data_9F0P
# 
_entry.id   9F0P 
# 
_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   9F0P         pdb_00009f0p 10.2210/pdb9f0p/pdb 
WWPDB D_1292137930 ?            ?                   
# 
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                        9F0P 
_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 
'Bartels, K.'  1 0000-0002-7980-1913 
'Prester, A.'  2 0000-0002-9939-602X 
'Bosman, R.'   3 0000-0003-2738-7682 
'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 '[(S)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' 363.325   2   ?       ? ? ? 
4 non-polymer nat 'ZINC ION'                                                                         65.409    6   ?       ? ? ? 
5 non-polymer syn '[(R)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' 363.325   1   ?       ? ? ? 
6 water       nat water                                                                              18.015    536 ?       ? ? ? 
# 
_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 '[(S)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' A1IKA 
4 'ZINC ION'                                                                         ZN    
5 '[(R)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' A1H8T 
6 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 
A1H8T non-polymer         . '[(R)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' 
'((Benzo[b]thiophene-2-carboxamido)(2-hydroxyphenyl)methyl)phosphonic acid' 'C16 H14 N O5 P S' 363.325 
A1IKA non-polymer         . '[(S)-(1-benzothiophen-2-ylcarbonylamino)-(2-hydroxyphenyl)methyl]phosphonic acid' 
'((Benzo[b]thiophene-2-carboxamido)(2-hydroxyphenyl)methyl)phosphonic acid' 'C16 H14 N O5 P S' 363.325 
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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1IKA ? ? A1IKA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1IKA ? ? A1IKA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 A1IKA 1   303 303 A1IKA LIS 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 2 FMT   1   301 302 FMT   FMT B . 
J 2 FMT   1   302 303 FMT   FMT B . 
K 3 A1IKA 1   303 304 A1IKA LIS B . 
L 5 A1H8T 1   304 305 A1H8T LIR B . 
M 4 ZN    1   305 3   ZN    ZN  B . 
N 4 ZN    1   306 4   ZN    ZN  B . 
O 4 ZN    1   307 5   ZN    ZN  B . 
P 6 HOH   1   401 335 HOH   HOH A . 
P 6 HOH   2   402 366 HOH   HOH A . 
P 6 HOH   3   403 172 HOH   HOH A . 
P 6 HOH   4   404 425 HOH   HOH A . 
P 6 HOH   5   405 109 HOH   HOH A . 
P 6 HOH   6   406 384 HOH   HOH A . 
P 6 HOH   7   407 131 HOH   HOH A . 
P 6 HOH   8   408 507 HOH   HOH A . 
P 6 HOH   9   409 76  HOH   HOH A . 
P 6 HOH   10  410 356 HOH   HOH A . 
P 6 HOH   11  411 398 HOH   HOH A . 
P 6 HOH   12  412 144 HOH   HOH A . 
P 6 HOH   13  413 102 HOH   HOH A . 
P 6 HOH   14  414 340 HOH   HOH A . 
P 6 HOH   15  415 170 HOH   HOH A . 
P 6 HOH   16  416 49  HOH   HOH A . 
P 6 HOH   17  417 389 HOH   HOH A . 
P 6 HOH   18  418 525 HOH   HOH A . 
P 6 HOH   19  419 163 HOH   HOH A . 
P 6 HOH   20  420 275 HOH   HOH A . 
P 6 HOH   21  421 269 HOH   HOH A . 
P 6 HOH   22  422 27  HOH   HOH A . 
P 6 HOH   23  423 89  HOH   HOH A . 
P 6 HOH   24  424 126 HOH   HOH A . 
P 6 HOH   25  425 521 HOH   HOH A . 
P 6 HOH   26  426 43  HOH   HOH A . 
P 6 HOH   27  427 91  HOH   HOH A . 
P 6 HOH   28  428 115 HOH   HOH A . 
P 6 HOH   29  429 336 HOH   HOH A . 
P 6 HOH   30  430 83  HOH   HOH A . 
P 6 HOH   31  431 414 HOH   HOH A . 
P 6 HOH   32  432 7   HOH   HOH A . 
P 6 HOH   33  433 347 HOH   HOH A . 
P 6 HOH   34  434 28  HOH   HOH A . 
P 6 HOH   35  435 234 HOH   HOH A . 
P 6 HOH   36  436 360 HOH   HOH A . 
P 6 HOH   37  437 538 HOH   HOH A . 
P 6 HOH   38  438 257 HOH   HOH A . 
P 6 HOH   39  439 96  HOH   HOH A . 
P 6 HOH   40  440 166 HOH   HOH A . 
P 6 HOH   41  441 494 HOH   HOH A . 
P 6 HOH   42  442 429 HOH   HOH A . 
P 6 HOH   43  443 5   HOH   HOH A . 
P 6 HOH   44  444 77  HOH   HOH A . 
P 6 HOH   45  445 471 HOH   HOH A . 
P 6 HOH   46  446 145 HOH   HOH A . 
P 6 HOH   47  447 259 HOH   HOH A . 
P 6 HOH   48  448 206 HOH   HOH A . 
P 6 HOH   49  449 19  HOH   HOH A . 
P 6 HOH   50  450 50  HOH   HOH A . 
P 6 HOH   51  451 386 HOH   HOH A . 
P 6 HOH   52  452 315 HOH   HOH A . 
P 6 HOH   53  453 105 HOH   HOH A . 
P 6 HOH   54  454 165 HOH   HOH A . 
P 6 HOH   55  455 98  HOH   HOH A . 
P 6 HOH   56  456 162 HOH   HOH A . 
P 6 HOH   57  457 424 HOH   HOH A . 
P 6 HOH   58  458 31  HOH   HOH A . 
P 6 HOH   59  459 194 HOH   HOH A . 
P 6 HOH   60  460 349 HOH   HOH A . 
P 6 HOH   61  461 3   HOH   HOH A . 
P 6 HOH   62  462 338 HOH   HOH A . 
P 6 HOH   63  463 14  HOH   HOH A . 
P 6 HOH   64  464 451 HOH   HOH A . 
P 6 HOH   65  465 66  HOH   HOH A . 
P 6 HOH   66  466 17  HOH   HOH A . 
P 6 HOH   67  467 401 HOH   HOH A . 
P 6 HOH   68  468 285 HOH   HOH A . 
P 6 HOH   69  469 82  HOH   HOH A . 
P 6 HOH   70  470 242 HOH   HOH A . 
P 6 HOH   71  471 283 HOH   HOH A . 
P 6 HOH   72  472 262 HOH   HOH A . 
P 6 HOH   73  473 199 HOH   HOH A . 
P 6 HOH   74  474 342 HOH   HOH A . 
P 6 HOH   75  475 355 HOH   HOH A . 
P 6 HOH   76  476 104 HOH   HOH A . 
P 6 HOH   77  477 255 HOH   HOH A . 
P 6 HOH   78  478 440 HOH   HOH A . 
P 6 HOH   79  479 16  HOH   HOH A . 
P 6 HOH   80  480 140 HOH   HOH A . 
P 6 HOH   81  481 111 HOH   HOH A . 
P 6 HOH   82  482 252 HOH   HOH A . 
P 6 HOH   83  483 106 HOH   HOH A . 
P 6 HOH   84  484 22  HOH   HOH A . 
P 6 HOH   85  485 188 HOH   HOH A . 
P 6 HOH   86  486 142 HOH   HOH A . 
P 6 HOH   87  487 409 HOH   HOH A . 
P 6 HOH   88  488 116 HOH   HOH A . 
P 6 HOH   89  489 541 HOH   HOH A . 
P 6 HOH   90  490 513 HOH   HOH A . 
P 6 HOH   91  491 460 HOH   HOH A . 
P 6 HOH   92  492 258 HOH   HOH A . 
P 6 HOH   93  493 34  HOH   HOH A . 
P 6 HOH   94  494 317 HOH   HOH A . 
P 6 HOH   95  495 318 HOH   HOH A . 
P 6 HOH   96  496 192 HOH   HOH A . 
P 6 HOH   97  497 152 HOH   HOH A . 
P 6 HOH   98  498 65  HOH   HOH A . 
P 6 HOH   99  499 113 HOH   HOH A . 
P 6 HOH   100 500 79  HOH   HOH A . 
P 6 HOH   101 501 528 HOH   HOH A . 
P 6 HOH   102 502 26  HOH   HOH A . 
P 6 HOH   103 503 161 HOH   HOH A . 
P 6 HOH   104 504 21  HOH   HOH A . 
P 6 HOH   105 505 195 HOH   HOH A . 
P 6 HOH   106 506 233 HOH   HOH A . 
P 6 HOH   107 507 117 HOH   HOH A . 
P 6 HOH   108 508 254 HOH   HOH A . 
P 6 HOH   109 509 205 HOH   HOH A . 
P 6 HOH   110 510 41  HOH   HOH A . 
P 6 HOH   111 511 244 HOH   HOH A . 
P 6 HOH   112 512 367 HOH   HOH A . 
P 6 HOH   113 513 418 HOH   HOH A . 
P 6 HOH   114 514 18  HOH   HOH A . 
P 6 HOH   115 515 92  HOH   HOH A . 
P 6 HOH   116 516 441 HOH   HOH A . 
P 6 HOH   117 517 319 HOH   HOH A . 
P 6 HOH   118 518 94  HOH   HOH A . 
P 6 HOH   119 519 133 HOH   HOH A . 
P 6 HOH   120 520 481 HOH   HOH A . 
P 6 HOH   121 521 72  HOH   HOH A . 
P 6 HOH   122 522 453 HOH   HOH A . 
P 6 HOH   123 523 232 HOH   HOH A . 
P 6 HOH   124 524 118 HOH   HOH A . 
P 6 HOH   125 525 324 HOH   HOH A . 
P 6 HOH   126 526 218 HOH   HOH A . 
P 6 HOH   127 527 276 HOH   HOH A . 
P 6 HOH   128 528 52  HOH   HOH A . 
P 6 HOH   129 529 48  HOH   HOH A . 
P 6 HOH   130 530 500 HOH   HOH A . 
P 6 HOH   131 531 381 HOH   HOH A . 
P 6 HOH   132 532 29  HOH   HOH A . 
P 6 HOH   133 533 62  HOH   HOH A . 
P 6 HOH   134 534 197 HOH   HOH A . 
P 6 HOH   135 535 20  HOH   HOH A . 
P 6 HOH   136 536 530 HOH   HOH A . 
P 6 HOH   137 537 213 HOH   HOH A . 
P 6 HOH   138 538 501 HOH   HOH A . 
P 6 HOH   139 539 73  HOH   HOH A . 
P 6 HOH   140 540 373 HOH   HOH A . 
P 6 HOH   141 541 45  HOH   HOH A . 
P 6 HOH   142 542 44  HOH   HOH A . 
P 6 HOH   143 543 305 HOH   HOH A . 
P 6 HOH   144 544 137 HOH   HOH A . 
P 6 HOH   145 545 87  HOH   HOH A . 
P 6 HOH   146 546 326 HOH   HOH A . 
P 6 HOH   147 547 150 HOH   HOH A . 
P 6 HOH   148 548 146 HOH   HOH A . 
P 6 HOH   149 549 419 HOH   HOH A . 
P 6 HOH   150 550 470 HOH   HOH A . 
P 6 HOH   151 551 201 HOH   HOH A . 
P 6 HOH   152 552 402 HOH   HOH A . 
P 6 HOH   153 553 312 HOH   HOH A . 
P 6 HOH   154 554 491 HOH   HOH A . 
P 6 HOH   155 555 449 HOH   HOH A . 
P 6 HOH   156 556 191 HOH   HOH A . 
P 6 HOH   157 557 158 HOH   HOH A . 
P 6 HOH   158 558 58  HOH   HOH A . 
P 6 HOH   159 559 531 HOH   HOH A . 
P 6 HOH   160 560 132 HOH   HOH A . 
P 6 HOH   161 561 267 HOH   HOH A . 
P 6 HOH   162 562 380 HOH   HOH A . 
P 6 HOH   163 563 209 HOH   HOH A . 
P 6 HOH   164 564 160 HOH   HOH A . 
P 6 HOH   165 565 6   HOH   HOH A . 
P 6 HOH   166 566 433 HOH   HOH A . 
P 6 HOH   167 567 459 HOH   HOH A . 
P 6 HOH   168 568 524 HOH   HOH A . 
P 6 HOH   169 569 332 HOH   HOH A . 
P 6 HOH   170 570 479 HOH   HOH A . 
P 6 HOH   171 571 486 HOH   HOH A . 
P 6 HOH   172 572 130 HOH   HOH A . 
P 6 HOH   173 573 287 HOH   HOH A . 
P 6 HOH   174 574 369 HOH   HOH A . 
P 6 HOH   175 575 231 HOH   HOH A . 
P 6 HOH   176 576 40  HOH   HOH A . 
P 6 HOH   177 577 427 HOH   HOH A . 
P 6 HOH   178 578 123 HOH   HOH A . 
P 6 HOH   179 579 458 HOH   HOH A . 
P 6 HOH   180 580 477 HOH   HOH A . 
P 6 HOH   181 581 468 HOH   HOH A . 
P 6 HOH   182 582 110 HOH   HOH A . 
P 6 HOH   183 583 135 HOH   HOH A . 
P 6 HOH   184 584 229 HOH   HOH A . 
P 6 HOH   185 585 298 HOH   HOH A . 
P 6 HOH   186 586 379 HOH   HOH A . 
P 6 HOH   187 587 331 HOH   HOH A . 
P 6 HOH   188 588 436 HOH   HOH A . 
P 6 HOH   189 589 430 HOH   HOH A . 
P 6 HOH   190 590 534 HOH   HOH A . 
P 6 HOH   191 591 228 HOH   HOH A . 
P 6 HOH   192 592 320 HOH   HOH A . 
P 6 HOH   193 593 442 HOH   HOH A . 
P 6 HOH   194 594 415 HOH   HOH A . 
P 6 HOH   195 595 493 HOH   HOH A . 
P 6 HOH   196 596 372 HOH   HOH A . 
P 6 HOH   197 597 387 HOH   HOH A . 
P 6 HOH   198 598 365 HOH   HOH A . 
P 6 HOH   199 599 281 HOH   HOH A . 
P 6 HOH   200 600 74  HOH   HOH A . 
P 6 HOH   201 601 321 HOH   HOH A . 
P 6 HOH   202 602 328 HOH   HOH A . 
P 6 HOH   203 603 526 HOH   HOH A . 
P 6 HOH   204 604 61  HOH   HOH A . 
P 6 HOH   205 605 296 HOH   HOH A . 
P 6 HOH   206 606 469 HOH   HOH A . 
P 6 HOH   207 607 171 HOH   HOH A . 
P 6 HOH   208 608 456 HOH   HOH A . 
P 6 HOH   209 609 352 HOH   HOH A . 
P 6 HOH   210 610 181 HOH   HOH A . 
P 6 HOH   211 611 362 HOH   HOH A . 
P 6 HOH   212 612 297 HOH   HOH A . 
P 6 HOH   213 613 288 HOH   HOH A . 
P 6 HOH   214 614 532 HOH   HOH A . 
P 6 HOH   215 615 280 HOH   HOH A . 
P 6 HOH   216 616 423 HOH   HOH A . 
P 6 HOH   217 617 292 HOH   HOH A . 
P 6 HOH   218 618 183 HOH   HOH A . 
P 6 HOH   219 619 337 HOH   HOH A . 
P 6 HOH   220 620 302 HOH   HOH A . 
P 6 HOH   221 621 310 HOH   HOH A . 
P 6 HOH   222 622 508 HOH   HOH A . 
P 6 HOH   223 623 190 HOH   HOH A . 
P 6 HOH   224 624 212 HOH   HOH A . 
P 6 HOH   225 625 325 HOH   HOH A . 
P 6 HOH   226 626 472 HOH   HOH A . 
P 6 HOH   227 627 431 HOH   HOH A . 
P 6 HOH   228 628 385 HOH   HOH A . 
P 6 HOH   229 629 64  HOH   HOH A . 
P 6 HOH   230 630 282 HOH   HOH A . 
P 6 HOH   231 631 519 HOH   HOH A . 
P 6 HOH   232 632 382 HOH   HOH A . 
P 6 HOH   233 633 391 HOH   HOH A . 
P 6 HOH   234 634 510 HOH   HOH A . 
P 6 HOH   235 635 241 HOH   HOH A . 
P 6 HOH   236 636 512 HOH   HOH A . 
P 6 HOH   237 637 539 HOH   HOH A . 
P 6 HOH   238 638 371 HOH   HOH A . 
P 6 HOH   239 639 341 HOH   HOH A . 
P 6 HOH   240 640 323 HOH   HOH A . 
P 6 HOH   241 641 235 HOH   HOH A . 
P 6 HOH   242 642 448 HOH   HOH A . 
P 6 HOH   243 643 497 HOH   HOH A . 
P 6 HOH   244 644 445 HOH   HOH A . 
P 6 HOH   245 645 272 HOH   HOH A . 
P 6 HOH   246 646 249 HOH   HOH A . 
P 6 HOH   247 647 487 HOH   HOH A . 
P 6 HOH   248 648 527 HOH   HOH A . 
P 6 HOH   249 649 522 HOH   HOH A . 
P 6 HOH   250 650 277 HOH   HOH A . 
P 6 HOH   251 651 374 HOH   HOH A . 
Q 6 HOH   1   401 492 HOH   HOH B . 
Q 6 HOH   2   402 327 HOH   HOH B . 
Q 6 HOH   3   403 107 HOH   HOH B . 
Q 6 HOH   4   404 119 HOH   HOH B . 
Q 6 HOH   5   405 411 HOH   HOH B . 
Q 6 HOH   6   406 404 HOH   HOH B . 
Q 6 HOH   7   407 243 HOH   HOH B . 
Q 6 HOH   8   408 284 HOH   HOH B . 
Q 6 HOH   9   409 167 HOH   HOH B . 
Q 6 HOH   10  410 120 HOH   HOH B . 
Q 6 HOH   11  411 370 HOH   HOH B . 
Q 6 HOH   12  412 304 HOH   HOH B . 
Q 6 HOH   13  413 204 HOH   HOH B . 
Q 6 HOH   14  414 278 HOH   HOH B . 
Q 6 HOH   15  415 413 HOH   HOH B . 
Q 6 HOH   16  416 198 HOH   HOH B . 
Q 6 HOH   17  417 452 HOH   HOH B . 
Q 6 HOH   18  418 503 HOH   HOH B . 
Q 6 HOH   19  419 222 HOH   HOH B . 
Q 6 HOH   20  420 216 HOH   HOH B . 
Q 6 HOH   21  421 357 HOH   HOH B . 
Q 6 HOH   22  422 230 HOH   HOH B . 
Q 6 HOH   23  423 363 HOH   HOH B . 
Q 6 HOH   24  424 71  HOH   HOH B . 
Q 6 HOH   25  425 265 HOH   HOH B . 
Q 6 HOH   26  426 138 HOH   HOH B . 
Q 6 HOH   27  427 128 HOH   HOH B . 
Q 6 HOH   28  428 81  HOH   HOH B . 
Q 6 HOH   29  429 476 HOH   HOH B . 
Q 6 HOH   30  430 271 HOH   HOH B . 
Q 6 HOH   31  431 35  HOH   HOH B . 
Q 6 HOH   32  432 121 HOH   HOH B . 
Q 6 HOH   33  433 263 HOH   HOH B . 
Q 6 HOH   34  434 308 HOH   HOH B . 
Q 6 HOH   35  435 164 HOH   HOH B . 
Q 6 HOH   36  436 465 HOH   HOH B . 
Q 6 HOH   37  437 223 HOH   HOH B . 
Q 6 HOH   38  438 189 HOH   HOH B . 
Q 6 HOH   39  439 32  HOH   HOH B . 
Q 6 HOH   40  440 125 HOH   HOH B . 
Q 6 HOH   41  441 523 HOH   HOH B . 
Q 6 HOH   42  442 293 HOH   HOH B . 
Q 6 HOH   43  443 185 HOH   HOH B . 
Q 6 HOH   44  444 78  HOH   HOH B . 
Q 6 HOH   45  445 177 HOH   HOH B . 
Q 6 HOH   46  446 149 HOH   HOH B . 
Q 6 HOH   47  447 498 HOH   HOH B . 
Q 6 HOH   48  448 496 HOH   HOH B . 
Q 6 HOH   49  449 47  HOH   HOH B . 
Q 6 HOH   50  450 108 HOH   HOH B . 
Q 6 HOH   51  451 55  HOH   HOH B . 
Q 6 HOH   52  452 544 HOH   HOH B . 
Q 6 HOH   53  453 378 HOH   HOH B . 
Q 6 HOH   54  454 159 HOH   HOH B . 
Q 6 HOH   55  455 84  HOH   HOH B . 
Q 6 HOH   56  456 339 HOH   HOH B . 
Q 6 HOH   57  457 214 HOH   HOH B . 
Q 6 HOH   58  458 63  HOH   HOH B . 
Q 6 HOH   59  459 24  HOH   HOH B . 
Q 6 HOH   60  460 136 HOH   HOH B . 
Q 6 HOH   61  461 37  HOH   HOH B . 
Q 6 HOH   62  462 2   HOH   HOH B . 
Q 6 HOH   63  463 143 HOH   HOH B . 
Q 6 HOH   64  464 10  HOH   HOH B . 
Q 6 HOH   65  465 178 HOH   HOH B . 
Q 6 HOH   66  466 1   HOH   HOH B . 
Q 6 HOH   67  467 203 HOH   HOH B . 
Q 6 HOH   68  468 88  HOH   HOH B . 
Q 6 HOH   69  469 101 HOH   HOH B . 
Q 6 HOH   70  470 376 HOH   HOH B . 
Q 6 HOH   71  471 97  HOH   HOH B . 
Q 6 HOH   72  472 238 HOH   HOH B . 
Q 6 HOH   73  473 240 HOH   HOH B . 
Q 6 HOH   74  474 141 HOH   HOH B . 
Q 6 HOH   75  475 220 HOH   HOH B . 
Q 6 HOH   76  476 42  HOH   HOH B . 
Q 6 HOH   77  477 151 HOH   HOH B . 
Q 6 HOH   78  478 11  HOH   HOH B . 
Q 6 HOH   79  479 193 HOH   HOH B . 
Q 6 HOH   80  480 75  HOH   HOH B . 
Q 6 HOH   81  481 200 HOH   HOH B . 
Q 6 HOH   82  482 15  HOH   HOH B . 
Q 6 HOH   83  483 8   HOH   HOH B . 
Q 6 HOH   84  484 334 HOH   HOH B . 
Q 6 HOH   85  485 537 HOH   HOH B . 
Q 6 HOH   86  486 450 HOH   HOH B . 
Q 6 HOH   87  487 129 HOH   HOH B . 
Q 6 HOH   88  488 169 HOH   HOH B . 
Q 6 HOH   89  489 221 HOH   HOH B . 
Q 6 HOH   90  490 99  HOH   HOH B . 
Q 6 HOH   91  491 176 HOH   HOH B . 
Q 6 HOH   92  492 124 HOH   HOH B . 
Q 6 HOH   93  493 179 HOH   HOH B . 
Q 6 HOH   94  494 343 HOH   HOH B . 
Q 6 HOH   95  495 488 HOH   HOH B . 
Q 6 HOH   96  496 51  HOH   HOH B . 
Q 6 HOH   97  497 156 HOH   HOH B . 
Q 6 HOH   98  498 237 HOH   HOH B . 
Q 6 HOH   99  499 25  HOH   HOH B . 
Q 6 HOH   100 500 4   HOH   HOH B . 
Q 6 HOH   101 501 268 HOH   HOH B . 
Q 6 HOH   102 502 174 HOH   HOH B . 
Q 6 HOH   103 503 426 HOH   HOH B . 
Q 6 HOH   104 504 122 HOH   HOH B . 
Q 6 HOH   105 505 33  HOH   HOH B . 
Q 6 HOH   106 506 36  HOH   HOH B . 
Q 6 HOH   107 507 333 HOH   HOH B . 
Q 6 HOH   108 508 533 HOH   HOH B . 
Q 6 HOH   109 509 12  HOH   HOH B . 
Q 6 HOH   110 510 60  HOH   HOH B . 
Q 6 HOH   111 511 30  HOH   HOH B . 
Q 6 HOH   112 512 291 HOH   HOH B . 
Q 6 HOH   113 513 289 HOH   HOH B . 
Q 6 HOH   114 514 499 HOH   HOH B . 
Q 6 HOH   115 515 39  HOH   HOH B . 
Q 6 HOH   116 516 454 HOH   HOH B . 
Q 6 HOH   117 517 187 HOH   HOH B . 
Q 6 HOH   118 518 69  HOH   HOH B . 
Q 6 HOH   119 519 403 HOH   HOH B . 
Q 6 HOH   120 520 112 HOH   HOH B . 
Q 6 HOH   121 521 67  HOH   HOH B . 
Q 6 HOH   122 522 114 HOH   HOH B . 
Q 6 HOH   123 523 247 HOH   HOH B . 
Q 6 HOH   124 524 260 HOH   HOH B . 
Q 6 HOH   125 525 250 HOH   HOH B . 
Q 6 HOH   126 526 447 HOH   HOH B . 
Q 6 HOH   127 527 57  HOH   HOH B . 
Q 6 HOH   128 528 438 HOH   HOH B . 
Q 6 HOH   129 529 38  HOH   HOH B . 
Q 6 HOH   130 530 224 HOH   HOH B . 
Q 6 HOH   131 531 134 HOH   HOH B . 
Q 6 HOH   132 532 153 HOH   HOH B . 
Q 6 HOH   133 533 543 HOH   HOH B . 
Q 6 HOH   134 534 407 HOH   HOH B . 
Q 6 HOH   135 535 329 HOH   HOH B . 
Q 6 HOH   136 536 301 HOH   HOH B . 
Q 6 HOH   137 537 93  HOH   HOH B . 
Q 6 HOH   138 538 23  HOH   HOH B . 
Q 6 HOH   139 539 444 HOH   HOH B . 
Q 6 HOH   140 540 410 HOH   HOH B . 
Q 6 HOH   141 541 180 HOH   HOH B . 
Q 6 HOH   142 542 9   HOH   HOH B . 
Q 6 HOH   143 543 307 HOH   HOH B . 
Q 6 HOH   144 544 506 HOH   HOH B . 
Q 6 HOH   145 545 393 HOH   HOH B . 
Q 6 HOH   146 546 273 HOH   HOH B . 
Q 6 HOH   147 547 217 HOH   HOH B . 
Q 6 HOH   148 548 70  HOH   HOH B . 
Q 6 HOH   149 549 377 HOH   HOH B . 
Q 6 HOH   150 550 253 HOH   HOH B . 
Q 6 HOH   151 551 207 HOH   HOH B . 
Q 6 HOH   152 552 59  HOH   HOH B . 
Q 6 HOH   153 553 139 HOH   HOH B . 
Q 6 HOH   154 554 344 HOH   HOH B . 
Q 6 HOH   155 555 68  HOH   HOH B . 
Q 6 HOH   156 556 358 HOH   HOH B . 
Q 6 HOH   157 557 474 HOH   HOH B . 
Q 6 HOH   158 558 100 HOH   HOH B . 
Q 6 HOH   159 559 261 HOH   HOH B . 
Q 6 HOH   160 560 505 HOH   HOH B . 
Q 6 HOH   161 561 103 HOH   HOH B . 
Q 6 HOH   162 562 408 HOH   HOH B . 
Q 6 HOH   163 563 353 HOH   HOH B . 
Q 6 HOH   164 564 184 HOH   HOH B . 
Q 6 HOH   165 565 348 HOH   HOH B . 
Q 6 HOH   166 566 239 HOH   HOH B . 
Q 6 HOH   167 567 313 HOH   HOH B . 
Q 6 HOH   168 568 405 HOH   HOH B . 
Q 6 HOH   169 569 443 HOH   HOH B . 
Q 6 HOH   170 570 294 HOH   HOH B . 
Q 6 HOH   171 571 399 HOH   HOH B . 
Q 6 HOH   172 572 383 HOH   HOH B . 
Q 6 HOH   173 573 80  HOH   HOH B . 
Q 6 HOH   174 574 95  HOH   HOH B . 
Q 6 HOH   175 575 535 HOH   HOH B . 
Q 6 HOH   176 576 350 HOH   HOH B . 
Q 6 HOH   177 577 395 HOH   HOH B . 
Q 6 HOH   178 578 345 HOH   HOH B . 
Q 6 HOH   179 579 13  HOH   HOH B . 
Q 6 HOH   180 580 489 HOH   HOH B . 
Q 6 HOH   181 581 361 HOH   HOH B . 
Q 6 HOH   182 582 388 HOH   HOH B . 
Q 6 HOH   183 583 461 HOH   HOH B . 
Q 6 HOH   184 584 514 HOH   HOH B . 
Q 6 HOH   185 585 225 HOH   HOH B . 
Q 6 HOH   186 586 502 HOH   HOH B . 
Q 6 HOH   187 587 485 HOH   HOH B . 
Q 6 HOH   188 588 518 HOH   HOH B . 
Q 6 HOH   189 589 215 HOH   HOH B . 
Q 6 HOH   190 590 422 HOH   HOH B . 
Q 6 HOH   191 591 227 HOH   HOH B . 
Q 6 HOH   192 592 251 HOH   HOH B . 
Q 6 HOH   193 593 400 HOH   HOH B . 
Q 6 HOH   194 594 46  HOH   HOH B . 
Q 6 HOH   195 595 248 HOH   HOH B . 
Q 6 HOH   196 596 330 HOH   HOH B . 
Q 6 HOH   197 597 210 HOH   HOH B . 
Q 6 HOH   198 598 274 HOH   HOH B . 
Q 6 HOH   199 599 368 HOH   HOH B . 
Q 6 HOH   200 600 540 HOH   HOH B . 
Q 6 HOH   201 601 53  HOH   HOH B . 
Q 6 HOH   202 602 182 HOH   HOH B . 
Q 6 HOH   203 603 186 HOH   HOH B . 
Q 6 HOH   204 604 412 HOH   HOH B . 
Q 6 HOH   205 605 354 HOH   HOH B . 
Q 6 HOH   206 606 484 HOH   HOH B . 
Q 6 HOH   207 607 529 HOH   HOH B . 
Q 6 HOH   208 608 236 HOH   HOH B . 
Q 6 HOH   209 609 463 HOH   HOH B . 
Q 6 HOH   210 610 536 HOH   HOH B . 
Q 6 HOH   211 611 446 HOH   HOH B . 
Q 6 HOH   212 612 264 HOH   HOH B . 
Q 6 HOH   213 613 435 HOH   HOH B . 
Q 6 HOH   214 614 219 HOH   HOH B . 
Q 6 HOH   215 615 462 HOH   HOH B . 
Q 6 HOH   216 616 516 HOH   HOH B . 
Q 6 HOH   217 617 211 HOH   HOH B . 
Q 6 HOH   218 618 420 HOH   HOH B . 
Q 6 HOH   219 619 432 HOH   HOH B . 
Q 6 HOH   220 620 478 HOH   HOH B . 
Q 6 HOH   221 621 85  HOH   HOH B . 
Q 6 HOH   222 622 517 HOH   HOH B . 
Q 6 HOH   223 623 309 HOH   HOH B . 
Q 6 HOH   224 624 364 HOH   HOH B . 
Q 6 HOH   225 625 175 HOH   HOH B . 
Q 6 HOH   226 626 245 HOH   HOH B . 
Q 6 HOH   227 627 54  HOH   HOH B . 
Q 6 HOH   228 628 270 HOH   HOH B . 
Q 6 HOH   229 629 397 HOH   HOH B . 
Q 6 HOH   230 630 542 HOH   HOH B . 
Q 6 HOH   231 631 375 HOH   HOH B . 
Q 6 HOH   232 632 56  HOH   HOH B . 
Q 6 HOH   233 633 154 HOH   HOH B . 
Q 6 HOH   234 634 466 HOH   HOH B . 
Q 6 HOH   235 635 316 HOH   HOH B . 
Q 6 HOH   236 636 155 HOH   HOH B . 
Q 6 HOH   237 637 359 HOH   HOH B . 
Q 6 HOH   238 638 266 HOH   HOH B . 
Q 6 HOH   239 639 490 HOH   HOH B . 
Q 6 HOH   240 640 455 HOH   HOH B . 
Q 6 HOH   241 641 439 HOH   HOH B . 
Q 6 HOH   242 642 246 HOH   HOH B . 
Q 6 HOH   243 643 346 HOH   HOH B . 
Q 6 HOH   244 644 279 HOH   HOH B . 
Q 6 HOH   245 645 256 HOH   HOH B . 
Q 6 HOH   246 646 473 HOH   HOH B . 
Q 6 HOH   247 647 416 HOH   HOH B . 
Q 6 HOH   248 648 306 HOH   HOH B . 
Q 6 HOH   249 649 475 HOH   HOH B . 
Q 6 HOH   250 650 127 HOH   HOH B . 
Q 6 HOH   251 651 406 HOH   HOH B . 
Q 6 HOH   252 652 86  HOH   HOH B . 
Q 6 HOH   253 653 504 HOH   HOH B . 
Q 6 HOH   254 654 90  HOH   HOH B . 
Q 6 HOH   255 655 196 HOH   HOH B . 
Q 6 HOH   256 656 495 HOH   HOH B . 
Q 6 HOH   257 657 428 HOH   HOH B . 
Q 6 HOH   258 658 147 HOH   HOH B . 
Q 6 HOH   259 659 392 HOH   HOH B . 
Q 6 HOH   260 660 226 HOH   HOH B . 
Q 6 HOH   261 661 437 HOH   HOH B . 
Q 6 HOH   262 662 464 HOH   HOH B . 
Q 6 HOH   263 663 314 HOH   HOH B . 
Q 6 HOH   264 664 300 HOH   HOH B . 
Q 6 HOH   265 665 417 HOH   HOH B . 
Q 6 HOH   266 666 148 HOH   HOH B . 
Q 6 HOH   267 667 157 HOH   HOH B . 
Q 6 HOH   268 668 286 HOH   HOH B . 
Q 6 HOH   269 669 467 HOH   HOH B . 
Q 6 HOH   270 670 322 HOH   HOH B . 
Q 6 HOH   271 671 168 HOH   HOH B . 
Q 6 HOH   272 672 173 HOH   HOH B . 
Q 6 HOH   273 673 520 HOH   HOH B . 
Q 6 HOH   274 674 208 HOH   HOH B . 
Q 6 HOH   275 675 421 HOH   HOH B . 
Q 6 HOH   276 676 311 HOH   HOH B . 
Q 6 HOH   277 677 396 HOH   HOH B . 
Q 6 HOH   278 678 351 HOH   HOH B . 
Q 6 HOH   279 679 303 HOH   HOH B . 
Q 6 HOH   280 680 457 HOH   HOH B . 
Q 6 HOH   281 681 299 HOH   HOH B . 
Q 6 HOH   282 682 290 HOH   HOH B . 
Q 6 HOH   283 683 515 HOH   HOH B . 
Q 6 HOH   284 684 295 HOH   HOH B . 
Q 6 HOH   285 685 390 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 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.1.7       3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.1.7       4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.1.7       5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   130.730 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F0P 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     102.145 
_cell.length_a_esd                 ? 
_cell.length_b                     79.019 
_cell.length_b_esd                 ? 
_cell.length_c                     67.896 
_cell.length_c_esd                 ? 
_cell.volume                       415282.187 
_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                         9F0P 
_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                   9F0P 
_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          35.19 
_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                          15.12 
_reflns.entry_id                                       9F0P 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.34 
_reflns.d_resolution_low                               55.29 
_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                                     90818 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_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                                0.07 
_reflns.pdbx_Rpim_I_all                                0.027 
_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                              0.07 
_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                                    1.34 
_reflns_shell.d_res_low                                     1.36 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4037 
_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                               5.5 
_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                               0.67 
_reflns_shell.pdbx_Rpim_I_all                               0.280 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.865 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          87.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.61 
_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                               21.95 
_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                                 9F0P 
_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                            1.34 
_refine.ls_d_res_low                             39.51 
_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                     90789 
_refine.ls_number_reflns_R_free                  4319 
_refine.ls_number_reflns_R_work                  86470 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.22 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1734 
_refine.ls_R_factor_R_free                       0.1885 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1727 
_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                          1.34 
_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                 20.7763 
_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                            0.1395 
_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                       1.34 
_refine_hist.d_res_low                        39.51 
_refine_hist.number_atoms_solvent             536 
_refine_hist.number_atoms_total               4112 
_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         90 
_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' ? 0.0088  ? 3973 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9816  ? 5483 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0847  ? 601  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0074  ? 730  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.7879 ? 1385 ? 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' 1.34 1.35  . . 126 2508 86.13 . . . . 0.2744 . . . . . . . . . . . 0.3277 
'X-RAY DIFFRACTION' 1.35 1.37  . . 99  2648 89.54 . . . . 0.2624 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 1.37 1.38  . . 130 2710 92.48 . . . . 0.2430 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 1.38 1.40  . . 109 2844 96.19 . . . . 0.2393 . . . . . . . . . . . 0.2712 
'X-RAY DIFFRACTION' 1.40 1.42  . . 167 2910 99.19 . . . . 0.2376 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 1.42 1.44  . . 159 2876 99.54 . . . . 0.2257 . . . . . . . . . . . 0.2636 
'X-RAY DIFFRACTION' 1.44 1.46  . . 137 2900 99.12 . . . . 0.2191 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 1.46 1.48  . . 114 2929 98.86 . . . . 0.2103 . . . . . . . . . . . 0.2564 
'X-RAY DIFFRACTION' 1.48 1.50  . . 126 2919 99.35 . . . . 0.2056 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 1.50 1.53  . . 156 2874 99.21 . . . . 0.2042 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 1.53 1.56  . . 154 2923 99.29 . . . . 0.2012 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 1.56 1.58  . . 149 2909 99.45 . . . . 0.2016 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 1.58 1.61  . . 152 2914 99.16 . . . . 0.2001 . . . . . . . . . . . 0.2221 
'X-RAY DIFFRACTION' 1.61 1.65  . . 146 2903 99.35 . . . . 0.1979 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 1.65 1.68  . . 147 2867 99.37 . . . . 0.1900 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 1.68 1.72  . . 162 2913 99.42 . . . . 0.1825 . . . . . . . . . . . 0.1902 
'X-RAY DIFFRACTION' 1.72 1.76  . . 163 2888 99.03 . . . . 0.1826 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 1.76 1.81  . . 185 2870 99.64 . . . . 0.1845 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 1.81 1.87  . . 165 2892 99.54 . . . . 0.1787 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 1.87 1.93  . . 154 2918 99.42 . . . . 0.1841 . . . . . . . . . . . 0.2086 
'X-RAY DIFFRACTION' 1.93 2.00  . . 115 2949 99.38 . . . . 0.1776 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 2.00 2.07  . . 143 2909 99.54 . . . . 0.1661 . . . . . . . . . . . 0.2226 
'X-RAY DIFFRACTION' 2.07 2.17  . . 129 2960 99.23 . . . . 0.1666 . . . . . . . . . . . 0.1725 
'X-RAY DIFFRACTION' 2.17 2.28  . . 131 2901 99.25 . . . . 0.1721 . . . . . . . . . . . 0.1873 
'X-RAY DIFFRACTION' 2.28 2.43  . . 182 2880 98.68 . . . . 0.1686 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 2.43 2.61  . . 120 2925 98.96 . . . . 0.1735 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 2.61 2.88  . . 154 2929 99.42 . . . . 0.1701 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 2.88 3.29  . . 158 2938 99.77 . . . . 0.1636 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 3.29 4.15  . . 171 2933 99.61 . . . . 0.1413 . . . . . . . . . . . 0.1503 
'X-RAY DIFFRACTION' 4.15 39.51 . . 116 3031 99.40 . . . . 0.1505 . . . . . . . . . . . 0.1351 
# 
_struct.entry_id                     9F0P 
_struct.title                        
'VIM-2 in complex with GKV61 (5c) - 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        9F0P 
_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 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 5 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 6 ? 
Q N N 6 ? 
# 
_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 9F0P A 15 ? 254 ? B8QIQ9 27 ? 266 ? 27 266 
2 1 9F0P 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 9F0P MET A 1  ? UNP B8QIQ9 ? ? 'initiating methionine' 13 1  
1 9F0P HIS A 2  ? UNP B8QIQ9 ? ? 'expression tag'        14 2  
1 9F0P HIS A 3  ? UNP B8QIQ9 ? ? 'expression tag'        15 3  
1 9F0P HIS A 4  ? UNP B8QIQ9 ? ? 'expression tag'        16 4  
1 9F0P HIS A 5  ? UNP B8QIQ9 ? ? 'expression tag'        17 5  
1 9F0P HIS A 6  ? UNP B8QIQ9 ? ? 'expression tag'        18 6  
1 9F0P HIS A 7  ? UNP B8QIQ9 ? ? 'expression tag'        19 7  
1 9F0P GLU A 8  ? UNP B8QIQ9 ? ? 'expression tag'        20 8  
1 9F0P ASN A 9  ? UNP B8QIQ9 ? ? 'expression tag'        21 9  
1 9F0P LEU A 10 ? UNP B8QIQ9 ? ? 'expression tag'        22 10 
1 9F0P TYR A 11 ? UNP B8QIQ9 ? ? 'expression tag'        23 11 
1 9F0P PHE A 12 ? UNP B8QIQ9 ? ? 'expression tag'        24 12 
1 9F0P GLN A 13 ? UNP B8QIQ9 ? ? 'expression tag'        25 13 
1 9F0P GLY A 14 ? UNP B8QIQ9 ? ? 'expression tag'        26 14 
2 9F0P MET B 1  ? UNP B8QIQ9 ? ? 'initiating methionine' 13 15 
2 9F0P HIS B 2  ? UNP B8QIQ9 ? ? 'expression tag'        14 16 
2 9F0P HIS B 3  ? UNP B8QIQ9 ? ? 'expression tag'        15 17 
2 9F0P HIS B 4  ? UNP B8QIQ9 ? ? 'expression tag'        16 18 
2 9F0P HIS B 5  ? UNP B8QIQ9 ? ? 'expression tag'        17 19 
2 9F0P HIS B 6  ? UNP B8QIQ9 ? ? 'expression tag'        18 20 
2 9F0P HIS B 7  ? UNP B8QIQ9 ? ? 'expression tag'        19 21 
2 9F0P GLU B 8  ? UNP B8QIQ9 ? ? 'expression tag'        20 22 
2 9F0P ASN B 9  ? UNP B8QIQ9 ? ? 'expression tag'        21 23 
2 9F0P LEU B 10 ? UNP B8QIQ9 ? ? 'expression tag'        22 24 
2 9F0P TYR B 11 ? UNP B8QIQ9 ? ? 'expression tag'        23 25 
2 9F0P PHE B 12 ? UNP B8QIQ9 ? ? 'expression tag'        24 26 
2 9F0P GLN B 13 ? UNP B8QIQ9 ? ? 'expression tag'        25 27 
2 9F0P 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,P   
2 1 B,I,J,K,L,M,N,O,Q 
# 
_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 ? ? ? ? ? ? ? 2.147 ? ? 
metalc2  metalc ? ? A HIS   104 ND1 ? ? ? 1_555 F ZN . ZN ? ? A HIS   116 A ZN 304 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc3  metalc ? ? A ASP   106 OD2 ? ? ? 1_555 H ZN . ZN ? ? A ASP   118 A ZN 306 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc4  metalc ? ? A HIS   141 NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS   153 A ZN 305 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc5  metalc ? ? A HIS   167 NE2 ? ? ? 1_555 F ZN . ZN ? ? A HIS   179 A ZN 304 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc6  metalc ? ? A CYS   186 SG  ? ? ? 1_555 H ZN . ZN ? ? A CYS   198 A ZN 306 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc7  metalc ? ? A HIS   228 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS   240 A ZN 306 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc8  metalc ? ? A HIS   239 ND1 ? ? ? 1_555 G ZN . ZN ? ? A HIS   251 A ZN 305 4_545 ? ? ? ? ? ? ? 2.123 ? ? 
metalc9  metalc ? ? C FMT   .   O1  ? ? ? 1_555 G ZN . ZN ? ? A FMT   301 A ZN 305 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc10 metalc ? ? C FMT   .   O2  ? ? ? 1_555 G ZN . ZN ? ? A FMT   301 A ZN 305 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc11 metalc ? ? D FMT   .   O1  ? ? ? 1_555 G ZN . ZN ? ? A FMT   302 A ZN 305 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc12 metalc ? ? D FMT   .   O2  ? ? ? 1_555 G ZN . ZN ? ? A FMT   302 A ZN 305 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc13 metalc ? ? E A1IKA .   O15 A ? ? 1_555 F ZN . ZN ? ? A A1IKA 303 A ZN 304 1_555 ? ? ? ? ? ? ? 1.899 ? ? 
metalc14 metalc ? ? E A1IKA .   O15 B ? ? 1_555 F ZN . ZN ? ? A A1IKA 303 A ZN 304 1_555 ? ? ? ? ? ? ? 1.888 ? ? 
metalc15 metalc ? ? E A1IKA .   O14 A ? ? 1_555 H ZN . ZN ? ? A A1IKA 303 A ZN 306 1_555 ? ? ? ? ? ? ? 2.243 ? ? 
metalc16 metalc ? ? E A1IKA .   O14 B ? ? 1_555 H ZN . ZN ? ? A A1IKA 303 A ZN 306 1_555 ? ? ? ? ? ? ? 1.770 ? ? 
metalc17 metalc ? ? B HIS   102 NE2 ? ? ? 1_555 M ZN . ZN ? ? B HIS   114 B ZN 305 1_555 ? ? ? ? ? ? ? 2.121 ? ? 
metalc18 metalc ? ? B HIS   104 ND1 ? ? ? 1_555 M ZN . ZN ? ? B HIS   116 B ZN 305 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc19 metalc ? ? B ASP   106 OD2 ? ? ? 1_555 O ZN . ZN ? ? B ASP   118 B ZN 307 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc20 metalc ? ? B HIS   141 NE2 ? ? ? 1_555 N ZN . ZN ? ? B HIS   153 B ZN 306 4_546 ? ? ? ? ? ? ? 2.213 ? ? 
metalc21 metalc ? ? B HIS   167 NE2 ? ? ? 1_555 M ZN . ZN ? ? B HIS   179 B ZN 305 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc22 metalc ? ? B CYS   186 SG  ? ? ? 1_555 O ZN . ZN ? ? B CYS   198 B ZN 307 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc23 metalc ? ? B HIS   228 NE2 ? ? ? 1_555 O ZN . ZN ? ? B HIS   240 B ZN 307 1_555 ? ? ? ? ? ? ? 2.137 ? ? 
metalc24 metalc ? ? B HIS   239 ND1 ? ? ? 1_555 N ZN . ZN ? ? B HIS   251 B ZN 306 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc25 metalc ? ? I FMT   .   O1  ? ? ? 1_555 N ZN . ZN ? ? B FMT   301 B ZN 306 1_555 ? ? ? ? ? ? ? 1.951 ? ? 
metalc26 metalc ? ? I FMT   .   O2  ? ? ? 1_555 N ZN . ZN ? ? B FMT   301 B ZN 306 1_555 ? ? ? ? ? ? ? 2.401 ? ? 
metalc27 metalc ? ? L A1H8T .   O13 ? ? ? 1_555 M ZN . ZN ? ? B A1H8T 304 B ZN 305 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
metalc28 metalc ? ? L A1H8T .   O15 ? ? ? 1_555 O ZN . ZN ? ? B A1H8T 304 B ZN 307 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
# 
_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 98.7  ? 
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 99.3  ? 
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_555 112.2 ? 
4  NE2 ? A HIS   102 ? A HIS   114 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 A E A1IKA .   ? A A1IKA 303 ? 1_555 119.3 ? 
5  ND1 ? A HIS   104 ? A HIS   116 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 A E A1IKA .   ? A A1IKA 303 ? 1_555 110.1 ? 
6  NE2 ? A HIS   167 ? A HIS   179 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 A E A1IKA .   ? A A1IKA 303 ? 1_555 115.8 ? 
7  NE2 ? A HIS   102 ? A HIS   114 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 B E A1IKA .   ? A A1IKA 303 ? 1_555 123.0 ? 
8  ND1 ? A HIS   104 ? A HIS   116 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 B E A1IKA .   ? A A1IKA 303 ? 1_555 102.4 ? 
9  NE2 ? A HIS   167 ? A HIS   179 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 B E A1IKA .   ? A A1IKA 303 ? 1_555 119.6 ? 
10 O15 A E A1IKA .   ? A A1IKA 303 ? 1_555 ZN ? F ZN . ? A ZN 304 ? 1_555 O15 B E A1IKA .   ? A A1IKA 303 ? 1_555 7.8   ? 
11 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_555 113.6 ? 
12 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 93.7  ? 
13 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_555 108.8 ? 
14 OD2 ? A ASP   106 ? A ASP   118 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 A E A1IKA .   ? A A1IKA 303 ? 1_555 116.5 ? 
15 SG  ? A CYS   186 ? A CYS   198 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 A E A1IKA .   ? A A1IKA 303 ? 1_555 117.1 ? 
16 NE2 ? A HIS   228 ? A HIS   240 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 A E A1IKA .   ? A A1IKA 303 ? 1_555 103.5 ? 
17 OD2 ? A ASP   106 ? A ASP   118 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 B E A1IKA .   ? A A1IKA 303 ? 1_555 109.5 ? 
18 SG  ? A CYS   186 ? A CYS   198 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 B E A1IKA .   ? A A1IKA 303 ? 1_555 120.5 ? 
19 NE2 ? A HIS   228 ? A HIS   240 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 B E A1IKA .   ? A A1IKA 303 ? 1_555 107.3 ? 
20 O14 A E A1IKA .   ? A A1IKA 303 ? 1_555 ZN ? H ZN . ? A ZN 306 ? 1_555 O14 B E A1IKA .   ? A A1IKA 303 ? 1_555 7.5   ? 
21 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 47.2  ? 
22 NE2 ? A HIS   141 ? A HIS   153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? C FMT   .   ? A FMT   301 ? 1_555 122.6 ? 
23 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 97.2  ? 
24 NE2 ? A HIS   141 ? A HIS   153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? C FMT   .   ? A FMT   301 ? 1_555 75.2  ? 
25 ND1 ? A HIS   239 ? A HIS   251 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? C FMT   .   ? A FMT   301 ? 1_555 86.4  ? 
26 O1  ? C FMT   .   ? A FMT   301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? C FMT   .   ? A FMT   301 ? 1_555 56.5  ? 
27 NE2 ? A HIS   141 ? A HIS   153 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 129.8 ? 
28 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 85.2  ? 
29 O1  ? C FMT   .   ? A FMT   301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 69.8  ? 
30 O2  ? C FMT   .   ? A FMT   301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O1  ? D FMT   .   ? A FMT   302 ? 1_555 124.0 ? 
31 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 81.8  ? 
32 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 67.9  ? 
33 O1  ? C FMT   .   ? A FMT   301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 131.2 ? 
34 O2  ? C FMT   .   ? A FMT   301 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 153.3 ? 
35 O1  ? D FMT   .   ? A FMT   302 ? 1_555 ZN ? G ZN . ? A ZN 305 ? 1_555 O2  ? D FMT   .   ? A FMT   302 ? 1_555 63.0  ? 
36 NE2 ? B HIS   102 ? B HIS   114 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 ND1 ? B HIS   104 ? B HIS   116 ? 1_555 100.8 ? 
37 NE2 ? B HIS   102 ? B HIS   114 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 NE2 ? B HIS   167 ? B HIS   179 ? 1_555 99.6  ? 
38 ND1 ? B HIS   104 ? B HIS   116 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 NE2 ? B HIS   167 ? B HIS   179 ? 1_555 111.8 ? 
39 NE2 ? B HIS   102 ? B HIS   114 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 O13 ? L A1H8T .   ? B A1H8T 304 ? 1_555 121.1 ? 
40 ND1 ? B HIS   104 ? B HIS   116 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 O13 ? L A1H8T .   ? B A1H8T 304 ? 1_555 104.7 ? 
41 NE2 ? B HIS   167 ? B HIS   179 ? 1_555 ZN ? M ZN . ? B ZN 305 ? 1_555 O13 ? L A1H8T .   ? B A1H8T 304 ? 1_555 117.8 ? 
42 OD2 ? B ASP   106 ? B ASP   118 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 SG  ? B CYS   186 ? B CYS   198 ? 1_555 117.5 ? 
43 OD2 ? B ASP   106 ? B ASP   118 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 NE2 ? B HIS   228 ? B HIS   240 ? 1_555 91.6  ? 
44 SG  ? B CYS   186 ? B CYS   198 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 NE2 ? B HIS   228 ? B HIS   240 ? 1_555 109.8 ? 
45 OD2 ? B ASP   106 ? B ASP   118 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 O15 ? L A1H8T .   ? B A1H8T 304 ? 1_555 110.0 ? 
46 SG  ? B CYS   186 ? B CYS   198 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 O15 ? L A1H8T .   ? B A1H8T 304 ? 1_555 119.8 ? 
47 NE2 ? B HIS   228 ? B HIS   240 ? 1_555 ZN ? O ZN . ? B ZN 307 ? 1_555 O15 ? L A1H8T .   ? B A1H8T 304 ? 1_555 103.5 ? 
48 NE2 ? B HIS   141 ? B HIS   153 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 ND1 ? B HIS   239 ? B HIS   251 ? 1_555 36.7  ? 
49 NE2 ? B HIS   141 ? B HIS   153 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 O1  ? I FMT   .   ? B FMT   301 ? 1_555 34.5  ? 
50 ND1 ? B HIS   239 ? B HIS   251 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 O1  ? I FMT   .   ? B FMT   301 ? 1_555 2.2   ? 
51 NE2 ? B HIS   141 ? B HIS   153 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 O2  ? I FMT   .   ? B FMT   301 ? 1_555 36.4  ? 
52 ND1 ? B HIS   239 ? B HIS   251 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 O2  ? I FMT   .   ? B FMT   301 ? 1_555 2.3   ? 
53 O1  ? I FMT   .   ? B FMT   301 ? 1_555 ZN ? N ZN . ? B ZN 306 ? 4_546 O2  ? I FMT   .   ? B FMT   301 ? 1_555 3.0   ? 
# 
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 TRP A 42  ? N TRP A 54  O ILE A 61  ? O ILE A 73  
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 TRP B 42  ? N TRP B 54  O ILE B 61  ? O ILE B 73  
AA3 3 4 N LEU B 60  ? N LEU B 72  O ILE B 71  ? O ILE B 83  
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 GLY B 184 ? N GLY B 196 O ILE B 225 ? O ILE B 237 
# 
_pdbx_entry_details.entry_id                   9F0P 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 O1  B FMT 302 ? ? ZN B ZN  306 ? ? 1.45 
2  1 O   B HOH 516 ? ? O  B HOH 583 ? ? 1.59 
3  1 ND2 B ASN 254 ? A O2 B FMT 302 ? ? 1.63 
4  1 O   A HOH 569 ? ? O  A HOH 587 ? ? 1.75 
5  1 O   B HOH 447 ? ? O  B HOH 586 ? ? 1.80 
6  1 O   B HOH 519 ? ? O  B HOH 593 ? ? 1.85 
7  1 O   B HOH 557 ? ? O  B HOH 640 ? ? 1.90 
8  1 O   B HOH 486 ? ? O  B HOH 611 ? ? 1.99 
9  1 OD1 A ASP 247 ? B O  A HOH 401 ? ? 2.04 
10 1 OH  A TYR 134 ? ? O  A HOH 402 ? ? 2.04 
11 1 OD2 A ASP 247 ? A O  A HOH 403 ? ? 2.05 
12 1 O   A HOH 491 ? ? O  A HOH 567 ? ? 2.06 
13 1 O   B HOH 592 ? ? O  B HOH 662 ? ? 2.07 
14 1 OE2 A GLU 224 ? B O  A HOH 404 ? ? 2.09 
15 1 O   A HOH 445 ? ? O  A HOH 555 ? ? 2.12 
16 1 O   B HOH 420 ? ? O  B HOH 559 ? ? 2.14 
# 
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 606 ? ? 1_555 O B HOH 583 ? ? 4_546 1.80 
2 1 O A HOH 606 ? ? 1_555 O B HOH 516 ? ? 4_546 1.86 
3 1 O A HOH 538 ? ? 1_555 O A HOH 603 ? ? 4_555 2.13 
# 
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  ? ? 75.65   144.96  
2 1 ALA A 86  ? ? -99.05  32.79   
3 1 TRP A 87  ? ? 64.41   68.60   
4 1 ALA A 178 ? ? -152.59 -104.67 
5 1 ASP B 84  ? ? 77.72   146.58  
6 1 TRP B 87  ? ? 69.77   73.39   
7 1 ALA B 178 ? ? -152.64 -104.92 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 489 ? P HOH . 
2 1 B HOH 575 ? Q HOH . 
# 
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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       685 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.01 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A 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 
A1H8T C17  C  Y N 1   
A1H8T C20  C  Y N 2   
A1H8T C21  C  Y N 3   
A1H8T C22  C  Y N 4   
A1H8T C16  C  Y N 5   
A1H8T C19  C  Y N 6   
A1H8T C23  C  Y N 7   
A1H8T C02  C  N N 8   
A1H8T C04  C  N R 9   
A1H8T C05  C  Y N 10  
A1H8T C06  C  Y N 11  
A1H8T C07  C  Y N 12  
A1H8T C08  C  Y N 13  
A1H8T C09  C  Y N 14  
A1H8T C10  C  Y N 15  
A1H8T C18  C  Y N 16  
A1H8T N03  N  N N 17  
A1H8T O01  O  N N 18  
A1H8T O11  O  N N 19  
A1H8T O13  O  N N 20  
A1H8T O14  O  N N 21  
A1H8T O15  O  N N 22  
A1H8T P12  P  N N 23  
A1H8T S24  S  Y N 24  
A1H8T H1   H  N N 25  
A1H8T H2   H  N N 26  
A1H8T H3   H  N N 27  
A1H8T H4   H  N N 28  
A1H8T H5   H  N N 29  
A1H8T H6   H  N N 30  
A1H8T H7   H  N N 31  
A1H8T H8   H  N N 32  
A1H8T H9   H  N N 33  
A1H8T H10  H  N N 34  
A1H8T H11  H  N N 35  
A1H8T H12  H  N N 36  
A1H8T H13  H  N N 37  
A1H8T H14  H  N N 38  
A1IKA C02  C  N N 39  
A1IKA C04  C  N S 40  
A1IKA C05  C  Y N 41  
A1IKA C06  C  Y N 42  
A1IKA C07  C  Y N 43  
A1IKA C08  C  Y N 44  
A1IKA C09  C  Y N 45  
A1IKA C10  C  Y N 46  
A1IKA C16  C  Y N 47  
A1IKA C17  C  Y N 48  
A1IKA C18  C  Y N 49  
A1IKA C19  C  Y N 50  
A1IKA C20  C  Y N 51  
A1IKA C21  C  Y N 52  
A1IKA C22  C  Y N 53  
A1IKA C23  C  Y N 54  
A1IKA N03  N  N N 55  
A1IKA O01  O  N N 56  
A1IKA O11  O  N N 57  
A1IKA O13  O  N N 58  
A1IKA O14  O  N N 59  
A1IKA O15  O  N N 60  
A1IKA P12  P  N N 61  
A1IKA S24  S  Y N 62  
A1IKA H1   H  N N 63  
A1IKA H2   H  N N 64  
A1IKA H3   H  N N 65  
A1IKA H4   H  N N 66  
A1IKA H5   H  N N 67  
A1IKA H6   H  N N 68  
A1IKA H7   H  N N 69  
A1IKA H8   H  N N 70  
A1IKA H9   H  N N 71  
A1IKA H10  H  N N 72  
A1IKA H11  H  N N 73  
A1IKA H12  H  N N 74  
A1IKA H13  H  N N 75  
A1IKA H14  H  N N 76  
ALA   N    N  N N 77  
ALA   CA   C  N S 78  
ALA   C    C  N N 79  
ALA   O    O  N N 80  
ALA   CB   C  N N 81  
ALA   OXT  O  N N 82  
ALA   H    H  N N 83  
ALA   H2   H  N N 84  
ALA   HA   H  N N 85  
ALA   HB1  H  N N 86  
ALA   HB2  H  N N 87  
ALA   HB3  H  N N 88  
ALA   HXT  H  N N 89  
ARG   N    N  N N 90  
ARG   CA   C  N S 91  
ARG   C    C  N N 92  
ARG   O    O  N N 93  
ARG   CB   C  N N 94  
ARG   CG   C  N N 95  
ARG   CD   C  N N 96  
ARG   NE   N  N N 97  
ARG   CZ   C  N N 98  
ARG   NH1  N  N N 99  
ARG   NH2  N  N N 100 
ARG   OXT  O  N N 101 
ARG   H    H  N N 102 
ARG   H2   H  N N 103 
ARG   HA   H  N N 104 
ARG   HB2  H  N N 105 
ARG   HB3  H  N N 106 
ARG   HG2  H  N N 107 
ARG   HG3  H  N N 108 
ARG   HD2  H  N N 109 
ARG   HD3  H  N N 110 
ARG   HE   H  N N 111 
ARG   HH11 H  N N 112 
ARG   HH12 H  N N 113 
ARG   HH21 H  N N 114 
ARG   HH22 H  N N 115 
ARG   HXT  H  N N 116 
ASN   N    N  N N 117 
ASN   CA   C  N S 118 
ASN   C    C  N N 119 
ASN   O    O  N N 120 
ASN   CB   C  N N 121 
ASN   CG   C  N N 122 
ASN   OD1  O  N N 123 
ASN   ND2  N  N N 124 
ASN   OXT  O  N N 125 
ASN   H    H  N N 126 
ASN   H2   H  N N 127 
ASN   HA   H  N N 128 
ASN   HB2  H  N N 129 
ASN   HB3  H  N N 130 
ASN   HD21 H  N N 131 
ASN   HD22 H  N N 132 
ASN   HXT  H  N N 133 
ASP   N    N  N N 134 
ASP   CA   C  N S 135 
ASP   C    C  N N 136 
ASP   O    O  N N 137 
ASP   CB   C  N N 138 
ASP   CG   C  N N 139 
ASP   OD1  O  N N 140 
ASP   OD2  O  N N 141 
ASP   OXT  O  N N 142 
ASP   H    H  N N 143 
ASP   H2   H  N N 144 
ASP   HA   H  N N 145 
ASP   HB2  H  N N 146 
ASP   HB3  H  N N 147 
ASP   HD2  H  N N 148 
ASP   HXT  H  N N 149 
CYS   N    N  N N 150 
CYS   CA   C  N R 151 
CYS   C    C  N N 152 
CYS   O    O  N N 153 
CYS   CB   C  N N 154 
CYS   SG   S  N N 155 
CYS   OXT  O  N N 156 
CYS   H    H  N N 157 
CYS   H2   H  N N 158 
CYS   HA   H  N N 159 
CYS   HB2  H  N N 160 
CYS   HB3  H  N N 161 
CYS   HG   H  N N 162 
CYS   HXT  H  N N 163 
FMT   C    C  N N 164 
FMT   O1   O  N N 165 
FMT   O2   O  N N 166 
FMT   H    H  N N 167 
FMT   HO2  H  N N 168 
GLN   N    N  N N 169 
GLN   CA   C  N S 170 
GLN   C    C  N N 171 
GLN   O    O  N N 172 
GLN   CB   C  N N 173 
GLN   CG   C  N N 174 
GLN   CD   C  N N 175 
GLN   OE1  O  N N 176 
GLN   NE2  N  N N 177 
GLN   OXT  O  N N 178 
GLN   H    H  N N 179 
GLN   H2   H  N N 180 
GLN   HA   H  N N 181 
GLN   HB2  H  N N 182 
GLN   HB3  H  N N 183 
GLN   HG2  H  N N 184 
GLN   HG3  H  N N 185 
GLN   HE21 H  N N 186 
GLN   HE22 H  N N 187 
GLN   HXT  H  N N 188 
GLU   N    N  N N 189 
GLU   CA   C  N S 190 
GLU   C    C  N N 191 
GLU   O    O  N N 192 
GLU   CB   C  N N 193 
GLU   CG   C  N N 194 
GLU   CD   C  N N 195 
GLU   OE1  O  N N 196 
GLU   OE2  O  N N 197 
GLU   OXT  O  N N 198 
GLU   H    H  N N 199 
GLU   H2   H  N N 200 
GLU   HA   H  N N 201 
GLU   HB2  H  N N 202 
GLU   HB3  H  N N 203 
GLU   HG2  H  N N 204 
GLU   HG3  H  N N 205 
GLU   HE2  H  N N 206 
GLU   HXT  H  N N 207 
GLY   N    N  N N 208 
GLY   CA   C  N N 209 
GLY   C    C  N N 210 
GLY   O    O  N N 211 
GLY   OXT  O  N N 212 
GLY   H    H  N N 213 
GLY   H2   H  N N 214 
GLY   HA2  H  N N 215 
GLY   HA3  H  N N 216 
GLY   HXT  H  N N 217 
HIS   N    N  N N 218 
HIS   CA   C  N S 219 
HIS   C    C  N N 220 
HIS   O    O  N N 221 
HIS   CB   C  N N 222 
HIS   CG   C  Y N 223 
HIS   ND1  N  Y N 224 
HIS   CD2  C  Y N 225 
HIS   CE1  C  Y N 226 
HIS   NE2  N  Y N 227 
HIS   OXT  O  N N 228 
HIS   H    H  N N 229 
HIS   H2   H  N N 230 
HIS   HA   H  N N 231 
HIS   HB2  H  N N 232 
HIS   HB3  H  N N 233 
HIS   HD1  H  N N 234 
HIS   HD2  H  N N 235 
HIS   HE1  H  N N 236 
HIS   HE2  H  N N 237 
HIS   HXT  H  N N 238 
HOH   O    O  N N 239 
HOH   H1   H  N N 240 
HOH   H2   H  N N 241 
ILE   N    N  N N 242 
ILE   CA   C  N S 243 
ILE   C    C  N N 244 
ILE   O    O  N N 245 
ILE   CB   C  N S 246 
ILE   CG1  C  N N 247 
ILE   CG2  C  N N 248 
ILE   CD1  C  N N 249 
ILE   OXT  O  N N 250 
ILE   H    H  N N 251 
ILE   H2   H  N N 252 
ILE   HA   H  N N 253 
ILE   HB   H  N N 254 
ILE   HG12 H  N N 255 
ILE   HG13 H  N N 256 
ILE   HG21 H  N N 257 
ILE   HG22 H  N N 258 
ILE   HG23 H  N N 259 
ILE   HD11 H  N N 260 
ILE   HD12 H  N N 261 
ILE   HD13 H  N N 262 
ILE   HXT  H  N N 263 
LEU   N    N  N N 264 
LEU   CA   C  N S 265 
LEU   C    C  N N 266 
LEU   O    O  N N 267 
LEU   CB   C  N N 268 
LEU   CG   C  N N 269 
LEU   CD1  C  N N 270 
LEU   CD2  C  N N 271 
LEU   OXT  O  N N 272 
LEU   H    H  N N 273 
LEU   H2   H  N N 274 
LEU   HA   H  N N 275 
LEU   HB2  H  N N 276 
LEU   HB3  H  N N 277 
LEU   HG   H  N N 278 
LEU   HD11 H  N N 279 
LEU   HD12 H  N N 280 
LEU   HD13 H  N N 281 
LEU   HD21 H  N N 282 
LEU   HD22 H  N N 283 
LEU   HD23 H  N N 284 
LEU   HXT  H  N N 285 
LYS   N    N  N N 286 
LYS   CA   C  N S 287 
LYS   C    C  N N 288 
LYS   O    O  N N 289 
LYS   CB   C  N N 290 
LYS   CG   C  N N 291 
LYS   CD   C  N N 292 
LYS   CE   C  N N 293 
LYS   NZ   N  N N 294 
LYS   OXT  O  N N 295 
LYS   H    H  N N 296 
LYS   H2   H  N N 297 
LYS   HA   H  N N 298 
LYS   HB2  H  N N 299 
LYS   HB3  H  N N 300 
LYS   HG2  H  N N 301 
LYS   HG3  H  N N 302 
LYS   HD2  H  N N 303 
LYS   HD3  H  N N 304 
LYS   HE2  H  N N 305 
LYS   HE3  H  N N 306 
LYS   HZ1  H  N N 307 
LYS   HZ2  H  N N 308 
LYS   HZ3  H  N N 309 
LYS   HXT  H  N N 310 
MET   N    N  N N 311 
MET   CA   C  N S 312 
MET   C    C  N N 313 
MET   O    O  N N 314 
MET   CB   C  N N 315 
MET   CG   C  N N 316 
MET   SD   S  N N 317 
MET   CE   C  N N 318 
MET   OXT  O  N N 319 
MET   H    H  N N 320 
MET   H2   H  N N 321 
MET   HA   H  N N 322 
MET   HB2  H  N N 323 
MET   HB3  H  N N 324 
MET   HG2  H  N N 325 
MET   HG3  H  N N 326 
MET   HE1  H  N N 327 
MET   HE2  H  N N 328 
MET   HE3  H  N N 329 
MET   HXT  H  N N 330 
PHE   N    N  N N 331 
PHE   CA   C  N S 332 
PHE   C    C  N N 333 
PHE   O    O  N N 334 
PHE   CB   C  N N 335 
PHE   CG   C  Y N 336 
PHE   CD1  C  Y N 337 
PHE   CD2  C  Y N 338 
PHE   CE1  C  Y N 339 
PHE   CE2  C  Y N 340 
PHE   CZ   C  Y N 341 
PHE   OXT  O  N N 342 
PHE   H    H  N N 343 
PHE   H2   H  N N 344 
PHE   HA   H  N N 345 
PHE   HB2  H  N N 346 
PHE   HB3  H  N N 347 
PHE   HD1  H  N N 348 
PHE   HD2  H  N N 349 
PHE   HE1  H  N N 350 
PHE   HE2  H  N N 351 
PHE   HZ   H  N N 352 
PHE   HXT  H  N N 353 
PRO   N    N  N N 354 
PRO   CA   C  N S 355 
PRO   C    C  N N 356 
PRO   O    O  N N 357 
PRO   CB   C  N N 358 
PRO   CG   C  N N 359 
PRO   CD   C  N N 360 
PRO   OXT  O  N N 361 
PRO   H    H  N N 362 
PRO   HA   H  N N 363 
PRO   HB2  H  N N 364 
PRO   HB3  H  N N 365 
PRO   HG2  H  N N 366 
PRO   HG3  H  N N 367 
PRO   HD2  H  N N 368 
PRO   HD3  H  N N 369 
PRO   HXT  H  N N 370 
SER   N    N  N N 371 
SER   CA   C  N S 372 
SER   C    C  N N 373 
SER   O    O  N N 374 
SER   CB   C  N N 375 
SER   OG   O  N N 376 
SER   OXT  O  N N 377 
SER   H    H  N N 378 
SER   H2   H  N N 379 
SER   HA   H  N N 380 
SER   HB2  H  N N 381 
SER   HB3  H  N N 382 
SER   HG   H  N N 383 
SER   HXT  H  N N 384 
THR   N    N  N N 385 
THR   CA   C  N S 386 
THR   C    C  N N 387 
THR   O    O  N N 388 
THR   CB   C  N R 389 
THR   OG1  O  N N 390 
THR   CG2  C  N N 391 
THR   OXT  O  N N 392 
THR   H    H  N N 393 
THR   H2   H  N N 394 
THR   HA   H  N N 395 
THR   HB   H  N N 396 
THR   HG1  H  N N 397 
THR   HG21 H  N N 398 
THR   HG22 H  N N 399 
THR   HG23 H  N N 400 
THR   HXT  H  N N 401 
TRP   N    N  N N 402 
TRP   CA   C  N S 403 
TRP   C    C  N N 404 
TRP   O    O  N N 405 
TRP   CB   C  N N 406 
TRP   CG   C  Y N 407 
TRP   CD1  C  Y N 408 
TRP   CD2  C  Y N 409 
TRP   NE1  N  Y N 410 
TRP   CE2  C  Y N 411 
TRP   CE3  C  Y N 412 
TRP   CZ2  C  Y N 413 
TRP   CZ3  C  Y N 414 
TRP   CH2  C  Y N 415 
TRP   OXT  O  N N 416 
TRP   H    H  N N 417 
TRP   H2   H  N N 418 
TRP   HA   H  N N 419 
TRP   HB2  H  N N 420 
TRP   HB3  H  N N 421 
TRP   HD1  H  N N 422 
TRP   HE1  H  N N 423 
TRP   HE3  H  N N 424 
TRP   HZ2  H  N N 425 
TRP   HZ3  H  N N 426 
TRP   HH2  H  N N 427 
TRP   HXT  H  N N 428 
TYR   N    N  N N 429 
TYR   CA   C  N S 430 
TYR   C    C  N N 431 
TYR   O    O  N N 432 
TYR   CB   C  N N 433 
TYR   CG   C  Y N 434 
TYR   CD1  C  Y N 435 
TYR   CD2  C  Y N 436 
TYR   CE1  C  Y N 437 
TYR   CE2  C  Y N 438 
TYR   CZ   C  Y N 439 
TYR   OH   O  N N 440 
TYR   OXT  O  N N 441 
TYR   H    H  N N 442 
TYR   H2   H  N N 443 
TYR   HA   H  N N 444 
TYR   HB2  H  N N 445 
TYR   HB3  H  N N 446 
TYR   HD1  H  N N 447 
TYR   HD2  H  N N 448 
TYR   HE1  H  N N 449 
TYR   HE2  H  N N 450 
TYR   HH   H  N N 451 
TYR   HXT  H  N N 452 
VAL   N    N  N N 453 
VAL   CA   C  N S 454 
VAL   C    C  N N 455 
VAL   O    O  N N 456 
VAL   CB   C  N N 457 
VAL   CG1  C  N N 458 
VAL   CG2  C  N N 459 
VAL   OXT  O  N N 460 
VAL   H    H  N N 461 
VAL   H2   H  N N 462 
VAL   HA   H  N N 463 
VAL   HB   H  N N 464 
VAL   HG11 H  N N 465 
VAL   HG12 H  N N 466 
VAL   HG13 H  N N 467 
VAL   HG21 H  N N 468 
VAL   HG22 H  N N 469 
VAL   HG23 H  N N 470 
VAL   HXT  H  N N 471 
ZN    ZN   ZN N N 472 
# 
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 
A1H8T O15 P12  doub N N 1   
A1H8T C06 C07  doub Y N 2   
A1H8T C06 C05  sing Y N 3   
A1H8T C07 C08  sing Y N 4   
A1H8T O13 P12  sing N N 5   
A1H8T P12 C04  sing N N 6   
A1H8T P12 O14  sing N N 7   
A1H8T O01 C02  doub N N 8   
A1H8T C04 C05  sing N N 9   
A1H8T C04 N03  sing N N 10  
A1H8T C05 C10  doub Y N 11  
A1H8T C08 C09  doub Y N 12  
A1H8T C02 N03  sing N N 13  
A1H8T C02 C16  sing N N 14  
A1H8T C10 C09  sing Y N 15  
A1H8T C10 O11  sing N N 16  
A1H8T C16 S24  sing Y N 17  
A1H8T C16 C17  doub Y N 18  
A1H8T S24 C23  sing Y N 19  
A1H8T C17 C18  sing Y N 20  
A1H8T C23 C18  doub Y N 21  
A1H8T C23 C22  sing Y N 22  
A1H8T C18 C19  sing Y N 23  
A1H8T C22 C21  doub Y N 24  
A1H8T C19 C20  doub Y N 25  
A1H8T C21 C20  sing Y N 26  
A1H8T C17 H1   sing N N 27  
A1H8T C20 H2   sing N N 28  
A1H8T C21 H3   sing N N 29  
A1H8T C22 H4   sing N N 30  
A1H8T C19 H5   sing N N 31  
A1H8T C04 H6   sing N N 32  
A1H8T C06 H7   sing N N 33  
A1H8T C07 H8   sing N N 34  
A1H8T C08 H9   sing N N 35  
A1H8T C09 H10  sing N N 36  
A1H8T N03 H11  sing N N 37  
A1H8T O11 H12  sing N N 38  
A1H8T O13 H13  sing N N 39  
A1H8T O14 H14  sing N N 40  
A1IKA C20 C21  sing Y N 41  
A1IKA C20 C19  doub Y N 42  
A1IKA C21 C22  doub Y N 43  
A1IKA C19 C18  sing Y N 44  
A1IKA C22 C23  sing Y N 45  
A1IKA C18 C23  doub Y N 46  
A1IKA C18 C17  sing Y N 47  
A1IKA C23 S24  sing Y N 48  
A1IKA C17 C16  doub Y N 49  
A1IKA S24 C16  sing Y N 50  
A1IKA C16 C02  sing N N 51  
A1IKA C02 O01  doub N N 52  
A1IKA C02 N03  sing N N 53  
A1IKA N03 C04  sing N N 54  
A1IKA C06 C07  doub Y N 55  
A1IKA C06 C05  sing Y N 56  
A1IKA C07 C08  sing Y N 57  
A1IKA C04 C05  sing N N 58  
A1IKA C04 P12  sing N N 59  
A1IKA C05 C10  doub Y N 60  
A1IKA O14 P12  doub N N 61  
A1IKA C08 C09  doub Y N 62  
A1IKA P12 O13  sing N N 63  
A1IKA P12 O15  sing N N 64  
A1IKA C10 C09  sing Y N 65  
A1IKA C10 O11  sing N N 66  
A1IKA C04 H1   sing N N 67  
A1IKA C06 H2   sing N N 68  
A1IKA C07 H3   sing N N 69  
A1IKA C08 H4   sing N N 70  
A1IKA C09 H5   sing N N 71  
A1IKA C17 H6   sing N N 72  
A1IKA C19 H7   sing N N 73  
A1IKA C20 H8   sing N N 74  
A1IKA C21 H9   sing N N 75  
A1IKA C22 H10  sing N N 76  
A1IKA N03 H11  sing N N 77  
A1IKA O11 H12  sing N N 78  
A1IKA O13 H13  sing N N 79  
A1IKA O15 H14  sing N N 80  
ALA   N   CA   sing N N 81  
ALA   N   H    sing N N 82  
ALA   N   H2   sing N N 83  
ALA   CA  C    sing N N 84  
ALA   CA  CB   sing N N 85  
ALA   CA  HA   sing N N 86  
ALA   C   O    doub N N 87  
ALA   C   OXT  sing N N 88  
ALA   CB  HB1  sing N N 89  
ALA   CB  HB2  sing N N 90  
ALA   CB  HB3  sing N N 91  
ALA   OXT HXT  sing N N 92  
ARG   N   CA   sing N N 93  
ARG   N   H    sing N N 94  
ARG   N   H2   sing N N 95  
ARG   CA  C    sing N N 96  
ARG   CA  CB   sing N N 97  
ARG   CA  HA   sing N N 98  
ARG   C   O    doub N N 99  
ARG   C   OXT  sing N N 100 
ARG   CB  CG   sing N N 101 
ARG   CB  HB2  sing N N 102 
ARG   CB  HB3  sing N N 103 
ARG   CG  CD   sing N N 104 
ARG   CG  HG2  sing N N 105 
ARG   CG  HG3  sing N N 106 
ARG   CD  NE   sing N N 107 
ARG   CD  HD2  sing N N 108 
ARG   CD  HD3  sing N N 109 
ARG   NE  CZ   sing N N 110 
ARG   NE  HE   sing N N 111 
ARG   CZ  NH1  sing N N 112 
ARG   CZ  NH2  doub N N 113 
ARG   NH1 HH11 sing N N 114 
ARG   NH1 HH12 sing N N 115 
ARG   NH2 HH21 sing N N 116 
ARG   NH2 HH22 sing N N 117 
ARG   OXT HXT  sing N N 118 
ASN   N   CA   sing N N 119 
ASN   N   H    sing N N 120 
ASN   N   H2   sing N N 121 
ASN   CA  C    sing N N 122 
ASN   CA  CB   sing N N 123 
ASN   CA  HA   sing N N 124 
ASN   C   O    doub N N 125 
ASN   C   OXT  sing N N 126 
ASN   CB  CG   sing N N 127 
ASN   CB  HB2  sing N N 128 
ASN   CB  HB3  sing N N 129 
ASN   CG  OD1  doub N N 130 
ASN   CG  ND2  sing N N 131 
ASN   ND2 HD21 sing N N 132 
ASN   ND2 HD22 sing N N 133 
ASN   OXT HXT  sing N N 134 
ASP   N   CA   sing N N 135 
ASP   N   H    sing N N 136 
ASP   N   H2   sing N N 137 
ASP   CA  C    sing N N 138 
ASP   CA  CB   sing N N 139 
ASP   CA  HA   sing N N 140 
ASP   C   O    doub N N 141 
ASP   C   OXT  sing N N 142 
ASP   CB  CG   sing N N 143 
ASP   CB  HB2  sing N N 144 
ASP   CB  HB3  sing N N 145 
ASP   CG  OD1  doub N N 146 
ASP   CG  OD2  sing N N 147 
ASP   OD2 HD2  sing N N 148 
ASP   OXT HXT  sing N N 149 
CYS   N   CA   sing N N 150 
CYS   N   H    sing N N 151 
CYS   N   H2   sing N N 152 
CYS   CA  C    sing N N 153 
CYS   CA  CB   sing N N 154 
CYS   CA  HA   sing N N 155 
CYS   C   O    doub N N 156 
CYS   C   OXT  sing N N 157 
CYS   CB  SG   sing N N 158 
CYS   CB  HB2  sing N N 159 
CYS   CB  HB3  sing N N 160 
CYS   SG  HG   sing N N 161 
CYS   OXT HXT  sing N N 162 
FMT   C   O1   doub N N 163 
FMT   C   O2   sing N N 164 
FMT   C   H    sing N N 165 
FMT   O2  HO2  sing N N 166 
GLN   N   CA   sing N N 167 
GLN   N   H    sing N N 168 
GLN   N   H2   sing N N 169 
GLN   CA  C    sing N N 170 
GLN   CA  CB   sing N N 171 
GLN   CA  HA   sing N N 172 
GLN   C   O    doub N N 173 
GLN   C   OXT  sing N N 174 
GLN   CB  CG   sing N N 175 
GLN   CB  HB2  sing N N 176 
GLN   CB  HB3  sing N N 177 
GLN   CG  CD   sing N N 178 
GLN   CG  HG2  sing N N 179 
GLN   CG  HG3  sing N N 180 
GLN   CD  OE1  doub N N 181 
GLN   CD  NE2  sing N N 182 
GLN   NE2 HE21 sing N N 183 
GLN   NE2 HE22 sing N N 184 
GLN   OXT HXT  sing N N 185 
GLU   N   CA   sing N N 186 
GLU   N   H    sing N N 187 
GLU   N   H2   sing N N 188 
GLU   CA  C    sing N N 189 
GLU   CA  CB   sing N N 190 
GLU   CA  HA   sing N N 191 
GLU   C   O    doub N N 192 
GLU   C   OXT  sing N N 193 
GLU   CB  CG   sing N N 194 
GLU   CB  HB2  sing N N 195 
GLU   CB  HB3  sing N N 196 
GLU   CG  CD   sing N N 197 
GLU   CG  HG2  sing N N 198 
GLU   CG  HG3  sing N N 199 
GLU   CD  OE1  doub N N 200 
GLU   CD  OE2  sing N N 201 
GLU   OE2 HE2  sing N N 202 
GLU   OXT HXT  sing N N 203 
GLY   N   CA   sing N N 204 
GLY   N   H    sing N N 205 
GLY   N   H2   sing N N 206 
GLY   CA  C    sing N N 207 
GLY   CA  HA2  sing N N 208 
GLY   CA  HA3  sing N N 209 
GLY   C   O    doub N N 210 
GLY   C   OXT  sing N N 211 
GLY   OXT HXT  sing N N 212 
HIS   N   CA   sing N N 213 
HIS   N   H    sing N N 214 
HIS   N   H2   sing N N 215 
HIS   CA  C    sing N N 216 
HIS   CA  CB   sing N N 217 
HIS   CA  HA   sing N N 218 
HIS   C   O    doub N N 219 
HIS   C   OXT  sing N N 220 
HIS   CB  CG   sing N N 221 
HIS   CB  HB2  sing N N 222 
HIS   CB  HB3  sing N N 223 
HIS   CG  ND1  sing Y N 224 
HIS   CG  CD2  doub Y N 225 
HIS   ND1 CE1  doub Y N 226 
HIS   ND1 HD1  sing N N 227 
HIS   CD2 NE2  sing Y N 228 
HIS   CD2 HD2  sing N N 229 
HIS   CE1 NE2  sing Y N 230 
HIS   CE1 HE1  sing N N 231 
HIS   NE2 HE2  sing N N 232 
HIS   OXT HXT  sing N N 233 
HOH   O   H1   sing N N 234 
HOH   O   H2   sing N N 235 
ILE   N   CA   sing N N 236 
ILE   N   H    sing N N 237 
ILE   N   H2   sing N N 238 
ILE   CA  C    sing N N 239 
ILE   CA  CB   sing N N 240 
ILE   CA  HA   sing N N 241 
ILE   C   O    doub N N 242 
ILE   C   OXT  sing N N 243 
ILE   CB  CG1  sing N N 244 
ILE   CB  CG2  sing N N 245 
ILE   CB  HB   sing N N 246 
ILE   CG1 CD1  sing N N 247 
ILE   CG1 HG12 sing N N 248 
ILE   CG1 HG13 sing N N 249 
ILE   CG2 HG21 sing N N 250 
ILE   CG2 HG22 sing N N 251 
ILE   CG2 HG23 sing N N 252 
ILE   CD1 HD11 sing N N 253 
ILE   CD1 HD12 sing N N 254 
ILE   CD1 HD13 sing N N 255 
ILE   OXT HXT  sing N N 256 
LEU   N   CA   sing N N 257 
LEU   N   H    sing N N 258 
LEU   N   H2   sing N N 259 
LEU   CA  C    sing N N 260 
LEU   CA  CB   sing N N 261 
LEU   CA  HA   sing N N 262 
LEU   C   O    doub N N 263 
LEU   C   OXT  sing N N 264 
LEU   CB  CG   sing N N 265 
LEU   CB  HB2  sing N N 266 
LEU   CB  HB3  sing N N 267 
LEU   CG  CD1  sing N N 268 
LEU   CG  CD2  sing N N 269 
LEU   CG  HG   sing N N 270 
LEU   CD1 HD11 sing N N 271 
LEU   CD1 HD12 sing N N 272 
LEU   CD1 HD13 sing N N 273 
LEU   CD2 HD21 sing N N 274 
LEU   CD2 HD22 sing N N 275 
LEU   CD2 HD23 sing N N 276 
LEU   OXT HXT  sing N N 277 
LYS   N   CA   sing N N 278 
LYS   N   H    sing N N 279 
LYS   N   H2   sing N N 280 
LYS   CA  C    sing N N 281 
LYS   CA  CB   sing N N 282 
LYS   CA  HA   sing N N 283 
LYS   C   O    doub N N 284 
LYS   C   OXT  sing N N 285 
LYS   CB  CG   sing N N 286 
LYS   CB  HB2  sing N N 287 
LYS   CB  HB3  sing N N 288 
LYS   CG  CD   sing N N 289 
LYS   CG  HG2  sing N N 290 
LYS   CG  HG3  sing N N 291 
LYS   CD  CE   sing N N 292 
LYS   CD  HD2  sing N N 293 
LYS   CD  HD3  sing N N 294 
LYS   CE  NZ   sing N N 295 
LYS   CE  HE2  sing N N 296 
LYS   CE  HE3  sing N N 297 
LYS   NZ  HZ1  sing N N 298 
LYS   NZ  HZ2  sing N N 299 
LYS   NZ  HZ3  sing N N 300 
LYS   OXT HXT  sing N N 301 
MET   N   CA   sing N N 302 
MET   N   H    sing N N 303 
MET   N   H2   sing N N 304 
MET   CA  C    sing N N 305 
MET   CA  CB   sing N N 306 
MET   CA  HA   sing N N 307 
MET   C   O    doub N N 308 
MET   C   OXT  sing N N 309 
MET   CB  CG   sing N N 310 
MET   CB  HB2  sing N N 311 
MET   CB  HB3  sing N N 312 
MET   CG  SD   sing N N 313 
MET   CG  HG2  sing N N 314 
MET   CG  HG3  sing N N 315 
MET   SD  CE   sing N N 316 
MET   CE  HE1  sing N N 317 
MET   CE  HE2  sing N N 318 
MET   CE  HE3  sing N N 319 
MET   OXT HXT  sing N N 320 
PHE   N   CA   sing N N 321 
PHE   N   H    sing N N 322 
PHE   N   H2   sing N N 323 
PHE   CA  C    sing N N 324 
PHE   CA  CB   sing N N 325 
PHE   CA  HA   sing N N 326 
PHE   C   O    doub N N 327 
PHE   C   OXT  sing N N 328 
PHE   CB  CG   sing N N 329 
PHE   CB  HB2  sing N N 330 
PHE   CB  HB3  sing N N 331 
PHE   CG  CD1  doub Y N 332 
PHE   CG  CD2  sing Y N 333 
PHE   CD1 CE1  sing Y N 334 
PHE   CD1 HD1  sing N N 335 
PHE   CD2 CE2  doub Y N 336 
PHE   CD2 HD2  sing N N 337 
PHE   CE1 CZ   doub Y N 338 
PHE   CE1 HE1  sing N N 339 
PHE   CE2 CZ   sing Y N 340 
PHE   CE2 HE2  sing N N 341 
PHE   CZ  HZ   sing N N 342 
PHE   OXT HXT  sing N N 343 
PRO   N   CA   sing N N 344 
PRO   N   CD   sing N N 345 
PRO   N   H    sing N N 346 
PRO   CA  C    sing N N 347 
PRO   CA  CB   sing N N 348 
PRO   CA  HA   sing N N 349 
PRO   C   O    doub N N 350 
PRO   C   OXT  sing N N 351 
PRO   CB  CG   sing N N 352 
PRO   CB  HB2  sing N N 353 
PRO   CB  HB3  sing N N 354 
PRO   CG  CD   sing N N 355 
PRO   CG  HG2  sing N N 356 
PRO   CG  HG3  sing N N 357 
PRO   CD  HD2  sing N N 358 
PRO   CD  HD3  sing N N 359 
PRO   OXT HXT  sing N N 360 
SER   N   CA   sing N N 361 
SER   N   H    sing N N 362 
SER   N   H2   sing N N 363 
SER   CA  C    sing N N 364 
SER   CA  CB   sing N N 365 
SER   CA  HA   sing N N 366 
SER   C   O    doub N N 367 
SER   C   OXT  sing N N 368 
SER   CB  OG   sing N N 369 
SER   CB  HB2  sing N N 370 
SER   CB  HB3  sing N N 371 
SER   OG  HG   sing N N 372 
SER   OXT HXT  sing N N 373 
THR   N   CA   sing N N 374 
THR   N   H    sing N N 375 
THR   N   H2   sing N N 376 
THR   CA  C    sing N N 377 
THR   CA  CB   sing N N 378 
THR   CA  HA   sing N N 379 
THR   C   O    doub N N 380 
THR   C   OXT  sing N N 381 
THR   CB  OG1  sing N N 382 
THR   CB  CG2  sing N N 383 
THR   CB  HB   sing N N 384 
THR   OG1 HG1  sing N N 385 
THR   CG2 HG21 sing N N 386 
THR   CG2 HG22 sing N N 387 
THR   CG2 HG23 sing N N 388 
THR   OXT HXT  sing N N 389 
TRP   N   CA   sing N N 390 
TRP   N   H    sing N N 391 
TRP   N   H2   sing N N 392 
TRP   CA  C    sing N N 393 
TRP   CA  CB   sing N N 394 
TRP   CA  HA   sing N N 395 
TRP   C   O    doub N N 396 
TRP   C   OXT  sing N N 397 
TRP   CB  CG   sing N N 398 
TRP   CB  HB2  sing N N 399 
TRP   CB  HB3  sing N N 400 
TRP   CG  CD1  doub Y N 401 
TRP   CG  CD2  sing Y N 402 
TRP   CD1 NE1  sing Y N 403 
TRP   CD1 HD1  sing N N 404 
TRP   CD2 CE2  doub Y N 405 
TRP   CD2 CE3  sing Y N 406 
TRP   NE1 CE2  sing Y N 407 
TRP   NE1 HE1  sing N N 408 
TRP   CE2 CZ2  sing Y N 409 
TRP   CE3 CZ3  doub Y N 410 
TRP   CE3 HE3  sing N N 411 
TRP   CZ2 CH2  doub Y N 412 
TRP   CZ2 HZ2  sing N N 413 
TRP   CZ3 CH2  sing Y N 414 
TRP   CZ3 HZ3  sing N N 415 
TRP   CH2 HH2  sing N N 416 
TRP   OXT HXT  sing N N 417 
TYR   N   CA   sing N N 418 
TYR   N   H    sing N N 419 
TYR   N   H2   sing N N 420 
TYR   CA  C    sing N N 421 
TYR   CA  CB   sing N N 422 
TYR   CA  HA   sing N N 423 
TYR   C   O    doub N N 424 
TYR   C   OXT  sing N N 425 
TYR   CB  CG   sing N N 426 
TYR   CB  HB2  sing N N 427 
TYR   CB  HB3  sing N N 428 
TYR   CG  CD1  doub Y N 429 
TYR   CG  CD2  sing Y N 430 
TYR   CD1 CE1  sing Y N 431 
TYR   CD1 HD1  sing N N 432 
TYR   CD2 CE2  doub Y N 433 
TYR   CD2 HD2  sing N N 434 
TYR   CE1 CZ   doub Y N 435 
TYR   CE1 HE1  sing N N 436 
TYR   CE2 CZ   sing Y N 437 
TYR   CE2 HE2  sing N N 438 
TYR   CZ  OH   sing N N 439 
TYR   OH  HH   sing N N 440 
TYR   OXT HXT  sing N N 441 
VAL   N   CA   sing N N 442 
VAL   N   H    sing N N 443 
VAL   N   H2   sing N N 444 
VAL   CA  C    sing N N 445 
VAL   CA  CB   sing N N 446 
VAL   CA  HA   sing N N 447 
VAL   C   O    doub N N 448 
VAL   C   OXT  sing N N 449 
VAL   CB  CG1  sing N N 450 
VAL   CB  CG2  sing N N 451 
VAL   CB  HB   sing N N 452 
VAL   CG1 HG11 sing N N 453 
VAL   CG1 HG12 sing N N 454 
VAL   CG1 HG13 sing N N 455 
VAL   CG2 HG21 sing N N 456 
VAL   CG2 HG22 sing N N 457 
VAL   CG2 HG23 sing N N 458 
VAL   OXT HXT  sing N N 459 
# 
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                    9F0P 
_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]   0.009790 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008430 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012655 
_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]   0.019436 
_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.
