C   . LEU   B 1 84  ? -13.23738 11.78808  18.46717  1.000 18.18556 ?  96  LEU   B C   1 
ATOM   2319 O  O   . LEU   B 1 84  ? -13.06200 11.70684  17.24697  1.000 16.59315 ?  96  LEU   B O   1 
ATOM   2320 C  CB  . LEU   B 1 84  ? -12.18219 10.08791  19.96994  1.000 14.95773 ?  96  LEU   B CB  1 
ATOM   2321 C  CG  . LEU   B 1 84  ? -10.94586 9.61749   20.74078  1.000 14.92241 ?  96  LEU   B CG  1 
ATOM   2322 C  CD1 . LEU   B 1 84  ? -11.17955 8.22089   21.30541  1.000 17.91982 ?  96  LEU   B CD1 1 
ATOM   2323 C  CD2 . LEU   B 1 84  ? -9.70555  9.62414   19.83753  1.000 16.88690 ?  96  LEU   B CD2 1 
ATOM   2324 N  N   . ALA   B 1 85  ? -14.39827 12.17178  19.00044  1.000 15.45333 ?  97  ALA   B N   1 
ATOM   2325 C  CA  . ALA   B 1 85  ? -15.53460 12.48594  18.14087  1.000 17.95484 ?  97  ALA   B CA  1 
ATOM   2326 C  C   . ALA   B 1 85  ? -15.25097 13.71980  17.30042  1.000 20.17244 ?  97  ALA   B C   1 
ATOM   2327 O  O   . ALA   B 1 85  ? -15.60698 13.76515  16.11616  1.000 20.93793 ?  97  ALA   B O   1 
ATOM   2328 C  CB  . ALA   B 1 85  ? -16.78330 12.70273  18.98956  1.000 19.03573 ?  97  ALA   B CB  1 
ATOM   2329 N  N   . GLU   B 1 86  ? -14.59570 14.72570  17.88915  1.000 20.02726 ?  98  GLU   B N   1 
ATOM   2330 C  CA  . GLU   B 1 86  ? -14.29243 15.93726  17.13794  1.000 16.22415 ?  98  GLU   B CA  1 
ATOM   2331 C  C   . GLU   B 1 86  ? -13.23715 15.66446  16.07502  1.000 18.86869 ?  98  GLU   B C   1 
ATOM   2332 O  O   . GLU   B 1 86  ? -13.30136 16.21949  14.97122  1.000 17.73929 ?  98  GLU   B O   1 
ATOM   2333 C  CB  . GLU   B 1 86  ? -13.82237 17.03770  18.09148  1.000 21.52717 ?  98  GLU   B CB  1 
ATOM   2334 C  CG  . GLU   B 1 86  ? -13.95435 18.43423  17.52241  1.000 26.65166 ?  98  GLU   B CG  1 
ATOM   2335 C  CD  . GLU   B 1 86  ? -15.40248 18.82529  17.28789  1.000 26.01691 ?  98  GLU   B CD  1 
ATOM   2336 O  OE1 . GLU   B 1 86  ? -16.25904 18.49509  18.13474  1.000 32.17776 ?  98  GLU   B OE1 1 
ATOM   2337 O  OE2 . GLU   B 1 86  ? -15.68197 19.45519  16.25946  1.000 37.29738 ?  98  GLU   B OE2 1 
ATOM   2338 N  N   . ILE   B 1 87  ? -12.25917 14.80869  16.38330  1.000 16.96941 ?  99  ILE   B N   1 
ATOM   2339 C  CA  . ILE   B 1 87  ? -11.28467 14.40254  15.37076  1.000 16.45033 ?  99  ILE   B CA  1 
ATOM   2340 C  C   . ILE   B 1 87  ? -11.98464 13.71613  14.20223  1.000 19.83664 ?  99  ILE   B C   1 
ATOM   2341 O  O   . ILE   B 1 87  ? -11.71791 14.01091  13.03110  1.000 18.24717 ?  99  ILE   B O   1 
ATOM   2342 C  CB  . ILE   B 1 87  ? -10.19298 13.51225  15.99684  1.000 16.73179 ?  99  ILE   B CB  1 
ATOM   2343 C  CG1 . ILE   B 1 87  ? -9.23182  14.35684  16.83752  1.000 14.57794 ?  99  ILE   B CG1 1 
ATOM   2344 C  CG2 . ILE   B 1 87  ? -9.41920  12.78453  14.92571  1.000 16.81293 ?  99  ILE   B CG2 1 
ATOM   2345 C  CD1 . ILE   B 1 87  ? -8.33843  13.54400  17.75935  1.000 15.73658 ?  99  ILE   B CD1 1 
ATOM   2346 N  N   . GLU   B 1 88  ? -12.88940 12.78383  14.50658  1.000 18.77761 ?  100 GLU   B N   1 
ATOM   2347 C  CA  . GLU   B 1 88  ? -13.62031 12.08834  13.45333  1.000 19.51755 ?  100 GLU   B CA  1 
ATOM   2348 C  C   . GLU   B 1 88  ? -14.41669 13.05366  12.59339  1.000 23.21332 ?  100 GLU   B C   1 
ATOM   2349 O  O   . GLU   B 1 88  ? -14.46644 12.90686  11.36708  1.000 20.98179 ?  100 GLU   B O   1 
ATOM   2350 C  CB  . GLU   B 1 88  ? -14.55483 11.06155  14.08290  1.000 14.62926 ?  100 GLU   B CB  1 
ATOM   2351 C  CG  . GLU   B 1 88  ? -15.50862 10.38697  13.10044  1.000 18.44767 ?  100 GLU   B CG  1 
ATOM   2352 C  CD  . GLU   B 1 88  ? -14.81640 9.71031   11.94158  1.000 22.73677 ?  100 GLU   B CD  1 
ATOM   2353 O  OE1 . GLU   B 1 88  ? -13.59891 9.43723   12.01422  1.000 22.28518 ?  100 GLU   B OE1 1 
ATOM   2354 O  OE2 . GLU   B 1 88  ? -15.51545 9.40829   10.94805  1.000 20.68931 ?  100 GLU   B OE2 1 
ATOM   2355 N  N   . LYS   B 1 89  ? -15.04669 14.04500  13.21284  1.000 18.01172 ?  101 LYS   B N   1 
ATOM   2356 C  CA  . LYS   B 1 89  ? -15.90486 14.94502  12.45170  1.000 22.98172 ?  101 LYS   B CA  1 
ATOM   2357 C  C   . LYS   B 1 89  ? -15.09572 15.92724  11.60218  1.000 26.48554 ?  101 LYS   B C   1 
ATOM   2358 O  O   . LYS   B 1 89  ? -15.47397 16.21384  10.45955  1.000 22.17799 ?  101 LYS   B O   1 
ATOM   2359 C  CB  . LYS   B 1 89  ? -16.90038 15.64005  13.38243  1.000 23.33182 ?  101 LYS   B CB  1 
ATOM   2360 C  CG  . LYS   B 1 89  ? -17.42741 16.99721  12.92110  1.000 29.58395 ?  101 LYS   B CG  1 
ATOM   2361 C  CD  . LYS   B 1 89  ? -18.07855 17.73278  14.08233  1.000 25.88110 ?  101 LYS   B CD  1 
ATOM   2362 C  CE  . LYS   B 1 89  ? -19.03283 18.82264  13.59534  1.000 33.90786 ?  101 LYS   B CE  1 
ATOM   2363 N  NZ  . LYS   B 1 89  ? -19.31895 19.82096  14.66639  1.000 37.49551 ?  101 LYS   B NZ  1 
ATOM   2364 N  N   . GLN   B 1 90  ? -13.97331 16.44752  12.11822  1.000 20.47775 ?  102 GLN   B N   1 
ATOM   2365 C  CA  . GLN   B 1 90  ? -13.24635 17.46543  11.35907  1.000 21.17788 ?  102 GLN   B CA  1 
ATOM   2366 C  C   . GLN   B 1 90  ? -12.06583 16.95051  10.55236  1.000 19.29816 ?  102 GLN   B C   1 
ATOM   2367 O  O   . GLN   B 1 90  ? -11.65510 17.62547  9.60172   1.000 22.28483 ?  102 GLN   B O   1 
ATOM   2368 C  CB  . GLN   B 1 90  ? -12.79363 18.65325  12.21943  1.000 27.15076 ?  102 GLN   B CB  1 
ATOM   2369 C  CG  . GLN   B 1 90  ? -13.83003 19.22094  13.15427  1.000 27.20254 ?  102 GLN   B CG  1 
ATOM   2370 C  CD  . GLN   B 1 90  ? -13.26719 20.35083  13.98185  1.000 32.73286 ?  102 GLN   B CD  1 
ATOM   2371 O  OE1 . GLN   B 1 90  ? -13.60003 20.50967  15.15313  1.000 39.85701 ?  102 GLN   B OE1 1 
ATOM   2372 N  NE2 . GLN   B 1 90  ? -12.41874 21.16473  13.36258  1.000 32.43865 ?  102 GLN   B NE2 1 
ATOM   2373 N  N   . ILE   B 1 91  ? -11.49874 15.79909  10.90036  1.000 17.60974 ?  103 ILE   B N   1 
ATOM   2374 C  CA  . ILE   B 1 91  ? -10.35940 15.23585  10.18767  1.000 16.24788 ?  103 ILE   B CA  1 
ATOM   2375 C  C   . ILE   B 1 91  ? -10.70081 13.89258  9.55325   1.000 19.43290 ?  103 ILE   B C   1 
ATOM   2376 O  O   . ILE   B 1 91  ? -10.40405 13.65457  8.37843   1.000 20.77851 ?  103 ILE   B O   1 
ATOM   2377 C  CB  . ILE   B 1 91  ? -9.11616  15.12695  11.10367  1.000 13.95110 ?  103 ILE   B CB  1 
ATOM   2378 C  CG1 . ILE   B 1 91  ? -8.83446  16.49726  11.74445  1.000 17.10559 ?  103 ILE   B CG1 1 
ATOM   2379 C  CG2 . ILE   B 1 91  ? -7.90568  14.58042  10.33776  1.000 15.56080 ?  103 ILE   B CG2 1 
ATOM   2380 C  CD1 . ILE   B 1 91  ? -7.77200  16.47967  12.84992  1.000 17.41886 ?  103 ILE   B CD1 1 
ATOM   2381 N  N   . GLY   B 1 92  ? -11.32112 12.99832  10.31771  1.000 16.40980 ?  104 GLY   B N   1 
ATOM   2382 C  CA  . GLY   B 1 92  ? -11.83617 11.77149  9.74605   1.000 18.86503 ?  104 GLY   B CA  1 
ATOM   2383 C  C   . GLY   B 1 92  ? -10.81712 10.68872  9.49283   1.000 26.57703 ?  104 GLY   B C   1 
ATOM   2384 O  O   . GLY   B 1 92  ? -11.12366 9.73368   8.77276   1.000 27.19418 ?  104 GLY   B O   1 
ATOM   2385 N  N   . LEU   B 1 93  ? -9.60614  10.80713  10.04954  1.000 16.77104 ?  105 LEU   B N   1 
ATOM   2386 C  CA  . LEU   B 1 93  ? -8.59425  9.77685   10.01941  1.000 17.49035 ?  105 LEU   B CA  1 
ATOM   2387 C  C   . LEU   B 1 93  ? -8.47976  9.13906   11.40265  1.000 16.57087 ?  105 LEU   B C   1 
ATOM   2388 O  O   . LEU   B 1 93  ? -8.77623  9.79135   12.40822  1.000 18.43434 ?  105 LEU   B O   1 
ATOM   2389 C  CB  . LEU   B 1 93  ? -7.24415  10.40236  9.64947   1.000 16.40321 ?  105 LEU   B CB  1 
ATOM   2390 C  CG  . LEU   B 1 93  ? -7.17857  11.07486  8.27452   1.000 22.49924 ?  105 LEU   B CG  1 
ATOM   2391 C  CD1 . LEU   B 1 93  ? -5.83609  11.77855  8.09092   1.000 21.93632 ?  105 LEU   B CD1 1 
ATOM   2392 C  CD2 . LEU   B 1 93  ? -7.38468  10.04878  7.16667   1.000 23.13621 ?  105 LEU   B CD2 1 
ATOM   2393 N  N   . PRO   B 1 94  ? -8.07086  7.87257   11.48323  1.000 19.62715 ?  106 PRO   B N   1 
ATOM   2394 C  CA  . PRO   B 1 94  ? -7.99008  7.19668   12.78563  1.000 16.83130 ?  106 PRO   B CA  1 
ATOM   2395 C  C   . PRO   B 1 94  ? -6.75443  7.59572   13.58070  1.000 18.11779 ?  106 PRO   B C   1 
ATOM   2396 O  O   . PRO   B 1 94  ? -5.64194  7.66050   13.05662  1.000 15.88298 ?  106 PRO   B O   1 
ATOM   2397 C  CB  . PRO   B 1 94  ? -7.90628  5.71345   12.40084  1.000 21.35138 ?  106 PRO   B CB  1 
ATOM   2398 C  CG  . PRO   B 1 94  ? -7.24328  5.72122   11.06192  1.000 18.91314 ?  106 PRO   B CG  1 
ATOM   2399 C  CD  . PRO   B 1 94  ? -7.73422  6.97032   10.36595  1.000 18.17727 ?  106 PRO   B CD  1 
ATOM   2400 N  N   . VAL   B 1 95  ? -6.95990  7.83702   14.87031  1.000 15.74860 ?  107 VAL   B N   1 
ATOM   2401 C  CA  . VAL   B 1 95  ? -5.84566  8.00254   15.79782  1.000 16.08023 ?  107 VAL   B CA  1 
ATOM   2402 C  C   . VAL   B 1 95  ? -5.31602  6.61034   16.10715  1.000 14.87937 ?  107 VAL   B C   1 
ATOM   2403 O  O   . VAL   B 1 95  ? -6.04510  5.76860   16.64459  1.000 18.62394 ?  107 VAL   B O   1 
ATOM   2404 C  CB  . VAL   B 1 95  ? -6.31017  8.70790   17.07990  1.000 15.22621 ?  107 VAL   B CB  1 
ATOM   2405 C  CG1 . VAL   B 1 95  ? -5.16946  8.81535   18.08394  1.000 15.90906 ?  107 VAL   B CG1 1 
ATOM   2406 C  CG2 . VAL   B 1 95  ? -6.89980  10.07155  16.76493  1.000 19.55056 ?  107 VAL   B CG2 1 
ATOM   2407 N  N   . THR   B 1 96  ? -4.06981  6.34702   15.73587  1.000 12.76853 ?  108 THR   B N   1 
ATOM   2408 C  CA  . THR   B 1 96  ? -3.49881  5.03215   15.97849  1.000 14.58706 ?  108 THR   B CA  1 
ATOM   2409 C  C   . THR   B 1 96  ? -2.50932  4.99966   17.13105  1.000 15.49020 ?  108 THR   B C   1 
ATOM   2410 O  O   . THR   B 1 96  ? -2.32013  3.93797   17.73226  1.000 14.55193 ?  108 THR   B O   1 
ATOM   2411 C  CB  . THR   B 1 96  ? -2.83066  4.49352   14.71386  1.000 17.25796 ?  108 THR   B CB  1 
ATOM   2412 O  OG1 . THR   B 1 96  ? -1.86580  5.43686   14.23555  1.000 16.33065 ?  108 THR   B OG1 1 
ATOM   2413 C  CG2 . THR   B 1 96  ? -3.87843  4.25494   13.62984  1.000 20.63765 ?  108 THR   B CG2 1 
ATOM   2414 N  N   . ARG   B 1 97  ? -1.86438  6.12344   17.45228  1.000 13.03422 ?  109 ARG   B N   1 
ATOM   2415 C  CA  . ARG   B 1 97  ? -0.94329  6.18448   18.57609  1.000 11.22485 ?  109 ARG   B CA  1 
ATOM   2416 C  C   . ARG   B 1 97  ? -1.15376  7.48776   19.32620  1.000 11.76525 ?  109 ARG   B C   1 
ATOM   2417 O  O   . ARG   B 1 97  ? -1.56470  8.49379   18.74530  1.000 13.26111 ?  109 ARG   B O   1 
ATOM   2418 C  CB  . ARG   B 1 97  ? 0.52406   6.09336   18.14955  1.000 14.38243 ?  109 ARG   B CB  1 
ATOM   2419 C  CG  . ARG   B 1 97  ? 0.90989   4.77144   17.45552  1.000 13.85600 ?  109 ARG   B CG  1 
ATOM   2420 C  CD  . ARG   B 1 97  ? 2.38195   4.72250   17.12006  1.000 18.20022 ?  109 ARG   B CD  1 
ATOM   2421 N  NE  . ARG   B 1 97  ? 2.73261   5.65251   16.04846  1.000 16.26844 ?  109 ARG   B NE  1 
ATOM   2422 C  CZ  . ARG   B 1 97  ? 3.94700   5.75388   15.52335  1.000 18.32697 ?  109 ARG   B CZ  1 
ATOM   2423 N  NH1 . ARG   B 1 97  ? 4.96311   5.04116   15.98664  1.000 21.83617 ?  109 ARG   B NH1 1 
ATOM   2424 N  NH2 . ARG   B 1 97  ? 4.14833   6.58911   14.50401  1.000 21.25457 ?  109 ARG   B NH2 1 
ATOM   2425 N  N   . ALA   B 1 98  ? -0.88013  7.45193   20.62888  1.000 11.45329 ?  110 ALA   B N   1 
ATOM   2426 C  CA  . ALA   B 1 98  ? -0.90290  8.65547   21.44395  1.000 11.14129 ?  110 ALA   B CA  1 
ATOM   2427 C  C   . ALA   B 1 98  ? 0.30126   8.65234   22.36397  1.000 9.61870  ?  110 ALA   B C   1 
ATOM   2428 O  O   . ALA   B 1 98  ? 0.73679   7.60173   22.82905  1.000 11.68106 ?  110 ALA   B O   1 
ATOM   2429 C  CB  . ALA   B 1 98  ? -2.17668  8.72767   22.29091  1.000 12.48637 ?  110 ALA   B CB  1 
ATOM   2430 N  N   . VAL   B 1 99  ? 0.81788   9.84643   22.63907  1.000 9.60858  ?  111 VAL   B N   1 
ATOM   2431 C  CA  . VAL   B 1 99  ? 1.91944   10.04519  23.57477  1.000 8.57588  ?  111 VAL   B CA  1 
ATOM   2432 C  C   . VAL   B 1 99  ? 1.43299   11.00570  24.65121  1.000 8.24445  ?  111 VAL   B C   1 
ATOM   2433 O  O   . VAL   B 1 99  ? 0.87022   12.06306  24.34042  1.000 10.04761 ?  111 VAL   B O   1 
ATOM   2434 C  CB  . VAL   B 1 99  ? 3.14167   10.64761  22.85104  1.000 9.61840  ?  111 VAL   B CB  1 
ATOM   2435 C  CG1 . VAL   B 1 99  ? 4.21886   11.12327  23.84739  1.000 10.17891 ?  111 VAL   B CG1 1 
ATOM   2436 C  CG2 . VAL   B 1 99  ? 3.70827   9.65564   21.85522  1.000 10.46618 ?  111 VAL   B CG2 1 
ATOM   2437 N  N   . SER   B 1 100 ? 1.64268   10.64557  25.91539  1.000 9.40764  ?  112 SER   B N   1 
ATOM   2438 C  CA  . SER   B 1 100 ? 1.40059   11.56937  27.01808  1.000 8.68614  ?  112 SER   B CA  1 
ATOM   2439 C  C   . SER   B 1 100 ? 2.72305   12.18029  27.47202  1.000 9.63852  ?  112 SER   B C   1 
ATOM   2440 O  O   . SER   B 1 100 ? 3.70524   11.45575  27.68591  1.000 9.14469  ?  112 SER   B O   1 
ATOM   2441 C  CB  . SER   B 1 100 ? 0.72882   10.85118  28.19065  1.000 9.69155  ?  112 SER   B CB  1 
ATOM   2442 O  OG  . SER   B 1 100 ? -0.59159  10.47624  27.82543  1.000 10.77658 ?  112 SER   B OG  1 
ATOM   2443 N  N   . THR   B 1 101 ? 2.73296   13.51436  27.64330  1.000 9.84832  ?  113 THR   B N   1 
ATOM   2444 C  CA  . THR   B 1 101 ? 3.98384   14.23424  27.86091  1.000 8.44732  ?  113 THR   B CA  1 
ATOM   2445 C  C   . THR   B 1 101 ? 4.39538   14.38129  29.32079  1.000 8.39039  ?  113 THR   B C   1 
ATOM   2446 O  O   . THR   B 1 101 ? 5.52632   14.79333  29.56847  1.000 9.60330  ?  113 THR   B O   1 
ATOM   2447 C  CB  . THR   B 1 101 ? 3.97642   15.60353  27.15379  1.000 9.04339  ?  113 THR   B CB  1 
ATOM   2448 O  OG1 . THR   B 1 101 ? 2.89738   16.39859  27.64535  1.000 9.79466  ?  113 THR   B OG1 1 
ATOM   2449 C  CG2 . THR   B 1 101 ? 3.83343   15.42735  25.64555  1.000 10.58672 ?  113 THR   B CG2 1 
ATOM   2450 N  N   . HIS   B 1 102 ? 3.51351   14.10899  30.28506  1.000 8.99679  ?  114 HIS   B N   1 
ATOM   2451 C  CA  . HIS   B 1 102 ? 3.91818   13.85416  31.66237  1.000 7.72666  ?  114 HIS   B CA  1 
ATOM   2452 C  C   . HIS   B 1 102 ? 2.76190   13.17082  32.37711  1.000 9.35179  ?  114 HIS   B C   1 
ATOM   2453 O  O   . HIS   B 1 102 ? 1.71981   12.88887  31.78061  1.000 10.80983 ?  114 HIS   B O   1 
ATOM   2454 C  CB  . HIS   B 1 102 ? 4.46804   15.10103  32.39579  1.000 10.63299 ?  114 HIS   B CB  1 
ATOM   2455 C  CG  . HIS   B 1 102 ? 3.45336   16.15434  32.71963  1.000 10.47014 ?  114 HIS   B CG  1 
ATOM   2456 N  ND1 . HIS   B 1 102 ? 3.04824   17.11441  31.81133  1.000 9.59596  ?  114 HIS   B ND1 1 
ATOM   2457 C  CD2 . HIS   B 1 102 ? 2.78408   16.42060  33.86687  1.000 10.04324 ?  114 HIS   B CD2 1 
ATOM   2458 C  CE1 . HIS   B 1 102 ? 2.17113   17.92211  32.38023  1.000 11.05497 ?  114 HIS   B CE1 1 
ATOM   2459 N  NE2 . HIS   B 1 102 ? 1.97857   17.50396  33.61720  1.000 9.63428  ?  114 HIS   B NE2 1 
ATOM   2460 N  N   . PHE   B 1 103 ? 2.96151   12.89482  33.66651  1.000 10.10853 ?  115 PHE   B N   1 
ATOM   2461 C  CA  . PHE   B 1 103 ? 2.10205   11.95202  34.37652  1.000 11.21675 ?  115 PHE   B CA  1 
ATOM   2462 C  C   . PHE   B 1 103 ? 0.82242   12.54620  34.95502  1.000 10.56261 ?  115 PHE   B C   1 
ATOM   2463 O  O   . PHE   B 1 103 ? -0.01262  11.77865  35.45419  1.000 11.84349 ?  115 PHE   B O   1 
ATOM   2464 C  CB  . PHE   B 1 103 ? 2.89340   11.24056  35.47521  1.000 10.67975 ?  115 PHE   B CB  1 
ATOM   2465 C  CG  . PHE   B 1 103 ? 3.16200   12.08956  36.70052  1.000 11.30137 ?  115 PHE   B CG  1 
ATOM   2466 C  CD1 . PHE   B 1 103 ? 4.20388   12.98927  36.72703  1.000 10.48333 ?  115 PHE   B CD1 1 
ATOM   2467 C  CD2 . PHE   B 1 103 ? 2.37102   11.96028  37.84115  1.000 12.89085 ?  115 PHE   B CD2 1 
ATOM   2468 C  CE1 . PHE   B 1 103 ? 4.47724   13.74303  37.87302  1.000 12.49245 ?  115 PHE   B CE1 1 
ATOM   2469 C  CE2 . PHE   B 1 103 ? 2.63112   12.71104  38.98197  1.000 15.17141 ?  115 PHE   B CE2 1 
ATOM   2470 C  CZ  . PHE   B 1 103 ? 3.68153   13.60907  38.99636  1.000 14.76494 ?  115 PHE   B CZ  1 
ATOM   2471 N  N   . HIS   B 1 104 ? 0.64770   13.85909  34.94454  1.000 10.14738 ?  116 HIS   B N   1 
ATOM   2472 C  CA  . HIS   B 1 104 ? -0.51716  14.44196  35.59856  1.000 10.26597 ?  116 HIS   B CA  1 
ATOM   2473 C  C   . HIS   B 1 104 ? -1.79609  14.19445  34.78717  1.000 13.26662 ?  116 HIS   B C   1 
ATOM   2474 O  O   . HIS   B 1 104 ? -1.76583  13.82519  33.60849  1.000 13.24883 ?  116 HIS   B O   1 
ATOM   2475 C  CB  . HIS   B 1 104 ? -0.30519  15.93648  35.81776  1.000 11.59275 ?  116 HIS   B CB  1 
ATOM   2476 C  CG  . HIS   B 1 104 ? 0.69127   16.25486  36.89819  1.000 11.81662 ?  116 HIS   B CG  1 
ATOM   2477 N  ND1 . HIS   B 1 104 ? 1.41917   17.42143  36.91400  1.000 15.81881 ?  116 HIS   B ND1 1 
ATOM   2478 C  CD2 . HIS   B 1 104 ? 1.08907   15.56538  37.98861  1.000 14.81925 ?  116 HIS   B CD2 1 
ATOM   2479 C  CE1 . HIS   B 1 104 ? 2.20893   17.45198  37.96638  1.000 16.13405 ?  116 HIS   B CE1 1 
ATOM   2480 N  NE2 . HIS   B 1 104 ? 2.02479   16.33797  38.64184  1.000 14.98433 ?  116 HIS   B NE2 1 
ATOM   2481 N  N   . ASP   B 1 105 ? -2.94215  14.40769  35.44785  1.000 15.46483 ?  117 ASP   B N   1 
ATOM   2482 C  CA  . ASP   B 1 105 ? -4.22855  14.02218  34.86881  1.000 15.28409 ?  117 ASP   B CA  1 
ATOM   2483 C  C   . ASP   B 1 105 ? -4.57727  14.77449  33.59449  1.000 16.55460 ?  117 ASP   B C   1 
ATOM   2484 O  O   . ASP   B 1 105 ? -5.30012  14.23373  32.74782  1.000 17.05448 ?  117 ASP   B O   1 
ATOM   2485 C  CB  . ASP   B 1 105 ? -5.34118  14.18127  35.90313  1.000 23.29372 ?  117 ASP   B CB  1 
ATOM   2486 C  CG  . ASP   B 1 105 ? -5.68906  12.88451  36.56931  1.000 31.69284 ?  117 ASP   B CG  1 
ATOM   2487 O  OD1 . ASP   B 1 105 ? -6.24099  12.00262  35.87132  1.000 42.42094 ?  117 ASP   B OD1 1 
ATOM   2488 O  OD2 . ASP   B 1 105 ? -5.42210  12.74678  37.77881  1.000 43.93590 ?  117 ASP   B OD2 1 
ATOM   2489 N  N   . ASP   B 1 106 ? -4.09335  16.00834  33.41249  1.000 15.42386 ?  118 ASP   B N   1 
ATOM   2490 C  CA  . ASP   B 1 106 ? -4.42510  16.69395  32.16892  1.000 16.37208 ?  118 ASP   B CA  1 
ATOM   2491 C  C   . ASP   B 1 106 ? -3.71542  16.10694  30.95411  1.000 14.97828 ?  118 ASP   B C   1 
ATOM   2492 O  O   . ASP   B 1 106 ? -4.03669  16.49462  29.82469  1.000 17.87496 ?  118 ASP   B O   1 
ATOM   2493 C  CB  . ASP   B 1 106 ? -4.26683  18.22324  32.24633  1.000 18.34281 ?  118 ASP   B CB  1 
ATOM   2494 C  CG  . ASP   B 1 106 ? -2.83560  18.68072  32.49737  1.000 15.34195 ?  118 ASP   B CG  1 
ATOM   2495 O  OD1 . ASP   B 1 106 ? -1.93800  17.84823  32.74240  1.000 18.43362 ?  118 ASP   B OD1 1 
ATOM   2496 O  OD2 . ASP   B 1 106 ? -2.61338  19.89990  32.40550  1.000 14.87754 ?  118 ASP   B OD2 1 
ATOM   2497 N  N   . ARG   B 1 107 ? -2.77313  15.18811  31.16283  1.000 13.14915 ?  119 ARG   B N   1 
ATOM   2498 C  CA  . ARG   B 1 107 ? -2.05806  14.53244  30.07593  1.000 11.49850 ?  119 ARG   B CA  1 
ATOM   2499 C  C   . ARG   B 1 107 ? -2.38673  13.05419  29.92001  1.000 11.26132 ?  119 ARG   B C   1 
ATOM   2500 O  O   . ARG   B 1 107 ? -2.32455  12.54488  28.80269  1.000 11.04155 ?  119 ARG   B O   1 
ATOM   2501 C  CB  . ARG   B 1 107 ? -0.53572  14.65029  30.25793  1.000 11.01641 ?  119 ARG   B CB  1 
ATOM   2502 C  CG  . ARG   B 1 107 ? -0.01394  16.03000  30.64209  1.000 11.65599 ?  119 ARG   B CG  1 
ATOM   2503 C  CD  . ARG   B 1 107 ? -0.11172  16.98797  29.47417  1.000 14.92016 ?  119 ARG   B CD  1 
ATOM   2504 N  NE  . ARG   B 1 107 ? -0.98750  18.12270  29.75224  1.000 13.32538 ?  119 ARG   B NE  1 
ATOM   2505 C  CZ  . ARG   B 1 107 ? -1.40169  18.96860  28.82018  1.000 15.39415 ?  119 ARG   B CZ  1 
ATOM   2506 N  NH1 . ARG   B 1 107 ? -1.02842  18.83549  27.55757  1.000 18.22629 ?  119 ARG   B NH1 1 
ATOM   2507 N  NH2 . ARG   B 1 107 ? -2.20804  19.96908  29.15851  1.000 20.23239 ?  119 ARG   B NH2 1 
ATOM   2508 N  N   . VAL   B 1 108 ? -2.71990  12.35079  31.00324  1.000 10.32972 ?  120 VAL   B N   1 
ATOM   2509 C  CA  . VAL   B 1 108 ? -3.05620  10.92716  30.94952  1.000 11.84901 ?  120 VAL   B CA  1 
ATOM   2510 C  C   . VAL   B 1 108 ? -4.51424  10.65424  31.25693  1.000 13.06350 ?  120 VAL   B C   1 
ATOM   2511 O  O   . VAL   B 1 108 ? -4.97737  9.52881   31.00593  1.000 12.06795 ?  120 VAL   B O   1 
ATOM   2512 C  CB  . VAL   B 1 108 ? -2.16302  10.07058  31.87282  1.000 11.24815 ?  120 VAL   B CB  1 
ATOM   2513 C  CG1 . VAL   B 1 108 ? -0.69083  10.22918  31.51653  1.000 13.32224 ?  120 VAL   B CG1 1 
ATOM   2514 C  CG2 . VAL   B 1 108 ? -2.40075  10.43002  33.35528  1.000 12.80412 ?  120 VAL   B CG2 1 
ATOM   2515 N  N   . GLY   B 1 109 ? -5.24499  11.61843  31.79904  1.000 12.53350 ?  121 GLY   B N   1 
ATOM   2516 C  CA  . GLY   B 1 109 ? -6.64656  11.37335  32.10107  1.000 13.48073 ?  121 GLY   B CA  1 
ATOM   2517 C  C   . GLY   B 1 109 ? -7.41328  11.22964  30.80955  1.000 14.17033 ?  121 GLY   B C   1 
ATOM   2518 O  O   . GLY   B 1 109 ? -7.52056  12.18836  30.04400  1.000 15.27871 ?  121 GLY   B O   1 
ATOM   2519 N  N   . GLY   B 1 110 ? -7.91520  10.02922  30.53774  1.000 13.74525 ?  122 GLY   B N   1 
ATOM   2520 C  CA  . GLY   B 1 110 ? -8.48108  9.72036   29.23588  1.000 15.63516 ?  122 GLY   B CA  1 
ATOM   2521 C  C   . GLY   B 1 110 ? -7.73819  8.64545   28.48052  1.000 13.98027 ?  122 GLY   B C   1 
ATOM   2522 O  O   . GLY   B 1 110 ? -8.21121  8.22480   27.41482  1.000 14.86666 ?  122 GLY   B O   1 
ATOM   2523 N  N   . VAL   B 1 111 ? -6.60330  8.17259   29.00547  1.000 13.15134 ?  123 VAL   B N   1 
ATOM   2524 C  CA  . VAL   B 1 111 ? -5.84439  7.09138   28.38822  1.000 12.68783 ?  123 VAL   B CA  1 
ATOM   2525 C  C   . VAL   B 1 111 ? -6.69249  5.83334   28.25590  1.000 17.24834 ?  123 VAL   B C   1 
ATOM   2526 O  O   . VAL   B 1 111 ? -6.59292  5.10709   27.25913  1.000 16.90690 ?  123 VAL   B O   1 
ATOM   2527 C  CB  . VAL   B 1 111 ? -4.53042  6.86263   29.16496  1.000 13.84605 ?  123 VAL   B CB  1 
ATOM   2528 C  CG1 . VAL   B 1 111 ? -4.01662  5.42607   29.04713  1.000 14.78785 ?  123 VAL   B CG1 1 
ATOM   2529 C  CG2 . VAL   B 1 111 ? -3.47274  7.84893   28.65978  1.000 12.90469 ?  123 VAL   B CG2 1 
ATOM   2530 N  N   . ASP   B 1 112 ? -7.55382  5.56116   29.24537  1.000 15.88231 ?  124 ASP   B N   1 
ATOM   2531 C  CA  . ASP   B 1 112 ? -8.37320  4.35484   29.15449  1.000 18.27193 ?  124 ASP   B CA  1 
ATOM   2532 C  C   . ASP   B 1 112 ? -9.35933  4.45226   27.99403  1.000 14.79420 ?  124 ASP   B C   1 
ATOM   2533 O  O   . ASP   B 1 112 ? -9.57267  3.47038   27.27133  1.000 16.98953 ?  124 ASP   B O   1 
ATOM   2534 C  CB  . ASP   B 1 112 ? -9.10150  4.08301   30.47816  1.000 16.86156 ?  124 ASP   B CB  1 
ATOM   2535 C  CG  . ASP   B 1 112 ? -8.15242  3.70046   31.62071  1.000 21.38967 ?  124 ASP   B CG  1 
ATOM   2536 O  OD1 . ASP   B 1 112 ? -6.94050  3.48918   31.39535  1.000 21.44956 ?  124 ASP   B OD1 1 
ATOM   2537 O  OD2 . ASP   B 1 112 ? -8.63122  3.58528   32.76731  1.000 24.86014 ?  124 ASP   B OD2 1 
ATOM   2538 N  N   . VAL   B 1 113 ? -9.94830  5.63409   27.78803  1.000 14.56799 ?  125 VAL   B N   1 
ATOM   2539 C  CA  . VAL   B 1 113 ? -10.83851 5.85603   26.64800  1.000 12.51882 ?  125 VAL   B CA  1 
ATOM   2540 C  C   . VAL   B 1 113 ? -10.09165 5.63901   25.33607  1.000 20.10884 ?  125 VAL   B C   1 
ATOM   2541 O  O   . VAL   B 1 113 ? -10.58153 4.95995   24.42353  1.000 20.30707 ?  125 VAL   B O   1 
ATOM   2542 C  CB  . VAL   B 1 113 ? -11.47331 7.25730   26.72956  1.000 14.95157 ?  125 VAL   B CB  1 
ATOM   2543 C  CG1 . VAL   B 1 113 ? -12.02230 7.69263   25.36603  1.000 19.51838 ?  125 VAL   B CG1 1 
ATOM   2544 C  CG2 . VAL   B 1 113 ? -12.57558 7.29379   27.79210  1.000 19.79262 ?  125 VAL   B CG2 1 
ATOM   2545 N  N   . LEU   B 1 114 ? -8.89249  6.22028   25.21825  1.000 18.80744 ?  126 LEU   B N   1 
ATOM   2546 C  CA  . LEU   B 1 114 ? -8.08457  6.01383   24.01989  1.000 17.56177 ?  126 LEU   B CA  1 
ATOM   2547 C  C   . LEU   B 1 114 ? -7.83123  4.53119   23.77734  1.000 15.24878 ?  126 LEU   B C   1 
ATOM   2548 O  O   . LEU   B 1 114 ? -8.03025  4.02940   22.66260  1.000 17.03420 ?  126 LEU   B O   1 
ATOM   2549 C  CB  . LEU   B 1 114 ? -6.75847  6.77813   24.13372  1.000 15.03582 ?  126 LEU   B CB  1 
ATOM   2550 C  CG  . LEU   B 1 114 ? -6.81625  8.29879   24.19601  1.000 13.06882 ?  126 LEU   B CG  1 
ATOM   2551 C  CD1 . LEU   B 1 114 ? -5.39414  8.85526   24.34061  1.000 15.68705 ?  126 LEU   B CD1 1 
ATOM   2552 C  CD2 . LEU   B 1 114 ? -7.45700  8.84533   22.93119  1.000 14.19188 ?  126 LEU   B CD2 1 
ATOM   2553 N  N   . ARG   B 1 115 ? -7.41087  3.80683   24.81619  1.000 16.94444 ?  127 ARG   B N   1 
ATOM   2554 C  CA  . ARG   B 1 115 ? -7.08528  2.39493   24.65201  1.000 15.72314 ?  127 ARG   B CA  1 
ATOM   2555 C  C   . ARG   B 1 115 ? -8.31135  1.58666   24.23094  1.000 17.70984 ?  127 ARG   B C   1 
ATOM   2556 O  O   . ARG   B 1 115 ? -8.21508  0.69449   23.37683  1.000 19.16350 ?  127 ARG   B O   1 
ATOM   2557 C  CB  . ARG   B 1 115 ? -6.50122  1.85260   25.95490  1.000 19.20902 ?  127 ARG   B CB  1 
ATOM   2558 C  CG  . ARG   B 1 115 ? -6.19442  0.38189   25.90993  1.000 19.62944 ?  127 ARG   B CG  1 
ATOM   2559 C  CD  . ARG   B 1 115 ? -5.77891  -0.14246  27.25528  1.000 19.41973 ?  127 ARG   B CD  1 
ATOM   2560 N  NE  . ARG   B 1 115 ? -4.69281  0.62241   27.85607  1.000 19.05378 ?  127 ARG   B NE  1 
ATOM   2561 C  CZ  . ARG   B 1 115 ? -4.81805  1.40789   28.91661  1.000 21.34325 ?  127 ARG   B CZ  1 
ATOM   2562 N  NH1 . ARG   B 1 115 ? -5.99038  1.61170   29.49451  1.000 22.68134 ?  127 ARG   B NH1 1 
ATOM   2563 N  NH2 . ARG   B 1 115 ? -3.73758  2.00993   29.40618  1.000 24.74873 ?  127 ARG   B NH2 1 
ATOM   2564 N  N   . ALA   B 1 116 ? -9.46699  1.88243   24.82151  1.000 19.02597 ?  128 ALA   B N   1 
ATOM   2565 C  CA  . ALA   B 1 116 ? -10.68895 1.17553   24.44556  1.000 21.53241 ?  128 ALA   B CA  1 
ATOM   2566 C  C   . ALA   B 1 116 ? -11.05976 1.44936   22.99888  1.000 26.13475 ?  128 ALA   B C   1 
ATOM   2567 O  O   . ALA   B 1 116 ? -11.70840 0.61678   22.35564  1.000 25.02031 ?  128 ALA   B O   1 