;
? 
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  ? 36.14300  -14.96200 12.05800  1.000 40.95965 ? 32  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 20  ? 36.85200  -13.72700 12.36600  1.000 35.58246 ? 32  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 20  ? 35.93800  -12.49800 12.25900  1.000 36.28772 ? 32  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 20  ? 36.06000  -11.57000 13.04800  1.000 31.92451 ? 32  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 20  ? 38.07800  -13.57400 11.45900  1.000 41.87881 ? 32  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 20  ? 37.79500  -13.77900 9.96800   1.000 47.31889 ? 32  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 20  ? 39.05800  -13.96500 9.12900   1.000 70.07050 ? 32  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 20  ? 39.57600  -15.10200 9.07000   1.000 73.70563 ? 32  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 20  ? 39.54000  -12.98200 8.52700   1.000 73.27705 ? 32  GLU   A OE2 1 
ATOM   10   N  N   . TYR   A 1 21  ? 35.03700  -12.49600 11.27700  1.000 34.53248 ? 33  TYR   A N   1 
ATOM   11   C  CA  . TYR   A 1 21  ? 34.12600  -11.36100 11.10200  1.000 26.27892 ? 33  TYR   A CA  1 
ATOM   12   C  C   . TYR   A 1 21  ? 33.18200  -11.27700 12.29200  1.000 23.42796 ? 33  TYR   A C   1 
ATOM   13   O  O   . TYR   A 1 21  ? 32.58300  -12.28800 12.67000  1.000 31.33125 ? 33  TYR   A O   1 
ATOM   14   C  CB  . TYR   A 1 21  ? 33.28900  -11.52400 9.83400   1.000 23.66498 ? 33  TYR   A CB  1 
ATOM   15   C  CG  . TYR   A 1 21  ? 32.70800  -10.21000 9.33400   1.000 19.20235 ? 33  TYR   A CG  1 
ATOM   16   C  CD1 . TYR   A 1 21  ? 33.47600  -9.35000  8.56900   1.000 20.06197 ? 33  TYR   A CD1 1 
ATOM   17   C  CD2 . TYR   A 1 21  ? 31.40800  -9.82700  9.65300   1.000 18.54425 ? 33  TYR   A CD2 1 
ATOM   18   C  CE1 . TYR   A 1 21  ? 32.96300  -8.15000  8.10600   1.000 19.11564 ? 33  TYR   A CE1 1 
ATOM   19   C  CE2 . TYR   A 1 21  ? 30.87700  -8.60100  9.19100   1.000 17.88444 ? 33  TYR   A CE2 1 
ATOM   20   C  CZ  . TYR   A 1 21  ? 31.66700  -7.78800  8.42600   1.000 17.60422 ? 33  TYR   A CZ  1 
ATOM   21   O  OH  . TYR   A 1 21  ? 31.17500  -6.59400  7.96200   1.000 18.06441 ? 33  TYR   A OH  1 
ATOM   22   N  N   . PRO   A 1 22  ? 33.01000  -10.10100 12.90100  1.000 25.48631 ? 34  PRO   A N   1 
ATOM   23   C  CA  . PRO   A 1 22  ? 32.14200  -10.01300 14.08000  1.000 26.33330 ? 34  PRO   A CA  1 
ATOM   24   C  C   . PRO   A 1 22  ? 30.68900  -10.24900 13.71400  1.000 35.00391 ? 34  PRO   A C   1 
ATOM   25   O  O   . PRO   A 1 22  ? 30.20100  -9.78900  12.67700  1.000 27.68812 ? 34  PRO   A O   1 
ATOM   26   C  CB  . PRO   A 1 22  ? 32.36700  -8.58600  14.59300  1.000 32.37434 ? 34  PRO   A CB  1 
ATOM   27   C  CG  . PRO   A 1 22  ? 32.83900  -7.83500  13.42500  1.000 27.37739 ? 34  PRO   A CG  1 
ATOM   28   C  CD  . PRO   A 1 22  ? 33.60900  -8.80200  12.56000  1.000 24.93419 ? 34  PRO   A CD  1 
ATOM   29   N  N   . THR   A 1 23  ? 30.00600  -10.99000 14.57500  1.000 35.41451 ? 35  THR   A N   1 
ATOM   30   C  CA  . THR   A 1 23  ? 28.61200  -11.35000 14.38600  1.000 37.09484 ? 35  THR   A CA  1 
ATOM   31   C  C   . THR   A 1 23  ? 27.74500  -10.57300 15.36300  1.000 29.36543 ? 35  THR   A C   1 
ATOM   32   O  O   . THR   A 1 23  ? 28.23800  -9.89300  16.26700  1.000 39.51652 ? 35  THR   A O   1 
ATOM   33   C  CB  . THR   A 1 23  ? 28.41200  -12.86400 14.54400  1.000 31.98023 ? 35  THR   A CB  1 
ATOM   34   O  OG1 . THR   A 1 23  ? 28.51000  -13.22000 15.92900  1.000 42.33818 ? 35  THR   A OG1 1 
ATOM   35   C  CG2 . THR   A 1 23  ? 29.46300  -13.62200 13.75400  1.000 38.42419 ? 35  THR   A CG2 1 
ATOM   36   N  N   . VAL   A 1 24  ? 26.42900  -10.68900 15.15700  1.000 43.53603 ? 36  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 24  ? 25.45300  -9.91700  15.92600  1.000 36.82862 ? 36  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 24  ? 25.67700  -10.08300 17.42000  1.000 39.36194 ? 36  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 24  ? 25.64300  -9.10800  18.18000  1.000 45.74853 ? 36  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 24  ? 24.02300  -10.33600 15.54200  1.000 39.01835 ? 36  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 24  ? 23.07900  -9.15000  15.64700  1.000 28.85055 ? 36  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 24  ? 23.99800  -10.98100 14.16900  1.000 35.53863 ? 36  VAL   A CG2 1 
ATOM   43   N  N   . SER   A 1 25  ? 25.89200  -11.32200 17.86300  1.000 49.74770 ? 37  SER   A N   1 
ATOM   44   C  CA  . SER   A 1 25  ? 25.97700  -11.62900 19.28500  1.000 54.68334 ? 37  SER   A CA  1 
ATOM   45   C  C   . SER   A 1 25  ? 27.27800  -11.16100 19.92100  1.000 53.70458 ? 37  SER   A C   1 
ATOM   46   O  O   . SER   A 1 25  ? 27.32500  -10.99000 21.14500  1.000 54.47817 ? 37  SER   A O   1 
ATOM   47   C  CB  . SER   A 1 25  ? 25.82000  -13.13800 19.49800  1.000 48.09498 ? 37  SER   A CB  1 
ATOM   48   O  OG  . SER   A 1 25  ? 25.21100  -13.42000 20.74600  1.000 54.09529 ? 37  SER   A OG  1 
ATOM   49   N  N   . GLU   A 1 26  ? 28.32600  -10.95300 19.12700  1.000 50.69694 ? 38  GLU   A N   1 
ATOM   50   C  CA  . GLU   A 1 26  ? 29.64200  -10.60300 19.64300  1.000 45.88109 ? 38  GLU   A CA  1 
ATOM   51   C  C   . GLU   A 1 26  ? 29.86100  -9.10100  19.77000  1.000 42.20550 ? 38  GLU   A C   1 
ATOM   52   O  O   . GLU   A 1 26  ? 30.91100  -8.68200  20.26500  1.000 52.09825 ? 38  GLU   A O   1 
ATOM   53   C  CB  . GLU   A 1 26  ? 30.73300  -11.23800 18.77100  1.000 41.86374 ? 38  GLU   A CB  1 
ATOM   54   C  CG  . GLU   A 1 26  ? 30.57400  -12.74300 18.61600  1.000 41.34969 ? 38  GLU   A CG  1 
ATOM   55   C  CD  . GLU   A 1 26  ? 31.28700  -13.29600 17.39700  1.000 53.53808 ? 38  GLU   A CD  1 
ATOM   56   O  OE1 . GLU   A 1 26  ? 31.84800  -12.49800 16.61500  1.000 43.40733 ? 38  GLU   A OE1 1 
ATOM   57   O  OE2 . GLU   A 1 26  ? 31.28100  -14.53400 17.21700  1.000 60.93436 ? 38  GLU   A OE2 1 
ATOM   58   N  N   . ILE   A 1 27  ? 28.90100  -8.28300  19.35000  1.000 44.37999 ? 39  ILE   A N   1 
ATOM   59   C  CA  . ILE   A 1 27  ? 29.03000  -6.83300  19.45600  1.000 47.80195 ? 39  ILE   A CA  1 
ATOM   60   C  C   . ILE   A 1 27  ? 27.99900  -6.29200  20.43700  1.000 51.60486 ? 39  ILE   A C   1 
ATOM   61   O  O   . ILE   A 1 27  ? 26.80800  -6.21500  20.10000  1.000 50.78575 ? 39  ILE   A O   1 
ATOM   62   C  CB  . ILE   A 1 27  ? 28.89900  -6.14800  18.08600  1.000 44.70395 ? 39  ILE   A CB  1 
ATOM   63   C  CG1 . ILE   A 1 27  ? 29.87800  -6.76100  17.09000  1.000 37.59531 ? 39  ILE   A CG1 1 
ATOM   64   C  CG2 . ILE   A 1 27  ? 29.10600  -4.64400  18.21000  1.000 43.49152 ? 39  ILE   A CG2 1 
ATOM   65   C  CD1 . ILE   A 1 27  ? 29.72600  -6.20200  15.70000  1.000 31.99697 ? 39  ILE   A CD1 1 
ATOM   66   N  N   . PRO   A 1 28  ? 28.40500  -5.93100  21.65300  1.000 53.33575 ? 40  PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 28  ? 27.49400  -5.22800  22.56200  1.000 47.12653 ? 40  PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 28  ? 26.79600  -4.08300  21.84600  1.000 50.46014 ? 40  PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 28  ? 27.42200  -3.30200  21.12400  1.000 49.59939 ? 40  PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 28  ? 28.43500  -4.71500  23.65300  1.000 49.46762 ? 40  PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 28  ? 29.48100  -5.78100  23.73700  1.000 56.22014 ? 40  PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 28  ? 29.67200  -6.28900  22.31600  1.000 55.33454 ? 40  PRO   A CD  1 
ATOM   73   N  N   . VAL   A 1 29  ? 25.47600  -4.00500  22.03200  1.000 57.61288 ? 41  VAL   A N   1 
ATOM   74   C  CA  . VAL   A 1 29  ? 24.68400  -2.99000  21.35000  1.000 50.15005 ? 41  VAL   A CA  1 
ATOM   75   C  C   . VAL   A 1 29  ? 25.21700  -1.60500  21.68600  1.000 50.32283 ? 41  VAL   A C   1 
ATOM   76   O  O   . VAL   A 1 29  ? 25.62200  -1.32900  22.82300  1.000 55.36654 ? 41  VAL   A O   1 
ATOM   77   C  CB  . VAL   A 1 29  ? 23.20000  -3.13200  21.72800  1.000 55.74734 ? 41  VAL   A CB  1 
ATOM   78   C  CG1 . VAL   A 1 29  ? 22.57300  -4.29900  20.97600  1.000 57.03069 ? 41  VAL   A CG1 1 
ATOM   79   C  CG2 . VAL   A 1 29  ? 23.05000  -3.31300  23.23200  1.000 58.42206 ? 41  VAL   A CG2 1 
ATOM   80   N  N   . GLY   A 1 30  ? 25.22500  -0.72500  20.68500  1.000 47.14242 ? 42  GLY   A N   1 
ATOM   81   C  CA  . GLY   A 1 30  ? 25.75500  0.61100   20.83400  1.000 37.79027 ? 42  GLY   A CA  1 
ATOM   82   C  C   . GLY   A 1 30  ? 27.22100  0.75100   20.48200  1.000 33.14560 ? 42  GLY   A C   1 
ATOM   83   O  O   . GLY   A 1 30  ? 27.69700  1.88300   20.31900  1.000 35.43612 ? 42  GLY   A O   1 
ATOM   84   N  N   A GLU   A 1 31  ? 27.94800  -0.35600  20.37000  0.659 36.71880 ? 43  GLU   A N   1 
ATOM   85   N  N   B GLU   A 1 31  ? 27.94600  -0.35500  20.36400  0.341 36.68677 ? 43  GLU   A N   1 
ATOM   86   C  CA  A GLU   A 1 31  ? 29.35500  -0.33700  20.00900  0.659 33.22240 ? 43  GLU   A CA  1 
ATOM   87   C  CA  B GLU   A 1 31  ? 29.35300  -0.32800  20.00700  0.341 33.33716 ? 43  GLU   A CA  1 
ATOM   88   C  C   A GLU   A 1 31  ? 29.50700  -0.51500  18.50100  0.659 31.95672 ? 43  GLU   A C   1 
ATOM   89   C  C   B GLU   A 1 31  ? 29.50400  -0.50800  18.50100  0.341 31.92614 ? 43  GLU   A C   1 
ATOM   90   O  O   A GLU   A 1 31  ? 28.57800  -0.92400  17.79800  0.659 29.03877 ? 43  GLU   A O   1 
ATOM   91   O  O   B GLU   A 1 31  ? 28.57400  -0.91400  17.80000  0.341 29.15675 ? 43  GLU   A O   1 
ATOM   92   C  CB  A GLU   A 1 31  ? 30.11200  -1.44600  20.74300  0.659 34.68729 ? 43  GLU   A CB  1 
ATOM   93   C  CB  B GLU   A 1 31  ? 30.10600  -1.44000  20.73800  0.341 34.75922 ? 43  GLU   A CB  1 
ATOM   94   C  CG  A GLU   A 1 31  ? 30.18400  -1.24200  22.25400  0.659 39.87366 ? 43  GLU   A CG  1 
ATOM   95   C  CG  B GLU   A 1 31  ? 30.14500  -1.28300  22.25600  0.341 39.78646 ? 43  GLU   A CG  1 
ATOM   96   C  CD  A GLU   A 1 31  ? 30.98700  -2.31600  22.96700  0.659 38.76542 ? 43  GLU   A CD  1 
ATOM   97   C  CD  B GLU   A 1 31  ? 30.77300  0.02600   22.70100  0.341 35.72420 ? 43  GLU   A CD  1 
ATOM   98   O  OE1 A GLU   A 1 31  ? 31.74900  -3.04900  22.30100  0.659 35.96090 ? 43  GLU   A OE1 1 
ATOM   99   O  OE1 B GLU   A 1 31  ? 31.77800  0.44800   22.09100  0.341 38.52750 ? 43  GLU   A OE1 1 
ATOM   100  O  OE2 A GLU   A 1 31  ? 30.84700  -2.43400  24.20200  0.659 38.97978 ? 43  GLU   A OE2 1 
ATOM   101  O  OE2 B GLU   A 1 31  ? 30.26300  0.63400   23.66500  0.341 40.39264 ? 43  GLU   A OE2 1 
ATOM   102  N  N   . VAL   A 1 32  ? 30.69600  -0.19300  18.00400  1.000 23.37705 ? 44  VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 32  ? 31.00800  -0.33900  16.58900  1.000 19.59990 ? 44  VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 32  ? 32.33800  -1.06400  16.48000  1.000 22.34103 ? 44  VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 32  ? 33.30300  -0.70000  17.16200  1.000 23.93851 ? 44  VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 32  ? 31.07200  1.01900   15.86300  1.000 19.78938 ? 44  VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 32  ? 31.59200  0.83600   14.43700  1.000 19.60225 ? 44  VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 32  ? 29.70600  1.69900   15.85500  1.000 22.10593 ? 44  VAL   A CG2 1 
ATOM   109  N  N   . ARG   A 1 33  ? 32.38800  -2.09300  15.64600  1.000 17.97691 ? 45  ARG   A N   1 
ATOM   110  C  CA  . ARG   A 1 33  ? 33.62800  -2.77700  15.33400  1.000 20.93050 ? 45  ARG   A CA  1 
ATOM   111  C  C   . ARG   A 1 33  ? 34.07600  -2.43500  13.92200  1.000 17.01987 ? 45  ARG   A C   1 
ATOM   112  O  O   . ARG   A 1 33  ? 33.25500  -2.17400  13.03100  1.000 17.35090 ? 45  ARG   A O   1 
ATOM   113  C  CB  . ARG   A 1 33  ? 33.46400  -4.29700  15.42100  1.000 22.68356 ? 45  ARG   A CB  1 
ATOM   114  C  CG  . ARG   A 1 33  ? 33.03400  -4.80700  16.78100  1.000 31.99992 ? 45  ARG   A CG  1 
ATOM   115  C  CD  . ARG   A 1 33  ? 34.20600  -4.87300  17.74700  1.000 38.18110 ? 45  ARG   A CD  1 
ATOM   116  N  NE  . ARG   A 1 33  ? 33.80700  -5.43800  19.03400  1.000 52.34716 ? 45  ARG   A NE  1 
ATOM   117  C  CZ  . ARG   A 1 33  ? 33.36100  -4.74800  20.07700  1.000 50.32997 ? 45  ARG   A CZ  1 
ATOM   118  N  NH1 . ARG   A 1 33  ? 33.23700  -3.42800  20.04200  1.000 42.52687 ? 45  ARG   A NH1 1 
ATOM   119  N  NH2 . ARG   A 1 33  ? 33.02000  -5.40100  21.18500  1.000 52.75583 ? 45  ARG   A NH2 1 
ATOM   120  N  N   . LEU   A 1 34  ? 35.38500  -2.47300  13.71500  1.000 16.87142 ? 46  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 34  ? 35.96300  -2.32600  12.38700  1.000 16.83457 ? 46  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 34  ? 36.63500  -3.63800  12.01900  1.000 21.08282 ? 46  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 34  ? 37.24700  -4.28600  12.87100  1.000 21.17346 ? 46  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 34  ? 36.99400  -1.20100  12.36000  1.000 17.50541 ? 46  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 34  ? 36.52200  0.15300   12.88400  1.000 16.54525 ? 46  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 34  ? 37.67200  1.16100   12.78400  1.000 19.95647 ? 46  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 34  ? 35.28200  0.63700   12.14000  1.000 18.79748 ? 46  LEU   A CD2 1 
ATOM   128  N  N   . TYR   A 1 35  ? 36.51100  -4.03600  10.75800  1.000 17.79013 ? 47  TYR   A N   1 
ATOM   129  C  CA  . TYR   A 1 35  ? 37.07100  -5.28900  10.27500  1.000 17.29226 ? 47  TYR   A CA  1 
ATOM   130  C  C   . TYR   A 1 35  ? 37.86300  -4.96900  9.02200   1.000 19.93997 ? 47  TYR   A C   1 
ATOM   131  O  O   . TYR   A 1 35  ? 37.29600  -4.48200  8.03700   1.000 19.70153 ? 47  TYR   A O   1 
ATOM   132  C  CB  . TYR   A 1 35  ? 35.94600  -6.26000  9.93400   1.000 18.32260 ? 47  TYR   A CB  1 
ATOM   133  C  CG  . TYR   A 1 35  ? 36.43200  -7.58400  9.39500   1.000 23.71010 ? 47  TYR   A CG  1 
ATOM   134  C  CD1 . TYR   A 1 35  ? 36.82700  -8.60200  10.25200  1.000 24.31293 ? 47  TYR   A CD1 1 
ATOM   135  C  CD2 . TYR   A 1 35  ? 36.57300  -7.78800  8.02500   1.000 23.96888 ? 47  TYR   A CD2 1 
ATOM   136  C  CE1 . TYR   A 1 35  ? 37.28500  -9.81800  9.75900   1.000 33.44060 ? 47  TYR   A CE1 1 
ATOM   137  C  CE2 . TYR   A 1 35  ? 37.04000  -8.99900  7.52400   1.000 27.84927 ? 47  TYR   A CE2 1 
ATOM   138  C  CZ  . TYR   A 1 35  ? 37.39500  -10.00300 8.39600   1.000 35.60279 ? 47  TYR   A CZ  1 
ATOM   139  O  OH  . TYR   A 1 35  ? 37.86100  -11.20100 7.89700   1.000 39.43505 ? 47  TYR   A OH  1 
ATOM   140  N  N   . GLN   A 1 36  ? 39.16400  -5.23500  9.05400   1.000 18.56138 ? 48  GLN   A N   1 
ATOM   141  C  CA  . GLN   A 1 36  ? 40.02500  -4.94100  7.91400   1.000 21.11641 ? 48  GLN   A CA  1 
ATOM   142  C  C   . GLN   A 1 36  ? 39.87300  -6.03600  6.86300   1.000 24.51797 ? 48  GLN   A C   1 
ATOM   143  O  O   . GLN   A 1 36  ? 40.18300  -7.20200  7.12300   1.000 23.98465 ? 48  GLN   A O   1 
ATOM   144  C  CB  . GLN   A 1 36  ? 41.47900  -4.84900  8.36000   1.000 25.31289 ? 48  GLN   A CB  1 
ATOM   145  C  CG  . GLN   A 1 36  ? 42.44600  -4.61200  7.21900   1.000 34.20054 ? 48  GLN   A CG  1 
ATOM   146  C  CD  . GLN   A 1 36  ? 43.58900  -3.70800  7.62000   1.000 41.83200 ? 48  GLN   A CD  1 
ATOM   147  O  OE1 . GLN   A 1 36  ? 44.24500  -3.93700  8.63700   1.000 47.20384 ? 48  GLN   A OE1 1 
ATOM   148  N  NE2 . GLN   A 1 36  ? 43.83400  -2.67000  6.82600   1.000 43.14353 ? 48  GLN   A NE2 1 
ATOM   149  N  N   . ILE   A 1 37  ? 39.40800  -5.65800  5.67700   1.000 21.84377 ? 49  ILE   A N   1 
ATOM   150  C  CA  . ILE   A 1 37  ? 39.17200  -6.60000  4.58400   1.000 23.63813 ? 49  ILE   A CA  1 
ATOM   151  C  C   . ILE   A 1 37  ? 40.39800  -6.75700  3.70300   1.000 29.87489 ? 49  ILE   A C   1 
ATOM   152  O  O   . ILE   A 1 37  ? 40.70300  -7.85800  3.23000   1.000 27.14835 ? 49  ILE   A O   1 
ATOM   153  C  CB  . ILE   A 1 37  ? 37.98000  -6.07600  3.77000   1.000 25.07784 ? 49  ILE   A CB  1 
ATOM   154  C  CG1 . ILE   A 1 37  ? 36.78500  -5.90200  4.69000   1.000 25.50737 ? 49  ILE   A CG1 1 
ATOM   155  C  CG2 . ILE   A 1 37  ? 37.70700  -6.99400  2.58600   1.000 28.05255 ? 49  ILE   A CG2 1 
ATOM   156  C  CD1 . ILE   A 1 37  ? 35.65400  -5.19300  4.05400   1.000 26.83763 ? 49  ILE   A CD1 1 
ATOM   157  N  N   . ALA   A 1 38  ? 41.08200  -5.65600  3.44800   1.000 26.66404 ? 50  ALA   A N   1 
ATOM   158  C  CA  . ALA   A 1 38  ? 42.28400  -5.62200  2.63400   1.000 28.97898 ? 50  ALA   A CA  1 
ATOM   159  C  C   . ALA   A 1 38  ? 43.02800  -4.35000  3.00400   1.000 31.34669 ? 50  ALA   A C   1 
ATOM   160  O  O   . ALA   A 1 38  ? 42.57800  -3.57000  3.85100   1.000 30.66374 ? 50  ALA   A O   1 
ATOM   161  C  CB  . ALA   A 1 38  ? 41.94800  -5.68300  1.14000   1.000 30.25967 ? 50  ALA   A CB  1 
ATOM   162  N  N   . ASP   A 1 39  ? 44.17100  -4.14400  2.36700   1.000 30.33534 ? 51  ASP   A N   1 
ATOM   163  C  CA  . ASP   A 1 39  ? 44.95500  -2.94700  2.62600   1.000 27.54940 ? 51  ASP   A CA  1 
ATOM   164  C  C   . ASP   A 1 39  ? 44.11200  -1.70900  2.32400   1.000 26.99693 ? 51  ASP   A C   1 
ATOM   165  O  O   . ASP   A 1 39  ? 43.65300  -1.52000  1.19400   1.000 30.32176 ? 51  ASP   A O   1 
ATOM   166  C  CB  . ASP   A 1 39  ? 46.20600  -2.97400  1.75000   1.000 34.74500 ? 51  ASP   A CB  1 
ATOM   167  C  CG  . ASP   A 1 39  ? 47.12100  -1.79700  2.00700   1.000 50.85973 ? 51  ASP   A CG  1 
ATOM   168  O  OD1 . ASP   A 1 39  ? 47.09300  -1.26100  3.13600   1.000 54.65764 ? 51  ASP   A OD1 1 
ATOM   169  O  OD2 . ASP   A 1 39  ? 47.87600  -1.41600  1.08500   1.000 53.96843 ? 51  ASP   A OD2 1 
ATOM   170  N  N   . GLY   A 1 40  ? 43.88100  -0.88800  3.34800   1.000 22.71880 ? 52  GLY   A N   1 
ATOM   171  C  CA  . GLY   A 1 40  ? 43.11600  0.33400   3.17400   1.000 28.10971 ? 52  GLY   A CA  1 
ATOM   172  C  C   . GLY   A 1 40  ? 41.61600  0.17500   3.01200   1.000 20.09718 ? 52  GLY   A C   1 
ATOM   173  O  O   . GLY   A 1 40  ? 40.95200  1.11700   2.56400   1.000 21.95544 ? 52  GLY   A O   1 
ATOM   174  N  N   . VAL   A 1 41  ? 41.05400  -0.98100  3.35700   1.000 17.95930 ? 53  VAL   A N   1 
ATOM   175  C  CA  . VAL   A 1 41  ? 39.62100  -1.21600  3.20700   1.000 17.85981 ? 53  VAL   A CA  1 
ATOM   176  C  C   . VAL   A 1 41  ? 39.12300  -1.91000  4.46200   1.000 19.09106 ? 53  VAL   A C   1 
ATOM   177  O  O   . VAL   A 1 41  ? 39.59600  -3.00300  4.80000   1.000 20.75546 ? 53  VAL   A O   1 
ATOM   178  C  CB  . VAL   A 1 41  ? 39.26500  -2.06600  1.97500   1.000 20.11707 ? 53  VAL   A CB  1 
ATOM   179  C  CG1 . VAL   A 1 41  ? 37.75000  -2.15900  1.83700   1.000 19.74518 ? 53  VAL   A CG1 1 
ATOM   180  C  CG2 . VAL   A 1 41  ? 39.89900  -1.48800  0.71900   1.000 21.61480 ? 53  VAL   A CG2 1 
ATOM   181  N  N   . TRP   A 1 42  ? 38.15700  -1.29400  5.13400   1.000 15.69390 ? 54  TRP   A N   1 
ATOM   182  C  CA  . TRP   A 1 42  ? 37.51100  -1.88700  6.28900   1.000 16.94783 ? 54  TRP   A CA  1 
ATOM   183  C  C   . TRP   A 1 42  ? 36.00200  -1.92200  6.08500   1.000 15.88348 ? 54  TRP   A C   1 
ATOM   184  O  O   . TRP   A 1 42  ? 35.43300  -1.12100  5.34300   1.000 15.82773 ? 54  TRP   A O   1 
ATOM   185  C  CB  . TRP   A 1 42  ? 37.77700  -1.07800  7.56800   1.000 16.92227 ? 54  TRP   A CB  1 
ATOM   186  C  CG  . TRP   A 1 42  ? 39.20100  -0.84300  7.91800   1.000 17.39708 ? 54  TRP   A CG  1 
ATOM   187  C  CD1 . TRP   A 1 42  ? 39.90200  -1.48100  8.90700   1.000 18.80426 ? 54  TRP   A CD1 1 
ATOM   188  C  CD2 . TRP   A 1 42  ? 40.09100  0.14400   7.36600   1.000 18.34666 ? 54  TRP   A CD2 1 
ATOM   189  N  NE1 . TRP   A 1 42  ? 41.17500  -0.98600  8.97900   1.000 21.10841 ? 54  TRP   A NE1 1 
ATOM   190  C  CE2 . TRP   A 1 42  ? 41.32300  0.01500   8.05300   1.000 21.86906 ? 54  TRP   A CE2 1 
ATOM   191  C  CE3 . TRP   A 1 42  ? 39.97500  1.11100   6.35700   1.000 18.15978 ? 54  TRP   A CE3 1 
ATOM   192  C  CZ2 . TRP   A 1 42  ? 42.43300  0.81600   7.76300   1.000 25.63016 ? 54  TRP   A CZ2 1 
ATOM   193  C  CZ3 . TRP   A 1 42  ? 41.07600  1.91200   6.07300   1.000 18.11158 ? 54  TRP   A CZ3 1 
ATOM   194  C  CH2 . TRP   A 1 42  ? 42.29600  1.75300   6.77200   1.000 20.32351 ? 54  TRP   A CH2 1 
ATOM   195  N  N   . SER   A 1 43  ? 35.34700  -2.83700  6.77800   1.000 15.75322 ? 55  SER   A N   1 
ATOM   196  C  CA  . SER   A 1 43  ? 33.93100  -2.65500  7.02800   1.000 15.66837 ? 55  SER   A CA  1 
ATOM   197  C  C   . SER   A 1 43  ? 33.74700  -2.13800  8.44300   1.000 15.99019 ? 55  SER   A C   1 
ATOM   198  O  O   . SER   A 1 43  ? 34.62500  -2.28500  9.30700   1.000 15.49843 ? 55  SER   A O   1 
ATOM   199  C  CB  . SER   A 1 43  ? 33.11500  -3.93200  6.80000   1.000 16.56528 ? 55  SER   A CB  1 
ATOM   200  O  OG  . SER   A 1 43  ? 33.44700  -4.92700  7.74100   1.000 18.43551 ? 55  SER   A OG  1 
ATOM   201  N  N   . HIS   A 1 44  ? 32.62400  -1.46900  8.65200   1.000 14.03105 ? 56  HIS   A N   1 
ATOM   202  C  CA  . HIS   A 1 44  ? 32.19700  -1.09700  9.98700   1.000 13.59279 ? 56  HIS   A CA  1 
ATOM   203  C  C   . HIS   A 1 44  ? 30.91300  -1.84300  10.31900  1.000 15.00871 ? 56  HIS   A C   1 
ATOM   204  O  O   . HIS   A 1 44  ? 30.04300  -2.01200  9.46300   1.000 15.32259 ? 56  HIS   A O   1 
ATOM   205  C  CB  . HIS   A 1 44  ? 32.11700  0.43700   10.20600  1.000 13.87910 ? 56  HIS   A CB  1 
ATOM   206  C  CG  . HIS   A 1 44  ? 31.11900  1.17500   9.36100   1.000 14.46980 ? 56  HIS   A CG  1 
ATOM   207  N  ND1 . HIS   A 1 44  ? 29.78000  1.26100   9.68600   1.000 14.42902 ? 56  HIS   A ND1 1 
ATOM   208  C  CD2 . HIS   A 1 44  ? 31.29400  1.98200   8.28700   1.000 13.02137 ? 56  HIS   A CD2 1 
ATOM   209  C  CE1 . HIS   A 1 44  ? 29.16300  2.03000   8.80600   1.000 13.53812 ? 56  HIS   A CE1 1 
ATOM   210  N  NE2 . HIS   A 1 44  ? 30.06300  2.49400   7.95400   1.000 13.66910 ? 56  HIS   A NE2 1 
ATOM   211  N  N   . ILE   A 1 45  ? 30.82700  -2.34700  11.54400  1.000 15.72822 ? 57  ILE   A N   1 
ATOM   212  C  CA  . ILE   A 1 45  ? 29.73200  -3.22300  11.95200  1.000 15.82306 ? 57  ILE   A CA  1 
ATOM   213  C  C   . ILE   A 1 45  ? 29.11600  -2.67800  13.22800  1.000 17.30289 ? 57  ILE   A C   1 
ATOM   214  O  O   . ILE   A 1 45  ? 29.83700  -2.40900  14.20000  1.000 19.10048 ? 57  ILE   A O   1 
ATOM   215  C  CB  . ILE   A 1 45  ? 30.17500  -4.68700  12.14500  1.000 19.52822 ? 57  ILE   A CB  1 
ATOM   216  C  CG1 . ILE   A 1 45  ? 30.95700  -5.17300  10.92400  1.000 18.39695 ? 57  ILE   A CG1 1 
ATOM   217  C  CG2 . ILE   A 1 45  ? 28.96800  -5.59200  12.36400  1.000 21.54068 ? 57  ILE   A CG2 1 
ATOM   218  C  CD1 . ILE   A 1 45  ? 32.46900  -5.09500  11.01900  1.000 18.79841 ? 57  ILE   A CD1 1 
ATOM   219  N  N   . ALA   A 1 46  ? 27.79800  -2.47500  13.21500  1.000 18.61769 ? 58  ALA   A N   1 
ATOM   220  C  CA  . ALA   A 1 46  ? 27.06600  -1.90000  14.33900  1.000 21.14527 ? 58  ALA   A CA  1 
ATOM   221  C  C   . ALA   A 1 46  ? 25.76400  -2.67100  14.49800  1.000 22.76579 ? 58  ALA   A C   1 
ATOM   222  O  O   . ALA   A 1 46  ? 25.43800  -3.53500  13.69200  1.000 17.09130 ? 58  ALA   A O   1 
ATOM   223  C  CB  . ALA   A 1 46  ? 26.79000  -0.40800  14.14100  1.000 21.60548 ? 58  ALA   A CB  1 
ATOM   224  N  N   . THR   A 1 47  ? 25.01100  -2.33600  15.54500  1.000 29.50853 ? 59  THR   A N   1 
ATOM   225  C  CA  . THR   A 1 47  ? 23.77300  -3.02700  15.87200  1.000 31.76416 ? 59  THR   A CA  1 
ATOM   226  C  C   . THR   A 1 47  ? 22.66000  -2.02100  16.12600  1.000 35.36861 ? 59  THR   A C   1 
ATOM   227  O  O   . THR   A 1 47  ? 22.90200  -0.88800  16.55100  1.000 30.12776 ? 59  THR   A O   1 
ATOM   228  C  CB  . THR   A 1 47  ? 23.92000  -3.84800  17.15000  1.000 32.93758 ? 59  THR   A CB  1 
ATOM   229  O  OG1 . THR   A 1 47  ? 23.97700  -2.95300  18.26500  1.000 40.01909 ? 59  THR   A OG1 1 
ATOM   230  C  CG2 . THR   A 1 47  ? 25.18300  -4.69600  17.12000  1.000 36.19242 ? 59  THR   A CG2 1 
ATOM   231  N  N   . GLN   A 1 48  ? 21.42900  -2.46000  15.88100  1.000 30.25589 ? 60  GLN   A N   1 
ATOM   232  C  CA  . GLN   A 1 48  ? 20.23900  -1.70100  16.24000  1.000 38.12330 ? 60  GLN   A CA  1 
ATOM   233  C  C   . GLN   A 1 48  ? 19.23200  -2.68300  16.82000  1.000 48.98918 ? 60  GLN   A C   1 
ATOM   234  O  O   . GLN   A 1 48  ? 18.80800  -3.62100  16.13600  1.000 35.04214 ? 60  GLN   A O   1 
ATOM   235  C  CB  . GLN   A 1 48  ? 19.66800  -0.94200  15.03100  1.000 37.75947 ? 60  GLN   A CB  1 
ATOM   236  C  CG  . GLN   A 1 48  ? 18.81900  0.28000   15.38300  1.000 38.43454 ? 60  GLN   A CG  1 
ATOM   237  C  CD  . GLN   A 1 48  ? 19.39100  1.11300   16.52000  1.000 46.71089 ? 60  GLN   A CD  1 
ATOM   238  O  OE1 . GLN   A 1 48  ? 18.96600  0.97400   17.66500  1.000 46.40564 ? 60  GLN   A OE1 1 
ATOM   239  N  NE2 . GLN   A 1 48  ? 20.33000  2.00200   16.20500  1.000 36.94381 ? 60  GLN   A NE2 1 
ATOM   240  N  N   . SER   A 1 49  ? 18.89300  -2.49600  18.09400  1.000 61.69609 ? 61  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 49  ? 17.88500  -3.31400  18.76500  1.000 56.45387 ? 61  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 49  ? 16.54300  -2.62800  18.55600  1.000 52.33764 ? 61  SER   A C   1 
ATOM   243  O  O   . SER   A 1 49  ? 16.21700  -1.65100  19.23500  1.000 70.07311 ? 61  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 49  ? 18.20900  -3.47200  20.24700  1.000 65.67749 ? 61  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 49  ? 18.21800  -2.22100  20.91500  1.000 76.92095 ? 61  SER   A OG  1 
ATOM   246  N  N   . PHE   A 1 50  ? 15.76400  -3.13000  17.60200  1.000 53.65744 ? 62  PHE   A N   1 
ATOM   247  C  CA  . PHE   A 1 50  ? 14.49500  -2.52000  17.22900  1.000 55.66967 ? 62  PHE   A CA  1 
ATOM   248  C  C   . PHE   A 1 50  ? 13.39400  -3.57300  17.20800  1.000 66.36840 ? 62  PHE   A C   1 
ATOM   249  O  O   . PHE   A 1 50  ? 13.63000  -4.73000  16.84200  1.000 56.74112 ? 62  PHE   A O   1 
ATOM   250  C  CB  . PHE   A 1 50  ? 14.63600  -1.72700  15.89700  1.000 50.78936 ? 62  PHE   A CB  1 
ATOM   251  C  CG  . PHE   A 1 50  ? 13.98200  -2.37500  14.69800  1.000 63.33596 ? 62  PHE   A CG  1 
ATOM   252  C  CD1 . PHE   A 1 50  ? 12.60500  -2.33700  14.51600  1.000 64.00954 ? 62  PHE   A CD1 1 
ATOM   253  C  CD2 . PHE   A 1 50  ? 14.76100  -2.98900  13.72600  1.000 69.20772 ? 62  PHE   A CD2 1 
ATOM   254  C  CE1 . PHE   A 1 50  ? 12.01700  -2.92900  13.40800  1.000 67.28246 ? 62  PHE   A CE1 1 
ATOM   255  C  CE2 . PHE   A 1 50  ? 14.17900  -3.57900  12.61100  1.000 66.10586 ? 62  PHE   A CE2 1 
ATOM   256  C  CZ  . PHE   A 1 50  ? 12.80500  -3.54800  12.45300  1.000 67.17844 ? 62  PHE   A CZ  1 
ATOM   257  N  N   . ASP   A 1 51  ? 12.19000  -3.15800  17.61800  1.000 64.44189 ? 63  ASP   A N   1 
ATOM   258  C  CA  . ASP   A 1 51  ? 11.03200  -4.04900  17.73500  1.000 47.09265 ? 63  ASP   A CA  1 
ATOM   259  C  C   . ASP   A 1 51  ? 11.31600  -5.27000  18.60500  1.000 41.44042 ? 63  ASP   A C   1 
ATOM   260  O  O   . ASP   A 1 51  ? 10.66600  -6.30400  18.46000  1.000 46.53504 ? 63  ASP   A O   1 
ATOM   261  C  CB  . ASP   A 1 51  ? 10.45600  -4.46100  16.37200  1.000 53.32105 ? 63  ASP   A CB  1 
ATOM   262  C  CG  . ASP   A 1 51  ? 9.02300   -3.97600  16.16100  1.000 52.46355 ? 63  ASP   A CG  1 
ATOM   263  O  OD1 . ASP   A 1 51  ? 8.73600   -2.79600  16.45700  1.000 51.61897 ? 63  ASP   A OD1 1 
ATOM   264  O  OD2 . ASP   A 1 51  ? 8.18200   -4.78000  15.69800  1.000 42.27034 ? 63  ASP   A OD2 1 
ATOM   265  N  N   . GLY   A 1 52  ? 12.28900  -5.16500  19.51300  1.000 41.17811 ? 64  GLY   A N   1 
ATOM   266  C  CA  . GLY   A 1 52  ? 12.61400  -6.24400  20.42700  1.000 43.72797 ? 64  GLY   A CA  1 
ATOM   267  C  C   . GLY   A 1 52  ? 13.67600  -7.22500  19.96200  1.000 45.27130 ? 64  GLY   A C   1 
ATOM   268  O  O   . GLY   A 1 52  ? 14.03800  -8.12800  20.73200  1.000 39.64953 ? 64  GLY   A O   1 
ATOM   269  N  N   . ALA   A 1 53  ? 14.17100  -7.10000  18.73200  1.000 45.40477 ? 65  ALA   A N   1 
ATOM   270  C  CA  . ALA   A 1 53  ? 15.21400  -7.96900  18.20900  1.000 39.60595 ? 65  ALA   A CA  1 
ATOM   271  C  C   . ALA   A 1 53  ? 16.45000  -7.13900  17.88800  1.000 40.52790 ? 65  ALA   A C   1 
ATOM   272  O  O   . ALA   A 1 53  ? 16.38600  -5.91200  17.79100  1.000 41.58071 ? 65  ALA   A O   1 
ATOM   273  C  CB  . ALA   A 1 53  ? 14.75100  -8.70500  16.95000  1.000 29.78227 ? 65  ALA   A CB  1 
ATOM   274  N  N   . VAL   A 1 54  ? 17.58400  -7.81900  17.72300  1.000 29.24350 ? 66  VAL   A N   1 
ATOM   275  C  CA  . VAL   A 1 54  ? 18.87200  -7.16100  17.51000  1.000 30.50689 ? 66  VAL   A CA  1 
ATOM   276  C  C   . VAL   A 1 54  ? 19.36300  -7.49000  16.10500  1.000 25.05165 ? 66  VAL   A C   1 
ATOM   277  O  O   . VAL   A 1 54  ? 19.43900  -8.66500  15.72300  1.000 21.92596 ? 66  VAL   A O   1 
ATOM   278  C  CB  . VAL   A 1 54  ? 19.89900  -7.57500  18.57900  1.000 32.84582 ? 66  VAL   A CB  1 
ATOM   279  C  CG1 . VAL   A 1 54  ? 21.31700  -7.20900  18.14100  1.000 33.91125 ? 66  VAL   A CG1 1 
ATOM   280  C  CG2 . VAL   A 1 54  ? 19.55900  -6.92800  19.91500  1.000 38.56140 ? 66  VAL   A CG2 1 
ATOM   281  N  N   . TYR   A 1 55  ? 19.70800  -6.44500  15.33800  1.000 27.89169 ? 67  TYR   A N   1 
ATOM   282  C  CA  . TYR   A 1 55  ? 20.12800  -6.60200  13.95200  1.000 23.91243 ? 67  TYR   A CA  1 
ATOM   283  C  C   . TYR   A 1 55  ? 21.51700  -6.01100  13.74400  1.000 18.15080 ? 67  TYR   A C   1 
ATOM   284  O  O   . TYR   A 1 55  ? 21.80200  -4.92500  14.25500  1.000 23.54649 ? 67  TYR   A O   1 
ATOM   285  C  CB  . TYR   A 1 55  ? 19.15600  -5.88500  13.00400  1.000 23.12147 ? 67  TYR   A CB  1 
ATOM   286  C  CG  . TYR   A 1 55  ? 17.71400  -6.33200  13.13900  1.000 32.31648 ? 67  TYR   A CG  1 
ATOM   287  C  CD1 . TYR   A 1 55  ? 16.89900  -5.82400  14.14400  1.000 41.10116 ? 67  TYR   A CD1 1 
ATOM   288  C  CD2 . TYR   A 1 55  ? 17.18000  -7.28700  12.28500  1.000 30.99042 ? 67  TYR   A CD2 1 
ATOM   289  C  CE1 . TYR   A 1 55  ? 15.58800  -6.23800  14.27700  1.000 45.64810 ? 67  TYR   A CE1 1 
ATOM   290  C  CE2 . TYR   A 1 55  ? 15.87000  -7.70600  12.40700  1.000 32.47406 ? 67  TYR   A CE2 1 
ATOM   291  C  CZ  . TYR   A 1 55  ? 15.07800  -7.17400  13.40400  1.000 43.82009 ? 67  TYR   A CZ  1 
ATOM   292  O  OH  . TYR   A 1 55  ? 13.77200  -7.58700  13.53800  1.000 55.09938 ? 67  TYR   A OH  1 
ATOM   293  N  N   . PRO   A 1 56  ? 22.38900  -6.68400  13.00100  1.000 16.15459 ? 68  PRO   A N   1 
ATOM   294  C  CA  . PRO   A 1 56  ? 23.68100  -6.09700  12.63600  1.000 17.57191 ? 68  PRO   A CA  1 
ATOM   295  C  C   . PRO   A 1 56  ? 23.55900  -5.29500  11.34500  1.000 15.42734 ? 68  PRO   A C   1 
ATOM   296  O  O   . PRO   A 1 56  ? 22.63100  -5.47500  10.55600  1.000 15.74362 ? 68  PRO   A O   1 
ATOM   297  C  CB  . PRO   A 1 56  ? 24.54100  -7.34300  12.39000  1.000 18.56917 ? 68  PRO   A CB  1 
ATOM   298  C  CG  . PRO   A 1 56  ? 23.55700  -8.33200  11.79600  1.000 17.57478 ? 68  PRO   A CG  1 
ATOM   299  C  CD  . PRO   A 1 56  ? 22.20500  -8.02200  12.41500  1.000 18.41632 ? 68  PRO   A CD  1 
ATOM   300  N  N   . SER   A 1 57  ? 24.51300  -4.38900  11.14000  1.000 14.67693 ? 69  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 57  ? 24.52100  -3.60500  9.91500   1.000 15.92244 ? 69  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 57  ? 25.96300  -3.27400  9.55600   1.000 14.51977 ? 69  SER   A C   1 
ATOM   303  O  O   . SER   A 1 57  ? 26.77600  -2.97500  10.44000  1.000 15.70662 ? 69  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 57  ? 23.69100  -2.32800  10.08500  1.000 16.23786 ? 69  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 57  ? 23.57200  -1.62000  8.85300   1.000 18.47087 ? 69  SER   A OG  1 
ATOM   306  N  N   . ASN   A 1 58  ? 26.27100  -3.33400  8.26100   1.000 14.11295 ? 70  ASN   A N   1 
ATOM   307  C  CA  . ASN   A 1 58  ? 27.59900  -3.03300  7.74000   1.000 15.03305 ? 70  ASN   A CA  1 
ATOM   308  C  C   . ASN   A 1 58  ? 27.61500  -1.71700  6.97400   1.000 13.19695 ? 70  ASN   A C   1 
ATOM   309  O  O   . ASN   A 1 58  ? 26.64400  -1.35200  6.29800   1.000 14.19148 ? 70  ASN   A O   1 
ATOM   310  C  CB  . ASN   A 1 58  ? 28.04300  -4.08100  6.71500   1.000 14.41743 ? 70  ASN   A CB  1 
ATOM   311  C  CG  . ASN   A 1 58  ? 28.17100  -5.45500  7.30300   1.000 15.03523 ? 70  ASN   A CG  1 
ATOM   312  O  OD1 . ASN   A 1 58  ? 28.71100  -5.62900  8.40000   1.000 15.56405 ? 70  ASN   A OD1 1 
ATOM   313  N  ND2 . ASN   A 1 58  ? 27.68600  -6.44400  6.57400   1.000 14.19402 ? 70  ASN   A ND2 1 
ATOM   314  N  N   . GLY   A 1 59  ? 28.76300  -1.03600  7.04700   1.000 12.85501 ? 71  GLY   A N   1 
ATOM   315  C  CA  . GLY   A 1 59  ? 29.16700  -0.03400  6.06900   1.000 11.63263 ? 71  GLY   A CA  1 
ATOM   316  C  C   . GLY   A 1 59  ? 30.61600  -0.24700  5.67600   1.000 12.38873 ? 71  GLY   A C   1 
ATOM   317  O  O   . GLY   A 1 59  ? 31.20700  -1.28800  6.00800   1.000 13.91194 ? 71  GLY   A O   1 
ATOM   318  N  N   . LEU   A 1 60  ? 31.20700  0.69800   4.95300   1.000 13.34619 ? 72  LEU   A N   1 
ATOM   319  C  CA  . LEU   A 1 60  ? 32.55700  0.52900   4.43400   1.000 14.08502 ? 72  LEU   A CA  1 
ATOM   320  C  C   . LEU   A 1 60  ? 33.39200  1.76700   4.73900   1.000 12.47573 ? 72  LEU   A C   1 
ATOM   321  O  O   . LEU   A 1 60  ? 32.86200  2.87700   4.88700   1.000 13.21402 ? 72  LEU   A O   1 
ATOM   322  C  CB  . LEU   A 1 60  ? 32.52300  0.26800   2.90900   1.000 15.45325 ? 72  LEU   A CB  1 
ATOM   323  C  CG  . LEU   A 1 60  ? 33.71600  -0.47200  2.29000   1.000 16.15085 ? 72  LEU   A CG  1 
ATOM   324  C  CD1 . LEU   A 1 60  ? 33.72200  -1.92800  2.69800   1.000 17.21903 ? 72  LEU   A CD1 1 
ATOM   325  C  CD2 . LEU   A 1 60  ? 33.66900  -0.31300  0.77000   1.000 16.65118 ? 72  LEU   A CD2 1 
ATOM   326  N  N   . ILE   A 1 61  ? 34.70800  1.56200   4.86400   1.000 12.84654 ? 73  ILE   A N   1 
ATOM   327  C  CA  . ILE   A 1 61  ? 35.68500  2.63400   5.02400   1.000 13.72822 ? 73  ILE   A CA  1 
ATOM   328  C  C   . ILE   A 1 61  ? 36.80100  2.35800   4.03400   1.000 14.02143 ? 73  ILE   A C   1 
ATOM   329  O  O   . ILE   A 1 61  ? 37.33200  1.24600   4.00000   1.000 15.54576 ? 73  ILE   A O   1 
ATOM   330  C  CB  . ILE   A 1 61  ? 36.26800  2.66200   6.45000   1.000 14.20134 ? 73  ILE   A CB  1 
ATOM   331  C  CG1 . ILE   A 1 61  ? 35.15500  2.74900   7.49900   1.000 15.02443 ? 73  ILE   A CG1 1 
ATOM   332  C  CG2 . ILE   A 1 61  ? 37.27600  3.79800   6.60800   1.000 15.87597 ? 73  ILE   A CG2 1 
ATOM   333  C  CD1 . ILE   A 1 61  ? 35.59500  2.36900   8.88800   1.000 16.93340 ? 73  ILE   A CD1 1 
ATOM   334  N  N   . VAL   A 1 62  ? 37.16100  3.34900   3.23500   1.000 14.59404 ? 74  VAL   A N   1 
ATOM   335  C  CA  . VAL   A 1 62  ? 38.19800  3.16800   2.22800   1.000 14.88160 ? 74  VAL   A CA  1 
ATOM   336  C  C   . VAL   A 1 62  ? 39.22900  4.28200   2.36800   1.000 17.23455 ? 74  VAL   A C   1 
ATOM   337  O  O   . VAL   A 1 62  ? 38.88900  5.46600   2.28300   1.000 16.03692 ? 74  VAL   A O   1 
ATOM   338  C  CB  . VAL   A 1 62  ? 37.62400  3.14200   0.80300   1.000 15.88593 ? 74  VAL   A CB  1 
ATOM   339  C  CG1 . VAL   A 1 62  ? 38.72700  2.76500   -0.19300  1.000 17.89226 ? 74  VAL   A CG1 1 
ATOM   340  C  CG2 . VAL   A 1 62  ? 36.44100  2.16700   0.70100   1.000 16.52690 ? 74  VAL   A CG2 1 
ATOM   341  N  N   . ARG   A 1 63  ? 40.49600  3.90400   2.54000   1.000 17.72647 ? 75  ARG   A N   1 
ATOM   342  C  CA  . ARG   A 1 63  ? 41.55600  4.90000   2.60600   1.000 18.67590 ? 75  ARG   A CA  1 
ATOM   343  C  C   . ARG   A 1 63  ? 41.79700  5.52900   1.23700   1.000 18.56966 ? 75  ARG   A C   1 
ATOM   344  O  O   . ARG   A 1 63  ? 41.77900  4.84800   0.20900   1.000 20.52250 ? 75  ARG   A O   1 
ATOM   345  C  CB  . ARG   A 1 63  ? 42.84800  4.25500   3.10000   1.000 21.25630 ? 75  ARG   A CB  1 
ATOM   346  C  CG  . ARG   A 1 63  ? 44.01900  5.23200   3.16900   1.000 24.93920 ? 75  ARG   A CG  1 
ATOM   347  C  CD  . ARG   A 1 63  ? 45.15100  4.72600   4.04600   1.000 32.67751 ? 75  ARG   A CD  1 
ATOM   348  N  NE  . ARG   A 1 63  ? 46.13100  5.78000   4.28300   1.000 37.95488 ? 75  ARG   A NE  1 
ATOM   349  C  CZ  . ARG   A 1 63  ? 47.19300  5.66200   5.06900   1.000 49.67493 ? 75  ARG   A CZ  1 
ATOM   350  N  NH1 . ARG   A 1 63  ? 47.43800  4.54600   5.73700   1.000 40.11766 ? 75  ARG   A NH1 1 
ATOM   351  N  NH2 . ARG   A 1 63  ? 48.03100  6.69000   5.18600   1.000 36.66263 ? 75  ARG   A NH2 1 
ATOM   352  N  N   . ASP   A 1 64  ? 42.03200  6.83900   1.23300   1.000 20.14097 ? 76  ASP   A N   1 
ATOM   353  C  CA  . ASP   A 1 64  ? 42.38700  7.57100   0.01500   1.000 26.16136 ? 76  ASP   A CA  1 
ATOM   354  C  C   . ASP   A 1 64  ? 43.53300  8.51800   0.35500   1.000 22.22721 ? 76  ASP   A C   1 
ATOM   355  O  O   . ASP   A 1 64  ? 43.30200  9.63300   0.82900   1.000 22.96989 ? 76  ASP   A O   1 
ATOM   356  C  CB  . ASP   A 1 64  ? 41.19300  8.33900   -0.52700  1.000 28.32311 ? 76  ASP   A CB  1 
ATOM   357  C  CG  . ASP   A 1 64  ? 41.50300  9.02400   -1.83700  1.000 24.84469 ? 76  ASP   A CG  1 
ATOM   358  O  OD1 . ASP   A 1 64  ? 42.55400  8.71700   -2.44200  1.000 32.72102 ? 76  ASP   A OD1 1 
ATOM   359  O  OD2 . ASP   A 1 64  ? 40.69500  9.87800   -2.24600  1.000 25.09909 ? 76  ASP   A OD2 1 
ATOM   360  N  N   . GLY   A 1 65  ? 44.75200  8.07300   0.10700   1.000 31.83753 ? 77  GLY   A N   1 
ATOM   361  C  CA  . GLY   A 1 65  ? 45.90200  8.83300   0.55900   1.000 31.48181 ? 77  GLY   A CA  1 
ATOM   362  C  C   . GLY   A 1 65  ? 45.92800  8.86700   2.07000   1.000 31.88261 ? 77  GLY   A C   1 
ATOM   363  O  O   . GLY   A 1 65  ? 46.00500  7.82800   2.73600   1.000 31.79394 ? 77  GLY   A O   1 
ATOM   364  N  N   . ASP   A 1 66  ? 45.83900  10.07400  2.63200   1.000 24.61899 ? 78  ASP   A N   1 
ATOM   365  C  CA  . ASP   A 1 66  ? 45.88000  10.26600  4.07600   1.000 24.62097 ? 78  ASP   A CA  1 
ATOM   366  C  C   . ASP   A 1 66  ? 44.51800  10.64500  4.64800   1.000 24.29846 ? 78  ASP   A C   1 
ATOM   367  O  O   . ASP   A 1 66  ? 44.43600  11.18000  5.75600   1.000 24.89354 ? 78  ASP   A O   1 
ATOM   368  C  CB  . ASP   A 1 66  ? 46.95200  11.29400  4.45000   1.000 32.75801 ? 78  ASP   A CB  1 
ATOM   369  C  CG  . ASP   A 1 66  ? 48.36400  10.79700  4.15800   1.000 47.65369 ? 78  ASP   A CG  1 
ATOM   370  O  OD1 . ASP   A 1 66  ? 48.61400  9.58200   4.29600   1.000 39.47841 ? 78  ASP   A OD1 1 
ATOM   371  O  OD2 . ASP   A 1 66  ? 49.22300  11.62400  3.78300   1.000 55.50396 ? 78  ASP   A OD2 1 
ATOM   372  N  N   . GLU   A 1 67  ? 43.44800  10.38300  3.90200   1.000 22.01686 ? 79  GLU   A N   1 
ATOM   373  C  CA  . GLU   A 1 67  ? 42.08300  10.63200  4.33500   1.000 20.62731 ? 79  GLU   A CA  1 
ATOM   374  C  C   . GLU   A 1 67  ? 41.28000  9.34900   4.14700   1.000 17.95836 ? 79  GLU   A C   1 
ATOM   375  O  O   . GLU   A 1 67  ? 41.75300  8.37700   3.55700   1.000 19.18978 ? 79  GLU   A O   1 
ATOM   376  C  CB  . GLU   A 1 67  ? 41.44100  11.77500  3.53200   1.000 21.54696 ? 79  GLU   A CB  1 
ATOM   377  C  CG  . GLU   A 1 67  ? 42.27800  13.06000  3.43900   1.000 24.73533 ? 79  GLU   A CG  1 
ATOM   378  C  CD  . GLU   A 1 67  ? 41.69200  14.07200  2.46500   1.000 34.97328 ? 79  GLU   A CD  1 
ATOM   379  O  OE1 . GLU   A 1 67  ? 40.63400  13.78600  1.86600   1.000 31.20229 ? 79  GLU   A OE1 1 
ATOM   380  O  OE2 . GLU   A 1 67  ? 42.29800  15.14800  2.28400   1.000 47.24189 ? 79  GLU   A OE2 1 
ATOM   381  N  N   . LEU   A 1 68  ? 40.04800  9.35400   4.65400   1.000 19.33753 ? 80  LEU   A N   1 
ATOM   382  C  CA  . LEU   A 1 68  ? 39.15700  8.20700   4.54200   1.000 16.54252 ? 80  LEU   A CA  1 
ATOM   383  C  C   . LEU   A 1 68  ? 37.84600  8.61400   3.88500   1.000 16.14840 ? 80  LEU   A C   1 
ATOM   384  O  O   . LEU   A 1 68  ? 37.30000  9.67800   4.18400   1.000 15.10747 ? 80  LEU   A O   1 
ATOM   385  C  CB  . LEU   A 1 68  ? 38.82800  7.65900   5.93500   1.000 16.72440 ? 80  LEU   A CB  1 
ATOM   386  C  CG  . LEU   A 1 68  ? 39.98800  7.17800   6.79800   1.000 16.62510 ? 80  LEU   A CG  1 
ATOM   387  C  CD1 . LEU   A 1 68  ? 39.47000  6.74900   8.16200   1.000 18.78751 ? 80  LEU   A CD1 1 
ATOM   388  C  CD2 . LEU   A 1 68  ? 40.73500  6.05100   6.11200   1.000 19.26366 ? 80  LEU   A CD2 1 
ATOM   389  N  N   . LEU   A 1 69  ? 37.31700  7.72100   3.05100   1.000 15.11474 ? 81  LEU   A N   1 
ATOM   390  C  CA  . LEU   A 1 69  ? 35.95400  7.80700   2.54100   1.000 13.50757 ? 81  LEU   A CA  1 
ATOM   391  C  C   . LEU   A 1 69  ? 35.08700  6.83300   3.33100   1.000 12.50156 ? 81  LEU   A C   1 
ATOM   392  O  O   . LEU   A 1 69  ? 35.44200  5.66000   3.47000   1.000 13.95271 ? 81  LEU   A O   1 
ATOM   393  C  CB  . LEU   A 1 69  ? 35.93300  7.43100   1.05900   1.000 14.34631 ? 81  LEU   A CB  1 
ATOM   394  C  CG  . LEU   A 1 69  ? 34.54600  7.27200   0.42800   1.000 14.08224 ? 81  LEU   A CG  1 
ATOM   395  C  CD1 . LEU   A 1 69  ? 33.79300  8.58800   0.38400   1.000 15.61194 ? 81  LEU   A CD1 1 
ATOM   396  C  CD2 . LEU   A 1 69  ? 34.64800  6.69900   -0.97800  1.000 16.91057 ? 81  LEU   A CD2 1 
ATOM   397  N  N   . LEU   A 1 70  ? 33.95900  7.32200   3.85700   1.000 12.06346 ? 82  LEU   A N   1 
ATOM   398  C  CA  . LEU   A 1 70  ? 33.00700  6.49500   4.58900   1.000 12.25381 ? 82  LEU   A CA  1 
ATOM   399  C  C   . LEU   A 1 70  ? 31.83100  6.15000   3.68000   1.000 12.86601 ? 82  LEU   A C   1 
ATOM   400  O  O   . LEU   A 1 70  ? 31.29000  7.02600   2.98700   1.000 13.33461 ? 82  LEU   A O   1 
ATOM   401  C  CB  . LEU   A 1 70  ? 32.51200  7.25900   5.81300   1.000 13.32676 ? 82  LEU   A CB  1 
ATOM   402  C  CG  . LEU   A 1 70  ? 31.46300  6.54300   6.66700   1.000 13.32008 ? 82  LEU   A CG  1 
ATOM   403  C  CD1 . LEU   A 1 70  ? 32.08900  5.32600   7.31900   1.000 16.05799 ? 82  LEU   A CD1 1 
ATOM   404  C  CD2 . LEU   A 1 70  ? 30.92300  7.49200   7.73500   1.000 15.00258 ? 82  LEU   A CD2 1 
ATOM   405  N  N   . ILE   A 1 71  ? 31.44300  4.87300   3.67200   1.000 11.66474 ? 83  ILE   A N   1 
ATOM   406  C  CA  . ILE   A 1 71  ? 30.23200  4.44300   2.97900   1.000 12.67035 ? 83  ILE   A CA  1 
ATOM   407  C  C   . ILE   A 1 71  ? 29.22400  4.03400   4.04700   1.000 11.28848 ? 83  ILE   A C   1 
ATOM   408  O  O   . ILE   A 1 71  ? 29.42200  3.03700   4.75600   1.000 11.92240 ? 83  ILE   A O   1 
ATOM   409  C  CB  . ILE   A 1 71  ? 30.48000  3.27800   2.01200   1.000 11.79994 ? 83  ILE   A CB  1 
ATOM   410  C  CG1 . ILE   A 1 71  ? 31.64700  3.57900   1.06000   1.000 14.64308 ? 83  ILE   A CG1 1 
ATOM   411  C  CG2 . ILE   A 1 71  ? 29.19400  2.96700   1.26100   1.000 14.81675 ? 83  ILE   A CG2 1 
ATOM   412  C  CD1 . ILE   A 1 71  ? 31.43900  4.76300   0.12500   1.000 12.28703 ? 83  ILE   A CD1 1 
ATOM   413  N  N   . ASP   A 1 72  ? 28.14800  4.81400   4.14900   1.000 11.34230 ? 84  ASP   A N   1 
ATOM   414  C  CA  . ASP   A 1 72  ? 26.99500  4.58900   5.02100   1.000 11.47634 ? 84  ASP   A CA  1 
ATOM   415  C  C   . ASP   A 1 72  ? 27.25900  4.90800   6.47900   1.000 12.49844 ? 84  ASP   A C   1 
ATOM   416  O  O   . ASP   A 1 72  ? 28.37800  4.74800   6.97500   1.000 12.62739 ? 84  ASP   A O   1 
ATOM   417  C  CB  . ASP   A 1 72  ? 26.39800  3.19800   4.80700   1.000 10.96939 ? 84  ASP   A CB  1 
ATOM   418  C  CG  . ASP   A 1 72  ? 25.70600  3.08600   3.45300   1.000 12.37047 ? 84  ASP   A CG  1 
ATOM   419  O  OD1 . ASP   A 1 72  ? 25.16800  4.11300   3.00200   1.000 12.21007 ? 84  ASP   A OD1 1 
ATOM   420  O  OD2 . ASP   A 1 72  ? 25.72500  1.98800   2.83500   1.000 12.23883 ? 84  ASP   A OD2 1 
ATOM   421  N  N   . THR   A 1 73  ? 26.22700  5.42300   7.15000   1.000 12.54248 ? 85  THR   A N   1 
ATOM   422  C  CA  . THR   A 1 73  ? 26.28700  5.64500   8.58100   1.000 14.95767 ? 85  THR   A CA  1 
ATOM   423  C  C   . THR   A 1 73  ? 26.19800  4.30100   9.30400   1.000 14.90778 ? 85  THR   A C   1 
ATOM   424  O  O   . THR   A 1 73  ? 26.04700  3.23400   8.69800   1.000 14.64933 ? 85  THR   A O   1 
ATOM   425  C  CB  . THR   A 1 73  ? 25.12300  6.53600   9.01900   1.000 13.68603 ? 85  THR   A CB  1 
ATOM   426  O  OG1 . THR   A 1 73  ? 23.88800  5.83000   8.80800   1.000 18.88934 ? 85  THR   A OG1 1 
ATOM   427  C  CG2 . THR   A 1 73  ? 25.09800  7.84300   8.26300   1.000 16.07797 ? 85  THR   A CG2 1 
ATOM   428  N  N   . ALA   A 1 74  ? 26.28500  4.35000   10.63400  1.000 13.60523 ? 86  ALA   A N   1 
ATOM   429  C  CA  . ALA   A 1 74  ? 26.13200  3.15200   11.44600  1.000 15.10829 ? 86  ALA   A CA  1 
ATOM   430  C  C   . ALA   A 1 74  ? 24.73100  3.02100   12.03700  1.000 17.92797 ? 86  ALA   A C   1 
ATOM   431  O  O   . ALA   A 1 74  ? 24.57000  2.44600   13.11900  1.000 21.91094 ? 86  ALA   A O   1 
ATOM   432  C  CB  . ALA   A 1 74  ? 27.22800  3.04400   12.50900  1.000 15.89883 ? 86  ALA   A CB  1 
ATOM   433  N  N   . TRP   A 1 75  ? 23.70600  3.49200   11.31800  1.000 20.54407 ? 87  TRP   A N   1 
ATOM   434  C  CA  . TRP   A 1 75  ? 22.31200  3.33300   11.72200  1.000 21.38063 ? 87  TRP   A CA  1 
ATOM   435  C  C   . TRP   A 1 75  ? 21.99300  4.07000   13.01900  1.000 23.49948 ? 87  TRP   A C   1 
ATOM   436  O  O   . TRP   A 1 75  ? 21.70800  3.43700   14.04400  1.000 25.23949 ? 87  TRP   A O   1 
ATOM   437  C  CB  . TRP   A 1 75  ? 21.93500  1.85600   11.86700  1.000 20.19490 ? 87  TRP   A CB  1 
ATOM   438  C  CG  . TRP   A 1 75  ? 20.47500  1.56100   11.72200  1.000 18.54352 ? 87  TRP   A CG  1 
ATOM   439  C  CD1 . TRP   A 1 75  ? 19.42800  2.44900   11.77700  1.000 22.40088 ? 87  TRP   A CD1 1 
ATOM   440  C  CD2 . TRP   A 1 75  ? 19.89100  0.25800   11.67000  1.000 23.93103 ? 87  TRP   A CD2 1 
ATOM   441  N  NE1 . TRP   A 1 75  ? 18.22800  1.77100   11.66900  1.000 24.84633 ? 87  TRP   A NE1 1 
ATOM   442  C  CE2 . TRP   A 1 75  ? 18.49100  0.42600   11.60400  1.000 26.36475 ? 87  TRP   A CE2 1 
ATOM   443  C  CE3 . TRP   A 1 75  ? 20.41900  -1.03100  11.60900  1.000 19.70099 ? 87  TRP   A CE3 1 
ATOM   444  C  CZ2 . TRP   A 1 75  ? 17.61600  -0.65900  11.50500  1.000 29.88994 ? 87  TRP   A CZ2 1 
ATOM   445  C  CZ3 . TRP   A 1 75  ? 19.55100  -2.10900  11.52000  1.000 24.40645 ? 87  TRP   A CZ3 1 
ATOM   446  C  CH2 . TRP   A 1 75  ? 18.16600  -1.91300  11.46800  1.000 30.42836 ? 87  TRP   A CH2 1 
ATOM   447  N  N   . GLY   A 1 76  ? 22.00500  5.39100   12.98100  1.000 23.34944 ? 88  GLY   A N   1 
ATOM   448  C  CA  . GLY   A 1 76  ? 21.61900  6.17000   14.14800  1.000 19.63148 ? 88  GLY   A CA  1 
ATOM   449  C  C   . GLY   A 1 76  ? 22.69200  7.11300   14.65100  1.000 20.52340 ? 88  GLY   A C   1 
ATOM   450  O  O   . GLY   A 1 76  ? 23.88200  6.88200   14.43200  1.000 20.11178 ? 88  GLY   A O   1 
ATOM   451  N  N   . ALA   A 1 77  ? 22.27300  8.18400   15.33400  1.000 18.79585 ? 89  ALA   A N   1 
ATOM   452  C  CA  . ALA   A 1 77  ? 23.21100  9.21900   15.76600  1.000 18.20977 ? 89  ALA   A CA  1 
ATOM   453  C  C   . ALA   A 1 77  ? 24.23200  8.68600   16.76600  1.000 18.24354 ? 89  ALA   A C   1 
ATOM   454  O  O   . ALA   A 1 77  ? 25.43400  8.93500   16.62500  1.000 20.66960 ? 89  ALA   A O   1 
ATOM   455  C  CB  . ALA   A 1 77  ? 22.45800  10.41400  16.35700  1.000 20.61629 ? 89  ALA   A CB  1 
ATOM   456  N  N   A LYS   A 1 78  ? 23.77600  7.96500   17.79200  0.587 20.39683 ? 90  LYS   A N   1 
ATOM   457  N  N   B LYS   A 1 78  ? 23.77300  7.96100   17.79000  0.413 20.41569 ? 90  LYS   A N   1 
ATOM   458  C  CA  A LYS   A 1 78  ? 24.71100  7.46700   18.79800  0.587 21.24097 ? 90  LYS   A CA  1 
ATOM   459  C  CA  B LYS   A 1 78  ? 24.70000  7.45900   18.80200  0.413 21.30849 ? 90  LYS   A CA  1 
ATOM   460  C  C   A LYS   A 1 78  ? 25.67200  6.44500   18.20500  0.587 20.15691 ? 90  LYS   A C   1 
ATOM   461  C  C   B LYS   A 1 78  ? 25.66800  6.44200   18.20900  0.413 20.19438 ? 90  LYS   A C   1 
ATOM   462  O  O   A LYS   A 1 78  ? 26.87400  6.47800   18.49400  0.587 19.67489 ? 90  LYS   A O   1 
ATOM   463  O  O   B LYS   A 1 78  ? 26.87100  6.48600   18.49400  0.413 19.72353 ? 90  LYS   A O   1 
ATOM   464  C  CB  A LYS   A 1 78  ? 23.95600  6.88800   19.99500  0.587 25.85884 ? 90  LYS   A CB  1 
ATOM   465  C  CB  B LYS   A 1 78  ? 23.93300  6.86700   19.99000  0.413 25.83765 ? 90  LYS   A CB  1 
ATOM   466  C  CG  A LYS   A 1 78  ? 22.74900  7.71300   20.41200  0.587 26.37476 ? 90  LYS   A CG  1 
ATOM   467  C  CG  B LYS   A 1 78  ? 24.81500  6.37900   21.13600  0.413 25.67797 ? 90  LYS   A CG  1 
ATOM   468  C  CD  A LYS   A 1 78  ? 22.05100  7.11000   21.62200  0.587 28.44587 ? 90  LYS   A CD  1 
ATOM   469  C  CD  B LYS   A 1 78  ? 24.03400  5.58200   22.18200  0.413 31.10415 ? 90  LYS   A CD  1 
ATOM   470  C  CE  A LYS   A 1 78  ? 22.79500  7.42800   22.90600  0.587 30.38013 ? 90  LYS   A CE  1 
ATOM   471  C  CE  B LYS   A 1 78  ? 24.90700  5.16300   23.35600  0.413 29.94832 ? 90  LYS   A CE  1 
ATOM   472  N  NZ  A LYS   A 1 78  ? 22.38900  8.75200   23.46400  0.587 35.32010 ? 90  LYS   A NZ  1 
ATOM   473  N  NZ  B LYS   A 1 78  ? 25.31600  6.33500   24.18800  0.413 36.14750 ? 90  LYS   A NZ  1 
ATOM   474  N  N   . ASN   A 1 79  ? 25.16400  5.52200   17.38000  1.000 18.67970 ? 91  ASN   A N   1 
ATOM   475  C  CA  . ASN   A 1 79  ? 26.04000  4.55500   16.72300  1.000 16.41004 ? 91  ASN   A CA  1 
ATOM   476  C  C   . ASN   A 1 79  ? 27.04900  5.25500   15.81600  1.000 15.21440 ? 91  ASN   A C   1 
ATOM   477  O  O   . ASN   A 1 79  ? 28.21100  4.84700   15.74600  1.000 16.01610 ? 91  ASN   A O   1 
ATOM   478  C  CB  . ASN   A 1 79  ? 25.21100  3.60000   15.85600  1.000 20.61676 ? 91  ASN   A CB  1 
ATOM   479  C  CG  . ASN   A 1 79  ? 24.58600  2.45400   16.63800  1.000 25.31797 ? 91  ASN   A CG  1 
ATOM   480  O  OD1 . ASN   A 1 79  ? 24.83800  2.27500   17.82800  1.000 26.05826 ? 91  ASN   A OD1 1 
ATOM   481  N  ND2 . ASN   A 1 79  ? 23.74500  1.67600   15.95700  1.000 25.29381 ? 91  ASN   A ND2 1 
ATOM   482  N  N   . THR   A 1 80  ? 26.61300  6.29600   15.10100  1.000 15.57960 ? 92  THR   A N   1 
ATOM   483  C  CA  . THR   A 1 80  ? 27.50700  6.98200   14.17200  1.000 15.11511 ? 92  THR   A CA  1 
ATOM   484  C  C   . THR   A 1 80  ? 28.56100  7.79600   14.92200  1.000 15.84188 ? 92  THR   A C   1 
ATOM   485  O  O   . THR   A 1 80  ? 29.71500  7.88100   14.48900  1.000 17.23114 ? 92  THR   A O   1 
ATOM   486  C  CB  . THR   A 1 80  ? 26.68200  7.82100   13.19200  1.000 16.38779 ? 92  THR   A CB  1 
ATOM   487  O  OG1 . THR   A 1 80  ? 25.84100  6.93200   12.44200  1.000 15.79415 ? 92  THR   A OG1 1 
ATOM   488  C  CG2 . THR   A 1 80  ? 27.57200  8.56000   12.20400  1.000 15.48134 ? 92  THR   A CG2 1 
ATOM   489  N  N   . ALA   A 1 81  ? 28.19300  8.38800   16.06500  1.000 17.06416 ? 93  ALA   A N   1 
ATOM   490  C  CA  . ALA   A 1 81  ? 29.20100  8.99500   16.92700  1.000 18.10676 ? 93  ALA   A CA  1 
ATOM   491  C  C   . ALA   A 1 81  ? 30.22000  7.96000   17.39000  1.000 15.98693 ? 93  ALA   A C   1 
ATOM   492  O  O   . ALA   A 1 81  ? 31.43300  8.20300   17.33700  1.000 17.69956 ? 93  ALA   A O   1 
ATOM   493  C  CB  . ALA   A 1 81  ? 28.52700  9.69200   18.11200  1.000 18.15486 ? 93  ALA   A CB  1 
ATOM   494  N  N   . ALA   A 1 82  ? 29.75600  6.77900   17.80100  1.000 16.45659 ? 94  ALA   A N   1 
ATOM   495  C  CA  . ALA   A 1 82  ? 30.69500  5.73400   18.19600  1.000 18.48367 ? 94  ALA   A CA  1 
ATOM   496  C  C   . ALA   A 1 82  ? 31.55900  5.27600   17.02100  1.000 16.14590 ? 94  ALA   A C   1 
ATOM   497  O  O   . ALA   A 1 82  ? 32.74000  4.95400   17.19500  1.000 18.13329 ? 94  ALA   A O   1 
ATOM   498  C  CB  . ALA   A 1 82  ? 29.95800  4.55500   18.83300  1.000 16.90123 ? 94  ALA   A CB  1 
ATOM   499  N  N   . LEU   A 1 83  ? 30.98900  5.24800   15.81000  1.000 16.05122 ? 95  LEU   A N   1 
ATOM   500  C  CA  . LEU   A 1 83  ? 31.77100  4.89700   14.63000  1.000 14.20832 ? 95  LEU   A CA  1 
ATOM   501  C  C   . LEU   A 1 83  ? 32.91500  5.88100   14.42300  1.000 15.15846 ? 95  LEU   A C   1 
ATOM   502  O  O   . LEU   A 1 83  ? 34.06300  5.47200   14.22300  1.000 15.43973 ? 95  LEU   A O   1 
ATOM   503  C  CB  . LEU   A 1 83  ? 30.85600  4.88900   13.40600  1.000 15.75337 ? 95  LEU   A CB  1 
ATOM   504  C  CG  . LEU   A 1 83  ? 31.50400  4.88000   12.02200  1.000 15.35470 ? 95  LEU   A CG  1 
ATOM   505  C  CD1 . LEU   A 1 83  ? 32.32800  3.60200   11.80400  1.000 17.73791 ? 95  LEU   A CD1 1 
ATOM   506  C  CD2 . LEU   A 1 83  ? 30.41300  5.00900   10.93900  1.000 17.03090 ? 95  LEU   A CD2 1 
ATOM   507  N  N   . LEU   A 1 84  ? 32.62300  7.18400   14.47000  1.000 15.01827 ? 96  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 84  ? 33.69700  8.16000   14.31200  1.000 15.48361 ? 96  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 84  ? 34.74700  8.00400   15.41000  1.000 15.75372 ? 96  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 84  ? 35.95200  8.10300   15.14900  1.000 16.00457 ? 96  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 84  ? 33.12700  9.57500   14.29900  1.000 15.08734 ? 96  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 84  ? 32.22300  9.90200   13.11300  1.000 16.03742 ? 96  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 84  ? 31.81800  11.36700  13.16700  1.000 17.71425 ? 96  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 84  ? 32.92600  9.60400   11.81000  1.000 17.63122 ? 96  LEU   A CD2 1 
ATOM   515  N  N   . ALA   A 1 85  ? 34.31400  7.72000   16.63700  1.000 14.95456 ? 97  ALA   A N   1 
ATOM   516  C  CA  . ALA   A 1 85  ? 35.28500  7.55000   17.71600  1.000 16.16804 ? 97  ALA   A CA  1 
ATOM   517  C  C   . ALA   A 1 85  ? 36.15300  6.31800   17.48400  1.000 17.50301 ? 97  ALA   A C   1 
ATOM   518  O  O   . ALA   A 1 85  ? 37.36300  6.32700   17.76300  1.000 17.69566 ? 97  ALA   A O   1 
ATOM   519  C  CB  . ALA   A 1 85  ? 34.56500  7.48400   19.06300  1.000 16.67395 ? 97  ALA   A CB  1 
ATOM   520  N  N   . GLU   A 1 86  ? 35.56400  5.24300   16.95700  1.000 16.71493 ? 98  GLU   A N   1 
ATOM   521  C  CA  . GLU   A 1 86  ? 36.34600  4.03600   16.71900  1.000 16.36181 ? 98  GLU   A CA  1 
ATOM   522  C  C   . GLU   A 1 86  ? 37.32300  4.22400   15.56300  1.000 16.54974 ? 98  GLU   A C   1 
ATOM   523  O  O   . GLU   A 1 86  ? 38.46200  3.75000   15.61400  1.000 16.84123 ? 98  GLU   A O   1 
ATOM   524  C  CB  . GLU   A 1 86  ? 35.40000  2.86700   16.45900  1.000 19.77959 ? 98  GLU   A CB  1 
ATOM   525  C  CG  . GLU   A 1 86  ? 36.07700  1.52000   16.43300  1.000 22.59102 ? 98  GLU   A CG  1 
ATOM   526  C  CD  . GLU   A 1 86  ? 36.53100  1.07000   17.81200  1.000 25.74692 ? 98  GLU   A CD  1 
ATOM   527  O  OE1 . GLU   A 1 86  ? 35.95500  1.53300   18.81400  1.000 26.67905 ? 98  GLU   A OE1 1 
ATOM   528  O  OE2 . GLU   A 1 86  ? 37.44900  0.22900   17.88200  1.000 38.45940 ? 98  GLU   A OE2 1 
ATOM   529  N  N   . ILE   A 1 87  ? 36.89100  4.91800   14.51100  1.000 17.33110 ? 99  ILE   A N   1 
ATOM   530  C  CA  . ILE   A 1 87  ? 37.78800  5.24000   13.40300  1.000 17.69639 ? 99  ILE   A CA  1 
ATOM   531  C  C   . ILE   A 1 87  ? 38.98600  6.05000   13.89600  1.000 16.23142 ? 99  ILE   A C   1 
ATOM   532  O  O   . ILE   A 1 87  ? 40.13900  5.77300   13.53500  1.000 18.94370 ? 99  ILE   A O   1 
ATOM   533  C  CB  . ILE   A 1 87  ? 37.02000  5.98000   12.30000  1.000 16.66280 ? 99  ILE   A CB  1 
ATOM   534  C  CG1 . ILE   A 1 87  ? 36.02100  5.04500   11.62400  1.000 16.62671 ? 99  ILE   A CG1 1 
ATOM   535  C  CG2 . ILE   A 1 87  ? 37.98100  6.58500   11.29600  1.000 18.37363 ? 99  ILE   A CG2 1 
ATOM   536  C  CD1 . ILE   A 1 87  ? 35.18300  5.73800   10.59700  1.000 17.41190 ? 99  ILE   A CD1 1 
ATOM   537  N  N   . GLU   A 1 88  ? 38.73300  7.07800   14.71300  1.000 17.04283 ? 100 GLU   A N   1 
ATOM   538  C  CA  . GLU   A 1 88  ? 39.84800  7.87800   15.21800  1.000 19.10994 ? 100 GLU   A CA  1 
ATOM   539  C  C   . GLU   A 1 88  ? 40.77100  7.03400   16.08900  1.000 19.06174 ? 100 GLU   A C   1 
ATOM   540  O  O   . GLU   A 1 88  ? 42.00100  7.15700   16.01400  1.000 22.22906 ? 100 GLU   A O   1 
ATOM   541  C  CB  . GLU   A 1 88  ? 39.32700  9.10100   15.97000  1.000 23.45543 ? 100 GLU   A CB  1 
ATOM   542  C  CG  . GLU   A 1 88  ? 40.42000  10.10200  16.39600  1.000 33.47791 ? 100 GLU   A CG  1 
ATOM   543  C  CD  . GLU   A 1 88  ? 41.30900  10.62900  15.25400  1.000 44.89081 ? 100 GLU   A CD  1 
ATOM   544  O  OE1 . GLU   A 1 88  ? 40.92500  10.56100  14.06600  1.000 38.48051 ? 100 GLU   A OE1 1 
ATOM   545  O  OE2 . GLU   A 1 88  ? 42.42000  11.12000  15.55600  1.000 48.28507 ? 100 GLU   A OE2 1 
ATOM   546  N  N   . LYS   A 1 89  ? 40.19500  6.14000   16.88800  1.000 16.42632 ? 101 LYS   A N   1 
ATOM   547  C  CA  . LYS   A 1 89  ? 41.00100  5.30900   17.77500  1.000 18.08796 ? 101 LYS   A CA  1 
ATOM   548  C  C   . LYS   A 1 89  ? 41.84800  4.29100   17.00400  1.000 20.64324 ? 101 LYS   A C   1 
ATOM   549  O  O   . LYS   A 1 89  ? 43.03400  4.11100   17.30300  1.000 21.68155 ? 101 LYS   A O   1 
ATOM   550  C  CB  . LYS   A 1 89  ? 40.08700  4.60200   18.78100  1.000 19.94870 ? 101 LYS   A CB  1 
ATOM   551  C  CG  . LYS   A 1 89  ? 40.75200  3.51800   19.59700  1.000 25.50487 ? 101 LYS   A CG  1 
ATOM   552  C  CD  . LYS   A 1 89  ? 39.73500  2.84900   20.51300  1.000 25.31013 ? 101 LYS   A CD  1 
ATOM   553  C  CE  . LYS   A 1 89  ? 40.39800  1.95900   21.54300  1.000 29.39607 ? 101 LYS   A CE  1 
ATOM   554  N  NZ  . LYS   A 1 89  ? 39.40900  1.50200   22.55300  1.000 33.46052 ? 101 LYS   A NZ  1 
ATOM   555  N  N   A GLN   A 1 90  ? 41.26600  3.61800   16.01200  0.512 18.58521 ? 102 GLN   A N   1 
ATOM   556  N  N   B GLN   A 1 90  ? 41.26400  3.61500   16.01600  0.488 18.58922 ? 102 GLN   A N   1 
ATOM   557  C  CA  A GLN   A 1 90  ? 41.93200  2.49200   15.36300  0.512 19.25777 ? 102 GLN   A CA  1 
ATOM   558  C  CA  B GLN   A 1 90  ? 41.95000  2.50200   15.36900  0.488 19.24954 ? 102 GLN   A CA  1 
ATOM   559  C  C   A GLN   A 1 90  ? 42.68100  2.85700   14.09200  0.512 20.17549 ? 102 GLN   A C   1 
ATOM   560  C  C   B GLN   A 1 90  ? 42.72600  2.90200   14.12500  0.488 20.18055 ? 102 GLN   A C   1 
ATOM   561  O  O   A GLN   A 1 90  ? 43.66000  2.18500   13.75600  0.512 22.15871 ? 102 GLN   A O   1 
ATOM   562  O  O   B GLN   A 1 90  ? 43.77200  2.30800   13.84300  0.488 22.21727 ? 102 GLN   A O   1 
ATOM   563  C  CB  A GLN   A 1 90  ? 40.91900  1.39500   15.02000  0.512 22.56363 ? 102 GLN   A CB  1 
ATOM   564  C  CB  B GLN   A 1 90  ? 40.94000  1.41900   14.98600  0.488 22.54937 ? 102 GLN   A CB  1 
ATOM   565  C  CG  A GLN   A 1 90  ? 40.02900  0.98400   16.17100  0.512 21.41498 ? 102 GLN   A CG  1 
ATOM   566  C  CG  B GLN   A 1 90  ? 40.61500  0.45200   16.10300  0.488 25.11693 ? 102 GLN   A CG  1 
ATOM   567  C  CD  A GLN   A 1 90  ? 40.74300  0.11700   17.18900  0.512 27.01651 ? 102 GLN   A CD  1 
ATOM   568  C  CD  B GLN   A 1 90  ? 39.75600  -0.70200  15.63000  0.488 27.69454 ? 102 GLN   A CD  1 
ATOM   569  O  OE1 A GLN   A 1 90  ? 41.95500  -0.08500  17.11600  0.512 30.45509 ? 102 GLN   A OE1 1 
ATOM   570  O  OE1 B GLN   A 1 90  ? 40.18700  -1.52600  14.82000  0.488 28.07061 ? 102 GLN   A OE1 1 
ATOM   571  N  NE2 A GLN   A 1 90  ? 39.99000  -0.39400  18.15500  0.512 27.44783 ? 102 GLN   A NE2 1 
ATOM   572  N  NE2 B GLN   A 1 90  ? 38.52200  -0.75100  16.11300  0.488 26.57058 ? 102 GLN   A NE2 1 
ATOM   573  N  N   . ILE   A 1 91  ? 42.24200  3.87900   13.36400  1.000 19.24508 ? 103 ILE   A N   1 
ATOM   574  C  CA  . ILE   A 1 91  ? 42.84100  4.24100   12.08700  1.000 21.08706 ? 103 ILE   A CA  1 
ATOM   575  C  C   . ILE   A 1 91  ? 43.55100  5.58800   12.15400  1.000 22.70694 ? 103 ILE   A C   1 
ATOM   576  O  O   . ILE   A 1 91  ? 44.65000  5.74300   11.61400  1.000 22.50972 ? 103 ILE   A O   1 
ATOM   577  C  CB  . ILE   A 1 91  ? 41.81300  4.19300   10.93000  1.000 19.70349 ? 103 ILE   A CB  1 
ATOM   578  C  CG1 . ILE   A 1 91  ? 41.10200  2.83300   10.89600  1.000 17.87350 ? 103 ILE   A CG1 1 
ATOM   579  C  CG2 . ILE   A 1 91  ? 42.47500  4.53600   9.60000   1.000 19.26067 ? 103 ILE   A CG2 1 
ATOM   580  C  CD1 . ILE   A 1 91  ? 39.99100  2.73500   9.83100   1.000 17.79348 ? 103 ILE   A CD1 1 
ATOM   581  N  N   . GLY   A 1 92  ? 42.94200  6.57300   12.80800  1.000 18.73921 ? 104 GLY   A N   1 
ATOM   582  C  CA  . GLY   A 1 92  ? 43.61800  7.83800   13.04400  1.000 21.56623 ? 104 GLY   A CA  1 
ATOM   583  C  C   . GLY   A 1 92  ? 43.77400  8.73100   11.84000  1.000 20.79845 ? 104 GLY   A C   1 
ATOM   584  O  O   . GLY   A 1 92  ? 44.61500  9.63800   11.85600  1.000 25.45468 ? 104 GLY   A O   1 
ATOM   585  N  N   . LEU   A 1 93  ? 42.98100  8.51900   10.79700  1.000 20.34761 ? 105 LEU   A N   1 
ATOM   586  C  CA  . LEU   A 1 93  ? 42.93600  9.37000   9.62700   1.000 19.65421 ? 105 LEU   A CA  1 
ATOM   587  C  C   . LEU   A 1 93  ? 41.55900  10.01800  9.52700   1.000 21.08188 ? 105 LEU   A C   1 
ATOM   588  O  O   . LEU   A 1 93  ? 40.56300  9.43800   9.97000   1.000 22.03014 ? 105 LEU   A O   1 
ATOM   589  C  CB  . LEU   A 1 93  ? 43.19100  8.55700   8.35600   1.000 22.92790 ? 105 LEU   A CB  1 
ATOM   590  C  CG  . LEU   A 1 93  ? 44.59400  7.97200   8.21000   1.000 26.56533 ? 105 LEU   A CG  1 
ATOM   591  C  CD1 . LEU   A 1 93  ? 44.70100  7.16500   6.92400   1.000 27.09762 ? 105 LEU   A CD1 1 
ATOM   592  C  CD2 . LEU   A 1 93  ? 45.63500  9.08300   8.25300   1.000 30.09279 ? 105 LEU   A CD2 1 
ATOM   593  N  N   . PRO   A 1 94  ? 41.46400  11.22000  8.97200   1.000 20.57254 ? 106 PRO   A N   1 
ATOM   594  C  CA  . PRO   A 1 94  ? 40.18400  11.92800  8.99300   1.000 18.80564 ? 106 PRO   A CA  1 
ATOM   595  C  C   . PRO   A 1 94  ? 39.22700  11.39900  7.93400   1.000 19.38028 ? 106 PRO   A C   1 
ATOM   596  O  O   . PRO   A 1 94  ? 39.61600  11.08400  6.80500   1.000 18.28149 ? 106 PRO   A O   1 
ATOM   597  C  CB  . PRO   A 1 94  ? 40.58500  13.37800  8.70200   1.000 23.66413 ? 106 PRO   A CB  1 
ATOM   598  C  CG  . PRO   A 1 94  ? 41.80800  13.25000  7.85700   1.000 26.19004 ? 106 PRO   A CG  1 
ATOM   599  C  CD  . PRO   A 1 94  ? 42.54100  12.03500  8.37700   1.000 24.49605 ? 106 PRO   A CD  1 
ATOM   600  N  N   . VAL   A 1 95  ? 37.95900  11.29500  8.32500   1.000 19.29116 ? 107 VAL   A N   1 
ATOM   601  C  CA  . VAL   A 1 95  ? 36.87800  11.00500  7.38600   1.000 16.81906 ? 107 VAL   A CA  1 
ATOM   602  C  C   . VAL   A 1 95  ? 36.48700  12.33100  6.74700   1.000 16.67406 ? 107 VAL   A C   1 
ATOM   603  O  O   . VAL   A 1 95  ? 35.91600  13.19800  7.40700   1.000 17.71305 ? 107 VAL   A O   1 
ATOM   604  C  CB  . VAL   A 1 95  ? 35.68200  10.35700  8.09900   1.000 16.67028 ? 107 VAL   A CB  1 
ATOM   605  C  CG1 . VAL   A 1 95  ? 34.53700  10.09300  7.10600   1.000 15.93473 ? 107 VAL   A CG1 1 
ATOM   606  C  CG2 . VAL   A 1 95  ? 36.10600  9.08400   8.83100   1.000 18.82366 ? 107 VAL   A CG2 1 
ATOM   607  N  N   . THR   A 1 96  ? 36.81600  12.50400  5.47800   1.000 15.55754 ? 108 THR   A N   1 
ATOM   608  C  CA  . THR   A 1 96  ? 36.54900  13.77300  4.82000   1.000 17.13558 ? 108 THR   A CA  1 
ATOM   609  C  C   . THR   A 1 96  ? 35.27400  13.75900  3.98800   1.000 17.01523 ? 108 THR   A C   1 
ATOM   610  O  O   . THR   A 1 96  ? 34.65400  14.81000  3.80900   1.000 16.56099 ? 108 THR   A O   1 
ATOM   611  C  CB  . THR   A 1 96  ? 37.75300  14.18300  3.95600   1.000 18.47669 ? 108 THR   A CB  1 
ATOM   612  O  OG1 . THR   A 1 96  ? 38.06500  13.14000  3.03100   1.000 20.90565 ? 108 THR   A OG1 1 
ATOM   613  C  CG2 . THR   A 1 96  ? 38.97200  14.43800  4.83400   1.000 21.12280 ? 108 THR   A CG2 1 
ATOM   614  N  N   . ARG   A 1 97  ? 34.84500  12.58400  3.51200   1.000 15.02988 ? 109 ARG   A N   1 
ATOM   615  C  CA  . ARG   A 1 97  ? 33.62300  12.46800  2.73000   1.000 14.06761 ? 109 ARG   A CA  1 
ATOM   616  C  C   . ARG   A 1 97  ? 32.89200  11.19700  3.13000   1.000 13.38782 ? 109 ARG   A C   1 
ATOM   617  O  O   . ARG   A 1 97  ? 33.52000  10.20800  3.52300   1.000 15.54623 ? 109 ARG   A O   1 
ATOM   618  C  CB  . ARG   A 1 97  ? 33.90800  12.46000  1.21900   1.000 16.25610 ? 109 ARG   A CB  1 
ATOM   619  C  CG  . ARG   A 1 97  ? 34.52000  13.77700  0.71300   1.000 17.74291 ? 109 ARG   A CG  1 
ATOM   620  C  CD  . ARG   A 1 97  ? 34.68000  13.80600  -0.79500  1.000 21.39198 ? 109 ARG   A CD  1 
ATOM   621  N  NE  . ARG   A 1 97  ? 35.69900  12.86900  -1.24800  1.000 22.08719 ? 109 ARG   A NE  1 
ATOM   622  C  CZ  . ARG   A 1 97  ? 36.04200  12.69700  -2.51900  1.000 21.58843 ? 109 ARG   A CZ  1 
ATOM   623  N  NH1 . ARG   A 1 97  ? 35.45000  13.37300  -3.49300  1.000 25.50212 ? 109 ARG   A NH1 1 
ATOM   624  N  NH2 . ARG   A 1 97  ? 37.00800  11.83500  -2.82000  1.000 24.54056 ? 109 ARG   A NH2 1 
ATOM   625  N  N   . ALA   A 1 98  ? 31.56100  11.22200  2.97300   1.000 12.92476 ? 110 ALA   A N   1 
ATOM   626  C  CA  . ALA   A 1 98  ? 30.72500  10.05200  3.21300   1.000 13.22324 ? 110 ALA   A CA  1 
ATOM   627  C  C   . ALA   A 1 98  ? 29.65700  9.95300   2.13300   1.000 12.70338 ? 110 ALA   A C   1 
ATOM   628  O  O   . ALA   A 1 98  ? 29.10800  10.96800  1.69400   1.000 14.69279 ? 110 ALA   A O   1 
ATOM   629  C  CB  . ALA   A 1 98  ? 30.05000  10.12800  4.58500   1.000 14.53357 ? 110 ALA   A CB  1 
ATOM   630  N  N   . VAL   A 1 99  ? 29.36800  8.72600   1.71100   1.000 12.21082 ? 111 VAL   A N   1 
ATOM   631  C  CA  . VAL   A 1 99  ? 28.32400  8.44300   0.73600   1.000 11.91632 ? 111 VAL   A CA  1 
ATOM   632  C  C   . VAL   A 1 99  ? 27.29100  7.54800   1.39900   1.000 11.65466 ? 111 VAL   A C   1 
ATOM   633  O  O   . VAL   A 1 99  ? 27.65800  6.52400   1.98600   1.000 13.18670 ? 111 VAL   A O   1 
ATOM   634  C  CB  . VAL   A 1 99  ? 28.91800  7.71800   -0.48200  1.000 11.16734 ? 111 VAL   A CB  1 
ATOM   635  C  CG1 . VAL   A 1 99  ? 27.80900  7.26800   -1.43300  1.000 14.65047 ? 111 VAL   A CG1 1 
ATOM   636  C  CG2 . VAL   A 1 99  ? 29.89100  8.64300   -1.19500  1.000 14.78836 ? 111 VAL   A CG2 1 
ATOM   637  N  N   . SER   A 1 100 ? 26.01300  7.89100   1.25400   1.000 12.32486 ? 112 SER   A N   1 
ATOM   638  C  CA  . SER   A 1 100 ? 24.92100  7.02300   1.69000   1.000 12.60323 ? 112 SER   A CA  1 
ATOM   639  C  C   . SER   A 1 100 ? 24.34800  6.32500   0.47000   1.000 11.65865 ? 112 SER   A C   1 
ATOM   640  O  O   . SER   A 1 100 ? 24.05800  6.97500   -0.54500  1.000 12.47062 ? 112 SER   A O   1 
ATOM   641  C  CB  . SER   A 1 100 ? 23.81400  7.82000   2.38100   1.000 12.43532 ? 112 SER   A CB  1 
ATOM   642  O  OG  . SER   A 1 100 ? 24.24300  8.28000   3.66000   1.000 13.84332 ? 112 SER   A OG  1 
ATOM   643  N  N   . THR   A 1 101 ? 24.17400  5.00100   0.57700   1.000 11.29411 ? 113 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 101 ? 23.84500  4.17800   -0.58100  1.000 11.27512 ? 113 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 101 ? 22.35700  4.00500   -0.82400  1.000 10.74326 ? 113 THR   A C   1 
ATOM   646  O  O   . THR   A 1 101 ? 21.97600  3.57300   -1.92100  1.000 12.99730 ? 113 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 101 ? 24.53100  2.79800   -0.52500  1.000 12.14052 ? 113 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 101 ? 24.16200  2.09000   0.66700   1.000 11.90014 ? 113 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 101 ? 26.03500  2.93900   -0.57900  1.000 13.58697 ? 113 THR   A CG2 1 
ATOM   650  N  N   . HIS   A 1 102 ? 21.50200  4.33700   0.14100   1.000 10.95077 ? 114 HIS   A N   1 
ATOM   651  C  CA  . HIS   A 1 102 ? 20.09400  4.56300   -0.14300  1.000 10.74565 ? 114 HIS   A CA  1 
ATOM   652  C  C   . HIS   A 1 102 ? 19.49900  5.37700   1.00500   1.000 11.18977 ? 114 HIS   A C   1 
ATOM   653  O  O   . HIS   A 1 102 ? 20.19600  5.74600   1.95500   1.000 12.78782 ? 114 HIS   A O   1 
ATOM   654  C  CB  . HIS   A 1 102 ? 19.33100  3.28100   -0.53200  1.000 11.27850 ? 114 HIS   A CB  1 
ATOM   655  C  CG  . HIS   A 1 102 ? 19.08300  2.34300   0.59400   1.000 12.14123 ? 114 HIS   A CG  1 
ATOM   656  N  ND1 . HIS   A 1 102 ? 19.99800  1.39300   1.01400   1.000 11.67226 ? 114 HIS   A ND1 1 
ATOM   657  C  CD2 . HIS   A 1 102 ? 17.98200  2.17200   1.35700   1.000 12.36007 ? 114 HIS   A CD2 1 
ATOM   658  C  CE1 . HIS   A 1 102 ? 19.48200  0.70400   2.01400   1.000 13.26457 ? 114 HIS   A CE1 1 
ATOM   659  N  NE2 . HIS   A 1 102 ? 18.26500  1.16100   2.24100   1.000 13.82081 ? 114 HIS   A NE2 1 
ATOM   660  N  N   . PHE   A 1 103 ? 18.19500  5.63300   0.91300   1.000 11.64822 ? 115 PHE   A N   1 
ATOM   661  C  CA  . PHE   A 1 103 ? 17.59200  6.68900   1.72300   1.000 12.32380 ? 115 PHE   A CA  1 
ATOM   662  C  C   . PHE   A 1 103 ? 17.11800  6.24000   3.09500   1.000 14.04837 ? 115 PHE   A C   1 
ATOM   663  O  O   . PHE   A 1 103 ? 16.69700  7.09300   3.88300   1.000 14.10504 ? 115 PHE   A O   1 
ATOM   664  C  CB  . PHE   A 1 103 ? 16.41600  7.35100   0.99200   1.000 13.07582 ? 115 PHE   A CB  1 
ATOM   665  C  CG  . PHE   A 1 103 ? 15.15800  6.50100   0.90200   1.000 13.58874 ? 115 PHE   A CG  1 
ATOM   666  C  CD1 . PHE   A 1 103 ? 15.02000  5.53600   -0.08600  1.000 13.19704 ? 115 PHE   A CD1 1 
ATOM   667  C  CD2 . PHE   A 1 103 ? 14.08300  6.72000   1.77000   1.000 13.48383 ? 115 PHE   A CD2 1 
ATOM   668  C  CE1 . PHE   A 1 103 ? 13.85100  4.79700   -0.18700  1.000 15.44600 ? 115 PHE   A CE1 1 
ATOM   669  C  CE2 . PHE   A 1 103 ? 12.91600  5.99000   1.67800   1.000 15.37159 ? 115 PHE   A CE2 1 
ATOM   670  C  CZ  . PHE   A 1 103 ? 12.79600  5.02100   0.70500   1.000 14.05843 ? 115 PHE   A CZ  1 
ATOM   671  N  N   . HIS   A 1 104 ? 17.16000  4.95400   3.40500   1.000 12.51194 ? 116 HIS   A N   1 
ATOM   672  C  CA  . HIS   A 1 104 ? 16.60700  4.48600   4.66800   1.000 12.91004 ? 116 HIS   A CA  1 
ATOM   673  C  C   . HIS   A 1 104 ? 17.53500  4.81400   5.83900   1.000 13.51267 ? 116 HIS   A C   1 
ATOM   674  O  O   . HIS   A 1 104 ? 18.71400  5.12300   5.67000   1.000 12.88930 ? 116 HIS   A O   1 
ATOM   675  C  CB  . HIS   A 1 104 ? 16.37000  2.98400   4.59600   1.000 13.00440 ? 116 HIS   A CB  1 
ATOM   676  C  CG  . HIS   A 1 104 ? 15.21200  2.59100   3.73100   1.000 13.29802 ? 116 HIS   A CG  1 
ATOM   677  N  ND1 . HIS   A 1 104 ? 15.15700  1.37100   3.11000   1.000 14.21659 ? 116 HIS   A ND1 1 
ATOM   678  C  CD2 . HIS   A 1 104 ? 14.05500  3.21100   3.41000   1.000 15.87452 ? 116 HIS   A CD2 1 
ATOM   679  C  CE1 . HIS   A 1 104 ? 14.03700  1.24300   2.43600   1.000 14.05697 ? 116 HIS   A CE1 1 
ATOM   680  N  NE2 . HIS   A 1 104 ? 13.34300  2.35000   2.60300   1.000 14.73116 ? 116 HIS   A NE2 1 
ATOM   681  N  N   A ASP   A 1 105 ? 16.97400  4.73300   7.05100   0.677 14.57501 ? 117 ASP   A N   1 
ATOM   682  N  N   B ASP   A 1 105 ? 16.96500  4.70700   7.04700   0.323 14.72062 ? 117 ASP   A N   1 
ATOM   683  C  CA  A ASP   A 1 105 ? 17.66600  5.17600   8.26200   0.677 15.42986 ? 117 ASP   A CA  1 
ATOM   684  C  CA  B ASP   A 1 105 ? 17.63300  5.14900   8.26800   0.323 15.51808 ? 117 ASP   A CA  1 
ATOM   685  C  C   A ASP   A 1 105 ? 18.92900  4.38700   8.57400   0.677 14.80308 ? 117 ASP   A C   1 
ATOM   686  C  C   B ASP   A 1 105 ? 18.94300  4.41600   8.51100   0.323 14.86792 ? 117 ASP   A C   1 
ATOM   687  O  O   A ASP   A 1 105 ? 19.80700  4.88900   9.28800   0.677 15.36340 ? 117 ASP   A O   1 
ATOM   688  O  O   B ASP   A 1 105 ? 19.87000  4.98500   9.09900   0.323 16.21454 ? 117 ASP   A O   1 
ATOM   689  C  CB  A ASP   A 1 105 ? 16.72200  5.05500   9.46100   0.677 18.42919 ? 117 ASP   A CB  1 
ATOM   690  C  CB  B ASP   A 1 105 ? 16.71500  4.91900   9.47100   0.323 18.30063 ? 117 ASP   A CB  1 
ATOM   691  C  CG  A ASP   A 1 105 ? 17.15800  5.90100   10.63000  0.677 21.11787 ? 117 ASP   A CG  1 
ATOM   692  C  CG  B ASP   A 1 105 ? 15.81800  6.10300   9.75600   0.323 20.38841 ? 117 ASP   A CG  1 
ATOM   693  O  OD1 A ASP   A 1 105 ? 17.40200  7.10800   10.42600  0.677 22.22740 ? 117 ASP   A OD1 1 
ATOM   694  O  OD1 B ASP   A 1 105 ? 16.16900  7.22700   9.34800   0.323 19.81474 ? 117 ASP   A OD1 1 
ATOM   695  O  OD2 A ASP   A 1 105 ? 17.26200  5.35600   11.74800  0.677 24.24958 ? 117 ASP   A OD2 1 
ATOM   696  O  OD2 B ASP   A 1 105 ? 14.76700  5.90900   10.40600  0.323 23.41652 ? 117 ASP   A OD2 1 
ATOM   697  N  N   . ASP   A 1 106 ? 19.03800  3.15000   8.09900   1.000 13.05700 ? 118 ASP   A N   1 
ATOM   698  C  CA  . ASP   A 1 106 ? 20.27400  2.42200   8.34600   1.000 13.35096 ? 118 ASP   A CA  1 
ATOM   699  C  C   . ASP   A 1 106 ? 21.43000  2.91100   7.48000   1.000 15.53918 ? 118 ASP   A C   1 
ATOM   700  O  O   . ASP   A 1 106 ? 22.58000  2.50400   7.69800   1.000 16.58488 ? 118 ASP   A O   1 
ATOM   701  C  CB  . ASP   A 1 106 ? 20.07700  0.89500   8.28600   1.000 13.41299 ? 118 ASP   A CB  1 
ATOM   702  C  CG  . ASP   A 1 106 ? 19.81300  0.36300   6.89400   1.000 13.44773 ? 118 ASP   A CG  1 
ATOM   703  O  OD1 . ASP   A 1 106 ? 19.45900  1.10000   5.96400   1.000 15.68781 ? 118 ASP   A OD1 1 
ATOM   704  O  OD2 . ASP   A 1 106 ? 19.96700  -0.85800  6.73100   1.000 14.48522 ? 118 ASP   A OD2 1 
ATOM   705  N  N   . ARG   A 1 107 ? 21.15400  3.78700   6.52200   1.000 12.78087 ? 119 ARG   A N   1 
ATOM   706  C  CA  . ARG   A 1 107 ? 22.17900  4.35300   5.65900   1.000 13.31634 ? 119 ARG   A CA  1 
ATOM   707  C  C   . ARG   A 1 107 ? 22.40900  5.83200   5.88400   1.000 13.67274 ? 119 ARG   A C   1 
ATOM   708  O  O   . ARG   A 1 107 ? 23.53200  6.30200   5.66600   1.000 14.84121 ? 119 ARG   A O   1 
ATOM   709  C  CB  . ARG   A 1 107 ? 21.80400  4.18200   4.18300   1.000 11.32371 ? 119 ARG   A CB  1 
ATOM   710  C  CG  . ARG   A 1 107 ? 21.45500  2.76900   3.76300   1.000 12.61297 ? 119 ARG   A CG  1 
ATOM   711  C  CD  . ARG   A 1 107 ? 22.62500  1.82200   3.86700   1.000 13.43985 ? 119 ARG   A CD  1 
ATOM   712  N  NE  . ARG   A 1 107 ? 22.36600  0.74700   4.81100   1.000 14.39080 ? 119 ARG   A NE  1 
ATOM   713  C  CZ  . ARG   A 1 107 ? 23.32000  -0.02800  5.30400   1.000 16.18241 ? 119 ARG   A CZ  1 
ATOM   714  N  NH1 . ARG   A 1 107 ? 24.59100  0.16000   4.98800   1.000 17.65209 ? 119 ARG   A NH1 1 
ATOM   715  N  NH2 . ARG   A 1 107 ? 22.99400  -1.00400  6.15000   1.000 18.90180 ? 119 ARG   A NH2 1 
ATOM   716  N  N   . VAL   A 1 108 ? 21.35900  6.57300   6.25200   1.000 13.10949 ? 120 VAL   A N   1 
ATOM   717  C  CA  . VAL   A 1 108 ? 21.43100  8.02000   6.45500   1.000 12.31574 ? 120 VAL   A CA  1 
ATOM   718  C  C   . VAL   A 1 108 ? 21.26600  8.43400   7.90700   1.000 13.32772 ? 120 VAL   A C   1 
ATOM   719  O  O   . VAL   A 1 108 ? 21.49000  9.61500   8.22000   1.000 13.97802 ? 120 VAL   A O   1 
ATOM   720  C  CB  . VAL   A 1 108 ? 20.43500  8.80500   5.57300   1.000 12.42646 ? 120 VAL   A CB  1 
ATOM   721  C  CG1 . VAL   A 1 108 ? 20.68400  8.56200   4.10400   1.000 13.59343 ? 120 VAL   A CG1 1 
ATOM   722  C  CG2 . VAL   A 1 108 ? 18.98400  8.52400   5.95400   1.000 14.76330 ? 120 VAL   A CG2 1 
ATOM   723  N  N   . GLY   A 1 109 ? 20.83800  7.53400   8.79100   1.000 13.32926 ? 121 GLY   A N   1 
ATOM   724  C  CA  . GLY   A 1 109 ? 20.64400  7.88200   10.19300  1.000 14.99141 ? 121 GLY   A CA  1 
ATOM   725  C  C   . GLY   A 1 109 ? 22.00300  8.08800   10.80300  1.000 17.38081 ? 121 GLY   A C   1 
ATOM   726  O  O   . GLY   A 1 109 ? 22.76500  7.12600   10.89700  1.000 19.00391 ? 121 GLY   A O   1 
ATOM   727  N  N   . GLY   A 1 110 ? 22.32900  9.31100   11.21600  1.000 19.55486 ? 122 GLY   A N   1 
ATOM   728  C  CA  . GLY   A 1 110 ? 23.70300  9.64000   11.55200  1.000 17.03267 ? 122 GLY   A CA  1 
ATOM   729  C  C   . GLY   A 1 110 ? 24.34800  10.64200  10.62400  1.000 15.37906 ? 122 GLY   A C   1 
ATOM   730  O  O   . GLY   A 1 110 ? 25.45500  11.11700  10.92100  1.000 14.94636 ? 122 GLY   A O   1 
ATOM   731  N  N   . VAL   A 1 111 ? 23.68500  10.98900  9.51600   1.000 13.82294 ? 123 VAL   A N   1 
ATOM   732  C  CA  . VAL   A 1 111 ? 24.19800  12.02400  8.61400   1.000 12.78033 ? 123 VAL   A CA  1 
ATOM   733  C  C   . VAL   A 1 111 ? 24.40500  13.35200  9.34400   1.000 14.89125 ? 123 VAL   A C   1 
ATOM   734  O  O   . VAL   A 1 111 ? 25.40000  14.04900  9.10300   1.000 15.19100 ? 123 VAL   A O   1 
ATOM   735  C  CB  . VAL   A 1 111 ? 23.30000  12.15900  7.36600   1.000 12.76238 ? 123 VAL   A CB  1 
ATOM   736  C  CG1 . VAL   A 1 111 ? 23.37500  13.57700  6.77000   1.000 15.71000 ? 123 VAL   A CG1 1 
ATOM   737  C  CG2 . VAL   A 1 111 ? 23.71900  11.13500  6.32700   1.000 15.66426 ? 123 VAL   A CG2 1 
ATOM   738  N  N   . ASP   A 1 112 ? 23.48900  13.72000  10.25100  1.000 15.02863 ? 124 ASP   A N   1 
ATOM   739  C  CA  . ASP   A 1 112 ? 23.65300  14.98900  10.96300  1.000 16.09013 ? 124 ASP   A CA  1 
ATOM   740  C  C   . ASP   A 1 112 ? 24.88000  14.95600  11.87300  1.000 14.45690 ? 124 ASP   A C   1 
ATOM   741  O  O   . ASP   A 1 112 ? 25.58000  15.96700  12.01000  1.000 18.37495 ? 124 ASP   A O   1 
ATOM   742  C  CB  . ASP   A 1 112 ? 22.38600  15.33100  11.76100  1.000 20.32638 ? 124 ASP   A CB  1 
ATOM   743  C  CG  . ASP   A 1 112 ? 21.19700  15.72700  10.87700  1.000 21.39095 ? 124 ASP   A CG  1 
ATOM   744  O  OD1 . ASP   A 1 112 ? 21.34400  15.80000  9.64100   1.000 24.08602 ? 124 ASP   A OD1 1 
ATOM   745  O  OD2 . ASP   A 1 112 ? 20.09100  15.95000  11.42200  1.000 26.06485 ? 124 ASP   A OD2 1 
ATOM   746  N  N   . VAL   A 1 113 ? 25.16300  13.80300  12.48800  1.000 15.59643 ? 125 VAL   A N   1 
ATOM   747  C  CA  . VAL   A 1 113 ? 26.38200  13.63800  13.27800  1.000 15.43856 ? 125 VAL   A CA  1 
ATOM   748  C  C   . VAL   A 1 113 ? 27.62200  13.81400  12.40500  1.000 18.76644 ? 125 VAL   A C   1 
ATOM   749  O  O   . VAL   A 1 113 ? 28.58600  14.49400  12.78800  1.000 17.51555 ? 125 VAL   A O   1 
ATOM   750  C  CB  . VAL   A 1 113 ? 26.37200  12.27500  14.00000  1.000 15.49046 ? 125 VAL   A CB  1 
ATOM   751  C  CG1 . VAL   A 1 113 ? 27.76400  11.90600  14.49900  1.000 18.33872 ? 125 VAL   A CG1 1 
ATOM   752  C  CG2 . VAL   A 1 113 ? 25.37000  12.28900  15.16600  1.000 20.52146 ? 125 VAL   A CG2 1 
ATOM   753  N  N   . LEU   A 1 114 ? 27.63500  13.17500  11.23000  1.000 15.17816 ? 126 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 114 ? 28.75800  13.33900  10.31400  1.000 15.92278 ? 126 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 114 ? 28.93600  14.80000  9.93000   1.000 14.63553 ? 126 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 114 ? 30.05400  15.32000  9.94900   1.000 15.88660 ? 126 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 114 ? 28.53700  12.50500  9.04900   1.000 14.53952 ? 126 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 114 ? 28.42800  10.99000  9.18400   1.000 15.46732 ? 126 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 114 ? 28.20400  10.37800  7.81000   1.000 15.90508 ? 126 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 114 ? 29.71500  10.48000  9.78900   1.000 16.15145 ? 126 LEU   A CD2 1 
ATOM   761  N  N   . ARG   A 1 115 ? 27.83500  15.46500  9.56600   1.000 14.20073 ? 127 ARG   A N   1 
ATOM   762  C  CA  . ARG   A 1 115 ? 27.88500  16.86900  9.17000   1.000 13.97908 ? 127 ARG   A CA  1 
ATOM   763  C  C   . ARG   A 1 115 ? 28.42800  17.74700  10.29000  1.000 17.37063 ? 127 ARG   A C   1 
ATOM   764  O  O   . ARG   A 1 115 ? 29.24900  18.63600  10.04500  1.000 16.79808 ? 127 ARG   A O   1 
ATOM   765  C  CB  . ARG   A 1 115 ? 26.48000  17.33000  8.76700   1.000 15.30838 ? 127 ARG   A CB  1 
ATOM   766  C  CG  . ARG   A 1 115 ? 26.39300  18.73600  8.18700   1.000 16.16450 ? 127 ARG   A CG  1 
ATOM   767  C  CD  . ARG   A 1 115 ? 25.30000  18.77900  7.11100   1.000 21.62481 ? 127 ARG   A CD  1 
ATOM   768  N  NE  . ARG   A 1 115 ? 24.07500  18.15200  7.58800   1.000 25.83340 ? 127 ARG   A NE  1 
ATOM   769  C  CZ  . ARG   A 1 115 ? 23.21200  17.49800  6.82800   1.000 20.84351 ? 127 ARG   A CZ  1 
ATOM   770  N  NH1 . ARG   A 1 115 ? 23.43100  17.30700  5.53700   1.000 16.76000 ? 127 ARG   A NH1 1 
ATOM   771  N  NH2 . ARG   A 1 115 ? 22.11000  16.99900  7.38400   1.000 21.93435 ? 127 ARG   A NH2 1 
ATOM   772  N  N   . ALA   A 1 116 ? 27.98700  17.51400  11.52600  1.000 16.40072 ? 128 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 116 ? 28.47800  18.32300  12.63800  1.000 17.03240 ? 128 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 116 ? 29.96700  18.11600  12.87200  1.000 17.34042 ? 128 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 116 ? 30.65600  19.03700  13.33000  1.000 22.54717 ? 128 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 116 ? 27.68700  18.01100  13.90500  1.000 19.34537 ? 128 ALA   A CB  1 
ATOM   777  N  N   . ALA   A 1 117 ? 30.48200  16.92900  12.56800  1.000 17.62805 ? 129 ALA   A N   1 
ATOM   778  C  CA  . ALA   A 1 117 ? 31.89300  16.61600  12.73100  1.000 17.48727 ? 129 ALA   A CA  1 
ATOM   779  C  C   . ALA   A 1 117 ? 32.74900  17.11300  11.57200  1.000 17.68112 ? 129 ALA   A C   1 
ATOM   780  O  O   . ALA   A 1 117 ? 33.95800  16.86600  11.56900  1.000 19.50346 ? 129 ALA   A O   1 
ATOM   781  C  CB  . ALA   A 1 117 ? 32.09700  15.10800  12.94400  1.000 19.50537 ? 129 ALA   A CB  1 
ATOM   782  N  N   . GLY   A 1 118 ? 32.15300  17.79200  10.59400  1.000 16.77073 ? 130 GLY   A N   1 
ATOM   783  C  CA  . GLY   A 1 118 ? 32.87800  18.32300  9.46100   1.000 16.88730 ? 130 GLY   A CA  1 
ATOM   784  C  C   . GLY   A 1 118 ? 33.04700  17.39300  8.28100   1.000 17.39679 ? 130 GLY   A C   1 
ATOM   785  O  O   . GLY   A 1 118 ? 33.84800  17.69600  7.39200   1.000 18.76851 ? 130 GLY   A O   1 
ATOM   786  N  N   . VAL   A 1 119 ? 32.31600  16.27600  8.22800   1.000 15.35832 ? 131 VAL   A N   1 
ATOM   787  C  CA  . VAL   A 1 119 ? 32.38400  15.35700  7.10100   1.000 15.82311 ? 131 VAL   A CA  1 
ATOM   788  C  C   . VAL   A 1 119 ? 31.43800  15.85800  6.02900   1.000 14.84329 ? 131 VAL   A C   1 
ATOM   789  O  O   . VAL   A 1 119 ? 30.27600  16.16400  6.32200   1.000 14.67932 ? 131 VAL   A O   1 
ATOM   790  C  CB  . VAL   A 1 119 ? 31.94400  13.95500  7.54400   1.000 13.90584 ? 131 VAL   A CB  1 
ATOM   791  C  CG1 . VAL   A 1 119 ? 32.02500  12.97100  6.38400   1.000 15.99544 ? 131 VAL   A CG1 1 
ATOM   792  C  CG2 . VAL   A 1 119 ? 32.78900  13.47500  8.71300   1.000 17.39981 ? 131 VAL   A CG2 1 
ATOM   793  N  N   . ALA   A 1 120 ? 31.91600  15.92700  4.78600   1.000 13.84572 ? 132 ALA   A N   1 
ATOM   794  C  CA  . ALA   A 1 120 ? 31.04800  16.27600  3.66300   1.000 12.77977 ? 132 ALA   A CA  1 
ATOM   795  C  C   . ALA   A 1 120 ? 30.21500  15.04700  3.29200   1.000 13.07219 ? 132 ALA   A C   1 
ATOM   796  O  O   . ALA   A 1 120 ? 30.77400  13.98900  2.97300   1.000 15.03262 ? 132 ALA   A O   1 
ATOM   797  C  CB  . ALA   A 1 120 ? 31.91000  16.71900  2.47800   1.000 14.60446 ? 132 ALA   A CB  1 
ATOM   798  N  N   . THR   A 1 121 ? 28.89500  15.17100  3.32600   1.000 12.33587 ? 133 THR   A N   1 
ATOM   799  C  CA  . THR   A 1 121 ? 28.01200  14.02600  3.10700   1.000 12.15598 ? 133 THR   A CA  1 
ATOM   800  C  C   . THR   A 1 121 ? 27.40600  14.10400  1.71200   1.000 13.00839 ? 133 THR   A C   1 
ATOM   801  O  O   . THR   A 1 121 ? 27.09200  15.20000  1.22000   1.000 13.57407 ? 133 THR   A O   1 
ATOM   802  C  CB  . THR   A 1 121 ? 26.90100  13.95900  4.16100   1.000 13.09330 ? 133 THR   A CB  1 
ATOM   803  O  OG1 . THR   A 1 121 ? 26.17300  15.19800  4.18900   1.000 13.19703 ? 133 THR   A OG1 1 
ATOM   804  C  CG2 . THR   A 1 121 ? 27.48600  13.63900  5.54900   1.000 12.98239 ? 133 THR   A CG2 1 
ATOM   805  N  N   . TYR   A 1 122 ? 27.25700  12.92700  1.08000   1.000 12.91064 ? 134 TYR   A N   1 
ATOM   806  C  CA  . TYR   A 1 122 ? 26.85500  12.81000  -0.31700  1.000 13.80759 ? 134 TYR   A CA  1 
ATOM   807  C  C   . TYR   A 1 122 ? 25.81900  11.70800  -0.47500  1.000 12.67052 ? 134 TYR   A C   1 
ATOM   808  O  O   . TYR   A 1 122 ? 25.85500  10.69200  0.22600   1.000 12.60622 ? 134 TYR   A O   1 
ATOM   809  C  CB  . TYR   A 1 122 ? 28.04400  12.38800  -1.20100  1.000 14.54753 ? 134 TYR   A CB  1 
ATOM   810  C  CG  . TYR   A 1 122 ? 29.08800  13.45600  -1.37400  1.000 14.36081 ? 134 TYR   A CG  1 
ATOM   811  C  CD1 . TYR   A 1 122 ? 29.99300  13.74900  -0.35800  1.000 15.20818 ? 134 TYR   A CD1 1 
ATOM   812  C  CD2 . TYR   A 1 122 ? 29.18200  14.15200  -2.56600  1.000 13.75018 ? 134 TYR   A CD2 1 
ATOM   813  C  CE1 . TYR   A 1 122 ? 30.95200  14.75400  -0.51400  1.000 16.61003 ? 134 TYR   A CE1 1 
ATOM   814  C  CE2 . TYR   A 1 122 ? 30.14300  15.15300  -2.73500  1.000 15.47434 ? 134 TYR   A CE2 1 
ATOM   815  C  CZ  . TYR   A 1 122 ? 31.02500  15.42000  -1.71000  1.000 17.11680 ? 134 TYR   A CZ  1 
ATOM   816  O  OH  . TYR   A 1 122 ? 31.97800  16.40800  -1.87800  1.000 23.18994 ? 134 TYR   A OH  1 
ATOM   817  N  N   . ALA   A 1 123 ? 24.93100  11.88700  -1.44700  1.000 12.39427 ? 135 ALA   A N   1 
ATOM   818  C  CA  . ALA   A 1 123 ? 24.06600  10.81500  -1.92900  1.000 12.74402 ? 135 ALA   A CA  1 
ATOM   819  C  C   . ALA   A 1 123 ? 23.57500  11.23000  -3.30700  1.000 14.79170 ? 135 ALA   A C   1 
ATOM   820  O  O   . ALA   A 1 123 ? 23.73900  12.38000  -3.71700  1.000 13.66290 ? 135 ALA   A O   1 
ATOM   821  C  CB  . ALA   A 1 123 ? 22.87700  10.59200  -0.99000  1.000 12.76490 ? 135 ALA   A CB  1 
ATOM   822  N  N   . SER   A 1 124 ? 22.98300  10.28400  -4.03700  1.000 13.15934 ? 136 SER   A N   1 
ATOM   823  C  CA  . SER   A 1 124 ? 22.37900  10.65600  -5.31000  1.000 12.51357 ? 136 SER   A CA  1 
ATOM   824  C  C   . SER   A 1 124 ? 21.20700  11.60400  -5.06300  1.000 15.15218 ? 136 SER   A C   1 
ATOM   825  O  O   . SER   A 1 124 ? 20.65800  11.65600  -3.95300  1.000 13.69342 ? 136 SER   A O   1 
ATOM   826  C  CB  . SER   A 1 124 ? 21.87800  9.41400   -6.04100  1.000 14.74262 ? 136 SER   A CB  1 
ATOM   827  O  OG  . SER   A 1 124 ? 20.66800  8.96800   -5.46100  1.000 14.30864 ? 136 SER   A OG  1 
ATOM   828  N  N   . PRO   A 1 125 ? 20.80200  12.36800  -6.08200  1.000 14.54886 ? 137 PRO   A N   1 
ATOM   829  C  CA  . PRO   A 1 125 ? 19.62100  13.23100  -5.90500  1.000 14.98350 ? 137 PRO   A CA  1 
ATOM   830  C  C   . PRO   A 1 125 ? 18.35200  12.43800  -5.64600  1.000 14.35482 ? 137 PRO   A C   1 
ATOM   831  O  O   . PRO   A 1 125 ? 17.45700  12.90900  -4.93400  1.000 14.26134 ? 137 PRO   A O   1 
ATOM   832  C  CB  . PRO   A 1 125 ? 19.57600  14.07000  -7.19400  1.000 17.07299 ? 137 PRO   A CB  1 
ATOM   833  C  CG  . PRO   A 1 125 ? 20.43200  13.33100  -8.17700  1.000 20.29133 ? 137 PRO   A CG  1 
ATOM   834  C  CD  . PRO   A 1 125 ? 21.47100  12.58300  -7.38000  1.000 15.08680 ? 137 PRO   A CD  1 
ATOM   835  N  N   A SER   A 1 126 ? 18.26200  11.22400  -6.19300  0.668 13.54327 ? 138 SER   A N   1 
ATOM   836  N  N   B SER   A 1 126 ? 18.25500  11.21500  -6.16900  0.332 13.63559 ? 138 SER   A N   1 
ATOM   837  C  CA  A SER   A 1 126 ? 17.11000  10.38200  -5.91000  0.668 16.07796 ? 138 SER   A CA  1 
ATOM   838  C  CA  B SER   A 1 126 ? 17.07500  10.40200  -5.88900  0.332 16.03541 ? 138 SER   A CA  1 
ATOM   839  C  C   A SER   A 1 126 ? 17.07700  10.00000  -4.43700  0.668 12.90754 ? 138 SER   A C   1 
ATOM   840  C  C   B SER   A 1 126 ? 17.06000  9.93300   -4.43900  0.332 12.99522 ? 138 SER   A C   1 
ATOM   841  O  O   A SER   A 1 126 ? 16.03000  10.09900  -3.78900  0.668 14.91875 ? 138 SER   A O   1 
ATOM   842  O  O   B SER   A 1 126 ? 15.99400  9.85800   -3.81700  0.332 15.32369 ? 138 SER   A O   1 
ATOM   843  C  CB  A SER   A 1 126 ? 17.13000  9.14100   -6.80300  0.668 16.82049 ? 138 SER   A CB  1 
ATOM   844  C  CB  B SER   A 1 126 ? 17.00300  9.21600   -6.84800  0.332 16.96047 ? 138 SER   A CB  1 
ATOM   845  O  OG  A SER   A 1 126 ? 16.09400  8.24200   -6.45400  0.668 19.50200 ? 138 SER   A OG  1 
ATOM   846  O  OG  B SER   A 1 126 ? 18.13400  8.38400   -6.69400  0.332 15.44004 ? 138 SER   A OG  1 
ATOM   847  N  N   . THR   A 1 127 ? 18.23000  9.61900   -3.87900  1.000 13.30811 ? 139 THR   A N   1 
ATOM   848  C  CA  . THR   A 1 127 ? 18.29600  9.29800   -2.45400  1.000 12.49714 ? 139 THR   A CA  1 
ATOM   849  C  C   . THR   A 1 127 ? 17.93500  10.50400  -1.59300  1.000 12.66217 ? 139 THR   A C   1 
ATOM   850  O  O   . THR   A 1 127 ? 17.18700  10.37200  -0.62100  1.000 13.93492 ? 139 THR   A O   1 
ATOM   851  C  CB  . THR   A 1 127 ? 19.69100  8.79300   -2.09900  1.000 12.71433 ? 139 THR   A CB  1 
ATOM   852  O  OG1 . THR   A 1 127 ? 19.93300  7.53500   -2.74300  1.000 12.74421 ? 139 THR   A OG1 1 
ATOM   853  C  CG2 . THR   A 1 127 ? 19.85000  8.62500   -0.58700  1.000 12.96123 ? 139 THR   A CG2 1 
ATOM   854  N  N   . ARG   A 1 128 ? 18.48300  11.68300  -1.91200  1.000 12.80005 ? 140 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 128 ? 18.17500  12.86500  -1.10900  1.000 11.78225 ? 140 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 128 ? 16.68000  13.15600  -1.09800  1.000 12.85013 ? 140 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 128 ? 16.11200  13.48400  -0.04900  1.000 14.77584 ? 140 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 128 ? 18.95100  14.07800  -1.63700  1.000 12.34361 ? 140 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 128 ? 20.46600  13.98400  -1.43500  1.000 14.58134 ? 140 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 128 ? 21.21500  15.20100  -1.96500  1.000 15.20277 ? 140 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 128 ? 20.96400  16.38500  -1.14800  1.000 17.90276 ? 140 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 128 ? 20.11600  17.36700  -1.44400  1.000 19.64151 ? 140 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 128 ? 19.38900  17.34600  -2.55100  1.000 18.81068 ? 140 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 128 ? 20.00100  18.40000  -0.61000  1.000 23.96312 ? 140 ARG   A NH2 1 
ATOM   865  N  N   . ARG   A 1 129 ? 16.03400  13.08500  -2.26200  1.000 13.64574 ? 141 ARG   A N   1 
ATOM   866  C  CA  . ARG   A 1 129 ? 14.59800  13.33000  -2.32900  1.000 13.70437 ? 141 ARG   A CA  1 
ATOM   867  C  C   . ARG   A 1 129 ? 13.81500  12.31800  -1.50100  1.000 14.46735 ? 141 ARG   A C   1 
ATOM   868  O  O   . ARG   A 1 129 ? 12.92200  12.68600  -0.72600  1.000 15.79092 ? 141 ARG   A O   1 
ATOM   869  C  CB  . ARG   A 1 129 ? 14.12800  13.29700  -3.78600  1.000 15.26992 ? 141 ARG   A CB  1 
ATOM   870  C  CG  . ARG   A 1 129 ? 12.63300  13.54600  -3.94600  1.000 17.93749 ? 141 ARG   A CG  1 
ATOM   871  C  CD  . ARG   A 1 129 ? 12.19100  13.50000  -5.39600  1.000 19.93897 ? 141 ARG   A CD  1 
ATOM   872  N  NE  . ARG   A 1 129 ? 12.85400  14.51800  -6.19800  1.000 23.65014 ? 141 ARG   A NE  1 
ATOM   873  C  CZ  . ARG   A 1 129 ? 13.78400  14.25000  -7.10100  1.000 30.67066 ? 141 ARG   A CZ  1 
ATOM   874  N  NH1 . ARG   A 1 129 ? 14.20500  13.01300  -7.30900  1.000 28.18306 ? 141 ARG   A NH1 1 
ATOM   875  N  NH2 . ARG   A 1 129 ? 14.30900  15.24800  -7.80900  1.000 29.44275 ? 141 ARG   A NH2 1 
ATOM   876  N  N   . LEU   A 1 130 ? 14.11400  11.03100  -1.67100  1.000 14.03988 ? 142 LEU   A N   1 
ATOM   877  C  CA  . LEU   A 1 130 ? 13.40500  10.00600  -0.90900  1.000 13.47143 ? 142 LEU   A CA  1 
ATOM   878  C  C   . LEU   A 1 130 ? 13.62900  10.16800  0.59200   1.000 13.61226 ? 142 LEU   A C   1 
ATOM   879  O  O   . LEU   A 1 130 ? 12.70400  9.95000   1.39300   1.000 15.11545 ? 142 LEU   A O   1 
ATOM   880  C  CB  . LEU   A 1 130 ? 13.82800  8.61200   -1.39400  1.000 13.02718 ? 142 LEU   A CB  1 
ATOM   881  C  CG  . LEU   A 1 130 ? 13.23300  8.25200   -2.76200  1.000 13.74278 ? 142 LEU   A CG  1 
ATOM   882  C  CD1 . LEU   A 1 130 ? 14.01500  7.12300   -3.43200  1.000 15.54152 ? 142 LEU   A CD1 1 
ATOM   883  C  CD2 . LEU   A 1 130 ? 11.75800  7.87300   -2.59900  1.000 19.90004 ? 142 LEU   A CD2 1 
ATOM   884  N  N   . ALA   A 1 131 ? 14.85500  10.50600  1.00200   1.000 13.47067 ? 143 ALA   A N   1 
ATOM   885  C  CA  . ALA   A 1 131 ? 15.10700  10.74700  2.41900   1.000 13.38075 ? 143 ALA   A CA  1 
ATOM   886  C  C   . ALA   A 1 131 ? 14.25600  11.89700  2.93000   1.000 14.89645 ? 143 ALA   A C   1 
ATOM   887  O  O   . ALA   A 1 131 ? 13.66100  11.79900  4.00700   1.000 16.47808 ? 143 ALA   A O   1 
ATOM   888  C  CB  . ALA   A 1 131 ? 16.59100  11.04200  2.66000   1.000 13.00147 ? 143 ALA   A CB  1 
ATOM   889  N  N   . GLU   A 1 132 ? 14.16200  12.97600  2.15500   1.000 15.90787 ? 144 GLU   A N   1 
ATOM   890  C  CA  . GLU   A 1 132 ? 13.33700  14.10300  2.58300   1.000 16.50696 ? 144 GLU   A CA  1 
ATOM   891  C  C   . GLU   A 1 132 ? 11.87800  13.69100  2.73100   1.000 17.24540 ? 144 GLU   A C   1 
ATOM   892  O  O   . GLU   A 1 132 ? 11.23500  14.00400  3.74200   1.000 18.01011 ? 144 GLU   A O   1 
ATOM   893  C  CB  . GLU   A 1 132 ? 13.47500  15.23800  1.58300   1.000 17.19127 ? 144 GLU   A CB  1 
ATOM   894  C  CG  . GLU   A 1 132 ? 12.74400  16.51500  1.98000   1.000 18.28182 ? 144 GLU   A CG  1 
ATOM   895  C  CD  . GLU   A 1 132 ? 13.10400  17.65600  1.06000   1.000 31.99328 ? 144 GLU   A CD  1 
ATOM   896  O  OE1 . GLU   A 1 132 ? 12.77100  17.56900  -0.14000  1.000 40.05634 ? 144 GLU   A OE1 1 
ATOM   897  O  OE2 . GLU   A 1 132 ? 13.74000  18.62400  1.52600   1.000 40.00505 ? 144 GLU   A OE2 1 
ATOM   898  N  N   . VAL   A 1 133 ? 11.34400  12.95800  1.74900   1.000 17.61418 ? 145 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 133 ? 9.94800   12.53000  1.81600   1.000 19.37507 ? 145 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 133 ? 9.70500   11.68600  3.06200   1.000 19.66838 ? 145 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 133 ? 8.65700   11.79500  3.72200   1.000 22.18548 ? 145 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 133 ? 9.54700   11.78400  0.52900   1.000 19.76437 ? 145 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 133 ? 8.19300   11.08600  0.71000   1.000 21.06703 ? 145 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 133 ? 9.51100   12.73700  -0.64700  1.000 23.56267 ? 145 VAL   A CG2 1 
ATOM   905  N  N   . GLU   A 1 134 ? 10.67500  10.84700  3.41700   1.000 15.70739 ? 146 GLU   A N   1 
ATOM   906  C  CA  . GLU   A 1 134 ? 10.57900  9.96200   4.57100   1.000 18.02384 ? 146 GLU   A CA  1 
ATOM   907  C  C   . GLU   A 1 134 ? 10.78100  10.69300  5.88900   1.000 17.81333 ? 146 GLU   A C   1 
ATOM   908  O  O   . GLU   A 1 134 ? 10.52800  10.09700  6.94000   1.000 18.24657 ? 146 GLU   A O   1 
ATOM   909  C  CB  . GLU   A 1 134 ? 11.62400  8.83400   4.43600   1.000 16.82112 ? 146 GLU   A CB  1 
ATOM   910  C  CG  . GLU   A 1 134 ? 11.34600  7.57500   5.24700   1.000 18.25879 ? 146 GLU   A CG  1 
ATOM   911  C  CD  . GLU   A 1 134 ? 10.17100  6.77600   4.71300   1.000 31.25924 ? 146 GLU   A CD  1 
ATOM   912  O  OE1 . GLU   A 1 134 ? 9.79300   6.95700   3.52900   1.000 25.25986 ? 146 GLU   A OE1 1 
ATOM   913  O  OE2 . GLU   A 1 134 ? 9.62000   5.96600   5.49000   1.000 37.17828 ? 146 GLU   A OE2 1 
ATOM   914  N  N   . GLY   A 1 135 ? 11.23200  11.94400  5.86000   1.000 16.71440 ? 147 GLY   A N   1 
ATOM   915  C  CA  . GLY   A 1 135 ? 11.57100  12.65300  7.08200   1.000 19.35581 ? 147 GLY   A CA  1 
ATOM   916  C  C   . GLY   A 1 135 ? 12.89300  12.24600  7.67600   1.000 19.17369 ? 147 GLY   A C   1 
ATOM   917  O  O   . GLY   A 1 135 ? 13.13800  12.49100  8.86400   1.000 17.66481 ? 147 GLY   A O   1 
ATOM   918  N  N   . ASN   A 1 136 ? 13.75000  11.59600  6.88700   1.000 14.28629 ? 148 ASN   A N   1 
ATOM   919  C  CA  . ASN   A 1 136 ? 15.04500  11.13900  7.35000   1.000 15.36942 ? 148 ASN   A CA  1 
ATOM   920  C  C   . ASN   A 1 136 ? 16.08600  12.24200  7.16500   1.000 14.04479 ? 148 ASN   A C   1 
ATOM   921  O  O   . ASN   A 1 136 ? 15.82200  13.30700  6.59300   1.000 15.24925 ? 148 ASN   A O   1 
ATOM   922  C  CB  . ASN   A 1 136 ? 15.48000  9.91300   6.54300   1.000 14.58734 ? 148 ASN   A CB  1 
ATOM   923  C  CG  . ASN   A 1 136 ? 14.67200  8.68600   6.87300   1.000 16.44645 ? 148 ASN   A CG  1 
ATOM   924  O  OD1 . ASN   A 1 136 ? 13.86900  8.68000   7.80700   1.000 18.00072 ? 148 ASN   A OD1 1 
ATOM   925  N  ND2 . ASN   A 1 136 ? 14.88200  7.61000   6.10800   1.000 15.69928 ? 148 ASN   A ND2 1 
ATOM   926  N  N   . GLU   A 1 137 ? 17.29000  11.98800  7.67300   1.000 15.22009 ? 149 GLU   A N   1 
ATOM   927  C  CA  . GLU   A 1 137 ? 18.36600  12.95100  7.50600   1.000 15.58780 ? 149 GLU   A CA  1 
ATOM   928  C  C   . GLU   A 1 137 ? 18.80300  12.95600  6.04500   1.000 13.99175 ? 149 GLU   A C   1 
ATOM   929  O  O   . GLU   A 1 137 ? 18.72500  11.93600  5.35500   1.000 15.43712 ? 149 GLU   A O   1 
ATOM   930  C  CB  . GLU   A 1 137 ? 19.52700  12.58200  8.41500   1.000 16.39769 ? 149 GLU   A CB  1 
ATOM   931  C  CG  . GLU   A 1 137 ? 19.14800  12.75400  9.88400   1.000 16.93150 ? 149 GLU   A CG  1 
ATOM   932  C  CD  . GLU   A 1 137 ? 19.96100  11.87300  10.77400  1.000 23.51771 ? 149 GLU   A CD  1 
ATOM   933  O  OE1 . GLU   A 1 137 ? 21.16100  12.15500  10.92300  1.000 19.79780 ? 149 GLU   A OE1 1 
ATOM   934  O  OE2 . GLU   A 1 137 ? 19.40900  10.87700  11.30200  1.000 27.50721 ? 149 GLU   A OE2 1 
ATOM   935  N  N   . ILE   A 1 138 ? 19.24700  14.11500  5.57200   1.000 13.85475 ? 150 ILE   A N   1 
ATOM   936  C  CA  . ILE   A 1 138 ? 19.46900  14.33600  4.14300   1.000 13.56573 ? 150 ILE   A CA  1 
ATOM   937  C  C   . ILE   A 1 138 ? 20.92900  14.69900  3.90700   1.000 13.86584 ? 150 ILE   A C   1 
ATOM   938  O  O   . ILE   A 1 138 ? 21.37600  15.76100  4.37100   1.000 14.60686 ? 150 ILE   A O   1 
ATOM   939  C  CB  . ILE   A 1 138 ? 18.56100  15.45800  3.61000   1.000 12.76487 ? 150 ILE   A CB  1 
ATOM   940  C  CG1 . ILE   A 1 138 ? 17.07700  15.15800  3.86900   1.000 17.02743 ? 150 ILE   A CG1 1 
ATOM   941  C  CG2 . ILE   A 1 138 ? 18.82900  15.70100  2.12100   1.000 16.81463 ? 150 ILE   A CG2 1 
ATOM   942  C  CD1 . ILE   A 1 138 ? 16.21200  16.43400  3.81500   1.000 19.25276 ? 150 ILE   A CD1 1 
ATOM   943  N  N   . PRO   A 1 139 ? 21.70200  13.86500  3.20600   1.000 11.75840 ? 151 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 139 ? 23.08100  14.24100  2.86300   1.000 13.10615 ? 151 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 139 ? 23.13800  15.56600  2.10900   1.000 15.01885 ? 151 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 139 ? 22.24100  15.89800  1.33300   1.000 14.97565 ? 151 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 139 ? 23.54800  13.08200  1.97100   1.000 12.41586 ? 151 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 139 ? 22.74900  11.88700  2.47300   1.000 12.85984 ? 151 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 139 ? 21.37800  12.48200  2.77600   1.000 11.96778 ? 151 PRO   A CD  1 
ATOM   950  N  N   . THR   A 1 140 ? 24.23700  16.29500  2.31400   1.000 14.30690 ? 152 THR   A N   1 
ATOM   951  C  CA  . THR   A 1 140 ? 24.34900  17.65000  1.77400   1.000 13.50303 ? 152 THR   A CA  1 
ATOM   952  C  C   . THR   A 1 140 ? 24.45800  17.65100  0.25200   1.000 14.12905 ? 152 THR   A C   1 
ATOM   953  O  O   . THR   A 1 140 ? 23.72900  18.38400  -0.43300  1.000 14.63553 ? 152 THR   A O   1 
ATOM   954  C  CB  . THR   A 1 140 ? 25.56500  18.33400  2.39800   1.000 14.21044 ? 152 THR   A CB  1 
ATOM   955  O  OG1 . THR   A 1 140 ? 25.29500  18.56000  3.78400   1.000 16.98216 ? 152 THR   A OG1 1 
ATOM   956  C  CG2 . THR   A 1 140 ? 25.83600  19.69800  1.72800   1.000 14.38669 ? 152 THR   A CG2 1 
ATOM   957  N  N   . HIS   A 1 141 ? 25.37900  16.86100  -0.29300  1.000 13.16436 ? 153 HIS   A N   1 
ATOM   958  C  CA  . HIS   A 1 141 ? 25.74100  16.96900  -1.69500  1.000 13.10181 ? 153 HIS   A CA  1 
ATOM   959  C  C   . HIS   A 1 141 ? 25.03800  15.92200  -2.53600  1.000 15.36248 ? 153 HIS   A C   1 
ATOM   960  O  O   . HIS   A 1 141 ? 24.73800  14.82600  -2.06300  1.000 14.42652 ? 153 HIS   A O   1 
ATOM   961  C  CB  . HIS   A 1 141 ? 27.23100  16.76100  -1.88800  1.000 14.74060 ? 153 HIS   A CB  1 
ATOM   962  C  CG  . HIS   A 1 141 ? 28.04900  17.90100  -1.42600  1.000 15.79509 ? 153 HIS   A CG  1 
ATOM   963  N  ND1 . HIS   A 1 141 ? 28.20300  19.04400  -2.17600  1.000 16.21483 ? 153 HIS   A ND1 1 
ATOM   964  C  CD2 . HIS   A 1 141 ? 28.75500  18.08100  -0.29500  1.000 12.94691 ? 153 HIS   A CD2 1 
ATOM   965  C  CE1 . HIS   A 1 141 ? 28.98100  19.88300  -1.52500  1.000 15.69997 ? 153 HIS   A CE1 1 
ATOM   966  N  NE2 . HIS   A 1 141 ? 29.31000  19.32900  -0.37700  1.000 15.88123 ? 153 HIS   A NE2 1 
ATOM   967  N  N   . SER   A 1 142 ? 24.85300  16.25100  -3.80800  1.000 14.56784 ? 154 SER   A N   1 
ATOM   968  C  CA  . SER   A 1 142 ? 24.19700  15.39400  -4.78500  1.000 17.77043 ? 154 SER   A CA  1 
ATOM   969  C  C   . SER   A 1 142 ? 25.24100  14.79800  -5.71600  1.000 17.19737 ? 154 SER   A C   1 
ATOM   970  O  O   . SER   A 1 142 ? 26.03600  15.53100  -6.32100  1.000 18.89116 ? 154 SER   A O   1 
ATOM   971  C  CB  . SER   A 1 142 ? 23.22000  16.21600  -5.62800  1.000 16.60675 ? 154 SER   A CB  1 
ATOM   972  O  OG  . SER   A 1 142 ? 22.14300  16.65200  -4.84000  1.000 18.71487 ? 154 SER   A OG  1 
ATOM   973  N  N   . LEU   A 1 143 ? 25.21000  13.47400  -5.86700  1.000 13.56653 ? 155 LEU   A N   1 
ATOM   974  C  CA  . LEU   A 1 143 ? 26.09400  12.76900  -6.78600  1.000 16.81621 ? 155 LEU   A CA  1 
ATOM   975  C  C   . LEU   A 1 143 ? 25.45000  12.70400  -8.16600  1.000 18.22493 ? 155 LEU   A C   1 
ATOM   976  O  O   . LEU   A 1 143 ? 24.40500  12.06100  -8.33900  1.000 19.45332 ? 155 LEU   A O   1 
ATOM   977  C  CB  . LEU   A 1 143 ? 26.31400  11.34900  -6.26800  1.000 15.97838 ? 155 LEU   A CB  1 
ATOM   978  C  CG  . LEU   A 1 143 ? 27.05400  11.20700  -4.93500  1.000 15.37809 ? 155 LEU   A CG  1 
ATOM   979  C  CD1 . LEU   A 1 143 ? 26.87800  9.77800   -4.40900  1.000 15.84662 ? 155 LEU   A CD1 1 
ATOM   980  C  CD2 . LEU   A 1 143 ? 28.52000  11.54100  -5.07000  1.000 21.21009 ? 155 LEU   A CD2 1 
ATOM   981  N  N   A GLU   A 1 144 ? 26.07900  13.35100  -9.14500  0.391 22.44443 ? 156 GLU   A N   1 
ATOM   982  N  N   B GLU   A 1 144 ? 26.07900  13.35000  -9.14300  0.609 22.39407 ? 156 GLU   A N   1 
ATOM   983  C  CA  A GLU   A 1 144 ? 25.60200  13.30400  -10.51900 0.391 20.49091 ? 156 GLU   A CA  1 
ATOM   984  C  CA  B GLU   A 1 144 ? 25.59600  13.30300  -10.51700 0.609 20.29151 ? 156 GLU   A CA  1 
ATOM   985  C  C   A GLU   A 1 144 ? 26.08800  12.03400  -11.22000 0.391 20.22837 ? 156 GLU   A C   1 
ATOM   986  C  C   B GLU   A 1 144 ? 26.09500  12.04300  -11.22600 0.609 20.16518 ? 156 GLU   A C   1 
ATOM   987  O  O   A GLU   A 1 144 ? 27.02300  11.36400  -10.77400 0.391 20.58921 ? 156 GLU   A O   1 
ATOM   988  O  O   B GLU   A 1 144 ? 27.04500  11.38800  -10.79200 0.609 20.53177 ? 156 GLU   A O   1 
ATOM   989  C  CB  A GLU   A 1 144 ? 26.08200  14.53400  -11.29300 0.391 28.59933 ? 156 GLU   A CB  1 
ATOM   990  C  CB  B GLU   A 1 144 ? 26.05400  14.54700  -11.28400 0.609 28.57511 ? 156 GLU   A CB  1 
ATOM   991  C  CG  A GLU   A 1 144 ? 27.56700  14.52300  -11.62500 0.391 31.48661 ? 156 GLU   A CG  1 
ATOM   992  C  CG  B GLU   A 1 144 ? 25.41700  15.83800  -10.78600 0.609 25.73740 ? 156 GLU   A CG  1 
ATOM   993  C  CD  A GLU   A 1 144 ? 28.01700  15.77800  -12.35700 0.391 43.21838 ? 156 GLU   A CD  1 
ATOM   994  C  CD  B GLU   A 1 144 ? 25.93600  17.06900  -11.50600 0.609 46.95851 ? 156 GLU   A CD  1 
ATOM   995  O  OE1 A GLU   A 1 144 ? 27.27900  16.78500  -12.32400 0.391 47.47182 ? 156 GLU   A OE1 1 
ATOM   996  O  OE1 B GLU   A 1 144 ? 26.92600  16.95200  -12.26000 0.609 48.70616 ? 156 GLU   A OE1 1 
ATOM   997  O  OE2 A GLU   A 1 144 ? 29.10900  15.75800  -12.96500 0.391 44.65882 ? 156 GLU   A OE2 1 
ATOM   998  O  OE2 B GLU   A 1 144 ? 25.35100  18.15600  -11.31600 0.609 51.08691 ? 156 GLU   A OE2 1 
ATOM   999  N  N   . GLY   A 1 145 ? 25.43300  11.71000  -12.33400 1.000 20.06823 ? 157 GLY   A N   1 
ATOM   1000 C  CA  . GLY   A 1 145 ? 25.88600  10.62200  -13.18100 1.000 18.37781 ? 157 GLY   A CA  1 
ATOM   1001 C  C   . GLY   A 1 145 ? 25.43100  9.24100   -12.78100 1.000 16.72308 ? 157 GLY   A C   1 
ATOM   1002 O  O   . GLY   A 1 145 ? 25.98600  8.25200   -13.27800 1.000 18.03403 ? 157 GLY   A O   1 
ATOM   1003 N  N   . LEU   A 1 146 ? 24.41300  9.13400   -11.91800 1.000 17.71717 ? 158 LEU   A N   1 
ATOM   1004 C  CA  . LEU   A 1 146 ? 23.97600  7.83700   -11.40200 1.000 14.98314 ? 158 LEU   A CA  1 
ATOM   1005 C  C   . LEU   A 1 146 ? 22.47900  7.60600   -11.57800 1.000 15.66011 ? 158 LEU   A C   1 
ATOM   1006 O  O   . LEU   A 1 146 ? 21.90800  6.76600   -10.88400 1.000 18.71597 ? 158 LEU   A O   1 
ATOM   1007 C  CB  . LEU   A 1 146 ? 24.36100  7.69300   -9.92500  1.000 14.23355 ? 158 LEU   A CB  1 
ATOM   1008 C  CG  . LEU   A 1 146 ? 25.85500  7.55700   -9.64300  1.000 13.75741 ? 158 LEU   A CG  1 
ATOM   1009 C  CD1 . LEU   A 1 146 ? 26.20300  7.79300   -8.16300  1.000 15.00782 ? 158 LEU   A CD1 1 
ATOM   1010 C  CD2 . LEU   A 1 146 ? 26.33800  6.19200   -10.12300 1.000 16.89372 ? 158 LEU   A CD2 1 
ATOM   1011 N  N   . SER   A 1 147 ? 21.82900  8.31000   -12.50800 1.000 16.63509 ? 159 SER   A N   1 
ATOM   1012 C  CA  . SER   A 1 147 ? 20.37300  8.29300   -12.57000 1.000 19.30929 ? 159 SER   A CA  1 
ATOM   1013 C  C   . SER   A 1 147 ? 19.79400  7.15600   -13.39800 1.000 19.98183 ? 159 SER   A C   1 
ATOM   1014 O  O   . SER   A 1 147 ? 18.60500  6.85900   -13.24400 1.000 21.47412 ? 159 SER   A O   1 
ATOM   1015 C  CB  . SER   A 1 147 ? 19.84400  9.62400   -13.11800 1.000 23.91823 ? 159 SER   A CB  1 
ATOM   1016 O  OG  . SER   A 1 147 ? 20.29700  9.83700   -14.44000 1.000 25.36526 ? 159 SER   A OG  1 
ATOM   1017 N  N   . SER   A 1 148 ? 20.58200  6.52000   -14.26700 1.000 18.39587 ? 160 SER   A N   1 
ATOM   1018 C  CA  . SER   A 1 148 ? 20.09100  5.43400   -15.11300 1.000 18.84347 ? 160 SER   A CA  1 
ATOM   1019 C  C   . SER   A 1 148 ? 20.80000  4.13300   -14.77000 1.000 14.64659 ? 160 SER   A C   1 
ATOM   1020 O  O   . SER   A 1 148 ? 22.00500  4.12600   -14.50000 1.000 15.06722 ? 160 SER   A O   1 
ATOM   1021 C  CB  . SER   A 1 148 ? 20.31800  5.74900   -16.58800 1.000 21.92509 ? 160 SER   A CB  1 
ATOM   1022 O  OG  . SER   A 1 148 ? 19.63400  6.94400   -16.94600 1.000 25.71194 ? 160 SER   A OG  1 
ATOM   1023 N  N   . SER   A 1 149 ? 20.04300  3.03700   -14.77500 1.000 16.43410 ? 161 SER   A N   1 
ATOM   1024 C  CA  A SER   A 1 149 ? 20.62500  1.74000   -14.46300 0.465 18.32441 ? 161 SER   A CA  1 
ATOM   1025 C  CA  B SER   A 1 149 ? 20.61000  1.72700   -14.48200 0.535 18.33776 ? 161 SER   A CA  1 
ATOM   1026 C  C   . SER   A 1 149 ? 21.84200  1.48100   -15.34100 1.000 15.73889 ? 161 SER   A C   1 
ATOM   1027 O  O   . SER   A 1 149 ? 21.83200  1.74200   -16.55400 1.000 19.38380 ? 161 SER   A O   1 
ATOM   1028 C  CB  A SER   A 1 149 ? 19.59600  0.62100   -14.64200 0.465 20.02283 ? 161 SER   A CB  1 
ATOM   1029 C  CB  B SER   A 1 149 ? 19.56600  0.65100   -14.76500 0.535 19.99832 ? 161 SER   A CB  1 
ATOM   1030 O  OG  A SER   A 1 149 ? 19.05200  0.60500   -15.94700 0.465 22.00869 ? 161 SER   A OG  1 
ATOM   1031 O  OG  B SER   A 1 149 ? 18.36400  0.92400   -14.07200 0.535 18.23696 ? 161 SER   A OG  1 
ATOM   1032 N  N   . GLY   A 1 150 ? 22.90300  0.97800   -14.71400 1.000 16.50641 ? 162 GLY   A N   1 
ATOM   1033 C  CA  . GLY   A 1 150 ? 24.15800  0.74000   -15.38500 1.000 17.30191 ? 162 GLY   A CA  1 
ATOM   1034 C  C   . GLY   A 1 150 ? 25.14100  1.88700   -15.30800 1.000 17.67649 ? 162 GLY   A C   1 
ATOM   1035 O  O   . GLY   A 1 150 ? 26.29300  1.73100   -15.72700 1.000 18.56498 ? 162 GLY   A O   1 
ATOM   1036 N  N   . ASP   A 1 151 ? 24.72700  3.04100   -14.78900 1.000 16.00390 ? 163 ASP   A N   1 
ATOM   1037 C  CA  . ASP   A 1 151 ? 25.64000  4.17300   -14.67100 1.000 15.50852 ? 163 ASP   A CA  1 
ATOM   1038 C  C   . ASP   A 1 151 ? 26.67500  3.93400   -13.57600 1.000 15.72376 ? 163 ASP   A C   1 
ATOM   1039 O  O   . ASP   A 1 151 ? 26.36100  3.40600   -12.50700 1.000 15.59438 ? 163 ASP   A O   1 
ATOM   1040 C  CB  . ASP   A 1 151 ? 24.87500  5.44800   -14.29700 1.000 16.19685 ? 163 ASP   A CB  1 
ATOM   1041 C  CG  . ASP   A 1 151 ? 24.14000  6.08800   -15.46800 1.000 18.64327 ? 163 ASP   A CG  1 
ATOM   1042 O  OD1 . ASP   A 1 151 ? 24.39200  5.70500   -16.63100 1.000 21.23811 ? 163 ASP   A OD1 1 
ATOM   1043 O  OD2 . ASP   A 1 151 ? 23.32400  7.01000   -15.20600 1.000 20.34174 ? 163 ASP   A OD2 1 
ATOM   1044 N  N   . ALA   A 1 152 ? 27.90900  4.36900   -13.82800 1.000 16.57090 ? 164 ALA   A N   1 
ATOM   1045 C  CA  . ALA   A 1 152 ? 28.99300  4.28400   -12.85900 1.000 19.17236 ? 164 ALA   A CA  1 
ATOM   1046 C  C   . ALA   A 1 152 ? 29.76000  5.60000   -12.85700 1.000 17.81320 ? 164 ALA   A C   1 
ATOM   1047 O  O   . ALA   A 1 152 ? 29.87100  6.26600   -13.89000 1.000 19.83984 ? 164 ALA   A O   1 
ATOM   1048 C  CB  . ALA   A 1 152 ? 29.95500  3.15100   -13.22400 1.000 17.58985 ? 164 ALA   A CB  1 
ATOM   1049 N  N   . VAL   A 1 153 ? 30.30300  5.97300   -11.69800 1.000 17.55630 ? 165 VAL   A N   1 
ATOM   1050 C  CA  . VAL   A 1 153 ? 31.18900  7.12700   -11.58300 1.000 18.48014 ? 165 VAL   A CA  1 
ATOM   1051 C  C   . VAL   A 1 153 ? 32.27500  6.81900   -10.56500 1.000 18.48728 ? 165 VAL   A C   1 
ATOM   1052 O  O   . VAL   A 1 153 ? 32.05500  6.07300   -9.60700  1.000 18.59167 ? 165 VAL   A O   1 
ATOM   1053 C  CB  . VAL   A 1 153 ? 30.44800  8.42400   -11.17000 1.000 18.61481 ? 165 VAL   A CB  1 
ATOM   1054 C  CG1 . VAL   A 1 153 ? 29.34500  8.77700   -12.14800 1.000 23.99111 ? 165 VAL   A CG1 1 
ATOM   1055 C  CG2 . VAL   A 1 153 ? 29.87400  8.30900   -9.77200  1.000 18.51184 ? 165 VAL   A CG2 1 
ATOM   1056 N  N   . ARG   A 1 154 ? 33.46500  7.37500   -10.77100 1.000 18.12318 ? 166 ARG   A N   1 
ATOM   1057 C  CA  . ARG   A 1 154 ? 34.50800  7.26400   -9.76100  1.000 18.71267 ? 166 ARG   A CA  1 
ATOM   1058 C  C   . ARG   A 1 154 ? 34.29900  8.33800   -8.70000  1.000 17.51953 ? 166 ARG   A C   1 
ATOM   1059 O  O   . ARG   A 1 154 ? 33.91100  9.47000   -9.00600  1.000 18.46045 ? 166 ARG   A O   1 
ATOM   1060 C  CB  . ARG   A 1 154 ? 35.90500  7.41100   -10.37900 1.000 21.32652 ? 166 ARG   A CB  1 
ATOM   1061 C  CG  . ARG   A 1 154 ? 36.60200  6.09500   -10.77400 1.000 29.75822 ? 166 ARG   A CG  1 
ATOM   1062 C  CD  . ARG   A 1 154 ? 36.74300  5.07200   -9.63700  1.000 29.76187 ? 166 ARG   A CD  1 
ATOM   1063 N  NE  . ARG   A 1 154 ? 37.87100  5.32600   -8.74100  1.000 29.99026 ? 166 ARG   A NE  1 
ATOM   1064 C  CZ  . ARG   A 1 154 ? 39.03200  4.68700   -8.80900  1.000 23.27129 ? 166 ARG   A CZ  1 
ATOM   1065 N  NH1 . ARG   A 1 154 ? 39.30000  3.85600   -9.79900  1.000 25.56795 ? 166 ARG   A NH1 1 
ATOM   1066 N  NH2 . ARG   A 1 154 ? 39.95000  4.90100   -7.87500  1.000 22.45411 ? 166 ARG   A NH2 1 
ATOM   1067 N  N   . PHE   A 1 155 ? 34.54600  7.96700   -7.44600  1.000 15.52003 ? 167 PHE   A N   1 
ATOM   1068 C  CA  . PHE   A 1 155 ? 34.43800  8.87900   -6.31000  1.000 15.56807 ? 167 PHE   A CA  1 
ATOM   1069 C  C   . PHE   A 1 155 ? 35.61200  8.54800   -5.39800  1.000 16.90525 ? 167 PHE   A C   1 
ATOM   1070 O  O   . PHE   A 1 155 ? 35.56300  7.58900   -4.62500  1.000 16.44823 ? 167 PHE   A O   1 
ATOM   1071 C  CB  . PHE   A 1 155 ? 33.09200  8.71100   -5.61700  1.000 15.73580 ? 167 PHE   A CB  1 
ATOM   1072 C  CG  . PHE   A 1 155 ? 32.75300  9.84100   -4.67600  1.000 15.79569 ? 167 PHE   A CG  1 
ATOM   1073 C  CD1 . PHE   A 1 155 ? 32.22900  11.02300  -5.15800  1.000 18.26318 ? 167 PHE   A CD1 1 
ATOM   1074 C  CD2 . PHE   A 1 155 ? 32.97600  9.72300   -3.31200  1.000 14.87512 ? 167 PHE   A CD2 1 
ATOM   1075 C  CE1 . PHE   A 1 155 ? 31.92600  12.06300  -4.28000  1.000 16.93859 ? 167 PHE   A CE1 1 
ATOM   1076 C  CE2 . PHE   A 1 155 ? 32.67000  10.75300  -2.44700  1.000 16.27416 ? 167 PHE   A CE2 1 
ATOM   1077 C  CZ  . PHE   A 1 155 ? 32.14700  11.90900  -2.93000  1.000 16.26808 ? 167 PHE   A CZ  1 
ATOM   1078 N  N   . GLY   A 1 156 ? 36.68500  9.32600   -5.50900  1.000 17.57815 ? 168 GLY   A N   1 
ATOM   1079 C  CA  . GLY   A 1 156 ? 37.89500  9.02700   -4.79200  1.000 17.98117 ? 168 GLY   A CA  1 
ATOM   1080 C  C   . GLY   A 1 156 ? 38.38300  7.62800   -5.11900  1.000 17.95971 ? 168 GLY   A C   1 
ATOM   1081 O  O   . GLY   A 1 156 ? 38.53500  7.24800   -6.28800  1.000 20.40545 ? 168 GLY   A O   1 
ATOM   1082 N  N   . PRO   A 1 157 ? 38.60700  6.81500   -4.08400  1.000 16.36943 ? 169 PRO   A N   1 
ATOM   1083 C  CA  . PRO   A 1 157 ? 39.16500  5.47800   -4.29000  1.000 16.90863 ? 169 PRO   A CA  1 
ATOM   1084 C  C   . PRO   A 1 157 ? 38.14500  4.41300   -4.68100  1.000 16.71646 ? 169 PRO   A C   1 
ATOM   1085 O  O   . PRO   A 1 157 ? 38.52800  3.24000   -4.78900  1.000 18.34780 ? 169 PRO   A O   1 
ATOM   1086 C  CB  . PRO   A 1 157 ? 39.78700  5.17100   -2.92100  1.000 18.53863 ? 169 PRO   A CB  1 
ATOM   1087 C  CG  . PRO   A 1 157 ? 38.84500  5.86300   -1.94700  1.000 19.80763 ? 169 PRO   A CG  1 
ATOM   1088 C  CD  . PRO   A 1 157 ? 38.40600  7.12800   -2.65200  1.000 17.59335 ? 169 PRO   A CD  1 
ATOM   1089 N  N   . VAL   A 1 158 ? 36.86800  4.76100   -4.89400  1.000 16.61869 ? 170 VAL   A N   1 
ATOM   1090 C  CA  . VAL   A 1 158 ? 35.85200  3.76900   -5.23300  1.000 16.67754 ? 170 VAL   A CA  1 
ATOM   1091 C  C   . VAL   A 1 158 ? 35.16900  4.12300   -6.54400  1.000 13.97330 ? 170 VAL   A C   1 
ATOM   1092 O  O   . VAL   A 1 158 ? 35.21400  5.25900   -7.02900  1.000 15.26543 ? 170 VAL   A O   1 
ATOM   1093 C  CB  . VAL   A 1 158 ? 34.78600  3.58400   -4.13200  1.000 14.73104 ? 170 VAL   A CB  1 
ATOM   1094 C  CG1 . VAL   A 1 158 ? 35.44400  3.28800   -2.81700  1.000 14.65564 ? 170 VAL   A CG1 1 
ATOM   1095 C  CG2 . VAL   A 1 158 ? 33.88000  4.83000   -4.03800  1.000 12.86875 ? 170 VAL   A CG2 1 
ATOM   1096 N  N   . GLU   A 1 159 ? 34.50400  3.12300   -7.11100  1.000 14.85076 ? 171 GLU   A N   1 
ATOM   1097 C  CA  . GLU   A 1 159 ? 33.48200  3.33600   -8.12100  1.000 14.37324 ? 171 GLU   A CA  1 
ATOM   1098 C  C   . GLU   A 1 159 ? 32.10700  3.18000   -7.47900  1.000 13.91611 ? 171 GLU   A C   1 
ATOM   1099 O  O   . GLU   A 1 159 ? 31.86000  2.20900   -6.74900  1.000 14.53631 ? 171 GLU   A O   1 
ATOM   1100 C  CB  . GLU   A 1 159 ? 33.62600  2.32400   -9.25100  1.000 16.19323 ? 171 GLU   A CB  1 
ATOM   1101 C  CG  . GLU   A 1 159 ? 32.69800  2.61700   -10.40300 1.000 18.36769 ? 171 GLU   A CG  1 
ATOM   1102 C  CD  . GLU   A 1 159 ? 33.08300  1.81700   -11.62700 1.000 20.17590 ? 171 GLU   A CD  1 
ATOM   1103 O  OE1 . GLU   A 1 159 ? 32.92500  0.58300   -11.61600 1.000 20.64336 ? 171 GLU   A OE1 1 
ATOM   1104 O  OE2 . GLU   A 1 159 ? 33.53500  2.44600   -12.61400 1.000 23.06831 ? 171 GLU   A OE2 1 
ATOM   1105 N  N   . LEU   A 1 160 ? 31.22300  4.13800   -7.74900  1.000 14.36059 ? 172 LEU   A N   1 
ATOM   1106 C  CA  . LEU   A 1 160 ? 29.81700  4.05700   -7.37600  1.000 12.89601 ? 172 LEU   A CA  1 
ATOM   1107 C  C   . LEU   A 1 160 ? 29.04900  3.56300   -8.58600  1.000 13.71964 ? 172 LEU   A C   1 
ATOM   1108 O  O   . LEU   A 1 160 ? 29.33800  3.97300   -9.71300  1.000 15.04111 ? 172 LEU   A O   1 
ATOM   1109 C  CB  . LEU   A 1 160 ? 29.30300  5.44200   -6.95700  1.000 13.19277 ? 172 LEU   A CB  1 
ATOM   1110 C  CG  . LEU   A 1 160 ? 30.12300  6.16100   -5.89000  1.000 13.18017 ? 172 LEU   A CG  1 
ATOM   1111 C  CD1 . LEU   A 1 160 ? 29.51100  7.52200   -5.59900  1.000 13.68986 ? 172 LEU   A CD1 1 
ATOM   1112 C  CD2 . LEU   A 1 160 ? 30.19500  5.35300   -4.62500  1.000 13.54280 ? 172 LEU   A CD2 1 
ATOM   1113 N  N   . PHE   A 1 161 ? 28.09200  2.66900   -8.36000  1.000 12.85409 ? 173 PHE   A N   1 
ATOM   1114 C  CA  . PHE   A 1 161 ? 27.35800  2.04900   -9.46300  1.000 13.92107 ? 173 PHE   A CA  1 
ATOM   1115 C  C   . PHE   A 1 161 ? 25.87400  2.02600   -9.13200  1.000 12.80621 ? 173 PHE   A C   1 
ATOM   1116 O  O   . PHE   A 1 161 ? 25.48900  1.58700   -8.04000  1.000 12.92083 ? 173 PHE   A O   1 
ATOM   1117 C  CB  . PHE   A 1 161 ? 27.88700  0.62200   -9.68900  1.000 13.24868 ? 173 PHE   A CB  1 
ATOM   1118 C  CG  . PHE   A 1 161 ? 27.23000  -0.14200  -10.82000 1.000 13.41165 ? 173 PHE   A CG  1 
ATOM   1119 C  CD1 . PHE   A 1 161 ? 27.35600  0.28500   -12.12600 1.000 17.17444 ? 173 PHE   A CD1 1 
ATOM   1120 C  CD2 . PHE   A 1 161 ? 26.55700  -1.32600  -10.57600 1.000 16.15026 ? 173 PHE   A CD2 1 
ATOM   1121 C  CE1 . PHE   A 1 161 ? 26.76900  -0.41700  -13.15300 1.000 17.61617 ? 173 PHE   A CE1 1 
ATOM   1122 C  CE2 . PHE   A 1 161 ? 25.97900  -2.04900  -11.61700 1.000 15.12313 ? 173 PHE   A CE2 1 
ATOM   1123 C  CZ  . PHE   A 1 161 ? 26.08700  -1.60200  -12.89600 1.000 16.23204 ? 173 PHE   A CZ  1 
ATOM   1124 N  N   . TYR   A 1 162 ? 25.03800  2.46900   -10.07500 1.000 13.67185 ? 174 TYR   A N   1 
ATOM   1125 C  CA  . TYR   A 1 162 ? 23.59700  2.34200   -9.89800  1.000 12.11914 ? 174 TYR   A CA  1 
ATOM   1126 C  C   . TYR   A 1 162 ? 23.13700  1.14700   -10.71500 1.000 13.69671 ? 174 TYR   A C   1 
ATOM   1127 O  O   . TYR   A 1 162 ? 23.09700  1.23900   -11.95500 1.000 14.38307 ? 174 TYR   A O   1 
ATOM   1128 C  CB  . TYR   A 1 162 ? 22.85700  3.61000   -10.33500 1.000 12.85189 ? 174 TYR   A CB  1 
ATOM   1129 C  CG  . TYR   A 1 162 ? 21.35400  3.44900   -10.26800 1.000 12.63314 ? 174 TYR   A CG  1 
ATOM   1130 C  CD1 . TYR   A 1 162 ? 20.73300  2.96100   -9.11400  1.000 12.43241 ? 174 TYR   A CD1 1 
ATOM   1131 C  CD2 . TYR   A 1 162 ? 20.54800  3.74900   -11.36400 1.000 13.80496 ? 174 TYR   A CD2 1 
ATOM   1132 C  CE1 . TYR   A 1 162 ? 19.35700  2.79100   -9.06200  1.000 13.04184 ? 174 TYR   A CE1 1 
ATOM   1133 C  CE2 . TYR   A 1 162 ? 19.16900  3.58200   -11.31700 1.000 14.67691 ? 174 TYR   A CE2 1 
ATOM   1134 C  CZ  . TYR   A 1 162 ? 18.57900  3.10500   -10.16000 1.000 13.36913 ? 174 TYR   A CZ  1 
ATOM   1135 O  OH  . TYR   A 1 162 ? 17.22200  2.93400   -10.07800 1.000 16.11038 ? 174 TYR   A OH  1 
ATOM   1136 N  N   . PRO   A 1 163 ? 22.80500  0.01400   -10.08800 1.000 13.00513 ? 175 PRO   A N   1 
ATOM   1137 C  CA  . PRO   A 1 163 ? 22.48300  -1.19400  -10.86500 1.000 12.23895 ? 175 PRO   A CA  1 
ATOM   1138 C  C   . PRO   A 1 163 ? 21.04900  -1.21400  -11.36500 1.000 12.82221 ? 175 PRO   A C   1 
ATOM   1139 O  O   . PRO   A 1 163 ? 20.70300  -2.10100  -12.15400 1.000 15.67219 ? 175 PRO   A O   1 
ATOM   1140 C  CB  . PRO   A 1 163 ? 22.70800  -2.31500  -9.84500  1.000 13.67476 ? 175 PRO   A CB  1 
ATOM   1141 C  CG  . PRO   A 1 163 ? 22.30600  -1.66700  -8.53300  1.000 13.10772 ? 175 PRO   A CG  1 
ATOM   1142 C  CD  . PRO   A 1 163 ? 22.79900  -0.24600  -8.63400  1.000 11.54874 ? 175 PRO   A CD  1 
ATOM   1143 N  N   . GLY   A 1 164 ? 20.22900  -0.25500  -10.95000 1.000 13.30151 ? 176 GLY   A N   1 
ATOM   1144 C  CA  . GLY   A 1 164 ? 18.79100  -0.31800  -11.09800 1.000 13.34461 ? 176 GLY   A CA  1 
ATOM   1145 C  C   . GLY   A 1 164 ? 18.10500  -0.54900  -9.76200  1.000 14.07547 ? 176 GLY   A C   1 
ATOM   1146 O  O   . GLY   A 1 164 ? 18.73000  -0.83700  -8.74100  1.000 13.08744 ? 176 GLY   A O   1 
ATOM   1147 N  N   . ALA   A 1 165 ? 16.78400  -0.42000  -9.79100  1.000 12.79633 ? 177 ALA   A N   1 
ATOM   1148 C  CA  . ALA   A 1 165 ? 15.99700  -0.58800  -8.57500  1.000 13.17516 ? 177 ALA   A CA  1 