ATOM   2568 C  CB  . ALA   B 1 116 ? -11.83116 1.59618   25.36981  1.000 23.17559 ?  128 ALA   B CB  1 
ATOM   2569 N  N   . ALA   B 1 117 ? -10.65444 2.60160   22.46832  1.000 22.39950 ?  129 ALA   B N   1 
ATOM   2570 C  CA  . ALA   B 1 117 ? -10.92630 2.94083   21.07939  1.000 18.51322 ?  129 ALA   B CA  1 
ATOM   2571 C  C   . ALA   B 1 117 ? -9.90108  2.36218   20.11770  1.000 20.97448 ?  129 ALA   B C   1 
ATOM   2572 O  O   . ALA   B 1 117 ? -9.98814  2.63282   18.91490  1.000 28.09363 ?  129 ALA   B O   1 
ATOM   2573 C  CB  . ALA   B 1 117 ? -11.01688 4.45945   20.91599  1.000 22.32071 ?  129 ALA   B CB  1 
ATOM   2574 N  N   . GLY   B 1 118 ? -8.94406  1.57714   20.60514  1.000 18.88461 ?  130 GLY   B N   1 
ATOM   2575 C  CA  . GLY   B 1 118 ? -7.94446  0.95782   19.76170  1.000 18.68820 ?  130 GLY   B CA  1 
ATOM   2576 C  C   . GLY   B 1 118 ? -6.65582  1.73650   19.60827  1.000 19.02674 ?  130 GLY   B C   1 
ATOM   2577 O  O   . GLY   B 1 118 ? -5.79867  1.32800   18.81499  1.000 16.44360 ?  130 GLY   B O   1 
ATOM   2578 N  N   . VAL   B 1 119 ? -6.48349  2.82917   20.35348  1.000 16.78580 ?  131 VAL   B N   1 
ATOM   2579 C  CA  . VAL   B 1 119 ? -5.27280  3.64036   20.25487  1.000 17.08947 ?  131 VAL   B CA  1 
ATOM   2580 C  C   . VAL   B 1 119 ? -4.17022  2.99309   21.07732  1.000 12.49803 ?  131 VAL   B C   1 
ATOM   2581 O  O   . VAL   B 1 119 ? -4.39369  2.59275   22.22439  1.000 15.23887 ?  131 VAL   B O   1 
ATOM   2582 C  CB  . VAL   B 1 119 ? -5.53264  5.06371   20.75869  1.000 13.77658 ?  131 VAL   B CB  1 
ATOM   2583 C  CG1 . VAL   B 1 119 ? -4.24126  5.89121   20.67120  1.000 12.32916 ?  131 VAL   B CG1 1 
ATOM   2584 C  CG2 . VAL   B 1 119 ? -6.67335  5.71703   19.99831  1.000 15.18198 ?  131 VAL   B CG2 1 
ATOM   2585 N  N   . ALA   B 1 120 ? -2.98255  2.89948   20.49690  1.000 12.35706 ?  132 ALA   B N   1 
ATOM   2586 C  CA  . ALA   B 1 120 ? -1.80130  2.43914   21.22094  1.000 10.87398 ?  132 ALA   B CA  1 
ATOM   2587 C  C   . ALA   B 1 120 ? -1.22176  3.62179   21.98958  1.000 13.05478 ?  132 ALA   B C   1 
ATOM   2588 O  O   . ALA   B 1 120 ? -0.71896  4.57286   21.38039  1.000 12.16518 ?  132 ALA   B O   1 
ATOM   2589 C  CB  . ALA   B 1 120 ? -0.78526  1.85427   20.24612  1.000 15.51703 ?  132 ALA   B CB  1 
ATOM   2590 N  N   . THR   B 1 121 ? -1.29954  3.58167   23.31954  1.000 10.89782 ?  133 THR   B N   1 
ATOM   2591 C  CA  . THR   B 1 121 ? -0.89684  4.71096   24.15374  1.000 11.48272 ?  133 THR   B CA  1 
ATOM   2592 C  C   . THR   B 1 121 ? 0.52886   4.53120   24.65949  1.000 12.41283 ?  133 THR   B C   1 
ATOM   2593 O  O   . THR   B 1 121 ? 0.94410   3.42151   25.01142  1.000 12.46145 ?  133 THR   B O   1 
ATOM   2594 C  CB  . THR   B 1 121 ? -1.85287  4.85893   25.33563  1.000 10.43865 ?  133 THR   B CB  1 
ATOM   2595 O  OG1 . THR   B 1 121 ? -1.87804  3.63828   26.09567  1.000 11.98110 ?  133 THR   B OG1 1 
ATOM   2596 C  CG2 . THR   B 1 121 ? -3.26415  5.20582   24.85001  1.000 12.80325 ?  133 THR   B CG2 1 
ATOM   2597 N  N   . TYR   B 1 122 ? 1.28056   5.64034   24.70211  1.000 11.21455 ?  134 TYR   B N   1 
ATOM   2598 C  CA  . TYR   B 1 122 ? 2.70585   5.61046   25.00493  1.000 9.77552  ?  134 TYR   B CA  1 
ATOM   2599 C  C   . TYR   B 1 122 ? 3.07309   6.70327   25.99585  1.000 9.36865  ?  134 TYR   B C   1 
ATOM   2600 O  O   . TYR   B 1 122 ? 2.45316   7.77118   26.02032  1.000 10.04715 ?  134 TYR   B O   1 
ATOM   2601 C  CB  . TYR   B 1 122 ? 3.53664   5.92177   23.75784  1.000 9.97417  ?  134 TYR   B CB  1 
ATOM   2602 C  CG  . TYR   B 1 122 ? 3.61012   4.80558   22.73159  1.000 10.28458 ?  134 TYR   B CG  1 
ATOM   2603 C  CD1 . TYR   B 1 122 ? 2.52298   4.51597   21.91234  1.000 13.00929 ?  134 TYR   B CD1 1 
ATOM   2604 C  CD2 . TYR   B 1 122 ? 4.77725   4.08886   22.55344  1.000 13.03392 ?  134 TYR   B CD2 1 
ATOM   2605 C  CE1 . TYR   B 1 122 ? 2.59443   3.49412   20.96379  1.000 15.43069 ?  134 TYR   B CE1 1 
ATOM   2606 C  CE2 . TYR   B 1 122 ? 4.85831   3.06680   21.61524  1.000 15.15336 ?  134 TYR   B CE2 1 
ATOM   2607 C  CZ  . TYR   B 1 122 ? 3.75921   2.78538   20.83085  1.000 15.93691 ?  134 TYR   B CZ  1 
ATOM   2608 O  OH  . TYR   B 1 122 ? 3.84215   1.77006   19.90045  1.000 19.08904 ?  134 TYR   B OH  1 
ATOM   2609 N  N   . ALA   B 1 123 ? 4.10769   6.42345   26.79078  1.000 8.80272  ?  135 ALA   B N   1 
ATOM   2610 C  CA  . ALA   B 1 123 ? 4.74684   7.41623   27.65047  1.000 10.21024 ?  135 ALA   B CA  1 
ATOM   2611 C  C   . ALA   B 1 123 ? 6.12536   6.89445   28.02066  1.000 12.95132 ?  135 ALA   B C   1 
ATOM   2612 O  O   . ALA   B 1 123 ? 6.43249   5.72186   27.82283  1.000 12.89872 ?  135 ALA   B O   1 
ATOM   2613 C  CB  . ALA   B 1 123 ? 3.92615   7.69063   28.91646  1.000 9.76562  ?  135 ALA   B CB  1 
ATOM   2614 N  N   . SER   B 1 124 ? 6.96520   7.76216   28.56101  1.000 9.58847  ?  136 SER   B N   1 
ATOM   2615 C  CA  . SER   B 1 124 ? 8.26033   7.28417   29.01652  1.000 9.74927  ?  136 SER   B CA  1 
ATOM   2616 C  C   . SER   B 1 124 ? 8.07744   6.37585   30.22912  1.000 11.16266 ?  136 SER   B C   1 
ATOM   2617 O  O   . SER   B 1 124 ? 7.06272   6.45860   30.94236  1.000 11.20618 ?  136 SER   B O   1 
ATOM   2618 C  CB  . SER   B 1 124 ? 9.15439   8.45450   29.41229  1.000 11.08782 ?  136 SER   B CB  1 
ATOM   2619 O  OG  . SER   B 1 124 ? 8.66876   9.04790   30.60343  1.000 11.02241 ?  136 SER   B OG  1 
ATOM   2620 N  N   . PRO   B 1 125 ? 9.06896   5.52583   30.51234  1.000 10.81117 ?  137 PRO   B N   1 
ATOM   2621 C  CA  . PRO   B 1 125 ? 8.99490   4.72990   31.74710  1.000 13.28908 ?  137 PRO   B CA  1 
ATOM   2622 C  C   . PRO   B 1 125 ? 8.82674   5.58685   32.98088  1.000 13.16646 ?  137 PRO   B C   1 
ATOM   2623 O  O   . PRO   B 1 125 ? 8.09102   5.21188   33.89679  1.000 14.06749 ?  137 PRO   B O   1 
ATOM   2624 C  CB  . PRO   B 1 125 ? 10.32420  3.96647   31.74556  1.000 15.00073 ?  137 PRO   B CB  1 
ATOM   2625 C  CG  . PRO   B 1 125 ? 10.63340  3.81539   30.29125  1.000 14.62022 ?  137 PRO   B CG  1 
ATOM   2626 C  CD  . PRO   B 1 125 ? 10.21444  5.13084   29.67585  1.000 12.53505 ?  137 PRO   B CD  1 
ATOM   2627 N  N   . SER   B 1 126 ? 9.48843   6.74188   33.02148  1.000 12.33234 ?  138 SER   B N   1 
ATOM   2628 C  CA  A SER   B 1 126 ? 9.33568   7.65055   34.15356  0.761 15.00850 ?  138 SER   B CA  1 
ATOM   2629 C  CA  B SER   B 1 126 ? 9.33383   7.63402   34.16370  0.239 15.05078 ?  138 SER   B CA  1 
ATOM   2630 C  C   . SER   B 1 126 ? 7.89794   8.12633   34.29102  1.000 10.62607 ?  138 SER   B C   1 
ATOM   2631 O  O   . SER   B 1 126 ? 7.34190   8.14126   35.39349  1.000 13.95583 ?  138 SER   B O   1 
ATOM   2632 C  CB  A SER   B 1 126 ? 10.26304  8.84629   33.98535  0.761 17.96815 ?  138 SER   B CB  1 
ATOM   2633 C  CB  B SER   B 1 126 ? 10.31632  8.79907   34.06700  0.239 17.95174 ?  138 SER   B CB  1 
ATOM   2634 O  OG  A SER   B 1 126 ? 10.12558  9.72483   35.08490  0.761 22.29049 ?  138 SER   B OG  1 
ATOM   2635 O  OG  B SER   B 1 126 ? 10.03555  9.61039   32.94567  0.239 15.43553 ?  138 SER   B OG  1 
ATOM   2636 N  N   . THR   B 1 127 ? 7.27344   8.51913   33.17394  1.000 10.60926 ?  139 THR   B N   1 
ATOM   2637 C  CA  . THR   B 1 127 ? 5.88692   8.96365   33.23615  1.000 14.14137 ?  139 THR   B CA  1 
ATOM   2638 C  C   . THR   B 1 127 ? 4.97614   7.83785   33.70537  1.000 9.89131  ?  139 THR   B C   1 
ATOM   2639 O  O   . THR   B 1 127 ? 4.08065   8.05694   34.52943  1.000 11.05407 ?  139 THR   B O   1 
ATOM   2640 C  CB  . THR   B 1 127 ? 5.45215   9.50782   31.87904  1.000 9.91943  ?  139 THR   B CB  1 
ATOM   2641 O  OG1 . THR   B 1 127 ? 6.19339   10.71275  31.60697  1.000 8.78223  ?  139 THR   B OG1 1 
ATOM   2642 C  CG2 . THR   B 1 127 ? 3.95761   9.83856   31.86917  1.000 12.38215 ?  139 THR   B CG2 1 
ATOM   2643 N  N   . ARG   B 1 128 ? 5.18965   6.62222   33.19702  1.000 11.56526 ?  140 ARG   B N   1 
ATOM   2644 C  CA  . ARG   B 1 128 ? 4.33910   5.50081   33.59328  1.000 13.89613 ?  140 ARG   B CA  1 
ATOM   2645 C  C   . ARG   B 1 128 ? 4.48724   5.19511   35.07595  1.000 13.92764 ?  140 ARG   B C   1 
ATOM   2646 O  O   . ARG   B 1 128 ? 3.49705   4.92797   35.76178  1.000 14.70958 ?  140 ARG   B O   1 
ATOM   2647 C  CB  . ARG   B 1 128 ? 4.68743   4.27112   32.76112  1.000 12.38180 ?  140 ARG   B CB  1 
ATOM   2648 C  CG  . ARG   B 1 128 ? 4.41105   4.45003   31.27060  1.000 14.24617 ?  140 ARG   B CG  1 
ATOM   2649 C  CD  . ARG   B 1 128 ? 4.81073   3.21278   30.47733  1.000 15.77260 ?  140 ARG   B CD  1 
ATOM   2650 N  NE  . ARG   B 1 128 ? 3.89916   2.09425   30.71392  1.000 16.86875 ?  140 ARG   B NE  1 
ATOM   2651 C  CZ  . ARG   B 1 128 ? 4.17738   1.01371   31.43056  1.000 21.50455 ?  140 ARG   B CZ  1 
ATOM   2652 N  NH1 . ARG   B 1 128 ? 5.36259   0.83895   31.99303  1.000 23.56837 ?  140 ARG   B NH1 1 
ATOM   2653 N  NH2 . ARG   B 1 128 ? 3.24242   0.07657   31.57765  1.000 31.15641 ?  140 ARG   B NH2 1 
ATOM   2654 N  N   . ARG   B 1 129 ? 5.72019   5.24417   35.57627  1.000 13.89070 ?  141 ARG   B N   1 
ATOM   2655 C  CA  A ARG   B 1 129 ? 5.96869   4.98248   36.99025  0.451 15.92257 ?  141 ARG   B CA  1 
ATOM   2656 C  CA  B ARG   B 1 129 ? 6.00673   4.99907   36.98567  0.549 15.92463 ?  141 ARG   B CA  1 
ATOM   2657 C  C   . ARG   B 1 129 ? 5.30916   6.03641   37.86538  1.000 15.71695 ?  141 ARG   B C   1 
ATOM   2658 O  O   . ARG   B 1 129 ? 4.60570   5.70159   38.83089  1.000 16.14183 ?  141 ARG   B O   1 
ATOM   2659 C  CB  A ARG   B 1 129 ? 7.47036   4.92514   37.26341  0.451 17.58315 ?  141 ARG   B CB  1 
ATOM   2660 C  CB  B ARG   B 1 129 ? 7.54146   5.02838   37.11480  0.549 17.65820 ?  141 ARG   B CB  1 
ATOM   2661 C  CG  A ARG   B 1 129 ? 7.82713   4.69537   38.72599  0.451 22.15544 ?  141 ARG   B CG  1 
ATOM   2662 C  CG  B ARG   B 1 129 ? 8.21266   5.20997   38.46090  0.549 24.93983 ?  141 ARG   B CG  1 
ATOM   2663 C  CD  A ARG   B 1 129 ? 9.33739   4.68945   38.90470  0.451 20.00267 ?  141 ARG   B CD  1 
ATOM   2664 C  CD  B ARG   B 1 129 ? 9.72714   5.58056   38.27849  0.549 22.44170 ?  141 ARG   B CD  1 
ATOM   2665 N  NE  A ARG   B 1 129 ? 9.95093   5.84227   38.25552  0.451 22.61955 ?  141 ARG   B NE  1 
ATOM   2666 N  NE  B ARG   B 1 129 ? 10.44642  4.76405   37.29273  0.549 23.30918 ?  141 ARG   B NE  1 
ATOM   2667 C  CZ  A ARG   B 1 129 ? 9.98241   7.06810   38.76087  0.451 16.75710 ?  141 ARG   B CZ  1 
ATOM   2668 C  CZ  B ARG   B 1 129 ? 11.37770  5.20939   36.44973  0.549 21.53184 ?  141 ARG   B CZ  1 
ATOM   2669 N  NH1 A ARG   B 1 129 ? 9.55412   7.32272   39.98653  0.451 19.34469 ?  141 ARG   B NH1 1 
ATOM   2670 N  NH1 B ARG   B 1 129 ? 11.76559  6.47875   36.43735  0.549 16.17138 ?  141 ARG   B NH1 1 
ATOM   2671 N  NH2 A ARG   B 1 129 ? 10.46145  8.06250   38.01894  0.451 19.37340 ?  141 ARG   B NH2 1 
ATOM   2672 N  NH2 B ARG   B 1 129 ? 11.94203  4.35850   35.59649  0.549 19.30267 ?  141 ARG   B NH2 1 
ATOM   2673 N  N   . LEU   B 1 130 ? 5.47238   7.31282   37.52037  1.000 13.59150 ?  142 LEU   B N   1 
ATOM   2674 C  CA  . LEU   B 1 130 ? 4.87443   8.37866   38.31491  1.000 13.48180 ?  142 LEU   B CA  1 
ATOM   2675 C  C   . LEU   B 1 130 ? 3.35292   8.34817   38.24708  1.000 14.51005 ?  142 LEU   B C   1 
ATOM   2676 O  O   . LEU   B 1 130 ? 2.68053   8.63688   39.24372  1.000 13.34598 ?  142 LEU   B O   1 
ATOM   2677 C  CB  . LEU   B 1 130 ? 5.42518   9.73612   37.86048  1.000 12.78329 ?  142 LEU   B CB  1 
ATOM   2678 C  CG  . LEU   B 1 130 ? 6.89639   9.95601   38.22128  1.000 13.42628 ?  142 LEU   B CG  1 
ATOM   2679 C  CD1 . LEU   B 1 130 ? 7.53825   11.02792  37.33236  1.000 14.37122 ?  142 LEU   B CD1 1 
ATOM   2680 C  CD2 . LEU   B 1 130 ? 7.06171   10.29007  39.71788  1.000 17.67890 ?  142 LEU   B CD2 1 
ATOM   2681 N  N   . ALA   B 1 131 ? 2.78736   8.03263   37.08021  1.000 11.89423 ?  143 ALA   B N   1 
ATOM   2682 C  CA  . ALA   B 1 131 ? 1.33286   7.94277   36.98008  1.000 11.99853 ?  143 ALA   B CA  1 
ATOM   2683 C  C   . ALA   B 1 131 ? 0.80278   6.82394   37.86563  1.000 13.54350 ?  143 ALA   B C   1 
ATOM   2684 O  O   . ALA   B 1 131 ? -0.21851  6.99293   38.54608  1.000 13.74875 ?  143 ALA   B O   1 
ATOM   2685 C  CB  . ALA   B 1 131 ? 0.91826   7.72261   35.52151  1.000 13.96260 ?  143 ALA   B CB  1 
ATOM   2686 N  N   . GLU   B 1 132 ? 1.48686   5.68288   37.87902  1.000 13.37242 ?  144 GLU   B N   1 
ATOM   2687 C  CA  . GLU   B 1 132 ? 1.06423   4.57756   38.73862  1.000 14.67717 ?  144 GLU   B CA  1 
ATOM   2688 C  C   . GLU   B 1 132 ? 1.10275   4.96923   40.21324  1.000 16.90873 ?  144 GLU   B C   1 
ATOM   2689 O  O   . GLU   B 1 132 ? 0.17477   4.65847   40.96978  1.000 19.53163 ?  144 GLU   B O   1 
ATOM   2690 C  CB  . GLU   B 1 132 ? 1.93016   3.34305   38.48644  1.000 15.14574 ?  144 GLU   B CB  1 
ATOM   2691 C  CG  . GLU   B 1 132 ? 1.42107   2.10151   39.25525  1.000 20.99581 ?  144 GLU   B CG  1 
ATOM   2692 C  CD  . GLU   B 1 132 ? 2.26012   0.85776   39.01530  1.000 31.42314 ?  144 GLU   B CD  1 
ATOM   2693 O  OE1 . GLU   B 1 132 ? 3.44815   0.98450   38.65499  1.000 39.92064 ?  144 GLU   B OE1 1 
ATOM   2694 O  OE2 . GLU   B 1 132 ? 1.71735   -0.25592  39.17077  1.000 36.97694 ?  144 GLU   B OE2 1 
ATOM   2695 N  N   . VAL   B 1 133 ? 2.17263   5.63627   40.64611  1.000 18.54222 ?  145 VAL   B N   1 
ATOM   2696 C  CA  . VAL   B 1 133 ? 2.26438   6.05462   42.04110  1.000 18.02949 ?  145 VAL   B CA  1 
ATOM   2697 C  C   . VAL   B 1 133 ? 1.13320   7.01265   42.38524  1.000 19.89407 ?  145 VAL   B C   1 
ATOM   2698 O  O   . VAL   B 1 133 ? 0.54306   6.93757   43.47089  1.000 20.63330 ?  145 VAL   B O   1 
ATOM   2699 C  CB  . VAL   B 1 133 ? 3.65152   6.65999   42.33425  1.000 19.05122 ?  145 VAL   B CB  1 
ATOM   2700 C  CG1 . VAL   B 1 133 ? 3.69353   7.23868   43.74741  1.000 27.13014 ?  145 VAL   B CG1 1 
ATOM   2701 C  CG2 . VAL   B 1 133 ? 4.73094   5.59883   42.14295  1.000 22.82052 ?  145 VAL   B CG2 1 
ATOM   2702 N  N   . GLU   B 1 134 ? 0.78713   7.90025   41.45235  1.000 16.17799 ?  146 GLU   B N   1 
ATOM   2703 C  CA  . GLU   B 1 134 ? -0.22241  8.92887   41.67699  1.000 17.77786 ?  146 GLU   B CA  1 
ATOM   2704 C  C   . GLU   B 1 134 ? -1.64371  8.37865   41.65299  1.000 23.11349 ?  146 GLU   B C   1 
ATOM   2705 O  O   . GLU   B 1 134 ? -2.56424  9.05153   42.13332  1.000 24.66879 ?  146 GLU   B O   1 
ATOM   2706 C  CB  . GLU   B 1 134 ? -0.08749  10.00793  40.59560  1.000 16.63433 ?  146 GLU   B CB  1 
ATOM   2707 C  CG  . GLU   B 1 134 ? -0.71279  11.33632  40.93161  1.000 24.17232 ?  146 GLU   B CG  1 
ATOM   2708 C  CD  . GLU   B 1 134 ? -0.14401  11.92540  42.19516  1.000 30.49368 ?  146 GLU   B CD  1 
ATOM   2709 O  OE1 . GLU   B 1 134 ? 1.08445   11.79489  42.40268  1.000 31.15590 ?  146 GLU   B OE1 1 
ATOM   2710 O  OE2 . GLU   B 1 134 ? -0.92252  12.51126  42.96988  1.000 41.39767 ?  146 GLU   B OE2 1 
ATOM   2711 N  N   . GLY   B 1 135 ? -1.84567  7.18587   41.10442  1.000 17.41503 ?  147 GLY   B N   1 
ATOM   2712 C  CA  . GLY   B 1 135 ? -3.18903  6.69164   40.86945  1.000 16.97159 ?  147 GLY   B CA  1 
ATOM   2713 C  C   . GLY   B 1 135 ? -3.81882  7.16260   39.58085  1.000 19.62695 ?  147 GLY   B C   1 
ATOM   2714 O  O   . GLY   B 1 135 ? -5.04208  7.08161   39.43428  1.000 21.19777 ?  147 GLY   B O   1 
ATOM   2715 N  N   . ASN   B 1 136 ? -3.02034  7.65569   38.63771  1.000 16.96736 ?  148 ASN   B N   1 
ATOM   2716 C  CA  . ASN   B 1 136 ? -3.52995  8.11694   37.35728  1.000 16.85540 ?  148 ASN   B CA  1 
ATOM   2717 C  C   . ASN   B 1 136 ? -3.50810  6.98407   36.33720  1.000 15.40207 ?  148 ASN   B C   1 
ATOM   2718 O  O   . ASN   B 1 136 ? -2.87300  5.95194   36.52842  1.000 16.42507 ?  148 ASN   B O   1 
ATOM   2719 C  CB  . ASN   B 1 136 ? -2.69761  9.29445   36.84124  1.000 16.66765 ?  148 ASN   B CB  1 
ATOM   2720 C  CG  . ASN   B 1 136 ? -2.87016  10.53274  37.68619  1.000 17.54000 ?  148 ASN   B CG  1 
ATOM   2721 O  OD1 . ASN   B 1 136 ? -3.80100  10.61441  38.49429  1.000 19.36995 ?  148 ASN   B OD1 1 
ATOM   2722 N  ND2 . ASN   B 1 136 ? -2.00856  11.51865  37.49126  1.000 16.15816 ?  148 ASN   B ND2 1 
ATOM   2723 N  N   . GLU   B 1 137 ? -4.22073  7.19308   35.23441  1.000 15.60445 ?  149 GLU   B N   1 
ATOM   2724 C  CA  . GLU   B 1 137 ? -4.19975  6.21802   34.15836  1.000 14.10162 ?  149 GLU   B CA  1 
ATOM   2725 C  C   . GLU   B 1 137 ? -2.79144  6.11370   33.58363  1.000 15.05371 ?  149 GLU   B C   1 
ATOM   2726 O  O   . GLU   B 1 137 ? -2.03191  7.08857   33.55867  1.000 14.53313 ?  149 GLU   B O   1 
ATOM   2727 C  CB  . GLU   B 1 137 ? -5.19617  6.63560   33.08456  1.000 15.36973 ?  149 GLU   B CB  1 
ATOM   2728 C  CG  . GLU   B 1 137 ? -6.64870  6.48131   33.54928  1.000 14.34825 ?  149 GLU   B CG  1 
ATOM   2729 C  CD  . GLU   B 1 137 ? -7.58730  7.39515   32.79974  1.000 19.72605 ?  149 GLU   B CD  1 
ATOM   2730 O  OE1 . GLU   B 1 137 ? -7.87415  7.11767   31.62195  1.000 19.02494 ?  149 GLU   B OE1 1 
ATOM   2731 O  OE2 . GLU   B 1 137 ? -8.03929  8.40245   33.38396  1.000 24.39218 ?  149 GLU   B OE2 1 
ATOM   2732 N  N   . ILE   B 1 138 ? -2.44335  4.90936   33.14055  1.000 14.95259 ?  150 ILE   B N   1 
ATOM   2733 C  CA  . ILE   B 1 138 ? -1.07376  4.55471   32.78106  1.000 12.77858 ?  150 ILE   B CA  1 
ATOM   2734 C  C   . ILE   B 1 138 ? -0.99418  4.18112   31.30860  1.000 16.90356 ?  150 ILE   B C   1 
ATOM   2735 O  O   . ILE   B 1 138 ? -1.50977  3.12649   30.90418  1.000 13.91808 ?  150 ILE   B O   1 
ATOM   2736 C  CB  . ILE   B 1 138 ? -0.55888  3.37214   33.61493  1.000 13.98462 ?  150 ILE   B CB  1 
ATOM   2737 C  CG1 . ILE   B 1 138 ? -0.75128  3.61137   35.11446  1.000 17.36619 ?  150 ILE   B CG1 1 
ATOM   2738 C  CG2 . ILE   B 1 138 ? 0.88789   3.11231   33.28004  1.000 18.11567 ?  150 ILE   B CG2 1 
ATOM   2739 C  CD1 . ILE   B 1 138 ? -0.43752  2.38103   35.96454  1.000 16.59284 ?  150 ILE   B CD1 1 
ATOM   2740 N  N   . PRO   B 1 139 ? -0.35168  5.00024   30.47815  1.000 13.35128 ?  151 PRO   B N   1 
ATOM   2741 C  CA  . PRO   B 1 139 ? -0.14073  4.61900   29.07801  1.000 13.65862 ?  151 PRO   B CA  1 
ATOM   2742 C  C   . PRO   B 1 139 ? 0.52289   3.24798   28.97801  1.000 13.15744 ?  151 PRO   B C   1 
ATOM   2743 O  O   . PRO   B 1 139 ? 1.39699   2.89240   29.77247  1.000 14.26267 ?  151 PRO   B O   1 
ATOM   2744 C  CB  . PRO   B 1 139 ? 0.76685   5.73481   28.55020  1.000 11.26223 ?  151 PRO   B CB  1 
ATOM   2745 C  CG  . PRO   B 1 139 ? 0.39971   6.93089   29.40010  1.000 12.72359 ?  151 PRO   B CG  1 
ATOM   2746 C  CD  . PRO   B 1 139 ? 0.12574   6.36371   30.78177  1.000 11.52644 ?  151 PRO   B CD  1 
ATOM   2747 N  N   . THR   B 1 140 ? 0.11443   2.47352   27.97070  1.000 12.72854 ?  152 THR   B N   1 
ATOM   2748 C  CA  . THR   B 1 140 ? 0.47880   1.05982   27.91676  1.000 12.38541 ?  152 THR   B CA  1 
ATOM   2749 C  C   . THR   B 1 140 ? 1.93510   0.84169   27.49875  1.000 13.02094 ?  152 THR   B C   1 
ATOM   2750 O  O   . THR   B 1 140 ? 2.65640   0.05497   28.12389  1.000 14.59983 ?  152 THR   B O   1 
ATOM   2751 C  CB  . THR   B 1 140 ? -0.49457  0.31934   26.99538  1.000 16.62082 ?  152 THR   B CB  1 
ATOM   2752 O  OG1 . THR   B 1 140 ? -1.78845  0.30578   27.61207  1.000 19.17221 ?  152 THR   B OG1 1 
ATOM   2753 C  CG2 . THR   B 1 140 ? -0.01265  -1.10802  26.72453  1.000 17.85338 ?  152 THR   B CG2 1 
ATOM   2754 N  N   . HIS   B 1 141 ? 2.39476   1.52150   26.45172  1.000 13.35226 ?  153 HIS   B N   1 
ATOM   2755 C  CA  . HIS   B 1 141 ? 3.70057   1.27245   25.86007  1.000 12.91144 ?  153 HIS   B CA  1 
ATOM   2756 C  C   . HIS   B 1 141 ? 4.71791   2.27466   26.38707  1.000 14.07972 ?  153 HIS   B C   1 
ATOM   2757 O  O   . HIS   B 1 141 ? 4.37097   3.40451   26.74273  1.000 12.81593 ?  153 HIS   B O   1 
ATOM   2758 C  CB  . HIS   B 1 141 ? 3.64838   1.47870   24.34686  1.000 14.67284 ?  153 HIS   B CB  1 
ATOM   2759 C  CG  . HIS   B 1 141 ? 2.92671   0.40424   23.61256  1.000 24.74589 ?  153 HIS   B CG  1 
ATOM   2760 N  ND1 . HIS   B 1 141 ? 1.55393   0.38234   23.52313  1.000 27.41327 ?  153 HIS   B ND1 1 
ATOM   2761 C  CD2 . HIS   B 1 141 ? 3.37216   -0.67236  22.92325  1.000 32.77483 ?  153 HIS   B CD2 1 
ATOM   2762 C  CE1 . HIS   B 1 141 ? 1.18176   -0.67579  22.82496  1.000 21.17232 ?  153 HIS   B CE1 1 
ATOM   2763 N  NE2 . HIS   B 1 141 ? 2.26404   -1.31492  22.42883  1.000 23.04649 ?  153 HIS   B NE2 1 
ATOM   2764 N  N   . SER   B 1 142 ? 5.98518   1.87906   26.35790  1.000 13.16681 ?  154 SER   B N   1 
ATOM   2765 C  CA  . SER   B 1 142 ? 7.07638   2.68544   26.88645  1.000 12.54507 ?  154 SER   B CA  1 
ATOM   2766 C  C   . SER   B 1 142 ? 7.85729   3.33880   25.75200  1.000 17.31076 ?  154 SER   B C   1 
ATOM   2767 O  O   . SER   B 1 142 ? 8.11675   2.71601   24.71527  1.000 19.91589 ?  154 SER   B O   1 
ATOM   2768 C  CB  . SER   B 1 142 ? 8.03266   1.82591   27.71859  1.000 15.06596 ?  154 SER   B CB  1 
ATOM   2769 O  OG  . SER   B 1 142 ? 7.42177   1.40072   28.92801  1.000 16.36461 ?  154 SER   B OG  1 
ATOM   2770 N  N   . LEU   B 1 143 ? 8.23794   4.59664   25.96204  1.000 12.62876 ?  155 LEU   B N   1 
ATOM   2771 C  CA  . LEU   B 1 143 ? 9.10835   5.32663   25.04590  1.000 12.81868 ?  155 LEU   B CA  1 
ATOM   2772 C  C   . LEU   B 1 143 ? 10.52330  5.22575   25.58806  1.000 13.82630 ?  155 LEU   B C   1 
ATOM   2773 O  O   . LEU   B 1 143 ? 10.83284  5.78882   26.64526  1.000 16.09145 ?  155 LEU   B O   1 
ATOM   2774 C  CB  . LEU   B 1 143 ? 8.67517   6.78761   24.96033  1.000 13.04718 ?  155 LEU   B CB  1 
ATOM   2775 C  CG  . LEU   B 1 143 ? 7.27667   7.01055   24.40662  1.000 12.70531 ?  155 LEU   B CG  1 
ATOM   2776 C  CD1 . LEU   B 1 143 ? 6.83210   8.43841   24.66184  1.000 13.94679 ?  155 LEU   B CD1 1 
ATOM   2777 C  CD2 . LEU   B 1 143 ? 7.22775   6.71670   22.91647  1.000 15.79731 ?  155 LEU   B CD2 1 
ATOM   2778 N  N   . GLU   B 1 144 ? 11.37862  4.49741   24.87485  1.000 16.18302 ?  156 GLU   B N   1 
ATOM   2779 C  CA  . GLU   B 1 144 ? 12.74706  4.30550   25.31817  1.000 17.62344 ?  156 GLU   B CA  1 
ATOM   2780 C  C   . GLU   B 1 144 ? 13.61724  5.43885   24.78378  1.000 14.49038 ?  156 GLU   B C   1 
ATOM   2781 O  O   . GLU   B 1 144 ? 13.25216  6.14351   23.84725  1.000 15.00375 ?  156 GLU   B O   1 
ATOM   2782 C  CB  . GLU   B 1 144 ? 13.28647  2.96385   24.81500  1.000 24.79489 ?  156 GLU   B CB  1 
ATOM   2783 C  CG  . GLU   B 1 144 ? 12.58965  1.70918   25.36990  1.000 29.83550 ?  156 GLU   B CG  1 
ATOM   2784 C  CD  . GLU   B 1 144 ? 12.44060  1.70110   26.88460  1.000 28.79939 ?  156 GLU   B CD  1 
ATOM   2785 O  OE1 . GLU   B 1 144 ? 13.41967  2.01205   27.59463  1.000 32.00085 ?  156 GLU   B OE1 1 
ATOM   2786 O  OE2 . GLU   B 1 144 ? 11.34638  1.34098   27.37397  1.000 40.03646 ?  156 GLU   B OE2 1 
ATOM   2787 N  N   . GLY   B 1 145 ? 14.76759  5.62517   25.41495  1.000 13.38668 ?  157 GLY   B N   1 
ATOM   2788 C  CA  . GLY   B 1 145 ? 15.74791  6.56465   24.90738  1.000 12.67507 ?  157 GLY   B CA  1 
ATOM   2789 C  C   . GLY   B 1 145 ? 15.56352  8.00044   25.34141  1.000 13.31441 ?  157 GLY   B C   1 
ATOM   2790 O  O   . GLY   B 1 145 ? 16.14731  8.90096   24.72810  1.000 14.00138 ?  157 GLY   B O   1 
ATOM   2791 N  N   . LEU   B 1 146 ? 14.77246  8.25414   26.38482  1.000 11.84103 ?  158 LEU   B N   1 
ATOM   2792 C  CA  . LEU   B 1 146 ? 14.45757  9.62423   26.77840  1.000 13.12381 ?  158 LEU   B CA  1 
ATOM   2793 C  C   . LEU   B 1 146 ? 14.77729  9.93119   28.23486  1.000 13.36312 ?  158 LEU   B C   1 
ATOM   2794 O  O   . LEU   B 1 146 ? 14.28422  10.92213  28.76926  1.000 13.06202 ?  158 LEU   B O   1 
ATOM   2795 C  CB  . LEU   B 1 146 ? 12.99725  9.95865   26.47289  1.000 11.84233 ?  158 LEU   B CB  1 
ATOM   2796 C  CG  . LEU   B 1 146 ? 12.62354  10.07244  25.00331  1.000 12.61235 ?  158 LEU   B CG  1 
ATOM   2797 C  CD1 . LEU   B 1 146 ? 11.10408  9.96578   24.88032  1.000 13.16767 ?  158 LEU   B CD1 1 
ATOM   2798 C  CD2 . LEU   B 1 146 ? 13.17602  11.36492  24.40767  1.000 12.68550 ?  158 LEU   B CD2 1 
ATOM   2799 N  N   . SER   B 1 147 ? 15.57578  9.10949   28.90698  1.000 11.98648 ?  159 SER   B N   1 
ATOM   2800 C  CA  . SER   B 1 147 ? 15.72008  9.28797   30.34665  1.000 13.44586 ?  159 SER   B CA  1 
ATOM   2801 C  C   . SER   B 1 147 ? 16.78039  10.30576  30.75130  1.000 13.81756 ?  159 SER   B C   1 
ATOM   2802 O  O   . SER   B 1 147 ? 16.81448  10.68702  31.92110  1.000 14.73591 ?  159 SER   B O   1 
ATOM   2803 C  CB  . SER   B 1 147 ? 15.99833  7.95788   31.06668  1.000 15.93315 ?  159 SER   B CB  1 
ATOM   2804 O  OG  . SER   B 1 147 ? 17.22042  7.41337   30.62616  1.000 16.05573 ?  159 SER   B OG  1 
ATOM   2805 N  N   . SER   B 1 148 ? 17.63360  10.76103  29.83606  1.000 13.60475 ?  160 SER   B N   1 
ATOM   2806 C  CA  A SER   B 1 148 ? 18.69329  11.70990  30.14941  0.610 14.76262 ?  160 SER   B CA  1 
ATOM   2807 C  CA  B SER   B 1 148 ? 18.68538  11.71425  30.15802  0.390 14.75891 ?  160 SER   B CA  1 
ATOM   2808 C  C   . SER   B 1 148 ? 18.37974  13.06009  29.51472  1.000 12.04626 ?  160 SER   B C   1 
ATOM   2809 O  O   . SER   B 1 148 ? 17.97270  13.12340  28.35237  1.000 12.13826 ?  160 SER   B O   1 
ATOM   2810 C  CB  A SER   B 1 148 ? 20.03281  11.19580  29.62956  0.610 15.90892 ?  160 SER   B CB  1 
ATOM   2811 C  CB  B SER   B 1 148 ? 20.04427  11.19502  29.68823  0.390 15.98529 ?  160 SER   B CB  1 
ATOM   2812 O  OG  A SER   B 1 148 ? 21.09088  11.91308  30.23563  0.610 16.84650 ?  160 SER   B OG  1 
ATOM   2813 O  OG  B SER   B 1 148 ? 20.58107  10.28857  30.63793  0.390 19.86415 ?  160 SER   B OG  1 
ATOM   2814 N  N   . SER   B 1 149 ? 18.55541  14.13522  30.28189  1.000 12.73832 ?  161 SER   B N   1 
ATOM   2815 C  CA  A SER   B 1 149 ? 18.27210  15.47632  29.77730  0.565 12.99506 ?  161 SER   B CA  1 
ATOM   2816 C  CA  B SER   B 1 149 ? 18.24257  15.45748  29.76180  0.435 13.01486 ?  161 SER   B CA  1 
ATOM   2817 C  C   . SER   B 1 149 ? 19.00807  15.71096  28.47069  1.000 13.09813 ?  161 SER   B C   1 