ATOM   1149 C  C   . ALA   A 1 165 ? 16.10300  -2.01800  -8.04800  1.000 13.72986 ? 177 ALA   A C   1 
ATOM   1150 O  O   . ALA   A 1 165 ? 16.15400  -2.99100  -8.81400  1.000 13.71965 ? 177 ALA   A O   1 
ATOM   1151 C  CB  . ALA   A 1 165 ? 14.53900  -0.23200  -8.85700  1.000 14.40735 ? 177 ALA   A CB  1 
ATOM   1152 N  N   . ALA   A 1 166 ? 16.15000  -2.15000  -6.72500  1.000 13.56925 ? 178 ALA   A N   1 
ATOM   1153 C  CA  . ALA   A 1 166 ? 16.25100  -3.46800  -6.12100  1.000 12.52603 ? 178 ALA   A CA  1 
ATOM   1154 C  C   . ALA   A 1 166 ? 15.62000  -3.40900  -4.73500  1.000 11.40960 ? 178 ALA   A C   1 
ATOM   1155 O  O   . ALA   A 1 166 ? 14.39200  -3.32900  -4.62300  1.000 13.97836 ? 178 ALA   A O   1 
ATOM   1156 C  CB  . ALA   A 1 166 ? 17.71500  -3.91100  -6.09500  1.000 14.27120 ? 178 ALA   A CB  1 
ATOM   1157 N  N   . HIS   A 1 167 ? 16.45300  -3.39200  -3.69000  1.000 11.67555 ? 179 HIS   A N   1 
ATOM   1158 C  CA  . HIS   A 1 167 ? 15.94800  -3.18500  -2.34200  1.000 12.46032 ? 179 HIS   A CA  1 
ATOM   1159 C  C   . HIS   A 1 167 ? 15.20800  -1.85400  -2.22700  1.000 13.21152 ? 179 HIS   A C   1 
ATOM   1160 O  O   . HIS   A 1 167 ? 14.22600  -1.74000  -1.48000  1.000 13.51351 ? 179 HIS   A O   1 
ATOM   1161 C  CB  . HIS   A 1 167 ? 17.14200  -3.23800  -1.38900  1.000 14.03437 ? 179 HIS   A CB  1 
ATOM   1162 C  CG  . HIS   A 1 167 ? 16.84000  -2.71800  -0.02500  1.000 13.19556 ? 179 HIS   A CG  1 
ATOM   1163 N  ND1 . HIS   A 1 167 ? 16.27500  -3.50200  0.96100   1.000 14.30436 ? 179 HIS   A ND1 1 
ATOM   1164 C  CD2 . HIS   A 1 167 ? 17.03700  -1.50200  0.52600   1.000 13.25868 ? 179 HIS   A CD2 1 
ATOM   1165 C  CE1 . HIS   A 1 167 ? 16.11600  -2.78000  2.05300   1.000 15.45525 ? 179 HIS   A CE1 1 
ATOM   1166 N  NE2 . HIS   A 1 167 ? 16.56300  -1.56300  1.80900   1.000 13.87035 ? 179 HIS   A NE2 1 
ATOM   1167 N  N   . SER   A 1 168 ? 15.66500  -0.84900  -2.96200  1.000 12.57754 ? 180 SER   A N   1 
ATOM   1168 C  CA  . SER   A 1 168 ? 14.99000  0.44100   -3.06300  1.000 12.19191 ? 180 SER   A CA  1 
ATOM   1169 C  C   . SER   A 1 168 ? 15.25300  0.95100   -4.46800  1.000 12.20236 ? 180 SER   A C   1 
ATOM   1170 O  O   . SER   A 1 168 ? 16.11300  0.41900   -5.18300  1.000 13.02489 ? 180 SER   A O   1 
ATOM   1171 C  CB  . SER   A 1 168 ? 15.48600  1.41200   -1.99800  1.000 12.57806 ? 180 SER   A CB  1 
ATOM   1172 O  OG  . SER   A 1 168 ? 16.88400  1.65300   -2.16400  1.000 13.65680 ? 180 SER   A OG  1 
ATOM   1173 N  N   . THR   A 1 169 ? 14.49800  1.97500   -4.88800  1.000 12.50400 ? 181 THR   A N   1 
ATOM   1174 C  CA  . THR   A 1 169 ? 14.69100  2.44500   -6.26000  1.000 14.86425 ? 181 THR   A CA  1 
ATOM   1175 C  C   . THR   A 1 169 ? 16.01000  3.17700   -6.44300  1.000 15.09563 ? 181 THR   A C   1 
ATOM   1176 O  O   . THR   A 1 169 ? 16.50400  3.26300   -7.57100  1.000 15.23007 ? 181 THR   A O   1 
ATOM   1177 C  CB  . THR   A 1 169 ? 13.53500  3.32400   -6.74300  1.000 16.14863 ? 181 THR   A CB  1 
ATOM   1178 O  OG1 . THR   A 1 169 ? 13.44300  4.50200   -5.92900  1.000 18.09532 ? 181 THR   A OG1 1 
ATOM   1179 C  CG2 . THR   A 1 169 ? 12.22600  2.56600   -6.71400  1.000 18.89423 ? 181 THR   A CG2 1 
ATOM   1180 N  N   . ASP   A 1 170 ? 16.60200  3.67700   -5.36100  1.000 12.58853 ? 182 ASP   A N   1 
ATOM   1181 C  CA  . ASP   A 1 170 ? 17.78100  4.53700   -5.40900  1.000 12.06655 ? 182 ASP   A CA  1 
ATOM   1182 C  C   . ASP   A 1 170 ? 19.06200  3.81000   -5.02800  1.000 11.96466 ? 182 ASP   A C   1 
ATOM   1183 O  O   . ASP   A 1 170 ? 20.12000  4.43500   -4.99500  1.000 12.60976 ? 182 ASP   A O   1 
ATOM   1184 C  CB  . ASP   A 1 170 ? 17.58800  5.72400   -4.44300  1.000 11.48390 ? 182 ASP   A CB  1 
ATOM   1185 C  CG  . ASP   A 1 170 ? 17.36600  5.27600   -3.00000  1.000 12.32451 ? 182 ASP   A CG  1 
ATOM   1186 O  OD1 . ASP   A 1 170 ? 16.62600  4.28500   -2.77100  1.000 12.14471 ? 182 ASP   A OD1 1 
ATOM   1187 O  OD2 . ASP   A 1 170 ? 17.90800  5.92900   -2.07800  1.000 12.61931 ? 182 ASP   A OD2 1 
ATOM   1188 N  N   . ASN   A 1 171 ? 19.00500  2.52000   -4.69600  1.000 11.51555 ? 183 ASN   A N   1 
ATOM   1189 C  CA  . ASN   A 1 171 ? 20.17600  1.87400   -4.10900  1.000 11.12406 ? 183 ASN   A CA  1 
ATOM   1190 C  C   . ASN   A 1 171 ? 21.41100  1.87600   -5.01100  1.000 10.89997 ? 183 ASN   A C   1 
ATOM   1191 O  O   . ASN   A 1 171 ? 21.33700  1.58100   -6.20700  1.000 12.10427 ? 183 ASN   A O   1 
ATOM   1192 C  CB  . ASN   A 1 171 ? 19.82500  0.48100   -3.56400  1.000 11.91149 ? 183 ASN   A CB  1 
ATOM   1193 C  CG  . ASN   A 1 171 ? 19.22700  -0.47500  -4.59600  1.000 11.61561 ? 183 ASN   A CG  1 
ATOM   1194 O  OD1 . ASN   A 1 171 ? 18.55700  -1.48800  -4.29000  1.000 14.36737 ? 183 ASN   A OD1 1 
ATOM   1195 N  ND2 . ASN   A 1 171 ? 19.53300  -0.17900  -5.82800  1.000 13.31134 ? 183 ASN   A ND2 1 
ATOM   1196 N  N   . LEU   A 1 172 ? 22.55200  2.23800   -4.41500  1.000 12.22519 ? 184 LEU   A N   1 
ATOM   1197 C  CA  . LEU   A 1 172 ? 23.85900  2.20700   -5.06100  1.000 12.38008 ? 184 LEU   A CA  1 
ATOM   1198 C  C   . LEU   A 1 172 ? 24.68700  1.06500   -4.50500  1.000 13.93471 ? 184 LEU   A C   1 
ATOM   1199 O  O   . LEU   A 1 172 ? 24.50800  0.64200   -3.35700  1.000 12.97135 ? 184 LEU   A O   1 
ATOM   1200 C  CB  . LEU   A 1 172 ? 24.63100  3.49700   -4.75700  1.000 12.69149 ? 184 LEU   A CB  1 
ATOM   1201 C  CG  . LEU   A 1 172 ? 24.00200  4.81600   -5.18300  1.000 11.33883 ? 184 LEU   A CG  1 
ATOM   1202 C  CD1 . LEU   A 1 172 ? 24.94400  5.97900   -4.86400  1.000 13.53596 ? 184 LEU   A CD1 1 
ATOM   1203 C  CD2 . LEU   A 1 172 ? 23.71100  4.79700   -6.67200  1.000 14.15650 ? 184 LEU   A CD2 1 
ATOM   1204 N  N   . VAL   A 1 173 ? 25.63300  0.58900   -5.31800  1.000 13.35251 ? 185 VAL   A N   1 
ATOM   1205 C  CA  . VAL   A 1 173 ? 26.67800  -0.31100  -4.84000  1.000 13.32280 ? 185 VAL   A CA  1 
ATOM   1206 C  C   . VAL   A 1 173 ? 28.02800  0.36000   -5.04800  1.000 11.99395 ? 185 VAL   A C   1 
ATOM   1207 O  O   . VAL   A 1 173 ? 28.15900  1.34100   -5.78900  1.000 12.92594 ? 185 VAL   A O   1 
ATOM   1208 C  CB  . VAL   A 1 173 ? 26.63300  -1.72700  -5.45200  1.000 15.24850 ? 185 VAL   A CB  1 
ATOM   1209 C  CG1 . VAL   A 1 173 ? 25.27800  -2.33900  -5.19400  1.000 15.33639 ? 185 VAL   A CG1 1 
ATOM   1210 C  CG2 . VAL   A 1 173 ? 26.94300  -1.71000  -6.93600  1.000 17.42227 ? 185 VAL   A CG2 1 
ATOM   1211 N  N   . VAL   A 1 174 ? 29.03100  -0.14400  -4.33800  1.000 11.80046 ? 186 VAL   A N   1 
ATOM   1212 C  CA  . VAL   A 1 174 ? 30.33600  0.50800   -4.25900  1.000 15.25040 ? 186 VAL   A CA  1 
ATOM   1213 C  C   . VAL   A 1 174 ? 31.40100  -0.54500  -4.51000  1.000 13.90375 ? 186 VAL   A C   1 
ATOM   1214 O  O   . VAL   A 1 174 ? 31.36200  -1.61600  -3.90000  1.000 13.95248 ? 186 VAL   A O   1 
ATOM   1215 C  CB  . VAL   A 1 174 ? 30.53300  1.16700   -2.88000  1.000 12.71187 ? 186 VAL   A CB  1 
ATOM   1216 C  CG1 . VAL   A 1 174 ? 31.88000  1.89300   -2.80800  1.000 14.15900 ? 186 VAL   A CG1 1 
ATOM   1217 C  CG2 . VAL   A 1 174 ? 29.39900  2.15300   -2.59700  1.000 14.29800 ? 186 VAL   A CG2 1 
ATOM   1218 N  N   . TYR   A 1 175 ? 32.33100  -0.26200  -5.42200  1.000 13.62304 ? 187 TYR   A N   1 
ATOM   1219 C  CA  . TYR   A 1 175 ? 33.42000  -1.18600  -5.72200  1.000 13.71859 ? 187 TYR   A CA  1 
ATOM   1220 C  C   . TYR   A 1 175 ? 34.75700  -0.52700  -5.42000  1.000 13.26316 ? 187 TYR   A C   1 
ATOM   1221 O  O   . TYR   A 1 175 ? 34.96900  0.63500   -5.77600  1.000 14.94669 ? 187 TYR   A O   1 
ATOM   1222 C  CB  . TYR   A 1 175 ? 33.39500  -1.57900  -7.19800  1.000 14.73353 ? 187 TYR   A CB  1 
ATOM   1223 C  CG  . TYR   A 1 175 ? 34.35500  -2.68600  -7.52300  1.000 15.55454 ? 187 TYR   A CG  1 
ATOM   1224 C  CD1 . TYR   A 1 175 ? 34.20900  -3.94100  -6.95000  1.000 14.68286 ? 187 TYR   A CD1 1 
ATOM   1225 C  CD2 . TYR   A 1 175 ? 35.42100  -2.47800  -8.39100  1.000 16.82031 ? 187 TYR   A CD2 1 
ATOM   1226 C  CE1 . TYR   A 1 175 ? 35.08200  -4.96600  -7.24100  1.000 16.43317 ? 187 TYR   A CE1 1 
ATOM   1227 C  CE2 . TYR   A 1 175 ? 36.30100  -3.50800  -8.68900  1.000 15.63605 ? 187 TYR   A CE2 1 
ATOM   1228 C  CZ  . TYR   A 1 175 ? 36.12400  -4.74000  -8.10400  1.000 17.85772 ? 187 TYR   A CZ  1 
ATOM   1229 O  OH  . TYR   A 1 175 ? 36.97900  -5.79900  -8.36700  1.000 19.73993 ? 187 TYR   A OH  1 
ATOM   1230 N  N   . VAL   A 1 176 ? 35.65200  -1.26500  -4.76600  1.000 13.77683 ? 188 VAL   A N   1 
ATOM   1231 C  CA  . VAL   A 1 176 ? 37.01800  -0.80400  -4.50400  1.000 15.43112 ? 188 VAL   A CA  1 
ATOM   1232 C  C   . VAL   A 1 176 ? 37.97400  -1.52800  -5.45300  1.000 16.71617 ? 188 VAL   A C   1 
ATOM   1233 O  O   . VAL   A 1 176 ? 38.37500  -2.66900  -5.17800  1.000 17.85466 ? 188 VAL   A O   1 
ATOM   1234 C  CB  . VAL   A 1 176 ? 37.43400  -1.01300  -3.04100  1.000 15.40808 ? 188 VAL   A CB  1 
ATOM   1235 C  CG1 . VAL   A 1 176 ? 38.75300  -0.28900  -2.76000  1.000 17.56498 ? 188 VAL   A CG1 1 
ATOM   1236 C  CG2 . VAL   A 1 176 ? 36.33700  -0.52100  -2.08900  1.000 17.92113 ? 188 VAL   A CG2 1 
ATOM   1237 N  N   . PRO   A 1 177 ? 38.36800  -0.91300  -6.56900  1.000 17.73275 ? 189 PRO   A N   1 
ATOM   1238 C  CA  . PRO   A 1 177 ? 39.16400  -1.66100  -7.55900  1.000 21.08122 ? 189 PRO   A CA  1 
ATOM   1239 C  C   . PRO   A 1 177 ? 40.51800  -2.12900  -7.04400  1.000 21.92576 ? 189 PRO   A C   1 
ATOM   1240 O  O   . PRO   A 1 177 ? 40.95100  -3.23500  -7.39700  1.000 23.37106 ? 189 PRO   A O   1 
ATOM   1241 C  CB  . PRO   A 1 177 ? 39.26100  -0.70100  -8.75400  1.000 23.55655 ? 189 PRO   A CB  1 
ATOM   1242 C  CG  . PRO   A 1 177 ? 38.88700  0.64500   -8.22400  1.000 30.73583 ? 189 PRO   A CG  1 
ATOM   1243 C  CD  . PRO   A 1 177 ? 37.95600  0.41100   -7.06200  1.000 19.11688 ? 189 PRO   A CD  1 
ATOM   1244 N  N   . SER   A 1 178 ? 41.18400  -1.35300  -6.18900  1.000 21.23351 ? 190 SER   A N   1 
ATOM   1245 C  CA  . SER   A 1 178 ? 42.49400  -1.78100  -5.69000  1.000 23.39760 ? 190 SER   A CA  1 
ATOM   1246 C  C   . SER   A 1 178 ? 42.41800  -3.07200  -4.88200  1.000 27.20963 ? 190 SER   A C   1 
ATOM   1247 O  O   . SER   A 1 178 ? 43.40800  -3.80700  -4.79400  1.000 26.57917 ? 190 SER   A O   1 
ATOM   1248 C  CB  . SER   A 1 178 ? 43.11700  -0.68200  -4.83100  1.000 25.75485 ? 190 SER   A CB  1 
ATOM   1249 O  OG  . SER   A 1 178 ? 42.43900  -0.55800  -3.58600  1.000 28.72419 ? 190 SER   A OG  1 
ATOM   1250 N  N   . ALA   A 1 179 ? 41.26800  -3.36600  -4.27800  1.000 20.91632 ? 191 ALA   A N   1 
ATOM   1251 C  CA  . ALA   A 1 179 ? 41.14100  -4.50300  -3.38100  1.000 21.67098 ? 191 ALA   A CA  1 
ATOM   1252 C  C   . ALA   A 1 179 ? 40.13700  -5.54600  -3.85300  1.000 17.92891 ? 191 ALA   A C   1 
ATOM   1253 O  O   . ALA   A 1 179 ? 39.97400  -6.57400  -3.18300  1.000 19.63738 ? 191 ALA   A O   1 
ATOM   1254 C  CB  . ALA   A 1 179 ? 40.76900  -4.02000  -1.97200  1.000 23.56962 ? 191 ALA   A CB  1 
ATOM   1255 N  N   A SER   A 1 180 ? 39.47300  -5.32100  -4.98800  0.718 18.24300 ? 192 SER   A N   1 
ATOM   1256 N  N   B SER   A 1 180 ? 39.45300  -5.31000  -4.97500  0.282 18.24033 ? 192 SER   A N   1 
ATOM   1257 C  CA  A SER   A 1 180 ? 38.45400  -6.23800  -5.50000  0.718 18.69876 ? 192 SER   A CA  1 
ATOM   1258 C  CA  B SER   A 1 180 ? 38.45600  -6.23900  -5.50900  0.282 18.70637 ? 192 SER   A CA  1 
ATOM   1259 C  C   A SER   A 1 180 ? 37.34500  -6.47300  -4.47700  0.718 17.67322 ? 192 SER   A C   1 
ATOM   1260 C  C   B SER   A 1 180 ? 37.28500  -6.44400  -4.55100  0.282 17.73484 ? 192 SER   A C   1 
ATOM   1261 O  O   A SER   A 1 180 ? 36.85000  -7.58900  -4.30700  0.718 17.25635 ? 192 SER   A O   1 
ATOM   1262 O  O   B SER   A 1 180 ? 36.68400  -7.52100  -4.50400  0.282 17.17254 ? 192 SER   A O   1 
ATOM   1263 C  CB  A SER   A 1 180 ? 39.05400  -7.55700  -5.99900  0.718 21.38693 ? 192 SER   A CB  1 
ATOM   1264 C  CB  B SER   A 1 180 ? 39.07200  -7.57800  -5.92600  0.282 21.22873 ? 192 SER   A CB  1 
ATOM   1265 O  OG  A SER   A 1 180 ? 39.97000  -7.32600  -7.06300  0.718 23.64400 ? 192 SER   A OG  1 
ATOM   1266 O  OG  B SER   A 1 180 ? 38.08400  -8.45100  -6.43200  0.282 22.03596 ? 192 SER   A OG  1 
ATOM   1267 N  N   . VAL   A 1 181 ? 36.94300  -5.40600  -3.79400  1.000 16.17938 ? 193 VAL   A N   1 
ATOM   1268 C  CA  . VAL   A 1 181 ? 35.90300  -5.47200  -2.77600  1.000 16.35380 ? 193 VAL   A CA  1 
ATOM   1269 C  C   . VAL   A 1 181 ? 34.64600  -4.83500  -3.33300  1.000 16.09852 ? 193 VAL   A C   1 
ATOM   1270 O  O   . VAL   A 1 181 ? 34.66500  -3.66700  -3.75300  1.000 14.99304 ? 193 VAL   A O   1 
ATOM   1271 C  CB  . VAL   A 1 181 ? 36.33800  -4.79200  -1.47200  1.000 17.63410 ? 193 VAL   A CB  1 
ATOM   1272 C  CG1 . VAL   A 1 181 ? 35.14000  -4.62900  -0.52700  1.000 16.93076 ? 193 VAL   A CG1 1 
ATOM   1273 C  CG2 . VAL   A 1 181 ? 37.47000  -5.58000  -0.82300  1.000 18.23329 ? 193 VAL   A CG2 1 
ATOM   1274 N  N   . LEU   A 1 182 ? 33.55800  -5.59700  -3.31600  1.000 14.01540 ? 194 LEU   A N   1 
ATOM   1275 C  CA  . LEU   A 1 182 ? 32.24700  -5.12300  -3.73600  1.000 15.16765 ? 194 LEU   A CA  1 
ATOM   1276 C  C   . LEU   A 1 182 ? 31.34700  -4.99900  -2.51300  1.000 13.77368 ? 194 LEU   A C   1 
ATOM   1277 O  O   . LEU   A 1 182 ? 31.05400  -5.99400  -1.84300  1.000 15.30719 ? 194 LEU   A O   1 
ATOM   1278 C  CB  . LEU   A 1 182 ? 31.63700  -6.07800  -4.75500  1.000 14.94865 ? 194 LEU   A CB  1 
ATOM   1279 C  CG  . LEU   A 1 182 ? 30.22000  -5.75100  -5.21000  1.000 14.72129 ? 194 LEU   A CG  1 
ATOM   1280 C  CD1 . LEU   A 1 182 ? 30.18000  -4.40100  -5.94200  1.000 16.77395 ? 194 LEU   A CD1 1 
ATOM   1281 C  CD2 . LEU   A 1 182 ? 29.69900  -6.87100  -6.09800  1.000 16.65719 ? 194 LEU   A CD2 1 
ATOM   1282 N  N   . TYR   A 1 183 ? 30.87700  -3.79200  -2.26100  1.000 15.33357 ? 195 TYR   A N   1 
ATOM   1283 C  CA  . TYR   A 1 183 ? 29.95900  -3.52100  -1.16100  1.000 12.59556 ? 195 TYR   A CA  1 
ATOM   1284 C  C   . TYR   A 1 183 ? 28.57300  -3.37900  -1.77100  1.000 12.24924 ? 195 TYR   A C   1 
ATOM   1285 O  O   . TYR   A 1 183 ? 28.31200  -2.42200  -2.51100  1.000 13.33205 ? 195 TYR   A O   1 
ATOM   1286 C  CB  . TYR   A 1 183 ? 30.37300  -2.24700  -0.44800  1.000 13.87205 ? 195 TYR   A CB  1 
ATOM   1287 C  CG  . TYR   A 1 183 ? 29.38400  -1.76500  0.57900   1.000 12.57079 ? 195 TYR   A CG  1 
ATOM   1288 C  CD1 . TYR   A 1 183 ? 29.29300  -2.37400  1.82100   1.000 16.66959 ? 195 TYR   A CD1 1 
ATOM   1289 C  CD2 . TYR   A 1 183 ? 28.52800  -0.70800  0.30200   1.000 13.43221 ? 195 TYR   A CD2 1 
ATOM   1290 C  CE1 . TYR   A 1 183 ? 28.39100  -1.92800  2.76400   1.000 19.72894 ? 195 TYR   A CE1 1 
ATOM   1291 C  CE2 . TYR   A 1 183 ? 27.64000  -0.24700  1.23900   1.000 15.19964 ? 195 TYR   A CE2 1 
ATOM   1292 C  CZ  . TYR   A 1 183 ? 27.56800  -0.85700  2.45500   1.000 18.37469 ? 195 TYR   A CZ  1 
ATOM   1293 O  OH  . TYR   A 1 183 ? 26.66700  -0.38500  3.37800   1.000 23.20276 ? 195 TYR   A OH  1 
ATOM   1294 N  N   . GLY   A 1 184 ? 27.70500  -4.36000  -1.49900  1.000 12.97854 ? 196 GLY   A N   1 
ATOM   1295 C  CA  . GLY   A 1 184 ? 26.39400  -4.38400  -2.12000  1.000 12.95694 ? 196 GLY   A CA  1 
ATOM   1296 C  C   . GLY   A 1 184 ? 25.32400  -3.59600  -1.40100  1.000 12.54548 ? 196 GLY   A C   1 
ATOM   1297 O  O   . GLY   A 1 184 ? 24.23700  -3.37700  -1.95900  1.000 12.37405 ? 196 GLY   A O   1 
ATOM   1298 N  N   . GLY   A 1 185 ? 25.59300  -3.17800  -0.16400  1.000 12.49452 ? 197 GLY   A N   1 
ATOM   1299 C  CA  . GLY   A 1 185 ? 24.54500  -2.58100  0.63300   1.000 12.59518 ? 197 GLY   A CA  1 
ATOM   1300 C  C   . GLY   A 1 185 ? 23.34200  -3.48900  0.71200   1.000 11.02275 ? 197 GLY   A C   1 
ATOM   1301 O  O   . GLY   A 1 185 ? 23.43900  -4.71400  0.59600   1.000 12.89595 ? 197 GLY   A O   1 
ATOM   1302 N  N   . CYS   A 1 186 ? 22.17600  -2.88400  0.91100   1.000 11.79583 ? 198 CYS   A N   1 
ATOM   1303 C  CA  . CYS   A 1 186 ? 20.99700  -3.67800  1.25800   1.000 11.70673 ? 198 CYS   A CA  1 
ATOM   1304 C  C   . CYS   A 1 186 ? 20.35400  -4.35700  0.05900   1.000 12.47606 ? 198 CYS   A C   1 
ATOM   1305 O  O   . CYS   A 1 186 ? 19.42900  -5.16500  0.24100   1.000 12.84260 ? 198 CYS   A O   1 
ATOM   1306 C  CB  . CYS   A 1 186 ? 20.01700  -2.82600  2.06200   1.000 13.04573 ? 198 CYS   A CB  1 
ATOM   1307 S  SG  . CYS   A 1 186 ? 20.89800  -2.10500  3.51400   1.000 14.60042 ? 198 CYS   A SG  1 
ATOM   1308 N  N   . ALA   A 1 187 ? 20.86300  -4.08700  -1.14900  1.000 12.34723 ? 199 ALA   A N   1 
ATOM   1309 C  CA  . ALA   A 1 187 ? 20.47600  -4.83900  -2.33300  1.000 11.96173 ? 199 ALA   A CA  1 
ATOM   1310 C  C   . ALA   A 1 187 ? 21.02700  -6.25900  -2.34400  1.000 12.47720 ? 199 ALA   A C   1 
ATOM   1311 O  O   . ALA   A 1 187 ? 20.57000  -7.06900  -3.16100  1.000 13.68242 ? 199 ALA   A O   1 
ATOM   1312 C  CB  . ALA   A 1 187 ? 20.95700  -4.10000  -3.58100  1.000 14.03116 ? 199 ALA   A CB  1 
ATOM   1313 N  N   . ILE   A 1 188 ? 22.01400  -6.57700  -1.50200  1.000 11.39982 ? 200 ILE   A N   1 
ATOM   1314 C  CA  . ILE   A 1 188 ? 22.62400  -7.90800  -1.47800  1.000 11.64284 ? 200 ILE   A CA  1 
ATOM   1315 C  C   . ILE   A 1 188 ? 22.42000  -8.48600  -0.08700  1.000 14.34262 ? 200 ILE   A C   1 
ATOM   1316 O  O   . ILE   A 1 188 ? 22.82200  -7.86500  0.90200   1.000 13.89335 ? 200 ILE   A O   1 
ATOM   1317 C  CB  . ILE   A 1 188 ? 24.12900  -7.84700  -1.80800  1.000 11.64771 ? 200 ILE   A CB  1 
ATOM   1318 C  CG1 . ILE   A 1 188 ? 24.35100  -7.28900  -3.21500  1.000 13.64595 ? 200 ILE   A CG1 1 
ATOM   1319 C  CG2 . ILE   A 1 188 ? 24.78800  -9.24100  -1.64400  1.000 13.01899 ? 200 ILE   A CG2 1 
ATOM   1320 C  CD1 . ILE   A 1 188 ? 23.68200  -8.11000  -4.30400  1.000 18.39149 ? 200 ILE   A CD1 1 
ATOM   1321 N  N   . TYR   A 1 189 ? 21.84000  -9.69100  -0.01500  1.000 13.29310 ? 201 TYR   A N   1 
ATOM   1322 C  CA  . TYR   A 1 189 ? 21.60600  -10.34700 1.26500   1.000 13.15129 ? 201 TYR   A CA  1 
ATOM   1323 C  C   . TYR   A 1 189 ? 22.76400  -11.27400 1.62200   1.000 12.28937 ? 201 TYR   A C   1 
ATOM   1324 O  O   . TYR   A 1 189 ? 23.36800  -11.90100 0.75100   1.000 13.35314 ? 201 TYR   A O   1 
ATOM   1325 C  CB  . TYR   A 1 189 ? 20.34500  -11.21100 1.18800   1.000 15.39174 ? 201 TYR   A CB  1 
ATOM   1326 C  CG  . TYR   A 1 189 ? 19.04200  -10.48000 1.32900   1.000 16.81164 ? 201 TYR   A CG  1 
ATOM   1327 C  CD1 . TYR   A 1 189 ? 18.92400  -9.14700  1.01000   1.000 17.58996 ? 201 TYR   A CD1 1 
ATOM   1328 C  CD2 . TYR   A 1 189 ? 17.91200  -11.14000 1.79700   1.000 25.29258 ? 201 TYR   A CD2 1 
ATOM   1329 C  CE1 . TYR   A 1 189 ? 17.71500  -8.49600  1.14400   1.000 16.79643 ? 201 TYR   A CE1 1 
ATOM   1330 C  CE2 . TYR   A 1 189 ? 16.70200  -10.49100 1.93500   1.000 24.68305 ? 201 TYR   A CE2 1 
ATOM   1331 C  CZ  . TYR   A 1 189 ? 16.61600  -9.16700  1.59600   1.000 23.20022 ? 201 TYR   A CZ  1 
ATOM   1332 O  OH  . TYR   A 1 189 ? 15.42300  -8.49700  1.72000   1.000 23.40112 ? 201 TYR   A OH  1 
ATOM   1333 N  N   . GLU   A 1 190 ? 23.03300  -11.40000 2.92100   1.000 14.15465 ? 202 GLU   A N   1 
ATOM   1334 C  CA  . GLU   A 1 190 ? 23.95200  -12.43300 3.37900   1.000 13.68365 ? 202 GLU   A CA  1 
ATOM   1335 C  C   . GLU   A 1 190 ? 23.31700  -13.81500 3.20500   1.000 13.98966 ? 202 GLU   A C   1 
ATOM   1336 O  O   . GLU   A 1 190 ? 22.10000  -13.96400 3.08700   1.000 13.39250 ? 202 GLU   A O   1 
ATOM   1337 C  CB  . GLU   A 1 190 ? 24.34100  -12.21300 4.85100   1.000 14.03734 ? 202 GLU   A CB  1 
ATOM   1338 C  CG  . GLU   A 1 190 ? 23.23200  -12.53000 5.86700   1.000 13.65234 ? 202 GLU   A CG  1 
ATOM   1339 C  CD  . GLU   A 1 190 ? 23.72100  -12.52500 7.31800   1.000 16.86249 ? 202 GLU   A CD  1 
ATOM   1340 O  OE1 . GLU   A 1 190 ? 24.85300  -13.00200 7.59500   1.000 17.63022 ? 202 GLU   A OE1 1 
ATOM   1341 O  OE2 . GLU   A 1 190 ? 22.97700  -12.02400 8.18900   1.000 18.79344 ? 202 GLU   A OE2 1 
ATOM   1342 N  N   . LEU   A 1 191 ? 24.18000  -14.83300 3.17800   1.000 14.74806 ? 203 LEU   A N   1 
ATOM   1343 C  CA  . LEU   A 1 191 ? 23.73300  -16.19800 2.89800   1.000 15.86753 ? 203 LEU   A CA  1 
ATOM   1344 C  C   . LEU   A 1 191 ? 22.76800  -16.72600 3.95200   1.000 14.77244 ? 203 LEU   A C   1 
ATOM   1345 O  O   . LEU   A 1 191 ? 21.83800  -17.46800 3.61700   1.000 16.78843 ? 203 LEU   A O   1 
ATOM   1346 C  CB  . LEU   A 1 191 ? 24.93200  -17.13600 2.79800   1.000 15.68361 ? 203 LEU   A CB  1 
ATOM   1347 C  CG  . LEU   A 1 191 ? 25.83900  -16.85500 1.60600   1.000 15.71719 ? 203 LEU   A CG  1 
ATOM   1348 C  CD1 . LEU   A 1 191 ? 26.92700  -17.93500 1.54200   1.000 16.23143 ? 203 LEU   A CD1 1 
ATOM   1349 C  CD2 . LEU   A 1 191 ? 25.02000  -16.82400 0.31200   1.000 16.30544 ? 203 LEU   A CD2 1 
ATOM   1350 N  N   A SER   A 1 192 ? 22.95700  -16.34600 5.21700   0.720 16.58038 ? 204 SER   A N   1 
ATOM   1351 N  N   B SER   A 1 192 ? 22.95800  -16.35800 5.22100   0.280 16.64402 ? 204 SER   A N   1 
ATOM   1352 C  CA  A SER   A 1 192 ? 22.10300  -16.85400 6.28600   0.720 17.74448 ? 204 SER   A CA  1 
ATOM   1353 C  CA  B SER   A 1 192 ? 22.08700  -16.88300 6.27000   0.280 17.76748 ? 204 SER   A CA  1 
ATOM   1354 C  C   A SER   A 1 192 ? 20.68900  -16.28300 6.24900   0.720 17.51686 ? 204 SER   A C   1 
ATOM   1355 C  C   B SER   A 1 192 ? 20.64900  -16.40100 6.11100   0.280 17.29270 ? 204 SER   A C   1 
ATOM   1356 O  O   A SER   A 1 192 ? 19.81500  -16.78300 6.96900   0.720 20.44322 ? 204 SER   A O   1 
ATOM   1357 O  O   B SER   A 1 192 ? 19.71500  -17.07700 6.56000   0.280 19.67219 ? 204 SER   A O   1 
ATOM   1358 C  CB  A SER   A 1 192 ? 22.74100  -16.56900 7.64700   0.720 18.29543 ? 204 SER   A CB  1 
ATOM   1359 C  CB  B SER   A 1 192 ? 22.61900  -16.49100 7.64700   0.280 18.45661 ? 204 SER   A CB  1 
ATOM   1360 O  OG  A SER   A 1 192 ? 22.60600  -15.20200 8.00200   0.720 21.03088 ? 204 SER   A OG  1 
ATOM   1361 O  OG  B SER   A 1 192 ? 23.88400  -17.07400 7.89200   0.280 15.54836 ? 204 SER   A OG  1 
ATOM   1362 N  N   A ARG   A 1 193 ? 20.44000  -15.24000 5.45600   0.720 17.07750 ? 205 ARG   A N   1 
ATOM   1363 N  N   B ARG   A 1 193 ? 20.45000  -15.24300 5.48800   0.280 17.31037 ? 205 ARG   A N   1 
ATOM   1364 C  CA  A ARG   A 1 193 ? 19.10300  -14.67700 5.32900   0.720 17.17398 ? 205 ARG   A CA  1 
ATOM   1365 C  CA  B ARG   A 1 193 ? 19.11900  -14.67500 5.32100   0.280 17.43205 ? 205 ARG   A CA  1 
ATOM   1366 C  C   A ARG   A 1 193 ? 18.41600  -15.35000 4.15100   0.720 21.06710 ? 205 ARG   A C   1 
ATOM   1367 C  C   B ARG   A 1 193 ? 18.43400  -15.36800 4.15000   0.280 21.08957 ? 205 ARG   A C   1 
ATOM   1368 O  O   A ARG   A 1 193 ? 18.78200  -15.11600 2.99600   0.720 19.46200 ? 205 ARG   A O   1 
ATOM   1369 O  O   B ARG   A 1 193 ? 18.81100  -15.16200 2.99200   0.280 19.48987 ? 205 ARG   A O   1 
ATOM   1370 C  CB  A ARG   A 1 193 ? 19.19900  -13.17500 5.10100   0.720 20.56470 ? 205 ARG   A CB  1 
ATOM   1371 C  CB  B ARG   A 1 193 ? 19.25500  -13.17800 5.06800   0.280 20.61166 ? 205 ARG   A CB  1 
ATOM   1372 C  CG  A ARG   A 1 193 ? 19.19100  -12.38400 6.37100   0.720 23.58014 ? 205 ARG   A CG  1 
ATOM   1373 C  CG  B ARG   A 1 193 ? 17.94800  -12.44700 4.89800   0.280 21.61373 ? 205 ARG   A CG  1 
ATOM   1374 C  CD  A ARG   A 1 193 ? 19.21600  -10.90400 6.07100   0.720 21.75686 ? 205 ARG   A CD  1 
ATOM   1375 C  CD  B ARG   A 1 193 ? 18.21900  -10.97800 4.73000   0.280 23.19481 ? 205 ARG   A CD  1 
ATOM   1376 N  NE  A ARG   A 1 193 ? 17.88300  -10.35800 5.86300   0.720 21.87000 ? 205 ARG   A NE  1 
ATOM   1377 N  NE  B ARG   A 1 193 ? 17.01200  -10.17700 4.58100   0.280 28.31733 ? 205 ARG   A NE  1 
ATOM   1378 C  CZ  A ARG   A 1 193 ? 17.64800  -9.10000  5.50200   0.720 29.17221 ? 205 ARG   A CZ  1 
ATOM   1379 C  CZ  B ARG   A 1 193 ? 16.98800  -8.85100  4.61000   0.280 28.30343 ? 205 ARG   A CZ  1 
ATOM   1380 N  NH1 A ARG   A 1 193 ? 18.63800  -8.25000  5.27700   0.720 28.20960 ? 205 ARG   A NH1 1 
ATOM   1381 N  NH1 B ARG   A 1 193 ? 18.08600  -8.14400  4.82900   0.280 28.76412 ? 205 ARG   A NH1 1 
ATOM   1382 N  NH2 A ARG   A 1 193 ? 16.38900  -8.68100  5.37600   0.720 28.35336 ? 205 ARG   A NH2 1 
ATOM   1383 N  NH2 B ARG   A 1 193 ? 15.83400  -8.22000  4.41800   0.280 28.99582 ? 205 ARG   A NH2 1 
ATOM   1384 N  N   . THR   A 1 194 ? 17.42800  -16.19500 4.44400   1.000 20.91978 ? 206 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 194 ? 16.75400  -16.99000 3.42800   1.000 23.97935 ? 206 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 194 ? 15.34600  -16.50700 3.12500   1.000 25.18103 ? 206 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 194 ? 14.67600  -17.09500 2.26800   1.000 30.28171 ? 206 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 194 ? 16.73300  -18.46700 3.83900   1.000 32.26293 ? 206 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 194 ? 15.83100  -18.63800 4.93500   1.000 32.26479 ? 206 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 194 ? 18.11400  -18.88000 4.29200   1.000 31.48282 ? 206 THR   A CG2 1 
ATOM   1391 N  N   . SER   A 1 195 ? 14.87400  -15.47000 3.80400   1.000 23.85359 ? 207 SER   A N   1 
ATOM   1392 C  CA  . SER   A 1 195 ? 13.58700  -14.86700 3.50600   1.000 28.02925 ? 207 SER   A CA  1 
ATOM   1393 C  C   . SER   A 1 195 ? 13.79800  -13.37300 3.32300   1.000 24.29139 ? 207 SER   A C   1 
ATOM   1394 O  O   . SER   A 1 195 ? 14.77100  -12.80300 3.82100   1.000 25.17400 ? 207 SER   A O   1 
ATOM   1395 C  CB  . SER   A 1 195 ? 12.56700  -15.12600 4.62300   1.000 32.18203 ? 207 SER   A CB  1 
ATOM   1396 O  OG  . SER   A 1 195 ? 12.94500  -14.46300 5.81600   1.000 39.51324 ? 207 SER   A OG  1 
ATOM   1397 N  N   . ALA   A 1 196 ? 12.86900  -12.73600 2.60900   1.000 25.85905 ? 208 ALA   A N   1 
ATOM   1398 C  CA  . ALA   A 1 196 ? 13.07500  -11.33700 2.24300   1.000 23.50424 ? 208 ALA   A CA  1 
ATOM   1399 C  C   . ALA   A 1 196 ? 12.94400  -10.40100 3.43400   1.000 25.38627 ? 208 ALA   A C   1 
ATOM   1400 O  O   . ALA   A 1 196 ? 13.60100  -9.35600  3.47300   1.000 24.70630 ? 208 ALA   A O   1 
ATOM   1401 C  CB  . ALA   A 1 196 ? 12.09500  -10.92900 1.14000   1.000 25.20126 ? 208 ALA   A CB  1 
ATOM   1402 N  N   . GLY   A 1 197 ? 12.09600  -10.73800 4.40100   1.000 26.62684 ? 209 GLY   A N   1 
ATOM   1403 C  CA  . GLY   A 1 197 ? 11.80900  -9.77900  5.45400   1.000 37.37600 ? 209 GLY   A CA  1 
ATOM   1404 C  C   . GLY   A 1 197 ? 11.02600  -8.59600  4.91000   1.000 37.45438 ? 209 GLY   A C   1 
ATOM   1405 O  O   . GLY   A 1 197 ? 10.13500  -8.74200  4.06300   1.000 34.29113 ? 209 GLY   A O   1 
ATOM   1406 N  N   . ASN   A 1 198 ? 11.36200  -7.40200  5.39800   1.000 41.01374 ? 210 ASN   A N   1 
ATOM   1407 C  CA  . ASN   A 1 198 ? 10.66600  -6.18900  4.98700   1.000 39.38946 ? 210 ASN   A CA  1 
ATOM   1408 C  C   . ASN   A 1 198 ? 11.26400  -5.65300  3.69400   1.000 36.63456 ? 210 ASN   A C   1 
ATOM   1409 O  O   . ASN   A 1 198 ? 12.46900  -5.39200  3.62000   1.000 36.61289 ? 210 ASN   A O   1 
ATOM   1410 C  CB  . ASN   A 1 198 ? 10.75800  -5.11800  6.07600   1.000 53.14150 ? 210 ASN   A CB  1 
ATOM   1411 C  CG  . ASN   A 1 198 ? 10.15700  -3.78300  5.64000   1.000 53.75110 ? 210 ASN   A CG  1 
ATOM   1412 O  OD1 . ASN   A 1 198 ? 10.79000  -2.99700  4.92700   1.000 49.75003 ? 210 ASN   A OD1 1 
ATOM   1413 N  ND2 . ASN   A 1 198 ? 8.92800   -3.52200  6.07500   1.000 54.24356 ? 210 ASN   A ND2 1 
ATOM   1414 N  N   . VAL   A 1 199 ? 10.40800  -5.46400  2.68800   1.000 28.51895 ? 211 VAL   A N   1 
ATOM   1415 C  CA  . VAL   A 1 199 ? 10.80800  -5.01100  1.36100   1.000 22.64220 ? 211 VAL   A CA  1 
ATOM   1416 C  C   . VAL   A 1 199 ? 9.80300   -3.96500  0.88600   1.000 22.68368 ? 211 VAL   A C   1 
ATOM   1417 O  O   . VAL   A 1 199 ? 9.45100   -3.90900  -0.30000  1.000 20.48426 ? 211 VAL   A O   1 
ATOM   1418 C  CB  . VAL   A 1 199 ? 10.87800  -6.20900  0.39100   1.000 22.84362 ? 211 VAL   A CB  1 
ATOM   1419 C  CG1 . VAL   A 1 199 ? 12.16700  -7.00100  0.60000   1.000 26.01915 ? 211 VAL   A CG1 1 
ATOM   1420 C  CG2 . VAL   A 1 199 ? 9.64700   -7.10300  0.54800   1.000 25.24486 ? 211 VAL   A CG2 1 
ATOM   1421 N  N   . ALA   A 1 200 ? 9.35100   -3.10800  1.80800   1.000 23.70482 ? 212 ALA   A N   1 
ATOM   1422 C  CA  . ALA   A 1 200 ? 8.23200   -2.21300  1.51300   1.000 25.90391 ? 212 ALA   A CA  1 
ATOM   1423 C  C   . ALA   A 1 200 ? 8.53300   -1.25000  0.37000   1.000 20.17906 ? 212 ALA   A C   1 
ATOM   1424 O  O   . ALA   A 1 200 ? 7.62000   -0.85300  -0.36500  1.000 23.28757 ? 212 ALA   A O   1 
ATOM   1425 C  CB  . ALA   A 1 200 ? 7.83200   -1.43800  2.76700   1.000 28.52479 ? 212 ALA   A CB  1 
ATOM   1426 N  N   . ASP   A 1 201 ? 9.79500   -0.86400  0.19600   1.000 18.43786 ? 213 ASP   A N   1 
ATOM   1427 C  CA  . ASP   A 1 201 ? 10.17300  0.10200   -0.82400  1.000 18.39043 ? 213 ASP   A CA  1 
ATOM   1428 C  C   . ASP   A 1 201 ? 10.91500  -0.53300  -1.99400  1.000 15.38091 ? 213 ASP   A C   1 
ATOM   1429 O  O   . ASP   A 1 201 ? 11.48800  0.19000   -2.81300  1.000 16.78437 ? 213 ASP   A O   1 
ATOM   1430 C  CB  . ASP   A 1 201 ? 10.98000  1.24900   -0.20500  1.000 18.05498 ? 213 ASP   A CB  1 
ATOM   1431 C  CG  . ASP   A 1 201 ? 10.19900  1.99100   0.86500   1.000 19.49984 ? 213 ASP   A CG  1 
ATOM   1432 O  OD1 . ASP   A 1 201 ? 8.97100   2.15200   0.69500   1.000 26.00702 ? 213 ASP   A OD1 1 
ATOM   1433 O  OD2 . ASP   A 1 201 ? 10.80700  2.41200   1.86900   1.000 19.81917 ? 213 ASP   A OD2 1 
ATOM   1434 N  N   . ALA   A 1 202 ? 10.89200  -1.86400  -2.10300  1.000 16.50043 ? 214 ALA   A N   1 
ATOM   1435 C  CA  . ALA   A 1 202 ? 11.67000  -2.56600  -3.10700  1.000 14.31335 ? 214 ALA   A CA  1 
ATOM   1436 C  C   . ALA   A 1 202 ? 10.94800  -2.59700  -4.44900  1.000 15.45481 ? 214 ALA   A C   1 
ATOM   1437 O  O   . ALA   A 1 202 ? 9.72700   -2.42600  -4.54700  1.000 20.15502 ? 214 ALA   A O   1 
ATOM   1438 C  CB  . ALA   A 1 202 ? 11.93000  -3.99500  -2.65100  1.000 15.87081 ? 214 ALA   A CB  1 
ATOM   1439 N  N   . ASP   A 1 203 ? 11.72800  -2.81400  -5.49700  1.000 14.50230 ? 215 ASP   A N   1 
ATOM   1440 C  CA  . ASP   A 1 203 ? 11.20600  -3.14200  -6.82200  1.000 15.95324 ? 215 ASP   A CA  1 
ATOM   1441 C  C   . ASP   A 1 203 ? 11.53400  -4.62100  -7.02600  1.000 14.04859 ? 215 ASP   A C   1 
ATOM   1442 O  O   . ASP   A 1 203 ? 12.59500  -4.98100  -7.53500  1.000 14.25304 ? 215 ASP   A O   1 
ATOM   1443 C  CB  . ASP   A 1 203 ? 11.83400  -2.24100  -7.88400  1.000 16.03703 ? 215 ASP   A CB  1 
ATOM   1444 C  CG  . ASP   A 1 203 ? 11.15300  -2.36700  -9.24600  1.000 17.69174 ? 215 ASP   A CG  1 
ATOM   1445 O  OD1 . ASP   A 1 203 ? 10.74000  -3.48600  -9.59800  1.000 17.98085 ? 215 ASP   A OD1 1 
ATOM   1446 O  OD2 . ASP   A 1 203 ? 11.03600  -1.33900  -9.95800  1.000 24.09087 ? 215 ASP   A OD2 1 
ATOM   1447 N  N   . LEU   A 1 204 ? 10.62000  -5.48200  -6.57100  1.000 16.68492 ? 216 LEU   A N   1 
ATOM   1448 C  CA  . LEU   A 1 204 ? 10.83700  -6.92100  -6.69000  1.000 14.80613 ? 216 LEU   A CA  1 
ATOM   1449 C  C   . LEU   A 1 204 ? 10.96200  -7.35600  -8.13900  1.000 15.86503 ? 216 LEU   A C   1 
ATOM   1450 O  O   . LEU   A 1 204 ? 11.72800  -8.27900  -8.45000  1.000 15.36784 ? 216 LEU   A O   1 
ATOM   1451 C  CB  . LEU   A 1 204 ? 9.69600   -7.68200  -6.01800  1.000 17.91744 ? 216 LEU   A CB  1 
ATOM   1452 C  CG  . LEU   A 1 204 ? 9.60600   -7.53400  -4.49600  1.000 18.57667 ? 216 LEU   A CG  1 
ATOM   1453 C  CD1 . LEU   A 1 204 ? 8.30800   -8.13400  -4.00800  1.000 24.75830 ? 216 LEU   A CD1 1 
ATOM   1454 C  CD2 . LEU   A 1 204 ? 10.79900  -8.20100  -3.83000  1.000 20.29102 ? 216 LEU   A CD2 1 
ATOM   1455 N  N   . ALA   A 1 205 ? 10.22700  -6.70000  -9.03500  1.000 16.23514 ? 217 ALA   A N   1 
ATOM   1456 C  CA  . ALA   A 1 205 ? 10.24300  -7.09200  -10.43800 1.000 14.88129 ? 217 ALA   A CA  1 
ATOM   1457 C  C   . ALA   A 1 205 ? 11.58900  -6.82600  -11.08700 1.000 15.04972 ? 217 ALA   A C   1 
ATOM   1458 O  O   . ALA   A 1 205 ? 12.00700  -7.58300  -11.96500 1.000 17.00941 ? 217 ALA   A O   1 
ATOM   1459 C  CB  . ALA   A 1 205 ? 9.12500   -6.37400  -11.19100 1.000 19.11460 ? 217 ALA   A CB  1 
ATOM   1460 N  N   . GLU   A 1 206 ? 12.27200  -5.75800  -10.67900 1.000 14.71139 ? 218 GLU   A N   1 
ATOM   1461 C  CA  . GLU   A 1 206 ? 13.54600  -5.37900  -11.26800 1.000 14.08272 ? 218 GLU   A CA  1 
ATOM   1462 C  C   . GLU   A 1 206 ? 14.75700  -5.89300  -10.51500 1.000 12.68296 ? 218 GLU   A C   1 
ATOM   1463 O  O   . GLU   A 1 206 ? 15.84700  -5.91100  -11.08400 1.000 14.53274 ? 218 GLU   A O   1 
ATOM   1464 C  CB  . GLU   A 1 206 ? 13.62600  -3.85000  -11.34300 1.000 15.35602 ? 218 GLU   A CB  1 
ATOM   1465 C  CG  . GLU   A 1 206 ? 12.69400  -3.25400  -12.39500 1.000 20.74461 ? 218 GLU   A CG  1 
ATOM   1466 C  CD  . GLU   A 1 206 ? 12.93400  -3.82700  -13.78600 1.000 23.05599 ? 218 GLU   A CD  1 
ATOM   1467 O  OE1 . GLU   A 1 206 ? 14.08500  -4.23200  -14.08400 1.000 19.99550 ? 218 GLU   A OE1 1 
ATOM   1468 O  OE2 . GLU   A 1 206 ? 11.96200  -3.93500  -14.57000 1.000 26.21012 ? 218 GLU   A OE2 1 
ATOM   1469 N  N   . TRP   A 1 207 ? 14.57900  -6.32800  -9.27100  1.000 13.37695 ? 219 TRP   A N   1 
ATOM   1470 C  CA  . TRP   A 1 207 ? 15.72100  -6.66300  -8.42000  1.000 14.58243 ? 219 TRP   A CA  1 
ATOM   1471 C  C   . TRP   A 1 207 ? 16.63500  -7.71400  -9.04600  1.000 13.75541 ? 219 TRP   A C   1 
ATOM   1472 O  O   . TRP   A 1 207 ? 17.85900  -7.50000  -9.06900  1.000 13.50719 ? 219 TRP   A O   1 
ATOM   1473 C  CB  . TRP   A 1 207 ? 15.19800  -7.01900  -7.02700  1.000 12.62567 ? 219 TRP   A CB  1 
ATOM   1474 C  CG  . TRP   A 1 207 ? 16.15200  -7.08300  -5.87400  1.000 11.39054 ? 219 TRP   A CG  1 
ATOM   1475 C  CD1 . TRP   A 1 207 ? 17.50400  -7.28000  -5.90400  1.000 11.40433 ? 219 TRP   A CD1 1 
ATOM   1476 C  CD2 . TRP   A 1 207 ? 15.78900  -6.95900  -4.49400  1.000 12.08540 ? 219 TRP   A CD2 1 
ATOM   1477 N  NE1 . TRP   A 1 207 ? 18.00700  -7.28200  -4.60800  1.000 12.41528 ? 219 TRP   A NE1 1 
ATOM   1478 C  CE2 . TRP   A 1 207 ? 16.97100  -7.07800  -3.73000  1.000 11.28829 ? 219 TRP   A CE2 1 
ATOM   1479 C  CE3 . TRP   A 1 207 ? 14.57500  -6.73400  -3.83400  1.000 14.46814 ? 219 TRP   A CE3 1 
ATOM   1480 C  CZ2 . TRP   A 1 207 ? 16.96200  -7.01800  -2.32000  1.000 12.18687 ? 219 TRP   A CZ2 1 
ATOM   1481 C  CZ3 . TRP   A 1 207 ? 14.56400  -6.65800  -2.45200  1.000 13.13007 ? 219 TRP   A CZ3 1 
ATOM   1482 C  CH2 . TRP   A 1 207 ? 15.74500  -6.79700  -1.71000  1.000 12.69272 ? 219 TRP   A CH2 1 
ATOM   1483 N  N   . PRO   A 1 208 ? 16.13900  -8.85100  -9.57400  1.000 13.76193 ? 220 PRO   A N   1 
ATOM   1484 C  CA  . PRO   A 1 208 ? 17.06300  -9.80600  -10.22400 1.000 13.42647 ? 220 PRO   A CA  1 
ATOM   1485 C  C   . PRO   A 1 208 ? 17.82200  -9.21500  -11.40500 1.000 14.28993 ? 220 PRO   A C   1 
ATOM   1486 O  O   . PRO   A 1 208 ? 19.01000  -9.51100  -11.58800 1.000 15.05580 ? 220 PRO   A O   1 
ATOM   1487 C  CB  . PRO   A 1 208 ? 16.14700  -10.97600 -10.62600 1.000 14.85357 ? 220 PRO   A CB  1 
ATOM   1488 C  CG  . PRO   A 1 208 ? 14.97900  -10.88600 -9.65100  1.000 15.01062 ? 220 PRO   A CG  1 
ATOM   1489 C  CD  . PRO   A 1 208 ? 14.77200  -9.39600  -9.47600  1.000 15.25258 ? 220 PRO   A CD  1 
ATOM   1490 N  N   . THR   A 1 209 ? 17.16700  -8.37700  -12.21700 1.000 14.91155 ? 221 THR   A N   1 
ATOM   1491 C  CA  . THR   A 1 209 ? 17.87000  -7.74500  -13.32300 1.000 14.80640 ? 221 THR   A CA  1 
ATOM   1492 C  C   . THR   A 1 209 ? 18.96100  -6.81500  -12.81200 1.000 15.64036 ? 221 THR   A C   1 
ATOM   1493 O  O   . THR   A 1 209 ? 20.06900  -6.79300  -13.35800 1.000 14.87322 ? 221 THR   A O   1 
ATOM   1494 C  CB  . THR   A 1 209 ? 16.87500  -6.98500  -14.19000 1.000 14.79175 ? 221 THR   A CB  1 
ATOM   1495 O  OG1 . THR   A 1 209 ? 15.93200  -7.92200  -14.72900 1.000 17.30116 ? 221 THR   A OG1 1 
ATOM   1496 C  CG2 . THR   A 1 209 ? 17.59200  -6.26400  -15.33800 1.000 17.05151 ? 221 THR   A CG2 1 
ATOM   1497 N  N   . SER   A 1 210 ? 18.67100  -6.06300  -11.74400 1.000 14.06520 ? 222 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 210 ? 19.68200  -5.17500  -11.18300 1.000 13.36852 ? 222 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 210 ? 20.87500  -5.96500  -10.64500 1.000 12.88405 ? 222 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 210 ? 22.03200  -5.56100  -10.83300 1.000 14.12847 ? 222 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 210 ? 19.04400  -4.29500  -10.10700 1.000 14.16101 ? 222 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 210 ? 17.97100  -3.54800  -10.66600 1.000 13.69234 ? 222 SER   A OG  1 
ATOM   1503 N  N   . ILE   A 1 211 ? 20.61600  -7.12200  -10.02200 1.000 13.23475 ? 223 ILE   A N   1 
ATOM   1504 C  CA  . ILE   A 1 211 ? 21.69900  -7.97800  -9.55200  1.000 14.48422 ? 223 ILE   A CA  1 
ATOM   1505 C  C   . ILE   A 1 211 ? 22.54200  -8.47200  -10.72400 1.000 15.22090 ? 223 ILE   A C   1 
ATOM   1506 O  O   . ILE   A 1 211 ? 23.77700  -8.51800  -10.63900 1.000 14.32965 ? 223 ILE   A O   1 
ATOM   1507 C  CB  . ILE   A 1 211 ? 21.13700  -9.12600  -8.69500  1.000 12.06793 ? 223 ILE   A CB  1 
ATOM   1508 C  CG1 . ILE   A 1 211 ? 20.73500  -8.57400  -7.33100  1.000 15.10543 ? 223 ILE   A CG1 1 
ATOM   1509 C  CG2 . ILE   A 1 211 ? 22.16100  -10.26400 -8.58200  1.000 15.26880 ? 223 ILE   A CG2 1 
ATOM   1510 C  CD1 . ILE   A 1 211 ? 19.97400  -9.58100  -6.47300  1.000 17.82087 ? 223 ILE   A CD1 1 
ATOM   1511 N  N   A GLU   A 1 212 ? 21.90300  -8.82300  -11.84100 0.506 15.32955 ? 224 GLU   A N   1 
ATOM   1512 N  N   B GLU   A 1 212 ? 21.88600  -8.84300  -11.83200 0.494 15.36208 ? 224 GLU   A N   1 
ATOM   1513 C  CA  A GLU   A 1 212 ? 22.68600  -9.27700  -12.98500 0.506 14.89534 ? 224 GLU   A CA  1 
ATOM   1514 C  CA  B GLU   A 1 212 ? 22.60600  -9.25300  -13.03400 0.494 14.92757 ? 224 GLU   A CA  1 
ATOM   1515 C  C   A GLU   A 1 212 ? 23.57200  -8.16300  -13.53200 0.506 15.47297 ? 224 GLU   A C   1 
ATOM   1516 C  C   B GLU   A 1 212 ? 23.56900  -8.16600  -13.48700 0.494 15.46786 ? 224 GLU   A C   1 
ATOM   1517 O  O   A GLU   A 1 212 ? 24.68200  -8.43600  -14.00400 0.506 17.05370 ? 224 GLU   A O   1 
ATOM   1518 O  O   B GLU   A 1 212 ? 24.71300  -8.45500  -13.86200 0.494 17.01494 ? 224 GLU   A O   1 
ATOM   1519 C  CB  A GLU   A 1 212 ? 21.78400  -9.85500  -14.07100 0.506 19.50722 ? 224 GLU   A CB  1 
ATOM   1520 C  CB  B GLU   A 1 212 ? 21.62200  -9.56000  -14.16400 0.494 18.64630 ? 224 GLU   A CB  1 
ATOM   1521 C  CG  A GLU   A 1 212 ? 22.55100  -10.47200 -15.24100 0.506 16.26580 ? 224 GLU   A CG  1 
ATOM   1522 C  CG  B GLU   A 1 212 ? 20.82400  -10.83500 -14.00400 0.494 16.92773 ? 224 GLU   A CG  1 
ATOM   1523 C  CD  A GLU   A 1 212 ? 23.73400  -11.32900 -14.80400 0.506 24.52716 ? 224 GLU   A CD  1 
ATOM   1524 C  CD  B GLU   A 1 212 ? 19.81700  -11.04600 -15.13100 0.494 23.22772 ? 224 GLU   A CD  1 
ATOM   1525 O  OE1 A GLU   A 1 212 ? 23.54700  -12.26900 -13.99800 0.506 21.79308 ? 224 GLU   A OE1 1 
ATOM   1526 O  OE1 B GLU   A 1 212 ? 19.58900  -10.11100 -15.93700 0.494 23.15344 ? 224 GLU   A OE1 1 
ATOM   1527 O  OE2 A GLU   A 1 212 ? 24.85800  -11.06900 -15.28800 0.506 24.53663 ? 224 GLU   A OE2 1 
ATOM   1528 O  OE2 B GLU   A 1 212 ? 19.25300  -12.15600 -15.20300 0.494 26.75259 ? 224 GLU   A OE2 1 
ATOM   1529 N  N   . ARG   A 1 213 ? 23.12500  -6.90300  -13.45100 1.000 15.43395 ? 225 ARG   A N   1 
ATOM   1530 C  CA  . ARG   A 1 213 ? 23.99900  -5.80400  -13.84600 1.000 12.77551 ? 225 ARG   A CA  1 
ATOM   1531 C  C   . ARG   A 1 213 ? 25.22100  -5.72500  -12.94200 1.000 14.88898 ? 225 ARG   A C   1 
ATOM   1532 O  O   . ARG   A 1 213 ? 26.32900  -5.42300  -13.40500 1.000 16.07116 ? 225 ARG   A O   1 
ATOM   1533 C  CB  . ARG   A 1 213 ? 23.25700  -4.46100  -13.83100 1.000 14.89320 ? 225 ARG   A CB  1 
ATOM   1534 C  CG  . ARG   A 1 213 ? 22.16300  -4.32900  -14.88200 1.000 14.82891 ? 225 ARG   A CG  1 
ATOM   1535 C  CD  . ARG   A 1 213 ? 21.79800  -2.86600  -15.14600 1.000 13.23683 ? 225 ARG   A CD  1 
ATOM   1536 N  NE  . ARG   A 1 213 ? 20.63500  -2.75800  -16.01700 1.000 14.92539 ? 225 ARG   A NE  1 
ATOM   1537 C  CZ  . ARG   A 1 213 ? 19.37500  -2.85100  -15.61400 1.000 18.67821 ? 225 ARG   A CZ  1 
ATOM   1538 N  NH1 . ARG   A 1 213 ? 19.05800  -2.91400  -14.33100 1.000 16.05810 ? 225 ARG   A NH1 1 
ATOM   1539 N  NH2 . ARG   A 1 213 ? 18.40300  -2.90700  -16.52200 1.000 19.85525 ? 225 ARG   A NH2 1 
ATOM   1540 N  N   . ILE   A 1 214 ? 25.04000  -5.97500  -11.64200 1.000 12.79206 ? 226 ILE   A N   1 
ATOM   1541 C  CA  . ILE   A 1 214 ? 26.18600  -5.98600  -10.72900 1.000 13.94538 ? 226 ILE   A CA  1 
ATOM   1542 C  C   . ILE   A 1 214 ? 27.17300  -7.07600  -11.13200 1.000 14.23733 ? 226 ILE   A C   1 
ATOM   1543 O  O   . ILE   A 1 214 ? 28.38000  -6.83200  -11.23500 1.000 14.63913 ? 226 ILE   A O   1 
ATOM   1544 C  CB  . ILE   A 1 214 ? 25.72900  -6.16300  -9.26900  1.000 12.63797 ? 226 ILE   A CB  1 
ATOM   1545 C  CG1 . ILE   A 1 214 ? 24.78900  -5.02700  -8.85000  1.000 13.75046 ? 226 ILE   A CG1 1 
ATOM   1546 C  CG2 . ILE   A 1 214 ? 26.93400  -6.19400  -8.34000  1.000 13.30839 ? 226 ILE   A CG2 1 
ATOM   1547 C  CD1 . ILE   A 1 214 ? 24.11300  -5.27500  -7.50600  1.000 14.64926 ? 226 ILE   A CD1 1 
ATOM   1548 N  N   . GLN   A 1 215 ? 26.67400  -8.29800  -11.35400 1.000 14.80836 ? 227 GLN   A N   1 
ATOM   1549 C  CA  . GLN   A 1 215 ? 27.53700  -9.40000  -11.78600 1.000 14.33390 ? 227 GLN   A CA  1 
ATOM   1550 C  C   . GLN   A 1 215 ? 28.28200  -9.05600  -13.07100 1.000 16.22835 ? 227 GLN   A C   1 
ATOM   1551 O  O   . GLN   A 1 215 ? 29.49300  -9.31300  -13.18400 1.000 16.75191 ? 227 GLN   A O   1 
ATOM   1552 C  CB  . GLN   A 1 215 ? 26.69300  -10.66600 -11.96300 1.000 16.67058 ? 227 GLN   A CB  1 
ATOM   1553 C  CG  . GLN   A 1 215 ? 27.39900  -11.85600 -12.68600 1.000 16.17680 ? 227 GLN   A CG  1 
ATOM   1554 C  CD  . GLN   A 1 215 ? 28.56400  -12.42900 -11.89600 1.000 21.21730 ? 227 GLN   A CD  1 
ATOM   1555 O  OE1 . GLN   A 1 215 ? 28.42100  -12.76200 -10.71700 1.000 21.22184 ? 227 GLN   A OE1 1 
ATOM   1556 N  NE2 . GLN   A 1 215 ? 29.72500  -12.55000 -12.54100 1.000 20.31740 ? 227 GLN   A NE2 1 
ATOM   1557 N  N   . GLN   A 1 216 ? 27.57600  -8.46500  -14.04100 1.000 15.74329 ? 228 GLN   A N   1 
ATOM   1558 C  CA  . GLN   A 1 216 ? 28.17900  -8.14400  -15.33000 1.000 18.49788 ? 228 GLN   A CA  1 
ATOM   1559 C  C   . GLN   A 1 216 ? 29.28800  -7.11500  -15.17800 1.000 18.01431 ? 228 GLN   A C   1 
ATOM   1560 O  O   . GLN   A 1 216 ? 30.30400  -7.16900  -15.88200 1.000 19.63967 ? 228 GLN   A O   1 
ATOM   1561 C  CB  . GLN   A 1 216 ? 27.09800  -7.59500  -16.26200 1.000 19.74760 ? 228 GLN   A CB  1 
ATOM   1562 C  CG  . GLN   A 1 216 ? 26.17900  -8.62200  -16.88900 1.000 32.12843 ? 228 GLN   A CG  1 
ATOM   1563 C  CD  . GLN   A 1 216 ? 26.93400  -9.70500  -17.62100 1.000 49.54007 ? 228 GLN   A CD  1 
ATOM   1564 O  OE1 . GLN   A 1 216 ? 27.05200  -10.83400 -17.13900 1.000 47.40513 ? 228 GLN   A OE1 1 
ATOM   1565 N  NE2 . GLN   A 1 216 ? 27.47200  -9.36000  -18.78800 1.000 46.48552 ? 228 GLN   A NE2 1 
ATOM   1566 N  N   . HIS   A 1 217 ? 29.09500  -6.17000  -14.26300 1.000 15.87051 ? 229 HIS   A N   1 
ATOM   1567 C  CA  . HIS   A 1 217 ? 30.02400  -5.06400  -14.09600 1.000 15.69381 ? 229 HIS   A CA  1 
ATOM   1568 C  C   . HIS   A 1 217 ? 31.20300  -5.40700  -13.20200 1.000 16.78887 ? 229 HIS   A C   1 
ATOM   1569 O  O   . HIS   A 1 217 ? 32.29400  -4.87300  -13.42400 1.000 17.10898 ? 229 HIS   A O   1 
ATOM   1570 C  CB  . HIS   A 1 217 ? 29.30800  -3.81800  -13.55100 1.000 16.97170 ? 229 HIS   A CB  1 
ATOM   1571 C  CG  . HIS   A 1 217 ? 29.86400  -2.53000  -14.07400 1.000 20.01487 ? 229 HIS   A CG  1 
ATOM   1572 N  ND1 . HIS   A 1 217 ? 29.54900  -2.04100  -15.32400 1.000 27.86862 ? 229 HIS   A ND1 1 
ATOM   1573 C  CD2 . HIS   A 1 217 ? 30.70700  -1.62500  -13.51800 1.000 23.98072 ? 229 HIS   A CD2 1 
ATOM   1574 C  CE1 . HIS   A 1 217 ? 30.17600  -0.89400  -15.51700 1.000 30.71468 ? 229 HIS   A CE1 1 
ATOM   1575 N  NE2 . HIS   A 1 217 ? 30.89400  -0.62400  -14.44200 1.000 26.55197 ? 229 HIS   A NE2 1 
ATOM   1576 N  N   . TYR   A 1 218 ? 31.02600  -6.30300  -12.21800 1.000 14.47668 ? 230 TYR   A N   1 
ATOM   1577 C  CA  . TYR   A 1 218 ? 32.08300  -6.62300  -11.26300 1.000 15.06038 ? 230 TYR   A CA  1 
ATOM   1578 C  C   . TYR   A 1 218 ? 32.34900  -8.12200  -11.17700 1.000 16.80145 ? 230 TYR   A C   1 
ATOM   1579 O  O   . TYR   A 1 218 ? 32.40100  -8.68700  -10.08100 1.000 16.16123 ? 230 TYR   A O   1 
ATOM   1580 C  CB  . TYR   A 1 218 ? 31.76200  -6.03700  -9.88600  1.000 14.18777 ? 230 TYR   A CB  1 
ATOM   1581 C  CG  . TYR   A 1 218 ? 31.56300  -4.53700  -9.94600  1.000 16.15548 ? 230 TYR   A CG  1 
ATOM   1582 C  CD1 . TYR   A 1 218 ? 32.62600  -3.69100  -10.23400 1.000 15.17429 ? 230 TYR   A CD1 1 
ATOM   1583 C  CD2 . TYR   A 1 218 ? 30.30900  -3.96800  -9.75100  1.000 17.45096 ? 230 TYR   A CD2 1 
ATOM   1584 C  CE1 . TYR   A 1 218 ? 32.46000  -2.32400  -10.32000 1.000 15.57077 ? 230 TYR   A CE1 1 
ATOM   1585 C  CE2 . TYR   A 1 218 ? 30.13500  -2.58600  -9.81900  1.000 15.21880 ? 230 TYR   A CE2 1 
ATOM   1586 C  CZ  . TYR   A 1 218 ? 31.21500  -1.78300  -10.10000 1.000 18.10401 ? 230 TYR   A CZ  1 
ATOM   1587 O  OH  . TYR   A 1 218 ? 31.06500  -0.41900  -10.19200 1.000 19.25961 ? 230 TYR   A OH  1 
ATOM   1588 N  N   . PRO   A 1 219 ? 32.56500  -8.79800  -12.31800 1.000 16.77691 ? 231 PRO   A N   1 
ATOM   1589 C  CA  . PRO   A 1 219 ? 32.77800  -10.25200 -12.27400 1.000 17.80737 ? 231 PRO   A CA  1 
ATOM   1590 C  C   . PRO   A 1 219 ? 34.06600  -10.65300 -11.59000 1.000 15.40296 ? 231 PRO   A C   1 
ATOM   1591 O  O   . PRO   A 1 219 ? 34.19600  -11.81600 -11.19700 1.000 16.28270 ? 231 PRO   A O   1 
ATOM   1592 C  CB  . PRO   A 1 219 ? 32.78900  -10.64200 -13.75500 1.000 17.39918 ? 231 PRO   A CB  1 
ATOM   1593 C  CG  . PRO   A 1 219 ? 33.33300  -9.46200  -14.42300 1.000 15.76966 ? 231 PRO   A CG  1 
ATOM   1594 C  CD  . PRO   A 1 219 ? 32.78200  -8.26600  -13.67600 1.000 16.96332 ? 231 PRO   A CD  1 
ATOM   1595 N  N   . GLU   A 1 220 ? 34.99900  -9.72300  -11.41700 1.000 16.38652 ? 232 GLU   A N   1 
ATOM   1596 C  CA  . GLU   A 1 220 ? 36.27100  -9.97800  -10.76500 1.000 18.31361 ? 232 GLU   A CA  1 
ATOM   1597 C  C   . GLU   A 1 220 ? 36.22800  -9.75800  -9.25400  1.000 18.33310 ? 232 GLU   A C   1 
ATOM   1598 O  O   . GLU   A 1 220 ? 37.25200  -9.93000  -8.58500  1.000 18.26693 ? 232 GLU   A O   1 
ATOM   1599 C  CB  . GLU   A 1 220 ? 37.36500  -9.11400  -11.40700 1.000 20.22987 ? 232 GLU   A CB  1 
ATOM   1600 C  CG  . GLU   A 1 220 ? 37.41400  -7.66000  -10.96000 1.000 19.31375 ? 232 GLU   A CG  1 
ATOM   1601 C  CD  . GLU   A 1 220 ? 36.44000  -6.72600  -11.67700 1.000 24.23347 ? 232 GLU   A CD  1 
ATOM   1602 O  OE1 . GLU   A 1 220 ? 35.38800  -7.16000  -12.18100 1.000 20.87434 ? 232 GLU   A OE1 1 
ATOM   1603 O  OE2 . GLU   A 1 220 ? 36.73600  -5.51000  -11.73800 1.000 26.18307 ? 232 GLU   A OE2 1 
ATOM   1604 N  N   . ALA   A 1 221 ? 35.07800  -9.37900  -8.69000  1.000 17.04349 ? 233 ALA   A N   1 
ATOM   1605 C  CA  . ALA   A 1 221 ? 35.02900  -9.12200  -7.24900  1.000 16.22653 ? 233 ALA   A CA  1 
ATOM   1606 C  C   . ALA   A 1 221 ? 35.40600  -10.36900 -6.45300  1.000 16.84822 ? 233 ALA   A C   1 
ATOM   1607 O  O   . ALA   A 1 221 ? 34.91400  -11.46800 -6.72200  1.000 18.58615 ? 233 ALA   A O   1 
ATOM   1608 C  CB  . ALA   A 1 221 ? 33.62400  -8.66500  -6.85700  1.000 16.48854 ? 233 ALA   A CB  1 
ATOM   1609 N  N   . GLN   A 1 222 ? 36.25900  -10.18800 -5.44400  1.000 17.26923 ? 234 GLN   A N   1 
ATOM   1610 C  CA  . GLN   A 1 222 ? 36.71400  -11.28800 -4.59900  1.000 18.39090 ? 234 GLN   A CA  1 
ATOM   1611 C  C   . GLN   A 1 222 ? 36.06400  -11.29700 -3.23000  1.000 18.04057 ? 234 GLN   A C   1 
ATOM   1612 O  O   . GLN   A 1 222 ? 36.05900  -12.33600 -2.56800  1.000 19.82226 ? 234 GLN   A O   1 
ATOM   1613 C  CB  . GLN   A 1 222 ? 38.22900  -11.19900 -4.37800  1.000 21.44082 ? 234 GLN   A CB  1 
ATOM   1614 C  CG  . GLN   A 1 222 ? 39.05100  -11.33900 -5.64900  1.000 27.63766 ? 234 GLN   A CG  1 
ATOM   1615 C  CD  . GLN   A 1 222 ? 38.80300  -12.65300 -6.34500  1.000 31.74669 ? 234 GLN   A CD  1 
ATOM   1616 O  OE1 . GLN   A 1 222 ? 38.32600  -12.68700 -7.48100  1.000 35.29763 ? 234 GLN   A OE1 1 
ATOM   1617 N  NE2 . GLN   A 1 222 ? 39.11600  -13.74700 -5.66300  1.000 33.20366 ? 234 GLN   A NE2 1 
ATOM   1618 N  N   A PHE   A 1 223 ? 35.62000  -10.13900 -2.76700  0.570 17.91498 ? 235 PHE   A N   1 
ATOM   1619 N  N   B PHE   A 1 223 ? 35.48100  -10.17900 -2.79700  0.430 17.88989 ? 235 PHE   A N   1 
ATOM   1620 C  CA  A PHE   A 1 223 ? 34.91200  -9.99700  -1.51300  0.570 17.61079 ? 235 PHE   A CA  1 
ATOM   1621 C  CA  B PHE   A 1 223 ? 34.93200  -10.04400 -1.45300  0.430 17.63464 ? 235 PHE   A CA  1 
ATOM   1622 C  C   A PHE   A 1 223 ? 33.60900  -9.29200  -1.83100  0.570 14.74615 ? 235 PHE   A C   1 
ATOM   1623 C  C   B PHE   A 1 223 ? 33.68100  -9.19000  -1.55200  0.430 15.75304 ? 235 PHE   A C   1 
ATOM   1624 O  O   A PHE   A 1 223 ? 33.58300  -8.34200  -2.62000  0.570 14.75924 ? 235 PHE   A O   1 
ATOM   1625 O  O   B PHE   A 1 223 ? 33.77700  -8.00700  -1.88600  0.430 14.76686 ? 235 PHE   A O   1 
ATOM   1626 C  CB  A PHE   A 1 223 ? 35.71800  -9.15900  -0.50900  0.570 19.09223 ? 235 PHE   A CB  1 
ATOM   1627 C  CB  B PHE   A 1 223 ? 35.95200  -9.35100  -0.54800  0.430 18.84180 ? 235 PHE   A CB  1 
ATOM   1628 C  CG  A PHE   A 1 223 ? 37.13700  -9.63800  -0.30800  0.570 19.60924 ? 235 PHE   A CG  1 
ATOM   1629 C  CG  B PHE   A 1 223 ? 35.74800  -9.59700  0.92000   0.430 18.87689 ? 235 PHE   A CG  1 
ATOM   1630 C  CD1 A PHE   A 1 223 ? 37.43200  -10.58100 0.66200   0.570 19.60645 ? 235 PHE   A CD1 1 
ATOM   1631 C  CD1 B PHE   A 1 223 ? 36.29900  -10.70900 1.53300   0.430 21.53847 ? 235 PHE   A CD1 1 
ATOM   1632 C  CD2 A PHE   A 1 223 ? 38.17400  -9.13400  -1.08200  0.570 20.31253 ? 235 PHE   A CD2 1 
ATOM   1633 C  CD2 B PHE   A 1 223 ? 35.02400  -8.70200  1.69400   0.430 19.68081 ? 235 PHE   A CD2 1 
ATOM   1634 C  CE1 A PHE   A 1 223 ? 38.73100  -11.01700 0.85300   0.570 23.32608 ? 235 PHE   A CE1 1 
ATOM   1635 C  CE1 B PHE   A 1 223 ? 36.12900  -10.93100 2.88600   0.430 20.50291 ? 235 PHE   A CE1 1 
ATOM   1636 C  CE2 A PHE   A 1 223 ? 39.47400  -9.56800  -0.89600  0.570 20.66474 ? 235 PHE   A CE2 1 
ATOM   1637 C  CE2 B PHE   A 1 223 ? 34.86100  -8.91500  3.04700   0.430 19.68788 ? 235 PHE   A CE2 1 
ATOM   1638 C  CZ  A PHE   A 1 223 ? 39.74900  -10.51300 0.07300   0.570 19.36240 ? 235 PHE   A CZ  1 
ATOM   1639 C  CZ  B PHE   A 1 223 ? 35.41100  -10.03800 3.64400   0.430 18.84596 ? 235 PHE   A CZ  1 
ATOM   1640 N  N   . VAL   A 1 224 ? 32.52400  -9.77700  -1.24700  1.000 14.49892 ? 236 VAL   A N   1 
ATOM   1641 C  CA  . VAL   A 1 224 ? 31.21900  -9.14600  -1.42400  1.000 15.39193 ? 236 VAL   A CA  1 
ATOM   1642 C  C   . VAL   A 1 224 ? 30.63600  -8.91200  -0.04000  1.000 14.20767 ? 236 VAL   A C   1 
ATOM   1643 O  O   . VAL   A 1 224 ? 30.47400  -9.86000  0.73900   1.000 15.64845 ? 236 VAL   A O   1 
ATOM   1644 C  CB  . VAL   A 1 224 ? 30.28500  -10.01200 -2.28600  1.000 16.41275 ? 236 VAL   A CB  1 
ATOM   1645 C  CG1 . VAL   A 1 224 ? 28.93300  -9.33900  -2.43300  1.000 17.62196 ? 236 VAL   A CG1 1 
ATOM   1646 C  CG2 . VAL   A 1 224 ? 30.89200  -10.26300 -3.65700  1.000 17.44630 ? 236 VAL   A CG2 1 
ATOM   1647 N  N   . ILE   A 1 225 ? 30.30300  -7.66600  0.26100   1.000 13.48998 ? 237 ILE   A N   1 
ATOM   1648 C  CA  A ILE   A 1 225 ? 29.83800  -7.25300  1.58500   0.431 14.07500 ? 237 ILE   A CA  1 
ATOM   1649 C  CA  B ILE   A 1 225 ? 29.82900  -7.27400  1.58600   0.569 14.02202 ? 237 ILE   A CA  1 
ATOM   1650 C  C   . ILE   A 1 225 ? 28.34900  -6.94400  1.48600   1.000 12.29630 ? 237 ILE   A C   1 
ATOM   1651 O  O   . ILE   A 1 225 ? 27.97300  -6.00500  0.76200   1.000 13.08830 ? 237 ILE   A O   1 
ATOM   1652 C  CB  A ILE   A 1 225 ? 30.61000  -6.02000  2.08400   0.431 16.28650 ? 237 ILE   A CB  1 
ATOM   1653 C  CB  B ILE   A 1 225 ? 30.60300  -6.07200  2.13200   0.569 16.34281 ? 237 ILE   A CB  1 
ATOM   1654 C  CG1 A ILE   A 1 225 ? 32.10300  -6.13400  1.76100   0.431 16.13867 ? 237 ILE   A CG1 1 
ATOM   1655 C  CG1 B ILE   A 1 225 ? 32.06000  -6.43800  2.32300   0.569 15.58344 ? 237 ILE   A CG1 1 
ATOM   1656 C  CG2 A ILE   A 1 225 ? 30.39000  -5.81300  3.58100   0.431 15.47030 ? 237 ILE   A CG2 1 
ATOM   1657 C  CG2 B ILE   A 1 225 ? 29.98400  -5.58900  3.44200   0.569 14.78040 ? 237 ILE   A CG2 1 
ATOM   1658 C  CD1 A ILE   A 1 225 ? 32.79200  -7.28600  2.44600   0.431 15.18592 ? 237 ILE   A CD1 1 
ATOM   1659 C  CD1 B ILE   A 1 225 ? 32.88600  -5.24300  2.27100   0.569 16.87152 ? 237 ILE   A CD1 1 
ATOM   1660 N  N   . PRO   A 1 226 ? 27.48400  -7.66100  2.19700   1.000 12.84896 ? 238 PRO   A N   1 
ATOM   1661 C  CA  . PRO   A 1 226 ? 26.05800  -7.33400  2.20700   1.000 12.28684 ? 238 PRO   A CA  1 
ATOM   1662 C  C   . PRO   A 1 226 ? 25.81300  -6.16400  3.15200   1.000 13.07059 ? 238 PRO   A C   1 
ATOM   1663 O  O   . PRO   A 1 226 ? 26.66400  -5.80000  3.96600   1.000 13.95086 ? 238 PRO   A O   1 
ATOM   1664 C  CB  . PRO   A 1 226 ? 25.42300  -8.62400  2.75700   1.000 13.71892 ? 238 PRO   A CB  1 
ATOM   1665 C  CG  . PRO   A 1 226 ? 26.45500  -9.12900  3.73700   1.000 13.86991 ? 238 PRO   A CG  1 
ATOM   1666 C  CD  . PRO   A 1 226 ? 27.79200  -8.82500  3.06200   1.000 13.15034 ? 238 PRO   A CD  1 
ATOM   1667 N  N   . GLY   A 1 227 ? 24.61600  -5.58000  3.04000   1.000 12.81305 ? 239 GLY   A N   1 
ATOM   1668 C  CA  . GLY   A 1 227 ? 24.24300  -4.50200  3.94500   1.000 12.82681 ? 239 GLY   A CA  1 
ATOM   1669 C  C   . GLY   A 1 227 ? 24.17400  -4.96100  5.38800   1.000 12.99450 ? 239 GLY   A C   1 
ATOM   1670 O  O   . GLY   A 1 227 ? 24.38200  -4.16700  6.30800   1.000 13.52949 ? 239 GLY   A O   1 
ATOM   1671 N  N   . HIS   A 1 228 ? 23.88100  -6.24900  5.60700   1.000 12.46677 ? 240 HIS   A N   1 
ATOM   1672 C  CA  . HIS   A 1 228 ? 23.76600  -6.81100  6.95000   1.000 12.41496 ? 240 HIS   A CA  1 
ATOM   1673 C  C   . HIS   A 1 228 ? 24.37200  -8.20300  6.95300   1.000 14.04471 ? 240 HIS   A C   1 
ATOM   1674 O  O   . HIS   A 1 228 ? 24.00500  -9.03600  6.12600   1.000 14.42588 ? 240 HIS   A O   1 
ATOM   1675 C  CB  . HIS   A 1 228 ? 22.29800  -6.90800  7.35300   1.000 13.43588 ? 240 HIS   A CB  1 
ATOM   1676 C  CG  . HIS   A 1 228 ? 21.58600  -5.61300  7.24000   1.000 12.89152 ? 240 HIS   A CG  1 
ATOM   1677 N  ND1 . HIS   A 1 228 ? 21.57600  -4.67100  8.24900   1.000 12.60369 ? 240 HIS   A ND1 1 
ATOM   1678 C  CD2 . HIS   A 1 228 ? 20.92500  -5.07100  6.19900   1.000 13.79878 ? 240 HIS   A CD2 1 
ATOM   1679 C  CE1 . HIS   A 1 228 ? 20.91800  -3.60600  7.83500   1.000 12.98672 ? 240 HIS   A CE1 1 
ATOM   1680 N  NE2 . HIS   A 1 228 ? 20.51000  -3.83200  6.60000   1.000 12.95840 ? 240 HIS   A NE2 1 
ATOM   1681 N  N   . GLY   A 1 229 ? 25.28900  -8.44800  7.87300   1.000 13.65746 ? 241 GLY   A N   1 
ATOM   1682 C  CA  . GLY   A 1 229 ? 25.78600  -9.78600  8.09800   1.000 14.56661 ? 241 GLY   A CA  1 
ATOM   1683 C  C   . GLY   A 1 229 ? 27.09200  -10.09100 7.39200   1.000 15.46727 ? 241 GLY   A C   1 
ATOM   1684 O  O   . GLY   A 1 229 ? 27.90500  -9.21800  7.07000   1.000 14.49719 ? 241 GLY   A O   1 
ATOM   1685 N  N   . LEU   A 1 230 ? 27.29500  -11.40300 7.15300   1.000 14.76614 ? 242 LEU   A N   1 
ATOM   1686 C  CA  . LEU   A 1 230 ? 28.62500  -11.90500 6.85000   1.000 15.63955 ? 242 LEU   A CA  1 
ATOM   1687 C  C   . LEU   A 1 230 ? 28.97900  -11.68300 5.38500   1.000 13.68896 ? 242 LEU   A C   1 
ATOM   1688 O  O   . LEU   A 1 230 ? 28.17300  -11.96600 4.49400   1.000 15.79351 ? 242 LEU   A O   1 
ATOM   1689 C  CB  . LEU   A 1 230 ? 28.69000  -13.40600 7.14500   1.000 16.74465 ? 242 LEU   A CB  1 
ATOM   1690 C  CG  . LEU   A 1 230 ? 28.60600  -13.81400 8.61200   1.000 23.22010 ? 242 LEU   A CG  1 
ATOM   1691 C  CD1 . LEU   A 1 230 ? 28.86300  -15.31300 8.72700   1.000 23.06204 ? 242 LEU   A CD1 1 
ATOM   1692 C  CD2 . LEU   A 1 230 ? 29.57500  -13.03600 9.47800   1.000 31.98871 ? 242 LEU   A CD2 1 
ATOM   1693 N  N   . PRO   A 1 231 ? 30.19600  -11.21400 5.11700   1.000 15.61084 ? 243 PRO   A N   1 
ATOM   1694 C  CA  . PRO   A 1 231 ? 30.68800  -11.16400 3.74200   1.000 16.44993 ? 243 PRO   A CA  1 
ATOM   1695 C  C   . PRO   A 1 231 ? 30.84200  -12.55800 3.15300   1.000 14.74540 ? 243 PRO   A C   1 
ATOM   1696 O  O   . PRO   A 1 231 ? 30.89900  -13.57000 3.85800   1.000 16.84005 ? 243 PRO   A O   1 
ATOM   1697 C  CB  . PRO   A 1 231 ? 32.05500  -10.49200 3.88800   1.000 20.84975 ? 243 PRO   A CB  1 
ATOM   1698 C  CG  . PRO   A 1 231 ? 31.95900  -9.69300  5.18900   1.000 22.67000 ? 243 PRO   A CG  1 
ATOM   1699 C  CD  . PRO   A 1 231 ? 31.15700  -10.62600 6.06900   1.000 20.84893 ? 243 PRO   A CD  1 
ATOM   1700 N  N   . GLY   A 1 232 ? 30.89800  -12.59600 1.84200   1.000 14.66292 ? 244 GLY   A N   1 
ATOM   1701 C  CA  . GLY   A 1 232 ? 31.22300  -13.81400 1.12400   1.000 15.23476 ? 244 GLY   A CA  1 
ATOM   1702 C  C   . GLY   A 1 232 ? 31.79500  -13.43900 -0.21200  1.000 17.13801 ? 244 GLY   A C   1 
ATOM   1703 O  O   . GLY   A 1 232 ? 32.46400  -12.41500 -0.36000  1.000 15.17123 ? 244 GLY   A O   1 
ATOM   1704 N  N   . GLY   A 1 233 ? 31.54900  -14.28800 -1.20800  1.000 17.85779 ? 245 GLY   A N   1 
ATOM   1705 C  CA  . GLY   A 1 233 ? 31.92300  -14.00300 -2.56500  1.000 18.33937 ? 245 GLY   A CA  1 
ATOM   1706 C  C   . GLY   A 1 233 ? 30.72800  -13.63900 -3.42200  1.000 15.74948 ? 245 GLY   A C   1 
ATOM   1707 O  O   . GLY   A 1 233 ? 29.64000  -13.32200 -2.92400  1.000 16.51046 ? 245 GLY   A O   1 
ATOM   1708 N  N   . LEU   A 1 234 ? 30.92500  -13.71500 -4.74200  1.000 15.36011 ? 246 LEU   A N   1 
ATOM   1709 C  CA  . LEU   A 1 234 ? 29.86900  -13.34000 -5.67600  1.000 15.53787 ? 246 LEU   A CA  1 
ATOM   1710 C  C   . LEU   A 1 234 ? 28.64600  -14.23300 -5.56200  1.000 14.85620 ? 246 LEU   A C   1 
ATOM   1711 O  O   . LEU   A 1 234 ? 27.58400  -13.87300 -6.08400  1.000 15.47853 ? 246 LEU   A O   1 
ATOM   1712 C  CB  . LEU   A 1 234 ? 30.40100  -13.30200 -7.11200  1.000 16.59477 ? 246 LEU   A CB  1 
ATOM   1713 C  CG  . LEU   A 1 234 ? 31.11800  -11.99500 -7.48100  1.000 16.15063 ? 246 LEU   A CG  1 
ATOM   1714 C  CD1 . LEU   A 1 234 ? 31.95500  -12.18300 -8.74600  1.000 19.35065 ? 246 LEU   A CD1 1 
ATOM   1715 C  CD2 . LEU   A 1 234 ? 30.14600  -10.83200 -7.66100  1.000 16.51300 ? 246 LEU   A CD2 1 
ATOM   1716 N  N   A ASP   A 1 235 ? 28.77600  -15.40200 -4.92600  0.539 15.70848 ? 247 ASP   A N   1 
ATOM   1717 N  N   B ASP   A 1 235 ? 28.78200  -15.39300 -4.90600  0.461 15.81696 ? 247 ASP   A N   1 
ATOM   1718 C  CA  A ASP   A 1 235 ? 27.62300  -16.25500 -4.65700  0.539 16.85991 ? 247 ASP   A CA  1 
ATOM   1719 C  CA  B ASP   A 1 235 ? 27.65400  -16.27300 -4.61800  0.461 16.95714 ? 247 ASP   A CA  1 
ATOM   1720 C  C   A ASP   A 1 235 ? 26.50100  -15.50000 -3.96400  0.539 17.26780 ? 247 ASP   A C   1 
ATOM   1721 C  C   B ASP   A 1 235 ? 26.54000  -15.56800 -3.86000  0.461 16.90480 ? 247 ASP   A C   1 
ATOM   1722 O  O   A ASP   A 1 235 ? 25.32700  -15.86600 -4.09700  0.539 14.48734 ? 247 ASP   A O   1 
ATOM   1723 O  O   B ASP   A 1 235 ? 25.40400  -16.05000 -3.84800  0.461 15.04641 ? 247 ASP   A O   1 
ATOM   1724 C  CB  A ASP   A 1 235 ? 28.04600  -17.41700 -3.75400  0.539 20.02701 ? 247 ASP   A CB  1 
ATOM   1725 C  CB  B ASP   A 1 235 ? 28.13000  -17.47400 -3.78400  0.461 19.91331 ? 247 ASP   A CB  1 
ATOM   1726 C  CG  A ASP   A 1 235 ? 28.57200  -18.59900 -4.52400  0.539 25.44575 ? 247 ASP   A CG  1 
ATOM   1727 C  CG  B ASP   A 1 235 ? 28.97400  -17.06000 -2.58200  0.461 18.02853 ? 247 ASP   A CG  1 
ATOM   1728 O  OD1 A ASP   A 1 235 ? 28.65400  -18.54200 -5.76800  0.539 17.42412 ? 247 ASP   A OD1 1 
ATOM   1729 O  OD1 B ASP   A 1 235 ? 30.07400  -16.49100 -2.76400  0.461 19.89614 ? 247 ASP   A OD1 1 
ATOM   1730 O  OD2 A ASP   A 1 235 ? 28.92500  -19.58800 -3.86400  0.539 23.30296 ? 247 ASP   A OD2 1 
ATOM   1731 O  OD2 B ASP   A 1 235 ? 28.53900  -17.30700 -1.43700  0.461 22.02284 ? 247 ASP   A OD2 1 
ATOM   1732 N  N   . LEU   A 1 236 ? 26.82700  -14.43400 -3.22800  1.000 14.48605 ? 248 LEU   A N   1 
ATOM   1733 C  CA  . LEU   A 1 236 ? 25.76700  -13.71700 -2.52900  1.000 15.47645 ? 248 LEU   A CA  1 
ATOM   1734 C  C   . LEU   A 1 236 ? 24.75600  -13.13700 -3.51300  1.000 12.56410 ? 248 LEU   A C   1 
ATOM   1735 O  O   . LEU   A 1 236 ? 23.57800  -12.98700 -3.17600  1.000 14.42832 ? 248 LEU   A O   1 
ATOM   1736 C  CB  . LEU   A 1 236 ? 26.34700  -12.64100 -1.62000  1.000 15.27099 ? 248 LEU   A CB  1 
ATOM   1737 C  CG  . LEU   A 1 236 ? 26.70400  -13.05700 -0.18300  1.000 15.89869 ? 248 LEU   A CG  1 
ATOM   1738 C  CD1 . LEU   A 1 236 ? 27.77100  -14.17300 -0.13800  1.000 17.88915 ? 248 LEU   A CD1 1 
ATOM   1739 C  CD2 . LEU   A 1 236 ? 27.15200  -11.81700 0.61300   1.000 14.51117 ? 248 LEU   A CD2 1 
ATOM   1740 N  N   . LEU   A 1 237 ? 25.18200  -12.85500 -4.74700  1.000 13.89545 ? 249 LEU   A N   1 
ATOM   1741 C  CA  . LEU   A 1 237 ? 24.26400  -12.25200 -5.71000  1.000 14.87839 ? 249 LEU   A CA  1 
ATOM   1742 C  C   . LEU   A 1 237 ? 23.16600  -13.23300 -6.10300  1.000 14.78534 ? 249 LEU   A C   1 
ATOM   1743 O  O   . LEU   A 1 237 ? 21.97500  -12.92600 -5.99000  1.000 15.00699 ? 249 LEU   A O   1 
ATOM   1744 C  CB  . LEU   A 1 237 ? 25.03800  -11.76300 -6.93500  1.000 14.91968 ? 249 LEU   A CB  1 
ATOM   1745 C  CG  . LEU   A 1 237 ? 25.65100  -10.36600 -6.84100  1.000 14.28366 ? 249 LEU   A CG  1 
ATOM   1746 C  CD1 . LEU   A 1 237 ? 26.64400  -10.22600 -5.68100  1.000 17.07786 ? 249 LEU   A CD1 1 
ATOM   1747 C  CD2 . LEU   A 1 237 ? 26.32200  -10.05800 -8.15800  1.000 15.54600 ? 249 LEU   A CD2 1 
ATOM   1748 N  N   A LYS   A 1 238 ? 23.55600  -14.43400 -6.54500  0.419 15.02127 ? 250 LYS   A N   1 
ATOM   1749 N  N   B LYS   A 1 238 ? 23.54600  -14.43600 -6.55300  0.581 15.04434 ? 250 LYS   A N   1 
ATOM   1750 C  CA  A LYS   A 1 238 ? 22.56200  -15.42300 -6.94000  0.419 14.53391 ? 250 LYS   A CA  1 
ATOM   1751 C  CA  B LYS   A 1 238 ? 22.52900  -15.40900 -6.94000  0.581 14.46347 ? 250 LYS   A CA  1 
ATOM   1752 C  C   A LYS   A 1 238 ? 21.70900  -15.86100 -5.75500  0.419 15.10176 ? 250 LYS   A C   1 
ATOM   1753 C  C   B LYS   A 1 238 ? 21.70000  -15.87100 -5.74900  0.581 15.04424 ? 250 LYS   A C   1 
ATOM   1754 O  O   A LYS   A 1 238 ? 20.52000  -16.15600 -5.92400  0.419 15.52734 ? 250 LYS   A O   1 
ATOM   1755 O  O   B LYS   A 1 238 ? 20.51400  -16.18600 -5.90500  0.581 15.54521 ? 250 LYS   A O   1 
ATOM   1756 C  CB  A LYS   A 1 238 ? 23.24300  -16.63000 -7.58300  0.419 17.10583 ? 250 LYS   A CB  1 
ATOM   1757 C  CB  B LYS   A 1 238 ? 23.16300  -16.59200 -7.66900  0.581 17.06412 ? 250 LYS   A CB  1 
ATOM   1758 C  CG  A LYS   A 1 238 ? 22.29200  -17.52000 -8.33300  0.419 22.13013 ? 250 LYS   A CG  1 
ATOM   1759 C  CG  B LYS   A 1 238 ? 23.53000  -16.26200 -9.09700  0.581 15.47479 ? 250 LYS   A CG  1 
ATOM   1760 C  CD  A LYS   A 1 238 ? 21.69000  -16.78500 -9.51200  0.419 22.00455 ? 250 LYS   A CD  1 
ATOM   1761 C  CD  B LYS   A 1 238 ? 23.69100  -17.51700 -9.92200  0.581 20.81280 ? 250 LYS   A CD  1 
ATOM   1762 C  CE  A LYS   A 1 238 ? 20.18400  -16.92500 -9.55000  0.419 24.88670 ? 250 LYS   A CE  1 
ATOM   1763 C  CE  B LYS   A 1 238 ? 25.08100  -17.63400 -10.51300 0.581 29.67120 ? 250 LYS   A CE  1 
ATOM   1764 N  NZ  A LYS   A 1 238 ? 19.66200  -16.50900 -10.87800 0.419 20.37933 ? 250 LYS   A NZ  1 
ATOM   1765 N  NZ  B LYS   A 1 238 ? 25.11000  -18.67900 -11.56600 0.581 24.28501 ? 250 LYS   A NZ  1 
ATOM   1766 N  N   . HIS   A 1 239 ? 22.29000  -15.89100 -4.55200  1.000 14.06449 ? 251 HIS   A N   1 
ATOM   1767 C  CA  . HIS   A 1 239 ? 21.50100  -16.18800 -3.36400  1.000 13.19227 ? 251 HIS   A CA  1 
ATOM   1768 C  C   . HIS   A 1 239 ? 20.41300  -15.13000 -3.17000  1.000 13.82673 ? 251 HIS   A C   1 
ATOM   1769 O  O   . HIS   A 1 239 ? 19.25000  -15.45900 -2.88800  1.000 15.11664 ? 251 HIS   A O   1 
ATOM   1770 C  CB  . HIS   A 1 239 ? 22.41000  -16.21500 -2.14200  1.000 14.30820 ? 251 HIS   A CB  1 
ATOM   1771 C  CG  . HIS   A 1 239 ? 21.66000  -16.04300 -0.86700  1.000 12.13593 ? 251 HIS   A CG  1 
ATOM   1772 N  ND1 . HIS   A 1 239 ? 20.87900  -17.04300 -0.33000  1.000 13.78728 ? 251 HIS   A ND1 1 
ATOM   1773 C  CD2 . HIS   A 1 239 ? 21.54200  -14.98500 -0.03100  1.000 14.66682 ? 251 HIS   A CD2 1 
ATOM   1774 C  CE1 . HIS   A 1 239 ? 20.30300  -16.61200 0.77500   1.000 15.00028 ? 251 HIS   A CE1 1 
ATOM   1775 N  NE2 . HIS   A 1 239 ? 20.69000  -15.36100 0.97800   1.000 15.22781 ? 251 HIS   A NE2 1 
ATOM   1776 N  N   . THR   A 1 240 ? 20.76600  -13.85400 -3.33800  1.000 13.91564 ? 252 THR   A N   1 
ATOM   1777 C  CA  . THR   A 1 240 ? 19.77100  -12.80500 -3.16900  1.000 14.38377 ? 252 THR   A CA  1 
ATOM   1778 C  C   . THR   A 1 240 ? 18.67200  -12.92900 -4.21900  1.000 13.31786 ? 252 THR   A C   1 
ATOM   1779 O  O   . THR   A 1 240 ? 17.48100  -12.81600 -3.90400  1.000 13.81303 ? 252 THR   A O   1 
ATOM   1780 C  CB  . THR   A 1 240 ? 20.45200  -11.43100 -3.20200  1.000 14.86228 ? 252 THR   A CB  1 
ATOM   1781 O  OG1 . THR   A 1 240 ? 21.48300  -11.38600 -2.19300  1.000 13.59684 ? 252 THR   A OG1 1 
ATOM   1782 C  CG2 . THR   A 1 240 ? 19.44500  -10.32900 -2.92500  1.000 15.97275 ? 252 THR   A CG2 1 
ATOM   1783 N  N   . THR   A 1 241 ? 19.04500  -13.20300 -5.47100  1.000 13.22800 ? 253 THR   A N   1 
ATOM   1784 C  CA  . THR   A 1 241 ? 18.02900  -13.38500 -6.50100  1.000 13.12548 ? 253 THR   A CA  1 
ATOM   1785 C  C   . THR   A 1 241 ? 17.09300  -14.53100 -6.14000  1.000 15.15717 ? 253 THR   A C   1 
ATOM   1786 O  O   . THR   A 1 241 ? 15.87700  -14.43900 -6.35800  1.000 15.31450 ? 253 THR   A O   1 
ATOM   1787 C  CB  . THR   A 1 241 ? 18.71000  -13.65000 -7.83300  1.000 16.21601 ? 253 THR   A CB  1 
ATOM   1788 O  OG1 . THR   A 1 241 ? 19.35700  -12.44400 -8.24900  1.000 17.10589 ? 253 THR   A OG1 1 
ATOM   1789 C  CG2 . THR   A 1 241 ? 17.69300  -14.08500 -8.89300  1.000 15.90458 ? 253 THR   A CG2 1 
ATOM   1790 N  N   . ASN   A 1 242 ? 17.63900  -15.62200 -5.59100  1.000 14.12895 ? 254 ASN   A N   1 
ATOM   1791 C  CA  A ASN   A 1 242 ? 16.80100  -16.75000 -5.19500  0.501 16.13196 ? 254 ASN   A CA  1 
ATOM   1792 C  CA  B ASN   A 1 242 ? 16.79100  -16.74600 -5.20100  0.499 16.13692 ? 254 ASN   A CA  1 
ATOM   1793 C  C   . ASN   A 1 242 ? 15.79900  -16.34000 -4.12100  1.000 15.98093 ? 254 ASN   A C   1 
ATOM   1794 O  O   . ASN   A 1 242 ? 14.60600  -16.66200 -4.21200  1.000 16.36060 ? 254 ASN   A O   1 
ATOM   1795 C  CB  A ASN   A 1 242 ? 17.68500  -17.90100 -4.72400  0.501 17.86715 ? 254 ASN   A CB  1 
ATOM   1796 C  CB  B ASN   A 1 242 ? 17.63200  -17.93100 -4.73100  0.499 17.92618 ? 254 ASN   A CB  1 
ATOM   1797 C  CG  A ASN   A 1 242 ? 18.40800  -18.57400 -5.87300  0.501 19.77268 ? 254 ASN   A CG  1 
ATOM   1798 C  CG  B ASN   A 1 242 ? 16.78000  -19.14700 -4.42100  0.499 19.79645 ? 254 ASN   A CG  1 
ATOM   1799 O  OD1 A ASN   A 1 242 ? 18.03900  -18.40500 -7.03500  0.501 18.86664 ? 254 ASN   A OD1 1 
ATOM   1800 O  OD1 B ASN   A 1 242 ? 16.27000  -19.80300 -5.32800  0.499 27.50049 ? 254 ASN   A OD1 1 
ATOM   1801 N  ND2 A ASN   A 1 242 ? 19.45200  -19.32500 -5.55900  0.501 21.44116 ? 254 ASN   A ND2 1 
ATOM   1802 N  ND2 B ASN   A 1 242 ? 16.59200  -19.43500 -3.13500  0.499 21.96186 ? 254 ASN   A ND2 1 
ATOM   1803 N  N   . VAL   A 1 243 ? 16.26700  -15.61300 -3.09500  1.000 14.89600 ? 255 VAL   A N   1 
ATOM   1804 C  CA  . VAL   A 1 243 ? 15.38000  -15.13200 -2.03700  1.000 15.67673 ? 255 VAL   A CA  1 
ATOM   1805 C  C   . VAL   A 1 243 ? 14.31000  -14.21500 -2.61100  1.000 16.64390 ? 255 VAL   A C   1 
ATOM   1806 O  O   . VAL   A 1 243 ? 13.12700  -14.31200 -2.26200  1.000 15.37918 ? 255 VAL   A O   1 
ATOM   1807 C  CB  . VAL   A 1 243 ? 16.20100  -14.43400 -0.93400  1.000 16.91486 ? 255 VAL   A CB  1 
ATOM   1808 C  CG1 . VAL   A 1 243 ? 15.29200  -13.75400 0.07900   1.000 20.29739 ? 255 VAL   A CG1 1 
ATOM   1809 C  CG2 . VAL   A 1 243 ? 17.09700  -15.43600 -0.22900  1.000 16.16773 ? 255 VAL   A CG2 1 
ATOM   1810 N  N   . VAL   A 1 244 ? 14.70900  -13.29800 -3.49000  1.000 13.28117 ? 256 VAL   A N   1 
ATOM   1811 C  CA  . VAL   A 1 244 ? 13.76300  -12.33100 -4.03700  1.000 15.53365 ? 256 VAL   A CA  1 
ATOM   1812 C  C   . VAL   A 1 244 ? 12.70400  -13.02200 -4.89200  1.000 14.52990 ? 256 VAL   A C   1 
ATOM   1813 O  O   . VAL   A 1 244 ? 11.51200  -12.69500 -4.81900  1.000 14.18242 ? 256 VAL   A O   1 
ATOM   1814 C  CB  . VAL   A 1 244 ? 14.52700  -11.25700 -4.83400  1.000 15.78608 ? 256 VAL   A CB  1 
ATOM   1815 C  CG1 . VAL   A 1 244 ? 13.57400  -10.47000 -5.75400  1.000 20.18984 ? 256 VAL   A CG1 1 
ATOM   1816 C  CG2 . VAL   A 1 244 ? 15.30000  -10.33400 -3.88200  1.000 16.41019 ? 256 VAL   A CG2 1 
ATOM   1817 N  N   . LYS   A 1 245 ? 13.12300  -13.95300 -5.74400  1.000 14.96787 ? 257 LYS   A N   1 
ATOM   1818 C  CA  . LYS   A 1 245 ? 12.16100  -14.65600 -6.59100  1.000 14.57673 ? 257 LYS   A CA  1 
ATOM   1819 C  C   . LYS   A 1 245 ? 11.21600  -15.51600 -5.76500  1.000 15.53543 ? 257 LYS   A C   1 
ATOM   1820 O  O   . LYS   A 1 245 ? 10.01600  -15.57300 -6.05700  1.000 16.52313 ? 257 LYS   A O   1 
ATOM   1821 C  CB  . LYS   A 1 245 ? 12.90400  -15.48600 -7.63500  1.000 14.66678 ? 257 LYS   A CB  1 
ATOM   1822 C  CG  . LYS   A 1 245 ? 13.47700  -14.64000 -8.76100  1.000 16.25278 ? 257 LYS   A CG  1 
ATOM   1823 C  CD  . LYS   A 1 245 ? 14.06600  -15.53800 -9.83700  1.000 19.14592 ? 257 LYS   A CD  1 
ATOM   1824 C  CE  . LYS   A 1 245 ? 14.57100  -14.75800 -11.02400 1.000 19.82987 ? 257 LYS   A CE  1 
ATOM   1825 N  NZ  . LYS   A 1 245 ? 14.80800  -15.66600 -12.19400 1.000 26.49460 ? 257 LYS   A NZ  1 
ATOM   1826 N  N   . ALA   A 1 246 ? 11.73400  -16.17900 -4.72800  1.000 15.25459 ? 258 ALA   A N   1 
ATOM   1827 C  CA  . ALA   A 1 246 ? 10.86200  -16.96900 -3.86300  1.000 16.79917 ? 258 ALA   A CA  1 
ATOM   1828 C  C   . ALA   A 1 246 ? 9.83500   -16.08100 -3.18000  1.000 20.34600 ? 258 ALA   A C   1 
ATOM   1829 O  O   . ALA   A 1 246 ? 8.65700   -16.43900 -3.07900  1.000 19.76344 ? 258 ALA   A O   1 
ATOM   1830 C  CB  . ALA   A 1 246 ? 11.69500  -17.72600 -2.82600  1.000 18.57636 ? 258 ALA   A CB  1 
ATOM   1831 N  N   . HIS   A 1 247 ? 10.26100  -14.90100 -2.72400  1.000 15.58491 ? 259 HIS   A N   1 
ATOM   1832 C  CA  . HIS   A 1 247 ? 9.32700   -13.95900 -2.12800  1.000 17.34012 ? 259 HIS   A CA  1 
ATOM   1833 C  C   . HIS   A 1 247 ? 8.31300   -13.47400 -3.15200  1.000 17.95735 ? 259 HIS   A C   1 
ATOM   1834 O  O   . HIS   A 1 247 ? 7.12700   -13.33600 -2.84100  1.000 18.90581 ? 259 HIS   A O   1 
ATOM   1835 C  CB  . HIS   A 1 247 ? 10.08100  -12.76800 -1.54000  1.000 18.50125 ? 259 HIS   A CB  1 
ATOM   1836 C  CG  . HIS   A 1 247 ? 9.18400   -11.75800 -0.90300  1.000 20.13670 ? 259 HIS   A CG  1 
ATOM   1837 N  ND1 . HIS   A 1 247 ? 8.69300   -11.90400 0.37700   1.000 25.01428 ? 259 HIS   A ND1 1 
ATOM   1838 C  CD2 . HIS   A 1 247 ? 8.67100   -10.60100 -1.37800  1.000 22.96574 ? 259 HIS   A CD2 1 
ATOM   1839 C  CE1 . HIS   A 1 247 ? 7.92900   -10.86300 0.66700   1.000 23.54502 ? 259 HIS   A CE1 1 
ATOM   1840 N  NE2 . HIS   A 1 247 ? 7.89100   -10.06500 -0.38300  1.000 25.31607 ? 259 HIS   A NE2 1 
ATOM   1841 N  N   . THR   A 1 248 ? 8.77000   -13.20700 -4.37700  1.000 15.39027 ? 260 THR   A N   1 
ATOM   1842 C  CA  . THR   A 1 248 ? 7.87200   -12.79600 -5.45000  1.000 16.89637 ? 260 THR   A CA  1 
ATOM   1843 C  C   . THR   A 1 248 ? 6.73500   -13.79600 -5.63400  1.000 20.62786 ? 260 THR   A C   1 
ATOM   1844 O  O   . THR   A 1 248 ? 5.57500   -13.41000 -5.81600  1.000 21.98003 ? 260 THR   A O   1 
ATOM   1845 C  CB  . THR   A 1 248 ? 8.69200   -12.64200 -6.74000  1.000 18.47031 ? 260 THR   A CB  1 
ATOM   1846 O  OG1 . THR   A 1 248 ? 9.57700   -11.51300 -6.63400  1.000 19.56469 ? 260 THR   A OG1 1 
ATOM   1847 C  CG2 . THR   A 1 248 ? 7.78700   -12.47500 -7.95300  1.000 18.88154 ? 260 THR   A CG2 1 
ATOM   1848 N  N   . ASN   A 1 249 ? 7.04500   -15.08500 -5.56700  1.000 17.42132 ? 261 ASN   A N   1 
ATOM   1849 C  CA  . ASN   A 1 249 ? 6.06200   -16.15000 -5.73800  1.000 17.94023 ? 261 ASN   A CA  1 
ATOM   1850 C  C   . ASN   A 1 249 ? 5.35900   -16.53500 -4.43400  1.000 24.89765 ? 261 ASN   A C   1 
ATOM   1851 O  O   . ASN   A 1 249 ? 4.60200   -17.51000 -4.42400  1.000 30.15761 ? 261 ASN   A O   1 
ATOM   1852 C  CB  . ASN   A 1 249 ? 6.71500   -17.38300 -6.38100  1.000 18.28725 ? 261 ASN   A CB  1 
ATOM   1853 C  CG  . ASN   A 1 249 ? 7.09800   -17.15100 -7.84000  1.000 18.53718 ? 261 ASN   A CG  1 
ATOM   1854 O  OD1 . ASN   A 1 249 ? 6.70000   -16.16100 -8.44500  1.000 21.09505 ? 261 ASN   A OD1 1 
ATOM   1855 N  ND2 . ASN   A 1 249 ? 7.85100   -18.07200 -8.40500  1.000 18.53858 ? 261 ASN   A ND2 1 
ATOM   1856 N  N   . ARG   A 1 250 ? 5.57300   -15.78200 -3.35300  1.000 23.70376 ? 262 ARG   A N   1 
ATOM   1857 C  CA  . ARG   A 1 250 ? 5.04200   -16.14600 -2.04100  1.000 27.22910 ? 262 ARG   A CA  1 
ATOM   1858 C  C   . ARG   A 1 250 ? 3.53300   -16.34600 -2.07500  1.000 35.25330 ? 262 ARG   A C   1 
ATOM   1859 O  O   . ARG   A 1 250 ? 2.80400   -15.65300 -2.79300  1.000 38.68595 ? 262 ARG   A O   1 
ATOM   1860 C  CB  . ARG   A 1 250 ? 5.37700   -15.06900 -1.00700  1.000 28.98607 ? 262 ARG   A CB  1 
ATOM   1861 C  CG  . ARG   A 1 250 ? 4.54800   -13.77800 -1.13800  1.000 32.02912 ? 262 ARG   A CG  1 
ATOM   1862 C  CD  . ARG   A 1 250 ? 5.23500   -12.59100 -0.47900  1.000 26.61529 ? 262 ARG   A CD  1 
ATOM   1863 N  NE  . ARG   A 1 250 ? 4.50500   -11.34900 -0.69600  1.000 35.71106 ? 262 ARG   A NE  1 
ATOM   1864 C  CZ  . ARG   A 1 250 ? 4.58300   -10.61500 -1.79900  1.000 46.01592 ? 262 ARG   A CZ  1 
ATOM   1865 N  NH1 . ARG   A 1 250 ? 5.35800   -10.96900 -2.81200  1.000 30.98771 ? 262 ARG   A NH1 1 
ATOM   1866 N  NH2 . ARG   A 1 250 ? 3.86700   -9.49400  -1.88500  1.000 39.92019 ? 262 ARG   A NH2 1 
ATOM   1867 N  N   . GLU   B 1 20  ? -9.08200  34.22900  16.74700  1.000 46.63280 ? 32  GLU   B N   1 
ATOM   1868 C  CA  . GLU   B 1 20  ? -8.68100  33.15600  15.84300  1.000 43.95786 ? 32  GLU   B CA  1 
ATOM   1869 C  C   . GLU   B 1 20  ? -8.48700  31.86700  16.63600  1.000 37.37316 ? 32  GLU   B C   1 
ATOM   1870 O  O   . GLU   B 1 20  ? -9.29000  30.93400  16.54500  1.000 34.99427 ? 32  GLU   B O   1 
ATOM   1871 C  CB  . GLU   B 1 20  ? -7.39300  33.54500  15.11700  1.000 44.05593 ? 32  GLU   B CB  1 
ATOM   1872 C  CG  . GLU   B 1 20  ? -6.89500  32.54700  14.08500  1.000 45.39375 ? 32  GLU   B CG  1 
ATOM   1873 C  CD  . GLU   B 1 20  ? -5.58300  32.99200  13.46100  1.000 69.72094 ? 32  GLU   B CD  1 
ATOM   1874 O  OE1 . GLU   B 1 20  ? -4.79500  33.67200  14.15700  1.000 73.71426 ? 32  GLU   B OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 20  ? -5.34000  32.67500  12.27600  1.000 70.14728 ? 32  GLU   B OE2 1 
ATOM   1876 N  N   . TYR   B 1 21  ? -7.42900  31.82200  17.42900  1.000 40.14620 ? 33  TYR   B N   1 
ATOM   1877 C  CA  . TYR   B 1 21  ? -7.21900  30.67300  18.29300  1.000 29.30655 ? 33  TYR   B CA  1 
ATOM   1878 C  C   . TYR   B 1 21  ? -8.32500  30.62500  19.33600  1.000 29.80909 ? 33  TYR   B C   1 
ATOM   1879 O  O   . TYR   B 1 21  ? -8.62600  31.65200  19.95900  1.000 38.52008 ? 33  TYR   B O   1 
ATOM   1880 C  CB  . TYR   B 1 21  ? -5.86200  30.76300  18.97900  1.000 29.48738 ? 33  TYR   B CB  1 
ATOM   1881 C  CG  . TYR   B 1 21  ? -5.41400  29.42500  19.52300  1.000 25.68803 ? 33  TYR   B CG  1 
ATOM   1882 C  CD1 . TYR   B 1 21  ? -4.74800  28.51800  18.70900  1.000 27.67084 ? 33  TYR   B CD1 1 
ATOM   1883 C  CD2 . TYR   B 1 21  ? -5.66200  29.07100  20.84300  1.000 26.28559 ? 33  TYR   B CD2 1 
ATOM   1884 C  CE1 . TYR   B 1 21  ? -4.33800  27.28400  19.19200  1.000 22.76560 ? 33  TYR   B CE1 1 
ATOM   1885 C  CE2 . TYR   B 1 21  ? -5.25300  27.83300  21.34300  1.000 20.53816 ? 33  TYR   B CE2 1 
ATOM   1886 C  CZ  . TYR   B 1 21  ? -4.59100  26.95200  20.50900  1.000 19.23851 ? 33  TYR   B CZ  1 
ATOM   1887 O  OH  . TYR   B 1 21  ? -4.17800  25.72900  21.00400  1.000 17.72477 ? 33  TYR   B OH  1 
ATOM   1888 N  N   . PRO   B 1 22  ? -8.95400  29.47200  19.55300  1.000 30.95229 ? 34  PRO   B N   1 
ATOM   1889 C  CA  . PRO   B 1 22  ? -10.05800 29.39500  20.52200  1.000 30.90111 ? 34  PRO   B CA  1 
ATOM   1890 C  C   . PRO   B 1 22  ? -9.58000  29.70000  21.93200  1.000 42.23310 ? 34  PRO   B C   1 
ATOM   1891 O  O   . PRO   B 1 22  ? -8.66300  29.06100  22.45600  1.000 32.91417 ? 34  PRO   B O   1 
ATOM   1892 C  CB  . PRO   B 1 22  ? -10.56200 27.95300  20.39300  1.000 31.66852 ? 34  PRO   B CB  1 
ATOM   1893 C  CG  . PRO   B 1 22  ? -9.74900  27.29600  19.34500  1.000 34.72934 ? 34  PRO   B CG  1 
ATOM   1894 C  CD  . PRO   B 1 22  ? -8.63000  28.17900  18.93000  1.000 24.63995 ? 34  PRO   B CD  1 
ATOM   1895 N  N   . THR   B 1 23  ? -10.20500 30.69500  22.53900  1.000 44.98695 ? 35  THR   B N   1 
ATOM   1896 C  CA  . THR   B 1 23  ? -9.86700  31.06900  23.89700  1.000 44.19582 ? 35  THR   B CA  1 
ATOM   1897 C  C   . THR   B 1 23  ? -10.79300 30.36200  24.87700  1.000 30.15258 ? 35  THR   B C   1 
ATOM   1898 O  O   . THR   B 1 23  ? -11.83700 29.82200  24.51100  1.000 32.58910 ? 35  THR   B O   1 
ATOM   1899 C  CB  . THR   B 1 23  ? -9.94600  32.58400  24.06400  1.000 38.29652 ? 35  THR   B CB  1 
ATOM   1900 O  OG1 . THR   B 1 23  ? -11.32100 32.97700  24.15100  1.000 43.95002 ? 35  THR   B OG1 1 
ATOM   1901 C  CG2 . THR   B 1 23  ? -9.28500  33.27900  22.88100  1.000 44.34764 ? 35  THR   B CG2 1 
ATOM   1902 N  N   . VAL   B 1 24  ? -10.38700 30.38200  26.14800  1.000 33.34903 ? 36  VAL   B N   1 
ATOM   1903 C  CA  . VAL   B 1 24  ? -11.10800 29.66900  27.19700  1.000 32.90710 ? 36  VAL   B CA  1 
ATOM   1904 C  C   . VAL   B 1 24  ? -12.56700 30.10400  27.27100  1.000 44.46681 ? 36  VAL   B C   1 
ATOM   1905 O  O   . VAL   B 1 24  ? -13.45200 29.29200  27.57600  1.000 39.50031 ? 36  VAL   B O   1 
ATOM   1906 C  CB  . VAL   B 1 24  ? -10.36300 29.84600  28.53800  1.000 36.94123 ? 36  VAL   B CB  1 
ATOM   1907 C  CG1 . VAL   B 1 24  ? -9.98500  31.31600  28.75700  1.000 36.51570 ? 36  VAL   B CG1 1 
ATOM   1908 C  CG2 . VAL   B 1 24  ? -11.17800 29.29100  29.69500  1.000 34.99915 ? 36  VAL   B CG2 1 
ATOM   1909 N  N   . SER   B 1 25  ? -12.84700 31.37500  26.97200  1.000 47.22832 ? 37  SER   B N   1 
ATOM   1910 C  CA  . SER   B 1 25  ? -14.18300 31.94900  27.08700  1.000 52.13171 ? 37  SER   B CA  1 
ATOM   1911 C  C   . SER   B 1 25  ? -15.09400 31.61300  25.90800  1.000 55.17292 ? 37  SER   B C   1 
ATOM   1912 O  O   . SER   B 1 25  ? -16.14700 32.24200  25.76200  1.000 58.55746 ? 37  SER   B O   1 
ATOM   1913 C  CB  . SER   B 1 25  ? -14.08500 33.47000  27.23100  1.000 52.74844 ? 37  SER   B CB  1 
ATOM   1914 O  OG  . SER   B 1 25  ? -14.19100 34.10100  25.96600  1.000 61.35946 ? 37  SER   B OG  1 
ATOM   1915 N  N   . GLU   B 1 26  ? -14.71800 30.64600  25.06700  1.000 53.48171 ? 38  GLU   B N   1 
ATOM   1916 C  CA  . GLU   B 1 26  ? -15.51100 30.29400  23.89400  1.000 42.63383 ? 38  GLU   B CA  1 
ATOM   1917 C  C   . GLU   B 1 26  ? -15.69700 28.79100  23.73500  1.000 47.51884 ? 38  GLU   B C   1 
ATOM   1918 O  O   . GLU   B 1 26  ? -16.14900 28.34900  22.67300  1.000 53.00481 ? 38  GLU   B O   1 
ATOM   1919 C  CB  . GLU   B 1 26  ? -14.88800 30.87400  22.62300  1.000 47.96675 ? 38  GLU   B CB  1 
ATOM   1920 C  CG  . GLU   B 1 26  ? -14.89000 32.38600  22.56900  1.000 55.81056 ? 38  GLU   B CG  1 
ATOM   1921 C  CD  . GLU   B 1 26  ? -13.90600 32.92600  21.55700  1.000 55.90486 ? 38  GLU   B CD  1 
ATOM   1922 O  OE1 . GLU   B 1 26  ? -12.82500 32.31800  21.39900  1.000 55.45390 ? 38  GLU   B OE1 1 
ATOM   1923 O  OE2 . GLU   B 1 26  ? -14.21400 33.95500  20.92000  1.000 65.34207 ? 38  GLU   B OE2 1 
ATOM   1924 N  N   . ILE   B 1 27  ? -15.34800 27.99800  24.74400  1.000 46.16898 ? 39  ILE   B N   1 
ATOM   1925 C  CA  . ILE   B 1 27  ? -15.48200 26.54700  24.66400  1.000 39.23551 ? 39  ILE   B CA  1 
ATOM   1926 C  C   . ILE   B 1 27  ? -16.21900 26.04200  25.89700  1.000 42.01133 ? 39  ILE   B C   1 
ATOM   1927 O  O   . ILE   B 1 27  ? -15.67600 26.10600  27.00800  1.000 52.12588 ? 39  ILE   B O   1 
ATOM   1928 C  CB  . ILE   B 1 27  ? -14.11200 25.85900  24.53100  1.000 41.07711 ? 39  ILE   B CB  1 
ATOM   1929 C  CG1 . ILE   B 1 27  ? -13.32100 26.44900  23.36100  1.000 44.51580 ? 39  ILE   B CG1 1 
ATOM   1930 C  CG2 . ILE   B 1 27  ? -14.28300 24.34800  24.37400  1.000 36.22065 ? 39  ILE   B CG2 1 
ATOM   1931 C  CD1 . ILE   B 1 27  ? -11.82700 26.20400  23.44100  1.000 37.07941 ? 39  ILE   B CD1 1 
ATOM   1932 N  N   . PRO   B 1 28  ? -17.43800 25.52400  25.75600  1.000 52.65538 ? 40  PRO   B N   1 
ATOM   1933 C  CA  . PRO   B 1 28  ? -18.11600 24.92500  26.91100  1.000 44.44631 ? 40  PRO   B CA  1 
ATOM   1934 C  C   . PRO   B 1 28  ? -17.38300 23.67500  27.37500  1.000 46.87482 ? 40  PRO   B C   1 
ATOM   1935 O  O   . PRO   B 1 28  ? -16.85400 22.90900  26.56800  1.000 44.22818 ? 40  PRO   B O   1 
ATOM   1936 C  CB  . PRO   B 1 28  ? -19.50900 24.57700  26.36700  1.000 48.53192 ? 40  PRO   B CB  1 
ATOM   1937 C  CG  . PRO   B 1 28  ? -19.66600 25.41800  25.12900  1.000 55.73555 ? 40  PRO   B CG  1 
ATOM   1938 C  CD  . PRO   B 1 28  ? -18.28800 25.52300  24.55300  1.000 55.69521 ? 40  PRO   B CD  1 
ATOM   1939 N  N   . VAL   B 1 29  ? -17.34600 23.48300  28.69400  1.000 42.67107 ? 41  VAL   B N   1 
ATOM   1940 C  CA  . VAL   B 1 29  ? -16.68400 22.31200  29.25900  1.000 35.37852 ? 41  VAL   B CA  1 
ATOM   1941 C  C   . VAL   B 1 29  ? -17.39300 21.06000  28.76400  1.000 45.78027 ? 41  VAL   B C   1 
ATOM   1942 O  O   . VAL   B 1 29  ? -18.61100 20.91300  28.92400  1.000 49.56866 ? 41  VAL   B O   1 
ATOM   1943 C  CB  . VAL   B 1 29  ? -16.65400 22.39100  30.78800  1.000 42.73105 ? 41  VAL   B CB  1 
ATOM   1944 C  CG1 . VAL   B 1 29  ? -16.09300 21.09900  31.38300  1.000 31.48002 ? 41  VAL   B CG1 1 
ATOM   1945 C  CG2 . VAL   B 1 29  ? -15.85000 23.60600  31.24400  1.000 38.89281 ? 41  VAL   B CG2 1 
ATOM   1946 N  N   . GLY   B 1 30  ? -16.63200 20.14700  28.16000  1.000 38.74979 ? 42  GLY   B N   1 
ATOM   1947 C  CA  . GLY   B 1 30  ? -17.16900 18.97300  27.50700  1.000 39.32331 ? 42  GLY   B CA  1 
ATOM   1948 C  C   . GLY   B 1 30  ? -17.05500 19.00500  25.99600  1.000 36.97968 ? 42  GLY   B C   1 
ATOM   1949 O  O   . GLY   B 1 30  ? -17.16200 17.94800  25.35700  1.000 37.49028 ? 42  GLY   B O   1 
ATOM   1950 N  N   . GLU   B 1 31  ? -16.84800 20.18300  25.41200  1.000 37.00670 ? 43  GLU   B N   1 
ATOM   1951 C  CA  . GLU   B 1 31  ? -16.63100 20.35700  23.98400  1.000 37.54345 ? 43  GLU   B CA  1 
ATOM   1952 C  C   . GLU   B 1 31  ? -15.14000 20.51800  23.70800  1.000 35.28203 ? 43  GLU   B C   1 
ATOM   1953 O  O   . GLU   B 1 31  ? -14.36300 20.93000  24.57200  1.000 31.38791 ? 43  GLU   B O   1 
ATOM   1954 C  CB  . GLU   B 1 31  ? -17.36800 21.59900  23.47700  1.000 38.51253 ? 43  GLU   B CB  1 
ATOM   1955 C  CG  . GLU   B 1 31  ? -18.72500 21.82700  24.12000  1.000 51.19800 ? 43  GLU   B CG  1 
ATOM   1956 C  CD  . GLU   B 1 31  ? -19.81300 22.14800  23.11500  1.000 61.01079 ? 43  GLU   B CD  1 
ATOM   1957 O  OE1 . GLU   B 1 31  ? -19.65900 21.78300  21.92900  1.000 62.87168 ? 43  GLU   B OE1 1 
ATOM   1958 O  OE2 . GLU   B 1 31  ? -20.82600 22.76300  23.51700  1.000 61.64070 ? 43  GLU   B OE2 1 
ATOM   1959 N  N   . VAL   B 1 32  ? -14.74900 20.19400  22.48000  1.000 26.54794 ? 44  VAL   B N   1 
ATOM   1960 C  CA  . VAL   B 1 32  ? -13.35600 20.23700  22.05700  1.000 21.87990 ? 44  VAL   B CA  1 
ATOM   1961 C  C   . VAL   B 1 32  ? -13.29700 20.93800  20.71500  1.000 26.80454 ? 44  VAL   B C   1 
ATOM   1962 O  O   . VAL   B 1 32  ? -14.08700 20.63200  19.81400  1.000 25.97574 ? 44  VAL   B O   1 
ATOM   1963 C  CB  . VAL   B 1 32  ? -12.75000 18.82300  21.93400  1.000 22.71168 ? 44  VAL   B CB  1 
ATOM   1964 C  CG1 . VAL   B 1 32  ? -11.33400 18.90000  21.32900  1.000 19.66981 ? 44  VAL   B CG1 1 
ATOM   1965 C  CG2 . VAL   B 1 32  ? -12.73400 18.12000  23.28100  1.000 22.55349 ? 44  VAL   B CG2 1 
ATOM   1966 N  N   . ARG   B 1 33  ? -12.37000 21.87400  20.58400  1.000 21.06349 ? 45  ARG   B N   1 
ATOM   1967 C  CA  . ARG   B 1 33  ? -12.09800 22.55100  19.33000  1.000 20.53690 ? 45  ARG   B CA  1 
ATOM   1968 C  C   . ARG   B 1 33  ? -10.76400 22.07900  18.78200  1.000 24.48668 ? 45  ARG   B C   1 
ATOM   1969 O  O   . ARG   B 1 33  ? -9.85300  21.71600  19.53500  1.000 21.53782 ? 45  ARG   B O   1 
ATOM   1970 C  CB  . ARG   B 1 33  ? -12.02900 24.07400  19.50600  1.000 25.42774 ? 45  ARG   B CB  1 
ATOM   1971 C  CG  . ARG   B 1 33  ? -13.17900 24.68100  20.30200  1.000 33.55487 ? 45  ARG   B CG  1 
ATOM   1972 C  CD  . ARG   B 1 33  ? -14.38300 25.01900  19.43100  1.000 37.81409 ? 45  ARG   B CD  1 
ATOM   1973 N  NE  . ARG   B 1 33  ? -15.45000 25.63300  20.21600  1.000 45.65078 ? 45  ARG   B NE  1 
ATOM   1974 C  CZ  . ARG   B 1 33  ? -16.60400 25.04800  20.51300  1.000 46.12926 ? 45  ARG   B CZ  1 
ATOM   1975 N  NH1 . ARG   B 1 33  ? -16.89100 23.82800  20.09100  1.000 39.82896 ? 45  ARG   B NH1 1 
ATOM   1976 N  NH2 . ARG   B 1 33  ? -17.48800 25.70100  21.26400  1.000 47.32694 ? 45  ARG   B NH2 1 
ATOM   1977 N  N   . LEU   B 1 34  ? -10.66900 22.06600  17.46100  1.000 19.99720 ? 46  LEU   B N   1 
ATOM   1978 C  CA  . LEU   B 1 34  ? -9.41400  21.84700  16.77100  1.000 19.39187 ? 46  LEU   B CA  1 
ATOM   1979 C  C   . LEU   B 1 34  ? -9.01100  23.13600  16.07800  1.000 25.75053 ? 46  LEU   B C   1 
ATOM   1980 O  O   . LEU   B 1 34  ? -9.86100  23.90200  15.61600  1.000 30.26525 ? 46  LEU   B O   1 
ATOM   1981 C  CB  . LEU   B 1 34  ? -9.53100  20.72400  15.74100  1.000 19.88569 ? 46  LEU   B CB  1 
ATOM   1982 C  CG  . LEU   B 1 34  ? -10.10700 19.41300  16.26100  1.000 19.90178 ? 46  LEU   B CG  1 
ATOM   1983 C  CD1 . LEU   B 1 34  ? -10.07800 18.38100  15.14400  1.000 29.62794 ? 46  LEU   B CD1 1 
ATOM   1984 C  CD2 . LEU   B 1 34  ? -9.33800  18.93800  17.47300  1.000 20.41688 ? 46  LEU   B CD2 1 
ATOM   1985 N  N   . TYR   B 1 35  ? -7.70700  23.38000  16.02200  1.000 17.42909 ? 47  TYR   B N   1 
ATOM   1986 C  CA  . TYR   B 1 35  ? -7.14900  24.58000  15.40900  1.000 18.86243 ? 47  TYR   B CA  1 
ATOM   1987 C  C   . TYR   B 1 35  ? -6.02300  24.13400  14.49100  1.000 22.31121 ? 47  TYR   B C   1 
ATOM   1988 O  O   . TYR   B 1 35  ? -5.00400  23.61200  14.95800  1.000 21.12165 ? 47  TYR   B O   1 
ATOM   1989 C  CB  . TYR   B 1 35  ? -6.59800  25.51000  16.48300  1.000 23.80193 ? 47  TYR   B CB  1 
ATOM   1990 C  CG  . TYR   B 1 35  ? -6.01100  26.78000  15.92000  1.000 22.51135 ? 47  TYR   B CG  1 
ATOM   1991 C  CD1 . TYR   B 1 35  ? -6.82000  27.84800  15.55500  1.000 25.73178 ? 47  TYR   B CD1 1 
ATOM   1992 C  CD2 . TYR   B 1 35  ? -4.64100  26.89200  15.71100  1.000 22.80908 ? 47  TYR   B CD2 1 
ATOM   1993 C  CE1 . TYR   B 1 35  ? -6.27000  29.00300  15.03200  1.000 24.95335 ? 47  TYR   B CE1 1 
ATOM   1994 C  CE2 . TYR   B 1 35  ? -4.08600  28.03700  15.18800  1.000 32.50099 ? 47  TYR   B CE2 1 
ATOM   1995 C  CZ  . TYR   B 1 35  ? -4.90300  29.08900  14.84900  1.000 34.45315 ? 47  TYR   B CZ  1 
ATOM   1996 O  OH  . TYR   B 1 35  ? -4.34400  30.23500  14.32600  1.000 43.40037 ? 47  TYR   B OH  1 
ATOM   1997 N  N   . GLN   B 1 36  ? -6.18400  24.34100  13.18900  1.000 20.36584 ? 48  GLN   B N   1 
ATOM   1998 C  CA  . GLN   B 1 36  ? -5.17000  23.86900  12.26100  1.000 20.10559 ? 48  GLN   B CA  1 
ATOM   1999 C  C   . GLN   B 1 36  ? -4.03600  24.88400  12.18900  1.000 26.82719 ? 48  GLN   B C   1 
ATOM   2000 O  O   . GLN   B 1 36  ? -4.26000  26.06400  11.90600  1.000 30.49418 ? 48  GLN   B O   1 
ATOM   2001 C  CB  . GLN   B 1 36  ? -5.75000  23.54000  10.88700  1.000 24.14775 ? 48  GLN   B CB  1 
ATOM   2002 C  CG  . GLN   B 1 36  ? -4.70600  23.37200  9.80900   1.000 33.01827 ? 48  GLN   B CG  1 
ATOM   2003 C  CD  . GLN   B 1 36  ? -5.21900  22.55300  8.63900   1.000 35.88705 ? 48  GLN   B CD  1 
ATOM   2004 O  OE1 . GLN   B 1 36  ? -6.42900  22.42700  8.43400   1.000 43.78283 ? 48  GLN   B OE1 1 
ATOM   2005 N  NE2 . GLN   B 1 36  ? -4.30100  21.96800  7.88100   1.000 38.48002 ? 48  GLN   B NE2 1 
ATOM   2006 N  N   . ILE   B 1 37  ? -2.82500  24.42600  12.48500  1.000 26.84528 ? 49  ILE   B N   1 
ATOM   2007 C  CA  . ILE   B 1 37  ? -1.65500  25.28600  12.58500  1.000 26.61747 ? 49  ILE   B CA  1 
ATOM   2008 C  C   . ILE   B 1 37  ? -0.86500  25.29900  11.28800  1.000 31.21567 ? 49  ILE   B C   1 
ATOM   2009 O  O   . ILE   B 1 37  ? -0.36100  26.34200  10.86500  1.000 32.45652 ? 49  ILE   B O   1 
ATOM   2010 C  CB  . ILE   B 1 37  ? -0.79100  24.77100  13.75400  1.000 31.38279 ? 49  ILE   B CB  1 
ATOM   2011 C  CG1 . ILE   B 1 37  ? -1.51500  25.02800  15.06700  1.000 30.73643 ? 49  ILE   B CG1 1 
ATOM   2012 C  CG2 . ILE   B 1 37  ? 0.57900   25.43200  13.74300  1.000 28.62845 ? 49  ILE   B CG2 1 
ATOM   2013 C  CD1 . ILE   B 1 37  ? -0.89500  24.34300  16.22200  1.000 32.44710 ? 49  ILE   B CD1 1 
ATOM   2014 N  N   . ALA   B 1 38  ? -0.75200  24.14300  10.65500  1.000 29.82758 ? 50  ALA   B N   1 
ATOM   2015 C  CA  . ALA   B 1 38  ? -0.00800  23.99100  9.41700   1.000 29.36321 ? 50  ALA   B CA  1 
ATOM   2016 C  C   . ALA   B 1 38  ? -0.56000  22.77000  8.70500   1.000 32.45397 ? 50  ALA   B C   1 
ATOM   2017 O  O   . ALA   B 1 38  ? -1.50000  22.12400  9.17900   1.000 30.74060 ? 50  ALA   B O   1 
ATOM   2018 C  CB  . ALA   B 1 38  ? 1.49300   23.87000  9.69200   1.000 31.13855 ? 50  ALA   B CB  1 
ATOM   2019 N  N   . ASP   B 1 39  ? 0.02900   22.45800  7.55200   1.000 29.62551 ? 51  ASP   B N   1 
ATOM   2020 C  CA  . ASP   B 1 39  ? -0.34000  21.25900  6.82100   1.000 33.20714 ? 51  ASP   B CA  1 
ATOM   2021 C  C   . ASP   B 1 39  ? -0.16300  20.05600  7.73800   1.000 29.95059 ? 51  ASP   B C   1 
ATOM   2022 O  O   . ASP   B 1 39  ? 0.94900   19.77900  8.19300   1.000 30.95086 ? 51  ASP   B O   1 
ATOM   2023 C  CB  . ASP   B 1 39  ? 0.54900   21.11300  5.58600   1.000 35.01425 ? 51  ASP   B CB  1 
ATOM   2024 C  CG  . ASP   B 1 39  ? -0.21900  20.65400  4.37000   1.000 55.35951 ? 51  ASP   B CG  1 
ATOM   2025 O  OD1 . ASP   B 1 39  ? -0.59500  19.46400  4.31200   1.000 64.25203 ? 51  ASP   B OD1 1 
ATOM   2026 O  OD2 . ASP   B 1 39  ? -0.44200  21.48600  3.46500   1.000 72.50977 ? 51  ASP   B OD2 1 
ATOM   2027 N  N   . GLY   B 1 40  ? -1.26000  19.37500  8.05400   1.000 27.48116 ? 52  GLY   B N   1 
ATOM   2028 C  CA  . GLY   B 1 40  ? -1.19500  18.17500  8.86400   1.000 22.80236 ? 52  GLY   B CA  1 
ATOM   2029 C  C   . GLY   B 1 40  ? -0.84300  18.36800  10.32100  1.000 19.62996 ? 52  GLY   B C   1 
ATOM   2030 O  O   . GLY   B 1 40  ? -0.41900  17.40500  10.96800  1.000 21.49222 ? 52  GLY   B O   1 
ATOM   2031 N  N   . VAL   B 1 41  ? -1.01300  19.56800  10.87300  1.000 18.55206 ? 53  VAL   B N   1 
ATOM   2032 C  CA  . VAL   B 1 41  ? -0.72700  19.81200  12.28400  1.000 17.86880 ? 53  VAL   B CA  1 
ATOM   2033 C  C   . VAL   B 1 41  ? -1.86700  20.62400  12.86800  1.000 19.04056 ? 53  VAL   B C   1 
ATOM   2034 O  O   . VAL   B 1 41  ? -2.19400  21.69900  12.35000  1.000 22.69981 ? 53  VAL   B O   1 
ATOM   2035 C  CB  . VAL   B 1 41  ? 0.61600   20.54500  12.50700  1.000 21.01854 ? 53  VAL   B CB  1 
ATOM   2036 C  CG1 . VAL   B 1 41  ? 0.89000   20.70000  13.98900  1.000 21.37125 ? 53  VAL   B CG1 1 
ATOM   2037 C  CG2 . VAL   B 1 41  ? 1.76400   19.81900  11.82900  1.000 25.14739 ? 53  VAL   B CG2 1 
ATOM   2038 N  N   . TRP   B 1 42  ? -2.45100  20.12900  13.95600  1.000 17.25092 ? 54  TRP   B N   1 
ATOM   2039 C  CA  . TRP   B 1 42  ? -3.50600  20.81700  14.67500  1.000 17.08014 ? 54  TRP   B CA  1 
ATOM   2040 C  C   . TRP   B 1 42  ? -3.18600  20.82900  16.16300  1.000 18.81050 ? 54  TRP   B C   1 
ATOM   2041 O  O   . TRP   B 1 42  ? -2.49700  19.94000  16.67700  1.000 16.45162 ? 54  TRP   B O   1 
ATOM   2042 C  CB  . TRP   B 1 42  ? -4.86300  20.10800  14.55600  1.000 16.70578 ? 54  TRP   B CB  1 
ATOM   2043 C  CG  . TRP   B 1 42  ? -5.39800  19.86200  13.16600  1.000 18.98329 ? 54  TRP   B CG  1 
ATOM   2044 C  CD1 . TRP   B 1 42  ? -6.42300  20.54300  12.55700  1.000 21.24873 ? 54  TRP   B CD1 1 
ATOM   2045 C  CD2 . TRP   B 1 42  ? -4.99100  18.84000  12.24100  1.000 18.06987 ? 54  TRP   B CD2 1 
ATOM   2046 N  NE1 . TRP   B 1 42  ? -6.65700  20.02200  11.30600  1.000 20.43565 ? 54  TRP   B NE1 1 
ATOM   2047 C  CE2 . TRP   B 1 42  ? -5.79900  18.97600  11.08800  1.000 21.57624 ? 54  TRP   B CE2 1 
ATOM   2048 C  CE3 . TRP   B 1 42  ? -4.02600  17.82700  12.27200  1.000 20.32447 ? 54  TRP   B CE3 1 
ATOM   2049 C  CZ2 . TRP   B 1 42  ? -5.66300  18.14300  9.97500   1.000 19.28398 ? 54  TRP   B CZ2 1 
ATOM   2050 C  CZ3 . TRP   B 1 42  ? -3.89400  16.99700  11.16300  1.000 20.82664 ? 54  TRP   B CZ3 1 
ATOM   2051 C  CH2 . TRP   B 1 42  ? -4.71400  17.16400  10.03000  1.000 21.16029 ? 54  TRP   B CH2 1 
ATOM   2052 N  N   . SER   B 1 43  ? -3.70700  21.82800  16.86400  1.000 17.56315 ? 55  SER   B N   1 
ATOM   2053 C  CA  . SER   B 1 43  ? -3.86300  21.67600  18.29700  1.000 17.48763 ? 55  SER   B CA  1 
ATOM   2054 C  C   . SER   B 1 43  ? -5.29500  21.26600  18.59000  1.000 17.62003 ? 55  SER   B C   1 
ATOM   2055 O  O   . SER   B 1 43  ? -6.20800  21.50700  17.79000  1.000 16.75760 ? 55  SER   B O   1 
ATOM   2056 C  CB  . SER   B 1 43  ? -3.48100  22.94200  19.07300  1.000 20.82425 ? 55  SER   B CB  1 
ATOM   2057 O  OG  . SER   B 1 43  ? -4.33100  24.02400  18.74100  1.000 19.34771 ? 55  SER   B OG  1 
ATOM   2058 N  N   . HIS   B 1 44  ? -5.47700  20.58600  19.71000  1.000 16.24996 ? 56  HIS   B N   1 
ATOM   2059 C  CA  . HIS   B 1 44  ? -6.79700  20.38100  20.27400  1.000 16.76744 ? 56  HIS   B CA  1 
ATOM   2060 C  C   . HIS   B 1 44  ? -6.91900  21.18100  21.55800  1.000 15.92999 ? 56  HIS   B C   1 
ATOM   2061 O  O   . HIS   B 1 44  ? -5.95500  21.29900  22.32000  1.000 16.39811 ? 56  HIS   B O   1 
ATOM   2062 C  CB  . HIS   B 1 44  ? -7.15400  18.89600  20.44300  1.000 14.46715 ? 56  HIS   B CB  1 
ATOM   2063 C  CG  . HIS   B 1 44  ? -6.29300  18.10400  21.38300  1.000 15.06354 ? 56  HIS   B CG  1 
ATOM   2064 N  ND1 . HIS   B 1 44  ? -6.48200  18.09200  22.75200  1.000 15.74058 ? 56  HIS   B ND1 1 
ATOM   2065 C  CD2 . HIS   B 1 44  ? -5.34500  17.16500  21.12900  1.000 14.07712 ? 56  HIS   B CD2 1 
ATOM   2066 C  CE1 . HIS   B 1 44  ? -5.64700  17.22700  23.30400  1.000 14.19517 ? 56  HIS   B CE1 1 
ATOM   2067 N  NE2 . HIS   B 1 44  ? -4.95700  16.63500  22.33900  1.000 14.39526 ? 56  HIS   B NE2 1 
ATOM   2068 N  N   . ILE   B 1 45  ? -8.08100  21.79000  21.76000  1.000 17.25163 ? 57  ILE   B N   1 
ATOM   2069 C  CA  . ILE   B 1 45  ? -8.29300  22.71800  22.86500  1.000 17.06267 ? 57  ILE   B CA  1 
ATOM   2070 C  C   . ILE   B 1 45  ? -9.54500  22.27500  23.59600  1.000 16.56789 ? 57  ILE   B C   1 
ATOM   2071 O  O   . ILE   B 1 45  ? -10.60900 22.12100  22.98000  1.000 20.86385 ? 57  ILE   B O   1 
ATOM   2072 C  CB  . ILE   B 1 45  ? -8.42800  24.18100  22.39800  1.000 18.70075 ? 57  ILE   B CB  1 
ATOM   2073 C  CG1 . ILE   B 1 45  ? -7.27700  24.57800  21.48100  1.000 18.81312 ? 57  ILE   B CG1 1 
ATOM   2074 C  CG2 . ILE   B 1 45  ? -8.43800  25.11800  23.60300  1.000 22.72170 ? 57  ILE   B CG2 1 
ATOM   2075 C  CD1 . ILE   B 1 45  ? -7.57900  24.44000  19.98800  1.000 19.29344 ? 57  ILE   B CD1 1 
ATOM   2076 N  N   . ALA   B 1 46  ? -9.41800  22.02600  24.89300  1.000 19.51997 ? 58  ALA   B N   1 
ATOM   2077 C  CA  . ALA   B 1 46  ? -10.53500 21.62600  25.73100  1.000 20.77991 ? 58  ALA   B CA  1 
ATOM   2078 C  C   . ALA   B 1 46  ? -10.52400 22.49100  26.98300  1.000 20.44332 ? 58  ALA   B C   1 
ATOM   2079 O  O   . ALA   B 1 46  ? -9.58400  23.24400  27.23100  1.000 21.60157 ? 58  ALA   B O   1 
ATOM   2080 C  CB  . ALA   B 1 46  ? -10.46900 20.13800  26.09600  1.000 19.59806 ? 58  ALA   B CB  1 
ATOM   2081 N  N   . THR   B 1 47  ? -11.59500 22.40500  27.75800  1.000 25.59203 ? 59  THR   B N   1 
ATOM   2082 C  CA  . THR   B 1 47  ? -11.69500 23.16600  28.99300  1.000 24.42605 ? 59  THR   B CA  1 
ATOM   2083 C  C   . THR   B 1 47  ? -12.06200 22.23600  30.13500  1.000 26.86498 ? 59  THR   B C   1 
ATOM   2084 O  O   . THR   B 1 47  ? -12.67300 21.18300  29.94100  1.000 25.29980 ? 59  THR   B O   1 
ATOM   2085 C  CB  . THR   B 1 47  ? -12.70200 24.33500  28.89900  1.000 25.32676 ? 59  THR   B CB  1 
ATOM   2086 O  OG1 . THR   B 1 47  ? -13.96900 23.84200  28.44500  1.000 34.84172 ? 59  THR   B OG1 1 
ATOM   2087 C  CG2 . THR   B 1 47  ? -12.20000 25.40400  27.95800  1.000 30.77438 ? 59  THR   B CG2 1 
ATOM   2088 N  N   . GLN   B 1 48  ? -11.67100 22.63200  31.34000  1.000 24.64660 ? 60  GLN   B N   1 
ATOM   2089 C  CA  . GLN   B 1 48  ? -11.97500 21.81900  32.50200  1.000 25.50063 ? 60  GLN   B CA  1 
ATOM   2090 C  C   . GLN   B 1 48  ? -12.22800 22.73600  33.68700  1.000 33.17530 ? 60  GLN   B C   1 
ATOM   2091 O  O   . GLN   B 1 48  ? -11.51400 23.72600  33.88200  1.000 27.02838 ? 60  GLN   B O   1 
ATOM   2092 C  CB  . GLN   B 1 48  ? -10.84600 20.82400  32.80100  1.000 30.63675 ? 60  GLN   B CB  1 
ATOM   2093 C  CG  . GLN   B 1 48  ? -11.23800 19.67600  33.72100  1.000 25.30180 ? 60  GLN   B CG  1 
ATOM   2094 C  CD  . GLN   B 1 48  ? -12.54500 19.01100  33.32100  1.000 35.26192 ? 60  GLN   B CD  1 
ATOM   2095 O  OE1 . GLN   B 1 48  ? -13.62200 19.42900  33.75000  1.000 33.91495 ? 60  GLN   B OE1 1 
ATOM   2096 N  NE2 . GLN   B 1 48  ? -12.45900 17.98000  32.48800  1.000 32.26145 ? 60  GLN   B NE2 1 
ATOM   2097 N  N   A SER   B 1 49  ? -13.28400 22.43300  34.43300  0.772 32.41700 ? 61  SER   B N   1 
ATOM   2098 N  N   B SER   B 1 49  ? -13.25400 22.40400  34.46900  0.228 32.63687 ? 61  SER   B N   1 
ATOM   2099 C  CA  A SER   B 1 49  ? -13.52200 23.08100  35.71100  0.772 34.67392 ? 61  SER   B CA  1 
ATOM   2100 C  CA  B SER   B 1 49  ? -13.53700 23.09600  35.72100  0.228 34.51861 ? 61  SER   B CA  1 
ATOM   2101 C  C   A SER   B 1 49  ? -12.64500 22.39100  36.74400  0.772 34.04935 ? 61  SER   B C   1 
ATOM   2102 C  C   B SER   B 1 49  ? -12.71700 22.42200  36.81400  0.228 33.86890 ? 61  SER   B C   1 
ATOM   2103 O  O   A SER   B 1 49  ? -12.75800 21.18000  36.95500  0.772 31.37142 ? 61  SER   B O   1 
ATOM   2104 O  O   B SER   B 1 49  ? -12.95500 21.25900  37.15100  0.228 32.66071 ? 61  SER   B O   1 
ATOM   2105 C  CB  A SER   B 1 49  ? -14.99300 22.95700  36.09200  0.772 33.66559 ? 61  SER   B CB  1 
ATOM   2106 C  CB  B SER   B 1 49  ? -15.02800 23.03800  36.04100  0.228 33.59008 ? 61  SER   B CB  1 
ATOM   2107 O  OG  A SER   B 1 49  ? -15.22200 21.73900  36.77400  0.772 35.92731 ? 61  SER   B OG  1 
ATOM   2108 O  OG  B SER   B 1 49  ? -15.78100 23.76100  35.08500  0.228 34.86611 ? 61  SER   B OG  1 
ATOM   2109 N  N   . PHE   B 1 50  ? -11.74700 23.15000  37.36200  1.000 30.54375 ? 62  PHE   B N   1 
ATOM   2110 C  CA  . PHE   B 1 50  ? -10.79000 22.59200  38.30400  1.000 33.13476 ? 62  PHE   B CA  1 
ATOM   2111 C  C   . PHE   B 1 50  ? -10.67500 23.56300  39.46600  1.000 35.22635 ? 62  PHE   B C   1 
ATOM   2112 O  O   . PHE   B 1 50  ? -10.27800 24.71800  39.27500  1.000 28.78899 ? 62  PHE   B O   1 
ATOM   2113 C  CB  . PHE   B 1 50  ? -9.43200  22.40400  37.61300  1.000 36.97193 ? 62  PHE   B CB  1 
ATOM   2114 C  CG  . PHE   B 1 50  ? -8.38500  21.74900  38.47200  1.000 34.16026 ? 62  PHE   B CG  1 
ATOM   2115 C  CD1 . PHE   B 1 50  ? -8.63500  20.53100  39.08500  1.000 38.12907 ? 62  PHE   B CD1 1 
ATOM   2116 C  CD2 . PHE   B 1 50  ? -7.13800  22.33400  38.63800  1.000 35.61658 ? 62  PHE   B CD2 1 
ATOM   2117 C  CE1 . PHE   B 1 50  ? -7.67200  19.91900  39.86700  1.000 37.29294 ? 62  PHE   B CE1 1 
ATOM   2118 C  CE2 . PHE   B 1 50  ? -6.16700  21.72500  39.42100  1.000 37.99735 ? 62  PHE   B CE2 1 
ATOM   2119 C  CZ  . PHE   B 1 50  ? -6.43700  20.51600  40.03500  1.000 40.48740 ? 62  PHE   B CZ  1 
ATOM   2120 N  N   . ASP   B 1 51  ? -11.06200 23.10800  40.65600  1.000 33.87138 ? 63  ASP   B N   1 
ATOM   2121 C  CA  . ASP   B 1 51  ? -10.88500 23.88200  41.88200  1.000 33.21488 ? 63  ASP   B CA  1 
ATOM   2122 C  C   . ASP   B 1 51  ? -11.62300 25.22500  41.82700  1.000 31.97563 ? 63  ASP   B C   1 
ATOM   2123 O  O   . ASP   B 1 51  ? -11.15400 26.22600  42.37300  1.000 30.70648 ? 63  ASP   B O   1 
ATOM   2124 C  CB  . ASP   B 1 51  ? -9.39300  24.07500  42.18300  1.000 37.09748 ? 63  ASP   B CB  1 
ATOM   2125 C  CG  . ASP   B 1 51  ? -9.08100  24.06200  43.66100  1.000 38.11878 ? 63  ASP   B CG  1 
ATOM   2126 O  OD1 . ASP   B 1 51  ? -9.80400  23.38200  44.42000  1.000 40.99390 ? 63  ASP   B OD1 1 
ATOM   2127 O  OD2 . ASP   B 1 51  ? -8.09300  24.71500  44.05800  1.000 49.39493 ? 63  ASP   B OD2 1 
ATOM   2128 N  N   . GLY   B 1 52  ? -12.76900 25.27200  41.13200  1.000 27.91015 ? 64  GLY   B N   1 
ATOM   2129 C  CA  . GLY   B 1 52  ? -13.64300 26.43400  41.12600  1.000 25.98372 ? 64  GLY   B CA  1 
ATOM   2130 C  C   . GLY   B 1 52  ? -13.59800 27.28700  39.87200  1.000 30.98041 ? 64  GLY   B C   1 
ATOM   2131 O  O   . GLY   B 1 52  ? -14.55000 28.03900  39.61700  1.000 29.68403 ? 64  GLY   B O   1 
ATOM   2132 N  N   . ALA   B 1 53  ? -12.52400 27.21500  39.09400  1.000 29.88443 ? 65  ALA   B N   1 
ATOM   2133 C  CA  . ALA   B 1 53  ? -12.36200 28.03500  37.90100  1.000 24.37741 ? 65  ALA   B CA  1 
ATOM   2134 C  C   . ALA   B 1 53  ? -12.34900 27.14100  36.67000  1.000 28.38810 ? 65  ALA   B C   1 
ATOM   2135 O  O   . ALA   B 1 53  ? -12.28800 25.91900  36.77500  1.000 27.67958 ? 65  ALA   B O   1 
ATOM   2136 C  CB  . ALA   B 1 53  ? -11.06900 28.85200  37.97900  1.000 26.57673 ? 65  ALA   B CB  1 
ATOM   2137 N  N   . VAL   B 1 54  ? -12.40600 27.76200  35.49400  1.000 21.39653 ? 66  VAL   B N   1 
ATOM   2138 C  CA  . VAL   B 1 54  ? -12.35100 27.03400  34.23100  1.000 26.86733 ? 66  VAL   B CA  1 
ATOM   2139 C  C   . VAL   B 1 54  ? -11.03700 27.36300  33.54100  1.000 20.92325 ? 66  VAL   B C   1 
ATOM   2140 O  O   . VAL   B 1 54  ? -10.66400 28.53800  33.42100  1.000 24.95545 ? 66  VAL   B O   1 
ATOM   2141 C  CB  . VAL   B 1 54  ? -13.56100 27.35000  33.33500  1.000 26.59363 ? 66  VAL   B CB  1 
ATOM   2142 C  CG1 . VAL   B 1 54  ? -13.33900 26.80600  31.92400  1.000 30.60003 ? 66  VAL   B CG1 1 
ATOM   2143 C  CG2 . VAL   B 1 54  ? -14.81900 26.75800  33.93500  1.000 28.51151 ? 66  VAL   B CG2 1 
ATOM   2144 N  N   . TYR   B 1 55  ? -10.33600 26.31800  33.08500  1.000 24.18582 ? 67  TYR   B N   1 
ATOM   2145 C  CA  . TYR   B 1 55  ? -9.05300  26.43500  32.42600  1.000 23.13168 ? 67  TYR   B CA  1 
ATOM   2146 C  C   . TYR   B 1 55  ? -9.10300  25.77800  31.05500  1.000 19.06830 ? 67  TYR   B C   1 
ATOM   2147 O  O   . TYR   B 1 55  ? -9.67200  24.69100  30.91800  1.000 21.03272 ? 67  TYR   B O   1 
ATOM   2148 C  CB  . TYR   B 1 55  ? -7.98100  25.72400  33.25400  1.000 20.66817 ? 67  TYR   B CB  1 
ATOM   2149 C  CG  . TYR   B 1 55  ? -7.86200  26.29700  34.64300  1.000 24.07910 ? 67  TYR   B CG  1 
ATOM   2150 C  CD1 . TYR   B 1 55  ? -7.09100  27.42400  34.87400  1.000 25.05775 ? 67  TYR   B CD1 1 
ATOM   2151 C  CD2 . TYR   B 1 55  ? -8.52000  25.71600  35.71700  1.000 24.73456 ? 67  TYR   B CD2 1 
ATOM   2152 C  CE1 . TYR   B 1 55  ? -6.97700  27.96300  36.14400  1.000 28.73062 ? 67  TYR   B CE1 1 
ATOM   2153 C  CE2 . TYR   B 1 55  ? -8.41700  26.25700  36.99800  1.000 24.87401 ? 67  TYR   B CE2 1 
ATOM   2154 C  CZ  . TYR   B 1 55  ? -7.64000  27.37900  37.19200  1.000 26.24327 ? 67  TYR   B CZ  1 
ATOM   2155 O  OH  . TYR   B 1 55  ? -7.51800  27.92500  38.44700  1.000 30.81084 ? 67  TYR   B OH  1 
ATOM   2156 N  N   . PRO   B 1 56  ? -8.50500  26.39700  30.04300  1.000 18.58152 ? 68  PRO   B N   1 
ATOM   2157 C  CA  . PRO   B 1 56  ? -8.30500  25.71600  28.76400  1.000 18.68449 ? 68  PRO   B CA  1 
ATOM   2158 C  C   . PRO   B 1 56  ? -7.05300  24.85600  28.83700  1.000 17.19517 ? 68  PRO   B C   1 
ATOM   2159 O  O   . PRO   B 1 56  ? -6.18600  25.03100  29.69800  1.000 16.42125 ? 68  PRO   B O   1 
ATOM   2160 C  CB  . PRO   B 1 56  ? -8.06400  26.88100  27.79900  1.000 20.75023 ? 68  PRO   B CB  1 
ATOM   2161 C  CG  . PRO   B 1 56  ? -7.32400  27.88800  28.64900  1.000 21.17947 ? 68  PRO   B CG  1 
ATOM   2162 C  CD  . PRO   B 1 56  ? -7.80900  27.69500  30.08100  1.000 21.58304 ? 68  PRO   B CD  1 
ATOM   2163 N  N   . SER   B 1 57  ? -6.96400  23.90700  27.91200  1.000 17.95304 ? 69  SER   B N   1 
ATOM   2164 C  CA  . SER   B 1 57  ? -5.82500  23.00300  27.87300  1.000 17.02425 ? 69  SER   B CA  1 
ATOM   2165 C  C   . SER   B 1 57  ? -5.61500  22.57600  26.43200  1.000 13.90190 ? 69  SER   B C   1 
ATOM   2166 O  O   . SER   B 1 57  ? -6.58500  22.27400  25.72900  1.000 17.19889 ? 69  SER   B O   1 
ATOM   2167 C  CB  . SER   B 1 57  ? -6.08900  21.77200  28.74700  1.000 17.69309 ? 69  SER   B CB  1 
ATOM   2168 O  OG  . SER   B 1 57  ? -4.94000  20.95600  28.87200  1.000 19.07530 ? 69  SER   B OG  1 
ATOM   2169 N  N   . ASN   B 1 58  ? -4.35800  22.54300  26.00500  1.000 15.75482 ? 70  ASN   B N   1 
ATOM   2170 C  CA  . ASN   B 1 58  ? -3.98000  22.17800  24.64300  1.000 15.88747 ? 70  ASN   B CA  1 
ATOM   2171 C  C   . ASN   B 1 58  ? -3.35000  20.79800  24.57000  1.000 15.26644 ? 70  ASN   B C   1 
ATOM   2172 O  O   . ASN   B 1 58  ? -2.65300  20.36100  25.48800  1.000 14.88828 ? 70  ASN   B O   1 
ATOM   2173 C  CB  . ASN   B 1 58  ? -2.91900  23.11500  24.09200  1.000 15.47250 ? 70  ASN   B CB  1 
ATOM   2174 C  CG  . ASN   B 1 58  ? -3.38200  24.53200  24.01300  1.000 15.31366 ? 70  ASN   B CG  1 
ATOM   2175 O  OD1 . ASN   B 1 58  ? -4.49800  24.79800  23.55700  1.000 16.31129 ? 70  ASN   B OD1 1 
ATOM   2176 N  ND2 . ASN   B 1 58  ? -2.53300  25.45800  24.43500  1.000 15.85437 ? 70  ASN   B ND2 1 
ATOM   2177 N  N   . GLY   B 1 59  ? -3.56300  20.15400  23.43200  1.000 14.29005 ? 71  GLY   B N   1 
ATOM   2178 C  CA  . GLY   B 1 59  ? -2.77200  19.01900  22.98500  1.000 13.98153 ? 71  GLY   B CA  1 
ATOM   2179 C  C   . GLY   B 1 59  ? -2.45000  19.19900  21.51800  1.000 10.79131 ? 71  GLY   B C   1 
ATOM   2180 O  O   . GLY   B 1 59  ? -2.74800  20.25100  20.94400  1.000 14.49577 ? 71  GLY   B O   1 
ATOM   2181 N  N   . LEU   B 1 60  ? -1.87800  18.18100  20.87700  1.000 12.43207 ? 72  LEU   B N   1 
ATOM   2182 C  CA  . LEU   B 1 60  ? -1.46500  18.29000  19.48900  1.000 13.45458 ? 72  LEU   B CA  1 
ATOM   2183 C  C   . LEU   B 1 60  ? -1.96100  17.08400  18.69800  1.000 13.39191 ? 72  LEU   B C   1 
ATOM   2184 O  O   . LEU   B 1 60  ? -2.16400  16.00100  19.24900  1.000 12.47423 ? 72  LEU   B O   1 
ATOM   2185 C  CB  . LEU   B 1 60  ? 0.04900   18.35200  19.40900  1.000 14.91678 ? 72  LEU   B CB  1 
ATOM   2186 C  CG  . LEU   B 1 60  ? 0.59200   19.05000  18.17100  1.000 14.07915 ? 72  LEU   B CG  1 
ATOM   2187 C  CD1 . LEU   B 1 60  ? 0.30000   20.53700  18.22800  1.000 18.53727 ? 72  LEU   B CD1 1 
ATOM   2188 C  CD2 . LEU   B 1 60  ? 2.07900   18.76100  18.04700  1.000 16.02114 ? 72  LEU   B CD2 1 
ATOM   2189 N  N   . ILE   B 1 61  ? -2.19700  17.28500  17.40000  1.000 13.14610 ? 73  ILE   B N   1 
ATOM   2190 C  CA  . ILE   B 1 61  ? -2.50500  16.20300  16.46500  1.000 14.52822 ? 73  ILE   B CA  1 
ATOM   2191 C  C   . ILE   B 1 61  ? -1.59900  16.38400  15.26200  1.000 13.58953 ? 73  ILE   B C   1 
ATOM   2192 O  O   . ILE   B 1 61  ? -1.54200  17.48300  14.69700  1.000 14.78615 ? 73  ILE   B O   1 
ATOM   2193 C  CB  . ILE   B 1 61  ? -3.97400  16.25200  15.99200  1.000 15.11091 ? 73  ILE   B CB  1 
ATOM   2194 C  CG1 . ILE   B 1 61  ? -4.94900  16.24800  17.16200  1.000 15.45818 ? 73  ILE   B CG1 1 
ATOM   2195 C  CG2 . ILE   B 1 61  ? -4.27300  15.09500  15.01200  1.000 15.34671 ? 73  ILE   B CG2 1 
ATOM   2196 C  CD1 . ILE   B 1 61  ? -6.32500  16.76700  16.78300  1.000 16.99053 ? 73  ILE   B CD1 1 
ATOM   2197 N  N   . VAL   B 1 62  ? -0.91900  15.31700  14.85100  1.000 13.26713 ? 74  VAL   B N   1 
ATOM   2198 C  CA  . VAL   B 1 62  ? 0.01300   15.38500  13.72900  1.000 15.35923 ? 74  VAL   B CA  1 
ATOM   2199 C  C   . VAL   B 1 62  ? -0.30400  14.25900  12.76000  1.000 16.35627 ? 74  VAL   B C   1 
ATOM   2200 O  O   . VAL   B 1 62  ? -0.35600  13.08800  13.15500  1.000 15.15397 ? 74  VAL   B O   1 
ATOM   2201 C  CB  . VAL   B 1 62  ? 1.48300   15.28900  14.18800  1.000 13.91682 ? 74  VAL   B CB  1 
ATOM   2202 C  CG1 . VAL   B 1 62  ? 2.42300   15.50800  13.01700  1.000 15.20684 ? 74  VAL   B CG1 1 
ATOM   2203 C  CG2 . VAL   B 1 62  ? 1.75900   16.29100  15.28900  1.000 15.62973 ? 74  VAL   B CG2 1 
ATOM   2204 N  N   . ARG   B 1 63  ? -0.52300  14.61400  11.49300  1.000 17.15272 ? 75  ARG   B N   1 
ATOM   2205 C  CA  . ARG   B 1 63  ? -0.79900  13.59700  10.49000  1.000 18.57779 ? 75  ARG   B CA  1 
ATOM   2206 C  C   . ARG   B 1 63  ? 0.47000   12.81800  10.17400  1.000 18.85003 ? 75  ARG   B C   1 
ATOM   2207 O  O   . ARG   B 1 63  ? 1.55600   13.38700  10.05400  1.000 20.31962 ? 75  ARG   B O   1 
ATOM   2208 C  CB  . ARG   B 1 63  ? -1.32900  14.24500  9.20700   1.000 21.25478 ? 75  ARG   B CB  1 
ATOM   2209 C  CG  . ARG   B 1 63  ? -1.63700  13.23600  8.11500   1.000 21.85126 ? 75  ARG   B CG  1 
ATOM   2210 C  CD  . ARG   B 1 63  ? -2.51600  13.85500  7.02400   1.000 29.52118 ? 75  ARG   B CD  1 
ATOM   2211 N  NE  . ARG   B 1 63  ? -2.91300  12.85900  6.03600   1.000 34.58695 ? 75  ARG   B NE  1 
ATOM   2212 C  CZ  . ARG   B 1 63  ? -3.86500  13.03500  5.12900   1.000 39.74728 ? 75  ARG   B CZ  1 
ATOM   2213 N  NH1 . ARG   B 1 63  ? -4.54900  14.16600  5.05100   1.000 34.51163 ? 75  ARG   B NH1 1 
ATOM   2214 N  NH2 . ARG   B 1 63  ? -4.13800  12.05100  4.27800   1.000 38.36122 ? 75  ARG   B NH2 1 
ATOM   2215 N  N   . ASP   B 1 64  ? 0.33800   11.50300  10.03100  1.000 22.78792 ? 76  ASP   B N   1 
ATOM   2216 C  CA  . ASP   B 1 64  ? 1.46300   10.71000  9.53700   1.000 29.10400 ? 76  ASP   B CA  1 
ATOM   2217 C  C   . ASP   B 1 64  ? 0.93100   9.67900   8.55000   1.000 25.88963 ? 76  ASP   B C   1 
ATOM   2218 O  O   . ASP   B 1 64  ? 0.35500   8.65800   8.94900   1.000 26.19649 ? 76  ASP   B O   1 
ATOM   2219 C  CB  . ASP   B 1 64  ? 2.25800   10.07400  10.65800  1.000 35.08378 ? 76  ASP   B CB  1 
ATOM   2220 C  CG  . ASP   B 1 64  ? 3.44700   9.29100   10.14900  1.000 37.06610 ? 76  ASP   B CG  1 
ATOM   2221 O  OD1 . ASP   B 1 64  ? 4.10200   9.72500   9.16400   1.000 34.71700 ? 76  ASP   B OD1 1 
ATOM   2222 O  OD2 . ASP   B 1 64  ? 3.72500   8.24400   10.75600  1.000 33.90552 ? 76  ASP   B OD2 1 
ATOM   2223 N  N   . GLY   B 1 65  ? 1.12800   9.96500   7.26800   1.000 34.34094 ? 77  GLY   B N   1 
ATOM   2224 C  CA  . GLY   B 1 65  ? 0.52100   9.18800   6.21400   1.000 26.98023 ? 77  GLY   B CA  1 
ATOM   2225 C  C   . GLY   B 1 65  ? -0.98300  9.33300   6.24100   1.000 25.19145 ? 77  GLY   B C   1 
ATOM   2226 O  O   . GLY   B 1 65  ? -1.51100  10.44300  6.13000   1.000 31.27141 ? 77  GLY   B O   1 
ATOM   2227 N  N   . ASP   B 1 66  ? -1.67800  8.21000   6.41200   1.000 25.37839 ? 78  ASP   B N   1 
ATOM   2228 C  CA  . ASP   B 1 66  ? -3.13200  8.18500   6.47500   1.000 25.71536 ? 78  ASP   B CA  1 
ATOM   2229 C  C   . ASP   B 1 66  ? -3.63200  7.91300   7.88800   1.000 23.37538 ? 78  ASP   B C   1 
ATOM   2230 O  O   . ASP   B 1 66  ? -4.79100  7.53800   8.07200   1.000 25.83832 ? 78  ASP   B O   1 
ATOM   2231 C  CB  . ASP   B 1 66  ? -3.67300  7.15300   5.48800   1.000 29.54500 ? 78  ASP   B CB  1 
ATOM   2232 C  CG  . ASP   B 1 66  ? -3.50800  7.59100   4.04300   1.000 45.77568 ? 78  ASP   B CG  1 
ATOM   2233 O  OD1 . ASP   B 1 66  ? -3.28400  8.80000   3.80600   1.000 37.96655 ? 78  ASP   B OD1 1 
ATOM   2234 O  OD2 . ASP   B 1 66  ? -3.58000  6.72300   3.14800   1.000 56.24144 ? 78  ASP   B OD2 1 
ATOM   2235 N  N   . GLU   B 1 67  ? -2.77600  8.10300   8.88900   1.000 21.12751 ? 79  GLU   B N   1 
ATOM   2236 C  CA  . GLU   B 1 67  ? -3.12500  7.94800   10.29300  1.000 20.46475 ? 79  GLU   B CA  1 
ATOM   2237 C  C   . GLU   B 1 67  ? -2.81200  9.24500   11.02600  1.000 18.56451 ? 79  GLU   B C   1 
ATOM   2238 O  O   . GLU   B 1 67  ? -2.23900  10.18000  10.46300  1.000 18.88491 ? 79  GLU   B O   1 
ATOM   2239 C  CB  . GLU   B 1 67  ? -2.34100  6.79000   10.91900  1.000 18.09509 ? 79  GLU   B CB  1 
ATOM   2240 C  CG  . GLU   B 1 67  ? -2.22500  5.58000   10.01000  1.000 28.76452 ? 79  GLU   B CG  1 
ATOM   2241 C  CD  . GLU   B 1 67  ? -1.48300  4.43700   10.65900  1.000 34.43652 ? 79  GLU   B CD  1 
ATOM   2242 O  OE1 . GLU   B 1 67  ? -0.80300  4.66100   11.68400  1.000 29.38892 ? 79  GLU   B OE1 1 
ATOM   2243 O  OE2 . GLU   B 1 67  ? -1.59000  3.30500   10.14500  1.000 48.76407 ? 79  GLU   B OE2 1 
ATOM   2244 N  N   . LEU   B 1 68  ? -3.20300  9.30400   12.29600  1.000 16.61608 ? 80  LEU   B N   1 
ATOM   2245 C  CA  . LEU   B 1 68  ? -2.89400  10.45700  13.13200  1.000 15.49955 ? 80  LEU   B CA  1 
ATOM   2246 C  C   . LEU   B 1 68  ? -2.13100  10.03700  14.38100  1.000 14.81460 ? 80  LEU   B C   1 
ATOM   2247 O  O   . LEU   B 1 68  ? -2.44100  9.00800   15.00400  1.000 14.97716 ? 80  LEU   B O   1 
ATOM   2248 C  CB  . LEU   B 1 68  ? -4.15400  11.18800  13.57200  1.000 14.69828 ? 80  LEU   B CB  1 
ATOM   2249 C  CG  . LEU   B 1 68  ? -5.04600  11.70100  12.44100  1.000 15.38640 ? 80  LEU   B CG  1 
ATOM   2250 C  CD1 . LEU   B 1 68  ? -6.30600  12.32400  12.98100  1.000 17.78942 ? 80  LEU   B CD1 1 
ATOM   2251 C  CD2 . LEU   B 1 68  ? -4.31300  12.69900  11.57700  1.000 18.97145 ? 80  LEU   B CD2 1 
ATOM   2252 N  N   . LEU   B 1 69  ? -1.15800  10.86800  14.74400  1.000 14.09953 ? 81  LEU   B N   1 
ATOM   2253 C  CA  . LEU   B 1 69  ? -0.48700  10.81200  16.03500  1.000 13.29235 ? 81  LEU   B CA  1 
ATOM   2254 C  C   . LEU   B 1 69  ? -1.09000  11.87600  16.95100  1.000 12.50842 ? 81  LEU   B C   1 
ATOM   2255 O  O   . LEU   B 1 69  ? -1.15800  13.06300  16.58900  1.000 13.14161 ? 81  LEU   B O   1 
ATOM   2256 C  CB  . LEU   B 1 69  ? 1.00900   11.07900  15.86500  1.000 13.38060 ? 81  LEU   B CB  1 
ATOM   2257 C  CG  . LEU   B 1 69  ? 1.83400   11.22100  17.15300  1.000 13.58342 ? 81  LEU   B CG  1 
ATOM   2258 C  CD1 . LEU   B 1 69  ? 1.84500   9.91300   17.92400  1.000 13.13286 ? 81  LEU   B CD1 1 
ATOM   2259 C  CD2 . LEU   B 1 69  ? 3.24100   11.66800  16.85000  1.000 16.99418 ? 81  LEU   B CD2 1 
ATOM   2260 N  N   . LEU   B 1 70  ? -1.52600  11.45600  18.13700  1.000 13.05110 ? 82  LEU   B N   1 
ATOM   2261 C  CA  . LEU   B 1 70  ? -2.11900  12.35400  19.11900  1.000 13.23691 ? 82  LEU   B CA  1 
ATOM   2262 C  C   . LEU   B 1 70  ? -1.10300  12.64000  20.21900  1.000 12.26283 ? 82  LEU   B C   1 
ATOM   2263 O  O   . LEU   B 1 70  ? -0.44900  11.71900  20.72100  1.000 13.55948 ? 82  LEU   B O   1 
ATOM   2264 C  CB  . LEU   B 1 70  ? -3.36600  11.70000  19.70700  1.000 12.87736 ? 82  LEU   B CB  1 
ATOM   2265 C  CG  . LEU   B 1 70  ? -4.07300  12.50600  20.80200  1.000 12.65613 ? 82  LEU   B CG  1 
ATOM   2266 C  CD1 . LEU   B 1 70  ? -4.66200  13.80100  20.25400  1.000 15.44724 ? 82  LEU   B CD1 1 
ATOM   2267 C  CD2 . LEU   B 1 70  ? -5.15500  11.64500  21.46400  1.000 14.46348 ? 82  LEU   B CD2 1 
ATOM   2268 N  N   . ILE   B 1 71  ? -0.96800  13.90900  20.59000  1.000 12.30211 ? 83  ILE   B N   1 
ATOM   2269 C  CA  . ILE   B 1 71  ? -0.14500  14.29600  21.72900  1.000 11.80555 ? 83  ILE   B CA  1 
ATOM   2270 C  C   . ILE   B 1 71  ? -1.08700  14.80000  22.80900  1.000 11.05602 ? 83  ILE   B C   1 
ATOM   2271 O  O   . ILE   B 1 71  ? -1.72200  15.85700  22.64700  1.000 12.14150 ? 83  ILE   B O   1 
ATOM   2272 C  CB  . ILE   B 1 71  ? 0.87800   15.38100  21.37100  1.000 11.97341 ? 83  ILE   B CB  1 
ATOM   2273 C  CG1 . ILE   B 1 71  ? 1.68700   15.01700  20.12000  1.000 13.01227 ? 83  ILE   B CG1 1 
ATOM   2274 C  CG2 . ILE   B 1 71  ? 1.78800   15.62700  22.57600  1.000 14.56641 ? 83  ILE   B CG2 1 
ATOM   2275 C  CD1 . ILE   B 1 71  ? 2.56200   13.77800  20.25400  1.000 13.59887 ? 83  ILE   B CD1 1 
ATOM   2276 N  N   . ASP   B 1 72  ? -1.17700  14.03000  23.89800  1.000 11.56172 ? 84  ASP   B N   1 
ATOM   2277 C  CA  . ASP   B 1 72  ? -1.91300  14.35100  25.11800  1.000 11.34329 ? 84  ASP   B CA  1 
ATOM   2278 C  C   . ASP   B 1 72  ? -3.41500  14.14700  24.99500  1.000 12.51901 ? 84  ASP   B C   1 
ATOM   2279 O  O   . ASP   B 1 72  ? -3.99900  14.33600  23.92100  1.000 12.97849 ? 84  ASP   B O   1 
ATOM   2280 C  CB  . ASP   B 1 72  ? -1.53000  15.72700  25.67700  1.000 11.81010 ? 84  ASP   B CB  1 
ATOM   2281 C  CG  . ASP   B 1 72  ? -0.12400  15.73900  26.23500  1.000 10.85669 ? 84  ASP   B CG  1 
ATOM   2282 O  OD1 . ASP   B 1 72  ? 0.29400   14.70600  26.77200  1.000 13.40879 ? 84  ASP   B OD1 1 
ATOM   2283 O  OD2 . ASP   B 1 72  ? 0.57900   16.77200  26.11900  1.000 13.21989 ? 84  ASP   B OD2 1 
ATOM   2284 N  N   . THR   B 1 73  ? -4.04100  13.74300  26.10300  1.000 12.95791 ? 85  THR   B N   1 
ATOM   2285 C  CA  . THR   B 1 73  ? -5.48600  13.64400  26.15300  1.000 13.84891 ? 85  THR   B CA  1 
ATOM   2286 C  C   . THR   B 1 73  ? -6.09700  15.04200  26.27200  1.000 13.46889 ? 85  THR   B C   1 
ATOM   2287 O  O   . THR   B 1 73  ? -5.40100  16.06200  26.30600  1.000 14.36806 ? 85  THR   B O   1 
ATOM   2288 C  CB  . THR   B 1 73  ? -5.93400  12.81000  27.34400  1.000 16.09917 ? 85  THR   B CB  1 
ATOM   2289 O  OG1 . THR   B 1 73  ? -5.65400  13.55400  28.54000  1.000 15.89993 ? 85  THR   B OG1 1 
ATOM   2290 C  CG2 . THR   B 1 73  ? -5.25300  11.43700  27.39000  1.000 15.70302 ? 85  THR   B CG2 1 
ATOM   2291 N  N   . ALA   B 1 74  ? -7.43000  15.10000  26.27200  1.000 16.39453 ? 86  ALA   B N   1 
ATOM   2292 C  CA  . ALA   B 1 74  ? -8.15200  16.35800  26.42000  1.000 16.95566 ? 86  ALA   B CA  1 
ATOM   2293 C  C   . ALA   B 1 74  ? -8.61500  16.58900  27.85400  1.000 21.37942 ? 86  ALA   B C   1 
ATOM   2294 O  O   . ALA   B 1 74  ? -9.58800  17.31400  28.08100  1.000 20.45602 ? 86  ALA   B O   1 
ATOM   2295 C  CB  . ALA   B 1 74  ? -9.30800  16.45500  25.42300  1.000 17.83913 ? 86  ALA   B CB  1 
ATOM   2296 N  N   . TRP   B 1 75  ? -7.90900  16.00600  28.82400  1.000 16.87640 ? 87  TRP   B N   1 
ATOM   2297 C  CA  . TRP   B 1 75  ? -8.13800  16.21000  30.25400  1.000 18.88494 ? 87  TRP   B CA  1 
ATOM   2298 C  C   . TRP   B 1 75  ? -9.44600  15.57500  30.70100  1.000 18.75003 ? 87  TRP   B C   1 
ATOM   2299 O  O   . TRP   B 1 75  ? -10.42900 16.27500  30.98300  1.000 21.45035 ? 87  TRP   B O   1 
ATOM   2300 C  CB  . TRP   B 1 75  ? -8.05800  17.68600  30.63100  1.000 19.67299 ? 87  TRP   B CB  1 
ATOM   2301 C  CG  . TRP   B 1 75  ? -7.90400  17.97200  32.09700  1.000 20.03196 ? 87  TRP   B CG  1 
ATOM   2302 C  CD1 . TRP   B 1 75  ? -7.96500  17.08400  33.13600  1.000 23.14922 ? 87  TRP   B CD1 1 