ATOM   2818 O  O   . SER   B 1 149 ? 20.20223  15.40533  28.35309  1.000 16.31629 ?  161 SER   B O   1 
ATOM   2819 C  CB  A SER   B 1 149 ? 18.72712  16.51981  30.79406  0.565 13.75642 ?  161 SER   B CB  1 
ATOM   2820 C  CB  B SER   B 1 149 ? 18.57877  16.52704  30.79340  0.435 13.81576 ?  161 SER   B CB  1 
ATOM   2821 O  OG  A SER   B 1 149 ? 18.10035  16.31948  32.04112  0.565 12.72997 ?  161 SER   B OG  1 
ATOM   2822 O  OG  B SER   B 1 149 ? 19.93320  16.43594  31.17302  0.435 16.96688 ?  161 SER   B OG  1 
ATOM   2823 N  N   . GLY   B 1 150 ? 18.29604  16.26033  27.48693  1.000 11.26157 ?  162 GLY   B N   1 
ATOM   2824 C  CA  . GLY   B 1 150 ? 18.85135  16.45107  26.16977  1.000 14.62149 ?  162 GLY   B CA  1 
ATOM   2825 C  C   . GLY   B 1 150 ? 18.61329  15.30380  25.20729  1.000 13.96486 ?  162 GLY   B C   1 
ATOM   2826 O  O   . GLY   B 1 150 ? 18.95274  15.43161  24.02049  1.000 16.75143 ?  162 GLY   B O   1 
ATOM   2827 N  N   . ASP   B 1 151 ? 18.02668  14.19781  25.66682  1.000 12.39869 ?  163 ASP   B N   1 
ATOM   2828 C  CA  . ASP   B 1 151 ? 17.75532  13.06599  24.78462  1.000 11.30636 ?  163 ASP   B CA  1 
ATOM   2829 C  C   . ASP   B 1 151 ? 16.61586  13.39077  23.81892  1.000 14.23144 ?  163 ASP   B C   1 
ATOM   2830 O  O   . ASP   B 1 151 ? 15.61715  14.00231  24.19880  1.000 12.34010 ?  163 ASP   B O   1 
ATOM   2831 C  CB  . ASP   B 1 151 ? 17.30460  11.84991  25.60988  1.000 12.78937 ?  163 ASP   B CB  1 
ATOM   2832 C  CG  . ASP   B 1 151 ? 18.45861  11.08219  26.25367  1.000 15.59534 ?  163 ASP   B CG  1 
ATOM   2833 O  OD1 . ASP   B 1 151 ? 19.64638  11.30630  25.90408  1.000 18.00772 ?  163 ASP   B OD1 1 
ATOM   2834 O  OD2 . ASP   B 1 151 ? 18.15547  10.21710  27.11143  1.000 16.52728 ?  163 ASP   B OD2 1 
ATOM   2835 N  N   . ALA   B 1 152 ? 16.74389  12.93389  22.57806  1.000 13.48994 ?  164 ALA   B N   1 
ATOM   2836 C  CA  . ALA   B 1 152 ? 15.71952  13.09129  21.55669  1.000 13.79549 ?  164 ALA   B CA  1 
ATOM   2837 C  C   . ALA   B 1 152 ? 15.55986  11.77047  20.82021  1.000 17.39601 ?  164 ALA   B C   1 
ATOM   2838 O  O   . ALA   B 1 152 ? 16.54874  11.07167  20.56631  1.000 16.13087 ?  164 ALA   B O   1 
ATOM   2839 C  CB  . ALA   B 1 152 ? 16.09730  14.18421  20.54555  1.000 15.43714 ?  164 ALA   B CB  1 
ATOM   2840 N  N   . VAL   B 1 153 ? 14.31974  11.41998  20.48404  1.000 13.12819 ?  165 VAL   B N   1 
ATOM   2841 C  CA  . VAL   B 1 153 ? 14.04057  10.23586  19.68542  1.000 12.75180 ?  165 VAL   B CA  1 
ATOM   2842 C  C   . VAL   B 1 153 ? 12.95536  10.58113  18.68259  1.000 14.27887 ?  165 VAL   B C   1 
ATOM   2843 O  O   . VAL   B 1 153 ? 12.07511  11.40898  18.94130  1.000 14.12953 ?  165 VAL   B O   1 
ATOM   2844 C  CB  . VAL   B 1 153 ? 13.61747  8.99997   20.52542  1.000 17.80256 ?  165 VAL   B CB  1 
ATOM   2845 C  CG1 . VAL   B 1 153 ? 14.69831  8.61240   21.52756  1.000 19.06035 ?  165 VAL   B CG1 1 
ATOM   2846 C  CG2 . VAL   B 1 153 ? 12.30394  9.23944   21.24306  1.000 17.23451 ?  165 VAL   B CG2 1 
ATOM   2847 N  N   . ARG   B 1 154 ? 13.00506  9.93560   17.53112  1.000 13.34304 ?  166 ARG   B N   1 
ATOM   2848 C  CA  . ARG   B 1 154 ? 11.95253  10.12422  16.55816  1.000 13.02309 ?  166 ARG   B CA  1 
ATOM   2849 C  C   . ARG   B 1 154 ? 10.74784  9.25594   16.89669  1.000 15.37074 ?  166 ARG   B C   1 
ATOM   2850 O  O   . ARG   B 1 154 ? 10.88210  8.12313   17.37826  1.000 16.60668 ?  166 ARG   B O   1 
ATOM   2851 C  CB  . ARG   B 1 154 ? 12.45846  9.77830   15.16258  1.000 12.40181 ?  166 ARG   B CB  1 
ATOM   2852 C  CG  . ARG   B 1 154 ? 11.42953  10.04188  14.11417  1.000 13.69162 ?  166 ARG   B CG  1 
ATOM   2853 C  CD  . ARG   B 1 154 ? 11.94476  9.70195   12.75084  1.000 16.73231 ?  166 ARG   B CD  1 
ATOM   2854 N  NE  . ARG   B 1 154 ? 10.89164  9.91538   11.77479  1.000 17.23316 ?  166 ARG   B NE  1 
ATOM   2855 C  CZ  . ARG   B 1 154 ? 11.08266  9.82625   10.46802  1.000 19.50682 ?  166 ARG   B CZ  1 
ATOM   2856 N  NH1 . ARG   B 1 154 ? 12.26267  9.50564   9.97318   1.000 20.65571 ?  166 ARG   B NH1 1 
ATOM   2857 N  NH2 . ARG   B 1 154 ? 10.06759  10.06709  9.64653   1.000 16.79842 ?  166 ARG   B NH2 1 
ATOM   2858 N  N   . PHE   B 1 155 ? 9.56363   9.78589   16.63774  1.000 13.23522 ?  167 PHE   B N   1 
ATOM   2859 C  CA  . PHE   B 1 155 ? 8.33251   9.02647   16.80926  1.000 11.65009 ?  167 PHE   B CA  1 
ATOM   2860 C  C   . PHE   B 1 155 ? 7.45352   9.39129   15.62232  1.000 13.52269 ?  167 PHE   B C   1 
ATOM   2861 O  O   . PHE   B 1 155 ? 6.60975   10.28495  15.69010  1.000 12.81315 ?  167 PHE   B O   1 
ATOM   2862 C  CB  . PHE   B 1 155 ? 7.65538   9.33114   18.14705  1.000 13.51281 ?  167 PHE   B CB  1 
ATOM   2863 C  CG  . PHE   B 1 155 ? 6.70767   8.25698   18.60471  1.000 10.88335 ?  167 PHE   B CG  1 
ATOM   2864 C  CD1 . PHE   B 1 155 ? 7.17566   7.06014   19.13313  1.000 14.80574 ?  167 PHE   B CD1 1 
ATOM   2865 C  CD2 . PHE   B 1 155 ? 5.34121   8.45478   18.52053  1.000 11.94163 ?  167 PHE   B CD2 1 
ATOM   2866 C  CE1 . PHE   B 1 155 ? 6.28512   6.08471   19.56570  1.000 15.14091 ?  167 PHE   B CE1 1 
ATOM   2867 C  CE2 . PHE   B 1 155 ? 4.44369   7.46998   18.95037  1.000 14.88182 ?  167 PHE   B CE2 1 
ATOM   2868 C  CZ  . PHE   B 1 155 ? 4.92923   6.28737   19.47676  1.000 13.72756 ?  167 PHE   B CZ  1 
ATOM   2869 N  N   . GLY   B 1 156 ? 7.68922   8.71889   14.50310  1.000 13.24003 ?  168 GLY   B N   1 
ATOM   2870 C  CA  . GLY   B 1 156 ? 6.97906   9.03163   13.28955  1.000 13.93882 ?  168 GLY   B CA  1 
ATOM   2871 C  C   . GLY   B 1 156 ? 7.23453   10.45871  12.84336  1.000 12.59076 ?  168 GLY   B C   1 
ATOM   2872 O  O   . GLY   B 1 156 ? 8.38033   10.87741  12.63543  1.000 13.07517 ?  168 GLY   B O   1 
ATOM   2873 N  N   . PRO   B 1 157 ? 6.16420   11.24325  12.70158  1.000 13.20864 ?  169 PRO   B N   1 
ATOM   2874 C  CA  . PRO   B 1 157 ? 6.28734   12.60393  12.16172  1.000 13.59497 ?  169 PRO   B CA  1 
ATOM   2875 C  C   . PRO   B 1 157 ? 6.71236   13.64799  13.18051  1.000 11.79625 ?  169 PRO   B C   1 
ATOM   2876 O  O   . PRO   B 1 157 ? 6.71190   14.84065  12.85420  1.000 12.51154 ?  169 PRO   B O   1 
ATOM   2877 C  CB  . PRO   B 1 157 ? 4.86097   12.89074  11.68145  1.000 12.59373 ?  169 PRO   B CB  1 
ATOM   2878 C  CG  . PRO   B 1 157 ? 4.01367   12.20085  12.73487  1.000 15.25172 ?  169 PRO   B CG  1 
ATOM   2879 C  CD  . PRO   B 1 157 ? 4.76855   10.91188  13.03763  1.000 12.80892 ?  169 PRO   B CD  1 
ATOM   2880 N  N   . VAL   B 1 158 ? 7.05151   13.23803  14.40653  1.000 10.41797 ?  170 VAL   B N   1 
ATOM   2881 C  CA  . VAL   B 1 158 ? 7.53841   14.16184  15.41332  1.000 10.15226 ?  170 VAL   B CA  1 
ATOM   2882 C  C   . VAL   B 1 158 ? 8.86588   13.66890  15.96552  1.000 10.18052 ?  170 VAL   B C   1 
ATOM   2883 O  O   . VAL   B 1 158 ? 9.24181   12.50206  15.82051  1.000 11.68470 ?  170 VAL   B O   1 
ATOM   2884 C  CB  . VAL   B 1 158 ? 6.51544   14.38322  16.54763  1.000 9.12189  ?  170 VAL   B CB  1 
ATOM   2885 C  CG1 . VAL   B 1 158 ? 5.16004   14.75910  15.97659  1.000 11.01712 ?  170 VAL   B CG1 1 
ATOM   2886 C  CG2 . VAL   B 1 158 ? 6.42807   13.15629  17.48142  1.000 11.32637 ?  170 VAL   B CG2 1 
ATOM   2887 N  N   . GLU   B 1 159 ? 9.57681   14.58903  16.60403  1.000 9.73693  ?  171 GLU   B N   1 
ATOM   2888 C  CA  . GLU   B 1 159 ? 10.67598  14.27849  17.50037  1.000 7.99471  ?  171 GLU   B CA  1 
ATOM   2889 C  C   . GLU   B 1 159 ? 10.19870  14.49720  18.92898  1.000 11.70971 ?  171 GLU   B C   1 
ATOM   2890 O  O   . GLU   B 1 159 ? 9.55697   15.51639  19.23699  1.000 10.78983 ?  171 GLU   B O   1 
ATOM   2891 C  CB  . GLU   B 1 159 ? 11.88539  15.17809  17.21330  1.000 10.62235 ?  171 GLU   B CB  1 
ATOM   2892 C  CG  . GLU   B 1 159 ? 13.10475  14.83044  18.04961  1.000 14.80874 ?  171 GLU   B CG  1 
ATOM   2893 C  CD  . GLU   B 1 159 ? 14.35642  15.49708  17.52965  1.000 16.52394 ?  171 GLU   B CD  1 
ATOM   2894 O  OE1 . GLU   B 1 159 ? 14.58733  16.68417  17.85510  1.000 15.31595 ?  171 GLU   B OE1 1 
ATOM   2895 O  OE2 . GLU   B 1 159 ? 15.12174  14.82838  16.79855  1.000 19.53316 ?  171 GLU   B OE2 1 
ATOM   2896 N  N   . LEU   B 1 160 ? 10.50495  13.53927  19.79627  1.000 9.87402  ?  172 LEU   B N   1 
ATOM   2897 C  CA  . LEU   B 1 160 ? 10.27877  13.67682  21.22811  1.000 9.93890  ?  172 LEU   B CA  1 
ATOM   2898 C  C   . LEU   B 1 160 ? 11.58381  14.09386  21.89335  1.000 10.55784 ?  172 LEU   B C   1 
ATOM   2899 O  O   . LEU   B 1 160 ? 12.64469  13.55911  21.57970  1.000 11.77607 ?  172 LEU   B O   1 
ATOM   2900 C  CB  . LEU   B 1 160 ? 9.81075   12.34277  21.81068  1.000 8.81994  ?  172 LEU   B CB  1 
ATOM   2901 C  CG  . LEU   B 1 160 ? 8.57051   11.76464  21.11009  1.000 9.23926  ?  172 LEU   B CG  1 
ATOM   2902 C  CD1 . LEU   B 1 160 ? 8.19598   10.41910  21.71102  1.000 14.00889 ?  172 LEU   B CD1 1 
ATOM   2903 C  CD2 . LEU   B 1 160 ? 7.36224   12.68929  21.17303  1.000 11.90262 ?  172 LEU   B CD2 1 
ATOM   2904 N  N   . PHE   B 1 161 ? 11.50470  15.03714  22.82932  1.000 8.93515  ?  173 PHE   B N   1 
ATOM   2905 C  CA  . PHE   B 1 161 ? 12.68035  15.58485  23.49284  1.000 10.75656 ?  173 PHE   B CA  1 
ATOM   2906 C  C   . PHE   B 1 161 ? 12.44325  15.64351  24.99163  1.000 9.42370  ?  173 PHE   B C   1 
ATOM   2907 O  O   . PHE   B 1 161 ? 11.41468  16.16246  25.43135  1.000 10.26844 ?  173 PHE   B O   1 
ATOM   2908 C  CB  . PHE   B 1 161 ? 12.93203  17.00573  22.94869  1.000 11.50609 ?  173 PHE   B CB  1 
ATOM   2909 C  CG  . PHE   B 1 161 ? 14.18112  17.66436  23.45091  1.000 11.17629 ?  173 PHE   B CG  1 
ATOM   2910 C  CD1 . PHE   B 1 161 ? 15.44168  17.17472  23.09186  1.000 13.66214 ?  173 PHE   B CD1 1 
ATOM   2911 C  CD2 . PHE   B 1 161 ? 14.10286  18.81800  24.22183  1.000 11.08056 ?  173 PHE   B CD2 1 
ATOM   2912 C  CE1 . PHE   B 1 161 ? 16.59484  17.80109  23.53372  1.000 12.88182 ?  173 PHE   B CE1 1 
ATOM   2913 C  CE2 . PHE   B 1 161 ? 15.25884  19.45793  24.66812  1.000 11.32972 ?  173 PHE   B CE2 1 
ATOM   2914 C  CZ  . PHE   B 1 161 ? 16.51014  18.94453  24.31810  1.000 14.10757 ?  173 PHE   B CZ  1 
ATOM   2915 N  N   . TYR   B 1 162 ? 13.39151  15.12959  25.78242  1.000 9.17242  ?  174 TYR   B N   1 
ATOM   2916 C  CA  . TYR   B 1 162 ? 13.35885  15.29562  27.22483  1.000 10.12227 ?  174 TYR   B CA  1 
ATOM   2917 C  C   . TYR   B 1 162 ? 14.30857  16.42068  27.59428  1.000 10.67482 ?  174 TYR   B C   1 
ATOM   2918 O  O   . TYR   B 1 162 ? 15.54084  16.23639  27.52213  1.000 12.00209 ?  174 TYR   B O   1 
ATOM   2919 C  CB  . TYR   B 1 162 ? 13.74974  14.00793  27.94540  1.000 10.62889 ?  174 TYR   B CB  1 
ATOM   2920 C  CG  . TYR   B 1 162 ? 13.88003  14.20647  29.42977  1.000 9.29783  ?  174 TYR   B CG  1 
ATOM   2921 C  CD1 . TYR   B 1 162 ? 12.86815  14.82221  30.16232  1.000 9.39023  ?  174 TYR   B CD1 1 
ATOM   2922 C  CD2 . TYR   B 1 162 ? 15.00018  13.77329  30.11675  1.000 9.82807  ?  174 TYR   B CD2 1 
ATOM   2923 C  CE1 . TYR   B 1 162 ? 12.96781  15.01376  31.53082  1.000 10.60233 ?  174 TYR   B CE1 1 
ATOM   2924 C  CE2 . TYR   B 1 162 ? 15.11658  13.97696  31.50694  1.000 11.30885 ?  174 TYR   B CE2 1 
ATOM   2925 C  CZ  . TYR   B 1 162 ? 14.08840  14.58740  32.20238  1.000 11.04575 ?  174 TYR   B CZ  1 
ATOM   2926 O  OH  . TYR   B 1 162 ? 14.14639  14.80451  33.57003  1.000 12.54599 ?  174 TYR   B OH  1 
ATOM   2927 N  N   . PRO   B 1 163 ? 13.80187  17.59863  27.97012  1.000 10.14424 ?  175 PRO   B N   1 
ATOM   2928 C  CA  . PRO   B 1 163 ? 14.68370  18.74550  28.20341  1.000 9.71428  ?  175 PRO   B CA  1 
ATOM   2929 C  C   . PRO   B 1 163 ? 15.30697  18.75473  29.58808  1.000 11.74380 ?  175 PRO   B C   1 
ATOM   2930 O  O   . PRO   B 1 163 ? 16.15683  19.62037  29.85917  1.000 10.88658 ?  175 PRO   B O   1 
ATOM   2931 C  CB  . PRO   B 1 163 ? 13.72381  19.93516  28.04132  1.000 10.93753 ?  175 PRO   B CB  1 
ATOM   2932 C  CG  . PRO   B 1 163 ? 12.42167  19.38853  28.59459  1.000 10.55216 ?  175 PRO   B CG  1 
ATOM   2933 C  CD  . PRO   B 1 163 ? 12.37614  17.97473  28.03401  1.000 9.35990  ?  175 PRO   B CD  1 
ATOM   2934 N  N   . GLY   B 1 164 ? 14.92227  17.83126  30.46318  1.000 10.27761 ?  176 GLY   B N   1 
ATOM   2935 C  CA  . GLY   B 1 164 ? 15.23528  17.90422  31.87429  1.000 9.40652  ?  176 GLY   B CA  1 
ATOM   2936 C  C   . GLY   B 1 164 ? 14.00413  18.27788  32.68709  1.000 9.52003  ?  176 GLY   B C   1 
ATOM   2937 O  O   . GLY   B 1 164 ? 12.95982  18.66335  32.16129  1.000 9.77925  ?  176 GLY   B O   1 
ATOM   2938 N  N   . ALA   B 1 165 ? 14.15462  18.19162  34.00141  1.000 10.17865 ?  177 ALA   B N   1 
ATOM   2939 C  CA  . ALA   B 1 165 ? 13.03439  18.46147  34.89268  1.000 9.64171  ?  177 ALA   B CA  1 
ATOM   2940 C  C   . ALA   B 1 165 ? 12.62344  19.91922  34.79353  1.000 10.81231 ?  177 ALA   B C   1 
ATOM   2941 O  O   . ALA   B 1 165 ? 13.46489  20.81635  34.66847  1.000 11.15393 ?  177 ALA   B O   1 
ATOM   2942 C  CB  . ALA   B 1 165 ? 13.41010  18.11335  36.33198  1.000 11.11078 ?  177 ALA   B CB  1 
ATOM   2943 N  N   . ALA   B 1 166 ? 11.31234  20.16136  34.84928  1.000 9.83067  ?  178 ALA   B N   1 
ATOM   2944 C  CA  . ALA   B 1 166 ? 10.80392  21.52494  34.75099  1.000 8.56058  ?  178 ALA   B CA  1 
ATOM   2945 C  C   . ALA   B 1 166 ? 9.47491   21.59965  35.49894  1.000 9.70524  ?  178 ALA   B C   1 
ATOM   2946 O  O   . ALA   B 1 166 ? 9.45439   21.55455  36.73595  1.000 10.48585 ?  178 ALA   B O   1 
ATOM   2947 C  CB  . ALA   B 1 166 ? 10.69897  21.96541  33.27974  1.000 10.15501 ?  178 ALA   B CB  1 
ATOM   2948 N  N   . HIS   B 1 167 ? 8.35844   21.69483  34.75895  1.000 8.50652  ?  179 HIS   B N   1 
ATOM   2949 C  CA  . HIS   B 1 167 ? 7.04701   21.55970  35.37573  1.000 8.85439  ?  179 HIS   B CA  1 
ATOM   2950 C  C   . HIS   B 1 167 ? 6.93093   20.25326  36.16726  1.000 10.33236 ?  179 HIS   B C   1 
ATOM   2951 O  O   . HIS   B 1 167 ? 6.29538   20.21180  37.23059  1.000 9.76182  ?  179 HIS   B O   1 
ATOM   2952 C  CB  . HIS   B 1 167 ? 5.99131   21.62538  34.26853  1.000 8.96485  ?  179 HIS   B CB  1 
ATOM   2953 C  CG  . HIS   B 1 167 ? 4.63335   21.24965  34.73895  1.000 11.15877 ?  179 HIS   B CG  1 
ATOM   2954 N  ND1 . HIS   B 1 167 ? 3.78026   22.14477  35.34999  1.000 11.71555 ?  179 HIS   B ND1 1 
ATOM   2955 C  CD2 . HIS   B 1 167 ? 3.98462   20.06744  34.70432  1.000 9.63011  ?  179 HIS   B CD2 1 
ATOM   2956 C  CE1 . HIS   B 1 167 ? 2.66303   21.52834  35.67648  1.000 11.83934 ?  179 HIS   B CE1 1 
ATOM   2957 N  NE2 . HIS   B 1 167 ? 2.76759   20.26963  35.30012  1.000 10.87473 ?  179 HIS   B NE2 1 
ATOM   2958 N  N   . SER   B 1 168 ? 7.49915   19.17213  35.64234  1.000 9.47016  ?  180 SER   B N   1 
ATOM   2959 C  CA  . SER   B 1 168 ? 7.59387   17.90403  36.34891  1.000 9.23806  ?  180 SER   B CA  1 
ATOM   2960 C  C   . SER   B 1 168 ? 8.91879   17.26408  35.96501  1.000 10.35952 ?  180 SER   B C   1 
ATOM   2961 O  O   . SER   B 1 168 ? 9.62547   17.73748  35.06512  1.000 9.81390  ?  180 SER   B O   1 
ATOM   2962 C  CB  . SER   B 1 168 ? 6.41842   16.99258  35.97484  1.000 9.53373  ?  180 SER   B CB  1 
ATOM   2963 O  OG  . SER   B 1 168 ? 6.46801   16.68712  34.58391  1.000 10.02175 ?  180 SER   B OG  1 
ATOM   2964 N  N   . THR   B 1 169 ? 9.28623   16.18948  36.65848  1.000 8.70277  ?  181 THR   B N   1 
ATOM   2965 C  CA  . THR   B 1 169 ? 10.57845  15.58812  36.34668  1.000 10.44549 ?  181 THR   B CA  1 
ATOM   2966 C  C   . THR   B 1 169 ? 10.56794  14.82045  35.03688  1.000 11.10456 ?  181 THR   B C   1 
ATOM   2967 O  O   . THR   B 1 169 ? 11.63223  14.61497  34.43735  1.000 11.59189 ?  181 THR   B O   1 
ATOM   2968 C  CB  . THR   B 1 169 ? 11.06150  14.69304  37.48534  1.000 11.64238 ?  181 THR   B CB  1 
ATOM   2969 O  OG1 . THR   B 1 169 ? 10.14056  13.61358  37.68022  1.000 15.54934 ?  181 THR   B OG1 1 
ATOM   2970 C  CG2 . THR   B 1 169 ? 11.20330  15.49690  38.76928  1.000 14.14021 ?  181 THR   B CG2 1 
ATOM   2971 N  N   . ASP   B 1 170 ? 9.38949   14.42376  34.56370  1.000 9.18183  ?  182 ASP   B N   1 
ATOM   2972 C  CA  . ASP   B 1 170 ? 9.25654   13.57292  33.39447  1.000 9.04702  ?  182 ASP   B CA  1 
ATOM   2973 C  C   . ASP   B 1 170 ? 8.81654   14.32369  32.15618  1.000 9.39806  ?  182 ASP   B C   1 
ATOM   2974 O  O   . ASP   B 1 170 ? 8.59015   13.69432  31.11951  1.000 9.95383  ?  182 ASP   B O   1 
ATOM   2975 C  CB  . ASP   B 1 170 ? 8.24088   12.45021  33.68152  1.000 9.63992  ?  182 ASP   B CB  1 
ATOM   2976 C  CG  . ASP   B 1 170 ? 6.85796   12.98567  34.05445  1.000 10.44722 ?  182 ASP   B CG  1 
ATOM   2977 O  OD1 . ASP   B 1 170 ? 6.76507   14.03714  34.73096  1.000 10.00854 ?  182 ASP   B OD1 1 
ATOM   2978 O  OD2 . ASP   B 1 170 ? 5.84639   12.33936  33.68379  1.000 10.86564 ?  182 ASP   B OD2 1 
ATOM   2979 N  N   . ASN   B 1 171 ? 8.65119   15.64122  32.23478  1.000 8.36423  ?  183 ASN   B N   1 
ATOM   2980 C  CA  . ASN   B 1 171 ? 8.01759   16.36178  31.13139  1.000 8.45382  ?  183 ASN   B CA  1 
ATOM   2981 C  C   . ASN   B 1 171 ? 8.77596   16.23704  29.81591  1.000 9.07382  ?  183 ASN   B C   1 
ATOM   2982 O  O   . ASN   B 1 171 ? 9.99449   16.43024  29.75109  1.000 9.89058  ?  183 ASN   B O   1 
ATOM   2983 C  CB  . ASN   B 1 171 ? 7.63692   17.79787  31.51470  1.000 8.27435  ?  183 ASN   B CB  1 
ATOM   2984 C  CG  . ASN   B 1 171 ? 8.80046   18.64875  32.00500  1.000 9.87834  ?  183 ASN   B CG  1 
ATOM   2985 O  OD1 . ASN   B 1 171 ? 9.98808   18.40994  31.70647  1.000 12.22994 ?  183 ASN   B OD1 1 
ATOM   2986 N  ND2 . ASN   B 1 171 ? 8.45518   19.64235  32.76607  1.000 7.40548  ?  183 ASN   B ND2 1 
ATOM   2987 N  N   . LEU   B 1 172 ? 8.04544   15.87351  28.76481  1.000 8.66289  ?  184 LEU   B N   1 
ATOM   2988 C  CA  . LEU   B 1 172 ? 8.56977   15.83380  27.40475  1.000 8.04848  ?  184 LEU   B CA  1 
ATOM   2989 C  C   . LEU   B 1 172 ? 8.02936   16.99900  26.58798  1.000 8.16131  ?  184 LEU   B C   1 
ATOM   2990 O  O   . LEU   B 1 172 ? 6.93053   17.51090  26.83923  1.000 9.53991  ?  184 LEU   B O   1 
ATOM   2991 C  CB  . LEU   B 1 172 ? 8.12690   14.55678  26.67264  1.000 8.04787  ?  184 LEU   B CB  1 
ATOM   2992 C  CG  . LEU   B 1 172 ? 8.51187   13.19861  27.28887  1.000 8.61460  ?  184 LEU   B CG  1 
ATOM   2993 C  CD1 . LEU   B 1 172 ? 8.00844   12.04245  26.44527  1.000 10.59380 ?  184 LEU   B CD1 1 
ATOM   2994 C  CD2 . LEU   B 1 172 ? 10.02908  13.10243  27.48476  1.000 12.57553 ?  184 LEU   B CD2 1 
ATOM   2995 N  N   . VAL   B 1 173 ? 8.80579   17.40826  25.59527  1.000 8.16256  ?  185 VAL   B N   1 
ATOM   2996 C  CA  . VAL   B 1 173 ? 8.30626   18.32808  24.57850  1.000 8.24192  ?  185 VAL   B CA  1 
ATOM   2997 C  C   . VAL   B 1 173 ? 8.33615   17.62044  23.22458  1.000 8.62166  ?  185 VAL   B C   1 
ATOM   2998 O  O   . VAL   B 1 173 ? 9.00109   16.59584  23.04135  1.000 8.23943  ?  185 VAL   B O   1 
ATOM   2999 C  CB  . VAL   B 1 173 ? 9.05024   19.68141  24.54146  1.000 11.27279 ?  185 VAL   B CB  1 
ATOM   3000 C  CG1 . VAL   B 1 173 ? 9.03804   20.36103  25.91260  1.000 13.99788 ?  185 VAL   B CG1 1 
ATOM   3001 C  CG2 . VAL   B 1 173 ? 10.46140  19.49448  24.02355  1.000 14.85298 ?  185 VAL   B CG2 1 
ATOM   3002 N  N   . VAL   B 1 174 ? 7.54501   18.13878  22.28499  1.000 9.07073  ?  186 VAL   B N   1 
ATOM   3003 C  CA  . VAL   B 1 174 ? 7.31156   17.47599  21.00550  1.000 11.14027 ?  186 VAL   B CA  1 
ATOM   3004 C  C   . VAL   B 1 174 ? 7.53470   18.48133  19.88803  1.000 10.13487 ?  186 VAL   B C   1 
ATOM   3005 O  O   . VAL   B 1 174 ? 6.96605   19.57948  19.91233  1.000 10.67192 ?  186 VAL   B O   1 
ATOM   3006 C  CB  . VAL   B 1 174 ? 5.88512   16.90085  20.92785  1.000 9.85042  ?  186 VAL   B CB  1 
ATOM   3007 C  CG1 . VAL   B 1 174 ? 5.63892   16.22126  19.56186  1.000 11.25332 ?  186 VAL   B CG1 1 
ATOM   3008 C  CG2 . VAL   B 1 174 ? 5.63648   15.90689  22.06436  1.000 9.88049  ?  186 VAL   B CG2 1 
ATOM   3009 N  N   . TYR   B 1 175 ? 8.32173   18.09993  18.88391  1.000 9.29324  ?  187 TYR   B N   1 
ATOM   3010 C  CA  . TYR   B 1 175 ? 8.58936   18.99585  17.76453  1.000 10.71669 ?  187 TYR   B CA  1 
ATOM   3011 C  C   . TYR   B 1 175 ? 8.12028   18.34725  16.46782  1.000 9.92171  ?  187 TYR   B C   1 
ATOM   3012 O  O   . TYR   B 1 175 ? 8.37002   17.16134  16.24031  1.000 9.94413  ?  187 TYR   B O   1 
ATOM   3013 C  CB  . TYR   B 1 175 ? 10.08692  19.31967  17.67690  1.000 12.01873 ?  187 TYR   B CB  1 
ATOM   3014 C  CG  . TYR   B 1 175 ? 10.39526  20.36431  16.61960  1.000 10.83089 ?  187 TYR   B CG  1 
ATOM   3015 C  CD1 . TYR   B 1 175 ? 9.94632   21.67528  16.76076  1.000 8.94666  ?  187 TYR   B CD1 1 
ATOM   3016 C  CD2 . TYR   B 1 175 ? 11.14026  20.03369  15.48589  1.000 11.50301 ?  187 TYR   B CD2 1 
ATOM   3017 C  CE1 . TYR   B 1 175 ? 10.22810  22.63745  15.78745  1.000 11.92175 ?  187 TYR   B CE1 1 
ATOM   3018 C  CE2 . TYR   B 1 175 ? 11.42330  20.99199  14.50398  1.000 11.63524 ?  187 TYR   B CE2 1 
ATOM   3019 C  CZ  . TYR   B 1 175 ? 10.95113  22.28440  14.67570  1.000 14.06619 ?  187 TYR   B CZ  1 
ATOM   3020 O  OH  . TYR   B 1 175 ? 11.19462  23.27384  13.74741  1.000 14.57098 ?  187 TYR   B OH  1 
ATOM   3021 N  N   . VAL   B 1 176 ? 7.43930   19.12000  15.62496  1.000 10.11244 ?  188 VAL   B N   1 
ATOM   3022 C  CA  . VAL   B 1 176 ? 6.98962   18.63792  14.31846  1.000 11.82818 ?  188 VAL   B CA  1 
ATOM   3023 C  C   . VAL   B 1 176 ? 7.89076   19.28302  13.27432  1.000 9.73406  ?  188 VAL   B C   1 
ATOM   3024 O  O   . VAL   B 1 176 ? 7.64916   20.44163  12.89854  1.000 11.48667 ?  188 VAL   B O   1 
ATOM   3025 C  CB  . VAL   B 1 176 ? 5.52271   19.00305  14.04485  1.000 10.18120 ?  188 VAL   B CB  1 
ATOM   3026 C  CG1 . VAL   B 1 176 ? 4.98666   18.23127  12.82583  1.000 10.91554 ?  188 VAL   B CG1 1 
ATOM   3027 C  CG2 . VAL   B 1 176 ? 4.64651   18.70453  15.26970  1.000 11.48356 ?  188 VAL   B CG2 1 
ATOM   3028 N  N   . PRO   B 1 177 ? 8.89651   18.56580  12.75344  1.000 11.46051 ?  189 PRO   B N   1 
ATOM   3029 C  CA  . PRO   B 1 177 ? 9.85633   19.22141  11.85023  1.000 15.30086 ?  189 PRO   B CA  1 
ATOM   3030 C  C   . PRO   B 1 177 ? 9.23873   19.76208  10.57783  1.000 13.52832 ?  189 PRO   B C   1 
ATOM   3031 O  O   . PRO   B 1 177 ? 9.65620   20.82728  10.11773  1.000 16.01178 ?  189 PRO   B O   1 
ATOM   3032 C  CB  . PRO   B 1 177 ? 10.91678  18.14147  11.59456  1.000 16.33058 ?  189 PRO   B CB  1 
ATOM   3033 C  CG  . PRO   B 1 177 ? 10.34154  16.87622  12.06273  1.000 19.40082 ?  189 PRO   B CG  1 
ATOM   3034 C  CD  . PRO   B 1 177 ? 9.29160   17.19353  13.09166  1.000 13.02546 ?  189 PRO   B CD  1 
ATOM   3035 N  N   . SER   B 1 178 ? 8.24495   19.08290  10.00748  1.000 12.79651 ?  190 SER   B N   1 
ATOM   3036 C  CA  . SER   B 1 178 ? 7.70120   19.53601  8.72770   1.000 14.82503 ?  190 SER   B CA  1 
ATOM   3037 C  C   . SER   B 1 178 ? 6.97191   20.86388  8.84634   1.000 19.09827 ?  190 SER   B C   1 
ATOM   3038 O  O   . SER   B 1 178 ? 6.84593   21.57909  7.84519   1.000 18.13509 ?  190 SER   B O   1 
ATOM   3039 C  CB  . SER   B 1 178 ? 6.74956   18.48992  8.14503   1.000 16.78494 ?  190 SER   B CB  1 
ATOM   3040 O  OG  . SER   B 1 178 ? 5.56259   18.39937  8.93181   1.000 22.34383 ?  190 SER   B OG  1 
ATOM   3041 N  N   . ALA   B 1 179 ? 6.49032   21.20852  10.03815  1.000 16.24981 ?  191 ALA   B N   1 
ATOM   3042 C  CA  . ALA   B 1 179 ? 5.70576   22.41590  10.25260  1.000 13.53104 ?  191 ALA   B CA  1 
ATOM   3043 C  C   . ALA   B 1 179 ? 6.38875   23.43693  11.14711  1.000 11.66962 ?  191 ALA   B C   1 
ATOM   3044 O  O   . ALA   B 1 179 ? 5.82337   24.51408  11.37128  1.000 14.20630 ?  191 ALA   B O   1 
ATOM   3045 C  CB  . ALA   B 1 179 ? 4.34406   22.06305  10.86199  1.000 15.10591 ?  191 ALA   B CB  1 
ATOM   3046 N  N   . SER   B 1 180 ? 7.54494   23.10498  11.71733  1.000 11.31692 ?  192 SER   B N   1 
ATOM   3047 C  CA  . SER   B 1 180 ? 8.25912   23.98533  12.63997  1.000 13.44752 ?  192 SER   B CA  1 
ATOM   3048 C  C   . SER   B 1 180 ? 7.41455   24.32344  13.86948  1.000 11.91210 ?  192 SER   B C   1 
ATOM   3049 O  O   . SER   B 1 180 ? 7.46863   25.43569  14.40749  1.000 14.06054 ?  192 SER   B O   1 
ATOM   3050 C  CB  . SER   B 1 180 ? 8.81218   25.23376  11.93680  1.000 15.12767 ?  192 SER   B CB  1 
ATOM   3051 O  OG  . SER   B 1 180 ? 9.68991   24.85465  10.87425  1.000 17.80511 ?  192 SER   B OG  1 
ATOM   3052 N  N   . VAL   B 1 181 ? 6.65187   23.33592  14.34353  1.000 10.57919 ?  193 VAL   B N   1 
ATOM   3053 C  CA  . VAL   B 1 181 ? 5.75988   23.49439  15.48780  1.000 10.87488 ?  193 VAL   B CA  1 
ATOM   3054 C  C   . VAL   B 1 181 ? 6.39574   22.81854  16.69659  1.000 9.11512  ?  193 VAL   B C   1 
ATOM   3055 O  O   . VAL   B 1 181 ? 6.69738   21.61665  16.66458  1.000 9.92541  ?  193 VAL   B O   1 
ATOM   3056 C  CB  . VAL   B 1 181 ? 4.37776   22.88613  15.20792  1.000 12.10381 ?  193 VAL   B CB  1 
ATOM   3057 C  CG1 . VAL   B 1 181 ? 3.55821   22.85629  16.48416  1.000 12.93866 ?  193 VAL   B CG1 1 
ATOM   3058 C  CG2 . VAL   B 1 181 ? 3.64788   23.63539  14.12226  1.000 14.71343 ?  193 VAL   B CG2 1 
ATOM   3059 N  N   . LEU   B 1 182 ? 6.58388   23.57981  17.76891  1.000 9.57745  ?  194 LEU   B N   1 
ATOM   3060 C  CA  . LEU   B 1 182 ? 7.11510   23.06729  19.02841  1.000 10.13674 ?  194 LEU   B CA  1 
ATOM   3061 C  C   . LEU   B 1 182 ? 5.98574   23.06176  20.04312  1.000 10.94890 ?  194 LEU   B C   1 
ATOM   3062 O  O   . LEU   B 1 182 ? 5.42171   24.11907  20.34487  1.000 12.07278 ?  194 LEU   B O   1 
ATOM   3063 C  CB  . LEU   B 1 182 ? 8.23890   23.97562  19.53251  1.000 12.46064 ?  194 LEU   B CB  1 
ATOM   3064 C  CG  . LEU   B 1 182 ? 8.85885   23.66240  20.90179  1.000 12.69593 ?  194 LEU   B CG  1 
ATOM   3065 C  CD1 . LEU   B 1 182 ? 9.50207   22.29202  20.90228  1.000 16.63091 ?  194 LEU   B CD1 1 
ATOM   3066 C  CD2 . LEU   B 1 182 ? 9.88215   24.73122  21.25543  1.000 15.07126 ?  194 LEU   B CD2 1 
ATOM   3067 N  N   . TYR   B 1 183 ? 5.66905   21.88008  20.57831  1.000 10.03204 ?  195 TYR   B N   1 