ATOM   2303 C  CD2 . TRP   B 1 75  ? -7.67400  19.25600  32.67300  1.000 19.25280 ? 87  TRP   B CD2 1 
ATOM   2304 N  NE1 . TRP   B 1 75  ? -7.77900  17.75300  34.33600  1.000 22.01430 ? 87  TRP   B NE1 1 
ATOM   2305 C  CE2 . TRP   B 1 75  ? -7.60000  19.08400  34.06900  1.000 22.61844 ? 87  TRP   B CE2 1 
ATOM   2306 C  CE3 . TRP   B 1 75  ? -7.50700  20.53700  32.13900  1.000 24.59104 ? 87  TRP   B CE3 1 
ATOM   2307 C  CZ2 . TRP   B 1 75  ? -7.37700  20.15300  34.93900  1.000 23.13812 ? 87  TRP   B CZ2 1 
ATOM   2308 C  CZ3 . TRP   B 1 75  ? -7.29400  21.59500  33.00400  1.000 26.59213 ? 87  TRP   B CZ3 1 
ATOM   2309 C  CH2 . TRP   B 1 75  ? -7.23400  21.39300  34.38600  1.000 26.15839 ? 87  TRP   B CH2 1 
ATOM   2310 N  N   . GLY   B 1 76  ? -9.45100  14.25200  30.78000  1.000 17.79884 ? 88  GLY   B N   1 
ATOM   2311 C  CA  . GLY   B 1 76  ? -10.61300 13.52600  31.25300  1.000 20.38653 ? 88  GLY   B CA  1 
ATOM   2312 C  C   . GLY   B 1 76  ? -11.25100 12.63100  30.21000  1.000 21.27743 ? 88  GLY   B C   1 
ATOM   2313 O  O   . GLY   B 1 76  ? -11.09000 12.85000  29.00300  1.000 18.96876 ? 88  GLY   B O   1 
ATOM   2314 N  N   . ALA   B 1 77  ? -12.00100 11.63500  30.67900  1.000 22.04708 ? 89  ALA   B N   1 
ATOM   2315 C  CA  . ALA   B 1 77  ? -12.63100 10.66100  29.79000  1.000 23.08526 ? 89  ALA   B CA  1 
ATOM   2316 C  C   . ALA   B 1 77  ? -13.65800 11.31600  28.87100  1.000 24.22628 ? 89  ALA   B C   1 
ATOM   2317 O  O   . ALA   B 1 77  ? -13.66800 11.06800  27.65900  1.000 24.33896 ? 89  ALA   B O   1 
ATOM   2318 C  CB  . ALA   B 1 77  ? -13.27800 9.54900   30.62100  1.000 26.28159 ? 89  ALA   B CB  1 
ATOM   2319 N  N   . LYS   B 1 78  ? -14.54000 12.15000  29.43200  1.000 23.85796 ? 90  LYS   B N   1 
ATOM   2320 C  CA  . LYS   B 1 78  ? -15.59600 12.76400  28.63000  1.000 28.43465 ? 90  LYS   B CA  1 
ATOM   2321 C  C   . LYS   B 1 78  ? -15.01200 13.68200  27.56300  1.000 24.29091 ? 90  LYS   B C   1 
ATOM   2322 O  O   . LYS   B 1 78  ? -15.40700 13.62200  26.39000  1.000 22.43120 ? 90  LYS   B O   1 
ATOM   2323 C  CB  . LYS   B 1 78  ? -16.57200 13.52500  29.53800  1.000 29.39474 ? 90  LYS   B CB  1 
ATOM   2324 C  CG  . LYS   B 1 78  ? -17.76200 14.14200  28.81900  1.000 33.77171 ? 90  LYS   B CG  1 
ATOM   2325 C  CD  . LYS   B 1 78  ? -18.64100 14.92200  29.78700  1.000 43.06795 ? 90  LYS   B CD  1 
ATOM   2326 C  CE  . LYS   B 1 78  ? -18.88900 16.34200  29.30700  1.000 55.94313 ? 90  LYS   B CE  1 
ATOM   2327 N  NZ  . LYS   B 1 78  ? -18.54300 17.34700  30.35500  1.000 55.42570 ? 90  LYS   B NZ  1 
ATOM   2328 N  N   . ASN   B 1 79  ? -14.06800 14.54500  27.95000  1.000 21.14567 ? 91  ASN   B N   1 
ATOM   2329 C  CA  . ASN   B 1 79  ? -13.42500 15.41300  26.97200  1.000 19.54347 ? 91  ASN   B CA  1 
ATOM   2330 C  C   . ASN   B 1 79  ? -12.69200 14.59400  25.92200  1.000 18.53719 ? 91  ASN   B C   1 
ATOM   2331 O  O   . ASN   B 1 79  ? -12.70400 14.94500  24.74200  1.000 18.94624 ? 91  ASN   B O   1 
ATOM   2332 C  CB  . ASN   B 1 79  ? -12.43900 16.35300  27.66000  1.000 20.46891 ? 91  ASN   B CB  1 
ATOM   2333 C  CG  . ASN   B 1 79  ? -13.10800 17.53200  28.34000  1.000 27.50194 ? 91  ASN   B CG  1 
ATOM   2334 O  OD1 . ASN   B 1 79  ? -14.32300 17.69000  28.28700  1.000 26.23701 ? 91  ASN   B OD1 1 
ATOM   2335 N  ND2 . ASN   B 1 79  ? -12.30400 18.37700  28.97900  1.000 26.39900 ? 91  ASN   B ND2 1 
ATOM   2336 N  N   . THR   B 1 80  ? -12.04100 13.50500  26.33100  1.000 18.98656 ? 92  THR   B N   1 
ATOM   2337 C  CA  . THR   B 1 80  ? -11.25000 12.73200  25.37200  1.000 17.93674 ? 92  THR   B CA  1 
ATOM   2338 C  C   . THR   B 1 80  ? -12.14300 11.99300  24.37600  1.000 19.96564 ? 92  THR   B C   1 
ATOM   2339 O  O   . THR   B 1 80  ? -11.79700 11.86900  23.19400  1.000 18.61590 ? 92  THR   B O   1 
ATOM   2340 C  CB  . THR   B 1 80  ? -10.26900 11.81500  26.10300  1.000 17.37946 ? 92  THR   B CB  1 
ATOM   2341 O  OG1 . THR   B 1 80  ? -9.38800  12.63100  26.89800  1.000 18.46882 ? 92  THR   B OG1 1 
ATOM   2342 C  CG2 . THR   B 1 80  ? -9.43700  10.99600  25.13800  1.000 17.04731 ? 92  THR   B CG2 1 
ATOM   2343 N  N   . ALA   B 1 81  ? -13.30600 11.51300  24.82500  1.000 20.24075 ? 93  ALA   B N   1 
ATOM   2344 C  CA  . ALA   B 1 81  ? -14.26400 10.95700  23.87700  1.000 22.48167 ? 93  ALA   B CA  1 
ATOM   2345 C  C   . ALA   B 1 81  ? -14.74000 12.02600  22.90600  1.000 22.28554 ? 93  ALA   B C   1 
ATOM   2346 O  O   . ALA   B 1 81  ? -14.87300 11.77100  21.70100  1.000 22.48750 ? 93  ALA   B O   1 
ATOM   2347 C  CB  . ALA   B 1 81  ? -15.44100 10.32300  24.62200  1.000 24.65150 ? 93  ALA   B CB  1 
ATOM   2348 N  N   . ALA   B 1 82  ? -14.97600 13.24000  23.40500  1.000 18.91914 ? 94  ALA   B N   1 
ATOM   2349 C  CA  . ALA   B 1 82  ? -15.36600 14.33400  22.53000  1.000 19.42320 ? 94  ALA   B CA  1 
ATOM   2350 C  C   . ALA   B 1 82  ? -14.24400 14.67900  21.56400  1.000 21.81536 ? 94  ALA   B C   1 
ATOM   2351 O  O   . ALA   B 1 82  ? -14.49300 15.00600  20.39700  1.000 21.70212 ? 94  ALA   B O   1 
ATOM   2352 C  CB  . ALA   B 1 82  ? -15.77600 15.55300  23.35700  1.000 22.69582 ? 94  ALA   B CB  1 
ATOM   2353 N  N   . LEU   B 1 83  ? -12.99700 14.59400  22.03400  1.000 19.76666 ? 95  LEU   B N   1 
ATOM   2354 C  CA  . LEU   B 1 83  ? -11.85200 14.83600  21.16700  1.000 18.14951 ? 95  LEU   B CA  1 
ATOM   2355 C  C   . LEU   B 1 83  ? -11.83700 13.85600  19.99700  1.000 17.83292 ? 95  LEU   B C   1 
ATOM   2356 O  O   . LEU   B 1 83  ? -11.68700 14.26000  18.83800  1.000 17.05498 ? 95  LEU   B O   1 
ATOM   2357 C  CB  . LEU   B 1 83  ? -10.56300 14.72600  21.98800  1.000 17.16388 ? 95  LEU   B CB  1 
ATOM   2358 C  CG  . LEU   B 1 83  ? -9.24200  14.62100  21.21900  1.000 15.49150 ? 95  LEU   B CG  1 
ATOM   2359 C  CD1 . LEU   B 1 83  ? -8.96300  15.88000  20.41300  1.000 17.97254 ? 95  LEU   B CD1 1 
ATOM   2360 C  CD2 . LEU   B 1 83  ? -8.09300  14.32300  22.19900  1.000 17.74729 ? 95  LEU   B CD2 1 
ATOM   2361 N  N   . LEU   B 1 84  ? -12.01400 12.56100  20.27500  1.000 16.33857 ? 96  LEU   B N   1 
ATOM   2362 C  CA  . LEU   B 1 84  ? -12.02500 11.58900  19.18600  1.000 16.48036 ? 96  LEU   B CA  1 
ATOM   2363 C  C   . LEU   B 1 84  ? -13.17700 11.85700  18.22100  1.000 18.03697 ? 96  LEU   B C   1 
ATOM   2364 O  O   . LEU   B 1 84  ? -13.00700 11.75200  17.00000  1.000 18.74221 ? 96  LEU   B O   1 
ATOM   2365 C  CB  . LEU   B 1 84  ? -12.11300 10.17300  19.74800  1.000 17.60752 ? 96  LEU   B CB  1 
ATOM   2366 C  CG  . LEU   B 1 84  ? -10.88700 9.69000   20.52400  1.000 18.15013 ? 96  LEU   B CG  1 
ATOM   2367 C  CD1 . LEU   B 1 84  ? -11.11200 8.27800   21.03700  1.000 21.00858 ? 96  LEU   B CD1 1 
ATOM   2368 C  CD2 . LEU   B 1 84  ? -9.62500  9.75800   19.67100  1.000 18.87347 ? 96  LEU   B CD2 1 
ATOM   2369 N  N   . ALA   B 1 85  ? -14.34900 12.22300  18.74800  1.000 18.44208 ? 97  ALA   B N   1 
ATOM   2370 C  CA  . ALA   B 1 85  ? -15.47900 12.52600  17.87400  1.000 19.34197 ? 97  ALA   B CA  1 
ATOM   2371 C  C   . ALA   B 1 85  ? -15.18000 13.74000  17.01100  1.000 19.31207 ? 97  ALA   B C   1 
ATOM   2372 O  O   . ALA   B 1 85  ? -15.51800 13.76700  15.82300  1.000 21.22070 ? 97  ALA   B O   1 
ATOM   2373 C  CB  . ALA   B 1 85  ? -16.73300 12.77400  18.71100  1.000 23.04288 ? 97  ALA   B CB  1 
ATOM   2374 N  N   . GLU   B 1 86  ? -14.54000 14.75800  17.58900  1.000 18.98626 ? 98  GLU   B N   1 
ATOM   2375 C  CA  . GLU   B 1 86  ? -14.21600 15.95300  16.82100  1.000 18.24169 ? 98  GLU   B CA  1 
ATOM   2376 C  C   . GLU   B 1 86  ? -13.16000 15.65600  15.76500  1.000 18.98987 ? 98  GLU   B C   1 
ATOM   2377 O  O   . GLU   B 1 86  ? -13.23500 16.17100  14.64400  1.000 20.24691 ? 98  GLU   B O   1 
ATOM   2378 C  CB  . GLU   B 1 86  ? -13.75900 17.06400  17.76700  1.000 22.91514 ? 98  GLU   B CB  1 
ATOM   2379 C  CG  . GLU   B 1 86  ? -13.91900 18.48000  17.23900  1.000 29.55814 ? 98  GLU   B CG  1 
ATOM   2380 C  CD  . GLU   B 1 86  ? -15.35900 18.85900  16.90200  1.000 24.66913 ? 98  GLU   B CD  1 
ATOM   2381 O  OE1 . GLU   B 1 86  ? -16.27500 18.46700  17.65200  1.000 34.11084 ? 98  GLU   B OE1 1 
ATOM   2382 O  OE2 . GLU   B 1 86  ? -15.55900 19.57800  15.90600  1.000 37.55096 ? 98  GLU   B OE2 1 
ATOM   2383 N  N   . ILE   B 1 87  ? -12.17800 14.80900  16.09200  1.000 19.53373 ? 99  ILE   B N   1 
ATOM   2384 C  CA  . ILE   B 1 87  ? -11.18600 14.41200  15.09400  1.000 18.19429 ? 99  ILE   B CA  1 
ATOM   2385 C  C   . ILE   B 1 87  ? -11.86700 13.70000  13.93400  1.000 22.50949 ? 99  ILE   B C   1 
ATOM   2386 O  O   . ILE   B 1 87  ? -11.57700 13.96400  12.76100  1.000 21.04960 ? 99  ILE   B O   1 
ATOM   2387 C  CB  . ILE   B 1 87  ? -10.08400 13.54700  15.74200  1.000 18.98647 ? 99  ILE   B CB  1 
ATOM   2388 C  CG1 . ILE   B 1 87  ? -9.15900  14.41400  16.59700  1.000 15.99798 ? 99  ILE   B CG1 1 
ATOM   2389 C  CG2 . ILE   B 1 87  ? -9.28400  12.76500  14.69100  1.000 17.50356 ? 99  ILE   B CG2 1 
ATOM   2390 C  CD1 . ILE   B 1 87  ? -8.15800  13.60600  17.40900  1.000 18.57771 ? 99  ILE   B CD1 1 
ATOM   2391 N  N   . GLU   B 1 88  ? -12.79900 12.80400  14.24600  1.000 18.98086 ? 100 GLU   B N   1 
ATOM   2392 C  CA  . GLU   B 1 88  ? -13.49300 12.07500  13.19300  1.000 20.72133 ? 100 GLU   B CA  1 
ATOM   2393 C  C   . GLU   B 1 88  ? -14.33500 13.00900  12.32900  1.000 21.85904 ? 100 GLU   B C   1 
ATOM   2394 O  O   . GLU   B 1 88  ? -14.38200 12.85300  11.10400  1.000 23.40434 ? 100 GLU   B O   1 
ATOM   2395 C  CB  . GLU   B 1 88  ? -14.32400 10.94600  13.79900  1.000 20.04069 ? 100 GLU   B CB  1 
ATOM   2396 C  CG  . GLU   B 1 88  ? -15.34300 10.36500  12.83000  1.000 24.31785 ? 100 GLU   B CG  1 
ATOM   2397 C  CD  . GLU   B 1 88  ? -14.71000 9.66100   11.65700  1.000 32.68711 ? 100 GLU   B CD  1 
ATOM   2398 O  OE1 . GLU   B 1 88  ? -13.48100 9.40200   11.67100  1.000 25.59811 ? 100 GLU   B OE1 1 
ATOM   2399 O  OE2 . GLU   B 1 88  ? -15.45600 9.39200   10.69000  1.000 28.84202 ? 100 GLU   B OE2 1 
ATOM   2400 N  N   . LYS   B 1 89  ? -14.98500 14.00300  12.94100  1.000 20.38196 ? 101 LYS   B N   1 
ATOM   2401 C  CA  . LYS   B 1 89  ? -15.81100 14.93500  12.17600  1.000 23.09731 ? 101 LYS   B CA  1 
ATOM   2402 C  C   . LYS   B 1 89  ? -14.96600 15.87100  11.31200  1.000 23.78525 ? 101 LYS   B C   1 
ATOM   2403 O  O   . LYS   B 1 89  ? -15.32600 16.15100  10.16300  1.000 26.67350 ? 101 LYS   B O   1 
ATOM   2404 C  CB  . LYS   B 1 89  ? -16.71600 15.72300  13.12500  1.000 25.47419 ? 101 LYS   B CB  1 
ATOM   2405 C  CG  . LYS   B 1 89  ? -17.23500 17.05100  12.58900  1.000 30.96013 ? 101 LYS   B CG  1 
ATOM   2406 C  CD  . LYS   B 1 89  ? -18.12300 17.72000  13.62600  1.000 34.33202 ? 101 LYS   B CD  1 
ATOM   2407 C  CE  . LYS   B 1 89  ? -18.90800 18.87300  13.03100  1.000 39.24142 ? 101 LYS   B CE  1 
ATOM   2408 N  NZ  . LYS   B 1 89  ? -19.79000 19.48500  14.05900  1.000 46.03771 ? 101 LYS   B NZ  1 
ATOM   2409 N  N   . GLN   B 1 90  ? -13.84800 16.38400  11.83400  1.000 21.10444 ? 102 GLN   B N   1 
ATOM   2410 C  CA  . GLN   B 1 90  ? -13.11400 17.40500  11.09000  1.000 21.23933 ? 102 GLN   B CA  1 
ATOM   2411 C  C   . GLN   B 1 90  ? -11.93100 16.88900  10.28400  1.000 21.33145 ? 102 GLN   B C   1 
ATOM   2412 O  O   . GLN   B 1 90  ? -11.51700 17.55800  9.32900   1.000 24.45902 ? 102 GLN   B O   1 
ATOM   2413 C  CB  . GLN   B 1 90  ? -12.66900 18.57900  11.97200  1.000 24.63213 ? 102 GLN   B CB  1 
ATOM   2414 C  CG  . GLN   B 1 90  ? -13.70500 19.08900  12.93900  1.000 26.33321 ? 102 GLN   B CG  1 
ATOM   2415 C  CD  . GLN   B 1 90  ? -13.24400 20.34600  13.64100  1.000 41.61171 ? 102 GLN   B CD  1 
ATOM   2416 O  OE1 . GLN   B 1 90  ? -12.51300 21.15700  13.06700  1.000 41.26630 ? 102 GLN   B OE1 1 
ATOM   2417 N  NE2 . GLN   B 1 90  ? -13.68300 20.52900  14.87800  1.000 38.84307 ? 102 GLN   B NE2 1 
ATOM   2418 N  N   . ILE   B 1 91  ? -11.36800 15.74200  10.63500  1.000 20.22589 ? 103 ILE   B N   1 
ATOM   2419 C  CA  . ILE   B 1 91  ? -10.20800 15.18900  9.94600   1.000 19.83299 ? 103 ILE   B CA  1 
ATOM   2420 C  C   . ILE   B 1 91  ? -10.53400 13.85400  9.29400   1.000 23.49769 ? 103 ILE   B C   1 
ATOM   2421 O  O   . ILE   B 1 91  ? -10.17400 13.61100  8.13800   1.000 23.69367 ? 103 ILE   B O   1 
ATOM   2422 C  CB  . ILE   B 1 91  ? -8.98500  15.06900  10.89100  1.000 18.24173 ? 103 ILE   B CB  1 
ATOM   2423 C  CG1 . ILE   B 1 91  ? -8.68500  16.42200  11.53900  1.000 19.60439 ? 103 ILE   B CG1 1 
ATOM   2424 C  CG2 . ILE   B 1 91  ? -7.76900  14.52700  10.14400  1.000 17.69868 ? 103 ILE   B CG2 1 
ATOM   2425 C  CD1 . ILE   B 1 91  ? -7.58300  16.39300  12.58600  1.000 18.40447 ? 103 ILE   B CD1 1 
ATOM   2426 N  N   . GLY   B 1 92  ? -11.21400 12.97300  10.02300  1.000 18.96244 ? 104 GLY   B N   1 
ATOM   2427 C  CA  . GLY   B 1 92  ? -11.67900 11.72600  9.44200   1.000 23.19152 ? 104 GLY   B CA  1 
ATOM   2428 C  C   . GLY   B 1 92  ? -10.60700 10.69700  9.18300   1.000 25.43540 ? 104 GLY   B C   1 
ATOM   2429 O  O   . GLY   B 1 92  ? -10.79100 9.83100   8.32600   1.000 28.52418 ? 104 GLY   B O   1 
ATOM   2430 N  N   . LEU   B 1 93  ? -9.48300  10.76600  9.88900   1.000 20.23221 ? 105 LEU   B N   1 
ATOM   2431 C  CA  . LEU   B 1 93  ? -8.45000  9.74700   9.83400   1.000 18.19613 ? 105 LEU   B CA  1 
ATOM   2432 C  C   . LEU   B 1 93  ? -8.33500  9.11700   11.21400  1.000 19.20317 ? 105 LEU   B C   1 
ATOM   2433 O  O   . LEU   B 1 93  ? -8.67300  9.76400   12.21200  1.000 19.94280 ? 105 LEU   B O   1 
ATOM   2434 C  CB  . LEU   B 1 93  ? -7.09300  10.35200  9.45500   1.000 18.74430 ? 105 LEU   B CB  1 
ATOM   2435 C  CG  . LEU   B 1 93  ? -6.98600  10.99300  8.06700   1.000 20.65554 ? 105 LEU   B CG  1 
ATOM   2436 C  CD1 . LEU   B 1 93  ? -5.63800  11.65600  7.88100   1.000 25.46197 ? 105 LEU   B CD1 1 
ATOM   2437 C  CD2 . LEU   B 1 93  ? -7.20900  9.96400   6.97200   1.000 27.52142 ? 105 LEU   B CD2 1 
ATOM   2438 N  N   . PRO   B 1 94  ? -7.87300  7.87000   11.31200  1.000 20.26123 ? 106 PRO   B N   1 
ATOM   2439 C  CA  . PRO   B 1 94  ? -7.81300  7.21600   12.62600  1.000 18.49927 ? 106 PRO   B CA  1 
ATOM   2440 C  C   . PRO   B 1 94  ? -6.60000  7.65900   13.42900  1.000 16.95796 ? 106 PRO   B C   1 
ATOM   2441 O  O   . PRO   B 1 94  ? -5.48900  7.78900   12.90900  1.000 16.87386 ? 106 PRO   B O   1 
ATOM   2442 C  CB  . PRO   B 1 94  ? -7.69800  5.72800   12.27200  1.000 21.87560 ? 106 PRO   B CB  1 
ATOM   2443 C  CG  . PRO   B 1 94  ? -6.98000  5.72900   10.94800  1.000 19.19286 ? 106 PRO   B CG  1 
ATOM   2444 C  CD  . PRO   B 1 94  ? -7.51900  6.94300   10.21400  1.000 19.64348 ? 106 PRO   B CD  1 
ATOM   2445 N  N   . VAL   B 1 95  ? -6.82300  7.87400   14.72300  1.000 18.12905 ? 107 VAL   B N   1 
ATOM   2446 C  CA  . VAL   B 1 95  ? -5.71200  8.04700   15.65500  1.000 15.81954 ? 107 VAL   B CA  1 
ATOM   2447 C  C   . VAL   B 1 95  ? -5.17500  6.66200   15.98900  1.000 16.18086 ? 107 VAL   B C   1 
ATOM   2448 O  O   . VAL   B 1 95  ? -5.89900  5.83000   16.54300  1.000 18.30984 ? 107 VAL   B O   1 
ATOM   2449 C  CB  . VAL   B 1 95  ? -6.18000  8.76900   16.92600  1.000 16.26575 ? 107 VAL   B CB  1 
ATOM   2450 C  CG1 . VAL   B 1 95  ? -5.01900  8.89800   17.89500  1.000 17.45624 ? 107 VAL   B CG1 1 
ATOM   2451 C  CG2 . VAL   B 1 95  ? -6.76300  10.14100  16.59900  1.000 18.70363 ? 107 VAL   B CG2 1 
ATOM   2452 N  N   . THR   B 1 96  ? -3.91600  6.40500   15.65200  1.000 14.63328 ? 108 THR   B N   1 
ATOM   2453 C  CA  . THR   B 1 96  ? -3.33400  5.09200   15.90700  1.000 15.73180 ? 108 THR   B CA  1 
ATOM   2454 C  C   . THR   B 1 96  ? -2.33700  5.06500   17.05600  1.000 16.80390 ? 108 THR   B C   1 
ATOM   2455 O  O   . THR   B 1 96  ? -2.17100  4.02000   17.68800  1.000 15.17543 ? 108 THR   B O   1 
ATOM   2456 C  CB  . THR   B 1 96  ? -2.67000  4.54100   14.64000  1.000 17.39643 ? 108 THR   B CB  1 
ATOM   2457 O  OG1 . THR   B 1 96  ? -1.71200  5.48800   14.16300  1.000 20.15462 ? 108 THR   B OG1 1 
ATOM   2458 C  CG2 . THR   B 1 96  ? -3.72000  4.30700   13.55400  1.000 21.85463 ? 108 THR   B CG2 1 
ATOM   2459 N  N   . ARG   B 1 97  ? -1.68600  6.18300   17.36800  1.000 14.53869 ? 109 ARG   B N   1 
ATOM   2460 C  CA  . ARG   B 1 97  ? -0.80200  6.24700   18.51800  1.000 13.45500 ? 109 ARG   B CA  1 
ATOM   2461 C  C   . ARG   B 1 97  ? -1.05600  7.55000   19.25200  1.000 12.73823 ? 109 ARG   B C   1 
ATOM   2462 O  O   . ARG   B 1 97  ? -1.44100  8.55300   18.64700  1.000 14.23021 ? 109 ARG   B O   1 
ATOM   2463 C  CB  . ARG   B 1 97  ? 0.67800   6.15300   18.13800  1.000 13.42373 ? 109 ARG   B CB  1 
ATOM   2464 C  CG  . ARG   B 1 97  ? 1.03300   4.89900   17.32900  1.000 15.70965 ? 109 ARG   B CG  1 
ATOM   2465 C  CD  . ARG   B 1 97  ? 2.52500   4.83400   17.05200  1.000 17.39337 ? 109 ARG   B CD  1 
ATOM   2466 N  NE  . ARG   B 1 97  ? 2.88900   5.74800   15.97100  1.000 19.09984 ? 109 ARG   B NE  1 
ATOM   2467 C  CZ  . ARG   B 1 97  ? 4.11400   5.88500   15.47900  1.000 21.29720 ? 109 ARG   B CZ  1 
ATOM   2468 N  NH1 . ARG   B 1 97  ? 5.13400   5.17900   15.95100  1.000 22.43592 ? 109 ARG   B NH1 1 
ATOM   2469 N  NH2 . ARG   B 1 97  ? 4.31900   6.74000   14.47500  1.000 24.00451 ? 109 ARG   B NH2 1 
ATOM   2470 N  N   . ALA   B 1 98  ? -0.80700  7.53500   20.55700  1.000 12.48264 ? 110 ALA   B N   1 
ATOM   2471 C  CA  . ALA   B 1 98  ? -0.86000  8.74500   21.36600  1.000 13.30758 ? 110 ALA   B CA  1 
ATOM   2472 C  C   . ALA   B 1 98  ? 0.34300   8.76000   22.29500  1.000 11.67788 ? 110 ALA   B C   1 
ATOM   2473 O  O   . ALA   B 1 98  ? 0.76400   7.71500   22.79400  1.000 13.20587 ? 110 ALA   B O   1 
ATOM   2474 C  CB  . ALA   B 1 98  ? -2.14500  8.81000   22.20300  1.000 14.46123 ? 110 ALA   B CB  1 
ATOM   2475 N  N   . VAL   B 1 99  ? 0.85500   9.96000   22.56600  1.000 12.43746 ? 111 VAL   B N   1 
ATOM   2476 C  CA  . VAL   B 1 99  ? 1.94100   10.17100  23.51700  1.000 11.78711 ? 111 VAL   B CA  1 
ATOM   2477 C  C   . VAL   B 1 99  ? 1.43700   11.13500  24.58200  1.000 11.52277 ? 111 VAL   B C   1 
ATOM   2478 O  O   . VAL   B 1 99  ? 0.88400   12.19400  24.25200  1.000 12.51578 ? 111 VAL   B O   1 
ATOM   2479 C  CB  . VAL   B 1 99  ? 3.17100   10.76600  22.80100  1.000 11.77148 ? 111 VAL   B CB  1 
ATOM   2480 C  CG1 . VAL   B 1 99  ? 4.19700   11.29600  23.79900  1.000 14.65580 ? 111 VAL   B CG1 1 
ATOM   2481 C  CG2 . VAL   B 1 99  ? 3.77500   9.75000   21.84000  1.000 14.44186 ? 111 VAL   B CG2 1 
ATOM   2482 N  N   . SER   B 1 100 ? 1.63600   10.78700  25.85600  1.000 12.11538 ? 112 SER   B N   1 
ATOM   2483 C  CA  . SER   B 1 100 ? 1.35700   11.70700  26.95400  1.000 12.72686 ? 112 SER   B CA  1 
ATOM   2484 C  C   . SER   B 1 100 ? 2.67200   12.31200  27.43100  1.000 12.35038 ? 112 SER   B C   1 
ATOM   2485 O  O   . SER   B 1 100 ? 3.64900   11.59000  27.66100  1.000 12.79803 ? 112 SER   B O   1 
ATOM   2486 C  CB  . SER   B 1 100 ? 0.65800   10.97000  28.09700  1.000 13.28756 ? 112 SER   B CB  1 
ATOM   2487 O  OG  . SER   B 1 100 ? -0.66900  10.62300  27.70300  1.000 13.11040 ? 112 SER   B OG  1 
ATOM   2488 N  N   . THR   B 1 101 ? 2.69300   13.64100  27.57200  1.000 10.72647 ? 113 THR   B N   1 
ATOM   2489 C  CA  . THR   B 1 101 ? 3.95000   14.34100  27.79000  1.000 11.61180 ? 113 THR   B CA  1 
ATOM   2490 C  C   . THR   B 1 101 ? 4.34400   14.50200  29.25000  1.000 12.17147 ? 113 THR   B C   1 
ATOM   2491 O  O   . THR   B 1 101 ? 5.48600   14.88900  29.51100  1.000 13.22187 ? 113 THR   B O   1 
ATOM   2492 C  CB  . THR   B 1 101 ? 3.96900   15.70900  27.08000  1.000 12.25291 ? 113 THR   B CB  1 
ATOM   2493 O  OG1 . THR   B 1 101 ? 2.87300   16.52100  27.51700  1.000 11.93903 ? 113 THR   B OG1 1 
ATOM   2494 C  CG2 . THR   B 1 101 ? 3.89700   15.53900  25.58500  1.000 12.79014 ? 113 THR   B CG2 1 
ATOM   2495 N  N   . HIS   B 1 102 ? 3.44000   14.23500  30.19800  1.000 11.40865 ? 114 HIS   B N   1 
ATOM   2496 C  CA  . HIS   B 1 102 ? 3.80400   14.01700  31.59900  1.000 11.79445 ? 114 HIS   B CA  1 
ATOM   2497 C  C   . HIS   B 1 102 ? 2.63000   13.34300  32.29000  1.000 12.29319 ? 114 HIS   B C   1 
ATOM   2498 O  O   . HIS   B 1 102 ? 1.60400   13.06500  31.67000  1.000 12.39905 ? 114 HIS   B O   1 
ATOM   2499 C  CB  . HIS   B 1 102 ? 4.33900   15.26800  32.32300  1.000 12.78260 ? 114 HIS   B CB  1 
ATOM   2500 C  CG  . HIS   B 1 102 ? 3.32200   16.32100  32.61400  1.000 13.04309 ? 114 HIS   B CG  1 
ATOM   2501 N  ND1 . HIS   B 1 102 ? 2.96200   17.28700  31.69700  1.000 12.37348 ? 114 HIS   B ND1 1 
ATOM   2502 C  CD2 . HIS   B 1 102 ? 2.64300   16.61000  33.75100  1.000 12.12761 ? 114 HIS   B CD2 1 
ATOM   2503 C  CE1 . HIS   B 1 102 ? 2.08100   18.11000  32.24100  1.000 12.51781 ? 114 HIS   B CE1 1 
ATOM   2504 N  NE2 . HIS   B 1 102 ? 1.86900   17.72000  33.48600  1.000 12.93733 ? 114 HIS   B NE2 1 
ATOM   2505 N  N   . PHE   B 1 103 ? 2.77100   13.11600  33.59900  1.000 11.45899 ? 115 PHE   B N   1 
ATOM   2506 C  CA  . PHE   B 1 103 ? 1.90800   12.16100  34.28600  1.000 12.52912 ? 115 PHE   B CA  1 
ATOM   2507 C  C   . PHE   B 1 103 ? 0.62400   12.75700  34.85100  1.000 13.26142 ? 115 PHE   B C   1 
ATOM   2508 O  O   . PHE   B 1 103 ? -0.20100  11.99100  35.36800  1.000 13.87018 ? 115 PHE   B O   1 
ATOM   2509 C  CB  . PHE   B 1 103 ? 2.67900   11.43400  35.39300  1.000 13.79787 ? 115 PHE   B CB  1 
ATOM   2510 C  CG  . PHE   B 1 103 ? 2.93000   12.27400  36.61600  1.000 13.99012 ? 115 PHE   B CG  1 
ATOM   2511 C  CD1 . PHE   B 1 103 ? 3.98700   13.17200  36.64600  1.000 13.99137 ? 115 PHE   B CD1 1 
ATOM   2512 C  CD2 . PHE   B 1 103 ? 2.12100   12.15400  37.74100  1.000 14.19844 ? 115 PHE   B CD2 1 
ATOM   2513 C  CE1 . PHE   B 1 103 ? 4.24000   13.93100  37.78100  1.000 15.00122 ? 115 PHE   B CE1 1 
ATOM   2514 C  CE2 . PHE   B 1 103 ? 2.35900   12.90800  38.88200  1.000 17.28889 ? 115 PHE   B CE2 1 
ATOM   2515 C  CZ  . PHE   B 1 103 ? 3.41500   13.80500  38.90600  1.000 15.13378 ? 115 PHE   B CZ  1 
ATOM   2516 N  N   . HIS   B 1 104 ? 0.43100   14.07700  34.79800  1.000 13.36873 ? 116 HIS   B N   1 
ATOM   2517 C  CA  . HIS   B 1 104 ? -0.74300  14.67400  35.42500  1.000 13.73896 ? 116 HIS   B CA  1 
ATOM   2518 C  C   . HIS   B 1 104 ? -2.00200  14.43400  34.58100  1.000 14.65883 ? 116 HIS   B C   1 
ATOM   2519 O  O   . HIS   B 1 104 ? -1.93800  14.08500  33.39700  1.000 15.43699 ? 116 HIS   B O   1 
ATOM   2520 C  CB  . HIS   B 1 104 ? -0.52500  16.16300  35.66300  1.000 15.03465 ? 116 HIS   B CB  1 
ATOM   2521 C  CG  . HIS   B 1 104 ? 0.45600   16.46300  36.75600  1.000 14.67027 ? 116 HIS   B CG  1 
ATOM   2522 N  ND1 . HIS   B 1 104 ? 1.26900   17.56800  36.73000  1.000 15.42503 ? 116 HIS   B ND1 1 
ATOM   2523 C  CD2 . HIS   B 1 104 ? 0.76100   15.81300  37.90100  1.000 20.42225 ? 116 HIS   B CD2 1 
ATOM   2524 C  CE1 . HIS   B 1 104 ? 2.02400   17.60500  37.80600  1.000 16.70332 ? 116 HIS   B CE1 1 
ATOM   2525 N  NE2 . HIS   B 1 104 ? 1.74000   16.54500  38.53500  1.000 18.47319 ? 116 HIS   B NE2 1 
ATOM   2526 N  N   . ASP   B 1 105 ? -3.16800  14.63900  35.21000  1.000 16.27985 ? 117 ASP   B N   1 
ATOM   2527 C  CA  . ASP   B 1 105 ? -4.43600  14.24900  34.59100  1.000 16.01257 ? 117 ASP   B CA  1 
ATOM   2528 C  C   . ASP   B 1 105 ? -4.74600  14.99500  33.30300  1.000 17.62991 ? 117 ASP   B C   1 
ATOM   2529 O  O   . ASP   B 1 105 ? -5.48600  14.48000  32.45700  1.000 16.20078 ? 117 ASP   B O   1 
ATOM   2530 C  CB  . ASP   B 1 105 ? -5.58900  14.43800  35.57200  1.000 20.20764 ? 117 ASP   B CB  1 
ATOM   2531 C  CG  . ASP   B 1 105 ? -5.98500  13.15200  36.23400  1.000 37.95544 ? 117 ASP   B CG  1 
ATOM   2532 O  OD1 . ASP   B 1 105 ? -6.32000  12.19600  35.49900  1.000 38.59384 ? 117 ASP   B OD1 1 
ATOM   2533 O  OD2 . ASP   B 1 105 ? -5.96100  13.09100  37.48100  1.000 56.33517 ? 117 ASP   B OD2 1 
ATOM   2534 N  N   . ASP   B 1 106 ? -4.22500  16.20800  33.12800  1.000 14.79332 ? 118 ASP   B N   1 
ATOM   2535 C  CA  . ASP   B 1 106 ? -4.50700  16.92400  31.89200  1.000 15.41776 ? 118 ASP   B CA  1 
ATOM   2536 C  C   . ASP   B 1 106 ? -3.76200  16.33700  30.70000  1.000 14.94200 ? 118 ASP   B C   1 
ATOM   2537 O  O   . ASP   B 1 106 ? -4.03200  16.72900  29.56000  1.000 16.06543 ? 118 ASP   B O   1 
ATOM   2538 C  CB  . ASP   B 1 106 ? -4.33300  18.45300  32.05100  1.000 14.60397 ? 118 ASP   B CB  1 
ATOM   2539 C  CG  . ASP   B 1 106 ? -2.89700  18.88300  32.26200  1.000 14.47375 ? 118 ASP   B CG  1 
ATOM   2540 O  OD1 . ASP   B 1 106 ? -2.00200  18.05400  32.53200  1.000 17.00821 ? 118 ASP   B OD1 1 
ATOM   2541 O  OD2 . ASP   B 1 106 ? -2.67600  20.08600  32.14900  1.000 16.08345 ? 118 ASP   B OD2 1 
ATOM   2542 N  N   . ARG   B 1 107 ? -2.85800  15.38800  30.94200  1.000 13.78082 ? 119 ARG   B N   1 
ATOM   2543 C  CA  . ARG   B 1 107 ? -2.12600  14.70200  29.88500  1.000 13.43237 ? 119 ARG   B CA  1 
ATOM   2544 C  C   . ARG   B 1 107 ? -2.49800  13.23800  29.73000  1.000 12.50662 ? 119 ARG   B C   1 
ATOM   2545 O  O   . ARG   B 1 107 ? -2.39100  12.71100  28.61600  1.000 13.68913 ? 119 ARG   B O   1 
ATOM   2546 C  CB  . ARG   B 1 107 ? -0.61400  14.74700  30.14500  1.000 12.17601 ? 119 ARG   B CB  1 
ATOM   2547 C  CG  . ARG   B 1 107 ? -0.05000  16.10600  30.52300  1.000 12.07109 ? 119 ARG   B CG  1 
ATOM   2548 C  CD  . ARG   B 1 107 ? -0.07400  17.08800  29.36600  1.000 13.77989 ? 119 ARG   B CD  1 
ATOM   2549 N  NE  . ARG   B 1 107 ? -1.00500  18.18900  29.62600  1.000 14.81876 ? 119 ARG   B NE  1 
ATOM   2550 C  CZ  . ARG   B 1 107 ? -1.45200  19.03100  28.70800  1.000 16.46656 ? 119 ARG   B CZ  1 
ATOM   2551 N  NH1 . ARG   B 1 107 ? -1.09000  18.92300  27.44200  1.000 15.89867 ? 119 ARG   B NH1 1 
ATOM   2552 N  NH2 . ARG   B 1 107 ? -2.25300  20.03300  29.07800  1.000 17.82680 ? 119 ARG   B NH2 1 
ATOM   2553 N  N   . VAL   B 1 108 ? -2.86200  12.55100  30.81800  1.000 12.96422 ? 120 VAL   B N   1 
ATOM   2554 C  CA  . VAL   B 1 108 ? -3.18300  11.12400  30.77600  1.000 14.69100 ? 120 VAL   B CA  1 
ATOM   2555 C  C   . VAL   B 1 108 ? -4.63800  10.82000  31.07000  1.000 14.10928 ? 120 VAL   B C   1 
ATOM   2556 O  O   . VAL   B 1 108 ? -5.06700  9.67100   30.84900  1.000 14.83742 ? 120 VAL   B O   1 
ATOM   2557 C  CB  . VAL   B 1 108 ? -2.28600  10.27800  31.70600  1.000 12.82770 ? 120 VAL   B CB  1 
ATOM   2558 C  CG1 . VAL   B 1 108 ? -0.81600  10.38000  31.31200  1.000 14.92711 ? 120 VAL   B CG1 1 
ATOM   2559 C  CG2 . VAL   B 1 108 ? -2.52700  10.62500  33.19100  1.000 14.36322 ? 120 VAL   B CG2 1 
ATOM   2560 N  N   . GLY   B 1 109 ? -5.39300  11.77000  31.60500  1.000 13.86022 ? 121 GLY   B N   1 
ATOM   2561 C  CA  . GLY   B 1 109 ? -6.79800  11.52600  31.88700  1.000 16.03898 ? 121 GLY   B CA  1 
ATOM   2562 C  C   . GLY   B 1 109 ? -7.54700  11.37900  30.58600  1.000 18.06653 ? 121 GLY   B C   1 
ATOM   2563 O  O   . GLY   B 1 109 ? -7.63300  12.33500  29.81500  1.000 16.95049 ? 121 GLY   B O   1 
ATOM   2564 N  N   . GLY   B 1 110 ? -8.07800  10.19000  30.32500  1.000 16.69789 ? 122 GLY   B N   1 
ATOM   2565 C  CA  . GLY   B 1 110 ? -8.62100  9.87400   29.01900  1.000 18.00225 ? 122 GLY   B CA  1 
ATOM   2566 C  C   . GLY   B 1 110 ? -7.85400  8.79500   28.28400  1.000 17.53585 ? 122 GLY   B C   1 
ATOM   2567 O  O   . GLY   B 1 110 ? -8.32400  8.32500   27.24100  1.000 17.12055 ? 122 GLY   B O   1 
ATOM   2568 N  N   . VAL   B 1 111 ? -6.69900  8.37400   28.81000  1.000 15.65192 ? 123 VAL   B N   1 
ATOM   2569 C  CA  . VAL   B 1 111 ? -5.93700  7.27200   28.22600  1.000 16.40988 ? 123 VAL   B CA  1 
ATOM   2570 C  C   . VAL   B 1 111 ? -6.79400  6.01400   28.08800  1.000 16.89995 ? 123 VAL   B C   1 
ATOM   2571 O  O   . VAL   B 1 111 ? -6.68600  5.27900   27.09400  1.000 18.15793 ? 123 VAL   B O   1 
ATOM   2572 C  CB  . VAL   B 1 111 ? -4.64300  7.04300   29.03500  1.000 16.29930 ? 123 VAL   B CB  1 
ATOM   2573 C  CG1 . VAL   B 1 111 ? -4.13700  5.59400   28.92400  1.000 17.71431 ? 123 VAL   B CG1 1 
ATOM   2574 C  CG2 . VAL   B 1 111 ? -3.56600  8.02000   28.56300  1.000 15.56415 ? 123 VAL   B CG2 1 
ATOM   2575 N  N   . ASP   B 1 112 ? -7.65000  5.73300   29.07600  1.000 16.91405 ? 124 ASP   B N   1 
ATOM   2576 C  CA  . ASP   B 1 112 ? -8.47200  4.52500   28.98700  1.000 19.05649 ? 124 ASP   B CA  1 
ATOM   2577 C  C   . ASP   B 1 112 ? -9.44500  4.61800   27.81300  1.000 16.38320 ? 124 ASP   B C   1 
ATOM   2578 O  O   . ASP   B 1 112 ? -9.68000  3.62500   27.10900  1.000 18.52258 ? 124 ASP   B O   1 
ATOM   2579 C  CB  . ASP   B 1 112 ? -9.22000  4.29300   30.30700  1.000 22.01331 ? 124 ASP   B CB  1 
ATOM   2580 C  CG  . ASP   B 1 112 ? -8.30200  3.85400   31.45300  1.000 27.10642 ? 124 ASP   B CG  1 
ATOM   2581 O  OD1 . ASP   B 1 112 ? -7.07900  3.66700   31.25000  1.000 26.44916 ? 124 ASP   B OD1 1 
ATOM   2582 O  OD2 . ASP   B 1 112 ? -8.81400  3.69700   32.58700  1.000 28.19451 ? 124 ASP   B OD2 1 
ATOM   2583 N  N   . VAL   B 1 113 ? -10.01700 5.80300   27.58500  1.000 16.85377 ? 125 VAL   B N   1 
ATOM   2584 C  CA  . VAL   B 1 113 ? -10.88000 6.01800   26.42200  1.000 18.43454 ? 125 VAL   B CA  1 
ATOM   2585 C  C   . VAL   B 1 113 ? -10.10800 5.77000   25.13000  1.000 20.36850 ? 125 VAL   B C   1 
ATOM   2586 O  O   . VAL   B 1 113 ? -10.58500 5.07400   24.22100  1.000 21.88298 ? 125 VAL   B O   1 
ATOM   2587 C  CB  . VAL   B 1 113 ? -11.49000 7.42900   26.47200  1.000 19.81502 ? 125 VAL   B CB  1 
ATOM   2588 C  CG1 . VAL   B 1 113 ? -12.01400 7.84800   25.09400  1.000 23.75163 ? 125 VAL   B CG1 1 
ATOM   2589 C  CG2 . VAL   B 1 113 ? -12.59800 7.47900   27.52400  1.000 22.66914 ? 125 VAL   B CG2 1 
ATOM   2590 N  N   . LEU   B 1 114 ? -8.89200  6.31700   25.03500  1.000 19.69031 ? 126 LEU   B N   1 
ATOM   2591 C  CA  . LEU   B 1 114 ? -8.06300  6.09900   23.85300  1.000 18.49610 ? 126 LEU   B CA  1 
ATOM   2592 C  C   . LEU   B 1 114 ? -7.79400  4.61500   23.63700  1.000 16.92452 ? 126 LEU   B C   1 
ATOM   2593 O  O   . LEU   B 1 114 ? -7.96600  4.09300   22.52700  1.000 19.06524 ? 126 LEU   B O   1 
ATOM   2594 C  CB  . LEU   B 1 114 ? -6.73600  6.85300   24.00500  1.000 17.90090 ? 126 LEU   B CB  1 
ATOM   2595 C  CG  . LEU   B 1 114 ? -6.77000  8.38100   24.05700  1.000 15.07583 ? 126 LEU   B CG  1 
ATOM   2596 C  CD1 . LEU   B 1 114 ? -5.34400  8.92500   24.24800  1.000 15.46316 ? 126 LEU   B CD1 1 
ATOM   2597 C  CD2 . LEU   B 1 114 ? -7.40200  8.91900   22.78400  1.000 18.86824 ? 126 LEU   B CD2 1 
ATOM   2598 N  N   . ARG   B 1 115 ? -7.37700  3.91700   24.69200  1.000 16.76241 ? 127 ARG   B N   1 
ATOM   2599 C  CA  . ARG   B 1 115 ? -7.06900  2.49700   24.55700  1.000 18.02204 ? 127 ARG   B CA  1 
ATOM   2600 C  C   . ARG   B 1 115 ? -8.29500  1.69000   24.12700  1.000 20.79153 ? 127 ARG   B C   1 
ATOM   2601 O  O   . ARG   B 1 115 ? -8.18800  0.79400   23.27600  1.000 19.34327 ? 127 ARG   B O   1 
ATOM   2602 C  CB  . ARG   B 1 115 ? -6.50900  1.97000   25.87600  1.000 18.01498 ? 127 ARG   B CB  1 
ATOM   2603 C  CG  . ARG   B 1 115 ? -6.22200  0.48700   25.85700  1.000 19.07781 ? 127 ARG   B CG  1 
ATOM   2604 C  CD  . ARG   B 1 115 ? -5.87000  -0.00400  27.22200  1.000 26.02907 ? 127 ARG   B CD  1 
ATOM   2605 N  NE  . ARG   B 1 115 ? -4.69900  0.68100   27.75000  1.000 25.11807 ? 127 ARG   B NE  1 
ATOM   2606 C  CZ  . ARG   B 1 115 ? -4.71800  1.53500   28.76200  1.000 27.32252 ? 127 ARG   B CZ  1 
ATOM   2607 N  NH1 . ARG   B 1 115 ? -5.84600  1.85300   29.38000  1.000 25.18004 ? 127 ARG   B NH1 1 
ATOM   2608 N  NH2 . ARG   B 1 115 ? -3.57700  2.09000   29.15800  1.000 24.50765 ? 127 ARG   B NH2 1 
ATOM   2609 N  N   . ALA   B 1 116 ? -9.46600  1.99900   24.69500  1.000 20.53716 ? 128 ALA   B N   1 
ATOM   2610 C  CA  . ALA   B 1 116 ? -10.68300 1.29100   24.30300  1.000 24.41505 ? 128 ALA   B CA  1 
ATOM   2611 C  C   . ALA   B 1 116 ? -10.99300 1.51000   22.83300  1.000 26.02833 ? 128 ALA   B C   1 
ATOM   2612 O  O   . ALA   B 1 116 ? -11.52200 0.61100   22.16700  1.000 25.94889 ? 128 ALA   B O   1 
ATOM   2613 C  CB  . ALA   B 1 116 ? -11.85800 1.75000   25.16300  1.000 25.02778 ? 128 ALA   B CB  1 
ATOM   2614 N  N   . ALA   B 1 117 ? -10.64800 2.68200   22.30200  1.000 25.10175 ? 129 ALA   B N   1 
ATOM   2615 C  CA  . ALA   B 1 117 ? -10.87700 2.99200   20.89800  1.000 21.84127 ? 129 ALA   B CA  1 
ATOM   2616 C  C   . ALA   B 1 117 ? -9.83000  2.39100   19.97100  1.000 22.41896 ? 129 ALA   B C   1 
ATOM   2617 O  O   . ALA   B 1 117 ? -9.91500  2.60200   18.75400  1.000 28.52508 ? 129 ALA   B O   1 
ATOM   2618 C  CB  . ALA   B 1 117 ? -10.96200 4.50800   20.69100  1.000 24.07615 ? 129 ALA   B CB  1 
ATOM   2619 N  N   . GLY   B 1 118 ? -8.86000  1.64800   20.49700  1.000 19.69551 ? 130 GLY   B N   1 
ATOM   2620 C  CA  . GLY   B 1 118 ? -7.84900  1.01700   19.67500  1.000 21.60053 ? 130 GLY   B CA  1 
ATOM   2621 C  C   . GLY   B 1 118 ? -6.57500  1.81100   19.49400  1.000 19.52932 ? 130 GLY   B C   1 
ATOM   2622 O  O   . GLY   B 1 118 ? -5.73300  1.42500   18.67300  1.000 18.97070 ? 130 GLY   B O   1 
ATOM   2623 N  N   . VAL   B 1 119 ? -6.40800  2.91000   20.22400  1.000 19.00060 ? 131 VAL   B N   1 
ATOM   2624 C  CA  . VAL   B 1 119 ? -5.19700  3.71200   20.11800  1.000 18.32452 ? 131 VAL   B CA  1 
ATOM   2625 C  C   . VAL   B 1 119 ? -4.10900  3.08100   20.96900  1.000 14.71719 ? 131 VAL   B C   1 
ATOM   2626 O  O   . VAL   B 1 119 ? -4.34900  2.68500   22.11600  1.000 17.71120 ? 131 VAL   B O   1 
ATOM   2627 C  CB  . VAL   B 1 119 ? -5.47100  5.14500   20.59700  1.000 14.96903 ? 131 VAL   B CB  1 
ATOM   2628 C  CG1 . VAL   B 1 119 ? -4.18700  5.98300   20.51800  1.000 15.73678 ? 131 VAL   B CG1 1 
ATOM   2629 C  CG2 . VAL   B 1 119 ? -6.59700  5.78200   19.79500  1.000 18.03583 ? 131 VAL   B CG2 1 
ATOM   2630 N  N   . ALA   B 1 120 ? -2.90500  2.99400   20.41800  1.000 13.55160 ? 132 ALA   B N   1 
ATOM   2631 C  CA  . ALA   B 1 120 ? -1.74500  2.54100   21.17400  1.000 15.18540 ? 132 ALA   B CA  1 
ATOM   2632 C  C   . ALA   B 1 120 ? -1.20300  3.73600   21.95200  1.000 14.33011 ? 132 ALA   B C   1 
ATOM   2633 O  O   . ALA   B 1 120 ? -0.74900  4.71900   21.34500  1.000 14.30567 ? 132 ALA   B O   1 
ATOM   2634 C  CB  . ALA   B 1 120 ? -0.69900  1.94300   20.23500  1.000 16.37541 ? 132 ALA   B CB  1 
ATOM   2635 N  N   . THR   B 1 121 ? -1.28000  3.68600   23.28200  1.000 13.42509 ? 133 THR   B N   1 
ATOM   2636 C  CA  . THR   B 1 121 ? -0.90200  4.81400   24.12800  1.000 13.19781 ? 133 THR   B CA  1 
ATOM   2637 C  C   . THR   B 1 121 ? 0.51700   4.63800   24.63600  1.000 14.07911 ? 133 THR   B C   1 
ATOM   2638 O  O   . THR   B 1 121 ? 0.92400   3.53200   25.01000  1.000 15.89558 ? 133 THR   B O   1 
ATOM   2639 C  CB  . THR   B 1 121 ? -1.86900  4.97300   25.30500  1.000 12.43023 ? 133 THR   B CB  1 
ATOM   2640 O  OG1 . THR   B 1 121 ? -1.93900  3.74500   26.04900  1.000 13.71142 ? 133 THR   B OG1 1 
ATOM   2641 C  CG2 . THR   B 1 121 ? -3.26300  5.35900   24.80600  1.000 13.82452 ? 133 THR   B CG2 1 
ATOM   2642 N  N   . TYR   B 1 122 ? 1.26000   5.75400   24.67900  1.000 12.24445 ? 134 TYR   B N   1 
ATOM   2643 C  CA  . TYR   B 1 122 ? 2.68200   5.74300   24.98300  1.000 13.28372 ? 134 TYR   B CA  1 
ATOM   2644 C  C   . TYR   B 1 122 ? 3.02100   6.83900   25.98800  1.000 12.47090 ? 134 TYR   B C   1 
ATOM   2645 O  O   . TYR   B 1 122 ? 2.41900   7.92300   25.98900  1.000 12.52988 ? 134 TYR   B O   1 
ATOM   2646 C  CB  . TYR   B 1 122 ? 3.53200   6.06700   23.75400  1.000 13.12637 ? 134 TYR   B CB  1 
ATOM   2647 C  CG  . TYR   B 1 122 ? 3.63700   4.97200   22.72600  1.000 12.69782 ? 134 TYR   B CG  1 
ATOM   2648 C  CD1 . TYR   B 1 122 ? 2.57200   4.68400   21.87800  1.000 14.12483 ? 134 TYR   B CD1 1 
ATOM   2649 C  CD2 . TYR   B 1 122 ? 4.81500   4.25800   22.57500  1.000 13.88138 ? 134 TYR   B CD2 1 
ATOM   2650 C  CE1 . TYR   B 1 122 ? 2.67000   3.65000   20.91300  1.000 16.35132 ? 134 TYR   B CE1 1 
ATOM   2651 C  CE2 . TYR   B 1 122 ? 4.93200   3.23500   21.61000  1.000 16.38068 ? 134 TYR   B CE2 1 
ATOM   2652 C  CZ  . TYR   B 1 122 ? 3.85200   2.95400   20.79400  1.000 15.88779 ? 134 TYR   B CZ  1 
ATOM   2653 O  OH  . TYR   B 1 122 ? 3.96500   1.93400   19.85400  1.000 20.11060 ? 134 TYR   B OH  1 
ATOM   2654 N  N   . ALA   B 1 123 ? 4.04000   6.56900   26.80300  1.000 12.71620 ? 135 ALA   B N   1 
ATOM   2655 C  CA  . ALA   B 1 123 ? 4.67400   7.57300   27.65500  1.000 14.22252 ? 135 ALA   B CA  1 
ATOM   2656 C  C   . ALA   B 1 123 ? 6.04700   7.04600   28.04100  1.000 13.98551 ? 135 ALA   B C   1 
ATOM   2657 O  O   . ALA   B 1 123 ? 6.34300   5.86300   27.85800  1.000 13.84723 ? 135 ALA   B O   1 
ATOM   2658 C  CB  . ALA   B 1 123 ? 3.84400   7.87800   28.90200  1.000 13.96690 ? 135 ALA   B CB  1 
ATOM   2659 N  N   . SER   B 1 124 ? 6.89800   7.91200   28.56900  1.000 12.77803 ? 136 SER   B N   1 
ATOM   2660 C  CA  . SER   B 1 124 ? 8.18700   7.42600   29.04900  1.000 12.14749 ? 136 SER   B CA  1 
ATOM   2661 C  C   . SER   B 1 124 ? 7.98300   6.52300   30.26600  1.000 13.65230 ? 136 SER   B C   1 
ATOM   2662 O  O   . SER   B 1 124 ? 6.95200   6.59800   30.94800  1.000 14.31632 ? 136 SER   B O   1 
ATOM   2663 C  CB  . SER   B 1 124 ? 9.08800   8.58600   29.44300  1.000 14.33536 ? 136 SER   B CB  1 
ATOM   2664 O  OG  . SER   B 1 124 ? 8.58300   9.21500   30.61300  1.000 14.51392 ? 136 SER   B OG  1 
ATOM   2665 N  N   . PRO   B 1 125 ? 8.96600   5.66700   30.57700  1.000 13.84041 ? 137 PRO   B N   1 
ATOM   2666 C  CA  . PRO   B 1 125 ? 8.86500   4.88000   31.82600  1.000 15.50827 ? 137 PRO   B CA  1 
ATOM   2667 C  C   . PRO   B 1 125 ? 8.68400   5.75400   33.05500  1.000 16.67272 ? 137 PRO   B C   1 
ATOM   2668 O  O   . PRO   B 1 125 ? 7.92700   5.39300   33.96300  1.000 17.33786 ? 137 PRO   B O   1 
ATOM   2669 C  CB  . PRO   B 1 125 ? 10.18000  4.09400   31.84900  1.000 14.80501 ? 137 PRO   B CB  1 
ATOM   2670 C  CG  . PRO   B 1 125 ? 10.52000  3.95400   30.39100  1.000 16.16071 ? 137 PRO   B CG  1 
ATOM   2671 C  CD  . PRO   B 1 125 ? 10.14000  5.27800   29.78200  1.000 13.61570 ? 137 PRO   B CD  1 
ATOM   2672 N  N   A SER   B 1 126 ? 9.35600   6.90500   33.09700  0.674 15.16676 ? 138 SER   B N   1 
ATOM   2673 N  N   B SER   B 1 126 ? 9.33600   6.91500   33.10300  0.326 15.32891 ? 138 SER   B N   1 
ATOM   2674 C  CA  A SER   B 1 126 ? 9.18900   7.82700   34.21300  0.674 16.16013 ? 138 SER   B CA  1 
ATOM   2675 C  CA  B SER   B 1 126 ? 9.16800   7.79700   34.25300  0.326 16.25120 ? 138 SER   B CA  1 
ATOM   2676 C  C   A SER   B 1 126 ? 7.73700   8.27700   34.33600  0.674 16.77200 ? 138 SER   B C   1 
ATOM   2677 C  C   B SER   B 1 126 ? 7.73900   8.32200   34.35200  0.326 16.77352 ? 138 SER   B C   1 
ATOM   2678 O  O   A SER   B 1 126 ? 7.15200   8.24200   35.42400  0.674 16.64479 ? 138 SER   B O   1 
ATOM   2679 O  O   B SER   B 1 126 ? 7.17800   8.40500   35.45100  0.326 16.90733 ? 138 SER   B O   1 
ATOM   2680 C  CB  A SER   B 1 126 ? 10.11900  9.02300   34.02200  0.674 18.62932 ? 138 SER   B CB  1 
ATOM   2681 C  CB  B SER   B 1 126 ? 10.17000  8.94500   34.18200  0.326 18.54474 ? 138 SER   B CB  1 
ATOM   2682 O  OG  A SER   B 1 126 ? 10.09500  9.88500   35.14500  0.674 24.91678 ? 138 SER   B OG  1 
ATOM   2683 O  OG  B SER   B 1 126 ? 9.98100   9.69400   32.99800  0.326 19.12678 ? 138 SER   B OG  1 
ATOM   2684 N  N   . THR   B 1 127 ? 7.13100   8.68200   33.21800  1.000 14.18976 ? 139 THR   B N   1 
ATOM   2685 C  CA  . THR   B 1 127 ? 5.74400   9.13800   33.25700  1.000 15.35689 ? 139 THR   B CA  1 
ATOM   2686 C  C   . THR   B 1 127 ? 4.82200   8.00700   33.69500  1.000 13.04291 ? 139 THR   B C   1 
ATOM   2687 O  O   . THR   B 1 127 ? 3.91600   8.22000   34.50700  1.000 14.56083 ? 139 THR   B O   1 
ATOM   2688 C  CB  . THR   B 1 127 ? 5.32800   9.68500   31.88800  1.000 11.47106 ? 139 THR   B CB  1 
ATOM   2689 O  OG1 . THR   B 1 127 ? 6.07200   10.87600  31.60300  1.000 12.33176 ? 139 THR   B OG1 1 
ATOM   2690 C  CG2 . THR   B 1 127 ? 3.84900   9.98800   31.83000  1.000 12.62879 ? 139 THR   B CG2 1 
ATOM   2691 N  N   . ARG   B 1 128 ? 5.04100   6.80000   33.17400  1.000 13.62544 ? 140 ARG   B N   1 
ATOM   2692 C  CA  . ARG   B 1 128 ? 4.22200   5.66100   33.58400  1.000 15.78586 ? 140 ARG   B CA  1 
ATOM   2693 C  C   . ARG   B 1 128 ? 4.34400   5.38400   35.08200  1.000 15.48264 ? 140 ARG   B C   1 
ATOM   2694 O  O   . ARG   B 1 128 ? 3.32800   5.16300   35.75700  1.000 16.27521 ? 140 ARG   B O   1 
ATOM   2695 C  CB  . ARG   B 1 128 ? 4.57400   4.42900   32.75000  1.000 15.96079 ? 140 ARG   B CB  1 
ATOM   2696 C  CG  . ARG   B 1 128 ? 4.24400   4.59900   31.28200  1.000 15.28501 ? 140 ARG   B CG  1 
ATOM   2697 C  CD  . ARG   B 1 128 ? 4.66700   3.40300   30.46000  1.000 17.92633 ? 140 ARG   B CD  1 
ATOM   2698 N  NE  . ARG   B 1 128 ? 3.79000   2.26000   30.70500  1.000 20.37621 ? 140 ARG   B NE  1 
ATOM   2699 C  CZ  . ARG   B 1 128 ? 4.09600   1.21200   31.45500  1.000 26.16343 ? 140 ARG   B CZ  1 
ATOM   2700 N  NH1 . ARG   B 1 128 ? 5.28100   1.09600   32.03100  1.000 24.95163 ? 140 ARG   B NH1 1 
ATOM   2701 N  NH2 . ARG   B 1 128 ? 3.19100   0.25000   31.62500  1.000 31.30212 ? 140 ARG   B NH2 1 
ATOM   2702 N  N   . ARG   B 1 129 ? 5.56600   5.40300   35.61800  1.000 14.54503 ? 141 ARG   B N   1 
ATOM   2703 C  CA  . ARG   B 1 129 ? 5.74700   5.15200   37.04600  1.000 17.37194 ? 141 ARG   B CA  1 
ATOM   2704 C  C   . ARG   B 1 129 ? 5.07700   6.22800   37.89700  1.000 18.31751 ? 141 ARG   B C   1 
ATOM   2705 O  O   . ARG   B 1 129 ? 4.39900   5.92000   38.89100  1.000 19.15311 ? 141 ARG   B O   1 
ATOM   2706 C  CB  . ARG   B 1 129 ? 7.23800   5.07400   37.36100  1.000 20.34778 ? 141 ARG   B CB  1 
ATOM   2707 C  CG  . ARG   B 1 129 ? 7.55000   4.81300   38.83100  1.000 28.62473 ? 141 ARG   B CG  1 
ATOM   2708 C  CD  . ARG   B 1 129 ? 9.04300   4.88600   39.09800  1.000 33.13918 ? 141 ARG   B CD  1 
ATOM   2709 N  NE  . ARG   B 1 129 ? 9.67500   5.98500   38.38000  1.000 32.41832 ? 141 ARG   B NE  1 
ATOM   2710 C  CZ  . ARG   B 1 129 ? 9.76200   7.22700   38.83800  1.000 31.82543 ? 141 ARG   B CZ  1 
ATOM   2711 N  NH1 . ARG   B 1 129 ? 9.30200   7.55700   40.03700  1.000 31.84725 ? 141 ARG   B NH1 1 
ATOM   2712 N  NH2 . ARG   B 1 129 ? 10.32300  8.16300   38.07300  1.000 30.83311 ? 141 ARG   B NH2 1 
ATOM   2713 N  N   . LEU   B 1 130 ? 5.24800   7.49800   37.52900  1.000 16.00679 ? 142 LEU   B N   1 
ATOM   2714 C  CA  . LEU   B 1 130 ? 4.64800   8.57500   38.30800  1.000 15.04870 ? 142 LEU   B CA  1 
ATOM   2715 C  C   . LEU   B 1 130 ? 3.13000   8.53700   38.22600  1.000 17.51140 ? 142 LEU   B C   1 
ATOM   2716 O  O   . LEU   B 1 130 ? 2.44500   8.80000   39.22300  1.000 16.40460 ? 142 LEU   B O   1 
ATOM   2717 C  CB  . LEU   B 1 130 ? 5.19600   9.92300   37.83000  1.000 14.77213 ? 142 LEU   B CB  1 
ATOM   2718 C  CG  . LEU   B 1 130 ? 6.66300   10.14500  38.19700  1.000 15.14438 ? 142 LEU   B CG  1 
ATOM   2719 C  CD1 . LEU   B 1 130 ? 7.32100   11.24300  37.34800  1.000 18.18283 ? 142 LEU   B CD1 1 
ATOM   2720 C  CD2 . LEU   B 1 130 ? 6.76900   10.46100  39.69500  1.000 21.22235 ? 142 LEU   B CD2 1 
ATOM   2721 N  N   . ALA   B 1 131 ? 2.58000   8.24100   37.04700  1.000 13.65709 ? 143 ALA   B N   1 
ATOM   2722 C  CA  . ALA   B 1 131 ? 1.12800   8.11400   36.93600  1.000 13.67723 ? 143 ALA   B CA  1 
ATOM   2723 C  C   . ALA   B 1 131 ? 0.60600   7.00000   37.84100  1.000 16.68440 ? 143 ALA   B C   1 
ATOM   2724 O  O   . ALA   B 1 131 ? -0.40300  7.17900   38.53800  1.000 18.17114 ? 143 ALA   B O   1 
ATOM   2725 C  CB  . ALA   B 1 131 ? 0.71700   7.87600   35.48100  1.000 16.34440 ? 143 ALA   B CB  1 
ATOM   2726 N  N   . GLU   B 1 132 ? 1.29000   5.85600   37.86000  1.000 15.49550 ? 144 GLU   B N   1 
ATOM   2727 C  CA  . GLU   B 1 132 ? 0.86200   4.76200   38.73100  1.000 17.65668 ? 144 GLU   B CA  1 
ATOM   2728 C  C   . GLU   B 1 132 ? 0.89500   5.17000   40.20600  1.000 22.10546 ? 144 GLU   B C   1 
ATOM   2729 O  O   . GLU   B 1 132 ? -0.03000  4.85300   40.96300  1.000 22.80971 ? 144 GLU   B O   1 
ATOM   2730 C  CB  . GLU   B 1 132 ? 1.73100   3.53500   38.48100  1.000 19.60843 ? 144 GLU   B CB  1 
ATOM   2731 C  CG  . GLU   B 1 132 ? 1.35100   2.34400   39.37000  1.000 23.41662 ? 144 GLU   B CG  1 
ATOM   2732 C  CD  . GLU   B 1 132 ? 2.10400   1.08600   39.01600  1.000 34.18387 ? 144 GLU   B CD  1 
ATOM   2733 O  OE1 . GLU   B 1 132 ? 3.33300   1.16300   38.80000  1.000 41.69373 ? 144 GLU   B OE1 1 
ATOM   2734 O  OE2 . GLU   B 1 132 ? 1.46700   0.01500   38.96400  1.000 45.52513 ? 144 GLU   B OE2 1 
ATOM   2735 N  N   . VAL   B 1 133 ? 1.94200   5.88500   40.63000  1.000 18.89167 ? 145 VAL   B N   1 
ATOM   2736 C  CA  . VAL   B 1 133 ? 2.01400   6.35400   42.01500  1.000 23.02286 ? 145 VAL   B CA  1 
ATOM   2737 C  C   . VAL   B 1 133 ? 0.85200   7.29600   42.32800  1.000 25.34884 ? 145 VAL   B C   1 
ATOM   2738 O  O   . VAL   B 1 133 ? 0.22100   7.19900   43.38900  1.000 24.01500 ? 145 VAL   B O   1 
ATOM   2739 C  CB  . VAL   B 1 133 ? 3.37900   7.02000   42.27800  1.000 23.86670 ? 145 VAL   B CB  1 
ATOM   2740 C  CG1 . VAL   B 1 133 ? 3.36000   7.79900   43.59900  1.000 27.31202 ? 145 VAL   B CG1 1 
ATOM   2741 C  CG2 . VAL   B 1 133 ? 4.50200   5.98700   42.24100  1.000 25.08438 ? 145 VAL   B CG2 1 
ATOM   2742 N  N   . GLU   B 1 134 ? 0.54900   8.21600   41.40900  1.000 18.31959 ? 146 GLU   B N   1 
ATOM   2743 C  CA  . GLU   B 1 134 ? -0.48200  9.22700   41.60800  1.000 20.83452 ? 146 GLU   B CA  1 
ATOM   2744 C  C   . GLU   B 1 134 ? -1.89300  8.65400   41.58600  1.000 23.09857 ? 146 GLU   B C   1 
ATOM   2745 O  O   . GLU   B 1 134 ? -2.82000  9.30200   42.08600  1.000 26.64048 ? 146 GLU   B O   1 
ATOM   2746 C  CB  . GLU   B 1 134 ? -0.36900  10.29100  40.50700  1.000 20.60337 ? 146 GLU   B CB  1 
ATOM   2747 C  CG  . GLU   B 1 134 ? -1.05700  11.61700  40.81700  1.000 24.45836 ? 146 GLU   B CG  1 
ATOM   2748 C  CD  . GLU   B 1 134 ? -0.51500  12.25900  42.07700  1.000 34.13745 ? 146 GLU   B CD  1 
ATOM   2749 O  OE1 . GLU   B 1 134 ? 0.69500   12.09500  42.34600  1.000 37.86134 ? 146 GLU   B OE1 1 
ATOM   2750 O  OE2 . GLU   B 1 134 ? -1.29800  12.92000  42.79300  1.000 51.47091 ? 146 GLU   B OE2 1 
ATOM   2751 N  N   . GLY   B 1 135 ? -2.07900  7.47300   41.01200  1.000 19.89946 ? 147 GLY   B N   1 
ATOM   2752 C  CA  . GLY   B 1 135 ? -3.41600  6.98200   40.74700  1.000 21.24495 ? 147 GLY   B CA  1 
ATOM   2753 C  C   . GLY   B 1 135 ? -4.02800  7.47700   39.45500  1.000 23.17749 ? 147 GLY   B C   1 
ATOM   2754 O  O   . GLY   B 1 135 ? -5.25300  7.46000   39.31700  1.000 23.10382 ? 147 GLY   B O   1 
ATOM   2755 N  N   . ASN   B 1 136 ? -3.21600  7.92700   38.49600  1.000 19.96052 ? 148 ASN   B N   1 
ATOM   2756 C  CA  . ASN   B 1 136 ? -3.71200  8.37000   37.20300  1.000 17.48884 ? 148 ASN   B CA  1 
ATOM   2757 C  C   . ASN   B 1 136 ? -3.64500  7.23700   36.18700  1.000 20.29244 ? 148 ASN   B C   1 
ATOM   2758 O  O   . ASN   B 1 136 ? -2.98700  6.22000   36.39500  1.000 19.06666 ? 148 ASN   B O   1 
ATOM   2759 C  CB  . ASN   B 1 136 ? -2.90100  9.56600   36.70300  1.000 18.16039 ? 148 ASN   B CB  1 
ATOM   2760 C  CG  . ASN   B 1 136 ? -3.10200  10.78800  37.55300  1.000 22.51313 ? 148 ASN   B CG  1 
ATOM   2761 O  OD1 . ASN   B 1 136 ? -3.99900  10.83000  38.39800  1.000 23.86346 ? 148 ASN   B OD1 1 
ATOM   2762 N  ND2 . ASN   B 1 136 ? -2.28700  11.80600  37.32900  1.000 18.74917 ? 148 ASN   B ND2 1 
ATOM   2763 N  N   . GLU   B 1 137 ? -4.33500  7.42500   35.06700  1.000 19.38321 ? 149 GLU   B N   1 
ATOM   2764 C  CA  . GLU   B 1 137 ? -4.30000  6.42400   34.01600  1.000 18.21662 ? 149 GLU   B CA  1 
ATOM   2765 C  C   . GLU   B 1 137 ? -2.88500  6.29000   33.46300  1.000 18.41371 ? 149 GLU   B C   1 
ATOM   2766 O  O   . GLU   B 1 137 ? -2.11500  7.25400   33.40800  1.000 18.00815 ? 149 GLU   B O   1 
ATOM   2767 C  CB  . GLU   B 1 137 ? -5.29400  6.80100   32.91900  1.000 18.81526 ? 149 GLU   B CB  1 
ATOM   2768 C  CG  . GLU   B 1 137 ? -6.75600  6.73100   33.40400  1.000 20.30628 ? 149 GLU   B CG  1 
ATOM   2769 C  CD  . GLU   B 1 137 ? -7.68700  7.61500   32.60100  1.000 23.09587 ? 149 GLU   B CD  1 
ATOM   2770 O  OE1 . GLU   B 1 137 ? -7.96000  7.28800   31.43500  1.000 25.68601 ? 149 GLU   B OE1 1 
ATOM   2771 O  OE2 . GLU   B 1 137 ? -8.14800  8.64400   33.14200  1.000 25.85424 ? 149 GLU   B OE2 1 
ATOM   2772 N  N   . ILE   B 1 138 ? -2.55100  5.07600   33.04700  1.000 17.04227 ? 150 ILE   B N   1 
ATOM   2773 C  CA  . ILE   B 1 138 ? -1.18300  4.71200   32.70500  1.000 15.07396 ? 150 ILE   B CA  1 
ATOM   2774 C  C   . ILE   B 1 138 ? -1.09700  4.32700   31.23500  1.000 17.29026 ? 150 ILE   B C   1 
ATOM   2775 O  O   . ILE   B 1 138 ? -1.63800  3.29000   30.82900  1.000 16.89237 ? 150 ILE   B O   1 
ATOM   2776 C  CB  . ILE   B 1 138 ? -0.68200  3.54800   33.57200  1.000 17.50123 ? 150 ILE   B CB  1 
ATOM   2777 C  CG1 . ILE   B 1 138 ? -0.86200  3.84900   35.06100  1.000 17.18281 ? 150 ILE   B CG1 1 
ATOM   2778 C  CG2 . ILE   B 1 138 ? 0.75800   3.25100   33.23600  1.000 18.40835 ? 150 ILE   B CG2 1 
ATOM   2779 C  CD1 . ILE   B 1 138 ? -0.63900  2.63800   35.95400  1.000 21.60435 ? 150 ILE   B CD1 1 
ATOM   2780 N  N   . PRO   B 1 139 ? -0.44000  5.13100   30.40100  1.000 14.18039 ? 151 PRO   B N   1 
ATOM   2781 C  CA  . PRO   B 1 139 ? -0.24400  4.72400   29.00500  1.000 14.56933 ? 151 PRO   B CA  1 
ATOM   2782 C  C   . PRO   B 1 139 ? 0.44800   3.36600   28.92400  1.000 15.83887 ? 151 PRO   B C   1 
ATOM   2783 O  O   . PRO   B 1 139 ? 1.30300   3.03100   29.74700  1.000 16.39619 ? 151 PRO   B O   1 
ATOM   2784 C  CB  . PRO   B 1 139 ? 0.63800   5.84700   28.44400  1.000 14.27313 ? 151 PRO   B CB  1 
ATOM   2785 C  CG  . PRO   B 1 139 ? 0.25400   7.05600   29.26900  1.000 15.05990 ? 151 PRO   B CG  1 
ATOM   2786 C  CD  . PRO   B 1 139 ? 0.04900   6.50200   30.66700  1.000 14.70950 ? 151 PRO   B CD  1 
ATOM   2787 N  N   . THR   B 1 140 ? 0.08600   2.58500   27.89900  1.000 14.58764 ? 152 THR   B N   1 
ATOM   2788 C  CA  . THR   B 1 140 ? 0.47200   1.17500   27.84000  1.000 14.64186 ? 152 THR   B CA  1 
ATOM   2789 C  C   . THR   B 1 140 ? 1.94000   0.97700   27.44900  1.000 17.20286 ? 152 THR   B C   1 
ATOM   2790 O  O   . THR   B 1 140 ? 2.65800   0.20000   28.09500  1.000 16.26673 ? 152 THR   B O   1 
ATOM   2791 C  CB  . THR   B 1 140 ? -0.46900  0.43100   26.89100  1.000 18.73657 ? 152 THR   B CB  1 
ATOM   2792 O  OG1 . THR   B 1 140 ? -1.78400  0.42800   27.45600  1.000 20.27247 ? 152 THR   B OG1 1 
ATOM   2793 C  CG2 . THR   B 1 140 ? -0.00700  -1.00200  26.68400  1.000 19.39061 ? 152 THR   B CG2 1 
ATOM   2794 N  N   . HIS   B 1 141 ? 2.40300   1.65300   26.39400  1.000 14.29739 ? 153 HIS   B N   1 
ATOM   2795 C  CA  . HIS   B 1 141 ? 3.73400   1.43400   25.86000  1.000 14.27330 ? 153 HIS   B CA  1 
ATOM   2796 C  C   . HIS   B 1 141 ? 4.71700   2.41600   26.44400  1.000 14.68530 ? 153 HIS   B C   1 
ATOM   2797 O  O   . HIS   B 1 141 ? 4.36000   3.53200   26.82200  1.000 14.43766 ? 153 HIS   B O   1 
ATOM   2798 C  CB  . HIS   B 1 141 ? 3.77700   1.66300   24.35500  1.000 14.37647 ? 153 HIS   B CB  1 
ATOM   2799 C  CG  . HIS   B 1 141 ? 2.96600   0.69800   23.59200  1.000 24.01871 ? 153 HIS   B CG  1 
ATOM   2800 N  ND1 . HIS   B 1 141 ? 3.51900   -0.30700  22.83100  1.000 33.00926 ? 153 HIS   B ND1 1 
ATOM   2801 C  CD2 . HIS   B 1 141 ? 1.63000   0.56700   23.49700  1.000 21.50903 ? 153 HIS   B CD2 1 
ATOM   2802 C  CE1 . HIS   B 1 141 ? 2.54500   -1.00700  22.28300  1.000 18.55104 ? 153 HIS   B CE1 1 
ATOM   2803 N  NE2 . HIS   B 1 141 ? 1.39400   -0.50400  22.68400  1.000 25.14273 ? 153 HIS   B NE2 1 
ATOM   2804 N  N   . SER   B 1 142 ? 5.98000   2.04000   26.38700  1.000 15.28188 ? 154 SER   B N   1 
ATOM   2805 C  CA  . SER   B 1 142 ? 7.06700   2.82400   26.94800  1.000 14.88987 ? 154 SER   B CA  1 
ATOM   2806 C  C   . SER   B 1 142 ? 7.88200   3.46500   25.83300  1.000 18.53303 ? 154 SER   B C   1 
ATOM   2807 O  O   . SER   B 1 142 ? 8.22900   2.80500   24.84300  1.000 20.78472 ? 154 SER   B O   1 
ATOM   2808 C  CB  . SER   B 1 142 ? 7.97700   1.94400   27.80800  1.000 18.36706 ? 154 SER   B CB  1 
ATOM   2809 O  OG  . SER   B 1 142 ? 7.31300   1.55900   29.00500  1.000 18.92349 ? 154 SER   B OG  1 
ATOM   2810 N  N   . LEU   B 1 143 ? 8.19300   4.74600   26.00300  1.000 14.52993 ? 155 LEU   B N   1 
ATOM   2811 C  CA  . LEU   B 1 143 ? 9.10400   5.46400   25.11500  1.000 15.04912 ? 155 LEU   B CA  1 
ATOM   2812 C  C   . LEU   B 1 143 ? 10.50000  5.35600   25.70300  1.000 17.62780 ? 155 LEU   B C   1 
ATOM   2813 O  O   . LEU   B 1 143 ? 10.78200  5.93300   26.75900  1.000 18.56944 ? 155 LEU   B O   1 
ATOM   2814 C  CB  . LEU   B 1 143 ? 8.69800   6.93100   24.99700  1.000 13.25891 ? 155 LEU   B CB  1 
ATOM   2815 C  CG  . LEU   B 1 143 ? 7.30500   7.15100   24.42400  1.000 13.94513 ? 155 LEU   B CG  1 
ATOM   2816 C  CD1 . LEU   B 1 143 ? 6.85700   8.58000   24.72300  1.000 16.27938 ? 155 LEU   B CD1 1 
ATOM   2817 C  CD2 . LEU   B 1 143 ? 7.28600   6.87900   22.91400  1.000 15.84372 ? 155 LEU   B CD2 1 
ATOM   2818 N  N   A GLU   B 1 144 ? 11.37100  4.60900   25.03800  0.604 17.56155 ? 156 GLU   B N   1 
ATOM   2819 N  N   B GLU   B 1 144 ? 11.36800  4.61800   25.01400  0.396 17.61070 ? 156 GLU   B N   1 
ATOM   2820 C  CA  A GLU   B 1 144 ? 12.74100  4.45300   25.50000  0.604 16.88339 ? 156 GLU   B CA  1 
ATOM   2821 C  CA  B GLU   B 1 144 ? 12.75600  4.44600   25.40800  0.396 16.98239 ? 156 GLU   B CA  1 
ATOM   2822 C  C   A GLU   B 1 144 ? 13.61700  5.55300   24.90100  0.604 17.18318 ? 156 GLU   B C   1 
ATOM   2823 C  C   B GLU   B 1 144 ? 13.59600  5.62300   24.92200  0.396 17.21210 ? 156 GLU   B C   1 
ATOM   2824 O  O   A GLU   B 1 144 ? 13.25300  6.20100   23.92100  0.604 18.39987 ? 156 GLU   B O   1 
ATOM   2825 O  O   B GLU   B 1 144 ? 13.19300  6.38800   24.04600  0.396 17.81661 ? 156 GLU   B O   1 
ATOM   2826 C  CB  A GLU   B 1 144 ? 13.28200  3.07200   25.11000  0.604 21.04685 ? 156 GLU   B CB  1 
ATOM   2827 C  CB  B GLU   B 1 144 ? 13.32000  3.14200   24.82700  0.396 20.53971 ? 156 GLU   B CB  1 
ATOM   2828 C  CG  A GLU   B 1 144 ? 12.49000  1.86300   25.64300  0.604 20.42751 ? 156 GLU   B CG  1 
ATOM   2829 C  CG  B GLU   B 1 144 ? 13.36100  3.08900   23.30700  0.396 25.52874 ? 156 GLU   B CG  1 
ATOM   2830 C  CD  A GLU   B 1 144 ? 12.42700  1.77900   27.15800  0.604 21.20466 ? 156 GLU   B CD  1 
ATOM   2831 C  CD  B GLU   B 1 144 ? 13.81200  1.73900   22.76100  0.396 31.09052 ? 156 GLU   B CD  1 
ATOM   2832 O  OE1 A GLU   B 1 144 ? 13.36100  2.25400   27.83500  0.604 22.70443 ? 156 GLU   B OE1 1 
ATOM   2833 O  OE1 B GLU   B 1 144 ? 14.41500  0.94700   23.52100  0.396 30.63349 ? 156 GLU   B OE1 1 
ATOM   2834 O  OE2 A GLU   B 1 144 ? 11.43900  1.21100   27.67600  0.604 27.58179 ? 156 GLU   B OE2 1 
ATOM   2835 O  OE2 B GLU   B 1 144 ? 13.56100  1.46900   21.56500  0.396 33.90542 ? 156 GLU   B OE2 1 
ATOM   2836 N  N   . GLY   B 1 145 ? 14.77600  5.76600   25.51800  1.000 17.61347 ? 157 GLY   B N   1 
ATOM   2837 C  CA  . GLY   B 1 145 ? 15.74400  6.72000   25.01100  1.000 16.17419 ? 157 GLY   B CA  1 
ATOM   2838 C  C   . GLY   B 1 145 ? 15.54200  8.15900   25.43500  1.000 15.07063 ? 157 GLY   B C   1 
ATOM   2839 O  O   . GLY   B 1 145 ? 16.12700  9.05700   24.81900  1.000 16.05533 ? 157 GLY   B O   1 
ATOM   2840 N  N   . LEU   B 1 146 ? 14.75700  8.41200   26.48500  1.000 13.73590 ? 158 LEU   B N   1 
ATOM   2841 C  CA  . LEU   B 1 146 ? 14.42500  9.77600   26.88000  1.000 14.95007 ? 158 LEU   B CA  1 
ATOM   2842 C  C   . LEU   B 1 146 ? 14.72800  10.06300  28.34300  1.000 14.83933 ? 158 LEU   B C   1 
ATOM   2843 O  O   . LEU   B 1 146 ? 14.22100  11.04600  28.89200  1.000 15.56724 ? 158 LEU   B O   1 
ATOM   2844 C  CB  . LEU   B 1 146 ? 12.95400  10.08000  26.58100  1.000 14.88597 ? 158 LEU   B CB  1 
ATOM   2845 C  CG  . LEU   B 1 146 ? 12.59400  10.22400  25.10900  1.000 13.81049 ? 158 LEU   B CG  1 
ATOM   2846 C  CD1 . LEU   B 1 146 ? 11.08600  10.11900  24.89700  1.000 13.43829 ? 158 LEU   B CD1 1 
ATOM   2847 C  CD2 . LEU   B 1 146 ? 13.17100  11.51000  24.51900  1.000 15.66594 ? 158 LEU   B CD2 1 
ATOM   2848 N  N   . SER   B 1 147 ? 15.53200  9.23900   29.00300  1.000 14.47350 ? 159 SER   B N   1 
ATOM   2849 C  CA  . SER   B 1 147 ? 15.65100  9.37100   30.45100  1.000 14.87036 ? 159 SER   B CA  1 
ATOM   2850 C  C   . SER   B 1 147 ? 16.68100  10.40500  30.89600  1.000 16.82863 ? 159 SER   B C   1 
ATOM   2851 O  O   . SER   B 1 147 ? 16.67100  10.78900  32.06400  1.000 16.99223 ? 159 SER   B O   1 
ATOM   2852 C  CB  . SER   B 1 147 ? 15.91800  8.02100   31.13500  1.000 18.55393 ? 159 SER   B CB  1 
ATOM   2853 O  OG  . SER   B 1 147 ? 17.13900  7.48500   30.68700  1.000 19.00200 ? 159 SER   B OG  1 
ATOM   2854 N  N   A SER   B 1 148 ? 17.57200  10.85000  30.01700  0.478 15.71969 ? 160 SER   B N   1 
ATOM   2855 N  N   B SER   B 1 148 ? 17.54200  10.87100  29.99800  0.522 15.68993 ? 160 SER   B N   1 
ATOM   2856 C  CA  A SER   B 1 148 ? 18.59200  11.82400  30.38300  0.478 16.35412 ? 160 SER   B CA  1 
ATOM   2857 C  CA  B SER   B 1 148 ? 18.59800  11.81700  30.33000  0.522 16.43172 ? 160 SER   B CA  1 
ATOM   2858 C  C   A SER   B 1 148 ? 18.30200  13.16200  29.71300  0.478 14.89979 ? 160 SER   B C   1 
ATOM   2859 C  C   B SER   B 1 148 ? 18.29000  13.17000  29.70000  0.522 14.87739 ? 160 SER   B C   1 
ATOM   2860 O  O   A SER   B 1 148 ? 17.92400  13.21000  28.53900  0.478 15.67700 ? 160 SER   B O   1 
ATOM   2861 O  O   B SER   B 1 148 ? 17.89100  13.24100  28.53300  0.522 15.63465 ? 160 SER   B O   1 
ATOM   2862 C  CB  A SER   B 1 148 ? 19.98600  11.33000  29.98900  0.478 20.63654 ? 160 SER   B CB  1 
ATOM   2863 C  CB  B SER   B 1 148 ? 19.93200  11.30300  29.79000  0.522 20.22827 ? 160 SER   B CB  1 
ATOM   2864 O  OG  A SER   B 1 148 ? 20.42800  10.31200  30.87600  0.478 20.85456 ? 160 SER   B OG  1 
ATOM   2865 O  OG  B SER   B 1 148 ? 20.99800  12.10400  30.24300  0.522 20.01634 ? 160 SER   B OG  1 
ATOM   2866 N  N   . SER   B 1 149 ? 18.48100  14.24500  30.46700  1.000 16.24828 ? 161 SER   B N   1 
ATOM   2867 C  CA  A SER   B 1 149 ? 18.21700  15.58400  29.94600  0.617 15.14385 ? 161 SER   B CA  1 
ATOM   2868 C  CA  B SER   B 1 149 ? 18.20700  15.57800  29.94200  0.383 15.21099 ? 161 SER   B CA  1 
ATOM   2869 C  C   . SER   B 1 149 ? 18.98100  15.81200  28.64900  1.000 16.53438 ? 161 SER   B C   1 
ATOM   2870 O  O   . SER   B 1 149 ? 20.17700  15.51200  28.55400  1.000 18.80005 ? 161 SER   B O   1 
ATOM   2871 C  CB  A SER   B 1 149 ? 18.62700  16.64000  30.97400  0.617 18.09047 ? 161 SER   B CB  1 
ATOM   2872 C  CB  B SER   B 1 149 ? 18.56700  16.64000  30.97600  0.383 18.04637 ? 161 SER   B CB  1 
ATOM   2873 O  OG  A SER   B 1 149 ? 17.97700  16.44700  32.22000  0.617 17.64670 ? 161 SER   B OG  1 
ATOM   2874 O  OG  B SER   B 1 149 ? 19.91800  16.51800  31.37000  0.383 18.84247 ? 161 SER   B OG  1 
ATOM   2875 N  N   . GLY   B 1 150 ? 18.28400  16.33100  27.64500  1.000 14.37867 ? 162 GLY   B N   1 
ATOM   2876 C  CA  . GLY   B 1 150 ? 18.86800  16.52300  26.33900  1.000 17.34143 ? 162 GLY   B CA  1 
ATOM   2877 C  C   . GLY   B 1 150 ? 18.63600  15.38100  25.36800  1.000 16.51809 ? 162 GLY   B C   1 
ATOM   2878 O  O   . GLY   B 1 150 ? 19.00500  15.50400  24.19300  1.000 18.61699 ? 162 GLY   B O   1 
ATOM   2879 N  N   . ASP   B 1 151 ? 18.01800  14.28300  25.80700  1.000 14.78469 ? 163 ASP   B N   1 
ATOM   2880 C  CA  . ASP   B 1 151 ? 17.75800  13.15000  24.91700  1.000 14.68461 ? 163 ASP   B CA  1 