ATOM   3068 C  CA  . TYR   B 1 183 ? 4.65528   21.73397  21.61762  1.000 10.60639 ?  195 TYR   B CA  1 
ATOM   3069 C  C   . TYR   B 1 183 ? 5.38249   21.57535  22.94155  1.000 9.64991  ?  195 TYR   B C   1 
ATOM   3070 O  O   . TYR   B 1 183 ? 6.06918   20.57649  23.16749  1.000 9.84699  ?  195 TYR   B O   1 
ATOM   3071 C  CB  . TYR   B 1 183 ? 3.76053   20.53531  21.30667  1.000 11.17434 ?  195 TYR   B CB  1 
ATOM   3072 C  CG  . TYR   B 1 183 ? 2.80066   20.15992  22.39275  1.000 10.25827 ?  195 TYR   B CG  1 
ATOM   3073 C  CD1 . TYR   B 1 183 ? 1.62742   20.86208  22.56351  1.000 15.70287 ?  195 TYR   B CD1 1 
ATOM   3074 C  CD2 . TYR   B 1 183 ? 3.05964   19.09236  23.23512  1.000 10.91594 ?  195 TYR   B CD2 1 
ATOM   3075 C  CE1 . TYR   B 1 183 ? 0.72887   20.51401  23.54539  1.000 18.58500 ?  195 TYR   B CE1 1 
ATOM   3076 C  CE2 . TYR   B 1 183 ? 2.17217   18.72928  24.20624  1.000 11.00564 ?  195 TYR   B CE2 1 
ATOM   3077 C  CZ  . TYR   B 1 183 ? 1.01928   19.44803  24.37352  1.000 15.44079 ?  195 TYR   B CZ  1 
ATOM   3078 O  OH  . TYR   B 1 183 ? 0.13272   19.07925  25.36411  1.000 20.56610 ?  195 TYR   B OH  1 
ATOM   3079 N  N   . GLY   B 1 184 ? 5.22296   22.56222  23.82162  1.000 8.30513  ?  196 GLY   B N   1 
ATOM   3080 C  CA  . GLY   B 1 184 ? 5.97343   22.53240  25.06039  1.000 10.12227 ?  196 GLY   B CA  1 
ATOM   3081 C  C   . GLY   B 1 184 ? 5.28410   21.83957  26.20105  1.000 9.37843  ?  196 GLY   B C   1 
ATOM   3082 O  O   . GLY   B 1 184 ? 5.90893   21.59551  27.23294  1.000 10.79044 ?  196 GLY   B O   1 
ATOM   3083 N  N   . GLY   B 1 185 ? 4.00771   21.50867  26.04812  1.000 10.72015 ?  197 GLY   B N   1 
ATOM   3084 C  CA  . GLY   B 1 185 ? 3.29177   20.98808  27.20187  1.000 10.26078 ?  197 GLY   B CA  1 
ATOM   3085 C  C   . GLY   B 1 185 ? 3.34423   21.96229  28.37607  1.000 9.44243  ?  197 GLY   B C   1 
ATOM   3086 O  O   . GLY   B 1 185 ? 3.53216   23.17818  28.22360  1.000 9.85571  ?  197 GLY   B O   1 
ATOM   3087 N  N   . CYS   B 1 186 ? 3.20213   21.40534  29.57800  1.000 9.83758  ?  198 CYS   B N   1 
ATOM   3088 C  CA  . CYS   B 1 186 ? 3.04128   22.25791  30.75291  1.000 9.77301  ?  198 CYS   B CA  1 
ATOM   3089 C  C   . CYS   B 1 186 ? 4.35301   22.87247  31.23631  1.000 8.81569  ?  198 CYS   B C   1 
ATOM   3090 O  O   . CYS   B 1 186 ? 4.33093   23.72184  32.13395  1.000 11.62733 ?  198 CYS   B O   1 
ATOM   3091 C  CB  . CYS   B 1 186 ? 2.28780   21.49902  31.84975  1.000 10.54946 ?  198 CYS   B CB  1 
ATOM   3092 S  SG  . CYS   B 1 186 ? 0.70800   20.86067  31.16621  1.000 14.09993 ?  198 CYS   B SG  1 
ATOM   3093 N  N   . ALA   B 1 187 ? 5.47704   22.52635  30.60616  1.000 9.12495  ?  199 ALA   B N   1 
ATOM   3094 C  CA  . ALA   B 1 187 ? 6.75355   23.18156  30.86382  1.000 10.33276 ?  199 ALA   B CA  1 
ATOM   3095 C  C   . ALA   B 1 187 ? 6.84866   24.57642  30.25416  1.000 8.96402  ?  199 ALA   B C   1 
ATOM   3096 O  O   . ALA   B 1 187 ? 7.75733   25.32502  30.61604  1.000 11.05876 ?  199 ALA   B O   1 
ATOM   3097 C  CB  . ALA   B 1 187 ? 7.89531   22.33982  30.29834  1.000 10.36275 ?  199 ALA   B CB  1 
ATOM   3098 N  N   . ILE   B 1 188 ? 5.93266   24.95481  29.36629  1.000 9.83731  ?  200 ILE   B N   1 
ATOM   3099 C  CA  . ILE   B 1 188 ? 5.95711   26.25937  28.71512  1.000 12.07112 ?  200 ILE   B CA  1 
ATOM   3100 C  C   . ILE   B 1 188 ? 4.64158   26.96548  29.00443  1.000 10.69047 ?  200 ILE   B C   1 
ATOM   3101 O  O   . ILE   B 1 188 ? 3.56652   26.38796  28.78249  1.000 11.48880 ?  200 ILE   B O   1 
ATOM   3102 C  CB  . ILE   B 1 188 ? 6.16094   26.11273  27.19702  1.000 11.02743 ?  200 ILE   B CB  1 
ATOM   3103 C  CG1 . ILE   B 1 188 ? 7.50641   25.46112  26.89345  1.000 11.11668 ?  200 ILE   B CG1 1 
ATOM   3104 C  CG2 . ILE   B 1 188 ? 6.07074   27.47814  26.49120  1.000 10.42830 ?  200 ILE   B CG2 1 
ATOM   3105 C  CD1 . ILE   B 1 188 ? 8.69897   26.16602  27.51903  1.000 13.02883 ?  200 ILE   B CD1 1 
ATOM   3106 N  N   . TYR   B 1 189 ? 4.73243   28.20964  29.48413  1.000 9.53974  ?  201 TYR   B N   1 
ATOM   3107 C  CA  . TYR   B 1 189 ? 3.58492   29.03847  29.83658  1.000 10.34099 ?  201 TYR   B CA  1 
ATOM   3108 C  C   . TYR   B 1 189 ? 3.22835   29.99544  28.69982  1.000 10.47579 ?  201 TYR   B C   1 
ATOM   3109 O  O   . TYR   B 1 189 ? 4.10827   30.51242  27.99726  1.000 11.62117 ?  201 TYR   B O   1 
ATOM   3110 C  CB  . TYR   B 1 189 ? 3.90942   29.89551  31.06367  1.000 11.17860 ?  201 TYR   B CB  1 
ATOM   3111 C  CG  . TYR   B 1 189 ? 3.94315   29.16670  32.39099  1.000 12.31780 ?  201 TYR   B CG  1 
ATOM   3112 C  CD1 . TYR   B 1 189 ? 3.58565   27.82870  32.50463  1.000 18.66077 ?  201 TYR   B CD1 1 
ATOM   3113 C  CD2 . TYR   B 1 189 ? 4.29149   29.84505  33.54715  1.000 23.23269 ?  201 TYR   B CD2 1 
ATOM   3114 C  CE1 . TYR   B 1 189 ? 3.60696   27.17779  33.74490  1.000 15.86123 ?  201 TYR   B CE1 1 
ATOM   3115 C  CE2 . TYR   B 1 189 ? 4.30419   29.21275  34.78213  1.000 26.67317 ?  201 TYR   B CE2 1 
ATOM   3116 C  CZ  . TYR   B 1 189 ? 3.95698   27.88420  34.87530  1.000 15.15624 ?  201 TYR   B CZ  1 
ATOM   3117 O  OH  . TYR   B 1 189 ? 3.97162   27.24948  36.10267  1.000 15.61005 ?  201 TYR   B OH  1 
ATOM   3118 N  N   . GLU   B 1 190 ? 1.92418   30.23778  28.53756  1.000 13.67323 ?  202 GLU   B N   1 
ATOM   3119 C  CA  . GLU   B 1 190 ? 1.46890   31.28088  27.63734  1.000 12.99018 ?  202 GLU   B CA  1 
ATOM   3120 C  C   . GLU   B 1 190 ? 1.81944   32.65314  28.21264  1.000 14.77250 ?  202 GLU   B C   1 
ATOM   3121 O  O   . GLU   B 1 190 ? 2.00542   32.82294  29.42527  1.000 14.11480 ?  202 GLU   B O   1 
ATOM   3122 C  CB  . GLU   B 1 190 ? -0.04449  31.19007  27.42190  1.000 15.55316 ?  202 GLU   B CB  1 
ATOM   3123 C  CG  . GLU   B 1 190 ? -0.88734  31.64678  28.60278  1.000 16.63360 ?  202 GLU   B CG  1 
ATOM   3124 C  CD  . GLU   B 1 190 ? -2.37691  31.76296  28.25901  1.000 15.45341 ?  202 GLU   B CD  1 
ATOM   3125 O  OE1 . GLU   B 1 190 ? -2.69954  32.25847  27.15116  1.000 17.28492 ?  202 GLU   B OE1 1 
ATOM   3126 O  OE2 . GLU   B 1 190 ? -3.20914  31.37809  29.10685  1.000 18.93148 ?  202 GLU   B OE2 1 
ATOM   3127 N  N   . LEU   B 1 191 ? 1.90671   33.63881  27.31500  1.000 12.68727 ?  203 LEU   B N   1 
ATOM   3128 C  CA  . LEU   B 1 191 ? 2.35945   34.97622  27.70436  1.000 12.04147 ?  203 LEU   B CA  1 
ATOM   3129 C  C   . LEU   B 1 191 ? 1.42311   35.63950  28.70761  1.000 20.90613 ?  203 LEU   B C   1 
ATOM   3130 O  O   . LEU   B 1 191 ? 1.87981   36.42365  29.54839  1.000 20.67757 ?  203 LEU   B O   1 
ATOM   3131 C  CB  . LEU   B 1 191 ? 2.47361   35.85793  26.46176  1.000 14.26666 ?  203 LEU   B CB  1 
ATOM   3132 C  CG  . LEU   B 1 191 ? 3.58637   35.50344  25.47846  1.000 13.54013 ?  203 LEU   B CG  1 
ATOM   3133 C  CD1 . LEU   B 1 191 ? 3.64661   36.43087  24.23920  1.000 17.47994 ?  203 LEU   B CD1 1 
ATOM   3134 C  CD2 . LEU   B 1 191 ? 4.93042   35.49682  26.19031  1.000 16.35874 ?  203 LEU   B CD2 1 
ATOM   3135 N  N   . SER   B 1 192 ? 0.12291   35.34691  28.63484  1.000 17.01359 ?  204 SER   B N   1 
ATOM   3136 C  CA  A SER   B 1 192 ? -0.85951  35.95223  29.53154  0.433 20.86160 ?  204 SER   B CA  1 
ATOM   3137 C  CA  B SER   B 1 192 ? -0.83234  35.98176  29.53402  0.567 20.85395 ?  204 SER   B CA  1 
ATOM   3138 C  C   . SER   B 1 192 ? -0.65330  35.53943  30.98009  1.000 26.41717 ?  204 SER   B C   1 
ATOM   3139 O  O   . SER   B 1 192 ? -1.11372  36.23683  31.89043  1.000 23.59754 ?  204 SER   B O   1 
ATOM   3140 C  CB  A SER   B 1 192 ? -2.26229  35.51235  29.11636  0.433 21.23994 ?  204 SER   B CB  1 
ATOM   3141 C  CB  B SER   B 1 192 ? -2.25651  35.71332  29.04495  0.567 21.76125 ?  204 SER   B CB  1 
ATOM   3142 O  OG  A SER   B 1 192 ? -2.64021  36.09583  27.88618  0.433 19.94227 ?  204 SER   B OG  1 
ATOM   3143 O  OG  B SER   B 1 192 ? -2.81256  34.56810  29.65999  0.567 20.87488 ?  204 SER   B OG  1 
ATOM   3144 N  N   . ARG   B 1 193 ? 0.00095   34.41119  31.21298  1.000 18.67503 ?  205 ARG   B N   1 
ATOM   3145 C  CA  A ARG   B 1 193 ? 0.20291   33.88977  32.55803  0.761 19.06725 ?  205 ARG   B CA  1 
ATOM   3146 C  CA  B ARG   B 1 193 ? 0.20308   33.88015  32.55387  0.239 19.22447 ?  205 ARG   B CA  1 
ATOM   3147 C  C   . ARG   B 1 193 ? 1.47959   34.49790  33.11634  1.000 17.74901 ?  205 ARG   B C   1 
ATOM   3148 O  O   . ARG   B 1 193 ? 2.57375   34.21747  32.62936  1.000 17.57960 ?  205 ARG   B O   1 
ATOM   3149 C  CB  A ARG   B 1 193 ? 0.29808   32.36876  32.52684  0.761 20.96081 ?  205 ARG   B CB  1 
ATOM   3150 C  CB  B ARG   B 1 193 ? 0.30293   32.36274  32.43696  0.239 21.04304 ?  205 ARG   B CB  1 
ATOM   3151 C  CG  A ARG   B 1 193 ? 0.51288   31.76211  33.88432  0.761 25.35082 ?  205 ARG   B CG  1 
ATOM   3152 C  CG  B ARG   B 1 193 ? 0.48648   31.56056  33.69769  0.239 25.25462 ?  205 ARG   B CG  1 
ATOM   3153 C  CD  A ARG   B 1 193 ? 0.84846   30.30192  33.74601  0.761 27.43547 ?  205 ARG   B CD  1 
ATOM   3154 C  CD  B ARG   B 1 193 ? 0.29062   30.11133  33.29353  0.239 25.47894 ?  205 ARG   B CD  1 
ATOM   3155 N  NE  A ARG   B 1 193 ? -0.22025  29.45432  34.25257  0.761 27.73595 ?  205 ARG   B NE  1 
ATOM   3156 N  NE  B ARG   B 1 193 ? 0.65639   29.12713  34.30128  0.239 25.30677 ?  205 ARG   B NE  1 
ATOM   3157 C  CZ  A ARG   B 1 193 ? -0.33736  28.16532  33.96775  0.761 29.13167 ?  205 ARG   B CZ  1 
ATOM   3158 C  CZ  B ARG   B 1 193 ? 0.36835   27.83755  34.19538  0.239 26.61196 ?  205 ARG   B CZ  1 
ATOM   3159 N  NH1 A ARG   B 1 193 ? 0.46706   27.57487  33.09633  0.761 24.34154 ?  205 ARG   B NH1 1 
ATOM   3160 N  NH1 B ARG   B 1 193 ? -0.31656  27.36688  33.16647  0.239 28.08069 ?  205 ARG   B NH1 1 
ATOM   3161 N  NH2 A ARG   B 1 193 ? -1.28996  27.45193  34.56331  0.761 36.19769 ?  205 ARG   B NH2 1 
ATOM   3162 N  NH2 B ARG   B 1 193 ? 0.77863   26.99924  35.14008  0.239 27.10754 ?  205 ARG   B NH2 1 
ATOM   3163 N  N   . THR   B 1 194 ? 1.34202   35.35532  34.12836  1.000 17.74596 ?  206 THR   B N   1 
ATOM   3164 C  CA  . THR   B 1 194 ? 2.49648   36.04269  34.69338  1.000 18.91355 ?  206 THR   B CA  1 
ATOM   3165 C  C   . THR   B 1 194 ? 2.86337   35.54855  36.07909  1.000 17.23800 ?  206 THR   B C   1 
ATOM   3166 O  O   . THR   B 1 194 ? 3.79888   36.09011  36.68188  1.000 19.75093 ?  206 THR   B O   1 
ATOM   3167 C  CB  . THR   B 1 194 ? 2.29783   37.56379  34.70624  1.000 21.08954 ?  206 THR   B CB  1 
ATOM   3168 O  OG1 . THR   B 1 194 ? 1.20452   37.88908  35.57346  1.000 21.46498 ?  206 THR   B OG1 1 
ATOM   3169 C  CG2 . THR   B 1 194 ? 2.00141   38.07055  33.30845  1.000 21.37632 ?  206 THR   B CG2 1 
ATOM   3170 N  N   . SER   B 1 195 ? 2.15392   34.55272  36.59977  1.000 15.88419 ?  207 SER   B N   1 
ATOM   3171 C  CA  A SER   B 1 195 ? 2.50680   33.90619  37.85294  0.559 18.36457 ?  207 SER   B CA  1 
ATOM   3172 C  CA  B SER   B 1 195 ? 2.50421   33.90693  37.85306  0.441 18.39756 ?  207 SER   B CA  1 
ATOM   3173 C  C   . SER   B 1 195 ? 2.55987   32.40391  37.62812  1.000 18.89065 ?  207 SER   B C   1 
ATOM   3174 O  O   . SER   B 1 195 ? 1.87809   31.87233  36.75013  1.000 17.73708 ?  207 SER   B O   1 
ATOM   3175 C  CB  A SER   B 1 195 ? 1.49048   34.22257  38.95925  0.559 21.10788 ?  207 SER   B CB  1 
ATOM   3176 C  CB  B SER   B 1 195 ? 1.48515   34.24140  38.95077  0.441 21.12578 ?  207 SER   B CB  1 
ATOM   3177 O  OG  A SER   B 1 195 ? 0.25997   33.57413  38.70776  0.559 26.73997 ?  207 SER   B OG  1 
ATOM   3178 O  OG  B SER   B 1 195 ? 1.60640   35.59948  39.33864  0.441 26.42484 ?  207 SER   B OG  1 
ATOM   3179 N  N   . ALA   B 1 196 ? 3.39401   31.72868  38.41492  1.000 16.09520 ?  208 ALA   B N   1 
ATOM   3180 C  CA  . ALA   B 1 196 ? 3.55224   30.29017  38.25594  1.000 17.15755 ?  208 ALA   B CA  1 
ATOM   3181 C  C   . ALA   B 1 196 ? 2.24212   29.57694  38.56715  1.000 19.06839 ?  208 ALA   B C   1 
ATOM   3182 O  O   . ALA   B 1 196 ? 1.44359   30.01724  39.40115  1.000 22.41051 ?  208 ALA   B O   1 
ATOM   3183 C  CB  . ALA   B 1 196 ? 4.64579   29.77878  39.19247  1.000 21.95208 ?  208 ALA   B CB  1 
ATOM   3184 N  N   . GLY   B 1 197 ? 2.00618   28.47170  37.88160  1.000 16.86169 ?  209 GLY   B N   1 
ATOM   3185 C  CA  . GLY   B 1 197 ? 0.82025   27.67672  38.13667  1.000 23.48217 ?  209 GLY   B CA  1 
ATOM   3186 C  C   . GLY   B 1 197 ? 1.00408   26.80388  39.35374  1.000 32.42236 ?  209 GLY   B C   1 
ATOM   3187 O  O   . GLY   B 1 197 ? 1.70293   27.15954  40.31385  1.000 31.54522 ?  209 GLY   B O   1 
ATOM   3188 N  N   . ASN   B 1 198 ? 0.36645   25.64422  39.32425  1.000 36.34472 ?  210 ASN   B N   1 
ATOM   3189 C  CA  . ASN   B 1 198 ? 0.70458   24.62803  40.30111  1.000 31.46855 ?  210 ASN   B CA  1 
ATOM   3190 C  C   . ASN   B 1 198 ? 2.10541   24.12116  39.99653  1.000 30.13207 ?  210 ASN   B C   1 
ATOM   3191 O  O   . ASN   B 1 198 ? 2.38692   23.65766  38.88431  1.000 29.09840 ?  210 ASN   B O   1 
ATOM   3192 C  CB  . ASN   B 1 198 ? -0.29766  23.48154  40.27027  1.000 33.90359 ?  210 ASN   B CB  1 
ATOM   3193 C  CG  . ASN   B 1 198 ? -0.00293  22.44538  41.32764  1.000 35.87058 ?  210 ASN   B CG  1 
ATOM   3194 O  OD1 . ASN   B 1 198 ? 0.83260   21.56202  41.12822  1.000 33.25417 ?  210 ASN   B OD1 1 
ATOM   3195 N  ND2 . ASN   B 1 198 ? -0.67339  22.55565  42.47005  1.000 45.02533 ?  210 ASN   B ND2 1 
ATOM   3196 N  N   . VAL   B 1 199 ? 2.99463   24.23682  40.97196  1.000 20.14219 ?  211 VAL   B N   1 
ATOM   3197 C  CA  . VAL   B 1 199 ? 4.36820   23.79321  40.80115  1.000 21.82243 ?  211 VAL   B CA  1 
ATOM   3198 C  C   . VAL   B 1 199 ? 4.72844   22.70884  41.81058  1.000 15.50878 ?  211 VAL   B C   1 
ATOM   3199 O  O   . VAL   B 1 199 ? 5.88571   22.48340  42.09219  1.000 19.34582 ?  211 VAL   B O   1 
ATOM   3200 C  CB  . VAL   B 1 199 ? 5.35336   24.97900  40.80554  1.000 21.41155 ?  211 VAL   B CB  1 
ATOM   3201 C  CG1 . VAL   B 1 199 ? 5.06844   25.89996  39.63094  1.000 25.81186 ?  211 VAL   B CG1 1 
ATOM   3202 C  CG2 . VAL   B 1 199 ? 5.23292   25.75851  42.10956  1.000 26.99787 ?  211 VAL   B CG2 1 
ATOM   3203 N  N   . ALA   B 1 200 ? 3.70796   22.02105  42.33864  1.000 20.07987 ?  212 ALA   B N   1 
ATOM   3204 C  CA  . ALA   B 1 200 ? 3.92703   21.07811  43.42925  1.000 19.74384 ?  212 ALA   B CA  1 
ATOM   3205 C  C   . ALA   B 1 200 ? 4.92524   19.99517  43.05923  1.000 17.81907 ?  212 ALA   B C   1 
ATOM   3206 O  O   . ALA   B 1 200 ? 5.68427   19.53940  43.91812  1.000 18.74297 ?  212 ALA   B O   1 
ATOM   3207 C  CB  . ALA   B 1 200 ? 2.59985   20.45778  43.87139  1.000 23.56297 ?  212 ALA   B CB  1 
ATOM   3208 N  N   . ASP   B 1 201 ? 4.95890   19.58074  41.79323  1.000 13.89542 ?  213 ASP   B N   1 
ATOM   3209 C  CA  . ASP   B 1 201 ? 5.85952   18.51996  41.35638  1.000 12.23062 ?  213 ASP   B CA  1 
ATOM   3210 C  C   . ASP   B 1 201 ? 7.00131   19.04073  40.49930  1.000 12.72844 ?  213 ASP   B C   1 
ATOM   3211 O  O   . ASP   B 1 201 ? 7.70753   18.25336  39.86233  1.000 13.20030 ?  213 ASP   B O   1 
ATOM   3212 C  CB  . ASP   B 1 201 ? 5.08229   17.41689  40.63403  1.000 15.15515 ?  213 ASP   B CB  1 
ATOM   3213 C  CG  . ASP   B 1 201 ? 4.11103   16.70164  41.55544  1.000 20.57292 ?  213 ASP   B CG  1 
ATOM   3214 O  OD1 . ASP   B 1 201 ? 4.46610   16.46120  42.73194  1.000 22.23108 ?  213 ASP   B OD1 1 
ATOM   3215 O  OD2 . ASP   B 1 201 ? 2.99824   16.36688  41.10133  1.000 15.73186 ?  213 ASP   B OD2 1 
ATOM   3216 N  N   . ALA   B 1 202 ? 7.20665   20.34954  40.49580  1.000 13.45753 ?  214 ALA   B N   1 
ATOM   3217 C  CA  . ALA   B 1 202 ? 8.17581   20.96141  39.61052  1.000 11.52731 ?  214 ALA   B CA  1 
ATOM   3218 C  C   . ALA   B 1 202 ? 9.56266   20.91854  40.22247  1.000 13.73742 ?  214 ALA   B C   1 
ATOM   3219 O  O   . ALA   B 1 202 ? 9.73193   20.74399  41.43582  1.000 15.35851 ?  214 ALA   B O   1 
ATOM   3220 C  CB  . ALA   B 1 202 ? 7.80235   22.41911  39.38217  1.000 12.73079 ?  214 ALA   B CB  1 
ATOM   3221 N  N   . ASP   B 1 203 ? 10.56220  21.08509  39.36217  1.000 12.07840 ?  215 ASP   B N   1 
ATOM   3222 C  CA  . ASP   B 1 203 ? 11.94133  21.30166  39.79013  1.000 13.75924 ?  215 ASP   B CA  1 
ATOM   3223 C  C   . ASP   B 1 203 ? 12.25014  22.74823  39.40876  1.000 12.93872 ?  215 ASP   B C   1 
ATOM   3224 O  O   . ASP   B 1 203 ? 12.70939  23.03237  38.29961  1.000 12.63982 ?  215 ASP   B O   1 
ATOM   3225 C  CB  . ASP   B 1 203 ? 12.85445  20.33770  39.07037  1.000 12.68209 ?  215 ASP   B CB  1 
ATOM   3226 C  CG  . ASP   B 1 203 ? 14.27128  20.38197  39.57970  1.000 18.05398 ?  215 ASP   B CG  1 
ATOM   3227 O  OD1 . ASP   B 1 203 ? 14.72076  21.46705  40.00616  1.000 14.97836 ?  215 ASP   B OD1 1 
ATOM   3228 O  OD2 . ASP   B 1 203 ? 14.93136  19.33205  39.52143  1.000 18.21546 ?  215 ASP   B OD2 1 
ATOM   3229 N  N   . LEU   B 1 204 ? 11.97952  23.66541  40.33739  1.000 12.11082 ?  216 LEU   B N   1 
ATOM   3230 C  CA  . LEU   B 1 204 ? 12.19038  25.08156  40.06996  1.000 12.71289 ?  216 LEU   B CA  1 
ATOM   3231 C  C   . LEU   B 1 204 ? 13.65120  25.37766  39.78523  1.000 11.41592 ?  216 LEU   B C   1 
ATOM   3232 O  O   . LEU   B 1 204 ? 13.96651  26.22226  38.93987  1.000 13.21600 ?  216 LEU   B O   1 
ATOM   3233 C  CB  . LEU   B 1 204 ? 11.72498  25.90437  41.26767  1.000 16.17013 ?  216 LEU   B CB  1 
ATOM   3234 C  CG  . LEU   B 1 204 ? 10.22707  25.88940  41.53642  1.000 15.86376 ?  216 LEU   B CG  1 
ATOM   3235 C  CD1 . LEU   B 1 204 ? 9.92824   26.61314  42.87136  1.000 18.31640 ?  216 LEU   B CD1 1 
ATOM   3236 C  CD2 . LEU   B 1 204 ? 9.49392   26.54081  40.39169  1.000 16.24986 ?  216 LEU   B CD2 1 
ATOM   3237 N  N   . ALA   B 1 205 ? 14.55601  24.68602  40.47913  1.000 13.02500 ?  217 ALA   B N   1 
ATOM   3238 C  CA  . ALA   B 1 205 ? 15.97113  24.98641  40.33472  1.000 13.39630 ?  217 ALA   B CA  1 
ATOM   3239 C  C   . ALA   B 1 205 ? 16.47702  24.64173  38.93996  1.000 12.35903 ?  217 ALA   B C   1 
ATOM   3240 O  O   . ALA   B 1 205 ? 17.36969  25.32268  38.41380  1.000 14.38151 ?  217 ALA   B O   1 
ATOM   3241 C  CB  . ALA   B 1 205 ? 16.76893  24.26027  41.41344  1.000 15.36847 ?  217 ALA   B CB  1 
ATOM   3242 N  N   . GLU   B 1 206 ? 15.90316  23.60777  38.31229  1.000 11.64896 ?  218 GLU   B N   1 
ATOM   3243 C  CA  A GLU   B 1 206 ? 16.35537  23.13987  37.00237  0.491 13.35307 ?  218 GLU   B CA  1 
ATOM   3244 C  CA  B GLU   B 1 206 ? 16.36077  23.14457  37.00594  0.509 13.34715 ?  218 GLU   B CA  1 
ATOM   3245 C  C   . GLU   B 1 206 ? 15.52922  23.67539  35.84452  1.000 9.59944  ?  218 GLU   B C   1 
ATOM   3246 O  O   . GLU   B 1 206 ? 16.00460  23.64429  34.70693  1.000 10.63001 ?  218 GLU   B O   1 
ATOM   3247 C  CB  A GLU   B 1 206 ? 16.35731  21.60532  36.91750  0.491 11.79137 ?  218 GLU   B CB  1 
ATOM   3248 C  CB  B GLU   B 1 206 ? 16.34837  21.60364  36.94978  0.509 11.78631 ?  218 GLU   B CB  1 
ATOM   3249 C  CG  A GLU   B 1 206 ? 17.37230  20.94515  37.78963  0.491 11.46654 ?  218 GLU   B CG  1 
ATOM   3250 C  CG  B GLU   B 1 206 ? 16.84608  20.93865  35.64666  0.509 14.28863 ?  218 GLU   B CG  1 
ATOM   3251 C  CD  A GLU   B 1 206 ? 18.74531  21.53960  37.59984  0.491 19.88092 ?  218 GLU   B CD  1 
ATOM   3252 C  CD  B GLU   B 1 206 ? 18.34675  21.09965  35.41136  0.509 17.87354 ?  218 GLU   B CD  1 
ATOM   3253 O  OE1 A GLU   B 1 206 ? 19.21538  21.63137  36.43704  0.491 20.60492 ?  218 GLU   B OE1 1 
ATOM   3254 O  OE1 B GLU   B 1 206 ? 19.01971  21.75612  36.22337  0.509 16.19077 ?  218 GLU   B OE1 1 
ATOM   3255 O  OE2 A GLU   B 1 206 ? 19.37231  21.87720  38.63054  0.491 18.11080 ?  218 GLU   B OE2 1 
ATOM   3256 O  OE2 B GLU   B 1 206 ? 18.85719  20.56420  34.40543  0.509 19.31161 ?  218 GLU   B OE2 1 
ATOM   3257 N  N   . TRP   B 1 207 ? 14.32419  24.17560  36.11228  1.000 10.06678 ?  219 TRP   B N   1 
ATOM   3258 C  CA  . TRP   B 1 207 ? 13.40782  24.56429  35.03940  1.000 8.65599  ?  219 TRP   B CA  1 
ATOM   3259 C  C   . TRP   B 1 207 ? 14.01999  25.54728  34.04460  1.000 12.41304 ?  219 TRP   B C   1 
ATOM   3260 O  O   . TRP   B 1 207 ? 13.90826  25.30595  32.83565  1.000 10.66580 ?  219 TRP   B O   1 
ATOM   3261 C  CB  . TRP   B 1 207 ? 12.10199  25.02495  35.69629  1.000 9.82223  ?  219 TRP   B CB  1 
ATOM   3262 C  CG  . TRP   B 1 207 ? 10.87894  25.15663  34.82390  1.000 8.56658  ?  219 TRP   B CG  1 
ATOM   3263 C  CD1 . TRP   B 1 207 ? 10.80853  25.35213  33.46484  1.000 10.70772 ?  219 TRP   B CD1 1 
ATOM   3264 C  CD2 . TRP   B 1 207 ? 9.53844   25.15320  35.30401  1.000 9.07118  ?  219 TRP   B CD2 1 
ATOM   3265 N  NE1 . TRP   B 1 207 ? 9.48409   25.44479  33.07496  1.000 11.06718 ?  219 TRP   B NE1 1 
ATOM   3266 C  CE2 . TRP   B 1 207 ? 8.69094   25.31985  34.19177  1.000 8.51145  ?  219 TRP   B CE2 1 
ATOM   3267 C  CE3 . TRP   B 1 207 ? 8.96925   24.97822  36.56924  1.000 11.98740 ?  219 TRP   B CE3 1 
ATOM   3268 C  CZ2 . TRP   B 1 207 ? 7.30191   25.33970  34.32432  1.000 10.29888 ?  219 TRP   B CZ2 1 
ATOM   3269 C  CZ3 . TRP   B 1 207 ? 7.60665   25.02432  36.69882  1.000 12.66977 ?  219 TRP   B CZ3 1 
ATOM   3270 C  CH2 . TRP   B 1 207 ? 6.77993   25.18616  35.58179  1.000 12.32062 ?  219 TRP   B CH2 1 
ATOM   3271 N  N   . PRO   B 1 208 ? 14.67992  26.63788  34.45607  1.000 10.85225 ?  220 PRO   B N   1 
ATOM   3272 C  CA  . PRO   B 1 208 ? 15.30658  27.50593  33.43752  1.000 10.29031 ?  220 PRO   B CA  1 
ATOM   3273 C  C   . PRO   B 1 208 ? 16.34730  26.80027  32.58821  1.000 11.18858 ?  220 PRO   B C   1 
ATOM   3274 O  O   . PRO   B 1 208 ? 16.42292  27.04814  31.38613  1.000 11.59630 ?  220 PRO   B O   1 
ATOM   3275 C  CB  . PRO   B 1 208 ? 15.90098  28.65007  34.27179  1.000 10.28201 ?  220 PRO   B CB  1 
ATOM   3276 C  CG  . PRO   B 1 208 ? 15.00905  28.69009  35.48735  1.000 11.11211 ?  220 PRO   B CG  1 
ATOM   3277 C  CD  . PRO   B 1 208 ? 14.77204  27.23512  35.80129  1.000 11.48076 ?  220 PRO   B CD  1 
ATOM   3278 N  N   . THR   B 1 209 ? 17.18351  25.95095  33.19319  1.000 11.08226 ?  221 THR   B N   1 
ATOM   3279 C  CA  . THR   B 1 209 ? 18.16833  25.21062  32.41463  1.000 11.88311 ?  221 THR   B CA  1 
ATOM   3280 C  C   . THR   B 1 209 ? 17.48762  24.29888  31.40503  1.000 11.38994 ?  221 THR   B C   1 
ATOM   3281 O  O   . THR   B 1 209 ? 17.93234  24.17530  30.25365  1.000 11.07481 ?  221 THR   B O   1 
ATOM   3282 C  CB  . THR   B 1 209 ? 19.03044  24.39234  33.37644  1.000 13.41973 ?  221 THR   B CB  1 
ATOM   3283 O  OG1 . THR   B 1 209 ? 19.71662  25.29470  34.26272  1.000 14.67088 ?  221 THR   B OG1 1 
ATOM   3284 C  CG2 . THR   B 1 209 ? 20.04646  23.56851  32.62580  1.000 16.93428 ?  221 THR   B CG2 1 
ATOM   3285 N  N   . SER   B 1 210 ? 16.38566  23.66492  31.81676  1.000 9.25688  ?  222 SER   B N   1 
ATOM   3286 C  CA  . SER   B 1 210 ? 15.64427  22.80655  30.89273  1.000 9.78866  ?  222 SER   B CA  1 
ATOM   3287 C  C   . SER   B 1 210 ? 15.06023  23.60301  29.73198  1.000 11.41886 ?  222 SER   B C   1 
ATOM   3288 O  O   . SER   B 1 210 ? 15.09450  23.14874  28.58017  1.000 10.70380 ?  222 SER   B O   1 
ATOM   3289 C  CB  . SER   B 1 210 ? 14.56571  22.04321  31.65726  1.000 9.65821  ?  222 SER   B CB  1 
ATOM   3290 O  OG  . SER   B 1 210 ? 15.18789  21.22253  32.64691  1.000 10.23662 ?  222 SER   B OG  1 
ATOM   3291 N  N   . ILE   B 1 211 ? 14.53985  24.80312  30.00906  1.000 10.90675 ?  223 ILE   B N   1 
ATOM   3292 C  CA  . ILE   B 1 211 ? 14.04606  25.65868  28.93171  1.000 10.33845 ?  223 ILE   B CA  1 
ATOM   3293 C  C   . ILE   B 1 211 ? 15.16907  26.01750  27.96318  1.000 11.01447 ?  223 ILE   B C   1 
ATOM   3294 O  O   . ILE   B 1 211 ? 14.97758  26.01317  26.74007  1.000 10.97034 ?  223 ILE   B O   1 
ATOM   3295 C  CB  . ILE   B 1 211 ? 13.34353  26.90229  29.50531  1.000 9.55297  ?  223 ILE   B CB  1 
ATOM   3296 C  CG1 . ILE   B 1 211 ? 11.97918  26.51061  30.07040  1.000 12.28806 ?  223 ILE   B CG1 1 
ATOM   3297 C  CG2 . ILE   B 1 211 ? 13.20237  28.01817  28.42153  1.000 12.04414 ?  223 ILE   B CG2 1 
ATOM   3298 C  CD1 . ILE   B 1 211 ? 11.35879  27.60940  30.88457  1.000 17.16356 ?  223 ILE   B CD1 1 
ATOM   3299 N  N   . GLU   B 1 212 ? 16.36032  26.32262  28.49620  1.000 12.47447 ?  224 GLU   B N   1 
ATOM   3300 C  CA  A GLU   B 1 212 ? 17.47140  26.65647  27.61297  0.648 10.70031 ?  224 GLU   B CA  1 
ATOM   3301 C  CA  B GLU   B 1 212 ? 17.51370  26.63658  27.65190  0.352 10.82924 ?  224 GLU   B CA  1 
ATOM   3302 C  C   . GLU   B 1 212 ? 17.84389  25.48243  26.71250  1.000 12.98837 ?  224 GLU   B C   1 
ATOM   3303 O  O   . GLU   B 1 212 ? 18.21548  25.69361  25.55291  1.000 12.71661 ?  224 GLU   B O   1 
ATOM   3304 C  CB  A GLU   B 1 212 ? 18.66705  27.18422  28.41645  0.648 14.73642 ?  224 GLU   B CB  1 
ATOM   3305 C  CB  B GLU   B 1 212 ? 18.72989  26.94448  28.53040  0.352 14.63557 ?  224 GLU   B CB  1 
ATOM   3306 C  CG  A GLU   B 1 212 ? 19.91306  27.51561  27.57550  0.648 15.82346 ?  224 GLU   B CG  1 
ATOM   3307 C  CG  B GLU   B 1 212 ? 18.61972  28.20704  29.35332  0.352 14.10104 ?  224 GLU   B CG  1 
ATOM   3308 C  CD  A GLU   B 1 212 ? 19.67302  28.58442  26.50942  0.648 17.27332 ?  224 GLU   B CD  1 
ATOM   3309 C  CD  B GLU   B 1 212 ? 19.78160  28.38350  30.31906  0.352 19.24663 ?  224 GLU   B CD  1 
ATOM   3310 O  OE1 A GLU   B 1 212 ? 18.77539  29.44337  26.66628  0.648 19.90066 ?  224 GLU   B OE1 1 
ATOM   3311 O  OE1 B GLU   B 1 212 ? 20.61319  27.45475  30.44655  0.352 24.16705 ?  224 GLU   B OE1 1 
ATOM   3312 O  OE2 A GLU   B 1 212 ? 20.40716  28.56592  25.49833  0.648 25.35962 ?  224 GLU   B OE2 1 
ATOM   3313 O  OE2 B GLU   B 1 212 ? 19.84806  29.44531  30.96947  0.352 24.54705 ?  224 GLU   B OE2 1 
ATOM   3314 N  N   . ARG   B 1 213 ? 17.72878  24.23998  27.20659  1.000 11.58420 ?  225 ARG   B N   1 
ATOM   3315 C  CA  . ARG   B 1 213 ? 17.95862  23.08577  26.33827  1.000 9.99328  ?  225 ARG   B CA  1 
ATOM   3316 C  C   . ARG   B 1 213 ? 16.95575  23.05087  25.18946  1.000 11.33138 ?  225 ARG   B C   1 
ATOM   3317 O  O   . ARG   B 1 213 ? 17.30975  22.67817  24.06451  1.000 12.06030 ?  225 ARG   B O   1 
ATOM   3318 C  CB  . ARG   B 1 213 ? 17.89411  21.77701  27.14036  1.000 12.54047 ?  225 ARG   B CB  1 
ATOM   3319 C  CG  . ARG   B 1 213 ? 19.01855  21.59431  28.16940  1.000 12.02386 ?  225 ARG   B CG  1 
ATOM   3320 C  CD  . ARG   B 1 213 ? 19.15461  20.12191  28.62708  1.000 14.15015 ?  225 ARG   B CD  1 
ATOM   3321 N  NE  . ARG   B 1 213 ? 20.07925  19.98957  29.74773  1.000 15.07472 ?  225 ARG   B NE  1 
ATOM   3322 C  CZ  . ARG   B 1 213 ? 19.75121  20.12664  31.02378  1.000 16.97528 ?  225 ARG   B CZ  1 
ATOM   3323 N  NH1 . ARG   B 1 213 ? 18.49357  20.30313  31.41040  1.000 14.52324 ?  225 ARG   B NH1 1 
ATOM   3324 N  NH2 . ARG   B 1 213 ? 20.70855  20.09637  31.94304  1.000 18.22363 ?  225 ARG   B NH2 1 
ATOM   3325 N  N   . ILE   B 1 214 ? 15.69180  23.41408  25.46014  1.000 10.38699 ?  226 ILE   B N   1 
ATOM   3326 C  CA  . ILE   B 1 214 ? 14.70160  23.47141  24.38699  1.000 9.91114  ?  226 ILE   B CA  1 
ATOM   3327 C  C   . ILE   B 1 214 ? 15.10929  24.51478  23.35030  1.000 10.76122 ?  226 ILE   B C   1 
ATOM   3328 O  O   . ILE   B 1 214 ? 15.07767  24.26525  22.13937  1.000 11.64104 ?  226 ILE   B O   1 
ATOM   3329 C  CB  . ILE   B 1 214 ? 13.30416  23.76398  24.95590  1.000 8.83421  ?  226 ILE   B CB  1 
ATOM   3330 C  CG1 . ILE   B 1 214 ? 12.85087  22.66549  25.91602  1.000 9.60099  ?  226 ILE   B CG1 1 
ATOM   3331 C  CG2 . ILE   B 1 214 ? 12.29945  23.88570  23.82592  1.000 10.36800 ?  226 ILE   B CG2 1 
ATOM   3332 C  CD1 . ILE   B 1 214 ? 11.63462  23.06885  26.74831  1.000 11.05466 ?  226 ILE   B CD1 1 
ATOM   3333 N  N   . GLN   B 1 215 ? 15.46636  25.71301  23.81624  1.000 11.53866 ?  227 GLN   B N   1 
ATOM   3334 C  CA  . GLN   B 1 215 ? 15.90930  26.75762  22.89254  1.000 13.54188 ?  227 GLN   B CA  1 
ATOM   3335 C  C   . GLN   B 1 215 ? 17.09895  26.29280  22.05771  1.000 13.96021 ?  227 GLN   B C   1 
ATOM   3336 O  O   . GLN   B 1 215 ? 17.14534  26.51376  20.84108  1.000 16.24182 ?  227 GLN   B O   1 
ATOM   3337 C  CB  . GLN   B 1 215 ? 16.27917  28.00979  23.67585  1.000 13.32477 ?  227 GLN   B CB  1 
ATOM   3338 C  CG  . GLN   B 1 215 ? 17.09064  29.02127  22.84654  1.000 16.39082 ?  227 GLN   B CG  1 
ATOM   3339 C  CD  . GLN   B 1 215 ? 16.25068  29.66226  21.75387  1.000 18.52884 ?  227 GLN   B CD  1 
ATOM   3340 O  OE1 . GLN   B 1 215 ? 15.14521  30.14060  22.01157  1.000 16.79746 ?  227 GLN   B OE1 1 
ATOM   3341 N  NE2 . GLN   B 1 215 ? 16.78000  29.70003  20.53484  1.000 18.81285 ?  227 GLN   B NE2 1 
ATOM   3342 N  N   . GLN   B 1 216 ? 18.08291  25.65984  22.70181  1.000 12.40102 ?  228 GLN   B N   1 
ATOM   3343 C  CA  . GLN   B 1 216 ? 19.26956  25.20301  21.98400  1.000 15.68236 ?  228 GLN   B CA  1 
ATOM   3344 C  C   . GLN   B 1 216 ? 18.93620  24.12553  20.96350  1.000 18.52744 ?  228 GLN   B C   1 
ATOM   3345 O  O   . GLN   B 1 216 ? 19.58362  24.03516  19.91266  1.000 15.66662 ?  228 GLN   B O   1 
ATOM   3346 C  CB  . GLN   B 1 216 ? 20.27511  24.65186  22.99354  1.000 19.05278 ?  228 GLN   B CB  1 
ATOM   3347 C  CG  . GLN   B 1 216 ? 21.10951  25.71203  23.70244  1.000 30.07398 ?  228 GLN   B CG  1 
ATOM   3348 C  CD  . GLN   B 1 216 ? 21.71063  26.72196  22.74593  1.000 37.75425 ?  228 GLN   B CD  1 
ATOM   3349 O  OE1 . GLN   B 1 216 ? 21.32297  27.89282  22.72699  1.000 39.10074 ?  228 GLN   B OE1 1 
ATOM   3350 N  NE2 . GLN   B 1 216 ? 22.65934  26.26849  21.93662  1.000 32.23356 ?  228 GLN   B NE2 1 
ATOM   3351 N  N   . HIS   B 1 217 ? 17.95033  23.28320  21.25198  1.000 13.98129 ?  229 HIS   B N   1 
ATOM   3352 C  CA  . HIS   B 1 217 ? 17.65220  22.17296  20.36162  1.000 12.62339 ?  229 HIS   B CA  1 
ATOM   3353 C  C   . HIS   B 1 217 ? 16.70239  22.53937  19.23029  1.000 12.10491 ?  229 HIS   B C   1 
ATOM   3354 O  O   . HIS   B 1 217 ? 16.81366  21.96710  18.13468  1.000 15.24912 ?  229 HIS   B O   1 
ATOM   3355 C  CB  . HIS   B 1 217 ? 17.09327  20.98663  21.14820  1.000 13.77502 ?  229 HIS   B CB  1 
ATOM   3356 C  CG  . HIS   B 1 217 ? 17.32669  19.66938  20.48154  1.000 16.01947 ?  229 HIS   B CG  1 
ATOM   3357 N  ND1 . HIS   B 1 217 ? 18.52034  18.98924  20.58734  1.000 28.05918 ?  229 HIS   B ND1 1 
ATOM   3358 C  CD2 . HIS   B 1 217 ? 16.53244  18.91139  19.68987  1.000 17.83587 ?  229 HIS   B CD2 1 
ATOM   3359 C  CE1 . HIS   B 1 217 ? 18.45103  17.86931  19.89149  1.000 21.20128 ?  229 HIS   B CE1 1 
ATOM   3360 N  NE2 . HIS   B 1 217 ? 17.25719  17.79766  19.33651  1.000 20.06214 ?  229 HIS   B NE2 1 
ATOM   3361 N  N   . TYR   B 1 218 ? 15.79674  23.49650  19.45683  1.000 11.72380 ?  230 TYR   B N   1 
ATOM   3362 C  CA  . TYR   B 1 218 ? 14.77682  23.86366  18.47167  1.000 11.85691 ?  230 TYR   B CA  1 
ATOM   3363 C  C   . TYR   B 1 218 ? 14.77397  25.36292  18.18187  1.000 13.57328 ?  230 TYR   B C   1 
ATOM   3364 O  O   . TYR   B 1 218 ? 13.71668  25.99818  18.16357  1.000 13.69317 ?  230 TYR   B O   1 
ATOM   3365 C  CB  . TYR   B 1 218 ? 13.40519  23.42400  18.97261  1.000 12.91383 ?  230 TYR   B CB  1 
ATOM   3366 C  CG  . TYR   B 1 218 ? 13.31460  21.94111  19.17304  1.000 12.41201 ?  230 TYR   B CG  1 
ATOM   3367 C  CD1 . TYR   B 1 218 ? 13.40345  21.07764  18.09673  1.000 11.16350 ?  230 TYR   B CD1 1 
ATOM   3368 C  CD2 . TYR   B 1 218 ? 13.15941  21.40224  20.45211  1.000 12.67149 ?  230 TYR   B CD2 1 
ATOM   3369 C  CE1 . TYR   B 1 218 ? 13.34783  19.70603  18.26903  1.000 12.84258 ?  230 TYR   B CE1 1 
ATOM   3370 C  CE2 . TYR   B 1 218 ? 13.08377  20.02230  20.63820  1.000 13.09449 ?  230 TYR   B CE2 1 
ATOM   3371 C  CZ  . TYR   B 1 218 ? 13.17767  19.18973  19.54278  1.000 14.07906 ?  230 TYR   B CZ  1 
ATOM   3372 O  OH  . TYR   B 1 218 ? 13.12323  17.82665  19.68888  1.000 15.57341 ?  230 TYR   B OH  1 
ATOM   3373 N  N   . PRO   B 1 219 ? 15.94050  25.95086  17.87335  1.000 14.40865 ?  231 PRO   B N   1 
ATOM   3374 C  CA  . PRO   B 1 219 ? 15.97569  27.40061  17.63286  1.000 14.72446 ?  231 PRO   B CA  1 
ATOM   3375 C  C   . PRO   B 1 219 ? 15.23947  27.82319  16.37659  1.000 12.55091 ?  231 PRO   B C   1 
ATOM   3376 O  O   . PRO   B 1 219 ? 14.92955  29.01058  16.23409  1.000 15.49717 ?  231 PRO   B O   1 
ATOM   3377 C  CB  . PRO   B 1 219 ? 17.47668  27.69697  17.53199  1.000 15.88216 ?  231 PRO   B CB  1 
ATOM   3378 C  CG  . PRO   B 1 219 ? 18.04247  26.47025  16.92194  1.000 14.28596 ?  231 PRO   B CG  1 
ATOM   3379 C  CD  . PRO   B 1 219 ? 17.24719  25.33003  17.59054  1.000 14.96217 ?  231 PRO   B CD  1 
ATOM   3380 N  N   . GLU   B 1 220 ? 14.92774  26.88283  15.49109  1.000 12.74480 ?  232 GLU   B N   1 
ATOM   3381 C  CA  . GLU   B 1 220 ? 14.19160  27.13954  14.25889  1.000 14.47771 ?  232 GLU   B CA  1 
ATOM   3382 C  C   . GLU   B 1 220 ? 12.67444  27.11172  14.44004  1.000 13.36256 ?  232 GLU   B C   1 
ATOM   3383 O  O   . GLU   B 1 220 ? 11.94072  27.32171  13.46872  1.000 14.58173 ?  232 GLU   B O   1 
ATOM   3384 C  CB  . GLU   B 1 220 ? 14.61957  26.13015  13.18060  1.000 13.21840 ?  232 GLU   B CB  1 
ATOM   3385 C  CG  . GLU   B 1 220 ? 13.96418  24.75151  13.29839  1.000 14.13072 ?  232 GLU   B CG  1 
ATOM   3386 C  CD  . GLU   B 1 220 ? 14.70967  23.80975  14.22328  1.000 14.26765 ?  232 GLU   B CD  1 
ATOM   3387 O  OE1 . GLU   B 1 220 ? 15.39767  24.28839  15.15253  1.000 17.55789 ?  232 GLU   B OE1 1 
ATOM   3388 O  OE2 . GLU   B 1 220 ? 14.58992  22.57777  14.02582  1.000 17.14221 ?  232 GLU   B OE2 1 
ATOM   3389 N  N   . ALA   B 1 221 ? 12.17484  26.85997  15.65463  1.000 12.60764 ?  233 ALA   B N   1 
ATOM   3390 C  CA  . ALA   B 1 221 ? 10.73458  26.71006  15.82434  1.000 13.21264 ?  233 ALA   B CA  1 
ATOM   3391 C  C   . ALA   B 1 221 ? 10.01306  28.01595  15.50108  1.000 14.81129 ?  233 ALA   B C   1 
ATOM   3392 O  O   . ALA   B 1 221 ? 10.45104  29.09785  15.89477  1.000 15.19042 ?  233 ALA   B O   1 
ATOM   3393 C  CB  . ALA   B 1 221 ? 10.42338  26.26551  17.25203  1.000 12.92352 ?  233 ALA   B CB  1 
ATOM   3394 N  N   . GLN   B 1 222 ? 8.90667   27.90973  14.76735  1.000 13.63985 ?  234 GLN   B N   1 
ATOM   3395 C  CA  . GLN   B 1 222 ? 8.09314   29.05898  14.37564  1.000 16.70634 ?  234 GLN   B CA  1 
ATOM   3396 C  C   . GLN   B 1 222 ? 6.80358   29.19462  15.16993  1.000 18.36433 ?  234 GLN   B C   1 
ATOM   3397 O  O   . GLN   B 1 222 ? 6.29722   30.30899  15.32472  1.000 21.04692 ?  234 GLN   B O   1 
ATOM   3398 C  CB  . GLN   B 1 222 ? 7.75969   29.00157  12.87787  1.000 16.08218 ?  234 GLN   B CB  1 
ATOM   3399 C  CG  . GLN   B 1 222 ? 8.96292   29.23007  12.00123  1.000 20.82240 ?  234 GLN   B CG  1 
ATOM   3400 C  CD  . GLN   B 1 222 ? 9.61659   30.56533  12.31435  1.000 32.70986 ?  234 GLN   B CD  1 
ATOM   3401 O  OE1 . GLN   B 1 222 ? 10.66849  30.62708  12.95277  1.000 35.97138 ?  234 GLN   B OE1 1 
ATOM   3402 N  NE2 . GLN   B 1 222 ? 8.98742   31.64998  11.86412  1.000 33.91237 ?  234 GLN   B NE2 1 
ATOM   3403 N  N   . PHE   B 1 223 ? 6.24345   28.08883  15.64123  1.000 12.92807 ?  235 PHE   B N   1 
ATOM   3404 C  CA  A PHE   B 1 223 ? 5.02395   28.10190  16.43205  0.641 11.78023 ?  235 PHE   B CA  1 
ATOM   3405 C  CA  B PHE   B 1 223 ? 5.01079   28.07340  16.41282  0.359 11.92611 ?  235 PHE   B CA  1 
ATOM   3406 C  C   . PHE   B 1 223 ? 5.31347   27.34534  17.71288  1.000 14.19814 ?  235 PHE   B C   1 
ATOM   3407 O  O   . PHE   B 1 223 ? 5.86207   26.23760  17.67948  1.000 17.45505 ?  235 PHE   B O   1 
ATOM   3408 C  CB  A PHE   B 1 223 ? 3.86267   27.41654  15.69736  0.641 14.68814 ?  235 PHE   B CB  1 
ATOM   3409 C  CB  B PHE   B 1 223 ? 3.97328   27.27313  15.61893  0.359 14.73024 ?  235 PHE   B CB  1 
ATOM   3410 C  CG  A PHE   B 1 223 ? 3.60871   27.94468  14.31801  0.641 18.58342 ?  235 PHE   B CG  1 
ATOM   3411 C  CG  B PHE   B 1 223 ? 2.54564   27.63939  15.90316  0.359 15.71944 ?  235 PHE   B CG  1 
ATOM   3412 C  CD1 A PHE   B 1 223 ? 4.24658   27.38785  13.22529  0.641 15.59968 ?  235 PHE   B CD1 1 
ATOM   3413 C  CD1 B PHE   B 1 223 ? 1.92959   28.68837  15.23187  0.359 16.46928 ?  235 PHE   B CD1 1 
ATOM   3414 C  CD2 A PHE   B 1 223 ? 2.71805   28.98672  14.10960  0.641 17.61068 ?  235 PHE   B CD2 1 
ATOM   3415 C  CD2 B PHE   B 1 223 ? 1.80513   26.90411  16.80871  0.359 16.75663 ?  235 PHE   B CD2 1 
ATOM   3416 C  CE1 A PHE   B 1 223 ? 4.01087   27.85876  11.94679  0.641 17.52500 ?  235 PHE   B CE1 1 
ATOM   3417 C  CE1 B PHE   B 1 223 ? 0.60679   29.01075  15.48503  0.359 19.03078 ?  235 PHE   B CE1 1 
ATOM   3418 C  CE2 A PHE   B 1 223 ? 2.47582   29.45960  12.83236  0.641 22.50325 ?  235 PHE   B CE2 1 
ATOM   3419 C  CE2 B PHE   B 1 223 ? 0.48396   27.21424  17.05732  0.359 14.35157 ?  235 PHE   B CE2 1 
ATOM   3420 C  CZ  A PHE   B 1 223 ? 3.13054   28.90204  11.75535  0.641 20.00088 ?  235 PHE   B CZ  1 
ATOM   3421 C  CZ  B PHE   B 1 223 ? -0.11570  28.27243  16.39463  0.359 16.83304 ?  235 PHE   B CZ  1 
ATOM   3422 N  N   . VAL   B 1 224 ? 4.98217   27.95452  18.84462  1.000 12.32436 ?  236 VAL   B N   1 
ATOM   3423 C  CA  . VAL   B 1 224 ? 5.21798   27.32890  20.14271  1.000 10.93394 ?  236 VAL   B CA  1 
ATOM   3424 C  C   . VAL   B 1 224 ? 3.88647   27.22469  20.86174  1.000 10.74555 ?  236 VAL   B C   1 
ATOM   3425 O  O   . VAL   B 1 224 ? 3.19550   28.23178  21.03893  1.000 12.20724 ?  236 VAL   B O   1 
ATOM   3426 C  CB  . VAL   B 1 224 ? 6.25424   28.10370  20.96676  1.000 10.29291 ?  236 VAL   B CB  1 
ATOM   3427 C  CG1 . VAL   B 1 224 ? 6.47642   27.42163  22.30866  1.000 13.26563 ?  236 VAL   B CG1 1 
ATOM   3428 C  CG2 . VAL   B 1 224 ? 7.56165   28.17666  20.16410  1.000 12.49214 ?  236 VAL   B CG2 1 
ATOM   3429 N  N   . ILE   B 1 225 ? 3.51812   26.01230  21.25970  1.000 11.37896 ?  237 ILE   B N   1 
ATOM   3430 C  CA  A ILE   B 1 225 ? 2.23089   25.72582  21.88957  0.542 10.46738 ?  237 ILE   B CA  1 
ATOM   3431 C  CA  B ILE   B 1 225 ? 2.23245   25.75035  21.89859  0.458 10.46226 ?  237 ILE   B CA  1 
ATOM   3432 C  C   . ILE   B 1 225 ? 2.46824   25.43859  23.36895  1.000 12.11343 ?  237 ILE   B C   1 
ATOM   3433 O  O   . ILE   B 1 225 ? 3.12569   24.44184  23.69482  1.000 10.55502 ?  237 ILE   B O   1 
ATOM   3434 C  CB  A ILE   B 1 225 ? 1.55355   24.51888  21.22375  0.542 11.48592 ?  237 ILE   B CB  1 
ATOM   3435 C  CB  B ILE   B 1 225 ? 1.49503   24.59344  21.22679  0.458 11.51702 ?  237 ILE   B CB  1 
ATOM   3436 C  CG1 A ILE   B 1 225 ? 1.63853   24.61077  19.69140  0.542 13.15353 ?  237 ILE   B CG1 1 
ATOM   3437 C  CG1 B ILE   B 1 225 ? 1.38445   24.87605  19.74288  0.458 13.79640 ?  237 ILE   B CG1 1 
ATOM   3438 C  CG2 A ILE   B 1 225 ? 0.12480   24.35985  21.74004  0.542 12.53439 ?  237 ILE   B CG2 1 
ATOM   3439 C  CG2 B ILE   B 1 225 ? 0.13507   24.38210  21.88738  0.458 12.32360 ?  237 ILE   B CG2 1 
ATOM   3440 C  CD1 A ILE   B 1 225 ? 0.95783   25.81547  19.09006  0.542 13.75687 ?  237 ILE   B CD1 1 
ATOM   3441 C  CD1 B ILE   B 1 225 ? 1.16678   23.67018  19.00567  0.458 12.90557 ?  237 ILE   B CD1 1 
ATOM   3442 N  N   . PRO   B 1 226 ? 1.90986   26.21888  24.27766  1.000 9.91662  ?  238 PRO   B N   1 
ATOM   3443 C  CA  . PRO   B 1 226 ? 2.02488   25.92210  25.70415  1.000 11.64960 ?  238 PRO   B CA  1 
ATOM   3444 C  C   . PRO   B 1 226 ? 0.98974   24.87179  26.08632  1.000 9.46706  ?  238 PRO   B C   1 
ATOM   3445 O  O   . PRO   B 1 226 ? 0.07093   24.56844  25.33147  1.000 10.01313 ?  238 PRO   B O   1 
ATOM   3446 C  CB  . PRO   B 1 226 ? 1.68478   27.27538  26.34494  1.000 12.30649 ?  238 PRO   B CB  1 
ATOM   3447 C  CG  . PRO   B 1 226 ? 0.65351   27.85958  25.40971  1.000 12.83228 ?  238 PRO   B CG  1 
ATOM   3448 C  CD  . PRO   B 1 226 ? 1.07168   27.40575  24.01018  1.000 12.19359 ?  238 PRO   B CD  1 
ATOM   3449 N  N   . GLY   B 1 227 ? 1.13811   24.32698  27.29643  1.000 11.45364 ?  239 GLY   B N   1 
ATOM   3450 C  CA  . GLY   B 1 227 ? 0.17982   23.34030  27.76932  1.000 12.07462 ?  239 GLY   B CA  1 
ATOM   3451 C  C   . GLY   B 1 227 ? -1.20876  23.91508  27.95469  1.000 10.77959 ?  239 GLY   B C   1 
ATOM   3452 O  O   . GLY   B 1 227 ? -2.20360  23.18235  27.88783  1.000 10.33745 ?  239 GLY   B O   1 
ATOM   3453 N  N   . HIS   B 1 228 ? -1.29274  25.21916  28.20701  1.000 11.84977 ?  240 HIS   B N   1 
ATOM   3454 C  CA  . HIS   B 1 228 ? -2.54256  25.92008  28.47742  1.000 12.73362 ?  240 HIS   B CA  1 
ATOM   3455 C  C   . HIS   B 1 228 ? -2.46277  27.28388  27.82484  1.000 11.28101 ?  240 HIS   B C   1 
ATOM   3456 O  O   . HIS   B 1 228 ? -1.48868  28.01144  28.01789  1.000 12.93029 ?  240 HIS   B O   1 
ATOM   3457 C  CB  . HIS   B 1 228 ? -2.74329  26.08893  29.98641  1.000 12.08892 ?  240 HIS   B CB  1 
ATOM   3458 C  CG  . HIS   B 1 228 ? -2.68210  24.79725  30.72119  1.000 11.26957 ?  240 HIS   B CG  1 
ATOM   3459 N  ND1 . HIS   B 1 228 ? -3.76501  23.95801  30.83967  1.000 12.88741 ?  240 HIS   B ND1 1 
ATOM   3460 C  CD2 . HIS   B 1 228 ? -1.64774  24.16503  31.32490  1.000 15.07951 ?  240 HIS   B CD2 1 
ATOM   3461 C  CE1 . HIS   B 1 228 ? -3.41311  22.87206  31.49838  1.000 15.04683 ?  240 HIS   B CE1 1 
ATOM   3462 N  NE2 . HIS   B 1 228 ? -2.13280  22.97823  31.80680  1.000 12.63587 ?  240 HIS   B NE2 1 
ATOM   3463 N  N   . GLY   B 1 229 ? -3.45945  27.62664  27.02404  1.000 12.12722 ?  241 GLY   B N   1 
ATOM   3464 C  CA  . GLY   B 1 229 ? -3.55559  28.98407  26.53419  1.000 13.77474 ?  241 GLY   B CA  1 
ATOM   3465 C  C   . GLY   B 1 229 ? -3.01953  29.18104  25.13055  1.000 13.87777 ?  241 GLY   B C   1 
ATOM   3466 O  O   . GLY   B 1 229 ? -2.86167  28.24068  24.34767  1.000 14.40412 ?  241 GLY   B O   1 
ATOM   3467 N  N   . LEU   B 1 230 ? -2.70182  30.44726  24.82515  1.000 13.59142 ?  242 LEU   B N   1 
ATOM   3468 C  CA  . LEU   B 1 230 ? -2.49626  30.90810  23.44494  1.000 13.18023 ?  242 LEU   B CA  1 
ATOM   3469 C  C   . LEU   B 1 230 ? -1.12101  30.51875  22.91160  1.000 17.64388 ?  242 LEU   B C   1 
ATOM   3470 O  O   . LEU   B 1 230 ? -0.10994  30.72791  23.58712  1.000 13.53981 ?  242 LEU   B O   1 
ATOM   3471 C  CB  . LEU   B 1 230 ? -2.62796  32.42236  23.36613  1.000 15.99577 ?  242 LEU   B CB  1 
ATOM   3472 C  CG  . LEU   B 1 230 ? -3.99322  33.01248  23.69806  1.000 25.36855 ?  242 LEU   B CG  1 
ATOM   3473 C  CD1 . LEU   B 1 230 ? -3.95864  34.50112  23.38885  1.000 21.97129 ?  242 LEU   B CD1 1 
ATOM   3474 C  CD2 . LEU   B 1 230 ? -5.08706  32.30603  22.90884  1.000 22.58169 ?  242 LEU   B CD2 1 
ATOM   3475 N  N   . PRO   B 1 231 ? -1.04069  29.99821  21.69349  1.000 12.50421 ?  243 PRO   B N   1 
ATOM   3476 C  CA  . PRO   B 1 231 ? 0.26189   29.79068  21.06097  1.000 13.83900 ?  243 PRO   B CA  1 
ATOM   3477 C  C   . PRO   B 1 231 ? 0.99904   31.09786  20.81644  1.000 15.47681 ?  243 PRO   B C   1 
ATOM   3478 O  O   . PRO   B 1 231 ? 0.42253   32.18771  20.80896  1.000 15.44435 ?  243 PRO   B O   1 
ATOM   3479 C  CB  . PRO   B 1 231 ? -0.07756  29.11762  19.72710  1.000 19.89508 ?  243 PRO   B CB  1 
ATOM   3480 C  CG  . PRO   B 1 231 ? -1.55285  29.08894  19.60456  1.000 27.43820 ?  243 PRO   B CG  1 
ATOM   3481 C  CD  . PRO   B 1 231 ? -2.18171  29.53213  20.88521  1.000 15.25834 ?  243 PRO   B CD  1 
ATOM   3482 N  N   . GLY   B 1 232 ? 2.28802   30.97368  20.61151  1.000 14.28528 ?  244 GLY   B N   1 
ATOM   3483 C  CA  . GLY   B 1 232 ? 3.12067   32.10437  20.24927  1.000 15.72443 ?  244 GLY   B CA  1 
ATOM   3484 C  C   . GLY   B 1 232 ? 4.35465   31.60988  19.53718  1.000 16.07914 ?  244 GLY   B C   1 
ATOM   3485 O  O   . GLY   B 1 232 ? 4.32631   30.59340  18.83890  1.000 14.57788 ?  244 GLY   B O   1 
ATOM   3486 N  N   . GLY   B 1 233 ? 5.45309   32.34751  19.68796  1.000 14.64069 ?  245 GLY   B N   1 
ATOM   3487 C  CA  . GLY   B 1 233 ? 6.72754   31.95726  19.15616  1.000 16.05753 ?  245 GLY   B CA  1 
ATOM   3488 C  C   . GLY   B 1 233 ? 7.68198   31.52438  20.24930  1.000 13.95024 ?  245 GLY   B C   1 
ATOM   3489 O  O   . GLY   B 1 233 ? 7.27937   31.23494  21.38377  1.000 15.36413 ?  245 GLY   B O   1 
ATOM   3490 N  N   . LEU   B 1 234 ? 8.97077   31.47467  19.90081  1.000 13.63853 ?  246 LEU   B N   1 
ATOM   3491 C  CA  . LEU   B 1 234 ? 9.98318   31.12149  20.88603  1.000 11.61564 ?  246 LEU   B CA  1 
ATOM   3492 C  C   . LEU   B 1 234 ? 10.04291  32.09749  22.05427  1.000 13.73907 ?  246 LEU   B C   1 
ATOM   3493 O  O   . LEU   B 1 234 ? 10.64543  31.76089  23.07817  1.000 12.28964 ?  246 LEU   B O   1 
ATOM   3494 C  CB  . LEU   B 1 234 ? 11.35451  30.94510  20.22523  1.000 13.45533 ?  246 LEU   B CB  1 
ATOM   3495 C  CG  . LEU   B 1 234 ? 11.52475  29.59285  19.52243  1.000 13.93182 ?  246 LEU   B CG  1 
ATOM   3496 C  CD1 . LEU   B 1 234 ? 12.74110  29.64355  18.60027  1.000 15.14139 ?  246 LEU   B CD1 1 
ATOM   3497 C  CD2 . LEU   B 1 234 ? 11.65683  28.44607  20.51227  1.000 14.02696 ?  246 LEU   B CD2 1 
ATOM   3498 N  N   . ASP   B 1 235 ? 9.43569   33.28816  21.94685  1.000 14.32725 ?  247 ASP   B N   1 
ATOM   3499 C  CA  A ASP   B 1 235 ? 9.37335   34.22156  23.07364  0.393 16.28839 ?  247 ASP   B CA  1 
ATOM   3500 C  CA  B ASP   B 1 235 ? 9.45603   34.18136  23.09991  0.607 16.23010 ?  247 ASP   B CA  1 
ATOM   3501 C  C   . ASP   B 1 235 ? 8.73036   33.59856  24.30712  1.000 14.97086 ?  247 ASP   B C   1 
ATOM   3502 O  O   . ASP   B 1 235 ? 8.95985   34.06738  25.42790  1.000 13.74431 ?  247 ASP   B O   1 
ATOM   3503 C  CB  A ASP   B 1 235 ? 8.56690   35.47269  22.68936  0.393 17.15822 ?  247 ASP   B CB  1 
ATOM   3504 C  CB  B ASP   B 1 235 ? 8.93126   35.57841  22.75851  0.607 17.61214 ?  247 ASP   B CB  1 
ATOM   3505 C  CG  A ASP   B 1 235 ? 9.44033   36.61473  22.18942  0.393 20.10791 ?  247 ASP   B CG  1 
ATOM   3506 C  CG  B ASP   B 1 235 ? 7.62597   35.55184  22.00053  0.607 16.72606 ?  247 ASP   B CG  1 
ATOM   3507 O  OD1 A ASP   B 1 235 ? 10.66070  36.40399  22.03718  0.393 24.87579 ?  247 ASP   B OD1 1 
ATOM   3508 O  OD1 B ASP   B 1 235 ? 6.99315   34.48374  21.92086  0.607 19.98594 ?  247 ASP   B OD1 1 
ATOM   3509 O  OD2 A ASP   B 1 235 ? 8.90384   37.72811  21.96247  0.393 25.30204 ?  247 ASP   B OD2 1 
ATOM   3510 O  OD2 B ASP   B 1 235 ? 7.22766   36.61765  21.48210  0.607 22.88502 ?  247 ASP   B OD2 1 
ATOM   3511 N  N   . LEU   B 1 236 ? 7.90529   32.56178  24.12391  1.000 12.37414 ?  248 LEU   B N   1 
ATOM   3512 C  CA  . LEU   B 1 236 ? 7.26158   31.93155  25.26961  1.000 10.75933 ?  248 LEU   B CA  1 
ATOM   3513 C  C   . LEU   B 1 236 ? 8.27157   31.28391  26.20000  1.000 11.85830 ?  248 LEU   B C   1 
ATOM   3514 O  O   . LEU   B 1 236 ? 7.97721   31.11680  27.38519  1.000 11.16299 ?  248 LEU   B O   1 
ATOM   3515 C  CB  . LEU   B 1 236 ? 6.23879   30.90035  24.79317  1.000 12.98576 ?  248 LEU   B CB  1 
ATOM   3516 C  CG  . LEU   B 1 236 ? 4.81050   31.40960  24.57411  1.000 15.06900 ?  248 LEU   B CG  1 
ATOM   3517 C  CD1 . LEU   B 1 236 ? 4.71984   32.50585  23.51367  1.000 17.33358 ?  248 LEU   B CD1 1 
ATOM   3518 C  CD2 . LEU   B 1 236 ? 3.88582   30.25612  24.23134  1.000 12.72975 ?  248 LEU   B CD2 1 
ATOM   3519 N  N   . LEU   B 1 237 ? 9.44366   30.91140  25.68433  1.000 12.20661 ?  249 LEU   B N   1 
ATOM   3520 C  CA  . LEU   B 1 237 ? 10.44434  30.24510  26.50820  1.000 10.32941 ?  249 LEU   B CA  1 
ATOM   3521 C  C   . LEU   B 1 237 ? 11.02873  31.20005  27.53860  1.000 13.57462 ?  249 LEU   B C   1 
ATOM   3522 O  O   . LEU   B 1 237 ? 11.02818  30.90294  28.73780  1.000 11.91186 ?  249 LEU   B O   1 
ATOM   3523 C  CB  . LEU   B 1 237 ? 11.53953  29.66112  25.61766  1.000 10.86825 ?  249 LEU   B CB  1 
ATOM   3524 C  CG  . LEU   B 1 237 ? 11.30179  28.25046  25.04730  1.000 13.70192 ?  249 LEU   B CG  1 
ATOM   3525 C  CD1 . LEU   B 1 237 ? 10.09490  28.25698  24.12251  1.000 17.99908 ?  249 LEU   B CD1 1 
ATOM   3526 C  CD2 . LEU   B 1 237 ? 12.54006  27.71943  24.31035  1.000 15.10410 ?  249 LEU   B CD2 1 
ATOM   3527 N  N   . LYS   B 1 238 ? 11.52884  32.35699  27.09613  1.000 12.15703 ?  250 LYS   B N   1 
ATOM   3528 C  CA  . LYS   B 1 238 ? 12.10470  33.28082  28.06401  1.000 12.68633 ?  250 LYS   B CA  1 
ATOM   3529 C  C   . LYS   B 1 238 ? 11.02537  33.86690  28.96468  1.000 13.54467 ?  250 LYS   B C   1 
ATOM   3530 O  O   . LYS   B 1 238 ? 11.29684  34.15785  30.13411  1.000 12.16099 ?  250 LYS   B O   1 
ATOM   3531 C  CB  . LYS   B 1 238 ? 12.92674  34.36372  27.34198  1.000 19.66333 ?  250 LYS   B CB  1 
ATOM   3532 C  CG  . LYS   B 1 238 ? 13.41226  35.53544  28.20099  1.000 27.92160 ?  250 LYS   B CG  1 
ATOM   3533 C  CD  . LYS   B 1 238 ? 12.65994  36.84022  27.97571  1.000 33.47399 ?  250 LYS   B CD  1 
ATOM   3534 C  CE  . LYS   B 1 238 ? 12.75802  37.68656  29.23437  1.000 30.67113 ?  250 LYS   B CE  1 
ATOM   3535 N  NZ  . LYS   B 1 238 ? 12.43947  39.14251  29.14013  1.000 22.29579 ?  250 LYS   B NZ  1 
ATOM   3536 N  N   . HIS   B 1 239 ? 9.79255   34.02018  28.46186  1.000 10.47711 ?  251 HIS   B N   1 
ATOM   3537 C  CA  . HIS   B 1 239 ? 8.68350   34.42322  29.32741  1.000 10.76911 ?  251 HIS   B CA  1 
ATOM   3538 C  C   . HIS   B 1 239 ? 8.47961   33.41485  30.46172  1.000 10.97351 ?  251 HIS   B C   1 
ATOM   3539 O  O   . HIS   B 1 239 ? 8.34496   33.79210  31.63274  1.000 11.09869 ?  251 HIS   B O   1 
ATOM   3540 C  CB  . HIS   B 1 239 ? 7.38958   34.59751  28.52480  1.000 9.92843  ?  251 HIS   B CB  1 
ATOM   3541 C  CG  . HIS   B 1 239 ? 6.15843   34.52320  29.36701  1.000 10.48465 ?  251 HIS   B CG  1 
ATOM   3542 N  ND1 . HIS   B 1 239 ? 5.76019   35.56539  30.16929  1.000 9.88611  ?  251 HIS   B ND1 1 
ATOM   3543 C  CD2 . HIS   B 1 239 ? 5.25302   33.54075  29.56475  1.000 12.60726 ?  251 HIS   B CD2 1 
ATOM   3544 C  CE1 . HIS   B 1 239 ? 4.66237   35.24127  30.81976  1.000 10.63811 ?  251 HIS   B CE1 1 
ATOM   3545 N  NE2 . HIS   B 1 239 ? 4.32875   34.00931  30.46906  1.000 13.73367 ?  251 HIS   B NE2 1 
ATOM   3546 N  N   . THR   B 1 240 ? 8.47991   32.11763  30.13308  1.000 11.65584 ?  252 THR   B N   1 
ATOM   3547 C  CA  . THR   B 1 240 ? 8.33713   31.09948  31.16605  1.000 8.61338  ?  252 THR   B CA  1 
ATOM   3548 C  C   . THR   B 1 240 ? 9.48209   31.15936  32.16746  1.000 9.47396  ?  252 THR   B C   1 
ATOM   3549 O  O   . THR   B 1 240 ? 9.25404   31.08489  33.38009  1.000 8.97151  ?  252 THR   B O   1 
ATOM   3550 C  CB  . THR   B 1 240 ? 8.24260   29.71783  30.53090  1.000 10.54068 ?  252 THR   B CB  1 
ATOM   3551 O  OG1 . THR   B 1 240 ? 7.12166   29.69841  29.62856  1.000 10.78174 ?  252 THR   B OG1 1 
ATOM   3552 C  CG2 . THR   B 1 240 ? 8.05184   28.64508  31.60078  1.000 10.48022 ?  252 THR   B CG2 1 
ATOM   3553 N  N   . THR   B 1 241 ? 10.71477  31.32701  31.67618  1.000 9.66770  ?  253 THR   B N   1 
ATOM   3554 C  CA  . THR   B 1 241 ? 11.83987  31.46352  32.59910  1.000 10.61778 ?  253 THR   B CA  1 
ATOM   3555 C  C   . THR   B 1 241 ? 11.64285  32.64611  33.53910  1.000 11.47957 ?  253 THR   B C   1 
ATOM   3556 O  O   . THR   B 1 241 ? 11.87673  32.52919  34.74581  1.000 10.95597 ?  253 THR   B O   1 
ATOM   3557 C  CB  . THR   B 1 241 ? 13.14519  31.54839  31.81697  1.000 11.39998 ?  253 THR   B CB  1 
ATOM   3558 O  OG1 . THR   B 1 241 ? 13.38686  30.26526  31.21609  1.000 15.81866 ?  253 THR   B OG1 1 
ATOM   3559 C  CG2 . THR   B 1 241 ? 14.31043  31.88367  32.74506  1.000 16.64175 ?  253 THR   B CG2 1 
ATOM   3560 N  N   . ASN   B 1 242 ? 11.17986  33.78188  33.01081  1.000 12.54006 ?  254 ASN   B N   1 
ATOM   3561 C  CA  A ASN   B 1 242 ? 10.91836  34.95665  33.84488  0.581 11.73833 ?  254 ASN   B CA  1 
ATOM   3562 C  CA  B ASN   B 1 242 ? 10.96112  34.93500  33.87022  0.419 11.74436 ?  254 ASN   B CA  1 
ATOM   3563 C  C   . ASN   B 1 242 ? 9.93467   34.63133  34.95545  1.000 11.76355 ?  254 ASN   B C   1 
ATOM   3564 O  O   . ASN   B 1 242 ? 10.12349  35.01661  36.11529  1.000 12.37401 ?  254 ASN   B O   1 
ATOM   3565 C  CB  A ASN   B 1 242 ? 10.27978  36.05708  33.00247  0.581 13.93413 ?  254 ASN   B CB  1 
ATOM   3566 C  CB  B ASN   B 1 242 ? 10.54477  36.14401  33.03636  0.419 13.48023 ?  254 ASN   B CB  1 
ATOM   3567 C  CG  A ASN   B 1 242 ? 11.26082  36.81281  32.17595  0.581 14.08279 ?  254 ASN   B CG  1 