ATOM   2881 C  C   . ASP   B 1 151 ? 16.63300  13.47900  23.94400  1.000 14.57044 ? 163 ASP   B C   1 
ATOM   2882 O  O   . ASP   B 1 151 ? 15.63300  14.10800  24.30700  1.000 15.80058 ? 163 ASP   B O   1 
ATOM   2883 C  CB  . ASP   B 1 151 ? 17.30200  11.92800  25.73200  1.000 16.62799 ? 163 ASP   B CB  1 
ATOM   2884 C  CG  . ASP   B 1 151 ? 18.44900  11.18100  26.40500  1.000 17.87703 ? 163 ASP   B CG  1 
ATOM   2885 O  OD1 . ASP   B 1 151 ? 19.63800  11.46100  26.11500  1.000 21.80876 ? 163 ASP   B OD1 1 
ATOM   2886 O  OD2 . ASP   B 1 151 ? 18.14000  10.30300  27.24600  1.000 18.79790 ? 163 ASP   B OD2 1 
ATOM   2887 N  N   . ALA   B 1 152 ? 16.78200  13.03400  22.70500  1.000 15.46105 ? 164 ALA   B N   1 
ATOM   2888 C  CA  . ALA   B 1 152 ? 15.76200  13.19500  21.68000  1.000 15.47952 ? 164 ALA   B CA  1 
ATOM   2889 C  C   . ALA   B 1 152 ? 15.61600  11.87600  20.94100  1.000 16.99595 ? 164 ALA   B C   1 
ATOM   2890 O  O   . ALA   B 1 152 ? 16.61000  11.17500  20.71300  1.000 19.69051 ? 164 ALA   B O   1 
ATOM   2891 C  CB  . ALA   B 1 152 ? 16.15600  14.27400  20.66900  1.000 18.26502 ? 164 ALA   B CB  1 
ATOM   2892 N  N   A VAL   B 1 153 ? 14.37900  11.50800  20.62100  0.704 15.64575 ? 165 VAL   B N   1 
ATOM   2893 N  N   B VAL   B 1 153 ? 14.38500  11.56100  20.53300  0.296 15.69543 ? 165 VAL   B N   1 
ATOM   2894 C  CA  A VAL   B 1 153 ? 14.11700  10.34200  19.79100  0.704 15.95531 ? 165 VAL   B CA  1 
ATOM   2895 C  CA  B VAL   B 1 153 ? 14.06600  10.31300  19.84500  0.296 16.10743 ? 165 VAL   B CA  1 
ATOM   2896 C  C   A VAL   B 1 153 ? 13.09500  10.73700  18.74200  0.704 16.56919 ? 165 VAL   B C   1 
ATOM   2897 C  C   B VAL   B 1 153 ? 12.97200  10.58400  18.82000  0.296 15.67239 ? 165 VAL   B C   1 
ATOM   2898 O  O   A VAL   B 1 153 ? 12.29900  11.66000  18.93700  0.704 14.52357 ? 165 VAL   B O   1 
ATOM   2899 O  O   B VAL   B 1 153 ? 11.98300  11.26100  19.11900  0.296 13.86681 ? 165 VAL   B O   1 
ATOM   2900 C  CB  A VAL   B 1 153 ? 13.60700  9.11900   20.58800  0.704 19.09625 ? 165 VAL   B CB  1 
ATOM   2901 C  CB  B VAL   B 1 153 ? 13.59800  9.23000   20.83900  0.296 19.00627 ? 165 VAL   B CB  1 
ATOM   2902 C  CG1 A VAL   B 1 153 ? 14.64700  8.63400   21.57900  0.704 19.68294 ? 165 VAL   B CG1 1 
ATOM   2903 C  CG1 B VAL   B 1 153 ? 13.12600  8.00800   20.09400  0.296 18.65704 ? 165 VAL   B CG1 1 
ATOM   2904 C  CG2 A VAL   B 1 153 ? 12.30700  9.44300   21.29700  0.704 15.82868 ? 165 VAL   B CG2 1 
ATOM   2905 C  CG2 B VAL   B 1 153 ? 14.71100  8.84900   21.80500  0.296 19.54562 ? 165 VAL   B CG2 1 
ATOM   2906 N  N   . ARG   B 1 154 ? 13.14100  10.05200  17.61100  1.000 15.79267 ? 166 ARG   B N   1 
ATOM   2907 C  CA  . ARG   B 1 154 ? 12.11600  10.20800  16.60000  1.000 14.34757 ? 166 ARG   B CA  1 
ATOM   2908 C  C   . ARG   B 1 154 ? 10.90800  9.35100   16.94700  1.000 15.60443 ? 166 ARG   B C   1 
ATOM   2909 O  O   . ARG   B 1 154 ? 11.04100  8.23700   17.47000  1.000 18.50195 ? 166 ARG   B O   1 
ATOM   2910 C  CB  . ARG   B 1 154 ? 12.66000  9.82000   15.22900  1.000 17.01567 ? 166 ARG   B CB  1 
ATOM   2911 C  CG  . ARG   B 1 154 ? 11.66300  10.10100  14.14900  1.000 17.39852 ? 166 ARG   B CG  1 
ATOM   2912 C  CD  . ARG   B 1 154 ? 12.19300  9.81900   12.77600  1.000 18.60933 ? 166 ARG   B CD  1 
ATOM   2913 N  NE  . ARG   B 1 154 ? 11.12100  10.01600  11.81300  1.000 19.66155 ? 166 ARG   B NE  1 
ATOM   2914 C  CZ  . ARG   B 1 154 ? 11.28200  9.94400   10.49800  1.000 20.24552 ? 166 ARG   B CZ  1 
ATOM   2915 N  NH1 . ARG   B 1 154 ? 12.45900  9.67600   9.96700   1.000 21.38714 ? 166 ARG   B NH1 1 
ATOM   2916 N  NH2 . ARG   B 1 154 ? 10.23800  10.16700  9.70400   1.000 21.01050 ? 166 ARG   B NH2 1 
ATOM   2917 N  N   . PHE   B 1 155 ? 9.71500   9.88300   16.66100  1.000 14.19916 ? 167 PHE   B N   1 
ATOM   2918 C  CA  . PHE   B 1 155 ? 8.46600   9.15000   16.82400  1.000 14.41414 ? 167 PHE   B CA  1 
ATOM   2919 C  C   . PHE   B 1 155 ? 7.58100   9.52100   15.63700  1.000 14.76137 ? 167 PHE   B C   1 
ATOM   2920 O  O   . PHE   B 1 155 ? 6.75100   10.43100  15.69400  1.000 15.91459 ? 167 PHE   B O   1 
ATOM   2921 C  CB  . PHE   B 1 155 ? 7.80600   9.44100   18.17300  1.000 14.76724 ? 167 PHE   B CB  1 
ATOM   2922 C  CG  . PHE   B 1 155 ? 6.84600   8.37800   18.62200  1.000 13.33734 ? 167 PHE   B CG  1 
ATOM   2923 C  CD1 . PHE   B 1 155 ? 7.30400   7.18400   19.15000  1.000 15.62605 ? 167 PHE   B CD1 1 
ATOM   2924 C  CD2 . PHE   B 1 155 ? 5.47800   8.56900   18.50400  1.000 14.17622 ? 167 PHE   B CD2 1 
ATOM   2925 C  CE1 . PHE   B 1 155 ? 6.41300   6.20800   19.57800  1.000 16.42441 ? 167 PHE   B CE1 1 
ATOM   2926 C  CE2 . PHE   B 1 155 ? 4.57500   7.59400   18.92300  1.000 16.52361 ? 167 PHE   B CE2 1 
ATOM   2927 C  CZ  . PHE   B 1 155 ? 5.04800   6.41500   19.46800  1.000 14.13127 ? 167 PHE   B CZ  1 
ATOM   2928 N  N   . GLY   B 1 156 ? 7.81800   8.84500   14.51900  1.000 15.81522 ? 168 GLY   B N   1 
ATOM   2929 C  CA  . GLY   B 1 156 ? 7.12000   9.13200   13.29300  1.000 18.05683 ? 168 GLY   B CA  1 
ATOM   2930 C  C   . GLY   B 1 156 ? 7.38200   10.55500  12.83400  1.000 14.84524 ? 168 GLY   B C   1 
ATOM   2931 O  O   . GLY   B 1 156 ? 8.52700   10.98400  12.65800  1.000 16.83835 ? 168 GLY   B O   1 
ATOM   2932 N  N   . PRO   B 1 157 ? 6.31300   11.33600  12.67400  1.000 14.92364 ? 169 PRO   B N   1 
ATOM   2933 C  CA  . PRO   B 1 157 ? 6.44900   12.69800  12.14400  1.000 16.19877 ? 169 PRO   B CA  1 
ATOM   2934 C  C   . PRO   B 1 157 ? 6.88800   13.72800  13.16900  1.000 14.06581 ? 169 PRO   B C   1 
ATOM   2935 O  O   . PRO   B 1 157 ? 6.90200   14.91900  12.84600  1.000 15.68170 ? 169 PRO   B O   1 
ATOM   2936 C  CB  . PRO   B 1 157 ? 5.02400   13.00600  11.66900  1.000 17.21142 ? 169 PRO   B CB  1 
ATOM   2937 C  CG  . PRO   B 1 157 ? 4.16800   12.28900  12.67000  1.000 18.89594 ? 169 PRO   B CG  1 
ATOM   2938 C  CD  . PRO   B 1 157 ? 4.91100   10.99100  12.95900  1.000 16.34561 ? 169 PRO   B CD  1 
ATOM   2939 N  N   . VAL   B 1 158 ? 7.22800   13.32600  14.39300  1.000 14.44240 ? 170 VAL   B N   1 
ATOM   2940 C  CA  . VAL   B 1 158 ? 7.69100   14.26900  15.39800  1.000 15.14307 ? 170 VAL   B CA  1 
ATOM   2941 C  C   . VAL   B 1 158 ? 9.01000   13.79300  15.97600  1.000 13.02690 ? 170 VAL   B C   1 
ATOM   2942 O  O   . VAL   B 1 158 ? 9.38800   12.62300  15.85200  1.000 14.07170 ? 170 VAL   B O   1 
ATOM   2943 C  CB  . VAL   B 1 158 ? 6.67200   14.50000  16.54000  1.000 12.65600 ? 170 VAL   B CB  1 
ATOM   2944 C  CG1 . VAL   B 1 158 ? 5.31700   14.87600  15.98300  1.000 14.99309 ? 170 VAL   B CG1 1 
ATOM   2945 C  CG2 . VAL   B 1 158 ? 6.59600   13.28500  17.48400  1.000 14.68800 ? 170 VAL   B CG2 1 
ATOM   2946 N  N   . GLU   B 1 159 ? 9.70300   14.71400  16.62800  1.000 14.20142 ? 171 GLU   B N   1 
ATOM   2947 C  CA  . GLU   B 1 159 ? 10.78100  14.39200  17.54700  1.000 13.22051 ? 171 GLU   B CA  1 
ATOM   2948 C  C   . GLU   B 1 159 ? 10.28700  14.63200  18.97100  1.000 11.85749 ? 171 GLU   B C   1 
ATOM   2949 O  O   . GLU   B 1 159 ? 9.63700   15.65100  19.25900  1.000 13.36862 ? 171 GLU   B O   1 
ATOM   2950 C  CB  . GLU   B 1 159 ? 12.01900  15.24300  17.26300  1.000 14.73150 ? 171 GLU   B CB  1 
ATOM   2951 C  CG  . GLU   B 1 159 ? 13.22100  14.87300  18.10300  1.000 17.36115 ? 171 GLU   B CG  1 
ATOM   2952 C  CD  . GLU   B 1 159 ? 14.49200  15.54100  17.62600  1.000 19.94042 ? 171 GLU   B CD  1 
ATOM   2953 O  OE1 . GLU   B 1 159 ? 14.68700  16.73300  17.93900  1.000 21.10522 ? 171 GLU   B OE1 1 
ATOM   2954 O  OE2 . GLU   B 1 159 ? 15.29000  14.86200  16.94000  1.000 23.12432 ? 171 GLU   B OE2 1 
ATOM   2955 N  N   . LEU   B 1 160 ? 10.55400  13.67100  19.84000  1.000 12.37182 ? 172 LEU   B N   1 
ATOM   2956 C  CA  . LEU   B 1 160 ? 10.32500  13.80100  21.27200  1.000 11.98683 ? 172 LEU   B CA  1 
ATOM   2957 C  C   . LEU   B 1 160 ? 11.62000  14.21700  21.95400  1.000 12.37642 ? 172 LEU   B C   1 
ATOM   2958 O  O   . LEU   B 1 160 ? 12.69200  13.70100  21.63300  1.000 14.58378 ? 172 LEU   B O   1 
ATOM   2959 C  CB  . LEU   B 1 160 ? 9.85800   12.45400  21.83400  1.000 12.64221 ? 172 LEU   B CB  1 
ATOM   2960 C  CG  . LEU   B 1 160 ? 8.64100   11.87100  21.11800  1.000 13.70944 ? 172 LEU   B CG  1 
ATOM   2961 C  CD1 . LEU   B 1 160 ? 8.29800   10.50500  21.70900  1.000 14.25790 ? 172 LEU   B CD1 1 
ATOM   2962 C  CD2 . LEU   B 1 160 ? 7.45800   12.80500  21.18900  1.000 15.41664 ? 172 LEU   B CD2 1 
ATOM   2963 N  N   . PHE   B 1 161 ? 11.53100  15.15300  22.89800  1.000 12.41429 ? 173 PHE   B N   1 
ATOM   2964 C  CA  . PHE   B 1 161 ? 12.71300  15.68500  23.56200  1.000 12.81597 ? 173 PHE   B CA  1 
ATOM   2965 C  C   . PHE   B 1 161 ? 12.46300  15.74800  25.05600  1.000 12.81779 ? 173 PHE   B C   1 
ATOM   2966 O  O   . PHE   B 1 161 ? 11.42800  16.26300  25.48800  1.000 13.31920 ? 173 PHE   B O   1 
ATOM   2967 C  CB  . PHE   B 1 161 ? 12.99400  17.09000  23.00600  1.000 12.50014 ? 173 PHE   B CB  1 
ATOM   2968 C  CG  . PHE   B 1 161 ? 14.22700  17.75300  23.55000  1.000 13.44599 ? 173 PHE   B CG  1 
ATOM   2969 C  CD1 . PHE   B 1 161 ? 15.48400  17.24200  23.27500  1.000 16.05416 ? 173 PHE   B CD1 1 
ATOM   2970 C  CD2 . PHE   B 1 161 ? 14.13500  18.93700  24.28600  1.000 13.99073 ? 173 PHE   B CD2 1 
ATOM   2971 C  CE1 . PHE   B 1 161 ? 16.63000  17.85900  23.74700  1.000 16.20947 ? 173 PHE   B CE1 1 
ATOM   2972 C  CE2 . PHE   B 1 161 ? 15.28000  19.56500  24.76300  1.000 14.88227 ? 173 PHE   B CE2 1 
ATOM   2973 C  CZ  . PHE   B 1 161 ? 16.53500  19.02500  24.49400  1.000 16.50809 ? 173 PHE   B CZ  1 
ATOM   2974 N  N   . TYR   B 1 162 ? 13.41300  15.26000  25.84700  1.000 12.70354 ? 174 TYR   B N   1 
ATOM   2975 C  CA  . TYR   B 1 162 ? 13.32900  15.40600  27.29400  1.000 12.55478 ? 174 TYR   B CA  1 
ATOM   2976 C  C   . TYR   B 1 162 ? 14.26800  16.53200  27.69300  1.000 13.35934 ? 174 TYR   B C   1 
ATOM   2977 O  O   . TYR   B 1 162 ? 15.49900  16.35100  27.63500  1.000 13.73333 ? 174 TYR   B O   1 
ATOM   2978 C  CB  . TYR   B 1 162 ? 13.71600  14.11200  28.01500  1.000 12.81156 ? 174 TYR   B CB  1 
ATOM   2979 C  CG  . TYR   B 1 162 ? 13.78300  14.30500  29.52400  1.000 12.60560 ? 174 TYR   B CG  1 
ATOM   2980 C  CD1 . TYR   B 1 162 ? 12.73900  14.92300  30.22500  1.000 12.42963 ? 174 TYR   B CD1 1 
ATOM   2981 C  CD2 . TYR   B 1 162 ? 14.90200  13.91300  30.24500  1.000 13.02831 ? 174 TYR   B CD2 1 
ATOM   2982 C  CE1 . TYR   B 1 162 ? 12.79900  15.10200  31.59600  1.000 13.24094 ? 174 TYR   B CE1 1 
ATOM   2983 C  CE2 . TYR   B 1 162 ? 14.97900  14.09900  31.62000  1.000 13.99255 ? 174 TYR   B CE2 1 
ATOM   2984 C  CZ  . TYR   B 1 162 ? 13.91700  14.69400  32.28700  1.000 14.47474 ? 174 TYR   B CZ  1 
ATOM   2985 O  OH  . TYR   B 1 162 ? 13.96500  14.91200  33.65500  1.000 15.45940 ? 174 TYR   B OH  1 
ATOM   2986 N  N   . PRO   B 1 163 ? 13.76000  17.70400  28.08300  1.000 12.52840 ? 175 PRO   B N   1 
ATOM   2987 C  CA  . PRO   B 1 163 ? 14.64200  18.85000  28.32800  1.000 13.78796 ? 175 PRO   B CA  1 
ATOM   2988 C  C   . PRO   B 1 163 ? 15.24400  18.86600  29.72300  1.000 12.63435 ? 175 PRO   B C   1 
ATOM   2989 O  O   . PRO   B 1 163 ? 16.08900  19.72200  30.00300  1.000 14.46968 ? 175 PRO   B O   1 
ATOM   2990 C  CB  . PRO   B 1 163 ? 13.69300  20.04500  28.13400  1.000 12.45898 ? 175 PRO   B CB  1 
ATOM   2991 C  CG  . PRO   B 1 163 ? 12.36400  19.51700  28.62700  1.000 11.93082 ? 175 PRO   B CG  1 
ATOM   2992 C  CD  . PRO   B 1 163 ? 12.33400  18.06400  28.13800  1.000 11.87954 ? 175 PRO   B CD  1 
ATOM   2993 N  N   . GLY   B 1 164 ? 14.85500  17.93800  30.58500  1.000 12.48606 ? 176 GLY   B N   1 
ATOM   2994 C  CA  . GLY   B 1 164 ? 15.13700  18.03300  32.00100  1.000 12.64642 ? 176 GLY   B CA  1 
ATOM   2995 C  C   . GLY   B 1 164 ? 13.88900  18.42000  32.78200  1.000 12.27020 ? 176 GLY   B C   1 
ATOM   2996 O  O   . GLY   B 1 164 ? 12.85500  18.79300  32.22600  1.000 12.63780 ? 176 GLY   B O   1 
ATOM   2997 N  N   . ALA   B 1 165 ? 13.99700  18.31700  34.10500  1.000 12.81385 ? 177 ALA   B N   1 
ATOM   2998 C  CA  . ALA   B 1 165 ? 12.86000  18.59600  34.96800  1.000 13.01798 ? 177 ALA   B CA  1 
ATOM   2999 C  C   . ALA   B 1 165 ? 12.44900  20.05800  34.84600  1.000 11.71651 ? 177 ALA   B C   1 
ATOM   3000 O  O   . ALA   B 1 165 ? 13.29000  20.95400  34.73400  1.000 13.01892 ? 177 ALA   B O   1 
ATOM   3001 C  CB  . ALA   B 1 165 ? 13.22700  18.28000  36.41600  1.000 14.22621 ? 177 ALA   B CB  1 
ATOM   3002 N  N   . ALA   B 1 166 ? 11.13800  20.30800  34.88800  1.000 12.47535 ? 178 ALA   B N   1 
ATOM   3003 C  CA  . ALA   B 1 166 ? 10.64600  21.68400  34.79900  1.000 11.59089 ? 178 ALA   B CA  1 
ATOM   3004 C  C   . ALA   B 1 166 ? 9.31100   21.76800  35.52100  1.000 10.49576 ? 178 ALA   B C   1 
ATOM   3005 O  O   . ALA   B 1 166 ? 9.26200   21.69700  36.75200  1.000 12.59227 ? 178 ALA   B O   1 
ATOM   3006 C  CB  . ALA   B 1 166 ? 10.54500  22.11500  33.32600  1.000 13.80342 ? 178 ALA   B CB  1 
ATOM   3007 N  N   . HIS   B 1 167 ? 8.21700   21.84100  34.76600  1.000 10.93129 ? 179 HIS   B N   1 
ATOM   3008 C  CA  . HIS   B 1 167 ? 6.89200   21.72100  35.36100  1.000 11.41521 ? 179 HIS   B CA  1 
ATOM   3009 C  C   . HIS   B 1 167 ? 6.73800   20.41500  36.15000  1.000 13.04187 ? 179 HIS   B C   1 
ATOM   3010 O  O   . HIS   B 1 167 ? 6.07200   20.37900  37.19500  1.000 12.56883 ? 179 HIS   B O   1 
ATOM   3011 C  CB  . HIS   B 1 167 ? 5.87900   21.78800  34.22100  1.000 12.73723 ? 179 HIS   B CB  1 
ATOM   3012 C  CG  . HIS   B 1 167 ? 4.50800   21.39800  34.62500  1.000 12.57069 ? 179 HIS   B CG  1 
ATOM   3013 N  ND1 . HIS   B 1 167 ? 3.62800   22.28200  35.21300  1.000 14.34594 ? 179 HIS   B ND1 1 
ATOM   3014 C  CD2 . HIS   B 1 167 ? 3.86900   20.21300  34.56300  1.000 12.12904 ? 179 HIS   B CD2 1 
ATOM   3015 C  CE1 . HIS   B 1 167 ? 2.49900   21.66300  35.48300  1.000 12.92612 ? 179 HIS   B CE1 1 
ATOM   3016 N  NE2 . HIS   B 1 167 ? 2.62600   20.40600  35.11100  1.000 12.89643 ? 179 HIS   B NE2 1 
ATOM   3017 N  N   . SER   B 1 168 ? 7.33400   19.33300  35.65600  1.000 11.75447 ? 180 SER   B N   1 
ATOM   3018 C  CA  . SER   B 1 168 ? 7.39100   18.06100  36.36300  1.000 10.99360 ? 180 SER   B CA  1 
ATOM   3019 C  C   . SER   B 1 168 ? 8.72000   17.42200  36.00700  1.000 12.24284 ? 180 SER   B C   1 
ATOM   3020 O  O   . SER   B 1 168 ? 9.41700   17.87700  35.09300  1.000 13.05683 ? 180 SER   B O   1 
ATOM   3021 C  CB  . SER   B 1 168 ? 6.22400   17.15700  35.95500  1.000 13.08098 ? 180 SER   B CB  1 
ATOM   3022 O  OG  . SER   B 1 168 ? 6.27400   16.88400  34.55700  1.000 12.97095 ? 180 SER   B OG  1 
ATOM   3023 N  N   . THR   B 1 169 ? 9.07500   16.35100  36.71700  1.000 13.39887 ? 181 THR   B N   1 
ATOM   3024 C  CA  . THR   B 1 169 ? 10.38300  15.77500  36.43700  1.000 14.64560 ? 181 THR   B CA  1 
ATOM   3025 C  C   . THR   B 1 169 ? 10.40200  15.02500  35.12200  1.000 13.68642 ? 181 THR   B C   1 
ATOM   3026 O  O   . THR   B 1 169 ? 11.47900  14.82500  34.55200  1.000 15.40810 ? 181 THR   B O   1 
ATOM   3027 C  CB  . THR   B 1 169 ? 10.84100  14.87700  37.58000  1.000 16.04751 ? 181 THR   B CB  1 
ATOM   3028 O  OG1 . THR   B 1 169 ? 9.93800   13.77500  37.70000  1.000 17.24059 ? 181 THR   B OG1 1 
ATOM   3029 C  CG2 . THR   B 1 169 ? 10.86500  15.64700  38.87800  1.000 17.62104 ? 181 THR   B CG2 1 
ATOM   3030 N  N   . ASP   B 1 170 ? 9.23200   14.62300  34.62700  1.000 11.86421 ? 182 ASP   B N   1 
ATOM   3031 C  CA  . ASP   B 1 170 ? 9.12200   13.75500  33.46700  1.000 11.69636 ? 182 ASP   B CA  1 
ATOM   3032 C  C   . ASP   B 1 170 ? 8.71300   14.49400  32.20600  1.000 11.65057 ? 182 ASP   B C   1 
ATOM   3033 O  O   . ASP   B 1 170 ? 8.52100   13.84300  31.17600  1.000 12.94593 ? 182 ASP   B O   1 
ATOM   3034 C  CB  . ASP   B 1 170 ? 8.11000   12.62300  33.74200  1.000 12.35598 ? 182 ASP   B CB  1 
ATOM   3035 C  CG  . ASP   B 1 170 ? 6.71700   13.15200  34.07200  1.000 13.33507 ? 182 ASP   B CG  1 
ATOM   3036 O  OD1 . ASP   B 1 170 ? 6.61400   14.19400  34.74600  1.000 12.00998 ? 182 ASP   B OD1 1 
ATOM   3037 O  OD2 . ASP   B 1 170 ? 5.70700   12.51800  33.68100  1.000 13.09360 ? 182 ASP   B OD2 1 
ATOM   3038 N  N   . ASN   B 1 171 ? 8.56500   15.82200  32.23900  1.000 10.35803 ? 183 ASN   B N   1 
ATOM   3039 C  CA  . ASN   B 1 171 ? 7.85000   16.46500  31.13400  1.000 10.56173 ? 183 ASN   B CA  1 
ATOM   3040 C  C   . ASN   B 1 171 ? 8.65500   16.33400  29.83000  1.000 11.88755 ? 183 ASN   B C   1 
ATOM   3041 O  O   . ASN   B 1 171 ? 9.88000   16.53700  29.80300  1.000 12.16030 ? 183 ASN   B O   1 
ATOM   3042 C  CB  . ASN   B 1 171 ? 7.56300   17.96900  31.35700  1.000 11.79779 ? 183 ASN   B CB  1 
ATOM   3043 C  CG  . ASN   B 1 171 ? 8.67700   18.74600  32.07400  1.000 10.67234 ? 183 ASN   B CG  1 
ATOM   3044 O  OD1 . ASN   B 1 171 ? 8.41500   19.64100  32.88800  1.000 12.43694 ? 183 ASN   B OD1 1 
ATOM   3045 N  ND2 . ASN   B 1 171 ? 9.89900   18.29900  31.90100  1.000 13.88775 ? 183 ASN   B ND2 1 
ATOM   3046 N  N   . LEU   B 1 172 ? 7.95100   16.01000  28.75500  1.000 11.58333 ? 184 LEU   B N   1 
ATOM   3047 C  CA  . LEU   B 1 172 ? 8.50200   15.93600  27.40700  1.000 11.90201 ? 184 LEU   B CA  1 
ATOM   3048 C  C   . LEU   B 1 172 ? 7.99800   17.11100  26.57900  1.000 12.00370 ? 184 LEU   B C   1 
ATOM   3049 O  O   . LEU   B 1 172 ? 6.90700   17.64500  26.82500  1.000 12.72060 ? 184 LEU   B O   1 
ATOM   3050 C  CB  . LEU   B 1 172 ? 8.04600   14.65600  26.69200  1.000 11.87318 ? 184 LEU   B CB  1 
ATOM   3051 C  CG  . LEU   B 1 172 ? 8.47000   13.33700  27.32000  1.000 11.68187 ? 184 LEU   B CG  1 
ATOM   3052 C  CD1 . LEU   B 1 172 ? 7.96400   12.15100  26.48500  1.000 13.02062 ? 184 LEU   B CD1 1 
ATOM   3053 C  CD2 . LEU   B 1 172 ? 9.99700   13.27800  27.48100  1.000 13.85833 ? 184 LEU   B CD2 1 
ATOM   3054 N  N   . VAL   B 1 173 ? 8.79500   17.50800  25.58700  1.000 12.73871 ? 185 VAL   B N   1 
ATOM   3055 C  CA  . VAL   B 1 173 ? 8.34000   18.43500  24.55700  1.000 11.24492 ? 185 VAL   B CA  1 
ATOM   3056 C  C   . VAL   B 1 173 ? 8.38600   17.71600  23.21800  1.000 12.60074 ? 185 VAL   B C   1 
ATOM   3057 O  O   . VAL   B 1 173 ? 9.05400   16.68500  23.05100  1.000 11.80370 ? 185 VAL   B O   1 
ATOM   3058 C  CB  . VAL   B 1 173 ? 9.11800   19.77200  24.52200  1.000 14.38224 ? 185 VAL   B CB  1 
ATOM   3059 C  CG1 . VAL   B 1 173 ? 9.07200   20.44900  25.86800  1.000 15.44206 ? 185 VAL   B CG1 1 
ATOM   3060 C  CG2 . VAL   B 1 173 ? 10.53400  19.55200  24.11200  1.000 18.26781 ? 185 VAL   B CG2 1 
ATOM   3061 N  N   . VAL   B 1 174 ? 7.61000   18.23700  22.27200  1.000 12.76449 ? 186 VAL   B N   1 
ATOM   3062 C  CA  . VAL   B 1 174 ? 7.41000   17.59100  20.97900  1.000 12.35964 ? 186 VAL   B CA  1 
ATOM   3063 C  C   . VAL   B 1 174 ? 7.65700   18.61400  19.87700  1.000 12.43798 ? 186 VAL   B C   1 
ATOM   3064 O  O   . VAL   B 1 174 ? 7.12000   19.72900  19.92900  1.000 13.74589 ? 186 VAL   B O   1 
ATOM   3065 C  CB  . VAL   B 1 174 ? 5.98500   17.01900  20.86500  1.000 11.66410 ? 186 VAL   B CB  1 
ATOM   3066 C  CG1 . VAL   B 1 174 ? 5.78300   16.31100  19.51400  1.000 14.23087 ? 186 VAL   B CG1 1 
ATOM   3067 C  CG2 . VAL   B 1 174 ? 5.69200   16.06800  22.02700  1.000 12.43856 ? 186 VAL   B CG2 1 
ATOM   3068 N  N   . TYR   B 1 175 ? 8.44800   18.24000  18.86700  1.000 12.36791 ? 187 TYR   B N   1 
ATOM   3069 C  CA  . TYR   B 1 175 ? 8.73900   19.12900  17.74800  1.000 12.07585 ? 187 TYR   B CA  1 
ATOM   3070 C  C   . TYR   B 1 175 ? 8.27600   18.47700  16.45200  1.000 15.11639 ? 187 TYR   B C   1 
ATOM   3071 O  O   . TYR   B 1 175 ? 8.53200   17.29400  16.22400  1.000 13.76635 ? 187 TYR   B O   1 
ATOM   3072 C  CB  . TYR   B 1 175 ? 10.23100  19.43500  17.66500  1.000 15.34138 ? 187 TYR   B CB  1 
ATOM   3073 C  CG  . TYR   B 1 175 ? 10.54600  20.46500  16.61700  1.000 13.16205 ? 187 TYR   B CG  1 
ATOM   3074 C  CD1 . TYR   B 1 175 ? 10.09500  21.77600  16.75100  1.000 14.08836 ? 187 TYR   B CD1 1 
ATOM   3075 C  CD2 . TYR   B 1 175 ? 11.30400  20.13700  15.49500  1.000 13.97885 ? 187 TYR   B CD2 1 
ATOM   3076 C  CE1 . TYR   B 1 175 ? 10.38200  22.74400  15.78100  1.000 15.04198 ? 187 TYR   B CE1 1 
ATOM   3077 C  CE2 . TYR   B 1 175 ? 11.59700  21.10200  14.52300  1.000 16.11190 ? 187 TYR   B CE2 1 
ATOM   3078 C  CZ  . TYR   B 1 175 ? 11.12100  22.39700  14.68600  1.000 16.00058 ? 187 TYR   B CZ  1 
ATOM   3079 O  OH  . TYR   B 1 175 ? 11.36800  23.39400  13.76700  1.000 17.34308 ? 187 TYR   B OH  1 
ATOM   3080 N  N   . VAL   B 1 176 ? 7.58600   19.24200  15.61300  1.000 13.88864 ? 188 VAL   B N   1 
ATOM   3081 C  CA  . VAL   B 1 176 ? 7.14000   18.75100  14.30400  1.000 13.54558 ? 188 VAL   B CA  1 
ATOM   3082 C  C   . VAL   B 1 176 ? 8.04200   19.38400  13.25000  1.000 15.66785 ? 188 VAL   B C   1 
ATOM   3083 O  O   . VAL   B 1 176 ? 7.83400   20.55500  12.89800  1.000 15.58294 ? 188 VAL   B O   1 
ATOM   3084 C  CB  . VAL   B 1 176 ? 5.66900   19.10200  14.02400  1.000 13.46272 ? 188 VAL   B CB  1 
ATOM   3085 C  CG1 . VAL   B 1 176 ? 5.16900   18.38500  12.77000  1.000 16.04902 ? 188 VAL   B CG1 1 
ATOM   3086 C  CG2 . VAL   B 1 176 ? 4.76500   18.79800  15.23700  1.000 13.86493 ? 188 VAL   B CG2 1 
ATOM   3087 N  N   . PRO   B 1 177 ? 9.05900   18.67600  12.74200  1.000 14.87520 ? 189 PRO   B N   1 
ATOM   3088 C  CA  . PRO   B 1 177 ? 10.03900  19.35100  11.87300  1.000 18.58745 ? 189 PRO   B CA  1 
ATOM   3089 C  C   . PRO   B 1 177 ? 9.46500   19.87700  10.57300  1.000 17.52564 ? 189 PRO   B C   1 
ATOM   3090 O  O   . PRO   B 1 177 ? 9.91300   20.93500  10.11300  1.000 19.62918 ? 189 PRO   B O   1 
ATOM   3091 C  CB  . PRO   B 1 177 ? 11.14100  18.30400  11.66400  1.000 20.98706 ? 189 PRO   B CB  1 
ATOM   3092 C  CG  . PRO   B 1 177 ? 10.59300  17.02600  12.16300  1.000 21.20950 ? 189 PRO   B CG  1 
ATOM   3093 C  CD  . PRO   B 1 177 ? 9.49800   17.33300  13.14100  1.000 15.42260 ? 189 PRO   B CD  1 
ATOM   3094 N  N   . SER   B 1 178 ? 8.45800   19.21800  9.99900   1.000 17.80039 ? 190 SER   B N   1 
ATOM   3095 C  CA  . SER   B 1 178 ? 7.92900   19.65800  8.71000   1.000 19.15332 ? 190 SER   B CA  1 
ATOM   3096 C  C   . SER   B 1 178 ? 7.17200   20.97500  8.81700   1.000 22.44187 ? 190 SER   B C   1 
ATOM   3097 O  O   . SER   B 1 178 ? 6.94900   21.64100  7.79900   1.000 20.95578 ? 190 SER   B O   1 
ATOM   3098 C  CB  . SER   B 1 178 ? 7.01600   18.57600  8.13600   1.000 22.13085 ? 190 SER   B CB  1 
ATOM   3099 O  OG  . SER   B 1 178 ? 5.79600   18.50800  8.87100   1.000 28.24858 ? 190 SER   B OG  1 
ATOM   3100 N  N   . ALA   B 1 179 ? 6.77700   21.36300  10.02400  1.000 19.09705 ? 191 ALA   B N   1 
ATOM   3101 C  CA  . ALA   B 1 179 ? 5.94500   22.53200  10.24600  1.000 18.18632 ? 191 ALA   B CA  1 
ATOM   3102 C  C   . ALA   B 1 179 ? 6.59500   23.55900  11.15900  1.000 16.83809 ? 191 ALA   B C   1 
ATOM   3103 O  O   . ALA   B 1 179 ? 6.01000   24.62600  11.38400  1.000 19.45005 ? 191 ALA   B O   1 
ATOM   3104 C  CB  . ALA   B 1 179 ? 4.59100   22.11400  10.83500  1.000 21.75617 ? 191 ALA   B CB  1 
ATOM   3105 N  N   . SER   B 1 180 ? 7.77200   23.25200  11.70900  1.000 16.40357 ? 192 SER   B N   1 
ATOM   3106 C  CA  . SER   B 1 180 ? 8.46100   24.12000  12.66100  1.000 16.45023 ? 192 SER   B CA  1 
ATOM   3107 C  C   . SER   B 1 180 ? 7.58400   24.44000  13.87200  1.000 18.26580 ? 192 SER   B C   1 
ATOM   3108 O  O   . SER   B 1 180 ? 7.60800   25.55500  14.40100  1.000 16.65311 ? 192 SER   B O   1 
ATOM   3109 C  CB  . SER   B 1 180 ? 8.97600   25.40400  11.99700  1.000 19.49316 ? 192 SER   B CB  1 
ATOM   3110 O  OG  . SER   B 1 180 ? 9.80000   25.10700  10.87500  1.000 23.09815 ? 192 SER   B OG  1 
ATOM   3111 N  N   . VAL   B 1 181 ? 6.82400   23.45000  14.33300  1.000 15.18318 ? 193 VAL   B N   1 
ATOM   3112 C  CA  . VAL   B 1 181 ? 5.93500   23.61200  15.47900  1.000 15.33604 ? 193 VAL   B CA  1 
ATOM   3113 C  C   . VAL   B 1 181 ? 6.57500   22.94900  16.68700  1.000 13.94942 ? 193 VAL   B C   1 
ATOM   3114 O  O   . VAL   B 1 181 ? 6.84000   21.73800  16.66900  1.000 14.31290 ? 193 VAL   B O   1 
ATOM   3115 C  CB  . VAL   B 1 181 ? 4.55100   23.00900  15.20800  1.000 14.40028 ? 193 VAL   B CB  1 
ATOM   3116 C  CG1 . VAL   B 1 181 ? 3.72500   22.98600  16.47900  1.000 17.32446 ? 193 VAL   B CG1 1 
ATOM   3117 C  CG2 . VAL   B 1 181 ? 3.83800   23.75500  14.11000  1.000 20.07024 ? 193 VAL   B CG2 1 
ATOM   3118 N  N   . LEU   B 1 182 ? 6.79600   23.73200  17.73400  1.000 13.30392 ? 194 LEU   B N   1 
ATOM   3119 C  CA  . LEU   B 1 182 ? 7.29800   23.24500  19.01300  1.000 15.20382 ? 194 LEU   B CA  1 
ATOM   3120 C  C   . LEU   B 1 182 ? 6.14900   23.22400  20.01500  1.000 14.10159 ? 194 LEU   B C   1 
ATOM   3121 O  O   . LEU   B 1 182 ? 5.58400   24.27300  20.34300  1.000 14.72352 ? 194 LEU   B O   1 
ATOM   3122 C  CB  . LEU   B 1 182 ? 8.44300   24.13200  19.50800  1.000 13.63872 ? 194 LEU   B CB  1 
ATOM   3123 C  CG  . LEU   B 1 182 ? 8.97100   23.82000  20.90700  1.000 15.11794 ? 194 LEU   B CG  1 
ATOM   3124 C  CD1 . LEU   B 1 182 ? 9.62600   22.45500  20.92000  1.000 18.18921 ? 194 LEU   B CD1 1 
ATOM   3125 C  CD2 . LEU   B 1 182 ? 9.95600   24.86200  21.36100  1.000 19.81309 ? 194 LEU   B CD2 1 
ATOM   3126 N  N   . TYR   B 1 183 ? 5.82000   22.03100  20.51600  1.000 13.39540 ? 195 TYR   B N   1 
ATOM   3127 C  CA  . TYR   B 1 183 ? 4.77800   21.84900  21.52200  1.000 13.14443 ? 195 TYR   B CA  1 
ATOM   3128 C  C   . TYR   B 1 183 ? 5.46800   21.69200  22.86200  1.000 11.83757 ? 195 TYR   B C   1 
ATOM   3129 O  O   . TYR   B 1 183 ? 6.13400   20.68500  23.11500  1.000 12.45449 ? 195 TYR   B O   1 
ATOM   3130 C  CB  . TYR   B 1 183 ? 3.95800   20.61600  21.17700  1.000 13.69966 ? 195 TYR   B CB  1 
ATOM   3131 C  CG  . TYR   B 1 183 ? 2.92500   20.22700  22.19200  1.000 13.45350 ? 195 TYR   B CG  1 
ATOM   3132 C  CD1 . TYR   B 1 183 ? 1.68000   20.83100  22.21500  1.000 17.29725 ? 195 TYR   B CD1 1 
ATOM   3133 C  CD2 . TYR   B 1 183 ? 3.17200   19.21300  23.10300  1.000 14.65536 ? 195 TYR   B CD2 1 
ATOM   3134 C  CE1 . TYR   B 1 183 ? 0.70800   20.43700  23.10800  1.000 18.64185 ? 195 TYR   B CE1 1 
ATOM   3135 C  CE2 . TYR   B 1 183 ? 2.21300   18.81800  23.99800  1.000 14.11075 ? 195 TYR   B CE2 1 
ATOM   3136 C  CZ  . TYR   B 1 183 ? 0.99100   19.42700  24.00600  1.000 18.97962 ? 195 TYR   B CZ  1 
ATOM   3137 O  OH  . TYR   B 1 183 ? 0.03400   19.00700  24.91000  1.000 21.07283 ? 195 TYR   B OH  1 
ATOM   3138 N  N   . GLY   B 1 184 ? 5.30500   22.68400  23.72400  1.000 12.10336 ? 196 GLY   B N   1 
ATOM   3139 C  CA  . GLY   B 1 184 ? 6.03600   22.67300  24.97600  1.000 12.04782 ? 196 GLY   B CA  1 
ATOM   3140 C  C   . GLY   B 1 184 ? 5.33500   21.98400  26.11600  1.000 12.75011 ? 196 GLY   B C   1 
ATOM   3141 O  O   . GLY   B 1 184 ? 5.95700   21.75000  27.14600  1.000 12.43322 ? 196 GLY   B O   1 
ATOM   3142 N  N   . GLY   B 1 185 ? 4.05800   21.65700  25.94800  1.000 12.80111 ? 197 GLY   B N   1 
ATOM   3143 C  CA  . GLY   B 1 185 ? 3.33600   21.14500  27.09600  1.000 13.92726 ? 197 GLY   B CA  1 
ATOM   3144 C  C   . GLY   B 1 185 ? 3.37600   22.11600  28.27700  1.000 10.96387 ? 197 GLY   B C   1 
ATOM   3145 O  O   . GLY   B 1 185 ? 3.59200   23.33100  28.14000  1.000 12.06259 ? 197 GLY   B O   1 
ATOM   3146 N  N   . CYS   B 1 186 ? 3.16400   21.56400  29.46600  1.000 12.70712 ? 198 CYS   B N   1 
ATOM   3147 C  CA  . CYS   B 1 186 ? 2.96200   22.42300  30.63300  1.000 12.90397 ? 198 CYS   B CA  1 
ATOM   3148 C  C   . CYS   B 1 186 ? 4.25500   23.02700  31.16600  1.000 12.12430 ? 198 CYS   B C   1 
ATOM   3149 O  O   . CYS   B 1 186 ? 4.21200   23.86700  32.07800  1.000 13.17068 ? 198 CYS   B O   1 
ATOM   3150 C  CB  . CYS   B 1 186 ? 2.15900   21.67900  31.70400  1.000 12.50216 ? 198 CYS   B CB  1 
ATOM   3151 S  SG  . CYS   B 1 186 ? 0.64300   21.02800  30.92700  1.000 13.95711 ? 198 CYS   B SG  1 
ATOM   3152 N  N   . ALA   B 1 187 ? 5.39600   22.65500  30.58400  1.000 12.55133 ? 199 ALA   B N   1 
ATOM   3153 C  CA  . ALA   B 1 187 ? 6.67100   23.30300  30.87800  1.000 12.96141 ? 199 ALA   B CA  1 
ATOM   3154 C  C   . ALA   B 1 187 ? 6.78300   24.70400  30.28100  1.000 10.95119 ? 199 ALA   B C   1 
ATOM   3155 O  O   . ALA   B 1 187 ? 7.69000   25.44400  30.67400  1.000 12.72182 ? 199 ALA   B O   1 
ATOM   3156 C  CB  . ALA   B 1 187 ? 7.82400   22.42600  30.38600  1.000 11.72564 ? 199 ALA   B CB  1 
ATOM   3157 N  N   . ILE   B 1 188 ? 5.91100   25.07200  29.34300  1.000 11.06715 ? 200 ILE   B N   1 
ATOM   3158 C  CA  . ILE   B 1 188 ? 5.96300   26.37700  28.68100  1.000 11.65933 ? 200 ILE   B CA  1 
ATOM   3159 C  C   . ILE   B 1 188 ? 4.63900   27.07800  28.93400  1.000 12.94899 ? 200 ILE   B C   1 
ATOM   3160 O  O   . ILE   B 1 188 ? 3.57200   26.49600  28.68500  1.000 13.17259 ? 200 ILE   B O   1 
ATOM   3161 C  CB  . ILE   B 1 188 ? 6.20600   26.23200  27.16600  1.000 11.09522 ? 200 ILE   B CB  1 
ATOM   3162 C  CG1 . ILE   B 1 188 ? 7.55400   25.57300  26.88200  1.000 13.35571 ? 200 ILE   B CG1 1 
ATOM   3163 C  CG2 . ILE   B 1 188 ? 6.10700   27.59400  26.46600  1.000 13.58800 ? 200 ILE   B CG2 1 
ATOM   3164 C  CD1 . ILE   B 1 188 ? 8.76300   26.22100  27.50600  1.000 15.72627 ? 200 ILE   B CD1 1 
ATOM   3165 N  N   . TYR   B 1 189 ? 4.70900   28.33000  29.41200  1.000 11.94388 ? 201 TYR   B N   1 
ATOM   3166 C  CA  . TYR   B 1 189 ? 3.54100   29.12500  29.77100  1.000 13.39445 ? 201 TYR   B CA  1 
ATOM   3167 C  C   . TYR   B 1 189 ? 3.16600   30.07000  28.63500  1.000 11.70326 ? 201 TYR   B C   1 
ATOM   3168 O  O   . TYR   B 1 189 ? 4.03400   30.62700  27.94900  1.000 14.34325 ? 201 TYR   B O   1 
ATOM   3169 C  CB  . TYR   B 1 189 ? 3.84300   30.00700  30.99000  1.000 13.84063 ? 201 TYR   B CB  1 
ATOM   3170 C  CG  . TYR   B 1 189 ? 3.74200   29.31600  32.32600  1.000 14.89672 ? 201 TYR   B CG  1 
ATOM   3171 C  CD1 . TYR   B 1 189 ? 4.01300   27.96100  32.47100  1.000 16.92565 ? 201 TYR   B CD1 1 
ATOM   3172 C  CD2 . TYR   B 1 189 ? 3.39900   30.03700  33.46700  1.000 17.83808 ? 201 TYR   B CD2 1 
ATOM   3173 C  CE1 . TYR   B 1 189 ? 3.92000   27.33700  33.71500  1.000 16.43083 ? 201 TYR   B CE1 1 
ATOM   3174 C  CE2 . TYR   B 1 189 ? 3.30600   29.42600  34.71000  1.000 17.84873 ? 201 TYR   B CE2 1 
ATOM   3175 C  CZ  . TYR   B 1 189 ? 3.58700   28.07700  34.83100  1.000 15.86113 ? 201 TYR   B CZ  1 
ATOM   3176 O  OH  . TYR   B 1 189 ? 3.50700   27.45900  36.05800  1.000 17.65534 ? 201 TYR   B OH  1 
ATOM   3177 N  N   . GLU   B 1 190 ? 1.86100   30.27300  28.46200  1.000 14.32977 ? 202 GLU   B N   1 
ATOM   3178 C  CA  . GLU   B 1 190 ? 1.40700   31.33900  27.58200  1.000 13.74327 ? 202 GLU   B CA  1 
ATOM   3179 C  C   . GLU   B 1 190 ? 1.72300   32.70200  28.19700  1.000 13.41471 ? 202 GLU   B C   1 
ATOM   3180 O  O   . GLU   B 1 190 ? 1.89300   32.84300  29.41400  1.000 14.59432 ? 202 GLU   B O   1 
ATOM   3181 C  CB  . GLU   B 1 190 ? -0.10100  31.23300  27.34500  1.000 16.40435 ? 202 GLU   B CB  1 
ATOM   3182 C  CG  . GLU   B 1 190 ? -0.96300  31.58500  28.55500  1.000 14.80655 ? 202 GLU   B CG  1 
ATOM   3183 C  CD  . GLU   B 1 190 ? -2.43300  31.67900  28.20700  1.000 16.16649 ? 202 GLU   B CD  1 
ATOM   3184 O  OE1 . GLU   B 1 190 ? -2.75000  32.15200  27.09400  1.000 19.41716 ? 202 GLU   B OE1 1 
ATOM   3185 O  OE2 . GLU   B 1 190 ? -3.24700  31.31500  29.07400  1.000 21.02243 ? 202 GLU   B OE2 1 
ATOM   3186 N  N   . LEU   B 1 191 ? 1.80600   33.70700  27.32400  1.000 14.92320 ? 203 LEU   B N   1 
ATOM   3187 C  CA  . LEU   B 1 191 ? 2.20600   35.04900  27.75000  1.000 15.63314 ? 203 LEU   B CA  1 
ATOM   3188 C  C   . LEU   B 1 191 ? 1.24800   35.63900  28.78600  1.000 19.33589 ? 203 LEU   B C   1 
ATOM   3189 O  O   . LEU   B 1 191 ? 1.67900   36.35300  29.69600  1.000 19.90307 ? 203 LEU   B O   1 
ATOM   3190 C  CB  . LEU   B 1 191 ? 2.30300   35.96400  26.52900  1.000 14.93563 ? 203 LEU   B CB  1 
ATOM   3191 C  CG  . LEU   B 1 191 ? 3.36900   35.62000  25.49400  1.000 15.48650 ? 203 LEU   B CG  1 
ATOM   3192 C  CD1 . LEU   B 1 191 ? 3.34800   36.60500  24.31200  1.000 19.22380 ? 203 LEU   B CD1 1 
ATOM   3193 C  CD2 . LEU   B 1 191 ? 4.76400   35.55300  26.12500  1.000 18.30728 ? 203 LEU   B CD2 1 
ATOM   3194 N  N   . SER   B 1 192 ? -0.04900  35.34500  28.68000  1.000 17.57802 ? 204 SER   B N   1 
ATOM   3195 C  CA  A SER   B 1 192 ? -1.03400  35.93100  29.58600  0.333 18.92610 ? 204 SER   B CA  1 
ATOM   3196 C  CA  B SER   B 1 192 ? -1.00400  35.96600  29.59100  0.667 18.85346 ? 204 SER   B CA  1 
ATOM   3197 C  C   . SER   B 1 192 ? -0.82000  35.52600  31.04000  1.000 24.34323 ? 204 SER   B C   1 
ATOM   3198 O  O   . SER   B 1 192 ? -1.30400  36.21700  31.94500  1.000 22.86589 ? 204 SER   B O   1 
ATOM   3199 C  CB  A SER   B 1 192 ? -2.44200  35.52500  29.15600  0.333 21.38242 ? 204 SER   B CB  1 
ATOM   3200 C  CB  B SER   B 1 192 ? -2.43600  35.70900  29.12700  0.667 21.41610 ? 204 SER   B CB  1 
ATOM   3201 O  OG  A SER   B 1 192 ? -2.73400  36.01800  27.86200  0.333 20.51776 ? 204 SER   B OG  1 
ATOM   3202 O  OG  B SER   B 1 192 ? -2.80900  34.36900  29.36200  0.667 19.18161 ? 204 SER   B OG  1 
ATOM   3203 N  N   . ARG   B 1 193 ? -0.13300  34.41100  31.29000  1.000 19.38434 ? 205 ARG   B N   1 
ATOM   3204 C  CA  . ARG   B 1 193 ? 0.09700   33.94500  32.65200  1.000 20.17733 ? 205 ARG   B CA  1 
ATOM   3205 C  C   . ARG   B 1 193 ? 1.39100   34.57600  33.14300  1.000 20.18263 ? 205 ARG   B C   1 
ATOM   3206 O  O   . ARG   B 1 193 ? 2.47000   34.24900  32.64100  1.000 19.06219 ? 205 ARG   B O   1 
ATOM   3207 C  CB  . ARG   B 1 193 ? 0.18400   32.42200  32.68400  1.000 20.82507 ? 205 ARG   B CB  1 
ATOM   3208 C  CG  . ARG   B 1 193 ? -1.15500  31.75400  32.53500  1.000 22.75811 ? 205 ARG   B CG  1 
ATOM   3209 C  CD  . ARG   B 1 193 ? -1.00400  30.24300  32.54200  1.000 22.44643 ? 205 ARG   B CD  1 
ATOM   3210 N  NE  . ARG   B 1 193 ? -0.64900  29.74500  33.86600  1.000 21.37081 ? 205 ARG   B NE  1 
ATOM   3211 C  CZ  . ARG   B 1 193 ? -0.11800  28.54900  34.08700  1.000 27.15548 ? 205 ARG   B CZ  1 
ATOM   3212 N  NH1 . ARG   B 1 193 ? 0.12900   27.70700  33.09400  1.000 21.34007 ? 205 ARG   B NH1 1 
ATOM   3213 N  NH2 . ARG   B 1 193 ? 0.17300   28.18700  35.33300  1.000 26.95533 ? 205 ARG   B NH2 1 
ATOM   3214 N  N   . THR   B 1 194 ? 1.29000   35.49500  34.11000  1.000 19.51058 ? 206 THR   B N   1 
ATOM   3215 C  CA  . THR   B 1 194 ? 2.46500   36.17400  34.64200  1.000 20.11157 ? 206 THR   B CA  1 
ATOM   3216 C  C   . THR   B 1 194 ? 2.82000   35.70200  36.04000  1.000 19.88290 ? 206 THR   B C   1 
ATOM   3217 O  O   . THR   B 1 194 ? 3.74900   36.24700  36.64800  1.000 23.00519 ? 206 THR   B O   1 
ATOM   3218 C  CB  . THR   B 1 194 ? 2.29100   37.70000  34.62500  1.000 19.12721 ? 206 THR   B CB  1 
ATOM   3219 O  OG1 . THR   B 1 194 ? 1.25900   38.04700  35.55300  1.000 22.01268 ? 206 THR   B OG1 1 
ATOM   3220 C  CG2 . THR   B 1 194 ? 1.91200   38.17800  33.23000  1.000 21.98072 ? 206 THR   B CG2 1 
ATOM   3221 N  N   A SER   B 1 195 ? 2.10700   34.71300  36.57100  0.626 19.00074 ? 207 SER   B N   1 
ATOM   3222 N  N   B SER   B 1 195 ? 2.09700   34.71200  36.56300  0.374 19.08470 ? 207 SER   B N   1 
ATOM   3223 C  CA  A SER   B 1 195 ? 2.46200   34.08000  37.83000  0.626 19.27153 ? 207 SER   B CA  1 
ATOM   3224 C  CA  B SER   B 1 195 ? 2.38900   34.06500  37.83100  0.374 19.36356 ? 207 SER   B CA  1 
ATOM   3225 C  C   A SER   B 1 195 ? 2.51200   32.57200  37.62800  0.626 20.85050 ? 207 SER   B C   1 
ATOM   3226 C  C   B SER   B 1 195 ? 2.53800   32.56900  37.59300  0.374 20.85006 ? 207 SER   B C   1 
ATOM   3227 O  O   A SER   B 1 195 ? 1.85600   32.02300  36.73700  0.626 19.28885 ? 207 SER   B O   1 
ATOM   3228 O  O   B SER   B 1 195 ? 1.97200   32.01800  36.64400  0.374 19.44340 ? 207 SER   B O   1 
ATOM   3229 C  CB  A SER   B 1 195 ? 1.47500   34.43700  38.95200  0.626 21.95270 ? 207 SER   B CB  1 
ATOM   3230 C  CB  B SER   B 1 195 ? 1.25900   34.30200  38.84300  0.374 21.68181 ? 207 SER   B CB  1 
ATOM   3231 O  OG  A SER   B 1 195 ? 0.25800   33.74800  38.77500  0.626 24.28197 ? 207 SER   B OG  1 
ATOM   3232 O  OG  B SER   B 1 195 ? 1.12700   35.67700  39.14700  0.374 23.67241 ? 207 SER   B OG  1 
ATOM   3233 N  N   . ALA   B 1 196 ? 3.31000   31.91100  38.46200  1.000 18.75744 ? 208 ALA   B N   1 
ATOM   3234 C  CA  . ALA   B 1 196 ? 3.55700   30.48500  38.28700  1.000 18.57969 ? 208 ALA   B CA  1 
ATOM   3235 C  C   . ALA   B 1 196 ? 2.30900   29.64600  38.52400  1.000 21.05313 ? 208 ALA   B C   1 
ATOM   3236 O  O   . ALA   B 1 196 ? 2.14700   28.58500  37.90400  1.000 18.41612 ? 208 ALA   B O   1 
ATOM   3237 C  CB  . ALA   B 1 196 ? 4.66400   30.05500  39.24000  1.000 19.40969 ? 208 ALA   B CB  1 
ATOM   3238 N  N   . GLY   B 1 197 ? 1.42700   30.08000  39.41700  1.000 18.17384 ? 209 GLY   B N   1 
ATOM   3239 C  CA  . GLY   B 1 197 ? 0.31100   29.21300  39.73600  1.000 25.53328 ? 209 GLY   B CA  1 
ATOM   3240 C  C   . GLY   B 1 197 ? 0.74100   27.91800  40.41000  1.000 26.45921 ? 209 GLY   B C   1 
ATOM   3241 O  O   . GLY   B 1 197 ? 1.71800   27.85800  41.16600  1.000 23.27432 ? 209 GLY   B O   1 
ATOM   3242 N  N   . ASN   B 1 198 ? -0.00200  26.85500  40.11200  1.000 25.26564 ? 210 ASN   B N   1 
ATOM   3243 C  CA  . ASN   B 1 198 ? 0.22400   25.56200  40.73600  1.000 23.71487 ? 210 ASN   B CA  1 
ATOM   3244 C  C   . ASN   B 1 198 ? 1.48500   24.92600  40.15900  1.000 20.03236 ? 210 ASN   B C   1 
ATOM   3245 O  O   . ASN   B 1 198 ? 1.52200   24.59000  38.97100  1.000 25.86921 ? 210 ASN   B O   1 
ATOM   3246 C  CB  . ASN   B 1 198 ? -0.97200  24.66600  40.43200  1.000 28.35923 ? 210 ASN   B CB  1 
ATOM   3247 C  CG  . ASN   B 1 198 ? -0.86900  23.31500  41.09300  1.000 31.10742 ? 210 ASN   B CG  1 
ATOM   3248 O  OD1 . ASN   B 1 198 ? 0.07100   23.04100  41.84500  1.000 30.15680 ? 210 ASN   B OD1 1 
ATOM   3249 N  ND2 . ASN   B 1 198 ? -1.82300  22.44400  40.79000  1.000 29.27155 ? 210 ASN   B ND2 1 
ATOM   3250 N  N   . VAL   B 1 199 ? 2.50400   24.73100  41.00800  1.000 20.93048 ? 211 VAL   B N   1 
ATOM   3251 C  CA  . VAL   B 1 199 ? 3.77500   24.12700  40.61000  1.000 22.58771 ? 211 VAL   B CA  1 
ATOM   3252 C  C   . VAL   B 1 199 ? 4.22000   23.07300  41.61900  1.000 19.83960 ? 211 VAL   B C   1 
ATOM   3253 O  O   . VAL   B 1 199 ? 5.41900   22.87700  41.84700  1.000 17.19208 ? 211 VAL   B O   1 
ATOM   3254 C  CB  . VAL   B 1 199 ? 4.86300   25.20000  40.39300  1.000 19.79943 ? 211 VAL   B CB  1 
ATOM   3255 C  CG1 . VAL   B 1 199 ? 4.51600   26.07100  39.19800  1.000 22.44054 ? 211 VAL   B CG1 1 
ATOM   3256 C  CG2 . VAL   B 1 199 ? 5.02500   26.07000  41.64200  1.000 25.57306 ? 211 VAL   B CG2 1 
ATOM   3257 N  N   . ALA   B 1 200 ? 3.26300   22.34200  42.19400  1.000 18.91236 ? 212 ALA   B N   1 
ATOM   3258 C  CA  . ALA   B 1 200 ? 3.57100   21.46100  43.32000  1.000 24.26312 ? 212 ALA   B CA  1 
ATOM   3259 C  C   . ALA   B 1 200 ? 4.59100   20.37700  42.97100  1.000 19.95805 ? 212 ALA   B C   1 
ATOM   3260 O  O   . ALA   B 1 200 ? 5.37800   19.96800  43.83200  1.000 22.51144 ? 212 ALA   B O   1 
ATOM   3261 C  CB  . ALA   B 1 200 ? 2.28400   20.83700  43.86700  1.000 24.35371 ? 212 ALA   B CB  1 
ATOM   3262 N  N   . ASP   B 1 201 ? 4.61200   19.90200  41.72500  1.000 16.28093 ? 213 ASP   B N   1 
ATOM   3263 C  CA  . ASP   B 1 201 ? 5.49600   18.81000  41.33500  1.000 16.55820 ? 213 ASP   B CA  1 
ATOM   3264 C  C   . ASP   B 1 201 ? 6.67700   19.28600  40.49900  1.000 14.08570 ? 213 ASP   B C   1 
ATOM   3265 O  O   . ASP   B 1 201 ? 7.38200   18.45800  39.89300  1.000 14.96628 ? 213 ASP   B O   1 
ATOM   3266 C  CB  . ASP   B 1 201 ? 4.72300   17.70400  40.61500  1.000 17.22338 ? 213 ASP   B CB  1 
ATOM   3267 C  CG  . ASP   B 1 201 ? 3.68800   17.04800  41.51100  1.000 19.87411 ? 213 ASP   B CG  1 
ATOM   3268 O  OD1 . ASP   B 1 201 ? 3.89000   17.01900  42.75200  1.000 22.81474 ? 213 ASP   B OD1 1 
ATOM   3269 O  OD2 . ASP   B 1 201 ? 2.67500   16.56000  40.97600  1.000 19.25741 ? 213 ASP   B OD2 1 
ATOM   3270 N  N   . ALA   B 1 202 ? 6.90000   20.59600  40.45800  1.000 14.65750 ? 214 ALA   B N   1 
ATOM   3271 C  CA  . ALA   B 1 202 ? 7.90900   21.19400  39.60600  1.000 14.27352 ? 214 ALA   B CA  1 
ATOM   3272 C  C   . ALA   B 1 202 ? 9.29100   21.11200  40.23400  1.000 15.27287 ? 214 ALA   B C   1 
ATOM   3273 O  O   . ALA   B 1 202 ? 9.45100   20.92700  41.44500  1.000 18.64957 ? 214 ALA   B O   1 
ATOM   3274 C  CB  . ALA   B 1 202 ? 7.57000   22.66000  39.36000  1.000 15.36240 ? 214 ALA   B CB  1 
ATOM   3275 N  N   . ASP   B 1 203 ? 10.30600  21.27500  39.38600  1.000 14.41967 ? 215 ASP   B N   1 
ATOM   3276 C  CA  . ASP   B 1 203 ? 11.68500  21.46400  39.82800  1.000 15.35759 ? 215 ASP   B CA  1 
ATOM   3277 C  C   . ASP   B 1 203 ? 12.01600  22.90900  39.48100  1.000 13.63216 ? 215 ASP   B C   1 
ATOM   3278 O  O   . ASP   B 1 203 ? 12.45500  23.22900  38.37400  1.000 14.27776 ? 215 ASP   B O   1 
ATOM   3279 C  CB  . ASP   B 1 203 ? 12.61500  20.49800  39.14100  1.000 13.60826 ? 215 ASP   B CB  1 
ATOM   3280 C  CG  . ASP   B 1 203 ? 14.01900  20.53900  39.70600  1.000 16.03480 ? 215 ASP   B CG  1 
ATOM   3281 O  OD1 . ASP   B 1 203 ? 14.46700  21.62300  40.12800  1.000 16.18345 ? 215 ASP   B OD1 1 
ATOM   3282 O  OD2 . ASP   B 1 203 ? 14.66300  19.46200  39.68700  1.000 21.09154 ? 215 ASP   B OD2 1 
ATOM   3283 N  N   . LEU   B 1 204 ? 11.74600  23.79500  40.42700  1.000 13.75256 ? 216 LEU   B N   1 
ATOM   3284 C  CA  . LEU   B 1 204 ? 11.98800  25.21100  40.18400  1.000 14.66700 ? 216 LEU   B CA  1 
ATOM   3285 C  C   . LEU   B 1 204 ? 13.45600  25.48800  39.90300  1.000 14.51479 ? 216 LEU   B C   1 
ATOM   3286 O  O   . LEU   B 1 204 ? 13.78300  26.33500  39.05800  1.000 14.60060 ? 216 LEU   B O   1 
ATOM   3287 C  CB  . LEU   B 1 204 ? 11.53500  26.02800  41.39100  1.000 17.45128 ? 216 LEU   B CB  1 
ATOM   3288 C  CG  . LEU   B 1 204 ? 10.03200  26.06000  41.60700  1.000 20.08985 ? 216 LEU   B CG  1 
ATOM   3289 C  CD1 . LEU   B 1 204 ? 9.73900   26.84500  42.88800  1.000 22.74640 ? 216 LEU   B CD1 1 
ATOM   3290 C  CD2 . LEU   B 1 204 ? 9.37700   26.70700  40.40700  1.000 19.58134 ? 216 LEU   B CD2 1 
ATOM   3291 N  N   . ALA   B 1 205 ? 14.35400  24.80400  40.62000  1.000 15.31977 ? 217 ALA   B N   1 
ATOM   3292 C  CA  . ALA   B 1 205 ? 15.77800  25.08400  40.47000  1.000 15.32924 ? 217 ALA   B CA  1 
ATOM   3293 C  C   . ALA   B 1 205 ? 16.28700  24.72800  39.08100  1.000 14.37726 ? 217 ALA   B C   1 
ATOM   3294 O  O   . ALA   B 1 205 ? 17.20400  25.38300  38.57000  1.000 16.66852 ? 217 ALA   B O   1 
ATOM   3295 C  CB  . ALA   B 1 205 ? 16.57300  24.34100  41.53400  1.000 16.54647 ? 217 ALA   B CB  1 
ATOM   3296 N  N   A GLU   B 1 206 ? 15.70400  23.70700  38.44800  0.607 13.30957 ? 218 GLU   B N   1 
ATOM   3297 N  N   B GLU   B 1 206 ? 15.70300  23.71300  38.45100  0.393 13.42526 ? 218 GLU   B N   1 
ATOM   3298 C  CA  A GLU   B 1 206 ? 16.17400  23.23200  37.15200  0.607 15.24295 ? 218 GLU   B CA  1 
ATOM   3299 C  CA  B GLU   B 1 206 ? 16.19200  23.25000  37.16300  0.393 15.23200 ? 218 GLU   B CA  1 
ATOM   3300 C  C   A GLU   B 1 206 ? 15.36600  23.74900  35.98000  0.607 12.97711 ? 218 GLU   B C   1 
ATOM   3301 C  C   B GLU   B 1 206 ? 15.39300  23.79800  35.98800  0.393 13.06554 ? 218 GLU   B C   1 
ATOM   3302 O  O   A GLU   B 1 206 ? 15.83900  23.66000  34.84500  0.607 13.36271 ? 218 GLU   B O   1 
ATOM   3303 O  O   B GLU   B 1 206 ? 15.91900  23.84000  34.87100  0.393 13.58305 ? 218 GLU   B O   1 
ATOM   3304 C  CB  A GLU   B 1 206 ? 16.13000  21.70400  37.10700  0.607 13.90208 ? 218 GLU   B CB  1 
ATOM   3305 C  CB  B GLU   B 1 206 ? 16.20900  21.71500  37.14500  0.393 14.09630 ? 218 GLU   B CB  1 
ATOM   3306 C  CG  A GLU   B 1 206 ? 17.19200  21.06900  37.97500  0.607 16.39628 ? 218 GLU   B CG  1 
ATOM   3307 C  CG  B GLU   B 1 206 ? 16.23400  21.09800  35.78500  0.393 19.53395 ? 218 GLU   B CG  1 
ATOM   3308 C  CD  A GLU   B 1 206 ? 18.56700  21.65100  37.70100  0.607 22.66482 ? 218 GLU   B CD  1 
ATOM   3309 C  CD  B GLU   B 1 206 ? 17.61500  21.06600  35.20500  0.393 21.21995 ? 218 GLU   B CD  1 
ATOM   3310 O  OE1 A GLU   B 1 206 ? 18.92300  21.78400  36.50900  0.607 14.58454 ? 218 GLU   B OE1 1 
ATOM   3311 O  OE1 B GLU   B 1 206 ? 18.58700  21.33200  35.94600  0.393 21.46142 ? 218 GLU   B OE1 1 
ATOM   3312 O  OE2 A GLU   B 1 206 ? 19.28500  21.98400  38.67400  0.607 21.23650 ? 218 GLU   B OE2 1 
ATOM   3313 O  OE2 B GLU   B 1 206 ? 17.71800  20.82200  33.99000  0.393 15.62776 ? 218 GLU   B OE2 1 
ATOM   3314 N  N   . TRP   B 1 207 ? 14.16600  24.26800  36.22300  1.000 13.59780 ? 219 TRP   B N   1 
ATOM   3315 C  CA  . TRP   B 1 207 ? 13.27500  24.67300  35.13200  1.000 12.73077 ? 219 TRP   B CA  1 
ATOM   3316 C  C   . TRP   B 1 207 ? 13.90400  25.64500  34.13400  1.000 12.63065 ? 219 TRP   B C   1 
ATOM   3317 O  O   . TRP   B 1 207 ? 13.79500  25.39100  32.92200  1.000 13.07639 ? 219 TRP   B O   1 
ATOM   3318 C  CB  . TRP   B 1 207 ? 11.97100  25.17400  35.76900  1.000 12.91347 ? 219 TRP   B CB  1 
ATOM   3319 C  CG  . TRP   B 1 207 ? 10.76700  25.30900  34.89900  1.000 10.75620 ? 219 TRP   B CG  1 
ATOM   3320 C  CD1 . TRP   B 1 207 ? 10.71300  25.47900  33.53400  1.000 11.16618 ? 219 TRP   B CD1 1 
ATOM   3321 C  CD2 . TRP   B 1 207 ? 9.40800   25.32600  35.35800  1.000 12.11591 ? 219 TRP   B CD2 1 
ATOM   3322 N  NE1 . TRP   B 1 207 ? 9.39000   25.58200  33.12400  1.000 11.57785 ? 219 TRP   B NE1 1 
ATOM   3323 C  CE2 . TRP   B 1 207 ? 8.58100   25.48800  34.23000  1.000 11.06166 ? 219 TRP   B CE2 1 
ATOM   3324 C  CE3 . TRP   B 1 207 ? 8.81100   25.20700  36.62100  1.000 13.35156 ? 219 TRP   B CE3 1 
ATOM   3325 C  CZ2 . TRP   B 1 207 ? 7.18600   25.54400  34.33300  1.000 13.29147 ? 219 TRP   B CZ2 1 
ATOM   3326 C  CZ3 . TRP   B 1 207 ? 7.42400   25.28000  36.72100  1.000 13.09087 ? 219 TRP   B CZ3 1 
ATOM   3327 C  CH2 . TRP   B 1 207 ? 6.62700   25.44300  35.58600  1.000 13.04154 ? 219 TRP   B CH2 1 
ATOM   3328 N  N   . PRO   B 1 208 ? 14.57000  26.74500  34.54400  1.000 12.73139 ? 220 PRO   B N   1 
ATOM   3329 C  CA  . PRO   B 1 208 ? 15.19900  27.61500  33.53100  1.000 12.84243 ? 220 PRO   B CA  1 
ATOM   3330 C  C   . PRO   B 1 208 ? 16.27100  26.91800  32.71000  1.000 13.92074 ? 220 PRO   B C   1 
ATOM   3331 O  O   . PRO   B 1 208 ? 16.36700  27.15300  31.49600  1.000 14.04228 ? 220 PRO   B O   1 
ATOM   3332 C  CB  . PRO   B 1 208 ? 15.76300  28.77500  34.36500  1.000 13.47172 ? 220 PRO   B CB  1 
ATOM   3333 C  CG  . PRO   B 1 208 ? 14.89000  28.77100  35.59700  1.000 14.05506 ? 220 PRO   B CG  1 
ATOM   3334 C  CD  . PRO   B 1 208 ? 14.64000  27.32700  35.89900  1.000 13.57623 ? 220 PRO   B CD  1 
ATOM   3335 N  N   . THR   B 1 209 ? 17.06900  26.04100  33.33500  1.000 13.49058 ? 221 THR   B N   1 
ATOM   3336 C  CA  . THR   B 1 209 ? 18.07300  25.28500  32.59100  1.000 15.25889 ? 221 THR   B CA  1 
ATOM   3337 C  C   . THR   B 1 209 ? 17.41900  24.38200  31.55400  1.000 13.99538 ? 221 THR   B C   1 
ATOM   3338 O  O   . THR   B 1 209 ? 17.89800  24.27300  30.41400  1.000 15.12233 ? 221 THR   B O   1 
ATOM   3339 C  CB  . THR   B 1 209 ? 18.92200  24.46700  33.57200  1.000 14.81310 ? 221 THR   B CB  1 
ATOM   3340 O  OG1 . THR   B 1 209 ? 19.62200  25.36000  34.45300  1.000 17.73592 ? 221 THR   B OG1 1 
ATOM   3341 C  CG2 . THR   B 1 209 ? 19.92900  23.58700  32.84800  1.000 16.88268 ? 221 THR   B CG2 1 
ATOM   3342 N  N   . SER   B 1 210 ? 16.32100  23.72500  31.92700  1.000 12.08020 ? 222 SER   B N   1 
ATOM   3343 C  CA  . SER   B 1 210 ? 15.59700  22.87300  30.98300  1.000 12.77729 ? 222 SER   B CA  1 
ATOM   3344 C  C   . SER   B 1 210 ? 15.03800  23.67300  29.81200  1.000 11.88652 ? 222 SER   B C   1 
ATOM   3345 O  O   . SER   B 1 210 ? 15.07600  23.20600  28.66400  1.000 12.98610 ? 222 SER   B O   1 
ATOM   3346 C  CB  . SER   B 1 210 ? 14.48800  22.12500  31.71300  1.000 13.15172 ? 222 SER   B CB  1 
ATOM   3347 O  OG  . SER   B 1 210 ? 15.08000  21.36900  32.75100  1.000 13.20621 ? 222 SER   B OG  1 
ATOM   3348 N  N   . ILE   B 1 211 ? 14.50900  24.87700  30.08000  1.000 12.88622 ? 223 ILE   B N   1 
ATOM   3349 C  CA  . ILE   B 1 211 ? 14.04000  25.74900  28.99900  1.000 12.43764 ? 223 ILE   B CA  1 
ATOM   3350 C  C   . ILE   B 1 211 ? 15.17700  26.12900  28.06500  1.000 13.14682 ? 223 ILE   B C   1 
ATOM   3351 O  O   . ILE   B 1 211 ? 15.00700  26.14500  26.83900  1.000 14.75779 ? 223 ILE   B O   1 
ATOM   3352 C  CB  . ILE   B 1 211 ? 13.31600  26.97900  29.56500  1.000 12.63544 ? 223 ILE   B CB  1 
ATOM   3353 C  CG1 . ILE   B 1 211 ? 11.93200  26.57100  30.05800  1.000 15.12895 ? 223 ILE   B CG1 1 
ATOM   3354 C  CG2 . ILE   B 1 211 ? 13.23900  28.09100  28.50200  1.000 14.88445 ? 223 ILE   B CG2 1 
ATOM   3355 C  CD1 . ILE   B 1 211 ? 11.26000  27.61000  30.91900  1.000 18.42410 ? 223 ILE   B CD1 1 
ATOM   3356 N  N   A GLU   B 1 212 ? 16.35900  26.41500  28.61800  0.599 13.93183 ? 224 GLU   B N   1 
ATOM   3357 N  N   B GLU   B 1 212 ? 16.35700  26.41100  28.63000  0.401 13.99585 ? 224 GLU   B N   1 
ATOM   3358 C  CA  A GLU   B 1 212 ? 17.49600  26.73900  27.76000  0.599 14.29467 ? 224 GLU   B CA  1 
ATOM   3359 C  CA  B GLU   B 1 212 ? 17.53200  26.71500  27.81700  0.401 14.45734 ? 224 GLU   B CA  1 
ATOM   3360 C  C   A GLU   B 1 212 ? 17.89200  25.56000  26.87400  0.599 13.63295 ? 224 GLU   B C   1 
ATOM   3361 C  C   B GLU   B 1 212 ? 17.87400  25.56200  26.88200  0.401 13.76309 ? 224 GLU   B C   1 
ATOM   3362 O  O   A GLU   B 1 212 ? 18.31300  25.76400  25.72900  0.599 15.67554 ? 224 GLU   B O   1 
ATOM   3363 O  O   B GLU   B 1 212 ? 18.24500  25.78300  25.72300  0.401 15.69748 ? 224 GLU   B O   1 
ATOM   3364 C  CB  A GLU   B 1 212 ? 18.67400  27.24600  28.59800  0.599 16.38830 ? 224 GLU   B CB  1 
ATOM   3365 C  CB  B GLU   B 1 212 ? 18.71500  27.04600  28.73000  0.401 15.95888 ? 224 GLU   B CB  1 
ATOM   3366 C  CG  A GLU   B 1 212 ? 19.92700  27.58700  27.78900  0.599 19.03424 ? 224 GLU   B CG  1 
ATOM   3367 C  CG  B GLU   B 1 212 ? 18.65900  28.44600  29.31000  0.401 19.64513 ? 224 GLU   B CG  1 
ATOM   3368 C  CD  A GLU   B 1 212 ? 19.69300  28.64400  26.70900  0.599 21.82803 ? 224 GLU   B CD  1 
ATOM   3369 C  CD  B GLU   B 1 212 ? 19.45400  28.59600  30.59500  0.401 22.63480 ? 224 GLU   B CD  1 
ATOM   3370 O  OE1 A GLU   B 1 212 ? 18.83400  29.53300  26.89000  0.599 23.04863 ? 224 GLU   B OE1 1 
ATOM   3371 O  OE1 B GLU   B 1 212 ? 20.18900  27.65600  30.96200  0.401 27.19236 ? 224 GLU   B OE1 1 
ATOM   3372 O  OE2 A GLU   B 1 212 ? 20.38200  28.58700  25.67100  0.599 29.51208 ? 224 GLU   B OE2 1 
ATOM   3373 O  OE2 B GLU   B 1 212 ? 19.33800  29.66000  31.23800  0.401 24.12590 ? 224 GLU   B OE2 1 
ATOM   3374 N  N   . ARG   B 1 213 ? 17.74900  24.32000  27.36600  1.000 14.39466 ? 225 ARG   B N   1 
ATOM   3375 C  CA  . ARG   B 1 213 ? 17.98000  23.15800  26.50100  1.000 13.42195 ? 225 ARG   B CA  1 
ATOM   3376 C  C   . ARG   B 1 213 ? 16.99800  23.13500  25.33600  1.000 14.01629 ? 225 ARG   B C   1 
ATOM   3377 O  O   . ARG   B 1 213 ? 17.36800  22.75000  24.21700  1.000 16.38362 ? 225 ARG   B O   1 
ATOM   3378 C  CB  . ARG   B 1 213 ? 17.89700  21.84100  27.28900  1.000 14.17581 ? 225 ARG   B CB  1 
ATOM   3379 C  CG  . ARG   B 1 213 ? 19.00300  21.63000  28.31000  1.000 14.96128 ? 225 ARG   B CG  1 
ATOM   3380 C  CD  . ARG   B 1 213 ? 19.06700  20.16100  28.77100  1.000 16.70937 ? 225 ARG   B CD  1 
ATOM   3381 N  NE  . ARG   B 1 213 ? 20.01700  20.00000  29.86600  1.000 16.02551 ? 225 ARG   B NE  1 
ATOM   3382 C  CZ  . ARG   B 1 213 ? 19.71400  20.16800  31.14400  1.000 16.95815 ? 225 ARG   B CZ  1 
ATOM   3383 N  NH1 . ARG   B 1 213 ? 18.46800  20.37200  31.53700  1.000 16.29552 ? 225 ARG   B NH1 1 
ATOM   3384 N  NH2 . ARG   B 1 213 ? 20.68700  20.15400  32.05100  1.000 19.82520 ? 225 ARG   B NH2 1 
ATOM   3385 N  N   . ILE   B 1 214 ? 15.73700  23.50400  25.57900  1.000 13.61090 ? 226 ILE   B N   1 
ATOM   3386 C  CA  . ILE   B 1 214 ? 14.75700  23.56700  24.49500  1.000 13.77686 ? 226 ILE   B CA  1 
ATOM   3387 C  C   . ILE   B 1 214 ? 15.17400  24.60500  23.45800  1.000 14.97152 ? 226 ILE   B C   1 
ATOM   3388 O  O   . ILE   B 1 214 ? 15.14800  24.34500  22.25000  1.000 16.33567 ? 226 ILE   B O   1 
ATOM   3389 C  CB  . ILE   B 1 214 ? 13.35200  23.87300  25.03900  1.000 12.39353 ? 226 ILE   B CB  1 
ATOM   3390 C  CG1 . ILE   B 1 214 ? 12.91000  22.81500  26.04700  1.000 12.90400 ? 226 ILE   B CG1 1 
ATOM   3391 C  CG2 . ILE   B 1 214 ? 12.35300  23.99700  23.89200  1.000 13.75642 ? 226 ILE   B CG2 1 
ATOM   3392 C  CD1 . ILE   B 1 214 ? 11.62500  23.17400  26.77800  1.000 13.43622 ? 226 ILE   B CD1 1 
ATOM   3393 N  N   . GLN   B 1 215 ? 15.53600  25.80700  23.91700  1.000 13.45661 ? 227 GLN   B N   1 
ATOM   3394 C  CA  . GLN   B 1 215 ? 15.96600  26.86100  23.00600  1.000 14.82768 ? 227 GLN   B CA  1 
ATOM   3395 C  C   . GLN   B 1 215 ? 17.16500  26.41800  22.19000  1.000 17.46027 ? 227 GLN   B C   1 
ATOM   3396 O  O   . GLN   B 1 215 ? 17.22500  26.66000  20.97800  1.000 18.13616 ? 227 GLN   B O   1 
ATOM   3397 C  CB  . GLN   B 1 215 ? 16.32300  28.11400  23.80100  1.000 16.81051 ? 227 GLN   B CB  1 
ATOM   3398 C  CG  . GLN   B 1 215 ? 17.14700  29.14100  23.00900  1.000 22.66636 ? 227 GLN   B CG  1 
ATOM   3399 C  CD  . GLN   B 1 215 ? 16.35500  29.75300  21.86200  1.000 23.49878 ? 227 GLN   B CD  1 
ATOM   3400 O  OE1 . GLN   B 1 215 ? 15.20400  30.15300  22.03500  1.000 22.91215 ? 227 GLN   B OE1 1 
ATOM   3401 N  NE2 . GLN   B 1 215 ? 16.97100  29.82700  20.68000  1.000 22.14533 ? 227 GLN   B NE2 1 
ATOM   3402 N  N   A GLN   B 1 216 ? 18.13500  25.77400  22.84000  0.568 16.84460 ? 228 GLN   B N   1 
ATOM   3403 N  N   B GLN   B 1 216 ? 18.12000  25.74500  22.82800  0.432 16.98842 ? 228 GLN   B N   1 
ATOM   3404 C  CA  A GLN   B 1 216 ? 19.34100  25.33900  22.14200  0.568 19.77335 ? 228 GLN   B CA  1 
ATOM   3405 C  CA  B GLN   B 1 216 ? 19.33900  25.35500  22.13000  0.432 19.79290 ? 228 GLN   B CA  1 
ATOM   3406 C  C   A GLN   B 1 216 ? 19.04400  24.25400  21.11500  0.568 20.94961 ? 228 GLN   B C   1 
ATOM   3407 C  C   B GLN   B 1 216 ? 19.09900  24.20300  21.15700  0.432 20.97479 ? 228 GLN   B C   1 
ATOM   3408 O  O   A GLN   B 1 216 ? 19.70600  24.19000  20.07200  0.568 19.70217 ? 228 GLN   B O   1 
ATOM   3409 O  O   B GLN   B 1 216 ? 19.85300  24.04500  20.18800  0.432 20.00867 ? 228 GLN   B O   1 
ATOM   3410 C  CB  A GLN   B 1 216 ? 20.37100  24.84100  23.15500  0.568 22.38998 ? 228 GLN   B CB  1 
ATOM   3411 C  CB  B GLN   B 1 216 ? 20.42400  25.01700  23.15200  0.432 22.22856 ? 228 GLN   B CB  1 
ATOM   3412 C  CG  A GLN   B 1 216 ? 21.10600  25.95400  23.88400  0.568 26.91837 ? 228 GLN   B CG  1 
ATOM   3413 C  CG  B GLN   B 1 216 ? 20.94100  26.24600  23.89400  0.432 26.35893 ? 228 GLN   B CG  1 
ATOM   3414 C  CD  A GLN   B 1 216 ? 21.87500  26.86500  22.94700  0.568 28.44266 ? 228 GLN   B CD  1 
ATOM   3415 C  CD  B GLN   B 1 216 ? 22.26400  26.01200  24.59800  0.432 26.12329 ? 228 GLN   B CD  1 
ATOM   3416 O  OE1 A GLN   B 1 216 ? 22.83800  26.44400  22.30400  0.568 29.56267 ? 228 GLN   B OE1 1 
ATOM   3417 O  OE1 B GLN   B 1 216 ? 23.06700  25.17700  24.18000  0.432 38.90771 ? 228 GLN   B OE1 1 
ATOM   3418 N  NE2 A GLN   B 1 216 ? 21.45500  28.12300  22.86800  0.568 27.45878 ? 228 GLN   B NE2 1 
ATOM   3419 N  NE2 B GLN   B 1 216 ? 22.49400  26.75000  25.67900  0.432 28.52228 ? 228 GLN   B NE2 1 
ATOM   3420 N  N   . HIS   B 1 217 ? 18.06100  23.39400  21.38300  1.000 17.22620 ? 229 HIS   B N   1 
ATOM   3421 C  CA  . HIS   B 1 217 ? 17.77400  22.27200  20.49600  1.000 14.65694 ? 229 HIS   B CA  1 
ATOM   3422 C  C   . HIS   B 1 217 ? 16.82800  22.62400  19.35700  1.000 15.23869 ? 229 HIS   B C   1 
ATOM   3423 O  O   . HIS   B 1 217 ? 16.94900  22.04200  18.26700  1.000 19.10901 ? 229 HIS   B O   1 
ATOM   3424 C  CB  . HIS   B 1 217 ? 17.20100  21.10000  21.29400  1.000 17.53474 ? 229 HIS   B CB  1 
ATOM   3425 C  CG  . HIS   B 1 217 ? 17.47800  19.77400  20.66800  1.000 19.70675 ? 229 HIS   B CG  1 
ATOM   3426 N  ND1 . HIS   B 1 217 ? 18.65500  19.09000  20.88500  1.000 29.26057 ? 229 HIS   B ND1 1 
ATOM   3427 C  CD2 . HIS   B 1 217 ? 16.74100  19.00400  19.83100  1.000 21.64598 ? 229 HIS   B CD2 1 
ATOM   3428 C  CE1 . HIS   B 1 217 ? 18.63300  17.95600  20.20700  1.000 27.87613 ? 229 HIS   B CE1 1 
ATOM   3429 N  NE2 . HIS   B 1 217 ? 17.48400  17.88000  19.56000  1.000 23.20513 ? 229 HIS   B NE2 1 
ATOM   3430 N  N   . TYR   B 1 218 ? 15.91300  23.57200  19.57300  1.000 16.40524 ? 230 TYR   B N   1 
ATOM   3431 C  CA  . TYR   B 1 218 ? 14.91500  23.94700  18.56700  1.000 16.00209 ? 230 TYR   B CA  1 
ATOM   3432 C  C   . TYR   B 1 218 ? 14.92400  25.44600  18.28000  1.000 16.62728 ? 230 TYR   B C   1 
ATOM   3433 O  O   . TYR   B 1 218 ? 13.87500  26.09000  18.27400  1.000 16.72582 ? 230 TYR   B O   1 
ATOM   3434 C  CB  . TYR   B 1 218 ? 13.52300  23.50600  19.01400  1.000 17.00684 ? 230 TYR   B CB  1 
ATOM   3435 C  CG  . TYR   B 1 218 ? 13.44100  22.02400  19.21600  1.000 15.98115 ? 230 TYR   B CG  1 
ATOM   3436 C  CD1 . TYR   B 1 218 ? 13.57700  21.15600  18.14100  1.000 15.72442 ? 230 TYR   B CD1 1 
ATOM   3437 C  CD2 . TYR   B 1 218 ? 13.26900  21.48500  20.48800  1.000 15.37766 ? 230 TYR   B CD2 1 
ATOM   3438 C  CE1 . TYR   B 1 218 ? 13.52500  19.78200  18.31900  1.000 17.87623 ? 230 TYR   B CE1 1 
ATOM   3439 C  CE2 . TYR   B 1 218 ? 13.19100  20.11300  20.67700  1.000 17.00750 ? 230 TYR   B CE2 1 
ATOM   3440 C  CZ  . TYR   B 1 218 ? 13.33000  19.27300  19.58900  1.000 16.64106 ? 230 TYR   B CZ  1 
ATOM   3441 O  OH  . TYR   B 1 218 ? 13.27200  17.90800  19.76000  1.000 17.81511 ? 230 TYR   B OH  1 
ATOM   3442 N  N   . PRO   B 1 219 ? 16.09600  26.03300  17.98700  1.000 17.72042 ? 231 PRO   B N   1 
ATOM   3443 C  CA  . PRO   B 1 219 ? 16.13400  27.48300  17.74700  1.000 18.40733 ? 231 PRO   B CA  1 
ATOM   3444 C  C   . PRO   B 1 219 ? 15.42900  27.91100  16.47100  1.000 16.65026 ? 231 PRO   B C   1 
ATOM   3445 O  O   . PRO   B 1 219 ? 15.12400  29.09900  16.31800  1.000 17.88955 ? 231 PRO   B O   1 
ATOM   3446 C  CB  . PRO   B 1 219 ? 17.63500  27.78500  17.70000  1.000 18.92943 ? 231 PRO   B CB  1 
ATOM   3447 C  CG  . PRO   B 1 219 ? 18.22400  26.55000  17.15000  1.000 18.54501 ? 231 PRO   B CG  1 
ATOM   3448 C  CD  . PRO   B 1 219 ? 17.42200  25.42000  17.78200  1.000 18.29675 ? 231 PRO   B CD  1 
ATOM   3449 N  N   . GLU   B 1 220 ? 15.12000  26.97100  15.59000  1.000 16.06331 ? 232 GLU   B N   1 
ATOM   3450 C  CA  . GLU   B 1 220 ? 14.39100  27.22600  14.35700  1.000 17.34800 ? 232 GLU   B CA  1 
ATOM   3451 C  C   . GLU   B 1 220 ? 12.87900  27.23000  14.54600  1.000 17.86450 ? 232 GLU   B C   1 
ATOM   3452 O  O   . GLU   B 1 220 ? 12.15600  27.49200  13.58100  1.000 19.15331 ? 232 GLU   B O   1 
ATOM   3453 C  CB  . GLU   B 1 220 ? 14.79600  26.19200  13.29300  1.000 17.82933 ? 232 GLU   B CB  1 
ATOM   3454 C  CG  . GLU   B 1 220 ? 14.16200  24.80600  13.46100  1.000 20.54248 ? 232 GLU   B CG  1 
ATOM   3455 C  CD  . GLU   B 1 220 ? 14.96300  23.87300  14.35200  1.000 20.62202 ? 232 GLU   B CD  1 
ATOM   3456 O  OE1 . GLU   B 1 220 ? 15.68900  24.35300  15.24800  1.000 19.16639 ? 232 GLU   B OE1 1 
ATOM   3457 O  OE2 . GLU   B 1 220 ? 14.87800  22.64300  14.15000  1.000 22.37259 ? 232 GLU   B OE2 1 