ATOM   3568 C  CG  B ASN   B 1 242 ? 10.77562  37.45361  33.75744  0.419 17.04319 ?  254 ASN   B CG  1 
ATOM   3569 O  OD1 A ASN   B 1 242 ? 12.47765  36.62408  32.27868  0.581 16.07432 ?  254 ASN   B OD1 1 
ATOM   3570 O  OD1 B ASN   B 1 242 ? 11.70248  37.57946  34.55304  0.419 20.83219 ?  254 ASN   B OD1 1 
ATOM   3571 N  ND2 A ASN   B 1 242 ? 10.72992  37.69309  31.32863  0.581 15.95103 ?  254 ASN   B ND2 1 
ATOM   3572 N  ND2 B ASN   B 1 242 ? 9.93122   38.43868  33.48060  0.419 18.43892 ?  254 ASN   B ND2 1 
ATOM   3573 N  N   . VAL   B 1 243 ? 8.85303   33.94568  34.60310  1.000 11.25319 ?  255 VAL   B N   1 
ATOM   3574 C  CA  . VAL   B 1 243 ? 7.80989   33.63542  35.57435  1.000 10.29237 ?  255 VAL   B CA  1 
ATOM   3575 C  C   . VAL   B 1 243 ? 8.32718   32.65947  36.62203  1.000 11.49314 ?  255 VAL   B C   1 
ATOM   3576 O  O   . VAL   B 1 243 ? 8.07495   32.81355  37.82993  1.000 11.47682 ?  255 VAL   B O   1 
ATOM   3577 C  CB  . VAL   B 1 243 ? 6.56547   33.09339  34.84977  1.000 10.90260 ?  255 VAL   B CB  1 
ATOM   3578 C  CG1 . VAL   B 1 243 ? 5.54167   32.62240  35.85703  1.000 12.34519 ?  255 VAL   B CG1 1 
ATOM   3579 C  CG2 . VAL   B 1 243 ? 5.97082   34.18573  33.96819  1.000 11.75303 ?  255 VAL   B CG2 1 
ATOM   3580 N  N   . VAL   B 1 244 ? 9.04152   31.63010  36.17398  1.000 11.33028 ?  256 VAL   B N   1 
ATOM   3581 C  CA  . VAL   B 1 244 ? 9.58941   30.63668  37.09087  1.000 10.09092 ?  256 VAL   B CA  1 
ATOM   3582 C  C   . VAL   B 1 244 ? 10.58557  31.28124  38.04981  1.000 9.78886  ?  256 VAL   B C   1 
ATOM   3583 O  O   . VAL   B 1 244 ? 10.56380  31.00644  39.25624  1.000 11.61033 ?  256 VAL   B O   1 
ATOM   3584 C  CB  . VAL   B 1 244 ? 10.21637  29.49694  36.27438  1.000 12.72949 ?  256 VAL   B CB  1 
ATOM   3585 C  CG1 . VAL   B 1 244 ? 11.13702  28.64764  37.14179  1.000 12.86441 ?  256 VAL   B CG1 1 
ATOM   3586 C  CG2 . VAL   B 1 244 ? 9.11372   28.67381  35.64876  1.000 13.68366 ?  256 VAL   B CG2 1 
ATOM   3587 N  N   . LYS   B 1 245 ? 11.46936  32.13846  37.53287  1.000 9.64182  ?  257 LYS   B N   1 
ATOM   3588 C  CA  . LYS   B 1 245 ? 12.44035  32.80157  38.40573  1.000 10.25707 ?  257 LYS   B CA  1 
ATOM   3589 C  C   . LYS   B 1 245 ? 11.75790  33.72824  39.40725  1.000 11.41364 ?  257 LYS   B C   1 
ATOM   3590 O  O   . LYS   B 1 245 ? 12.17170  33.79195  40.57189  1.000 12.48919 ?  257 LYS   B O   1 
ATOM   3591 C  CB  . LYS   B 1 245 ? 13.49539  33.52528  37.56505  1.000 12.76904 ?  257 LYS   B CB  1 
ATOM   3592 C  CG  . LYS   B 1 245 ? 14.45483  32.56927  36.86113  1.000 12.39939 ?  257 LYS   B CG  1 
ATOM   3593 C  CD  . LYS   B 1 245 ? 15.57127  33.32125  36.12916  1.000 16.13863 ?  257 LYS   B CD  1 
ATOM   3594 C  CE  . LYS   B 1 245 ? 16.57334  32.37490  35.45852  1.000 20.91857 ?  257 LYS   B CE  1 
ATOM   3595 N  NZ  . LYS   B 1 245 ? 17.90947  33.03449  35.24266  1.000 21.48382 ?  257 LYS   B NZ  1 
ATOM   3596 N  N   . ALA   B 1 246 ? 10.71291  34.44423  38.98364  1.000 12.01567 ?  258 ALA   B N   1 
ATOM   3597 C  CA  . ALA   B 1 246 ? 9.96328   35.27869  39.92103  1.000 11.93756 ?  258 ALA   B CA  1 
ATOM   3598 C  C   . ALA   B 1 246 ? 9.36619   34.43332  41.03754  1.000 15.40344 ?  258 ALA   B C   1 
ATOM   3599 O  O   . ALA   B 1 246 ? 9.42147   34.81243  42.21750  1.000 15.35999 ?  258 ALA   B O   1 
ATOM   3600 C  CB  . ALA   B 1 246 ? 8.87467   36.05351  39.18082  1.000 14.84756 ?  258 ALA   B CB  1 
ATOM   3601 N  N   . HIS   B 1 247 ? 8.82548   33.26643  40.69447  1.000 12.70890 ?  259 HIS   B N   1 
ATOM   3602 C  CA  . HIS   B 1 247 ? 8.28073   32.39772  41.72898  1.000 15.01896 ?  259 HIS   B CA  1 
ATOM   3603 C  C   . HIS   B 1 247 ? 9.38470   31.87462  42.64041  1.000 14.00346 ?  259 HIS   B C   1 
ATOM   3604 O  O   . HIS   B 1 247 ? 9.21153   31.80526  43.86458  1.000 16.70393 ?  259 HIS   B O   1 
ATOM   3605 C  CB  . HIS   B 1 247 ? 7.52633   31.23892  41.08937  1.000 14.39943 ?  259 HIS   B CB  1 
ATOM   3606 C  CG  . HIS   B 1 247 ? 6.80627   30.38900  42.08482  1.000 14.82564 ?  259 HIS   B CG  1 
ATOM   3607 N  ND1 . HIS   B 1 247 ? 5.58440   30.74196  42.61529  1.000 22.35262 ?  259 HIS   B ND1 1 
ATOM   3608 C  CD2 . HIS   B 1 247 ? 7.15665   29.22509  42.68110  1.000 19.91951 ?  259 HIS   B CD2 1 
ATOM   3609 C  CE1 . HIS   B 1 247 ? 5.20105   29.81617  43.47619  1.000 20.25213 ?  259 HIS   B CE1 1 
ATOM   3610 N  NE2 . HIS   B 1 247 ? 6.13920   28.88934  43.54052  1.000 21.49852 ?  259 HIS   B NE2 1 
ATOM   3611 N  N   . THR   B 1 248 ? 10.52387  31.50013  42.05778  1.000 13.57567 ?  260 THR   B N   1 
ATOM   3612 C  CA  . THR   B 1 248 ? 11.67555  31.06305  42.84481  1.000 13.79444 ?  260 THR   B CA  1 
ATOM   3613 C  C   . THR   B 1 248 ? 12.08569  32.11830  43.85593  1.000 17.81827 ?  260 THR   B C   1 
ATOM   3614 O  O   . THR   B 1 248 ? 12.48277  31.78323  44.98001  1.000 19.10305 ?  260 THR   B O   1 
ATOM   3615 C  CB  . THR   B 1 248 ? 12.83458  30.76996  41.89423  1.000 11.55170 ?  260 THR   B CB  1 
ATOM   3616 O  OG1 . THR   B 1 248 ? 12.50971  29.62330  41.09302  1.000 16.10757 ?  260 THR   B OG1 1 
ATOM   3617 C  CG2 . THR   B 1 248 ? 14.11779  30.48228  42.67758  1.000 14.87870 ?  260 THR   B CG2 1 
ATOM   3618 N  N   . ASN   B 1 249 ? 11.97601  33.39579  43.48599  1.000 13.53289 ?  261 ASN   B N   1 
ATOM   3619 C  CA  . ASN   B 1 249 ? 12.41739  34.50756  44.32038  1.000 16.26746 ?  261 ASN   B CA  1 
ATOM   3620 C  C   . ASN   B 1 249 ? 11.31759  35.04725  45.22004  1.000 20.89960 ?  261 ASN   B C   1 
ATOM   3621 O  O   . ASN   B 1 249 ? 11.47899  36.13484  45.78660  1.000 24.56020 ?  261 ASN   B O   1 
ATOM   3622 C  CB  . ASN   B 1 249 ? 12.99393  35.62956  43.45356  1.000 14.11026 ?  261 ASN   B CB  1 
ATOM   3623 C  CG  . ASN   B 1 249 ? 14.34335  35.28095  42.88768  1.000 16.87355 ?  261 ASN   B CG  1 
ATOM   3624 O  OD1 . ASN   B 1 249 ? 14.99749  34.34495  43.35821  1.000 17.79505 ?  261 ASN   B OD1 1 
ATOM   3625 N  ND2 . ASN   B 1 249 ? 14.77388  36.02313  41.87449  1.000 15.90577 ?  261 ASN   B ND2 1 
ATOM   3626 N  N   . ARG   B 1 250 ? 10.21432  34.32044  45.36106  1.000 17.09148 ?  262 ARG   B N   1 
ATOM   3627 C  CA  . ARG   B 1 250 ? 9.08091   34.77388  46.17886  1.000 22.99060 ?  262 ARG   B CA  1 
ATOM   3628 C  C   . ARG   B 1 250 ? 9.49316   35.05349  47.62429  1.000 29.20053 ?  262 ARG   B C   1 
ATOM   3629 O  O   . ARG   B 1 250 ? 10.45217  34.46742  48.12575  1.000 23.64572 ?  262 ARG   B O   1 
ATOM   3630 C  CB  . ARG   B 1 250 ? 7.94895   33.74396  46.13766  1.000 24.09028 ?  262 ARG   B CB  1 
ATOM   3631 C  CG  . ARG   B 1 250 ? 8.28564   32.39518  46.78325  1.000 25.26353 ?  262 ARG   B CG  1 
ATOM   3632 C  CD  . ARG   B 1 250 ? 7.25466   31.31563  46.41830  1.000 23.66439 ?  262 ARG   B CD  1 
ATOM   3633 N  NE  . ARG   B 1 250 ? 7.50444   30.05496  47.11145  1.000 26.69433 ?  262 ARG   B NE  1 
ATOM   3634 C  CZ  . ARG   B 1 250 ? 8.40112   29.15445  46.72833  1.000 28.76824 ?  262 ARG   B CZ  1 
ATOM   3635 N  NH1 . ARG   B 1 250 ? 9.13871   29.33449  45.64478  1.000 22.74581 ?  262 ARG   B NH1 1 
ATOM   3636 N  NH2 . ARG   B 1 250 ? 8.55877   28.04307  47.44735  1.000 24.79608 ?  262 ARG   B NH2 1 
HETATM 3637 C  C   . FMT   C 2 .   ? 32.48887  19.98514  0.56371   1.000 5.67836  ?  301 FMT   A C   1 
HETATM 3638 O  O1  . FMT   C 2 .   ? 32.00514  20.25792  1.63911   1.000 23.78410 ?  301 FMT   A O1  1 
HETATM 3639 O  O2  . FMT   C 2 .   ? 32.52914  20.70399  -0.40973  1.000 27.50529 ?  301 FMT   A O2  1 
HETATM 3640 C  C   . FMT   D 2 .   ? 28.86578  19.73022  3.02435   1.000 8.51530  ?  302 FMT   A C   1 
HETATM 3641 O  O1  . FMT   D 2 .   ? 29.99222  19.65625  3.12890   1.000 6.99493  ?  302 FMT   A O1  1 
HETATM 3642 O  O2  . FMT   D 2 .   ? 28.41447  20.22502  1.99092   1.000 38.89053 ?  302 FMT   A O2  1 
HETATM 3643 C  C13 . A1H8U E 3 .   ? 11.92507  0.63782   7.17673   0.803 35.01500 ?  303 A1H8U A C13 1 
HETATM 3644 C  C10 . A1H8U E 3 .   ? 12.97435  0.93242   8.28618   0.803 37.42767 ?  303 A1H8U A C10 1 
HETATM 3645 C  C11 . A1H8U E 3 .   ? 12.50302  0.27792   9.52826   0.803 46.20932 ?  303 A1H8U A C11 1 
HETATM 3646 C  C1  . A1H8U E 3 .   ? 15.43183  0.78030   7.85628   0.803 19.74839 ?  303 A1H8U A C1  1 
HETATM 3647 C  C12 . A1H8U E 3 .   ? 10.83980  -0.14850  7.63316   0.803 40.14046 ?  303 A1H8U A C12 1 
HETATM 3648 C  C2  . A1H8U E 3 .   ? 16.29507  -1.56479  7.46468   0.803 19.28873 ?  303 A1H8U A C2  1 
HETATM 3649 C  C3  . A1H8U E 3 .   ? 16.06957  -2.88424  8.21005   0.803 22.25369 ?  303 A1H8U A C3  1 
HETATM 3650 C  C4  . A1H8U E 3 .   ? 17.14816  -3.59172  8.72881   0.803 27.38701 ?  303 A1H8U A C4  1 
HETATM 3651 C  C5  . A1H8U E 3 .   ? 16.90448  -4.63692  9.62327   0.803 30.73684 ?  303 A1H8U A C5  1 
HETATM 3652 C  C6  . A1H8U E 3 .   ? 15.61827  -5.16923  9.73217   0.803 32.88869 ?  303 A1H8U A C6  1 
HETATM 3653 C  C7  . A1H8U E 3 .   ? 14.53563  -4.45275  9.22291   0.803 33.32378 ?  303 A1H8U A C7  1 
HETATM 3654 C  C8  . A1H8U E 3 .   ? 14.78188  -3.40294  8.33864   0.803 23.04470 ?  303 A1H8U A C8  1 
HETATM 3655 C  C9  . A1H8U E 3 .   ? 14.26413  1.75101   8.11991   0.803 24.91153 ?  303 A1H8U A C9  1 
HETATM 3656 N  N1  . A1H8U E 3 .   ? 15.18580  -0.66066  7.72267   0.803 23.52355 ?  303 A1H8U A N1  1 
HETATM 3657 O  O1  . A1H8U E 3 .   ? 16.53666  1.19930   7.75799   0.803 23.17426 ?  303 A1H8U A O1  1 
HETATM 3658 O  O2  . A1H8U E 3 .   ? 13.73889  -2.87309  7.56632   0.803 25.67080 ?  303 A1H8U A O2  1 
HETATM 3659 O  O3  . A1H8U E 3 .   ? 16.77922  -0.73629  4.83217   0.803 13.78897 -1 303 A1H8U A O3  1 
HETATM 3660 O  O4  . A1H8U E 3 .   ? 14.95213  -2.47013  4.99060   0.803 16.11933 -1 303 A1H8U A O4  1 
HETATM 3661 O  O5  . A1H8U E 3 .   ? 17.56536  -2.77700  5.03811   0.803 22.35113 ?  303 A1H8U A O5  1 
HETATM 3662 P  P1  . A1H8U E 3 .   ? 16.33111  -1.88119  5.63877   0.803 15.86578 ?  303 A1H8U A P1  1 
HETATM 3663 S  S1  . A1H8U E 3 .   ? 11.10518  -0.44967  9.15915   0.803 52.51981 ?  303 A1H8U A S1  1 
HETATM 3664 ZN ZN  . ZN    F 4 .   ? 16.45278  -0.14870  3.10184   0.955 11.24137 ?  304 ZN    A ZN  1 
HETATM 3665 ZN ZN  . ZN    G 4 .   ? 30.21903  20.39071  1.01528   0.959 11.97840 ?  305 ZN    A ZN  1 
HETATM 3666 ZN ZN  . ZN    H 4 .   ? 19.37743  -2.39781  5.43375   0.779 13.47443 ?  306 ZN    A ZN  1 
HETATM 3667 C  C13 A A1H8U I 3 .   ? -1.34915  18.21590  39.48121  0.855 29.55708 ?  301 A1H8U B C13 1 
HETATM 3668 C  C10 A A1H8U I 3 .   ? -2.87891  18.01319  39.25909  0.855 27.34913 ?  301 A1H8U B C10 1 
HETATM 3669 C  C11 A A1H8U I 3 .   ? -3.56343  18.53425  40.46891  0.855 33.95588 ?  301 A1H8U B C11 1 
HETATM 3670 C  C1  A A1H8U I 3 .   ? -3.36039  18.27822  36.78055  0.855 18.26372 ?  301 A1H8U B C1  1 
HETATM 3671 C  C12 A A1H8U I 3 .   ? -1.03630  18.81677  40.72803  0.855 31.66427 ?  301 A1H8U B C12 1 
HETATM 3672 C  C2  A A1H8U I 3 .   ? -2.85359  20.56389  35.80224  0.855 16.94458 ?  301 A1H8U B C2  1 
HETATM 3673 C  C3  A A1H8U I 3 .   ? -3.45627  21.93978  36.07386  0.855 17.34495 ?  301 A1H8U B C3  1 
HETATM 3674 C  C4  A A1H8U I 3 .   ? -4.14169  22.58195  35.04955  0.855 22.63753 ?  301 A1H8U B C4  1 
HETATM 3675 C  C5  A A1H8U I 3 .   ? -4.91334  23.70998  35.33911  0.855 25.69886 ?  301 A1H8U B C5  1 
HETATM 3676 C  C6  A A1H8U I 3 .   ? -4.88880  24.25043  36.62521  0.855 27.22889 ?  301 A1H8U B C6  1 
HETATM 3677 C  C7  A A1H8U I 3 .   ? -4.25236  23.55783  37.65434  0.855 27.32270 ?  301 A1H8U B C7  1 
HETATM 3678 C  C8  A A1H8U I 3 .   ? -3.40605  22.49379  37.34125  0.855 19.67191 ?  301 A1H8U B C8  1 
HETATM 3679 C  C9  A A1H8U I 3 .   ? -3.56358  17.38783  38.02251  0.855 27.49217 ?  301 A1H8U B C9  1 
HETATM 3680 N  N1  A A1H8U I 3 .   ? -3.05264  19.69872  36.95502  0.855 22.46399 ?  301 A1H8U B N1  1 
HETATM 3681 O  O1  A A1H8U I 3 .   ? -3.45003  17.82816  35.67594  0.855 22.07220 ?  301 A1H8U B O1  1 
HETATM 3682 O  O2  A A1H8U I 3 .   ? -2.45518  22.04293  38.27723  0.855 22.00208 ?  301 A1H8U B O2  1 
HETATM 3683 O  O3  A A1H8U I 3 .   ? -0.24725  21.18580  36.65803  0.855 17.37095 -1 301 A1H8U B O3  1 
HETATM 3684 O  O4  A A1H8U I 3 .   ? -0.61516  21.83733  34.32314  0.855 17.92883 -1 301 A1H8U B O4  1 
HETATM 3685 O  O5  A A1H8U I 3 .   ? -0.32755  19.35908  35.18083  0.855 16.54133 ?  301 A1H8U B O5  1 
HETATM 3686 P  P1  A A1H8U I 3 .   ? -1.04179  20.77883  35.49465  0.855 15.09870 ?  301 A1H8U B P1  1 
HETATM 3687 S  S1  A A1H8U I 3 .   ? -2.40850  19.07377  41.46617  0.855 40.14976 ?  301 A1H8U B S1  1 
HETATM 3688 C  C   . FMT   J 2 .   ? 5.93846   38.04145  32.49694  1.000 2.26893  ?  302 FMT   B C   1 
HETATM 3689 O  O1  . FMT   J 2 .   ? 7.05018   38.20721  32.11980  1.000 18.48461 ?  302 FMT   B O1  1 
HETATM 3690 O  O2  . FMT   J 2 .   ? 4.94179   38.20683  31.81196  1.000 37.05846 ?  302 FMT   B O2  1 
HETATM 3691 C  C   . FMT   K 2 .   ? 9.12234   37.90707  30.05383  1.000 3.91237  ?  303 FMT   B C   1 
HETATM 3692 O  O1  . FMT   K 2 .   ? 9.59019   38.28470  31.12525  1.000 37.85808 ?  303 FMT   B O1  1 
HETATM 3693 O  O2  . FMT   K 2 .   ? 7.94784   37.99763  29.70288  1.000 17.85267 ?  303 FMT   B O2  1 
HETATM 3694 ZN ZN  . ZN    L 4 .   ? 1.30158   18.77698  35.21939  0.977 11.99843 ?  304 ZN    B ZN  1 
HETATM 3695 ZN ZN  . ZN    M 4 .   ? 6.52629   37.55646  30.25014  0.954 14.35668 ?  305 ZN    B ZN  1 
HETATM 3696 ZN ZN  . ZN    N 4 .   ? -1.06003  21.19086  32.46614  0.807 13.41655 ?  306 ZN    B ZN  1 
HETATM 3697 O  O   . HOH   O 5 .   ? 15.03570  11.51141  -8.32257  1.000 50.31792 ?  401 HOH   A O   1 
HETATM 3698 O  O   . HOH   O 5 .   ? 31.37037  -17.04710 -4.28237  1.000 30.53474 ?  402 HOH   A O   1 
HETATM 3699 O  O   . HOH   O 5 .   ? 30.380    -21.290   -3.483    1.000 23.48698 ?  403 HOH   A O   1 
HETATM 3700 O  O   . HOH   O 5 .   ? 17.09909  -17.72813 -8.85883  1.000 22.92625 ?  404 HOH   A O   1 
HETATM 3701 O  O   . HOH   O 5 .   ? 38.269    13.813    18.559    1.000 27.02968 ?  405 HOH   A O   1 
HETATM 3702 O  O   . HOH   O 5 .   ? 19.70111  -17.60938 -8.30264  1.000 24.18427 ?  406 HOH   A O   1 
HETATM 3703 O  O   . HOH   O 5 .   ? 42.40816  4.56120   -7.83585  1.000 47.13428 ?  407 HOH   A O   1 
HETATM 3704 O  O   . HOH   O 5 .   ? 22.09347  10.55152  -14.12761 1.000 28.79226 ?  408 HOH   A O   1 
HETATM 3705 O  O   . HOH   O 5 .   ? 13.12093  -2.10897  3.52017   1.000 34.30592 ?  409 HOH   A O   1 
HETATM 3706 O  O   . HOH   O 5 .   ? 25.38835  -15.04302 -13.70348 1.000 39.26710 ?  410 HOH   A O   1 
HETATM 3707 O  O   . HOH   O 5 .   ? 3.30896   -13.92927 -5.23901  1.000 31.75334 ?  411 HOH   A O   1 
HETATM 3708 O  O   . HOH   O 5 .   ? 29.187    -19.844   -0.965    1.000 21.61223 ?  412 HOH   A O   1 
HETATM 3709 O  O   . HOH   O 5 .   ? 16.74520  6.78271   -14.87798 1.000 43.52440 ?  413 HOH   A O   1 
HETATM 3710 O  O   . HOH   O 5 .   ? 14.90493  6.08977   -7.28754  1.000 22.24941 ?  414 HOH   A O   1 
HETATM 3711 O  O   . HOH   O 5 .   ? 33.32457  17.25948  -0.17938  1.000 21.34166 ?  415 HOH   A O   1 
HETATM 3712 O  O   . HOH   O 5 .   ? 17.16254  -5.21972  4.84804   1.000 24.11655 ?  416 HOH   A O   1 
HETATM 3713 O  O   . HOH   O 5 .   ? 38.56186  10.51304  -0.68522  1.000 31.35252 ?  417 HOH   A O   1 
HETATM 3714 O  O   . HOH   O 5 .   ? 38.94722  9.65616   12.51540  1.000 19.61412 ?  418 HOH   A O   1 
HETATM 3715 O  O   . HOH   O 5 .   ? 19.06675  8.49659   15.79021  1.000 32.38510 ?  419 HOH   A O   1 
HETATM 3716 O  O   . HOH   O 5 .   ? 16.43011  -0.75956  -14.57022 1.000 32.86927 ?  420 HOH   A O   1 
HETATM 3717 O  O   . HOH   O 5 .   ? 27.51646  -17.85719 -7.88021  1.000 37.24869 ?  421 HOH   A O   1 
HETATM 3718 O  O   . HOH   O 5 .   ? 26.24418  -15.33092 -7.72469  1.000 18.30832 ?  422 HOH   A O   1 
HETATM 3719 O  O   . HOH   O 5 .   ? 27.41538  4.26652   22.09825  1.000 30.98114 ?  423 HOH   A O   1 
HETATM 3720 O  O   . HOH   O 5 .   ? 17.94196  6.65748   13.08678  1.000 33.74722 ?  424 HOH   A O   1 
HETATM 3721 O  O   . HOH   O 5 .   ? 40.78318  14.18794  16.63462  1.000 36.17643 ?  425 HOH   A O   1 
HETATM 3722 O  O   . HOH   O 5 .   ? 43.790    7.826     17.319    1.000 19.39930 ?  426 HOH   A O   1 
HETATM 3723 O  O   . HOH   O 5 .   ? 24.40309  0.60250   9.21046   1.000 22.46381 ?  427 HOH   A O   1 
HETATM 3724 O  O   . HOH   O 5 .   ? 45.74564  3.29751   7.82453   1.000 46.93943 ?  428 HOH   A O   1 
HETATM 3725 O  O   . HOH   O 5 .   ? 40.236    -8.759    -8.768    1.000 38.23497 ?  429 HOH   A O   1 
HETATM 3726 O  O   . HOH   O 5 .   ? 15.40492  -22.38840 -4.84651  1.000 35.02870 ?  430 HOH   A O   1 
HETATM 3727 O  O   . HOH   O 5 .   ? 31.54202  -8.77501  -17.35964 1.000 26.44404 ?  431 HOH   A O   1 
HETATM 3728 O  O   . HOH   O 5 .   ? 43.69972  -2.33892  -1.03339  1.000 22.84924 ?  432 HOH   A O   1 
HETATM 3729 O  O   . HOH   O 5 .   ? 11.64296  -0.99964  4.64738   1.000 43.60585 ?  433 HOH   A O   1 
HETATM 3730 O  O   . HOH   O 5 .   ? 44.30396  11.29952  14.27079  1.000 29.72207 ?  434 HOH   A O   1 
HETATM 3731 O  O   . HOH   O 5 .   ? 30.33411  -16.86365 0.45563   1.000 22.29223 ?  435 HOH   A O   1 
HETATM 3732 O  O   . HOH   O 5 .   ? 20.20465  6.51442   -6.51267  1.000 13.65716 ?  436 HOH   A O   1 
HETATM 3733 O  O   . HOH   O 5 .   ? 7.95204   -4.64408  -5.12958  1.000 24.30265 ?  437 HOH   A O   1 
HETATM 3734 O  O   . HOH   O 5 .   ? 6.03363   12.63260  3.08230   1.000 36.31326 ?  438 HOH   A O   1 
HETATM 3735 O  O   . HOH   O 5 .   ? 32.64577  1.52074   -14.80093 1.000 24.38889 ?  439 HOH   A O   1 
HETATM 3736 O  O   . HOH   O 5 .   ? 40.25583  11.83521  -3.87922  1.000 39.74970 ?  440 HOH   A O   1 
HETATM 3737 O  O   . HOH   O 5 .   ? 20.971    -20.175   -7.614    1.000 18.88821 ?  441 HOH   A O   1 
HETATM 3738 O  O   . HOH   O 5 .   ? 23.53433  7.05507   -18.61600 1.000 40.36033 ?  442 HOH   A O   1 
HETATM 3739 O  O   . HOH   O 5 .   ? 14.33390  -8.87185  -12.93676 1.000 13.65885 ?  443 HOH   A O   1 
HETATM 3740 O  O   . HOH   O 5 .   ? 34.86543  -3.94118  -12.61638 1.000 18.21242 ?  444 HOH   A O   1 
HETATM 3741 O  O   . HOH   O 5 .   ? 15.523    -19.889   -7.910    1.000 22.42739 ?  445 HOH   A O   1 
HETATM 3742 O  O   . HOH   O 5 .   ? 15.34544  2.81726   11.92981  1.000 40.22399 ?  446 HOH   A O   1 
HETATM 3743 O  O   . HOH   O 5 .   ? 45.28098  13.03531  7.43366   1.000 33.42704 ?  447 HOH   A O   1 
HETATM 3744 O  O   . HOH   O 5 .   ? 14.10474  -18.86240 0.00822   1.000 40.90355 ?  448 HOH   A O   1 
HETATM 3745 O  O   . HOH   O 5 .   ? 35.32047  -13.13314 -9.01349  1.000 22.39982 ?  449 HOH   A O   1 
HETATM 3746 O  O   . HOH   O 5 .   ? 24.02851  18.30937  11.92979  1.000 36.00710 ?  450 HOH   A O   1 
HETATM 3747 O  O   . HOH   O 5 .   ? 27.48606  7.04239   20.84693  1.000 24.44906 ?  451 HOH   A O   1 
HETATM 3748 O  O   . HOH   O 5 .   ? 25.46470  -0.89796  17.84847  1.000 23.65790 ?  452 HOH   A O   1 
HETATM 3749 O  O   . HOH   O 5 .   ? 29.57662  -9.91657  24.00261  1.000 40.11282 ?  453 HOH   A O   1 
HETATM 3750 O  O   . HOH   O 5 .   ? 27.72441  8.05874   -15.14154 1.000 24.31636 ?  454 HOH   A O   1 
HETATM 3751 O  O   . HOH   O 5 .   ? 19.03097  15.00788  13.84213  1.000 33.21150 ?  455 HOH   A O   1 
HETATM 3752 O  O   . HOH   O 5 .   ? 12.29911  2.48631   -3.16067  1.000 14.19677 ?  456 HOH   A O   1 
HETATM 3753 O  O   . HOH   O 5 .   ? 18.61241  8.56970   12.82618  1.000 34.79799 ?  457 HOH   A O   1 
HETATM 3754 O  O   . HOH   O 5 .   ? 33.39767  15.52730  -3.75089  1.000 23.20617 ?  458 HOH   A O   1 
HETATM 3755 O  O   . HOH   O 5 .   ? 39.710    -11.185   -9.198    1.000 41.33353 ?  459 HOH   A O   1 
HETATM 3756 O  O   . HOH   O 5 .   ? 22.53571  -1.09670  -2.14843  1.000 9.92806  ?  460 HOH   A O   1 
HETATM 3757 O  O   . HOH   O 5 .   ? 15.23018  -6.14422  1.97263   1.000 15.84126 ?  461 HOH   A O   1 
HETATM 3758 O  O   . HOH   O 5 .   ? 34.65795  -1.07978  -12.63059 1.000 23.80827 ?  462 HOH   A O   1 
HETATM 3759 O  O   . HOH   O 5 .   ? 23.61709  3.36345   -17.99469 1.000 24.45546 ?  463 HOH   A O   1 
HETATM 3760 O  O   . HOH   O 5 .   ? 14.38849  12.56516  10.89885  1.000 28.94535 ?  464 HOH   A O   1 
HETATM 3761 O  O   . HOH   O 5 .   ? 29.49874  -15.32493 -10.06297 1.000 29.51924 ?  465 HOH   A O   1 
HETATM 3762 O  O   . HOH   O 5 .   ? 32.56421  -17.61194 -2.28859  1.000 33.89058 ?  466 HOH   A O   1 
HETATM 3763 O  O   . HOH   O 5 .   ? 41.22202  12.34591  12.26480  1.000 31.70728 ?  467 HOH   A O   1 
HETATM 3764 O  O   . HOH   O 5 .   ? 25.98232  -13.82341 -9.98779  1.000 21.78690 ?  468 HOH   A O   1 
HETATM 3765 O  O   . HOH   O 5 .   ? 21.61206  -9.61823  4.63043   1.000 14.72360 ?  469 HOH   A O   1 
HETATM 3766 O  O   . HOH   O 5 .   ? 39.36970  -4.84915  -9.05799  1.000 21.48242 ?  470 HOH   A O   1 
HETATM 3767 O  O   . HOH   O 5 .   ? 43.938    4.706     19.804    1.000 26.83279 ?  471 HOH   A O   1 
HETATM 3768 O  O   . HOH   O 5 .   ? 15.08479  -11.81955 6.00087   1.000 21.73965 ?  472 HOH   A O   1 
HETATM 3769 O  O   . HOH   O 5 .   ? 21.66698  -7.24295  3.32776   1.000 12.89503 ?  473 HOH   A O   1 
HETATM 3770 O  O   . HOH   O 5 .   ? 37.78813  -9.67912  13.73172  1.000 37.93469 ?  474 HOH   A O   1 
HETATM 3771 O  O   . HOH   O 5 .   ? 13.81620  -19.08106 -5.96947  1.000 20.95852 ?  475 HOH   A O   1 
HETATM 3772 O  O   . HOH   O 5 .   ? 22.32698  11.96865  13.11346  1.000 16.43850 ?  476 HOH   A O   1 
HETATM 3773 O  O   . HOH   O 5 .   ? 22.05165  0.01992   0.32800   1.000 10.29839 ?  477 HOH   A O   1 
HETATM 3774 O  O   . HOH   O 5 .   ? 22.58622  18.62949  -3.13290  1.000 15.14594 ?  478 HOH   A O   1 
HETATM 3775 O  O   . HOH   O 5 .   ? 25.80781  20.90817  4.82079   1.000 18.87511 ?  479 HOH   A O   1 
HETATM 3776 O  O   . HOH   O 5 .   ? 13.95178  -6.75868  -16.12998 1.000 27.81147 ?  480 HOH   A O   1 
HETATM 3777 O  O   . HOH   O 5 .   ? 27.53651  17.04155  5.31523   1.000 12.12634 ?  481 HOH   A O   1 
HETATM 3778 O  O   . HOH   O 5 .   ? 29.24972  12.02538  -9.76797  1.000 28.30192 ?  482 HOH   A O   1 
HETATM 3779 O  O   . HOH   O 5 .   ? 22.44456  7.52625   -2.96331  1.000 8.96230  ?  483 HOH   A O   1 
HETATM 3780 O  O   . HOH   O 5 .   ? 11.69299  15.86833  5.34021   1.000 23.03731 ?  484 HOH   A O   1 
HETATM 3781 O  O   . HOH   O 5 .   ? 43.11203  10.53039  18.11773  1.000 20.35411 ?  485 HOH   A O   1 
HETATM 3782 O  O   . HOH   O 5 .   ? 17.39558  16.82977  10.25867  1.000 39.86016 ?  486 HOH   A O   1 
HETATM 3783 O  O   . HOH   O 5 .   ? 37.28973  2.76340   -11.12651 1.000 39.74292 ?  487 HOH   A O   1 
HETATM 3784 O  O   . HOH   O 5 .   ? 19.69397  -12.32702 -11.18036 1.000 27.50493 ?  488 HOH   A O   1 
HETATM 3785 O  O   . HOH   O 5 .   ? 20.30387  17.82146  -6.60546  1.000 27.93854 ?  489 HOH   A O   1 
HETATM 3786 O  O   . HOH   O 5 .   ? 26.98071  -14.49746 3.90640   1.000 14.51658 ?  490 HOH   A O   1 
HETATM 3787 O  O   . HOH   O 5 .   ? 37.43420  2.98316   24.27406  1.000 46.16679 ?  491 HOH   A O   1 
HETATM 3788 O  O   . HOH   O 5 .   ? 19.74876  2.06569   -18.34921 1.000 28.40647 ?  492 HOH   A O   1 
HETATM 3789 O  O   . HOH   O 5 .   ? 13.70657  15.30578  6.81804   1.000 19.86292 ?  493 HOH   A O   1 
HETATM 3790 O  O   . HOH   O 5 .   ? 33.46086  4.93558   -13.49378 1.000 41.78777 ?  494 HOH   A O   1 
HETATM 3791 O  O   . HOH   O 5 .   ? 8.05907   8.28234   7.07408   1.000 46.38736 ?  495 HOH   A O   1 
HETATM 3792 O  O   . HOH   O 5 .   ? 10.10092  8.20216   0.86067   1.000 20.19736 ?  496 HOH   A O   1 
HETATM 3793 O  O   . HOH   O 5 .   ? 11.05673  13.98199  10.24309  1.000 20.71650 ?  497 HOH   A O   1 
HETATM 3794 O  O   . HOH   O 5 .   ? 28.68236  14.91195  15.52266  1.000 23.57582 ?  498 HOH   A O   1 
HETATM 3795 O  O   . HOH   O 5 .   ? 11.22087  -11.16803 -9.05449  1.000 21.03070 ?  499 HOH   A O   1 
HETATM 3796 O  O   . HOH   O 5 .   ? 31.64953  11.28391  -8.66567  1.000 29.87969 ?  500 HOH   A O   1 
HETATM 3797 O  O   . HOH   O 5 .   ? 15.66990  -3.20160  -16.40489 1.000 25.41927 ?  501 HOH   A O   1 
HETATM 3798 O  O   . HOH   O 5 .   ? 16.57914  -3.50273  -13.18497 1.000 17.75044 ?  502 HOH   A O   1 
HETATM 3799 O  O   . HOH   O 5 .   ? 23.63321  -12.80160 -11.14011 1.000 25.35736 ?  503 HOH   A O   1 
HETATM 3800 O  O   . HOH   O 5 .   ? 27.19781  -0.60185  -17.08815 1.000 28.04930 ?  504 HOH   A O   1 
HETATM 3801 O  O   . HOH   O 5 .   ? 22.89120  -12.53452 21.26288  1.000 37.10410 ?  505 HOH   A O   1 
HETATM 3802 O  O   . HOH   O 5 .   ? 12.24526  6.30331   8.73107   1.000 24.82511 ?  506 HOH   A O   1 
HETATM 3803 O  O   . HOH   O 5 .   ? 17.06255  9.46949   9.21302   1.000 15.65451 ?  507 HOH   A O   1 
HETATM 3804 O  O   . HOH   O 5 .   ? 32.90315  4.05242   19.81866  1.000 22.16681 ?  508 HOH   A O   1 
HETATM 3805 O  O   . HOH   O 5 .   ? 35.41523  3.90953   20.37024  1.000 26.83624 ?  509 HOH   A O   1 
HETATM 3806 O  O   . HOH   O 5 .   ? 40.57053  1.55416   -5.02407  1.000 19.17526 ?  510 HOH   A O   1 
HETATM 3807 O  O   . HOH   O 5 .   ? 7.03680   10.90116  5.92966   1.000 37.29355 ?  511 HOH   A O   1 
HETATM 3808 O  O   . HOH   O 5 .   ? 15.65608  2.56369   -12.53973 1.000 32.28066 ?  512 HOH   A O   1 
HETATM 3809 O  O   . HOH   O 5 .   ? 28.60023  15.61582  -5.89238  1.000 33.45161 ?  513 HOH   A O   1 
HETATM 3810 O  O   . HOH   O 5 .   ? 27.55135  -9.42159  11.30263  1.000 19.55917 ?  514 HOH   A O   1 
HETATM 3811 O  O   . HOH   O 5 .   ? 42.65377  -1.49263  11.30016  1.000 35.24374 ?  515 HOH   A O   1 
HETATM 3812 O  O   . HOH   O 5 .   ? 9.44149   0.28145   -8.75358  1.000 40.54141 ?  516 HOH   A O   1 
HETATM 3813 O  O   . HOH   O 5 .   ? 17.99984  10.08721  -16.28688 1.000 25.67623 ?  517 HOH   A O   1 
HETATM 3814 O  O   . HOH   O 5 .   ? 33.74947  -13.85122 -5.53364  1.000 19.37421 ?  518 HOH   A O   1 
HETATM 3815 O  O   . HOH   O 5 .   ? 32.40060  -13.95198 -11.75024 1.000 18.41035 ?  519 HOH   A O   1 
HETATM 3816 O  O   . HOH   O 5 .   ? 33.02463  -3.22409  -15.48860 1.000 26.56813 ?  520 HOH   A O   1 
HETATM 3817 O  O   . HOH   O 5 .   ? 4.726     -7.794    -3.893    1.000 25.03823 ?  521 HOH   A O   1 
HETATM 3818 O  O   . HOH   O 5 .   ? 12.38228  -1.96569  0.69072   1.000 16.23496 ?  522 HOH   A O   1 
HETATM 3819 O  O   . HOH   O 5 .   ? 26.55992  -7.25043  9.88168   1.000 16.20090 ?  523 HOH   A O   1 
HETATM 3820 O  O   . HOH   O 5 .   ? 22.39554  8.58990   -17.22179 1.000 37.28593 ?  524 HOH   A O   1 
HETATM 3821 O  O   . HOH   O 5 .   ? 36.40836  9.84015   13.11891  1.000 18.68089 ?  525 HOH   A O   1 
HETATM 3822 O  O   . HOH   O 5 .   ? 22.51826  10.74581  -10.27350 1.000 14.52599 ?  526 HOH   A O   1 
HETATM 3823 O  O   . HOH   O 5 .   ? 26.38378  -4.30063  -15.94317 1.000 30.64826 ?  527 HOH   A O   1 
HETATM 3824 O  O   . HOH   O 5 .   ? 42.11653  -14.15611 9.53164   1.000 43.74187 ?  528 HOH   A O   1 
HETATM 3825 O  O   . HOH   O 5 .   ? 22.13572  4.56671   16.82213  1.000 26.34034 ?  529 HOH   A O   1 
HETATM 3826 O  O   . HOH   O 5 .   ? 8.94101   -1.67394  -12.15834 1.000 27.69413 ?  530 HOH   A O   1 
HETATM 3827 O  O   . HOH   O 5 .   ? 12.07628  -15.52017 0.09515   1.000 27.97556 ?  531 HOH   A O   1 
HETATM 3828 O  O   . HOH   O 5 .   ? 31.99725  10.78202  18.14739  1.000 25.10564 ?  532 HOH   A O   1 
HETATM 3829 O  O   . HOH   O 5 .   ? 27.11803  -0.22516  10.57459  1.000 15.64747 ?  533 HOH   A O   1 
HETATM 3830 O  O   . HOH   O 5 .   ? 17.58669  15.62746  -4.59812  1.000 16.55831 ?  534 HOH   A O   1 
HETATM 3831 O  O   . HOH   O 5 .   ? 6.36991   -7.97139  -1.56113  1.000 30.51247 ?  535 HOH   A O   1 
HETATM 3832 O  O   . HOH   O 5 .   ? 23.43119  13.39267  -13.59454 1.000 37.24205 ?  536 HOH   A O   1 
HETATM 3833 O  O   . HOH   O 5 .   ? 10.57216  4.84761   -5.18956  1.000 27.71289 ?  537 HOH   A O   1 
HETATM 3834 O  O   . HOH   O 5 .   ? 35.17075  4.66024   -11.93438 1.000 30.50007 ?  538 HOH   A O   1 
HETATM 3835 O  O   . HOH   O 5 .   ? 35.54393  -14.92651 -3.70647  1.000 26.66882 ?  539 HOH   A O   1 
HETATM 3836 O  O   . HOH   O 5 .   ? 36.53947  -0.04362  21.16186  1.000 49.52376 ?  540 HOH   A O   1 
HETATM 3837 O  O   . HOH   O 5 .   ? 26.19717  17.80806  -7.85101  1.000 33.43777 ?  541 HOH   A O   1 
HETATM 3838 O  O   . HOH   O 5 .   ? 9.12251   -20.11615 -6.73196  1.000 38.34058 ?  542 HOH   A O   1 
HETATM 3839 O  O   . HOH   O 5 .   ? 22.56113  18.99102  10.15703  1.000 31.46944 ?  543 HOH   A O   1 
HETATM 3840 O  O   . HOH   O 5 .   ? 44.44349  -0.07054  15.36689  1.000 38.50179 ?  544 HOH   A O   1 
HETATM 3841 O  O   . HOH   O 5 .   ? 10.10546  -9.58689  -13.37161 1.000 17.22154 ?  545 HOH   A O   1 
HETATM 3842 O  O   . HOH   O 5 .   ? 35.02745  16.51219  14.13604  1.000 32.81250 ?  546 HOH   A O   1 
HETATM 3843 O  O   . HOH   O 5 .   ? 17.16084  3.38117   -15.22885 1.000 21.78836 ?  547 HOH   A O   1 
HETATM 3844 O  O   . HOH   O 5 .   ? 24.14994  -11.46233 14.39924  1.000 35.97921 ?  548 HOH   A O   1 
HETATM 3845 O  O   . HOH   O 5 .   ? 17.73436  5.13039   14.24995  1.000 31.67958 ?  549 HOH   A O   1 
HETATM 3846 O  O   . HOH   O 5 .   ? 18.91651  16.20634  7.54855   1.000 20.04484 ?  550 HOH   A O   1 
HETATM 3847 O  O   . HOH   O 5 .   ? 37.04208  11.05439  1.28323   1.000 23.34031 ?  551 HOH   A O   1 
HETATM 3848 O  O   . HOH   O 5 .   ? 37.10259  -6.61127  14.92559  1.000 40.49172 ?  552 HOH   A O   1 
HETATM 3849 O  O   . HOH   O 5 .   ? 10.35190  1.10894   4.38450   1.000 38.16190 ?  553 HOH   A O   1 
HETATM 3850 O  O   . HOH   O 5 .   ? 25.61009  -15.57679 6.05662   1.000 15.72215 ?  554 HOH   A O   1 
HETATM 3851 O  O   . HOH   O 5 .   ? 36.69700  -2.62384  16.26204  1.000 28.53534 ?  555 HOH   A O   1 
HETATM 3852 O  O   . HOH   O 5 .   ? 19.14105  -6.23578  2.98857   1.000 14.33360 ?  556 HOH   A O   1 
HETATM 3853 O  O   . HOH   O 5 .   ? 37.27352  -16.02568 -5.11120  1.000 36.43928 ?  557 HOH   A O   1 
HETATM 3854 O  O   . HOH   O 5 .   ? 40.19292  -6.08166  11.74863  1.000 32.04121 ?  558 HOH   A O   1 
HETATM 3855 O  O   . HOH   O 5 .   ? 13.67248  17.98693  -6.96185  1.000 29.50783 ?  559 HOH   A O   1 
HETATM 3856 O  O   . HOH   O 5 .   ? 21.24828  -13.71656 -10.26553 1.000 25.08157 ?  560 HOH   A O   1 
HETATM 3857 O  O   . HOH   O 5 .   ? 7.97165   -6.06540  3.39815   1.000 25.53270 ?  561 HOH   A O   1 
HETATM 3858 O  O   . HOH   O 5 .   ? 25.64728  10.58874  3.35459   1.000 11.53464 ?  562 HOH   A O   1 
HETATM 3859 O  O   . HOH   O 5 .   ? 6.99589   -5.06631  -2.36793  1.000 44.02614 ?  563 HOH   A O   1 
HETATM 3860 O  O   . HOH   O 5 .   ? 12.50533  0.00232   -12.05886 1.000 29.08751 ?  564 HOH   A O   1 
HETATM 3861 O  O   . HOH   O 5 .   ? 15.32923  -0.00302  -12.38482 1.000 22.39127 ?  565 HOH   A O   1 
HETATM 3862 O  O   . HOH   O 5 .   ? 42.13456  2.36018   -7.35034  1.000 31.19058 ?  566 HOH   A O   1 
HETATM 3863 O  O   . HOH   O 5 .   ? 9.83042   -12.96594 4.31133   1.000 37.29477 ?  567 HOH   A O   1 
HETATM 3864 O  O   . HOH   O 5 .   ? 19.14596  7.03396   -9.00616  1.000 20.74609 ?  568 HOH   A O   1 
HETATM 3865 O  O   . HOH   O 5 .   ? 28.81726  5.03896   -16.45187 1.000 35.04784 ?  569 HOH   A O   1 
HETATM 3866 O  O   . HOH   O 5 .   ? 29.90604  -11.01998 -17.58944 1.000 31.42960 ?  570 HOH   A O   1 
HETATM 3867 O  O   . HOH   O 5 .   ? 41.68028  6.88804   -6.43590  1.000 32.92694 ?  571 HOH   A O   1 
HETATM 3868 O  O   . HOH   O 5 .   ? 42.52682  17.13304  0.48274   1.000 43.24347 ?  572 HOH   A O   1 
HETATM 3869 O  O   . HOH   O 5 .   ? 33.52604  8.88395   -13.14827 1.000 22.40065 ?  573 HOH   A O   1 
HETATM 3870 O  O   . HOH   O 5 .   ? 11.23255  15.11962  -1.43820  1.000 34.06498 ?  574 HOH   A O   1 
HETATM 3871 O  O   . HOH   O 5 .   ? 44.05661  5.67271   -1.35176  1.000 40.70128 ?  575 HOH   A O   1 
HETATM 3872 O  O   . HOH   O 5 .   ? 29.54874  -12.22765 -15.42615 1.000 23.11234 ?  576 HOH   A O   1 
HETATM 3873 O  O   . HOH   O 5 .   ? 32.16614  1.39427   19.84970  1.000 23.72633 ?  577 HOH   A O   1 
HETATM 3874 O  O   . HOH   O 5 .   ? 45.74140  3.51335   10.52762  1.000 34.02892 ?  578 HOH   A O   1 
HETATM 3875 O  O   . HOH   O 5 .   ? 42.85937  2.50987   -3.21422  1.000 37.96062 ?  579 HOH   A O   1 
HETATM 3876 O  O   . HOH   O 5 .   ? 36.94360  12.58227  11.09658  1.000 27.58003 ?  580 HOH   A O   1 
HETATM 3877 O  O   . HOH   O 5 .   ? 10.17451  -14.37249 1.72392   1.000 29.50055 ?  581 HOH   A O   1 
HETATM 3878 O  O   . HOH   O 5 .   ? 6.96837   2.19268   2.83189   1.000 44.46681 ?  582 HOH   A O   1 
HETATM 3879 O  O   . HOH   O 5 .   ? 42.79993  -6.52476  -5.74740  1.000 34.03252 ?  583 HOH   A O   1 
HETATM 3880 O  O   . HOH   O 5 .   ? 22.10289  2.70181   19.33465  1.000 40.84738 ?  584 HOH   A O   1 
HETATM 3881 O  O   . HOH   O 5 .   ? 15.61019  -13.35052 -13.98839 1.000 23.79230 ?  585 HOH   A O   1 
HETATM 3882 O  O   . HOH   O 5 .   ? 28.58853  14.37137  -8.46328  1.000 23.36228 ?  586 HOH   A O   1 
HETATM 3883 O  O   . HOH   O 5 .   ? 24.86425  -15.08498 9.91340   1.000 32.76171 ?  587 HOH   A O   1 
HETATM 3884 O  O   . HOH   O 5 .   ? 29.17452  -15.99654 3.17237   1.000 20.35612 ?  588 HOH   A O   1 
HETATM 3885 O  O   . HOH   O 5 .   ? 12.70011  -3.52445  19.66687  1.000 46.81023 ?  589 HOH   A O   1 
HETATM 3886 O  O   . HOH   O 5 .   ? 8.33437   -19.63238 -3.79930  1.000 28.40100 ?  590 HOH   A O   1 
HETATM 3887 O  O   . HOH   O 5 .   ? 38.37359  12.54795  -5.02819  1.000 27.08293 ?  591 HOH   A O   1 
HETATM 3888 O  O   . HOH   O 5 .   ? 38.10240  13.79711  14.98494  1.000 38.46164 ?  592 HOH   A O   1 
HETATM 3889 O  O   . HOH   O 5 .   ? 31.78335  -5.26150  24.31122  1.000 39.11562 ?  593 HOH   A O   1 
HETATM 3890 O  O   . HOH   O 5 .   ? 18.44602  19.79841  -4.10044  1.000 30.55558 ?  594 HOH   A O   1 
HETATM 3891 O  O   . HOH   O 5 .   ? 11.99750  17.42910  -5.99547  1.000 33.76058 ?  595 HOH   A O   1 
HETATM 3892 O  O   . HOH   O 5 .   ? 17.06719  -17.81275 -11.59344 1.000 37.10034 ?  596 HOH   A O   1 
HETATM 3893 O  O   . HOH   O 5 .   ? 25.94092  18.92536  -4.41881  1.000 15.47002 ?  597 HOH   A O   1 
HETATM 3894 O  O   . HOH   O 5 .   ? 45.19021  12.75643  1.43691   1.000 45.68311 ?  598 HOH   A O   1 
HETATM 3895 O  O   . HOH   O 5 .   ? 13.41802  10.41600  -5.86779  1.000 20.72841 ?  599 HOH   A O   1 
HETATM 3896 O  O   . HOH   O 5 .   ? 15.450    5.329     -10.000   1.000 27.43347 ?  600 HOH   A O   1 
HETATM 3897 O  O   . HOH   O 5 .   ? 15.34757  -5.67054  5.68990   1.000 54.73275 ?  601 HOH   A O   1 
HETATM 3898 O  O   . HOH   O 5 .   ? 35.29641  -6.37473  -15.02122 1.000 30.12838 ?  602 HOH   A O   1 
HETATM 3899 O  O   . HOH   O 5 .   ? 38.029    3.545     -12.379   1.000 41.34444 ?  603 HOH   A O   1 
HETATM 3900 O  O   . HOH   O 5 .   ? 42.83065  12.24228  -0.69293  1.000 47.54907 ?  604 HOH   A O   1 
HETATM 3901 O  O   . HOH   O 5 .   ? 13.30202  4.66223   6.55859   1.000 14.92419 ?  605 HOH   A O   1 
HETATM 3902 O  O   . HOH   O 5 .   ? 16.00122  10.95749  12.16519  1.000 32.20478 ?  606 HOH   A O   1 
HETATM 3903 O  O   . HOH   O 5 .   ? 2.716     -10.200   1.224     1.000 33.32760 ?  607 HOH   A O   1 
HETATM 3904 O  O   . HOH   O 5 .   ? 28.85551  -4.40648  -17.13184 1.000 46.31270 ?  608 HOH   A O   1 
HETATM 3905 O  O   . HOH   O 5 .   ? 25.93978  -11.33378 24.13462  1.000 52.31467 ?  609 HOH   A O   1 
HETATM 3906 O  O   . HOH   O 5 .   ? 35.77335  12.21229  -6.50281  1.000 25.10251 ?  610 HOH   A O   1 
HETATM 3907 O  O   . HOH   O 5 .   ? 10.901    -11.162   19.123    1.000 44.36182 ?  611 HOH   A O   1 
HETATM 3908 O  O   . HOH   O 5 .   ? 28.00434  19.87268  5.68409   1.000 18.09664 ?  612 HOH   A O   1 
HETATM 3909 O  O   . HOH   O 5 .   ? 27.18633  5.37345   -18.11252 1.000 48.61897 ?  613 HOH   A O   1 
HETATM 3910 O  O   . HOH   O 5 .   ? 43.90098  12.85226  12.38805  1.000 47.74693 ?  614 HOH   A O   1 
HETATM 3911 O  O   . HOH   O 5 .   ? 9.66435   5.99757   8.28420   1.000 38.00907 ?  615 HOH   A O   1 
HETATM 3912 O  O   . HOH   O 5 .   ? 26.84331  -18.03428 6.55752   1.000 33.30923 ?  616 HOH   A O   1 
HETATM 3913 O  O   . HOH   O 5 .   ? 34.76426  11.37926  17.43185  1.000 38.27932 ?  617 HOH   A O   1 
HETATM 3914 O  O   . HOH   O 5 .   ? 11.31150  3.22269   5.70608   1.000 46.22857 ?  618 HOH   A O   1 
HETATM 3915 O  O   . HOH   O 5 .   ? 15.97607  16.62509  -0.84340  1.000 36.12666 ?  619 HOH   A O   1 
HETATM 3916 O  O   . HOH   O 5 .   ? 21.41595  13.03397  -11.74109 1.000 25.49595 ?  620 HOH   A O   1 
HETATM 3917 O  O   . HOH   O 5 .   ? 33.35619  -6.01931  -16.74123 1.000 43.10848 ?  621 HOH   A O   1 
HETATM 3918 O  O   . HOH   O 5 .   ? 41.25474  8.83570   -5.58672  1.000 42.99930 ?  622 HOH   A O   1 
HETATM 3919 O  O   . HOH   O 5 .   ? 20.00990  15.65847  -10.73839 1.000 41.09105 ?  623 HOH   A O   1 
HETATM 3920 O  O   . HOH   O 5 .   ? 44.50868  -4.96865  -1.70702  1.000 33.85174 ?  624 HOH   A O   1 
HETATM 3921 O  O   . HOH   O 5 .   ? 17.90835  5.57436   16.42513  1.000 43.56578 ?  625 HOH   A O   1 
HETATM 3922 O  O   . HOH   O 5 .   ? 28.45752  18.17476  -5.34475  1.000 30.82423 ?  626 HOH   A O   1 
HETATM 3923 O  O   . HOH   O 5 .   ? 43.26182  12.01450  -2.78925  1.000 52.48109 ?  627 HOH   A O   1 
HETATM 3924 O  O   . HOH   O 5 .   ? 37.70650  -6.78118  -14.53908 1.000 45.26119 ?  628 HOH   A O   1 
HETATM 3925 O  O   . HOH   O 5 .   ? 30.33306  16.95043  16.21336  1.000 32.43883 ?  629 HOH   A O   1 
HETATM 3926 O  O   . HOH   O 5 .   ? 23.64504  16.04976  15.21662  1.000 30.86796 ?  630 HOH   A O   1 
HETATM 3927 O  O   . HOH   O 5 .   ? 43.10688  5.70590   -3.93555  1.000 37.56348 ?  631 HOH   A O   1 
HETATM 3928 O  O   . HOH   O 5 .   ? 11.34111  -19.02077 -7.30141  1.000 34.75044 ?  632 HOH   A O   1 
HETATM 3929 O  O   . HOH   O 5 .   ? 30.36292  7.68788   21.12894  1.000 24.30555 ?  633 HOH   A O   1 
HETATM 3930 O  O   . HOH   O 5 .   ? 20.02181  9.77687   -9.11514  1.000 14.95460 ?  634 HOH   A O   1 
HETATM 3931 O  O   . HOH   O 5 .   ? 38.14334  -10.56840 4.62076   1.000 38.49514 ?  635 HOH   A O   1 
HETATM 3932 O  O   . HOH   O 5 .   ? 12.67247  15.91527  9.52539   1.000 26.96228 ?  636 HOH   A O   1 
HETATM 3933 O  O   . HOH   O 5 .   ? 38.88306  -2.63955  -11.56566 1.000 33.22226 ?  637 HOH   A O   1 
HETATM 3934 O  O   . HOH   O 5 .   ? 33.45476  12.86858  -7.78055  1.000 31.88564 ?  638 HOH   A O   1 
HETATM 3935 O  O   . HOH   O 5 .   ? 18.05602  6.82904   21.06607  1.000 38.20931 ?  639 HOH   A O   1 
HETATM 3936 O  O   . HOH   O 5 .   ? 39.06793  13.38155  12.58005  1.000 32.75510 ?  640 HOH   A O   1 
HETATM 3937 O  O   . HOH   O 5 .   ? 19.89508  19.30238  9.87798   1.000 39.96814 ?  641 HOH   A O   1 
HETATM 3938 O  O   . HOH   O 5 .   ? 24.93072  1.21498   -19.11890 1.000 43.75935 ?  642 HOH   A O   1 
HETATM 3939 O  O   . HOH   O 5 .   ? 13.374    -12.079   8.448     1.000 40.17454 ?  643 HOH   A O   1 
HETATM 3940 O  O   . HOH   O 5 .   ? 42.81679  0.47090   -8.74501  1.000 37.27515 ?  644 HOH   A O   1 
HETATM 3941 O  O   . HOH   O 5 .   ? 40.23566  -3.01827  12.44289  1.000 42.76587 ?  645 HOH   A O   1 
HETATM 3942 O  O   . HOH   O 5 .   ? 22.349    -20.673   8.507     1.000 40.48216 ?  646 HOH   A O   1 
HETATM 3943 O  O   . HOH   O 5 .   ? 36.04994  -4.25699  -15.01680 1.000 38.61494 ?  647 HOH   A O   1 
HETATM 3944 O  O   . HOH   O 5 .   ? 30.230    -14.886   -15.486   1.000 32.12134 ?  648 HOH   A O   1 
HETATM 3945 O  O   . HOH   O 5 .   ? 15.08971  16.84409  -3.02268  1.000 35.67954 ?  649 HOH   A O   1 
HETATM 3946 O  O   . HOH   O 5 .   ? 23.29782  -7.26006  -17.28262 1.000 35.64454 ?  650 HOH   A O   1 
HETATM 3947 O  O   . HOH   O 5 .   ? 49.861    9.059     8.348     1.000 48.16190 ?  651 HOH   A O   1 
HETATM 3948 O  O   . HOH   O 5 .   ? 31.39020  10.36999  20.65406  1.000 32.89207 ?  652 HOH   A O   1 
HETATM 3949 O  O   . HOH   O 5 .   ? 17.57068  17.22984  -6.88860  1.000 37.38201 ?  653 HOH   A O   1 
HETATM 3950 O  O   . HOH   O 5 .   ? 50.188    11.384    7.874     1.000 38.26847 ?  654 HOH   A O   1 
HETATM 3951 O  O   . HOH   O 5 .   ? 32.73935  -20.04690 -2.73195  1.000 36.98954 ?  655 HOH   A O   1 
HETATM 3952 O  O   . HOH   O 5 .   ? 9.23489   5.95904   -0.61073  1.000 27.18163 ?  656 HOH   A O   1 
HETATM 3953 O  O   . HOH   O 5 .   ? 45.56348  1.73079   -4.16877  1.000 41.35353 ?  657 HOH   A O   1 
HETATM 3954 O  O   . HOH   O 5 .   ? 29.48571  -5.11160  -19.16006 1.000 39.60308 ?  658 HOH   A O   1 
HETATM 3955 O  O   . HOH   O 5 .   ? 15.15417  7.34380   14.77797  1.000 33.09065 ?  659 HOH   A O   1 
HETATM 3956 O  O   . HOH   O 5 .   ? 36.19040  19.42597  10.14976  1.000 33.15820 ?  660 HOH   A O   1 
HETATM 3957 O  O   . HOH   O 5 .   ? 36.67784  -0.66848  -11.07161 1.000 33.42099 ?  661 HOH   A O   1 
HETATM 3958 O  O   . HOH   O 5 .   ? 39.04296  -7.89011  12.99151  1.000 42.97403 ?  662 HOH   A O   1 
HETATM 3959 O  O   . HOH   O 5 .   ? 34.15128  -15.44841 -7.84275  1.000 31.89442 ?  663 HOH   A O   1 
HETATM 3960 O  O   . HOH   O 5 .   ? -1.587    -16.546   -2.084    1.000 44.10161 ?  664 HOH   A O   1 
HETATM 3961 O  O   . HOH   O 5 .   ? 26.58369  9.52540   21.42389  1.000 39.63213 ?  665 HOH   A O   1 
HETATM 3962 O  O   . HOH   O 5 .   ? 24.86086  -2.61900  -16.78286 1.000 26.50214 ?  666 HOH   A O   1 
HETATM 3963 O  O   . HOH   O 5 .   ? 10.22590  4.17860   -2.88959  1.000 24.16735 ?  667 HOH   A O   1 
HETATM 3964 O  O   . HOH   O 5 .   ? 36.18321  4.56311   22.58217  1.000 36.37605 ?  668 HOH   A O   1 
HETATM 3965 O  O   . HOH   O 5 .   ? 21.48598  4.49738   -20.07993 1.000 43.09577 ?  669 HOH   A O   1 
HETATM 3966 O  O   . HOH   O 5 .   ? 35.65747  -8.41529  16.23558  1.000 36.42237 ?  670 HOH   A O   1 
HETATM 3967 O  O   . HOH   O 5 .   ? 35.07455  -16.67310 -1.46850  1.000 39.47538 ?  671 HOH   A O   1 
HETATM 3968 O  O   . HOH   O 5 .   ? 31.23685  3.03831   -16.57731 1.000 34.97476 ?  672 HOH   A O   1 
HETATM 3969 O  O   . HOH   O 5 .   ? 42.77087  14.97425  13.67848  1.000 36.31889 ?  673 HOH   A O   1 
HETATM 3970 O  O   . HOH   O 5 .   ? 26.00642  -11.66484 11.86519  1.000 22.93129 ?  674 HOH   A O   1 
HETATM 3971 O  O   . HOH   O 5 .   ? 21.28626  13.75548  15.22674  1.000 28.68496 ?  675 HOH   A O   1 
HETATM 3972 O  O   . HOH   O 5 .   ? 35.98829  17.67016  -1.57260  1.000 41.34244 ?  676 HOH   A O   1 
HETATM 3973 O  O   . HOH   O 5 .   ? 44.34711  17.14492  -0.57398  1.000 39.20191 ?  677 HOH   A O   1 
HETATM 3974 O  O   . HOH   O 5 .   ? 6.71616   14.92085  0.98643   1.000 36.54723 ?  678 HOH   A O   1 
HETATM 3975 O  O   . HOH   O 5 .   ? 45.346    13.383    9.851     1.000 32.15299 ?  679 HOH   A O   1 
HETATM 3976 O  O   . HOH   O 5 .   ? 26.21974  15.63573  16.75415  1.000 29.00438 ?  680 HOH   A O   1 
HETATM 3977 O  O   . HOH   O 5 .   ? 10.06148  10.77472  -4.18186  1.000 29.65558 ?  681 HOH   A O   1 
HETATM 3978 O  O   . HOH   O 5 .   ? 8.852     -20.092   -0.298    1.000 46.97899 ?  682 HOH   A O   1 
HETATM 3979 O  O   . HOH   O 5 .   ? 31.86689  5.54869   21.75492  1.000 28.62893 ?  683 HOH   A O   1 
HETATM 3980 O  O   . HOH   O 5 .   ? 9.46434   15.45975  -3.19969  1.000 32.30217 ?  684 HOH   A O   1 
HETATM 3981 O  O   . HOH   O 5 .   ? 31.017    22.922    11.041    1.000 34.78529 ?  685 HOH   A O   1 
HETATM 3982 O  O   . HOH   O 5 .   ? 14.96040  17.78674  6.85460   1.000 35.83956 ?  686 HOH   A O   1 
HETATM 3983 O  O   . HOH   O 5 .   ? 32.09527  -15.84560 -9.89344  1.000 30.68889 ?  687 HOH   A O   1 
HETATM 3984 O  O   . HOH   O 5 .   ? 29.35388  7.34698   -18.37647 1.000 38.58754 ?  688 HOH   A O   1 
HETATM 3985 O  O   . HOH   O 5 .   ? 29.64547  12.75438  17.17048  1.000 33.11166 ?  689 HOH   A O   1 
HETATM 3986 O  O   . HOH   O 5 .   ? 9.62178   2.89756   -9.76132  1.000 36.70614 ?  690 HOH   A O   1 
HETATM 3987 O  O   . HOH   O 5 .   ? 35.05573  12.35147  12.49298  1.000 38.80341 ?  691 HOH   A O   1 
HETATM 3988 O  O   . HOH   O 5 .   ? 8.66700   2.86314   -6.25286  1.000 34.89852 ?  692 HOH   A O   1 
HETATM 3989 O  O   . HOH   O 5 .   ? 35.46301  -10.35128 3.87265   1.000 31.08201 ?  693 HOH   A O   1 
HETATM 3990 O  O   . HOH   O 5 .   ? 24.41310  -5.39908  -17.92372 1.000 39.01083 ?  694 HOH   A O   1 
HETATM 3991 O  O   . HOH   O 5 .   ? 26.44455  -14.41628 11.99478  1.000 31.23974 ?  695 HOH   A O   1 
HETATM 3992 O  O   . HOH   O 5 .   ? 45.83750  12.24145  -3.03765  1.000 48.14168 ?  696 HOH   A O   1 
HETATM 3993 O  O   . HOH   O 5 .   ? 29.74421  16.32226  -9.98361  1.000 36.22831 ?  697 HOH   A O   1 
HETATM 3994 O  O   . HOH   O 5 .   ? 34.379    -16.933   5.343     1.000 45.36533 ?  698 HOH   A O   1 
HETATM 3995 O  O   . HOH   O 5 .   ? 34.40551  13.18059  15.19806  1.000 31.96813 ?  699 HOH   A O   1 
HETATM 3996 O  O   . HOH   O 5 .   ? 3.252     -15.676   2.913     1.000 50.56560 ?  700 HOH   A O   1 
HETATM 3997 O  O   . HOH   O 5 .   ? 28.57613  13.25275  19.38622  1.000 36.00452 ?  701 HOH   A O   1 
HETATM 3998 O  O   . HOH   P 5 .   ? -3.15092  27.03943  33.84260  1.000 35.87313 ?  401 HOH   B O   1 
HETATM 3999 O  O   . HOH   P 5 .   ? -17.89262 12.97303  25.82035  1.000 27.80187 ?  402 HOH   B O   1 
HETATM 4000 O  O   . HOH   P 5 .   ? 11.72377  38.09892  21.09240  1.000 28.79124 ?  403 HOH   B O   1 
HETATM 4001 O  O   . HOH   P 5 .   ? -3.77202  4.29577   3.61724   1.000 38.94148 ?  404 HOH   B O   1 
HETATM 4002 O  O   . HOH   P 5 .   ? -15.22807 27.78258  20.18816  1.000 45.62253 ?  405 HOH   B O   1 
HETATM 4003 O  O   . HOH   P 5 .   ? -1.36897  9.15205   2.79549   1.000 42.65219 ?  406 HOH   B O   1 
HETATM 4004 O  O   . HOH   P 5 .   ? 21.02405  19.86603  34.75411  1.000 42.56114 ?  407 HOH   B O   1 
HETATM 4005 O  O   . HOH   P 5 .   ? 0.03330   24.06320  34.63353  1.000 22.27877 ?  408 HOH   B O   1 
HETATM 4006 O  O   . HOH   P 5 .   ? 9.86153   32.70939  9.96050   1.000 30.70806 ?  409 HOH   B O   1 
HETATM 4007 O  O   . HOH   P 5 .   ? 4.21896   9.74517   9.09190   1.000 32.00654 ?  410 HOH   B O   1 
HETATM 4008 O  O   . HOH   P 5 .   ? 11.84542  37.13773  36.87900  1.000 20.28527 ?  411 HOH   B O   1 
HETATM 4009 O  O   . HOH   P 5 .   ? -11.29811 23.31016  13.37832  1.000 55.54754 ?  412 HOH   B O   1 
HETATM 4010 O  O   . HOH   P 5 .   ? 14.23005  35.16654  31.46205  1.000 39.03556 ?  413 HOH   B O   1 
HETATM 4011 O  O   . HOH   P 5 .   ? 0.99764   -0.36688  32.40857  1.000 43.36842 ?  414 HOH   B O   1 
HETATM 4012 O  O   . HOH   P 5 .   ? 18.77281  17.77720  33.89285  1.000 29.83762 ?  415 HOH   B O   1 
HETATM 4013 O  O   . HOH   P 5 .   ? -17.61173 16.45022  17.90213  1.000 38.64176 ?  416 HOH   B O   1 
HETATM 4014 O  O   . HOH   P 5 .   ? 11.27201  11.71950  35.96671  1.000 22.99305 ?  417 HOH   B O   1 
HETATM 4015 O  O   . HOH   P 5 .   ? 5.16141   37.95165  21.28596  1.000 19.54509 ?  418 HOH   B O   1 
HETATM 4016 O  O   . HOH   P 5 .   ? -5.89689  9.61407   35.34015  1.000 22.85461 ?  419 HOH   B O   1 
HETATM 4017 O  O   . HOH   P 5 .   ? 1.38981   21.16761  38.75269  1.000 27.51371 ?  420 HOH   B O   1 
HETATM 4018 O  O   . HOH   P 5 .   ? -0.13149  36.98777  37.47552  1.000 38.86998 ?  421 HOH   B O   1 
HETATM 4019 O  O   . HOH   P 5 .   ? -3.36393  3.88082   37.85972  1.000 32.78006 ?  422 HOH   B O   1 
HETATM 4020 O  O   . HOH   P 5 .   ? -16.87353 7.27173   11.00121  1.000 19.00589 ?  423 HOH   B O   1 
HETATM 4021 O  O   . HOH   P 5 .   ? -15.85508 18.54093  35.01264  1.000 34.90667 ?  424 HOH   B O   1 
HETATM 4022 O  O   . HOH   P 5 .   ? 14.54435  35.72454  33.48354  1.000 42.46294 ?  425 HOH   B O   1 
HETATM 4023 O  O   . HOH   P 5 .   ? -1.975    3.290     40.658    1.000 26.55170 ?  426 HOH   B O   1 
HETATM 4024 O  O   . HOH   P 5 .   ? 9.75962   11.37956  30.56347  1.000 14.34167 ?  427 HOH   B O   1 
HETATM 4025 O  O   . HOH   P 5 .   ? -10.11081 9.92999   33.46826  1.000 32.95634 ?  428 HOH   B O   1 
HETATM 4026 O  O   . HOH   P 5 .   ? -11.11381 9.89016   13.49287  1.000 20.65208 ?  429 HOH   B O   1 
HETATM 4027 O  O   . HOH   P 5 .   ? 18.06553  26.18949  36.05013  1.000 13.06813 ?  430 HOH   B O   1 
HETATM 4028 O  O   . HOH   P 5 .   ? -15.95128 21.83367  18.82465  1.000 36.05360 ?  431 HOH   B O   1 
HETATM 4029 O  O   . HOH   P 5 .   ? -13.37594 22.74605  16.46473  1.000 27.40218 ?  432 HOH   B O   1 
HETATM 4030 O  O   . HOH   P 5 .   ? 10.735    9.770     39.968    1.000 30.30305 ?  433 HOH   B O   1 
HETATM 4031 O  O   . HOH   P 5 .   ? -5.69651  18.56021  28.06182  1.000 22.78982 ?  434 HOH   B O   1 
HETATM 4032 O  O   . HOH   P 5 .   ? 16.66777  19.22633  41.47144  1.000 32.15939 ?  435 HOH   B O   1 
HETATM 4033 O  O   . HOH   P 5 .   ? 1.80686   1.22761   18.34778  1.000 18.75379 ?  436 HOH   B O   1 
HETATM 4034 O  O   . HOH   P 5 .   ? 19.07459  20.37772  40.75936  1.000 39.33192 ?  437 HOH   B O   1 
HETATM 4035 O  O   . HOH   P 5 .   ? -13.02892 -1.43455  23.31462  1.000 38.38559 ?  438 HOH   B O   1 
HETATM 4036 O  O   . HOH   P 5 .   ? 14.81719  31.21351  24.38236  1.000 20.44669 ?  439 HOH   B O   1 
HETATM 4037 O  O   . HOH   P 5 .   ? -14.26157 9.44610   8.63902   1.000 25.53174 ?  440 HOH   B O   1 
HETATM 4038 O  O   . HOH   P 5 .   ? 21.83537  9.90882   26.33898  1.000 27.17700 ?  441 HOH   B O   1 
HETATM 4039 O  O   . HOH   P 5 .   ? -4.52176  12.62787  40.25093  1.000 32.18185 ?  442 HOH   B O   1 
HETATM 4040 O  O   . HOH   P 5 .   ? 22.07727  14.66865  30.05210  1.000 31.51960 ?  443 HOH   B O   1 
HETATM 4041 O  O   . HOH   P 5 .   ? -3.45595  12.93118  42.33128  1.000 40.63332 ?  444 HOH   B O   1 
HETATM 4042 O  O   . HOH   P 5 .   ? 9.93102   12.59496  40.11459  1.000 26.17054 ?  445 HOH   B O   1 
HETATM 4043 O  O   . HOH   P 5 .   ? 0.60176   28.08959  9.56957   1.000 36.98058 ?  446 HOH   B O   1 
HETATM 4044 O  O   . HOH   P 5 .   ? -5.66778  25.21840  42.60145  1.000 43.53799 ?  447 HOH   B O   1 
HETATM 4045 O  O   . HOH   P 5 .   ? 19.643    8.063     31.749    1.000 19.31984 ?  448 HOH   B O   1 
HETATM 4046 O  O   . HOH   P 5 .   ? 19.26604  7.80134   27.17866  1.000 21.45502 ?  449 HOH   B O   1 
HETATM 4047 O  O   . HOH   P 5 .   ? 11.72785  26.78400  10.86965  1.000 17.70233 ?  450 HOH   B O   1 
HETATM 4048 O  O   . HOH   P 5 .   ? 2.31259   14.14591  42.70168  1.000 36.06431 ?  451 HOH   B O   1 
HETATM 4049 O  O   . HOH   P 5 .   ? -11.47799 26.11416  16.42275  1.000 43.69922 ?  452 HOH   B O   1 
HETATM 4050 O  O   . HOH   P 5 .   ? 14.24787  12.62935  15.55536  1.000 21.48581 ?  453 HOH   B O   1 
HETATM 4051 O  O   . HOH   P 5 .   ? 3.29744   20.58275  7.85638   1.000 25.66513 ?  454 HOH   B O   1 
HETATM 4052 O  O   . HOH   P 5 .   ? -17.79057 12.61118  15.08843  1.000 24.36655 ?  455 HOH   B O   1 
HETATM 4053 O  O   . HOH   P 5 .   ? -4.901    9.117     43.436    1.000 26.49080 ?  456 HOH   B O   1 
HETATM 4054 O  O   . HOH   P 5 .   ? 12.65589  32.88339  24.44822  1.000 15.08639 ?  457 HOH   B O   1 
HETATM 4055 O  O   . HOH   P 5 .   ? 20.63708  17.37324  23.26353  1.000 30.00010 ?  458 HOH   B O   1 
HETATM 4056 O  O   . HOH   P 5 .   ? 5.22540   19.36077  46.55627  1.000 38.30735 ?  459 HOH   B O   1 
HETATM 4057 O  O   . HOH   P 5 .   ? 18.12030  8.58176   22.93707  1.000 28.11947 ?  460 HOH   B O   1 
HETATM 4058 O  O   . HOH   P 5 .   ? 3.03137   24.73729  36.19344  1.000 16.85486 ?  461 HOH   B O   1 
HETATM 4059 O  O   . HOH   P 5 .   ? 15.90232  20.95661  15.71960  1.000 16.25597 ?  462 HOH   B O   1 
HETATM 4060 O  O   . HOH   P 5 .   ? 10.68539  6.45637   19.47774  1.000 32.76793 ?  463 HOH   B O   1 
HETATM 4061 O  O   . HOH   P 5 .   ? 10.85863  22.61550  43.00194  1.000 26.59771 ?  464 HOH   B O   1 
HETATM 4062 O  O   . HOH   P 5 .   ? 1.55766   4.88650   12.11206  1.000 37.17387 ?  465 HOH   B O   1 
HETATM 4063 O  O   . HOH   P 5 .   ? 21.00851  27.59004  33.71262  1.000 39.16667 ?  466 HOH   B O   1 
HETATM 4064 O  O   . HOH   P 5 .   ? 4.40454   15.97342  9.06870   1.000 31.30638 ?  467 HOH   B O   1 
HETATM 4065 O  O   . HOH   P 5 .   ? 1.20550   25.91583  29.99234  1.000 14.15624 ?  468 HOH   B O   1 
HETATM 4066 O  O   . HOH   P 5 .   ? -0.67926  30.62385  36.63903  1.000 24.91315 ?  469 HOH   B O   1 
HETATM 4067 O  O   . HOH   P 5 .   ? 6.11514   19.23733  28.75286  1.000 10.12171 ?  470 HOH   B O   1 
HETATM 4068 O  O   . HOH   P 5 .   ? -10.24214 7.35946   30.33976  1.000 19.00763 ?  471 HOH   B O   1 
HETATM 4069 O  O   . HOH   P 5 .   ? 7.75700   32.56485  15.63923  1.000 31.78183 ?  472 HOH   B O   1 
HETATM 4070 O  O   . HOH   P 5 .   ? 8.28871   24.52307  8.57752   1.000 35.46075 ?  473 HOH   B O   1 
HETATM 4071 O  O   . HOH   P 5 .   ? -12.85627 33.55055  27.85267  1.000 41.80821 ?  474 HOH   B O   1 
HETATM 4072 O  O   . HOH   P 5 .   ? 16.94983  6.26024   28.18610  1.000 21.11087 ?  475 HOH   B O   1 
HETATM 4073 O  O   . HOH   P 5 .   ? 15.50404  18.12070  15.73733  1.000 22.34428 ?  476 HOH   B O   1 
HETATM 4074 O  O   . HOH   P 5 .   ? 3.61918   18.35626  29.45693  1.000 10.68298 ?  477 HOH   B O   1 
HETATM 4075 O  O   . HOH   P 5 .   ? -2.11022  29.76431  31.00518  1.000 37.29092 ?  478 HOH   B O   1 
HETATM 4076 O  O   . HOH   P 5 .   ? -13.26647 4.73597   23.97831  1.000 23.59662 ?  479 HOH   B O   1 
HETATM 4077 O  O   . HOH   P 5 .   ? -1.74604  24.89223  35.41401  1.000 38.86688 ?  480 HOH   B O   1 
HETATM 4078 O  O   . HOH   P 5 .   ? 21.26767  13.43415  26.78330  1.000 26.05274 ?  481 HOH   B O   1 
HETATM 4079 O  O   . HOH   P 5 .   ? -16.711   27.804    40.790    1.000 24.53580 ?  482 HOH   B O   1 
HETATM 4080 O  O   . HOH   P 5 .   ? -14.04370 20.72835  27.74628  1.000 19.25194 ?  483 HOH   B O   1 
HETATM 4081 O  O   . HOH   P 5 .   ? 1.03758   2.10215   10.01062  1.000 45.14203 ?  484 HOH   B O   1 
HETATM 4082 O  O   . HOH   P 5 .   ? 19.81906  14.90465  21.47359  1.000 38.51359 ?  485 HOH   B O   1 
HETATM 4083 O  O   . HOH   P 5 .   ? 12.92687  30.40678  14.98386  1.000 21.96142 ?  486 HOH   B O   1 
HETATM 4084 O  O   . HOH   P 5 .   ? 8.41290   19.52381  43.62885  1.000 24.75080 ?  487 HOH   B O   1 
HETATM 4085 O  O   . HOH   P 5 .   ? -18.090   16.370    9.638     1.000 38.35924 ?  488 HOH   B O   1 
HETATM 4086 O  O   . HOH   P 5 .   ? -5.91411  30.97396  28.85609  1.000 29.77154 ?  489 HOH   B O   1 
HETATM 4087 O  O   . HOH   P 5 .   ? 11.89833  22.23506  11.30372  1.000 17.46008 ?  490 HOH   B O   1 
HETATM 4088 O  O   . HOH   P 5 .   ? 16.14096  30.92816  17.79021  1.000 18.03309 ?  491 HOH   B O   1 
HETATM 4089 O  O   . HOH   P 5 .   ? 17.64006  15.62448  17.57199  1.000 22.25729 ?  492 HOH   B O   1 
HETATM 4090 O  O   . HOH   P 5 .   ? 11.810    28.689    45.806    1.000 26.88278 ?  493 HOH   B O   1 
HETATM 4091 O  O   . HOH   P 5 .   ? 0.14012   28.50444  30.18701  1.000 16.57801 ?  494 HOH   B O   1 
HETATM 4092 O  O   . HOH   P 5 .   ? 19.16244  30.71574  34.42603  1.000 23.76668 ?  495 HOH   B O   1 
HETATM 4093 O  O   . HOH   P 5 .   ? -15.86992 9.36021   20.78123  1.000 24.95439 ?  496 HOH   B O   1 
HETATM 4094 O  O   . HOH   P 5 .   ? 21.27672  26.03977  19.05126  1.000 36.52768 ?  497 HOH   B O   1 
HETATM 4095 O  O   . HOH   P 5 .   ? 14.54910  28.92745  39.36479  1.000 18.35450 ?  498 HOH   B O   1 
HETATM 4096 O  O   . HOH   P 5 .   ? -4.84965  33.99336  27.21506  1.000 30.15183 ?  499 HOH   B O   1 
HETATM 4097 O  O   . HOH   P 5 .   ? -9.04461  20.99861  10.23554  1.000 41.25638 ?  500 HOH   B O   1 
HETATM 4098 O  O   . HOH   P 5 .   ? -19.71180 23.71106  30.70596  1.000 41.86929 ?  501 HOH   B O   1 
HETATM 4099 O  O   . HOH   P 5 .   ? 6.17694   10.52508  28.84194  1.000 9.77775  ?  502 HOH   B O   1 
HETATM 4100 O  O   . HOH   P 5 .   ? 13.02145  6.39811   17.01428  1.000 40.97016 ?  503 HOH   B O   1 
HETATM 4101 O  O   . HOH   P 5 .   ? 18.99529  20.57713  17.13231  1.000 27.81567 ?  504 HOH   B O   1 
HETATM 4102 O  O   . HOH   P 5 .   ? -8.43754  14.48141  6.60180   1.000 25.08955 ?  505 HOH   B O   1 
HETATM 4103 O  O   . HOH   P 5 .   ? 14.67936  32.61300  20.83699  1.000 22.07160 ?  506 HOH   B O   1 
HETATM 4104 O  O   . HOH   P 5 .   ? 5.39731   -0.48980  28.73291  1.000 15.79001 ?  507 HOH   B O   1 
HETATM 4105 O  O   . HOH   P 5 .   ? -6.95600  28.63557  24.92998  1.000 23.01875 ?  508 HOH   B O   1 
HETATM 4106 O  O   . HOH   P 5 .   ? -1.14926  0.42660   31.44810  1.000 27.64364 ?  509 HOH   B O   1 
HETATM 4107 O  O   . HOH   P 5 .   ? -11.291   9.167     6.058     1.000 31.52572 ?  510 HOH   B O   1 
HETATM 4108 O  O   . HOH   P 5 .   ? 3.77078   9.95155   41.43525  1.000 26.39985 ?  511 HOH   B O   1 
HETATM 4109 O  O   . HOH   P 5 .   ? -6.274    12.726    2.748     1.000 38.06280 ?  512 HOH   B O   1 
HETATM 4110 O  O   . HOH   P 5 .   ? 7.66616   2.46485   33.95359  1.000 36.80457 ?  513 HOH   B O   1 
HETATM 4111 O  O   . HOH   P 5 .   ? -7.47706  16.81310  37.21666  1.000 29.65717 ?  514 HOH   B O   1 
HETATM 4112 O  O   . HOH   P 5 .   ? 7.19560   16.31069  10.53167  1.000 13.92830 ?  515 HOH   B O   1 
HETATM 4113 O  O   . HOH   P 5 .   ? 12.23942  5.61016   21.30176  1.000 29.07230 ?  516 HOH   B O   1 
HETATM 4114 O  O   . HOH   P 5 .   ? 16.19084  29.70245  30.55316  1.000 26.47354 ?  517 HOH   B O   1 
HETATM 4115 O  O   . HOH   P 5 .   ? 7.58050   15.61887  38.94221  1.000 13.75952 ?  518 HOH   B O   1 
HETATM 4116 O  O   . HOH   P 5 .   ? 12.40974  10.96456  30.84123  1.000 20.26986 ?  519 HOH   B O   1 
HETATM 4117 O  O   . HOH   P 5 .   ? -7.07200  8.13861   37.82847  1.000 38.97908 ?  520 HOH   B O   1 
HETATM 4118 O  O   . HOH   P 5 .   ? -3.41968  1.44457   17.10528  1.000 26.23345 ?  521 HOH   B O   1 
HETATM 4119 O  O   . HOH   P 5 .   ? 13.04162  6.74481   28.06955  1.000 14.31564 ?  522 HOH   B O   1 
HETATM 4120 O  O   . HOH   P 5 .   ? 21.18890  23.59161  36.08492  1.000 32.24055 ?  523 HOH   B O   1 
HETATM 4121 O  O   . HOH   P 5 .   ? 0.93987   33.12752  24.58997  1.000 14.89876 ?  524 HOH   B O   1 
HETATM 4122 O  O   . HOH   P 5 .   ? 9.50663   37.53664  42.90159  1.000 22.42235 ?  525 HOH   B O   1 
HETATM 4123 O  O   . HOH   P 5 .   ? 5.31832   2.74819   17.71655  1.000 27.11885 ?  526 HOH   B O   1 
HETATM 4124 O  O   . HOH   P 5 .   ? -3.09764  1.61699   24.56820  1.000 13.30014 ?  527 HOH   B O   1 
HETATM 4125 O  O   . HOH   P 5 .   ? -17.06782 16.01189  20.34500  1.000 26.84669 ?  528 HOH   B O   1 
HETATM 4126 O  O   . HOH   P 5 .   ? -4.20243  19.27372  6.78513   1.000 40.53980 ?  529 HOH   B O   1 
HETATM 4127 O  O   . HOH   P 5 .   ? -9.24836  18.64347  8.54826   1.000 39.70477 ?  530 HOH   B O   1 
HETATM 4128 O  O   . HOH   P 5 .   ? -5.71798  26.30740  25.83096  1.000 15.26726 ?  531 HOH   B O   1 
HETATM 4129 O  O   . HOH   P 5 .   ? 18.01789  31.15998  32.27545  1.000 37.91647 ?  532 HOH   B O   1 
HETATM 4130 O  O   . HOH   P 5 .   ? 16.00498  30.01292  26.74070  1.000 25.64712 ?  533 HOH   B O   1 
HETATM 4131 O  O   . HOH   P 5 .   ? 11.62491  0.57727   30.09016  1.000 36.27149 ?  534 HOH   B O   1 
HETATM 4132 O  O   . HOH   P 5 .   ? 8.61463   5.61418   42.05510  1.000 42.40959 ?  535 HOH   B O   1 
HETATM 4133 O  O   . HOH   P 5 .   ? -17.81305 10.95221  10.29513  1.000 17.27273 ?  536 HOH   B O   1 
HETATM 4134 O  O   . HOH   P 5 .   ? -16.39554 13.03996  9.27863   1.000 25.39757 ?  537 HOH   B O   1 
HETATM 4135 O  O   . HOH   P 5 .   ? 9.67784   31.57051  17.07763  1.000 19.69839 ?  538 HOH   B O   1 
HETATM 4136 O  O   . HOH   P 5 .   ? 20.33544  22.76308  17.47620  1.000 35.44248 ?  539 HOH   B O   1 
HETATM 4137 O  O   . HOH   P 5 .   ? 18.05113  24.36887  14.09694  1.000 19.69845 ?  540 HOH   B O   1 
HETATM 4138 O  O   . HOH   P 5 .   ? 12.89590  35.83882  23.72921  1.000 16.61010 ?  541 HOH   B O   1 
HETATM 4139 O  O   . HOH   P 5 .   ? -9.03588  0.95092   28.51462  1.000 30.54662 ?  542 HOH   B O   1 
HETATM 4140 O  O   . HOH   P 5 .   ? 18.899    27.102    40.051    1.000 17.32421 ?  543 HOH   B O   1 
HETATM 4141 O  O   . HOH   P 5 .   ? 10.56705  36.42935  25.61940  1.000 20.17739 ?  544 HOH   B O   1 
HETATM 4142 O  O   . HOH   P 5 .   ? -13.13937 15.13202  30.86881  1.000 24.45190 ?  545 HOH   B O   1 
HETATM 4143 O  O   . HOH   P 5 .   ? 2.04330   24.99984  43.56465  1.000 27.35313 ?  546 HOH   B O   1 
HETATM 4144 O  O   . HOH   P 5 .   ? -11.49844 9.55337   16.18109  1.000 19.54961 ?  547 HOH   B O   1 
HETATM 4145 O  O   . HOH   P 5 .   ? -3.91366  29.00989  30.56090  1.000 52.97609 ?  548 HOH   B O   1 
HETATM 4146 O  O   . HOH   P 5 .   ? -6.02352  15.85275  6.93906   1.000 41.69033 ?  549 HOH   B O   1 
HETATM 4147 O  O   . HOH   P 5 .   ? 10.62373  3.48692   22.29855  1.000 24.98547 ?  550 HOH   B O   1 
HETATM 4148 O  O   . HOH   P 5 .   ? -11.49596 7.65633   11.20377  1.000 32.94673 ?  551 HOH   B O   1 
HETATM 4149 O  O   . HOH   P 5 .   ? 16.38276  15.65342  14.35216  1.000 37.34216 ?  552 HOH   B O   1 
HETATM 4150 O  O   . HOH   P 5 .   ? 16.82586  17.90251  37.89738  1.000 26.91093 ?  553 HOH   B O   1 
HETATM 4151 O  O   . HOH   P 5 .   ? -21.93504 21.13277  25.79182  0.50  41.48166 ?  554 HOH   B O   1 
HETATM 4152 O  O   . HOH   P 5 .   ? 4.09755   20.50884  39.06346  1.000 14.45996 ?  555 HOH   B O   1 
HETATM 4153 O  O   . HOH   P 5 .   ? -1.04816  34.36900  26.09983  1.000 15.58366 ?  556 HOH   B O   1 
HETATM 4154 O  O   . HOH   P 5 .   ? 1.61191   34.40960  22.20581  1.000 17.64137 ?  557 HOH   B O   1 
HETATM 4155 O  O   . HOH   P 5 .   ? 5.07722   6.48564   10.75737  1.000 37.83045 ?  558 HOH   B O   1 
HETATM 4156 O  O   . HOH   P 5 .   ? 19.78280  21.22519  23.68009  1.000 25.98376 ?  559 HOH   B O   1 
HETATM 4157 O  O   . HOH   P 5 .   ? 20.68860  24.40444  29.39963  1.000 20.47218 ?  560 HOH   B O   1 
HETATM 4158 O  O   . HOH   P 5 .   ? 7.52261   0.32893   23.18523  1.000 27.36355 ?  561 HOH   B O   1 
HETATM 4159 O  O   . HOH   P 5 .   ? 1.42139   39.23053  30.10665  1.000 24.91680 ?  562 HOH   B O   1 
HETATM 4160 O  O   . HOH   P 5 .   ? 1.69785   24.89837  32.44716  1.000 17.86831 ?  563 HOH   B O   1 
HETATM 4161 O  O   . HOH   P 5 .   ? -6.98123  19.36177  25.49081  1.000 15.57708 ?  564 HOH   B O   1 
HETATM 4162 O  O   . HOH   P 5 .   ? 1.30609   31.73160  41.73878  1.000 34.91665 ?  565 HOH   B O   1 
HETATM 4163 O  O   . HOH   P 5 .   ? 15.19282  8.08329   17.05104  1.000 24.13365 ?  566 HOH   B O   1 
HETATM 4164 O  O   . HOH   P 5 .   ? -15.12332 17.01857  31.41884  1.000 28.96690 ?  567 HOH   B O   1 
HETATM 4165 O  O   . HOH   P 5 .   ? 0.39324   7.32680   14.90156  1.000 19.10657 ?  568 HOH   B O   1 
HETATM 4166 O  O   . HOH   P 5 .   ? 4.47469   25.57539  9.01610   1.000 34.09607 ?  569 HOH   B O   1 
HETATM 4167 O  O   . HOH   P 5 .   ? 1.26903   24.48762  6.16428   1.000 37.39716 ?  570 HOH   B O   1 
HETATM 4168 O  O   . HOH   P 5 .   ? 22.341    24.677    35.381    1.000 36.32551 ?  571 HOH   B O   1 
HETATM 4169 O  O   . HOH   P 5 .   ? -8.94472  25.31338  12.53766  1.000 28.25360 ?  572 HOH   B O   1 
HETATM 4170 O  O   . HOH   P 5 .   ? 20.64435  16.66996  34.00222  1.000 48.17759 ?  573 HOH   B O   1 
HETATM 4171 O  O   . HOH   P 5 .   ? -9.54927  7.55529   16.20981  1.000 25.70282 ?  574 HOH   B O   1 
HETATM 4172 O  O   . HOH   P 5 .   ? 5.29650   3.11623   40.02532  1.000 31.20187 ?  575 HOH   B O   1 
HETATM 4173 O  O   . HOH   P 5 .   ? 9.61526   0.12644   30.40490  1.000 32.47705 ?  576 HOH   B O   1 
HETATM 4174 O  O   . HOH   P 5 .   ? -0.38061  24.51287  36.71602  1.000 40.17351 ?  577 HOH   B O   1 
HETATM 4175 O  O   . HOH   P 5 .   ? 6.43996   5.65921   12.91252  1.000 28.25179 ?  578 HOH   B O   1 
HETATM 4176 O  O   . HOH   P 5 .   ? 16.93793  34.70302  33.00763  1.000 31.42088 ?  579 HOH   B O   1 
HETATM 4177 O  O   . HOH   P 5 .   ? 9.66297   6.55020   14.12670  1.000 25.17479 ?  580 HOH   B O   1 
HETATM 4178 O  O   . HOH   P 5 .   ? 5.65535   33.52507  39.38338  1.000 25.88149 ?  581 HOH   B O   1 
HETATM 4179 O  O   . HOH   P 5 .   ? 6.39031   -0.83958  25.23799  1.000 19.04401 ?  582 HOH   B O   1 
HETATM 4180 O  O   . HOH   P 5 .   ? 12.32911  6.76773   32.15247  1.000 25.68030 ?  583 HOH   B O   1 
HETATM 4181 O  O   . HOH   P 5 .   ? 15.25228  31.35161  29.16785  1.000 28.87848 ?  584 HOH   B O   1 
HETATM 4182 O  O   . HOH   P 5 .   ? -0.26960  5.70284   6.91923   1.000 42.74480 ?  585 HOH   B O   1 
HETATM 4183 O  O   . HOH   P 5 .   ? 16.83420  17.42268  35.06620  1.000 25.46169 ?  586 HOH   B O   1 
HETATM 4184 O  O   . HOH   P 5 .   ? -7.08697  27.55360  12.13489  1.000 34.10664 ?  587 HOH   B O   1 
HETATM 4185 O  O   . HOH   P 5 .   ? 7.91667   5.09587   15.51302  1.000 31.14451 ?  588 HOH   B O   1 
HETATM 4186 O  O   . HOH   P 5 .   ? -14.80999 12.42904  32.66390  1.000 29.26230 ?  589 HOH   B O   1 
HETATM 4187 O  O   . HOH   P 5 .   ? -0.57692  8.03722   26.08733  1.000 13.56765 ?  590 HOH   B O   1 
HETATM 4188 O  O   . HOH   P 5 .   ? -9.07614  11.79715  34.91049  1.000 31.14813 ?  591 HOH   B O   1 
HETATM 4189 O  O   . HOH   P 5 .   ? 4.14768   35.08479  21.17449  1.000 28.28308 ?  592 HOH   B O   1 
HETATM 4190 O  O   . HOH   P 5 .   ? -4.51184  2.73228   33.15284  1.000 25.75390 ?  593 HOH   B O   1 
HETATM 4191 O  O   . HOH   P 5 .   ? 14.46502  36.87897  35.51880  1.000 32.58764 ?  594 HOH   B O   1 
HETATM 4192 O  O   . HOH   P 5 .   ? 9.13661   34.53448  19.21783  1.000 26.32703 ?  595 HOH   B O   1 
HETATM 4193 O  O   . HOH   P 5 .   ? -20.50219 19.64748  27.04002  1.000 38.13483 ?  596 HOH   B O   1 
HETATM 4194 O  O   . HOH   P 5 .   ? -6.59862  5.27295   7.41997   1.000 33.11028 ?  597 HOH   B O   1 
HETATM 4195 O  O   . HOH   P 5 .   ? -3.197    39.058    28.289    1.000 35.56645 ?  598 HOH   B O   1 
HETATM 4196 O  O   . HOH   P 5 .   ? 12.99672  37.39192  39.81221  1.000 26.84133 ?  599 HOH   B O   1 
HETATM 4197 O  O   . HOH   P 5 .   ? -18.67975 20.57830  20.19902  1.000 42.40373 ?  600 HOH   B O   1 
HETATM 4198 O  O   . HOH   P 5 .   ? 1.670     40.890    35.914    1.000 38.81681 ?  601 HOH   B O   1 
HETATM 4199 O  O   . HOH   P 5 .   ? 14.39636  4.46898   29.13496  1.000 22.65150 ?  602 HOH   B O   1 
HETATM 4200 O  O   . HOH   P 5 .   ? 10.39643  22.15677  7.45443   1.000 33.58746 ?  603 HOH   B O   1 
HETATM 4201 O  O   . HOH   P 5 .   ? -2.35439  14.34781  38.63637  1.000 16.00082 ?  604 HOH   B O   1 
HETATM 4202 O  O   . HOH   P 5 .   ? 10.09917  13.42839  12.76106  1.000 17.63174 ?  605 HOH   B O   1 
HETATM 4203 O  O   . HOH   P 5 .   ? -16.97105 18.58077  21.24431  1.000 30.64744 ?  606 HOH   B O   1 
HETATM 4204 O  O   . HOH   P 5 .   ? 4.37129   33.14927  41.10363  1.000 32.61248 ?  607 HOH   B O   1 
HETATM 4205 O  O   . HOH   P 5 .   ? 3.81511   1.72401   35.67613  1.000 28.37292 ?  608 HOH   B O   1 
HETATM 4206 O  O   . HOH   P 5 .   ? 10.70831  -1.56813  26.53871  1.000 31.45157 ?  609 HOH   B O   1 
HETATM 4207 O  O   . HOH   P 5 .   ? 6.15339   -1.85958  33.28300  1.000 46.14278 ?  610 HOH   B O   1 
HETATM 4208 O  O   . HOH   P 5 .   ? -14.01539 29.36878  20.20950  1.000 45.63408 ?  611 HOH   B O   1 
HETATM 4209 O  O   . HOH   P 5 .   ? -11.81972 11.38136  34.00817  1.000 40.34466 ?  612 HOH   B O   1 
HETATM 4210 O  O   . HOH   P 5 .   ? 12.25877  11.76245  33.36033  1.000 26.17494 ?  613 HOH   B O   1 
HETATM 4211 O  O   . HOH   P 5 .   ? 1.56611   5.65665   9.00093   1.000 39.28901 ?  614 HOH   B O   1 
HETATM 4212 O  O   . HOH   P 5 .   ? 19.79536  29.02795  19.95994  1.000 25.12741 ?  615 HOH   B O   1 
HETATM 4213 O  O   . HOH   P 5 .   ? 23.974    10.743    29.768    1.000 47.40196 ?  616 HOH   B O   1 
HETATM 4214 O  O   . HOH   P 5 .   ? -7.04462  5.59824   37.48864  1.000 34.90332 ?  617 HOH   B O   1 
HETATM 4215 O  O   . HOH   P 5 .   ? 10.030    38.565    27.175    1.000 20.96828 ?  618 HOH   B O   1 
HETATM 4216 O  O   . HOH   P 5 .   ? 20.90939  7.42899   29.32416  1.000 24.77990 ?  619 HOH   B O   1 
HETATM 4217 O  O   . HOH   P 5 .   ? 23.03183  9.18818   28.93742  1.000 35.63284 ?  620 HOH   B O   1 
HETATM 4218 O  O   . HOH   P 5 .   ? -14.24908 2.53455   22.37374  1.000 36.89926 ?  621 HOH   B O   1 
HETATM 4219 O  O   . HOH   P 5 .   ? 6.76631   28.04842  50.08097  1.000 43.30920 ?  622 HOH   B O   1 
HETATM 4220 O  O   . HOH   P 5 .   ? -9.65459  22.57983  12.55125  1.000 37.38434 ?  623 HOH   B O   1 
HETATM 4221 O  O   . HOH   P 5 .   ? -4.16573  17.03323  6.47651   1.000 31.50211 ?  624 HOH   B O   1 
HETATM 4222 O  O   . HOH   P 5 .   ? 6.85499   9.87906   9.79834   1.000 26.82224 ?  625 HOH   B O   1 
HETATM 4223 O  O   . HOH   P 5 .   ? 6.47328   35.81069  18.44959  1.000 41.45437 ?  626 HOH   B O   1 
HETATM 4224 O  O   . HOH   P 5 .   ? 2.47636   16.25865  9.55087   1.000 33.02494 ?  627 HOH   B O   1 
HETATM 4225 O  O   . HOH   P 5 .   ? -5.964    10.334    2.273     1.000 43.73659 ?  628 HOH   B O   1 
HETATM 4226 O  O   . HOH   P 5 .   ? 17.79511  21.81063  14.13343  1.000 38.53691 ?  629 HOH   B O   1 
HETATM 4227 O  O   . HOH   P 5 .   ? 3.61308   32.18943  15.76433  1.000 39.17220 ?  630 HOH   B O   1 
HETATM 4228 O  O   . HOH   P 5 .   ? -19.12002 17.57911  22.98163  1.000 39.82529 ?  631 HOH   B O   1 
HETATM 4229 O  O   . HOH   P 5 .   ? 3.93186   23.11153  7.00259   1.000 35.67657 ?  632 HOH   B O   1 
HETATM 4230 O  O   . HOH   P 5 .   ? -1.08685  37.00959  25.00364  1.000 21.94518 ?  633 HOH   B O   1 
HETATM 4231 O  O   . HOH   P 5 .   ? -16.19194 8.62381   28.08899  1.000 34.80618 ?  634 HOH   B O   1 
HETATM 4232 O  O   . HOH   P 5 .   ? -9.65318  -1.05648  26.58374  1.000 26.06203 ?  635 HOH   B O   1 
HETATM 4233 O  O   . HOH   P 5 .   ? 10.77216  18.02571  7.93398   1.000 31.65222 ?  636 HOH   B O   1 
HETATM 4234 O  O   . HOH   P 5 .   ? 14.15037  20.12604  11.59009  1.000 38.44325 ?  637 HOH   B O   1 
HETATM 4235 O  O   . HOH   P 5 .   ? 12.86309  24.17292  9.51602   1.000 33.54495 ?  638 HOH   B O   1 
HETATM 4236 O  O   . HOH   P 5 .   ? 22.65187  22.40190  29.56452  1.000 38.30031 ?  639 HOH   B O   1 
HETATM 4237 O  O   . HOH   P 5 .   ? -18.41568 12.27755  23.04001  1.000 29.04142 ?  640 HOH   B O   1 
HETATM 4238 O  O   . HOH   P 5 .   ? 17.484    3.370     26.049    1.000 46.94446 ?  641 HOH   B O   1 
HETATM 4239 O  O   . HOH   P 5 .   ? 11.07745  37.75522  49.47463  1.000 34.86345 ?  642 HOH   B O   1 
HETATM 4240 O  O   . HOH   P 5 .   ? 5.05973   34.31700  16.67967  1.000 44.92822 ?  643 HOH   B O   1 
HETATM 4241 O  O   . HOH   P 5 .   ? 3.48914   23.31706  45.77169  1.000 34.56703 ?  644 HOH   B O   1 
HETATM 4242 O  O   . HOH   P 5 .   ? -14.421   20.030    8.971     1.000 36.90710 ?  645 HOH   B O   1 
HETATM 4243 O  O   . HOH   P 5 .   ? 12.28673  8.13462   30.35905  1.000 23.48618 ?  646 HOH   B O   1 
HETATM 4244 O  O   . HOH   P 5 .   ? -1.17463  15.36251  40.58326  1.000 38.35670 ?  647 HOH   B O   1 
HETATM 4245 O  O   . HOH   P 5 .   ? -14.01229 6.54834   14.35236  1.000 35.61378 ?  648 HOH   B O   1 
HETATM 4246 O  O   . HOH   P 5 .   ? -9.586    7.373     6.300     1.000 31.71354 ?  649 HOH   B O   1 
HETATM 4247 O  O   . HOH   P 5 .   ? -15.73981 8.81046   18.01442  1.000 26.72020 ?  650 HOH   B O   1 
HETATM 4248 O  O   . HOH   P 5 .   ? 8.89956   36.70396  50.70685  1.000 31.94104 ?  651 HOH   B O   1 
HETATM 4249 O  O   . HOH   P 5 .   ? 21.53103  24.32394  26.79677  1.000 29.17742 ?  652 HOH   B O   1 
HETATM 4250 O  O   . HOH   P 5 .   ? 6.16134   36.15673  43.64356  1.000 47.67630 ?  653 HOH   B O   1 
HETATM 4251 O  O   . HOH   P 5 .   ? 6.02012   26.40949  49.76965  1.000 45.42622 ?  654 HOH   B O   1 
HETATM 4252 O  O   . HOH   P 5 .   ? -18.50649 12.74364  12.24848  1.000 22.49916 ?  655 HOH   B O   1 
HETATM 4253 O  O   . HOH   P 5 .   ? 6.13664   1.24102   35.93766  1.000 29.80740 ?  656 HOH   B O   1 
HETATM 4254 O  O   . HOH   P 5 .   ? -0.63863  40.02140  31.27399  1.000 43.44715 ?  657 HOH   B O   1 
HETATM 4255 O  O   . HOH   P 5 .   ? -13.36694 7.89225   16.68590  1.000 26.52104 ?  658 HOH   B O   1 
HETATM 4256 O  O   . HOH   P 5 .   ? 12.45072  20.17293  7.51813   1.000 41.17315 ?  659 HOH   B O   1 
HETATM 4257 O  O   . HOH   P 5 .   ? 7.37679   12.58006  8.33074   1.000 28.41423 ?  660 HOH   B O   1 
HETATM 4258 O  O   . HOH   P 5 .   ? 5.47276   35.32912  41.18784  1.000 39.45422 ?  661 HOH   B O   1 
HETATM 4259 O  O   . HOH   P 5 .   ? -18.57082 10.21926  21.83673  1.000 33.91027 ?  662 HOH   B O   1 
HETATM 4260 O  O   . HOH   P 5 .   ? 5.50093   3.16502   12.51945  1.000 45.50733 ?  663 HOH   B O   1 
HETATM 4261 O  O   . HOH   P 5 .   ? -11.67695 6.44767   13.81313  1.000 39.56919 ?  664 HOH   B O   1 
HETATM 4262 O  O   . HOH   P 5 .   ? 2.000     -3.794    37.347    1.000 40.61698 ?  665 HOH   B O   1 
HETATM 4263 O  O   . HOH   P 5 .   ? 19.791    32.342    20.159    1.000 35.91844 ?  666 HOH   B O   1 
HETATM 4264 O  O   . HOH   P 5 .   ? 17.21016  17.03830  42.00163  1.000 35.13289 ?  667 HOH   B O   1 
HETATM 4265 O  O   . HOH   P 5 .   ? 7.62068   13.79735  40.91151  1.000 22.02312 ?  668 HOH   B O   1 
HETATM 4266 O  O   . HOH   P 5 .   ? -14.32293 4.07211   25.90789  1.000 39.07312 ?  669 HOH   B O   1 
HETATM 4267 O  O   . HOH   P 5 .   ? 18.00251  17.54128  15.25611  1.000 30.59231 ?  670 HOH   B O   1 
HETATM 4268 O  O   . HOH   P 5 .   ? -6.789    4.520     4.466     1.000 37.20115 ?  671 HOH   B O   1 
HETATM 4269 O  O   . HOH   P 5 .   ? 15.47805  39.18420  35.50169  1.000 37.02339 ?  672 HOH   B O   1 
HETATM 4270 O  O   . HOH   P 5 .   ? 5.71694   15.45491  5.92243   1.000 47.78580 ?  673 HOH   B O   1 
HETATM 4271 O  O   . HOH   P 5 .   ? -7.363    6.511     4.378     1.000 45.05423 ?  674 HOH   B O   1 
HETATM 4272 O  O   . HOH   P 5 .   ? 18.702    28.814    36.427    1.000 15.68858 ?  675 HOH   B O   1 
HETATM 4273 O  O   . HOH   P 5 .   ? 12.70179  13.69005  13.49507  1.000 25.48948 ?  676 HOH   B O   1 
HETATM 4274 O  O   . HOH   P 5 .   ? -16.687   20.249    9.796     1.000 46.27998 ?  677 HOH   B O   1 
HETATM 4275 O  O   . HOH   P 5 .   ? 13.89014  18.37633  13.69944  1.000 34.44169 ?  678 HOH   B O   1 
HETATM 4276 O  O   . HOH   P 5 .   ? 5.31898   12.31613  42.11929  1.000 27.65415 ?  679 HOH   B O   1 
HETATM 4277 O  O   . HOH   P 5 .   ? 16.01330  11.12311  14.72301  1.000 40.78678 ?  680 HOH   B O   1 
HETATM 4278 O  O   . HOH   P 5 .   ? 20.667    28.061    38.226    1.000 15.75342 ?  681 HOH   B O   1 
HETATM 4279 O  O   . HOH   P 5 .   ? -8.680    13.047    4.403     1.000 27.38193 ?  682 HOH   B O   1 
HETATM 4280 O  O   . HOH   P 5 .   ? 6.757     -2.843    29.124    1.000 23.17751 ?  683 HOH   B O   1 
HETATM 4281 O  O   . HOH   P 5 .   ? 5.17534   14.23272  7.92570   1.000 34.37430 ?  684 HOH   B O   1 
HETATM 4282 O  O   . HOH   P 5 .   ? -3.72323  0.45131   33.48033  1.000 38.94063 ?  685 HOH   B O   1 
HETATM 4283 O  O   . HOH   P 5 .   ? 4.545     40.651    35.915    1.000 27.64758 ?  686 HOH   B O   1 
HETATM 4284 O  O   . HOH   P 5 .   ? -12.31827 5.82683   31.43203  1.000 29.43331 ?  687 HOH   B O   1 
HETATM 4285 O  O   . HOH   P 5 .   ? -18.98385 14.72931  21.88191  1.000 33.65437 ?  688 HOH   B O   1 
HETATM 4286 O  O   . HOH   P 5 .   ? -19.205   19.395    10.287    1.000 42.46145 ?  689 HOH   B O   1 
HETATM 4287 O  O   . HOH   P 5 .   ? 20.50591  19.38409  25.27649  1.000 23.34561 ?  690 HOH   B O   1 
HETATM 4288 O  O   . HOH   P 5 .   ? 8.71370   14.69682  8.91701   1.000 27.66523 ?  691 HOH   B O   1 
HETATM 4289 O  O   . HOH   P 5 .   ? 14.47412  32.87831  18.33083  1.000 27.48930 ?  692 HOH   B O   1 
HETATM 4290 O  O   . HOH   P 5 .   ? -7.14446  30.90881  26.66635  1.000 23.88048 ?  693 HOH   B O   1 
HETATM 4291 O  O   . HOH   P 5 .   ? 11.89230  33.22161  17.06140  1.000 29.60692 ?  694 HOH   B O   1 
HETATM 4292 O  O   . HOH   P 5 .   ? 3.02828   2.81504   12.40560  1.000 39.79960 ?  695 HOH   B O   1 
HETATM 4293 O  O   . HOH   P 5 .   ? 2.83825   26.98347  8.49215   1.000 42.44998 ?  696 HOH   B O   1 
HETATM 4294 O  O   . HOH   P 5 .   ? 23.739    23.882    32.889    1.000 42.82657 ?  697 HOH   B O   1 
HETATM 4295 O  O   . HOH   P 5 .   ? -12.96507 27.61981  17.37199  1.000 34.10100 ?  698 HOH   B O   1 
HETATM 4296 O  O   . HOH   P 5 .   ? -13.06361 5.93191   18.71093  1.000 37.38501 ?  699 HOH   B O   1 
HETATM 4297 O  O   . HOH   P 5 .   ? -0.16172  18.28386  44.09182  1.000 35.48921 ?  700 HOH   B O   1 
HETATM 4298 O  O   . HOH   P 5 .   ? -12.74949 -1.78506  26.20459  1.000 40.21655 ?  701 HOH   B O   1 
HETATM 4299 O  O   . HOH   P 5 .   ? -14.70940 7.04271   22.74255  1.000 35.59781 ?  702 HOH   B O   1 
HETATM 4300 O  O   . HOH   P 5 .   ? 12.05703  1.42078   21.41219  1.000 44.63385 ?  703 HOH   B O   1 
HETATM 4301 O  O   . HOH   P 5 .   ? -7.08343  33.72085  26.29629  1.000 35.88625 ?  704 HOH   B O   1 
HETATM 4302 O  O   . HOH   P 5 .   ? -7.64452  17.22552  6.94048   1.000 34.77317 ?  705 HOH   B O   1 
HETATM 4303 O  O   . HOH   P 5 .   ? 5.55403   10.38277  42.92030  1.000 39.37415 ?  706 HOH   B O   1 
HETATM 4304 O  O   . HOH   P 5 .   ? -7.966    9.255     3.330     1.000 47.52002 ?  707 HOH   B O   1 
HETATM 4305 O  O   . HOH   P 5 .   ? 2.51195   20.04877  47.41892  1.000 44.11217 ?  708 HOH   B O   1 
HETATM 4306 O  O   . HOH   P 5 .   ? 3.26214   32.99684  12.81647  1.000 43.35879 ?  709 HOH   B O   1 
HETATM 4307 O  O   . HOH   P 5 .   ? 6.56083   37.21202  46.44028  1.000 30.25357 ?  710 HOH   B O   1 
HETATM 4308 O  O   . HOH   P 5 .   ? 0.53195   30.94669  9.92966   1.000 43.42261 ?  711 HOH   B O   1 
HETATM 4309 O  O   . HOH   P 5 .   ? -17.13317 13.88535  33.24423  1.000 44.90203 ?  712 HOH   B O   1 
HETATM 4310 O  O   . HOH   P 5 .   ? 7.24729   2.95084   41.78311  1.000 36.88028 ?  713 HOH   B O   1 
HETATM 4311 O  O   . HOH   P 5 .   ? 16.66266  33.57860  29.90424  1.000 37.49943 ?  714 HOH   B O   1 
HETATM 4312 O  O   . HOH   P 5 .   ? 7.26924   -1.99814  35.93675  1.000 44.78783 ?  715 HOH   B O   1 
HETATM 4313 O  O   . HOH   P 5 .   ? -16.12828 6.12023   27.17347  1.000 39.94533 ?  716 HOH   B O   1 
HETATM 4314 O  O   . HOH   P 5 .   ? -19.28534 8.77115   23.61984  1.000 42.52575 ?  717 HOH   B O   1 
HETATM 4315 O  O   . HOH   P 5 .   ? -16.779   21.027    7.845     1.000 49.55501 ?  718 HOH   B O   1 
HETATM 4316 O  O   . HOH   P 5 .   ? 5.22463   37.84722  44.86516  1.000 43.08013 ?  719 HOH   B O   1 
HETATM 4317 O  O   . HOH   P 5 .   ? -17.38012 6.90519   24.84321  1.000 37.35385 ?  720 HOH   B O   1 
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