ATOM   3458 N  N   . ALA   B 1 221 ? 12.37400  26.92500  15.75000  1.000 16.59021 ? 233 ALA   B N   1 
ATOM   3459 C  CA  . ALA   B 1 221 ? 10.93100  26.78600  15.91300  1.000 16.52090 ? 233 ALA   B CA  1 
ATOM   3460 C  C   . ALA   B 1 221 ? 10.21600  28.09500  15.60000  1.000 17.97166 ? 233 ALA   B C   1 
ATOM   3461 O  O   . ALA   B 1 221 ? 10.65400  29.17300  16.00600  1.000 18.44495 ? 233 ALA   B O   1 
ATOM   3462 C  CB  . ALA   B 1 221 ? 10.60100  26.34500  17.34000  1.000 15.66406 ? 233 ALA   B CB  1 
ATOM   3463 N  N   . GLN   B 1 222 ? 9.10700   27.99800  14.86700  1.000 16.89633 ? 234 GLN   B N   1 
ATOM   3464 C  CA  . GLN   B 1 222 ? 8.32600   29.16600  14.47000  1.000 18.86096 ? 234 GLN   B CA  1 
ATOM   3465 C  C   . GLN   B 1 222 ? 7.01800   29.31600  15.22000  1.000 23.43202 ? 234 GLN   B C   1 
ATOM   3466 O  O   . GLN   B 1 222 ? 6.54900   30.44000  15.40600  1.000 24.31171 ? 234 GLN   B O   1 
ATOM   3467 C  CB  . GLN   B 1 222 ? 8.01800   29.13100  12.96900  1.000 22.45267 ? 234 GLN   B CB  1 
ATOM   3468 C  CG  . GLN   B 1 222 ? 9.25000   29.34600  12.14200  1.000 22.89393 ? 234 GLN   B CG  1 
ATOM   3469 C  CD  . GLN   B 1 222 ? 9.83900   30.71400  12.42300  1.000 35.68748 ? 234 GLN   B CD  1 
ATOM   3470 O  OE1 . GLN   B 1 222 ? 10.85800  30.83000  13.10900  1.000 36.55215 ? 234 GLN   B OE1 1 
ATOM   3471 N  NE2 . GLN   B 1 222 ? 9.15900   31.76100  11.96900  1.000 35.58008 ? 234 GLN   B NE2 1 
ATOM   3472 N  N   A PHE   B 1 223 ? 6.44400   28.21500  15.71900  0.508 17.01317 ? 235 PHE   B N   1 
ATOM   3473 N  N   B PHE   B 1 223 ? 6.38300   28.21400  15.57400  0.492 17.40655 ? 235 PHE   B N   1 
ATOM   3474 C  CA  A PHE   B 1 223 ? 5.11900   28.18600  16.34000  0.508 17.31464 ? 235 PHE   B CA  1 
ATOM   3475 C  CA  B PHE   B 1 223 ? 5.18900   28.23700  16.38700  0.492 17.27195 ? 235 PHE   B CA  1 
ATOM   3476 C  C   A PHE   B 1 223 ? 5.23200   27.38800  17.63400  0.508 14.58917 ? 235 PHE   B C   1 
ATOM   3477 C  C   B PHE   B 1 223 ? 5.52700   27.49600  17.66300  0.492 15.85204 ? 235 PHE   B C   1 
ATOM   3478 O  O   A PHE   B 1 223 ? 5.44300   26.17200  17.58400  0.508 15.25139 ? 235 PHE   B O   1 
ATOM   3479 O  O   B PHE   B 1 223 ? 6.21500   26.46500  17.63300  0.492 14.76424 ? 235 PHE   B O   1 
ATOM   3480 C  CB  A PHE   B 1 223 ? 4.13100   27.49600  15.39500  0.508 18.75850 ? 235 PHE   B CB  1 
ATOM   3481 C  CB  B PHE   B 1 223 ? 4.01500   27.57000  15.66400  0.492 18.62495 ? 235 PHE   B CB  1 
ATOM   3482 C  CG  A PHE   B 1 223 ? 2.69800   27.90300  15.58700  0.508 21.25088 ? 235 PHE   B CG  1 
ATOM   3483 C  CG  B PHE   B 1 223 ? 3.83600   28.03400  14.24200  0.492 22.07438 ? 235 PHE   B CG  1 
ATOM   3484 C  CD1 A PHE   B 1 223 ? 2.17600   28.99300  14.90800  0.508 22.72905 ? 235 PHE   B CD1 1 
ATOM   3485 C  CD1 B PHE   B 1 223 ? 4.47700   27.38600  13.19900  0.492 21.01814 ? 235 PHE   B CD1 1 
ATOM   3486 C  CD2 A PHE   B 1 223 ? 1.86000   27.17600  16.41600  0.508 19.16832 ? 235 PHE   B CD2 1 
ATOM   3487 C  CD2 B PHE   B 1 223 ? 3.04300   29.13400  13.95300  0.492 21.94134 ? 235 PHE   B CD2 1 
ATOM   3488 C  CE1 A PHE   B 1 223 ? 0.85500   29.36800  15.07900  0.508 23.52740 ? 235 PHE   B CE1 1 
ATOM   3489 C  CE1 B PHE   B 1 223 ? 4.31900   27.81100  11.88900  0.492 20.48854 ? 235 PHE   B CE1 1 
ATOM   3490 C  CE2 A PHE   B 1 223 ? 0.53700   27.54800  16.58400  0.508 22.01856 ? 235 PHE   B CE2 1 
ATOM   3491 C  CE2 B PHE   B 1 223 ? 2.88300   29.56400  12.64500  0.492 24.82780 ? 235 PHE   B CE2 1 
ATOM   3492 C  CZ  A PHE   B 1 223 ? 0.03600   28.64300  15.91700  0.508 24.43527 ? 235 PHE   B CZ  1 
ATOM   3493 C  CZ  B PHE   B 1 223 ? 3.52300   28.90400  11.61500  0.492 24.38980 ? 235 PHE   B CZ  1 
ATOM   3494 N  N   . VAL   B 1 224 ? 5.09800   28.05600  18.78300  1.000 14.08007 ? 236 VAL   B N   1 
ATOM   3495 C  CA  . VAL   B 1 224 ? 5.30700   27.43800  20.09100  1.000 15.30964 ? 236 VAL   B CA  1 
ATOM   3496 C  C   . VAL   B 1 224 ? 3.96200   27.32400  20.79300  1.000 13.43544 ? 236 VAL   B C   1 
ATOM   3497 O  O   . VAL   B 1 224 ? 3.25300   28.32300  20.95600  1.000 15.31538 ? 236 VAL   B O   1 
ATOM   3498 C  CB  . VAL   B 1 224 ? 6.32800   28.21800  20.93800  1.000 16.22992 ? 236 VAL   B CB  1 
ATOM   3499 C  CG1 . VAL   B 1 224 ? 6.51300   27.54900  22.30800  1.000 18.29555 ? 236 VAL   B CG1 1 
ATOM   3500 C  CG2 . VAL   B 1 224 ? 7.64900   28.30600  20.20300  1.000 20.04814 ? 236 VAL   B CG2 1 
ATOM   3501 N  N   A ILE   B 1 225 ? 3.62400   26.10300  21.19400  0.263 13.97932 ? 237 ILE   B N   1 
ATOM   3502 N  N   B ILE   B 1 225 ? 3.61000   26.11900  21.22300  0.737 14.00512 ? 237 ILE   B N   1 
ATOM   3503 C  CA  A ILE   B 1 225 ? 2.35400   25.77900  21.83700  0.263 14.99041 ? 237 ILE   B CA  1 
ATOM   3504 C  CA  B ILE   B 1 225 ? 2.30700   25.84400  21.82300  0.737 14.94668 ? 237 ILE   B CA  1 
ATOM   3505 C  C   A ILE   B 1 225 ? 2.61800   25.59200  23.32700  0.263 15.00592 ? 237 ILE   B C   1 
ATOM   3506 C  C   B ILE   B 1 225 ? 2.49300   25.51600  23.30000  0.737 14.91114 ? 237 ILE   B C   1 
ATOM   3507 O  O   A ILE   B 1 225 ? 3.46400   24.75900  23.69300  0.263 14.96793 ? 237 ILE   B O   1 
ATOM   3508 O  O   B ILE   B 1 225 ? 3.12300   24.49800  23.63400  0.737 13.09486 ? 237 ILE   B O   1 
ATOM   3509 C  CB  A ILE   B 1 225 ? 1.75300   24.49700  21.24500  0.263 14.84875 ? 237 ILE   B CB  1 
ATOM   3510 C  CB  B ILE   B 1 225 ? 1.58500   24.70300  21.10400  0.737 15.82787 ? 237 ILE   B CB  1 
ATOM   3511 C  CG1 A ILE   B 1 225 ? 1.71300   24.58000  19.72100  0.263 16.37715 ? 237 ILE   B CG1 1 
ATOM   3512 C  CG1 B ILE   B 1 225 ? 1.55600   25.00000  19.60900  0.737 16.50072 ? 237 ILE   B CG1 1 
ATOM   3513 C  CG2 A ILE   B 1 225 ? 0.36500   24.24000  21.82200  0.263 13.81400 ? 237 ILE   B CG2 1 
ATOM   3514 C  CG2 B ILE   B 1 225 ? 0.17400   24.51000  21.66000  0.737 15.53395 ? 237 ILE   B CG2 1 
ATOM   3515 C  CD1 A ILE   B 1 225 ? 0.70400   25.55300  19.22600  0.263 18.05719 ? 237 ILE   B CD1 1 
ATOM   3516 C  CD1 B ILE   B 1 225 ? 1.22500   23.82300  18.82700  0.737 18.46259 ? 237 ILE   B CD1 1 
ATOM   3517 N  N   . PRO   B 1 226 ? 1.93100   26.31200  24.20600  1.000 13.27734 ? 238 PRO   B N   1 
ATOM   3518 C  CA  . PRO   B 1 226 ? 1.99700   25.99900  25.63500  1.000 12.45271 ? 238 PRO   B CA  1 
ATOM   3519 C  C   . PRO   B 1 226 ? 0.96800   24.92500  25.98000  1.000 12.44636 ? 238 PRO   B C   1 
ATOM   3520 O  O   . PRO   B 1 226 ? 0.05000   24.63500  25.21100  1.000 13.77923 ? 238 PRO   B O   1 
ATOM   3521 C  CB  . PRO   B 1 226 ? 1.62200   27.34000  26.28200  1.000 15.39634 ? 238 PRO   B CB  1 
ATOM   3522 C  CG  . PRO   B 1 226 ? 0.60100   27.89500  25.33300  1.000 15.31602 ? 238 PRO   B CG  1 
ATOM   3523 C  CD  . PRO   B 1 226 ? 1.10900   27.51500  23.94500  1.000 14.52458 ? 238 PRO   B CD  1 
ATOM   3524 N  N   . GLY   B 1 227 ? 1.12500   24.34400  27.17300  1.000 12.47853 ? 239 GLY   B N   1 
ATOM   3525 C  CA  . GLY   B 1 227 ? 0.14200   23.39000  27.65400  1.000 14.05891 ? 239 GLY   B CA  1 
ATOM   3526 C  C   . GLY   B 1 227 ? -1.24300  23.98600  27.81300  1.000 14.15526 ? 239 GLY   B C   1 
ATOM   3527 O  O   . GLY   B 1 227 ? -2.24600  23.27700  27.71300  1.000 13.90367 ? 239 GLY   B O   1 
ATOM   3528 N  N   . HIS   B 1 228 ? -1.31300  25.29000  28.09200  1.000 14.07397 ? 240 HIS   B N   1 
ATOM   3529 C  CA  . HIS   B 1 228 ? -2.57700  25.97900  28.33600  1.000 13.82092 ? 240 HIS   B CA  1 
ATOM   3530 C  C   . HIS   B 1 228 ? -2.50400  27.35200  27.69800  1.000 15.02268 ? 240 HIS   B C   1 
ATOM   3531 O  O   . HIS   B 1 228 ? -1.58700  28.12900  27.99000  1.000 15.64330 ? 240 HIS   B O   1 
ATOM   3532 C  CB  . HIS   B 1 228 ? -2.80800  26.13500  29.83600  1.000 14.94699 ? 240 HIS   B CB  1 
ATOM   3533 C  CG  . HIS   B 1 228 ? -2.78800  24.83000  30.55000  1.000 14.20242 ? 240 HIS   B CG  1 
ATOM   3534 N  ND1 . HIS   B 1 228 ? -3.88700  24.00100  30.63400  1.000 14.26218 ? 240 HIS   B ND1 1 
ATOM   3535 C  CD2 . HIS   B 1 228 ? -1.77900  24.18600  31.17800  1.000 15.24704 ? 240 HIS   B CD2 1 
ATOM   3536 C  CE1 . HIS   B 1 228 ? -3.55500  22.90000  31.27900  1.000 14.58943 ? 240 HIS   B CE1 1 
ATOM   3537 N  NE2 . HIS   B 1 228 ? -2.28400  22.99600  31.62500  1.000 13.91285 ? 240 HIS   B NE2 1 
ATOM   3538 N  N   . GLY   B 1 229 ? -3.45700  27.65300  26.83100  1.000 15.44654 ? 241 GLY   B N   1 
ATOM   3539 C  CA  . GLY   B 1 229 ? -3.58800  29.00100  26.31900  1.000 15.49732 ? 241 GLY   B CA  1 
ATOM   3540 C  C   . GLY   B 1 229 ? -2.99900  29.21700  24.93700  1.000 17.01309 ? 241 GLY   B C   1 
ATOM   3541 O  O   . GLY   B 1 229 ? -2.79700  28.29600  24.14000  1.000 17.69235 ? 241 GLY   B O   1 
ATOM   3542 N  N   . LEU   B 1 230 ? -2.72400  30.47100  24.65200  1.000 15.52309 ? 242 LEU   B N   1 
ATOM   3543 C  CA  . LEU   B 1 230 ? -2.48200  30.92100  23.28600  1.000 15.88217 ? 242 LEU   B CA  1 
ATOM   3544 C  C   . LEU   B 1 230 ? -1.07100  30.57700  22.81400  1.000 17.14699 ? 242 LEU   B C   1 
ATOM   3545 O  O   . LEU   B 1 230 ? -0.10300  30.77100  23.55100  1.000 15.70076 ? 242 LEU   B O   1 
ATOM   3546 C  CB  . LEU   B 1 230 ? -2.66000  32.43200  23.19700  1.000 17.07699 ? 242 LEU   B CB  1 
ATOM   3547 C  CG  . LEU   B 1 230 ? -4.01900  32.99700  23.57500  1.000 23.50969 ? 242 LEU   B CG  1 
ATOM   3548 C  CD1 . LEU   B 1 230 ? -3.99800  34.52800  23.41700  1.000 19.13369 ? 242 LEU   B CD1 1 
ATOM   3549 C  CD2 . LEU   B 1 230 ? -5.10100  32.36300  22.72400  1.000 23.73970 ? 242 LEU   B CD2 1 
ATOM   3550 N  N   . PRO   B 1 231 ? -0.93100  30.09300  21.58100  1.000 17.22562 ? 243 PRO   B N   1 
ATOM   3551 C  CA  . PRO   B 1 231 ? 0.40100   29.90100  21.00100  1.000 17.56851 ? 243 PRO   B CA  1 
ATOM   3552 C  C   . PRO   B 1 231 ? 1.12200   31.21500  20.76000  1.000 17.02767 ? 243 PRO   B C   1 
ATOM   3553 O  O   . PRO   B 1 231 ? 0.54100   32.30700  20.76200  1.000 18.21942 ? 243 PRO   B O   1 
ATOM   3554 C  CB  . PRO   B 1 231 ? 0.12400   29.18600  19.66900  1.000 21.06573 ? 243 PRO   B CB  1 
ATOM   3555 C  CG  . PRO   B 1 231 ? -1.27000  28.61800  19.81200  1.000 26.33813 ? 243 PRO   B CG  1 
ATOM   3556 C  CD  . PRO   B 1 231 ? -2.00400  29.57900  20.71800  1.000 22.21900 ? 243 PRO   B CD  1 
ATOM   3557 N  N   . GLY   B 1 232 ? 2.40800   31.09000  20.54400  1.000 16.29041 ? 244 GLY   B N   1 
ATOM   3558 C  CA  . GLY   B 1 232 ? 3.23800   32.22100  20.18000  1.000 17.28708 ? 244 GLY   B CA  1 
ATOM   3559 C  C   . GLY   B 1 232 ? 4.47300   31.73700  19.48600  1.000 19.06051 ? 244 GLY   B C   1 
ATOM   3560 O  O   . GLY   B 1 232 ? 4.46300   30.70200  18.81600  1.000 16.81745 ? 244 GLY   B O   1 
ATOM   3561 N  N   . GLY   B 1 233 ? 5.55800   32.49100  19.62700  1.000 18.26955 ? 245 GLY   B N   1 
ATOM   3562 C  CA  . GLY   B 1 233 ? 6.84200   32.09100  19.12600  1.000 21.20561 ? 245 GLY   B CA  1 
ATOM   3563 C  C   . GLY   B 1 233 ? 7.77300   31.67800  20.24200  1.000 17.43590 ? 245 GLY   B C   1 
ATOM   3564 O  O   . GLY   B 1 233 ? 7.35100   31.42700  21.38000  1.000 18.28060 ? 245 GLY   B O   1 
ATOM   3565 N  N   . LEU   B 1 234 ? 9.06500   31.60700  19.91500  1.000 17.28699 ? 246 LEU   B N   1 
ATOM   3566 C  CA  . LEU   B 1 234 ? 10.05900  31.23400  20.91100  1.000 17.51814 ? 246 LEU   B CA  1 
ATOM   3567 C  C   . LEU   B 1 234 ? 10.10200  32.20200  22.08800  1.000 17.31516 ? 246 LEU   B C   1 
ATOM   3568 O  O   . LEU   B 1 234 ? 10.66700  31.85300  23.12500  1.000 17.26543 ? 246 LEU   B O   1 
ATOM   3569 C  CB  . LEU   B 1 234 ? 11.44200  31.03800  20.26800  1.000 18.43860 ? 246 LEU   B CB  1 
ATOM   3570 C  CG  . LEU   B 1 234 ? 11.67200  29.67900  19.58800  1.000 17.41853 ? 246 LEU   B CG  1 
ATOM   3571 C  CD1 . LEU   B 1 234 ? 12.90500  29.69300  18.69300  1.000 21.78686 ? 246 LEU   B CD1 1 
ATOM   3572 C  CD2 . LEU   B 1 234 ? 11.77800  28.54900  20.59900  1.000 19.44606 ? 246 LEU   B CD2 1 
ATOM   3573 N  N   . ASP   B 1 235 ? 9.52000   33.40600  21.96900  1.000 18.28824 ? 247 ASP   B N   1 
ATOM   3574 C  CA  A ASP   B 1 235 ? 9.41200   34.33200  23.09600  0.462 18.61105 ? 247 ASP   B CA  1 
ATOM   3575 C  CA  B ASP   B 1 235 ? 9.49200   34.29200  23.12300  0.538 18.53053 ? 247 ASP   B CA  1 
ATOM   3576 C  C   . ASP   B 1 235 ? 8.73400   33.69700  24.30400  1.000 18.83068 ? 247 ASP   B C   1 
ATOM   3577 O  O   . ASP   B 1 235 ? 8.94000   34.13900  25.43500  1.000 15.44306 ? 247 ASP   B O   1 
ATOM   3578 C  CB  A ASP   B 1 235 ? 8.60000   35.57700  22.68200  0.462 21.18193 ? 247 ASP   B CB  1 
ATOM   3579 C  CB  B ASP   B 1 235 ? 8.96600   35.67900  22.75000  0.538 20.09583 ? 247 ASP   B CB  1 
ATOM   3580 C  CG  A ASP   B 1 235 ? 9.47500   36.75000  22.23900  0.462 24.31578 ? 247 ASP   B CG  1 
ATOM   3581 C  CG  B ASP   B 1 235 ? 7.72500   35.62400  21.88700  0.538 19.90892 ? 247 ASP   B CG  1 
ATOM   3582 O  OD1 A ASP   B 1 235 ? 10.69900  36.55800  22.07300  0.462 25.05068 ? 247 ASP   B OD1 1 
ATOM   3583 O  OD1 B ASP   B 1 235 ? 7.08200   34.55600  21.81000  0.538 22.86813 ? 247 ASP   B OD1 1 
ATOM   3584 O  OD2 A ASP   B 1 235 ? 8.93000   37.87000  22.06100  0.462 28.78952 ? 247 ASP   B OD2 1 
ATOM   3585 O  OD2 B ASP   B 1 235 ? 7.39500   36.66300  21.27900  0.538 24.49467 ? 247 ASP   B OD2 1 
ATOM   3586 N  N   . LEU   B 1 236 ? 7.91000   32.66600  24.09200  1.000 16.47496 ? 248 LEU   B N   1 
ATOM   3587 C  CA  . LEU   B 1 236 ? 7.25400   32.04000  25.23600  1.000 15.55466 ? 248 LEU   B CA  1 
ATOM   3588 C  C   . LEU   B 1 236 ? 8.26100   31.39200  26.17800  1.000 13.46757 ? 248 LEU   B C   1 
ATOM   3589 O  O   . LEU   B 1 236 ? 7.97700   31.24000  27.36900  1.000 14.11331 ? 248 LEU   B O   1 
ATOM   3590 C  CB  . LEU   B 1 236 ? 6.22100   31.01800  24.76700  1.000 14.61120 ? 248 LEU   B CB  1 
ATOM   3591 C  CG  . LEU   B 1 236 ? 4.77800   31.48100  24.50000  1.000 20.15311 ? 248 LEU   B CG  1 
ATOM   3592 C  CD1 . LEU   B 1 236 ? 4.65300   32.60500  23.45800  1.000 21.46244 ? 248 LEU   B CD1 1 
ATOM   3593 C  CD2 . LEU   B 1 236 ? 3.87900   30.29500  24.12900  1.000 16.38697 ? 248 LEU   B CD2 1 
ATOM   3594 N  N   . LEU   B 1 237 ? 9.43100   31.00000  25.67100  1.000 14.47324 ? 249 LEU   B N   1 
ATOM   3595 C  CA  . LEU   B 1 237 ? 10.42600  30.36000  26.52600  1.000 15.64516 ? 249 LEU   B CA  1 
ATOM   3596 C  C   . LEU   B 1 237 ? 11.00400  31.34400  27.53800  1.000 15.80924 ? 249 LEU   B C   1 
ATOM   3597 O  O   . LEU   B 1 237 ? 11.06600  31.05000  28.73600  1.000 14.31839 ? 249 LEU   B O   1 
ATOM   3598 C  CB  . LEU   B 1 237 ? 11.53700  29.76300  25.65900  1.000 15.09937 ? 249 LEU   B CB  1 
ATOM   3599 C  CG  . LEU   B 1 237 ? 11.31800  28.34800  25.11900  1.000 18.61610 ? 249 LEU   B CG  1 
ATOM   3600 C  CD1 . LEU   B 1 237 ? 10.09100  28.31100  24.23300  1.000 17.20160 ? 249 LEU   B CD1 1 
ATOM   3601 C  CD2 . LEU   B 1 237 ? 12.55600  27.88900  24.36000  1.000 20.93992 ? 249 LEU   B CD2 1 
ATOM   3602 N  N   . LYS   B 1 238 ? 11.46300  32.50700  27.06700  1.000 16.63202 ? 250 LYS   B N   1 
ATOM   3603 C  CA  . LYS   B 1 238 ? 11.95300  33.54300  27.97300  1.000 18.02251 ? 250 LYS   B CA  1 
ATOM   3604 C  C   . LYS   B 1 238 ? 10.86500  34.01200  28.92000  1.000 14.48287 ? 250 LYS   B C   1 
ATOM   3605 O  O   . LYS   B 1 238 ? 11.13300  34.27100  30.09900  1.000 14.71260 ? 250 LYS   B O   1 
ATOM   3606 C  CB  . LYS   B 1 238 ? 12.43200  34.73100  27.14100  1.000 19.68343 ? 250 LYS   B CB  1 
ATOM   3607 C  CG  . LYS   B 1 238 ? 12.96600  35.94200  27.89500  1.000 29.84590 ? 250 LYS   B CG  1 
ATOM   3608 C  CD  . LYS   B 1 238 ? 14.18700  35.70200  28.74000  1.000 33.09705 ? 250 LYS   B CD  1 
ATOM   3609 C  CE  . LYS   B 1 238 ? 14.68600  37.04900  29.28000  1.000 36.45043 ? 250 LYS   B CE  1 
ATOM   3610 N  NZ  . LYS   B 1 238 ? 15.76600  36.92800  30.30500  1.000 52.68239 ? 250 LYS   B NZ  1 
ATOM   3611 N  N   . HIS   B 1 239 ? 9.64100   34.17300  28.42000  1.000 13.11843 ? 251 HIS   B N   1 
ATOM   3612 C  CA  . HIS   B 1 239 ? 8.54100   34.55000  29.30400  1.000 13.98379 ? 251 HIS   B CA  1 
ATOM   3613 C  C   . HIS   B 1 239 ? 8.39300   33.53500  30.44300  1.000 14.90682 ? 251 HIS   B C   1 
ATOM   3614 O  O   . HIS   B 1 239 ? 8.24800   33.90900  31.61400  1.000 13.59134 ? 251 HIS   B O   1 
ATOM   3615 C  CB  . HIS   B 1 239 ? 7.24100   34.66400  28.51100  1.000 13.56942 ? 251 HIS   B CB  1 
ATOM   3616 C  CG  . HIS   B 1 239 ? 6.02000   34.61600  29.36700  1.000 12.85216 ? 251 HIS   B CG  1 
ATOM   3617 N  ND1 . HIS   B 1 239 ? 5.60800   35.70200  30.11200  1.000 12.23028 ? 251 HIS   B ND1 1 
ATOM   3618 C  CD2 . HIS   B 1 239 ? 5.14700   33.62300  29.64200  1.000 15.95427 ? 251 HIS   B CD2 1 
ATOM   3619 C  CE1 . HIS   B 1 239 ? 4.53100   35.38500  30.80000  1.000 12.44876 ? 251 HIS   B CE1 1 
ATOM   3620 N  NE2 . HIS   B 1 239 ? 4.23000   34.12100  30.53600  1.000 14.35307 ? 251 HIS   B NE2 1 
ATOM   3621 N  N   . THR   B 1 240 ? 8.44500   32.24000  30.11400  1.000 13.00096 ? 252 THR   B N   1 
ATOM   3622 C  CA  . THR   B 1 240 ? 8.29100   31.22400  31.14600  1.000 11.60021 ? 252 THR   B CA  1 
ATOM   3623 C  C   . THR   B 1 240 ? 9.42700   31.29600  32.15100  1.000 12.78627 ? 252 THR   B C   1 
ATOM   3624 O  O   . THR   B 1 240 ? 9.19700   31.22800  33.36000  1.000 12.88346 ? 252 THR   B O   1 
ATOM   3625 C  CB  . THR   B 1 240 ? 8.19400   29.83100  30.52300  1.000 11.80195 ? 252 THR   B CB  1 
ATOM   3626 O  OG1 . THR   B 1 240 ? 7.08800   29.80100  29.61100  1.000 12.68992 ? 252 THR   B OG1 1 
ATOM   3627 C  CG2 . THR   B 1 240 ? 7.94400   28.79400  31.60900  1.000 14.95798 ? 252 THR   B CG2 1 
ATOM   3628 N  N   A THR   B 1 241 ? 10.65600  31.44700  31.66800  0.688 12.41579 ? 253 THR   B N   1 
ATOM   3629 N  N   B THR   B 1 241 ? 10.66100  31.47200  31.68200  0.312 12.51956 ? 253 THR   B N   1 
ATOM   3630 C  CA  A THR   B 1 241 ? 11.77300  31.59100  32.59200  0.688 13.58744 ? 253 THR   B CA  1 
ATOM   3631 C  CA  B THR   B 1 241 ? 11.77400  31.57500  32.62100  0.312 13.73407 ? 253 THR   B CA  1 
ATOM   3632 C  C   A THR   B 1 241 ? 11.57700  32.79900  33.50500  0.688 15.08978 ? 253 THR   B C   1 
ATOM   3633 C  C   B THR   B 1 241 ? 11.60200  32.76700  33.55600  0.312 15.08231 ? 253 THR   B C   1 
ATOM   3634 O  O   A THR   B 1 241 ? 11.80500  32.71000  34.71600  0.688 14.80165 ? 253 THR   B O   1 
ATOM   3635 O  O   B THR   B 1 241 ? 11.89800  32.67800  34.75300  0.312 14.81221 ? 253 THR   B O   1 
ATOM   3636 C  CB  A THR   B 1 241 ? 13.09100  31.63000  31.81500  0.688 15.32929 ? 253 THR   B CB  1 
ATOM   3637 C  CB  B THR   B 1 241 ? 13.09300  31.66300  31.86100  0.312 15.34872 ? 253 THR   B CB  1 
ATOM   3638 O  OG1 A THR   B 1 241 ? 13.37100  30.30500  31.33200  0.688 15.92001 ? 253 THR   B OG1 1 
ATOM   3639 O  OG1 B THR   B 1 241 ? 13.12700  32.86400  31.09300  0.312 19.91225 ? 253 THR   B OG1 1 
ATOM   3640 C  CG2 A THR   B 1 241 ? 14.24700  32.07600  32.70500  0.688 15.69698 ? 253 THR   B CG2 1 
ATOM   3641 C  CG2 B THR   B 1 241 ? 13.20200  30.51300  30.91600  0.312 15.06015 ? 253 THR   B CG2 1 
ATOM   3642 N  N   A ASN   B 1 242 ? 11.11200  33.92200  32.95000  0.688 14.30050 ? 254 ASN   B N   1 
ATOM   3643 N  N   B ASN   B 1 242 ? 11.11700  33.88800  33.02700  0.312 14.35984 ? 254 ASN   B N   1 
ATOM   3644 C  CA  A ASN   B 1 242 ? 10.85100  35.09900  33.77400  0.688 14.75756 ? 254 ASN   B CA  1 
ATOM   3645 C  CA  B ASN   B 1 242 ? 10.91000  35.06700  33.85800  0.312 14.69204 ? 254 ASN   B CA  1 
ATOM   3646 C  C   A ASN   B 1 242 ? 9.89200   34.76200  34.90500  0.688 14.76615 ? 254 ASN   B C   1 
ATOM   3647 C  C   B ASN   B 1 242 ? 9.84600   34.82500  34.91800  0.312 14.89138 ? 254 ASN   B C   1 
ATOM   3648 O  O   A ASN   B 1 242 ? 10.14600  35.07900  36.07500  0.688 13.26486 ? 254 ASN   B O   1 
ATOM   3649 O  O   B ASN   B 1 242 ? 9.97900   35.28900  36.05700  0.312 14.90135 ? 254 ASN   B O   1 
ATOM   3650 C  CB  A ASN   B 1 242 ? 10.21300  36.20900  32.92800  0.688 16.01707 ? 254 ASN   B CB  1 
ATOM   3651 C  CB  B ASN   B 1 242 ? 10.51800  36.24200  32.97400  0.312 14.01606 ? 254 ASN   B CB  1 
ATOM   3652 C  CG  A ASN   B 1 242 ? 11.19600  36.93500  32.03400  0.688 17.75213 ? 254 ASN   B CG  1 
ATOM   3653 C  CG  B ASN   B 1 242 ? 10.60200  37.56900  33.68900  0.312 18.78308 ? 254 ASN   B CG  1 
ATOM   3654 O  OD1 A ASN   B 1 242 ? 12.41800  36.76700  32.13400  0.688 18.94499 ? 254 ASN   B OD1 1 
ATOM   3655 O  OD1 B ASN   B 1 242 ? 11.45800  37.77400  34.54500  0.312 20.24632 ? 254 ASN   B OD1 1 
ATOM   3656 N  ND2 A ASN   B 1 242 ? 10.64700  37.77000  31.14000  0.688 19.57282 ? 254 ASN   B ND2 1 
ATOM   3657 N  ND2 B ASN   B 1 242 ? 9.69000   38.47400  33.35700  0.312 20.44776 ? 254 ASN   B ND2 1 
ATOM   3658 N  N   . VAL   B 1 243 ? 8.77800   34.11000  34.56100  1.000 14.06027 ? 255 VAL   B N   1 
ATOM   3659 C  CA  . VAL   B 1 243 ? 7.74300   33.79100  35.54200  1.000 13.25668 ? 255 VAL   B CA  1 
ATOM   3660 C  C   . VAL   B 1 243 ? 8.27800   32.83100  36.59000  1.000 14.34058 ? 255 VAL   B C   1 
ATOM   3661 O  O   . VAL   B 1 243 ? 8.04400   33.00600  37.79600  1.000 13.52255 ? 255 VAL   B O   1 
ATOM   3662 C  CB  . VAL   B 1 243 ? 6.50200   33.22700  34.81800  1.000 14.85573 ? 255 VAL   B CB  1 
ATOM   3663 C  CG1 . VAL   B 1 243 ? 5.49700   32.72500  35.83500  1.000 16.54501 ? 255 VAL   B CG1 1 
ATOM   3664 C  CG2 . VAL   B 1 243 ? 5.86500   34.30300  33.91700  1.000 14.37532 ? 255 VAL   B CG2 1 
ATOM   3665 N  N   . VAL   B 1 244 ? 9.00300   31.80200  36.14300  1.000 13.42839 ? 256 VAL   B N   1 
ATOM   3666 C  CA  . VAL   B 1 244 ? 9.57000   30.81500  37.05800  1.000 13.09890 ? 256 VAL   B CA  1 
ATOM   3667 C  C   . VAL   B 1 244 ? 10.54800  31.47300  38.02300  1.000 13.01064 ? 256 VAL   B C   1 
ATOM   3668 O  O   . VAL   B 1 244 ? 10.51600  31.22200  39.23400  1.000 15.03738 ? 256 VAL   B O   1 
ATOM   3669 C  CB  . VAL   B 1 244 ? 10.20700  29.66200  36.26500  1.000 14.49497 ? 256 VAL   B CB  1 
ATOM   3670 C  CG1 . VAL   B 1 244 ? 11.02700  28.77500  37.19100  1.000 16.56251 ? 256 VAL   B CG1 1 
ATOM   3671 C  CG2 . VAL   B 1 244 ? 9.11100   28.87100  35.58600  1.000 15.95244 ? 256 VAL   B CG2 1 
ATOM   3672 N  N   . LYS   B 1 245 ? 11.42200  32.33200  37.50300  1.000 15.24865 ? 257 LYS   B N   1 
ATOM   3673 C  CA  . LYS   B 1 245 ? 12.40600  32.97500  38.36600  1.000 15.12652 ? 257 LYS   B CA  1 
ATOM   3674 C  C   . LYS   B 1 245 ? 11.73300  33.91900  39.35200  1.000 14.81794 ? 257 LYS   B C   1 
ATOM   3675 O  O   . LYS   B 1 245 ? 12.13500  33.98200  40.51900  1.000 17.03147 ? 257 LYS   B O   1 
ATOM   3676 C  CB  . LYS   B 1 245 ? 13.45700  33.69200  37.51700  1.000 17.11069 ? 257 LYS   B CB  1 
ATOM   3677 C  CG  . LYS   B 1 245 ? 14.48400  32.73800  36.90100  1.000 16.46998 ? 257 LYS   B CG  1 
ATOM   3678 C  CD  . LYS   B 1 245 ? 15.53700  33.52000  36.10800  1.000 22.13943 ? 257 LYS   B CD  1 
ATOM   3679 C  CE  . LYS   B 1 245 ? 16.62200  32.58900  35.55800  1.000 27.57930 ? 257 LYS   B CE  1 
ATOM   3680 N  NZ  . LYS   B 1 245 ? 17.79300  33.37200  35.04300  1.000 25.75250 ? 257 LYS   B NZ  1 
ATOM   3681 N  N   . ALA   B 1 246 ? 10.68300  34.62300  38.92000  1.000 14.07235 ? 258 ALA   B N   1 
ATOM   3682 C  CA  . ALA   B 1 246 ? 9.95200   35.49500  39.83900  1.000 16.26646 ? 258 ALA   B CA  1 
ATOM   3683 C  C   . ALA   B 1 246 ? 9.33700   34.68700  40.97500  1.000 20.40094 ? 258 ALA   B C   1 
ATOM   3684 O  O   . ALA   B 1 246 ? 9.39000   35.10300  42.14100  1.000 19.85698 ? 258 ALA   B O   1 
ATOM   3685 C  CB  . ALA   B 1 246 ? 8.87300   36.27100  39.09100  1.000 18.81337 ? 258 ALA   B CB  1 
ATOM   3686 N  N   . HIS   B 1 247 ? 8.79500   33.50200  40.66200  1.000 16.07270 ? 259 HIS   B N   1 
ATOM   3687 C  CA  . HIS   B 1 247 ? 8.23000   32.64400  41.69500  1.000 17.51893 ? 259 HIS   B CA  1 
ATOM   3688 C  C   . HIS   B 1 247 ? 9.31900   32.09500  42.60300  1.000 19.04272 ? 259 HIS   B C   1 
ATOM   3689 O  O   . HIS   B 1 247 ? 9.14800   32.03600  43.83100  1.000 19.59063 ? 259 HIS   B O   1 
ATOM   3690 C  CB  . HIS   B 1 247 ? 7.43600   31.50200  41.06200  1.000 18.39656 ? 259 HIS   B CB  1 
ATOM   3691 C  CG  . HIS   B 1 247 ? 6.77400   30.61100  42.06700  1.000 18.31566 ? 259 HIS   B CG  1 
ATOM   3692 N  ND1 . HIS   B 1 247 ? 5.55100   30.90700  42.62800  1.000 27.11588 ? 259 HIS   B ND1 1 
ATOM   3693 C  CD2 . HIS   B 1 247 ? 7.16500   29.43500  42.60800  1.000 23.63759 ? 259 HIS   B CD2 1 
ATOM   3694 C  CE1 . HIS   B 1 247 ? 5.21900   29.95200  43.47800  1.000 25.63055 ? 259 HIS   B CE1 1 
ATOM   3695 N  NE2 . HIS   B 1 247 ? 6.18100   29.04800  43.48600  1.000 25.76997 ? 259 HIS   B NE2 1 
ATOM   3696 N  N   . THR   B 1 248 ? 10.45100  31.70100  42.01800  1.000 18.25584 ? 260 THR   B N   1 
ATOM   3697 C  CA  . THR   B 1 248 ? 11.59900  31.27500  42.81400  1.000 20.10940 ? 260 THR   B CA  1 
ATOM   3698 C  C   . THR   B 1 248 ? 11.97900  32.33900  43.83000  1.000 20.90156 ? 260 THR   B C   1 
ATOM   3699 O  O   . THR   B 1 248 ? 12.37200  32.01800  44.95800  1.000 25.69576 ? 260 THR   B O   1 
ATOM   3700 C  CB  . THR   B 1 248 ? 12.77600  30.99200  41.88000  1.000 18.94342 ? 260 THR   B CB  1 
ATOM   3701 O  OG1 . THR   B 1 248 ? 12.46400  29.85100  41.07000  1.000 18.38945 ? 260 THR   B OG1 1 
ATOM   3702 C  CG2 . THR   B 1 248 ? 14.04800  30.68500  42.67900  1.000 18.97297 ? 260 THR   B CG2 1 
ATOM   3703 N  N   . ASN   B 1 249 ? 11.84400  33.60700  43.45800  1.000 17.63923 ? 261 ASN   B N   1 
ATOM   3704 C  CA  . ASN   B 1 249 ? 12.25300  34.71300  44.31000  1.000 18.19307 ? 261 ASN   B CA  1 
ATOM   3705 C  C   . ASN   B 1 249 ? 11.12400  35.25100  45.18700  1.000 25.30409 ? 261 ASN   B C   1 
ATOM   3706 O  O   . ASN   B 1 249 ? 11.26700  36.34200  45.74400  1.000 32.46066 ? 261 ASN   B O   1 
ATOM   3707 C  CB  . ASN   B 1 249 ? 12.88300  35.82900  43.47400  1.000 21.52776 ? 261 ASN   B CB  1 
ATOM   3708 C  CG  . ASN   B 1 249 ? 14.24400  35.45000  42.92000  1.000 19.46629 ? 261 ASN   B CG  1 
ATOM   3709 O  OD1 . ASN   B 1 249 ? 14.88000  34.50200  43.38500  1.000 22.03038 ? 261 ASN   B OD1 1 
ATOM   3710 N  ND2 . ASN   B 1 249 ? 14.69200  36.18200  41.90800  1.000 20.16389 ? 261 ASN   B ND2 1 
ATOM   3711 N  N   . ARG   B 1 250 ? 10.03200  34.50400  45.34700  1.000 25.71327 ? 262 ARG   B N   1 
ATOM   3712 C  CA  . ARG   B 1 250 ? 8.91100   34.95000  46.18500  1.000 27.93822 ? 262 ARG   B CA  1 
ATOM   3713 C  C   . ARG   B 1 250 ? 9.36900   35.24700  47.61200  1.000 34.10433 ? 262 ARG   B C   1 
ATOM   3714 O  O   . ARG   B 1 250 ? 10.36300  34.68700  48.07800  1.000 32.16378 ? 262 ARG   B O   1 
ATOM   3715 C  CB  . ARG   B 1 250 ? 7.78100   33.91200  46.20100  1.000 27.04485 ? 262 ARG   B CB  1 
ATOM   3716 C  CG  . ARG   B 1 250 ? 8.14300   32.54500  46.79100  1.000 27.18929 ? 262 ARG   B CG  1 
ATOM   3717 C  CD  . ARG   B 1 250 ? 7.12400   31.47300  46.35900  1.000 24.29586 ? 262 ARG   B CD  1 
ATOM   3718 N  NE  . ARG   B 1 250 ? 7.32500   30.20400  47.04900  1.000 30.48964 ? 262 ARG   B NE  1 
ATOM   3719 C  CZ  . ARG   B 1 250 ? 8.24200   29.30900  46.70800  1.000 39.81193 ? 262 ARG   B CZ  1 
ATOM   3720 N  NH1 . ARG   B 1 250 ? 9.04600   29.50600  45.67300  1.000 25.68372 ? 262 ARG   B NH1 1 
ATOM   3721 N  NH2 . ARG   B 1 250 ? 8.36100   28.19400  47.42700  1.000 33.76642 ? 262 ARG   B NH2 1 
HETATM 3722 C  C   . FMT   C 2 .   ? 32.78400  20.19200  -0.06300  0.998 10.45515 ? 301 FMT   A C   1 
HETATM 3723 O  O1  . FMT   C 2 .   ? 32.61900  20.19200  1.08700   0.998 17.25426 ? 301 FMT   A O1  1 
HETATM 3724 O  O2  . FMT   C 2 .   ? 31.89700  20.02200  -0.89700  0.998 41.95689 ? 301 FMT   A O2  1 
HETATM 3725 C  C   . FMT   D 2 .   ? 29.93500  19.74700  3.01800   1.000 5.26413  ? 302 FMT   A C   1 
HETATM 3726 O  O1  . FMT   D 2 .   ? 31.09300  20.06100  3.00300   1.000 26.85989 ? 302 FMT   A O1  1 
HETATM 3727 O  O2  . FMT   D 2 .   ? 29.06800  20.02400  2.21300   1.000 35.40925 ? 302 FMT   A O2  1 
HETATM 3728 C  C02 A A1IKA E 3 .   ? 16.42600  -4.24300  7.82200   0.375 18.77138 ? 303 A1IKA A C02 1 
HETATM 3729 C  C02 B A1IKA E 3 .   ? 17.48100  -3.88700  8.51600   0.436 22.51618 ? 303 A1IKA A C02 1 
HETATM 3730 C  C04 A A1IKA E 3 .   ? 16.92900  -1.72700  7.44200   0.375 17.03950 ? 303 A1IKA A C04 1 
HETATM 3731 C  C04 B A1IKA E 3 .   ? 16.61700  -1.82000  7.46000   0.436 16.75246 ? 303 A1IKA A C04 1 
HETATM 3732 C  C05 A A1IKA E 3 .   ? 15.87100  -0.93200  8.22400   0.375 18.86308 ? 303 A1IKA A C05 1 
HETATM 3733 C  C05 B A1IKA E 3 .   ? 15.58800  -0.86600  8.07100   0.436 17.94346 ? 303 A1IKA A C05 1 
HETATM 3734 C  C06 A A1IKA E 3 .   ? 14.93200  -1.56400  9.01900   0.375 19.90949 ? 303 A1IKA A C06 1 
HETATM 3735 C  C06 B A1IKA E 3 .   ? 14.51800  -1.37000  8.78600   0.436 21.72713 ? 303 A1IKA A C06 1 
HETATM 3736 C  C07 A A1IKA E 3 .   ? 14.00600  -0.80500  9.71800   0.375 22.07974 ? 303 A1IKA A C07 1 
HETATM 3737 C  C07 B A1IKA E 3 .   ? 13.60400  -0.49500  9.35100   0.436 23.94139 ? 303 A1IKA A C07 1 
HETATM 3738 C  C08 A A1IKA E 3 .   ? 14.01600  0.57800   9.62700   0.375 22.65195 ? 303 A1IKA A C08 1 
HETATM 3739 C  C08 B A1IKA E 3 .   ? 13.75800  0.87700   9.21100   0.436 22.62347 ? 303 A1IKA A C08 1 
HETATM 3740 C  C09 A A1IKA E 3 .   ? 14.95800  1.21100   8.84000   0.375 20.49559 ? 303 A1IKA A C09 1 
HETATM 3741 C  C09 B A1IKA E 3 .   ? 14.83400  1.37900   8.50200   0.436 21.44769 ? 303 A1IKA A C09 1 
HETATM 3742 C  C10 A A1IKA E 3 .   ? 15.88700  0.45600   8.14300   0.375 18.75876 ? 303 A1IKA A C10 1 
HETATM 3743 C  C10 B A1IKA E 3 .   ? 15.75400  0.50900   7.93900   0.436 19.31745 ? 303 A1IKA A C10 1 
HETATM 3744 C  C16 A A1IKA E 3 .   ? 16.99300  -5.56300  8.33500   0.375 21.68299 ? 303 A1IKA A C16 1 
HETATM 3745 C  C16 B A1IKA E 3 .   ? 17.48500  -5.38900  8.76200   0.436 20.98363 ? 303 A1IKA A C16 1 
HETATM 3746 C  C17 A A1IKA E 3 .   ? 16.40600  -6.80400  8.18700   0.375 28.46368 ? 303 A1IKA A C17 1 
HETATM 3747 C  C17 B A1IKA E 3 .   ? 18.63900  -6.10500  9.01800   0.436 25.38332 ? 303 A1IKA A C17 1 
HETATM 3748 C  C18 A A1IKA E 3 .   ? 17.13400  -7.87500  8.71100   0.375 27.34504 ? 303 A1IKA A C18 1 
HETATM 3749 C  C18 B A1IKA E 3 .   ? 18.48400  -7.47800  9.18100   0.436 27.08467 ? 303 A1IKA A C18 1 
HETATM 3750 C  C19 A A1IKA E 3 .   ? 16.70000  -9.20800  8.68300   0.375 28.61496 ? 303 A1IKA A C19 1 
HETATM 3751 C  C19 B A1IKA E 3 .   ? 19.54300  -8.35800  9.46300   0.436 26.97705 ? 303 A1IKA A C19 1 
HETATM 3752 C  C20 A A1IKA E 3 .   ? 17.49600  -10.19900 9.22600   0.375 30.81836 ? 303 A1IKA A C20 1 
HETATM 3753 C  C20 B A1IKA E 3 .   ? 19.28700  -9.70700  9.61400   0.436 27.77233 ? 303 A1IKA A C20 1 
HETATM 3754 C  C21 A A1IKA E 3 .   ? 18.71800  -9.87700  9.79800   0.375 28.48888 ? 303 A1IKA A C21 1 
HETATM 3755 C  C21 B A1IKA E 3 .   ? 17.98700  -10.17800 9.48600   0.436 29.79825 ? 303 A1IKA A C21 1 
HETATM 3756 C  C22 A A1IKA E 3 .   ? 19.14900  -8.55500  9.82600   0.375 28.79953 ? 303 A1IKA A C22 1 
HETATM 3757 C  C22 B A1IKA E 3 .   ? 16.94000  -9.30300  9.20400   0.436 28.65062 ? 303 A1IKA A C22 1 
HETATM 3758 C  C23 A A1IKA E 3 .   ? 18.35000  -7.55200  9.27800   0.375 27.10074 ? 303 A1IKA A C23 1 
HETATM 3759 C  C23 B A1IKA E 3 .   ? 17.19100  -7.94200  9.05100   0.436 27.97731 ? 303 A1IKA A C23 1 
HETATM 3760 N  N03 A A1IKA E 3 .   ? 17.25600  -3.06000  7.93800   0.375 19.41521 ? 303 A1IKA A N03 1 
HETATM 3761 N  N03 B A1IKA E 3 .   ? 16.46000  -3.23800  7.73300   0.436 17.98461 ? 303 A1IKA A N03 1 
HETATM 3762 O  O01 A A1IKA E 3 .   ? 15.34500  -4.21200  7.33800   0.375 20.97462 ? 303 A1IKA A O01 1 
HETATM 3763 O  O01 B A1IKA E 3 .   ? 18.36900  -3.23600  8.93700   0.436 19.93037 ? 303 A1IKA A O01 1 
HETATM 3764 O  O11 A A1IKA E 3 .   ? 16.83400  1.12300   7.34700   0.375 18.82036 ? 303 A1IKA A O11 1 
HETATM 3765 O  O11 B A1IKA E 3 .   ? 16.84000  1.04200   7.22300   0.436 18.92296 ? 303 A1IKA A O11 1 
HETATM 3766 O  O13 A A1IKA E 3 .   ? 15.18500  -2.22100  5.26500   0.375 14.95090 ? 303 A1IKA A O13 1 
HETATM 3767 O  O13 B A1IKA E 3 .   ? 15.43200  -2.53800  5.07000   0.436 14.29639 ? 303 A1IKA A O13 1 
HETATM 3768 O  O14 A A1IKA E 3 .   ? 17.53100  -3.00100  5.10900   0.375 14.99121 ? 303 A1IKA A O14 1 
HETATM 3769 O  O14 B A1IKA E 3 .   ? 17.91800  -2.65700  5.26000   0.436 11.51037 ? 303 A1IKA A O14 1 
HETATM 3770 O  O15 A A1IKA E 3 .   ? 17.02500  -0.55800  5.01900   0.375 13.23966 ? 303 A1IKA A O15 1 
HETATM 3771 O  O15 B A1IKA E 3 .   ? 16.80800  -0.42600  5.06100   0.436 12.19615 ? 303 A1IKA A O15 1 
HETATM 3772 P  P12 A A1IKA E 3 .   ? 16.62300  -1.90700  5.60600   0.375 13.34079 ? 303 A1IKA A P12 1 
HETATM 3773 P  P12 B A1IKA E 3 .   ? 16.67500  -1.85700  5.59600   0.436 13.72965 ? 303 A1IKA A P12 1 
HETATM 3774 S  S24 A A1IKA E 3 .   ? 18.51600  -5.83300  9.12400   0.375 27.04171 ? 303 A1IKA A S24 1 
HETATM 3775 S  S24 B A1IKA E 3 .   ? 16.20300  -6.55400  8.70400   0.436 34.53809 ? 303 A1IKA A S24 1 
HETATM 3776 ZN ZN  . ZN    F 4 .   ? 16.75600  -0.01100  3.22000   0.963 13.54701 ? 304 ZN    A ZN  1 
HETATM 3777 ZN ZN  . ZN    G 4 .   ? 30.52700  20.46300  0.94700   0.919 14.48503 ? 305 ZN    A ZN  1 
HETATM 3778 ZN ZN  . ZN    H 4 .   ? 19.65200  -2.32100  5.37400   0.858 12.71841 ? 306 ZN    A ZN  1 
HETATM 3779 C  C   . FMT   I 2 .   ? 5.90700   38.06700  32.46700  1.000 5.14371  ? 301 FMT   B C   1 
HETATM 3780 O  O1  . FMT   I 2 .   ? 7.00100   38.10000  31.98900  1.000 22.72709 ? 301 FMT   B O1  1 
HETATM 3781 O  O2  . FMT   I 2 .   ? 4.82500   38.21900  31.94500  1.000 30.06091 ? 301 FMT   B O2  1 
HETATM 3782 C  C   . FMT   J 2 .   ? 8.68200   38.06100  29.98700  1.000 9.88652  ? 302 FMT   B C   1 
HETATM 3783 O  O1  . FMT   J 2 .   ? 7.55000   38.14200  29.52600  1.000 21.51993 ? 302 FMT   B O1  1 
HETATM 3784 O  O2  . FMT   J 2 .   ? 9.04800   38.08000  31.15700  1.000 36.17131 ? 302 FMT   B O2  1 
HETATM 3785 C  C02 A A1IKA K 3 .   ? -2.92800  28.16600  37.99400  0.459 28.96302 ? 303 A1IKA B C02 1 
HETATM 3786 C  C02 B A1IKA K 3 .   ? -2.94300  28.01000  38.01900  0.341 28.93377 ? 303 A1IKA B C02 1 
HETATM 3787 C  C04 A A1IKA K 3 .   ? -3.26600  28.23200  40.48500  0.459 27.31100 ? 303 A1IKA B C04 1 
HETATM 3788 C  C04 B A1IKA K 3 .   ? -3.25500  28.52600  40.42700  0.341 27.95923 ? 303 A1IKA B C04 1 
HETATM 3789 C  C05 A A1IKA K 3 .   ? -4.00900  26.94800  40.85400  0.459 28.93072 ? 303 A1IKA B C05 1 
HETATM 3790 C  C05 B A1IKA K 3 .   ? -3.97900  27.26100  40.89600  0.341 28.66443 ? 303 A1IKA B C05 1 
HETATM 3791 C  C06 A A1IKA K 3 .   ? -4.97900  26.42700  40.01400  0.459 28.56616 ? 303 A1IKA B C06 1 
HETATM 3792 C  C06 B A1IKA K 3 .   ? -5.03500  26.73100  40.17300  0.341 28.60922 ? 303 A1IKA B C06 1 
HETATM 3793 C  C07 A A1IKA K 3 .   ? -5.63800  25.25900  40.35900  0.459 29.17902 ? 303 A1IKA B C07 1 
HETATM 3794 C  C07 B A1IKA K 3 .   ? -5.66800  25.58100  40.61400  0.341 29.25709 ? 303 A1IKA B C07 1 
HETATM 3795 C  C08 A A1IKA K 3 .   ? -5.33200  24.61200  41.54600  0.459 31.90889 ? 303 A1IKA B C08 1 
HETATM 3796 C  C08 B A1IKA K 3 .   ? -5.25000  24.95800  41.77900  0.341 31.30428 ? 303 A1IKA B C08 1 
HETATM 3797 C  C09 A A1IKA K 3 .   ? -4.36300  25.13100  42.38700  0.459 31.43998 ? 303 A1IKA B C09 1 
HETATM 3798 C  C09 B A1IKA K 3 .   ? -4.19200  25.48300  42.50100  0.341 31.08067 ? 303 A1IKA B C09 1 
HETATM 3799 C  C10 A A1IKA K 3 .   ? -3.70300  26.29800  42.03900  0.459 29.05716 ? 303 A1IKA B C10 1 
HETATM 3800 C  C10 B A1IKA K 3 .   ? -3.55900  26.63200  42.05600  0.341 29.67611 ? 303 A1IKA B C10 1 
HETATM 3801 C  C16 A A1IKA K 3 .   ? -3.36700  28.63100  36.61600  0.459 25.77669 ? 303 A1IKA B C16 1 
HETATM 3802 C  C16 B A1IKA K 3 .   ? -3.25500  28.27900  36.55800  0.341 26.88291 ? 303 A1IKA B C16 1 
HETATM 3803 C  C17 A A1IKA K 3 .   ? -3.45100  27.80800  35.51300  0.459 26.65938 ? 303 A1IKA B C17 1 
HETATM 3804 C  C17 B A1IKA K 3 .   ? -3.85000  29.38800  35.99000  0.341 28.31762 ? 303 A1IKA B C17 1 
HETATM 3805 C  C18 A A1IKA K 3 .   ? -3.89400  28.42400  34.34600  0.459 27.24985 ? 303 A1IKA B C18 1 
HETATM 3806 C  C18 B A1IKA K 3 .   ? -4.00800  29.33200  34.59500  0.341 26.24986 ? 303 A1IKA B C18 1 
HETATM 3807 C  C19 A A1IKA K 3 .   ? -4.04200  27.76100  33.11700  0.459 25.82226 ? 303 A1IKA B C19 1 
HETATM 3808 C  C19 B A1IKA K 3 .   ? -4.57800  30.34400  33.81100  0.341 28.81917 ? 303 A1IKA B C19 1 
HETATM 3809 C  C20 A A1IKA K 3 .   ? -4.48700  28.45800  32.01200  0.459 24.79402 ? 303 A1IKA B C20 1 
HETATM 3810 C  C20 B A1IKA K 3 .   ? -4.68400  30.17600  32.44100  0.341 28.12545 ? 303 A1IKA B C20 1 
HETATM 3811 C  C21 A A1IKA K 3 .   ? -4.78100  29.80800  32.12500  0.459 28.84115 ? 303 A1IKA B C21 1 
HETATM 3812 C  C21 B A1IKA K 3 .   ? -4.23300  29.01300  31.83300  0.341 25.70434 ? 303 A1IKA B C21 1 
HETATM 3813 C  C22 A A1IKA K 3 .   ? -4.63600  30.45800  33.34700  0.459 29.31455 ? 303 A1IKA B C22 1 
HETATM 3814 C  C22 B A1IKA K 3 .   ? -3.67000  28.01200  32.61300  0.341 24.57110 ? 303 A1IKA B C22 1 
HETATM 3815 C  C23 A A1IKA K 3 .   ? -4.18600  29.76900  34.46800  0.459 26.46230 ? 303 A1IKA B C23 1 
HETATM 3816 C  C23 B A1IKA K 3 .   ? -3.56100  28.17900  33.98900  0.341 26.84871 ? 303 A1IKA B C23 1 
HETATM 3817 N  N03 A A1IKA K 3 .   ? -3.63900  28.66600  39.15200  0.459 28.17847 ? 303 A1IKA B N03 1 
HETATM 3818 N  N03 B A1IKA K 3 .   ? -3.56900  28.81200  39.04200  0.341 27.90626 ? 303 A1IKA B N03 1 
HETATM 3819 O  O01 A A1IKA K 3 .   ? -2.05300  27.37400  38.10700  0.459 24.58468 ? 303 A1IKA B O01 1 
HETATM 3820 O  O01 B A1IKA K 3 .   ? -2.21100  27.12700  38.32000  0.341 24.29974 ? 303 A1IKA B O01 1 
HETATM 3821 O  O11 A A1IKA K 3 .   ? -2.71900  26.82900  42.88100  0.459 31.45035 ? 303 A1IKA B O11 1 
HETATM 3822 O  O11 B A1IKA K 3 .   ? -2.48900  27.17400  42.77700  0.341 30.48526 ? 303 A1IKA B O11 1 
HETATM 3823 O  O13 A A1IKA K 3 .   ? -5.15000  29.85100  41.73100  0.459 31.15313 ? 303 A1IKA B O13 1 
HETATM 3824 O  O13 B A1IKA K 3 .   ? -5.19200  30.29400  41.32200  0.341 28.11565 ? 303 A1IKA B O13 1 
HETATM 3825 O  O14 A A1IKA K 3 .   ? -3.00100  30.88000  41.10200  0.459 28.46497 ? 303 A1IKA B O14 1 
HETATM 3826 O  O14 B A1IKA K 3 .   ? -2.96900  31.23400  40.82100  0.341 27.88023 ? 303 A1IKA B O14 1 
HETATM 3827 O  O15 A A1IKA K 3 .   ? -3.10000  29.31300  43.01200  0.459 31.29013 ? 303 A1IKA B O15 1 
HETATM 3828 O  O15 B A1IKA K 3 .   ? -3.29200  29.84500  42.83900  0.341 31.96030 ? 303 A1IKA B O15 1 
HETATM 3829 P  P12 A A1IKA K 3 .   ? -3.65500  29.63100  41.64700  0.459 28.03793 ? 303 A1IKA B P12 1 
HETATM 3830 P  P12 B A1IKA K 3 .   ? -3.70100  30.04600  41.40000  0.341 29.20969 ? 303 A1IKA B P12 1 
HETATM 3831 S  S24 A A1IKA K 3 .   ? -3.88100  30.21500  36.12600  0.459 21.08245 ? 303 A1IKA B S24 1 
HETATM 3832 S  S24 B A1IKA K 3 .   ? -2.93600  27.19400  35.26500  0.341 29.85288 ? 303 A1IKA B S24 1 
HETATM 3833 C  C17 . A1H8T L 5 .   ? -3.58000  18.09600  39.04900  0.817 29.43645 ? 304 A1H8T B C17 1 
HETATM 3834 C  C20 . A1H8T L 5 .   ? -4.40400  16.56800  42.35400  0.817 45.59748 ? 304 A1H8T B C20 1 
HETATM 3835 C  C21 . A1H8T L 5 .   ? -5.60500  15.95300  42.02500  0.817 45.03296 ? 304 A1H8T B C21 1 
HETATM 3836 C  C22 . A1H8T L 5 .   ? -6.10900  16.06000  40.73300  0.817 41.66573 ? 304 A1H8T B C22 1 
HETATM 3837 C  C16 . A1H8T L 5 .   ? -4.25000  18.06900  37.83600  0.817 28.50634 ? 304 A1H8T B C16 1 
HETATM 3838 C  C19 . A1H8T L 5 .   ? -3.70400  17.28600  41.40000  0.817 38.86744 ? 304 A1H8T B C19 1 
HETATM 3839 C  C23 . A1H8T L 5 .   ? -5.40500  16.78300  39.76900  0.817 41.36708 ? 304 A1H8T B C23 1 
HETATM 3840 C  C02 . A1H8T L 5 .   ? -3.83600  18.74200  36.53100  0.817 24.87631 ? 304 A1H8T B C02 1 
HETATM 3841 C  C04 . A1H8T L 5 .   ? -2.99300  20.90100  35.50300  0.817 17.00815 ? 304 A1H8T B C04 1 
HETATM 3842 C  C05 . A1H8T L 5 .   ? -3.61800  22.27600  35.69600  0.817 18.86369 ? 304 A1H8T B C05 1 
HETATM 3843 C  C06 . A1H8T L 5 .   ? -4.38700  22.79000  34.67600  0.817 23.91225 ? 304 A1H8T B C06 1 
HETATM 3844 C  C07 . A1H8T L 5 .   ? -4.99600  24.02600  34.81800  0.817 27.41675 ? 304 A1H8T B C07 1 
HETATM 3845 C  C08 . A1H8T L 5 .   ? -4.83700  24.72700  36.00100  0.817 27.35069 ? 304 A1H8T B C08 1 
HETATM 3846 C  C09 . A1H8T L 5 .   ? -4.06600  24.21100  37.02900  0.817 23.83958 ? 304 A1H8T B C09 1 
HETATM 3847 C  C10 . A1H8T L 5 .   ? -3.45900  22.97200  36.88300  0.817 22.35796 ? 304 A1H8T B C10 1 
HETATM 3848 C  C18 . A1H8T L 5 .   ? -4.20800  17.39200  40.09300  0.817 40.53857 ? 304 A1H8T B C18 1 
HETATM 3849 N  N03 . A1H8T L 5 .   ? -3.39500  20.10500  36.64400  0.817 22.80987 ? 304 A1H8T B N03 1 
HETATM 3850 O  O01 . A1H8T L 5 .   ? -3.87900  18.18000  35.48100  0.817 23.62801 ? 304 A1H8T B O01 1 
HETATM 3851 O  O11 . A1H8T L 5 .   ? -2.68000  22.45600  37.93100  0.817 22.18817 ? 304 A1H8T B O11 1 
HETATM 3852 O  O13 . A1H8T L 5 .   ? -0.73500  19.53000  35.06800  0.817 14.04443 ? 304 A1H8T B O13 1 
HETATM 3853 O  O14 . A1H8T L 5 .   ? -0.54100  21.49500  36.63600  0.817 15.28101 ? 304 A1H8T B O14 1 
HETATM 3854 O  O15 . A1H8T L 5 .   ? -0.79600  21.76700  34.15600  0.817 15.03805 ? 304 A1H8T B O15 1 
HETATM 3855 P  P12 . A1H8T L 5 .   ? -1.15100  20.95100  35.35600  0.817 15.27854 ? 304 A1H8T B P12 1 
HETATM 3856 S  S24 . A1H8T L 5 .   ? -5.68300  17.13800  38.09100  0.817 40.11373 ? 304 A1H8T B S24 1 
HETATM 3857 ZN ZN  . ZN    M 4 .   ? 1.11900   18.93300  35.05600  1.000 14.69522 ? 305 ZN    B ZN  1 
HETATM 3858 ZN ZN  . ZN    N 4 .   ? 6.37000   37.64300  30.20000  0.875 14.64992 ? 306 ZN    B ZN  1 
HETATM 3859 ZN ZN  . ZN    O 4 .   ? -1.10800  21.35100  32.31500  0.910 13.98863 ? 307 ZN    B ZN  1 
HETATM 3860 O  O   . HOH   P 6 .   ? 31.22100  -16.85600 -4.40500  1.000 34.14188 ? 401 HOH   A O   1 
HETATM 3861 O  O   . HOH   P 6 .   ? 31.79100  18.19600  -2.83700  1.000 38.11950 ? 402 HOH   A O   1 
HETATM 3862 O  O   . HOH   P 6 .   ? 30.235    -21.105   -3.445    1.000 26.76742 ? 403 HOH   A O   1 
HETATM 3863 O  O   . HOH   P 6 .   ? 18.59400  -12.71800 -13.30100 1.000 39.50687 ? 404 HOH   A O   1 
HETATM 3864 O  O   . HOH   P 6 .   ? 16.95000  -17.65600 -8.79000  1.000 28.76698 ? 405 HOH   A O   1 
HETATM 3865 O  O   . HOH   P 6 .   ? 22.32500  10.77100  -14.27600 1.000 36.52977 ? 406 HOH   A O   1 
HETATM 3866 O  O   . HOH   P 6 .   ? 15.10000  6.35100   -7.17300  1.000 26.82546 ? 407 HOH   A O   1 
HETATM 3867 O  O   . HOH   P 6 .   ? 24.72000  -8.15600  20.02500  1.000 50.59686 ? 408 HOH   A O   1 
HETATM 3868 O  O   . HOH   P 6 .   ? 33.50600  17.33100  -0.34200  1.000 25.82798 ? 409 HOH   A O   1 
HETATM 3869 O  O   . HOH   P 6 .   ? 29.216    -19.528   -1.034    1.000 26.11686 ? 410 HOH   A O   1 
HETATM 3870 O  O   . HOH   P 6 .   ? 30.01300  21.11900  14.35900  1.000 35.96385 ? 411 HOH   A O   1 
HETATM 3871 O  O   . HOH   P 6 .   ? 38.82700  10.51400  -0.80400  1.000 32.85006 ? 412 HOH   A O   1 
HETATM 3872 O  O   . HOH   P 6 .   ? 15.43500  -19.78400 -7.63700  1.000 26.51391 ? 413 HOH   A O   1 
HETATM 3873 O  O   . HOH   P 6 .   ? 30.30400  -16.79100 0.19100   1.000 26.66462 ? 414 HOH   A O   1 
HETATM 3874 O  O   . HOH   P 6 .   ? 37.12200  -2.78700  16.08400  1.000 32.72238 ? 415 HOH   A O   1 
HETATM 3875 O  O   . HOH   P 6 .   ? 39.36200  9.64800   12.38300  1.000 23.15454 ? 416 HOH   A O   1 
HETATM 3876 O  O   . HOH   P 6 .   ? 16.48000  -0.68700  -14.35000 1.000 36.88028 ? 417 HOH   A O   1 
HETATM 3877 O  O   . HOH   P 6 .   ? 7.28200   2.56000   2.49000   1.000 38.78476 ? 418 HOH   A O   1 
HETATM 3878 O  O   . HOH   P 6 .   ? 44.10700  8.02100   17.05200  1.000 24.05968 ? 419 HOH   A O   1 
HETATM 3879 O  O   . HOH   P 6 .   ? 44.37700  11.72000  14.09300  1.000 40.84456 ? 420 HOH   A O   1 
HETATM 3880 O  O   . HOH   P 6 .   ? 14.53000  12.69800  10.96200  1.000 32.19874 ? 421 HOH   A O   1 
HETATM 3881 O  O   . HOH   P 6 .   ? 17.37800  -5.47600  4.58600   1.000 19.98621 ? 422 HOH   A O   1 
HETATM 3882 O  O   . HOH   P 6 .   ? 43.401    10.703    17.868    1.000 25.23529 ? 423 HOH   A O   1 
HETATM 3883 O  O   . HOH   P 6 .   ? 32.47800  1.32100   19.80200  1.000 28.75582 ? 424 HOH   A O   1 
HETATM 3884 O  O   . HOH   P 6 .   ? 7.51400   4.60000   5.02300   1.000 38.12811 ? 425 HOH   A O   1 
HETATM 3885 O  O   . HOH   P 6 .   ? 22.65300  12.08300  13.00800  1.000 22.10461 ? 426 HOH   A O   1 
HETATM 3886 O  O   . HOH   P 6 .   ? 24.62900  0.70500   9.22400   1.000 22.10798 ? 427 HOH   A O   1 
HETATM 3887 O  O   . HOH   P 6 .   ? 12.75900  6.38400   8.84800   1.000 24.98201 ? 428 HOH   A O   1 
HETATM 3888 O  O   . HOH   P 6 .   ? 26.13400  -15.24900 -7.73600  1.000 20.76967 ? 429 HOH   A O   1 
HETATM 3889 O  O   . HOH   P 6 .   ? 20.891    -19.989   -7.615    1.000 23.30286 ? 430 HOH   A O   1 
HETATM 3890 O  O   . HOH   P 6 .   ? 7.54200   11.29100  6.02600   1.000 40.26284 ? 431 HOH   A O   1 
HETATM 3891 O  O   . HOH   P 6 .   ? 20.33500  6.60400   -6.53200  1.000 16.02126 ? 432 HOH   A O   1 
HETATM 3892 O  O   . HOH   P 6 .   ? 7.88300   -5.87600  3.30700   1.000 35.11510 ? 433 HOH   A O   1 
HETATM 3893 O  O   . HOH   P 6 .   ? 14.28900  -8.62900  -12.79300 1.000 18.12882 ? 434 HOH   A O   1 
HETATM 3894 O  O   . HOH   P 6 .   ? 8.03300   -4.39800  -5.02800  1.000 31.55697 ? 435 HOH   A O   1 
HETATM 3895 O  O   . HOH   P 6 .   ? 2.87500   -13.64200 -4.51500  1.000 36.29803 ? 436 HOH   A O   1 
HETATM 3896 O  O   . HOH   P 6 .   ? 34.12700  -7.88100  18.05400  1.000 45.66338 ? 437 HOH   A O   1 
HETATM 3897 O  O   . HOH   P 6 .   ? 20.51900  17.91500  -6.51500  1.000 33.58297 ? 438 HOH   A O   1 
HETATM 3898 O  O   . HOH   P 6 .   ? 27.80700  8.15500   -15.21100 1.000 29.60930 ? 439 HOH   A O   1 
HETATM 3899 O  O   . HOH   P 6 .   ? 43.77600  -2.37300  -1.32000  1.000 32.17502 ? 440 HOH   A O   1 
HETATM 3900 O  O   . HOH   P 6 .   ? 19.52900  15.07700  13.87600  1.000 39.54702 ? 441 HOH   A O   1 
HETATM 3901 O  O   . HOH   P 6 .   ? 11.53000  15.44800  -1.19100  1.000 37.76854 ? 442 HOH   A O   1 
HETATM 3902 O  O   . HOH   P 6 .   ? 22.72000  -0.98900  -2.21500  1.000 13.47668 ? 443 HOH   A O   1 
HETATM 3903 O  O   . HOH   P 6 .   ? 35.29400  -13.07000 -9.08900  1.000 23.02917 ? 444 HOH   A O   1 
HETATM 3904 O  O   . HOH   P 6 .   ? 23.63800  7.43200   -18.54900 1.000 45.50816 ? 445 HOH   A O   1 
HETATM 3905 O  O   . HOH   P 6 .   ? 11.90100  15.93000  5.50500   1.000 24.94158 ? 446 HOH   A O   1 
HETATM 3906 O  O   . HOH   P 6 .   ? 19.69200  -12.08200 -11.15000 1.000 30.57418 ? 447 HOH   A O   1 
HETATM 3907 O  O   . HOH   P 6 .   ? 18.28000  10.15600  -16.20500 1.000 35.06259 ? 448 HOH   A O   1 
HETATM 3908 O  O   . HOH   P 6 .   ? 17.43000  9.61400   9.36800   1.000 18.86804 ? 449 HOH   A O   1 
HETATM 3909 O  O   . HOH   P 6 .   ? 15.46100  -5.83400  2.18700   1.000 21.61904 ? 450 HOH   A O   1 
HETATM 3910 O  O   . HOH   P 6 .   ? 40.41400  11.99900  -3.90400  1.000 42.05468 ? 451 HOH   A O   1 
HETATM 3911 O  O   . HOH   P 6 .   ? 32.66300  1.46300   -14.98400 1.000 27.40428 ? 452 HOH   A O   1 
HETATM 3912 O  O   . HOH   P 6 .   ? 27.87200  7.29800   20.87900  1.000 26.98018 ? 453 HOH   A O   1 
HETATM 3913 O  O   . HOH   P 6 .   ? 29.31000  -15.28300 -10.26200 1.000 28.18735 ? 454 HOH   A O   1 
HETATM 3914 O  O   . HOH   P 6 .   ? 14.05100  15.33200  6.98000   1.000 24.93078 ? 455 HOH   A O   1 
HETATM 3915 O  O   . HOH   P 6 .   ? 44.19600  4.86800   19.64300  1.000 27.17738 ? 456 HOH   A O   1 
HETATM 3916 O  O   . HOH   P 6 .   ? 35.665    17.209    4.598     1.000 32.26585 ? 457 HOH   A O   1 
HETATM 3917 O  O   . HOH   P 6 .   ? 34.89300  -3.84000  -12.84200 1.000 22.20112 ? 458 HOH   A O   1 
HETATM 3918 O  O   . HOH   P 6 .   ? 8.91200   4.87000   2.01700   1.000 34.74774 ? 459 HOH   A O   1 
HETATM 3919 O  O   . HOH   P 6 .   ? 14.08100  19.53400  4.07400   1.000 39.70284 ? 460 HOH   A O   1 
HETATM 3920 O  O   . HOH   P 6 .   ? 22.29300  0.11100   0.28700   1.000 11.77735 ? 461 HOH   A O   1 
HETATM 3921 O  O   . HOH   P 6 .   ? 28.79800  2.13100   -16.73300 1.000 40.03750 ? 462 HOH   A O   1 
HETATM 3922 O  O   . HOH   P 6 .   ? 27.02600  -14.36300 3.86100   1.000 16.69775 ? 463 HOH   A O   1 
HETATM 3923 O  O   . HOH   P 6 .   ? 22.65300  7.62800   -2.97900  1.000 12.14164 ? 464 HOH   A O   1 
HETATM 3924 O  O   . HOH   P 6 .   ? 26.16500  20.90100  4.89600   1.000 20.79801 ? 465 HOH   A O   1 
HETATM 3925 O  O   . HOH   P 6 .   ? 12.46600  2.73700   -3.03200  1.000 17.10288 ? 466 HOH   A O   1 
HETATM 3926 O  O   . HOH   P 6 .   ? 26.24900  17.84500  -7.77200  1.000 34.34884 ? 467 HOH   A O   1 
HETATM 3927 O  O   . HOH   P 6 .   ? 26.562    -20.976   -11.927   1.000 35.51008 ? 468 HOH   A O   1 
HETATM 3928 O  O   . HOH   P 6 .   ? 11.09500  -10.98200 -8.85600  1.000 22.62008 ? 469 HOH   A O   1 
HETATM 3929 O  O   . HOH   P 6 .   ? 9.76200   -2.37500  -14.06000 1.000 35.78839 ? 470 HOH   A O   1 
HETATM 3930 O  O   . HOH   P 6 .   ? 16.40400  18.76400  0.87100   1.000 34.84465 ? 471 HOH   A O   1 
HETATM 3931 O  O   . HOH   P 6 .   ? 4.95900   -10.57800 -5.50300  1.000 32.27613 ? 472 HOH   A O   1 
HETATM 3932 O  O   . HOH   P 6 .   ? 28.72000  15.78700  -5.76700  1.000 36.97808 ? 473 HOH   A O   1 
HETATM 3933 O  O   . HOH   P 6 .   ? 45.64500  12.56300  1.46400   1.000 39.18777 ? 474 HOH   A O   1 
HETATM 3934 O  O   . HOH   P 6 .   ? 31.09500  -19.10600 -6.91900  1.000 41.71641 ? 475 HOH   A O   1 
HETATM 3935 O  O   . HOH   P 6 .   ? 29.37500  14.96800  15.39500  1.000 23.33843 ? 476 HOH   A O   1 
HETATM 3936 O  O   . HOH   P 6 .   ? 32.37900  10.72900  17.94700  1.000 30.25530 ? 477 HOH   A O   1 
HETATM 3937 O  O   . HOH   P 6 .   ? 21.87700  -7.08100  3.38000   1.000 14.93881 ? 478 HOH   A O   1 
HETATM 3938 O  O   . HOH   P 6 .   ? 27.86300  17.08300  5.30300   1.000 14.84455 ? 479 HOH   A O   1 
HETATM 3939 O  O   . HOH   P 6 .   ? 34.68100  -1.14300  -12.88100 1.000 27.62497 ? 480 HOH   A O   1 
HETATM 3940 O  O   . HOH   P 6 .   ? 25.84200  -0.46500  17.80600  1.000 25.57123 ? 481 HOH   A O   1 
HETATM 3941 O  O   . HOH   P 6 .   ? 40.94900  -8.53500  9.42800   1.000 33.87328 ? 482 HOH   A O   1 
HETATM 3942 O  O   . HOH   P 6 .   ? 39.45800  -4.88400  -9.20500  1.000 25.81243 ? 483 HOH   A O   1 
HETATM 3943 O  O   . HOH   P 6 .   ? 16.52900  -3.36600  -13.09700 1.000 19.91824 ? 484 HOH   A O   1 
HETATM 3944 O  O   . HOH   P 6 .   ? 29.52400  12.07700  -9.75100  1.000 34.53286 ? 485 HOH   A O   1 
HETATM 3945 O  O   . HOH   P 6 .   ? 13.72100  -18.84900 -5.88000  1.000 23.33444 ? 486 HOH   A O   1 
HETATM 3946 O  O   . HOH   P 6 .   ? 6.44200   13.35400  3.10500   1.000 38.84507 ? 487 HOH   A O   1 
HETATM 3947 O  O   . HOH   P 6 .   ? 23.49800  3.45100   -17.99600 1.000 26.66319 ? 488 HOH   A O   1 
HETATM 3948 O  O   . HOH   P 6 .   ? 28.92159  -0.67700  25.72555  0.50  48.31688 ? 489 HOH   A O   1 
HETATM 3949 O  O   . HOH   P 6 .   ? 39.864    -10.554   -9.330    1.000 31.70913 ? 490 HOH   A O   1 
HETATM 3950 O  O   . HOH   P 6 .   ? 13.81600  17.86500  -6.98400  1.000 35.10605 ? 491 HOH   A O   1 
HETATM 3951 O  O   . HOH   P 6 .   ? 31.84200  11.34700  -9.00500  1.000 36.07322 ? 492 HOH   A O   1 
HETATM 3952 O  O   . HOH   P 6 .   ? 32.37200  -13.83600 -11.83600 1.000 18.62053 ? 493 HOH   A O   1 
HETATM 3953 O  O   . HOH   P 6 .   ? 15.06200  -11.46200 6.25700   1.000 26.38117 ? 494 HOH   A O   1 
HETATM 3954 O  O   . HOH   P 6 .   ? 25.91500  -13.74800 -9.95800  1.000 21.52102 ? 495 HOH   A O   1 
HETATM 3955 O  O   . HOH   P 6 .   ? 35.52000  -14.81300 -3.75300  1.000 30.33361 ? 496 HOH   A O   1 
HETATM 3956 O  O   . HOH   P 6 .   ? 16.40400  12.91300  -9.03800  1.000 26.90046 ? 497 HOH   A O   1 
HETATM 3957 O  O   . HOH   P 6 .   ? 33.79300  -13.79900 -5.65100  1.000 22.99013 ? 498 HOH   A O   1 
HETATM 3958 O  O   . HOH   P 6 .   ? 33.28000  3.99300   19.77500  1.000 27.29910 ? 499 HOH   A O   1 
HETATM 3959 O  O   . HOH   P 6 .   ? 11.27700  14.04600  10.28400  1.000 22.84278 ? 500 HOH   A O   1 
HETATM 3960 O  O   . HOH   P 6 .   ? 7.82200   -0.84400  -3.17000  1.000 43.02623 ? 501 HOH   A O   1 
HETATM 3961 O  O   . HOH   P 6 .   ? 21.63700  -9.43400  4.66000   1.000 17.43749 ? 502 HOH   A O   1 
HETATM 3962 O  O   . HOH   P 6 .   ? 35.60600  16.67100  13.84800  1.000 29.53670 ? 503 HOH   A O   1 
HETATM 3963 O  O   . HOH   P 6 .   ? 26.76300  -7.05200  9.85900   1.000 16.90003 ? 504 HOH   A O   1 
HETATM 3964 O  O   . HOH   P 6 .   ? 16.97600  -17.30700 -11.43300 1.000 37.32542 ? 505 HOH   A O   1 
HETATM 3965 O  O   . HOH   P 6 .   ? 15.74100  2.77800   -12.48000 1.000 40.04055 ? 506 HOH   A O   1 
HETATM 3966 O  O   . HOH   P 6 .   ? 40.78500  1.60500   -5.26000  1.000 24.07856 ? 507 HOH   A O   1 
HETATM 3967 O  O   . HOH   P 6 .   ? 38.55800  12.51300  -5.08500  1.000 32.99137 ? 508 HOH   A O   1 
HETATM 3968 O  O   . HOH   P 6 .   ? 15.58700  -3.01200  -16.27600 1.000 28.20563 ? 509 HOH   A O   1 
HETATM 3969 O  O   . HOH   P 6 .   ? 22.84800  18.79500  -3.09000  1.000 18.73730 ? 510 HOH   A O   1 
HETATM 3970 O  O   . HOH   P 6 .   ? 10.98400  5.90100   -5.88200  1.000 39.18560 ? 511 HOH   A O   1 
HETATM 3971 O  O   . HOH   P 6 .   ? 4.72700   -7.52600  -3.73800  1.000 33.51736 ? 512 HOH   A O   1 
HETATM 3972 O  O   . HOH   P 6 .   ? 42.78100  4.71300   -7.81900  1.000 38.69326 ? 513 HOH   A O   1 
HETATM 3973 O  O   . HOH   P 6 .   ? 19.45900  -6.01900  2.94800   1.000 16.08878 ? 514 HOH   A O   1 
HETATM 3974 O  O   . HOH   P 6 .   ? 12.59800  -1.69700  0.84700   1.000 21.14231 ? 515 HOH   A O   1 
HETATM 3975 O  O   . HOH   P 6 .   ? 46.29600  4.05600   10.02900  1.000 34.80346 ? 516 HOH   A O   1 
HETATM 3976 O  O   . HOH   P 6 .   ? 23.54400  -12.66700 -11.18500 1.000 25.06197 ? 517 HOH   A O   1 
HETATM 3977 O  O   . HOH   P 6 .   ? 33.70400  15.66000  -4.01400  1.000 29.15197 ? 518 HOH   A O   1 
HETATM 3978 O  O   . HOH   P 6 .   ? 19.68300  2.34800   -18.32000 1.000 32.00509 ? 519 HOH   A O   1 
HETATM 3979 O  O   . HOH   P 6 .   ? 37.32800  11.16900  1.11200   1.000 27.93961 ? 520 HOH   A O   1 
HETATM 3980 O  O   . HOH   P 6 .   ? 22.69900  10.90000  -10.30200 1.000 17.86203 ? 521 HOH   A O   1 
HETATM 3981 O  O   . HOH   P 6 .   ? 30.89700  -9.73900  -16.95900 1.000 27.74147 ? 522 HOH   A O   1 
HETATM 3982 O  O   . HOH   P 6 .   ? 12.08700  -15.27400 0.21000   1.000 33.97766 ? 523 HOH   A O   1 
HETATM 3983 O  O   . HOH   P 6 .   ? 10.35300  8.36600   0.99900   1.000 23.65221 ? 524 HOH   A O   1 
HETATM 3984 O  O   . HOH   P 6 .   ? 32.85100  -3.30800  -15.75700 1.000 35.19367 ? 525 HOH   A O   1 
HETATM 3985 O  O   . HOH   P 6 .   ? 35.73600  4.01800   20.22100  1.000 31.48523 ? 526 HOH   A O   1 
HETATM 3986 O  O   . HOH   P 6 .   ? 20.64800  -7.46400  -16.22100 1.000 28.69389 ? 527 HOH   A O   1 
HETATM 3987 O  O   . HOH   P 6 .   ? 29.23300  -15.80300 3.15500   1.000 19.93719 ? 528 HOH   A O   1 
HETATM 3988 O  O   . HOH   P 6 .   ? 27.78900  -9.29100  11.19500  1.000 21.10119 ? 529 HOH   A O   1 
HETATM 3989 O  O   . HOH   P 6 .   ? 6.14800   -8.22100  0.96800   1.000 45.36685 ? 530 HOH   A O   1 
HETATM 3990 O  O   . HOH   P 6 .   ? 27.43100  -17.46800 -8.14200  1.000 32.38039 ? 531 HOH   A O   1 
HETATM 3991 O  O   . HOH   P 6 .   ? 25.62400  -15.34300 6.10200   1.000 18.24714 ? 532 HOH   A O   1 
HETATM 3992 O  O   . HOH   P 6 .   ? 15.45500  -0.21700  -12.34200 1.000 25.78854 ? 533 HOH   A O   1 
HETATM 3993 O  O   . HOH   P 6 .   ? 15.60900  3.06800   12.34400  1.000 30.76714 ? 534 HOH   A O   1 
HETATM 3994 O  O   . HOH   P 6 .   ? 27.36600  -0.14900  10.51800  1.000 18.48293 ? 535 HOH   A O   1 
HETATM 3995 O  O   . HOH   P 6 .   ? 20.15200  -19.83400 7.30200   1.000 40.37320 ? 536 HOH   A O   1 
HETATM 3996 O  O   . HOH   P 6 .   ? 9.08000   -1.35700  -12.08400 1.000 34.70301 ? 537 HOH   A O   1 
HETATM 3997 O  O   . HOH   P 6 .   ? 33.303    20.174    13.086    1.000 40.77293 ? 538 HOH   A O   1 
HETATM 3998 O  O   . HOH   P 6 .   ? 22.38000  4.85500   16.96900  1.000 29.99581 ? 539 HOH   A O   1 
HETATM 3999 O  O   . HOH   P 6 .   ? 13.926    -6.508    -16.264   1.000 32.64328 ? 540 HOH   A O   1 
HETATM 4000 O  O   . HOH   P 6 .   ? 10.05700  -9.27800  -13.27100 1.000 20.51090 ? 541 HOH   A O   1 
HETATM 4001 O  O   . HOH   P 6 .   ? 17.69900  15.77200  -4.54100  1.000 20.82492 ? 542 HOH   A O   1 
HETATM 4002 O  O   . HOH   P 6 .   ? 0.42500   -14.62300 -1.46900  1.000 40.22239 ? 543 HOH   A O   1 
HETATM 4003 O  O   . HOH   P 6 .   ? 19.41900  8.42500   15.85700  1.000 29.65973 ? 544 HOH   A O   1 
HETATM 4004 O  O   . HOH   P 6 .   ? 19.28700  16.25800  7.54600   1.000 23.67585 ? 545 HOH   A O   1 
HETATM 4005 O  O   . HOH   P 6 .   ? 18.46200  19.91100  -3.58200  1.000 37.70215 ? 546 HOH   A O   1 
HETATM 4006 O  O   . HOH   P 6 .   ? 21.06800  -13.60300 -10.30600 1.000 26.96036 ? 547 HOH   A O   1 
HETATM 4007 O  O   . HOH   P 6 .   ? 33.71100  8.98100   -13.19900 1.000 29.24362 ? 548 HOH   A O   1 
HETATM 4008 O  O   . HOH   P 6 .   ? 10.13700  6.03100   8.36500   1.000 41.85209 ? 549 HOH   A O   1 
HETATM 4009 O  O   . HOH   P 6 .   ? 42.84500  -1.53100  11.31900  1.000 37.54123 ? 550 HOH   A O   1 
HETATM 4010 O  O   . HOH   P 6 .   ? 10.52500  -14.31200 1.81800   1.000 36.71538 ? 551 HOH   A O   1 
HETATM 4011 O  O   . HOH   P 6 .   ? 43.32600  12.15600  -0.67300  1.000 36.96360 ? 552 HOH   A O   1 
HETATM 4012 O  O   . HOH   P 6 .   ? 22.35000  2.84100   19.29500  1.000 36.04345 ? 553 HOH   A O   1 
HETATM 4013 O  O   . HOH   P 6 .   ? 40.46500  -5.99300  11.58500  1.000 35.81024 ? 554 HOH   A O   1 
HETATM 4014 O  O   . HOH   P 6 .   ? 22.28200  8.63100   -17.43900 1.000 36.28022 ? 555 HOH   A O   1 
HETATM 4015 O  O   . HOH   P 6 .   ? 23.57700  13.56700  -13.68000 1.000 36.78211 ? 556 HOH   A O   1 
HETATM 4016 O  O   . HOH   P 6 .   ? 17.15400  3.55200   -15.08500 1.000 27.73477 ? 557 HOH   A O   1 
HETATM 4017 O  O   . HOH   P 6 .   ? 36.75800  9.89200   12.93500  1.000 20.90520 ? 558 HOH   A O   1 
HETATM 4018 O  O   . HOH   P 6 .   ? 45.71300  -0.63600  5.78100   1.000 46.94474 ? 559 HOH   A O   1 
HETATM 4019 O  O   . HOH   P 6 .   ? 28.73600  14.48100  -8.46500  1.000 30.89655 ? 560 HOH   A O   1 
HETATM 4020 O  O   . HOH   P 6 .   ? 17.16100  5.99200   -8.53800  1.000 30.88289 ? 561 HOH   A O   1 
HETATM 4021 O  O   . HOH   P 6 .   ? 8.19600   -19.32200 -3.62400  1.000 33.41285 ? 562 HOH   A O   1 
HETATM 4022 O  O   . HOH   P 6 .   ? 41.65400  12.58000  11.99900  1.000 35.41367 ? 563 HOH   A O   1 
HETATM 4023 O  O   . HOH   P 6 .   ? 35.26800  -6.36100  -15.05200 1.000 27.93320 ? 564 HOH   A O   1 
HETATM 4024 O  O   . HOH   P 6 .   ? 25.97500  10.69400  3.28400   1.000 15.66050 ? 565 HOH   A O   1 
HETATM 4025 O  O   . HOH   P 6 .   ? 28.93600  4.59000   -16.64600 1.000 35.52635 ? 566 HOH   A O   1 
HETATM 4026 O  O   . HOH   P 6 .   ? 12.12300  17.42100  -5.90600  1.000 34.27422 ? 567 HOH   A O   1 
HETATM 4027 O  O   . HOH   P 6 .   ? 23.494    -14.828   10.861    1.000 40.04633 ? 568 HOH   A O   1 
HETATM 4028 O  O   . HOH   P 6 .   ? 36.861    11.476    -7.620    1.000 37.85356 ? 569 HOH   A O   1 
HETATM 4029 O  O   . HOH   P 6 .   ? 19.54800  6.89800   -9.00500  1.000 29.28871 ? 570 HOH   A O   1 
HETATM 4030 O  O   . HOH   P 6 .   ? 9.87900   -12.79700 4.60700   1.000 39.22080 ? 571 HOH   A O   1 
HETATM 4031 O  O   . HOH   P 6 .   ? 13.67600  10.39900  -5.70800  1.000 24.02483 ? 572 HOH   A O   1 
HETATM 4032 O  O   . HOH   P 6 .   ? 45.41600  -6.26700  0.57400   1.000 37.71164 ? 573 HOH   A O   1 
HETATM 4033 O  O   . HOH   P 6 .   ? 22.74600  19.10500  10.17300  1.000 34.73919 ? 574 HOH   A O   1 
HETATM 4034 O  O   . HOH   P 6 .   ? 6.42100   -7.55800  -1.35100  1.000 36.05239 ? 575 HOH   A O   1 
HETATM 4035 O  O   . HOH   P 6 .   ? 13.91000  4.68300   6.81400   1.000 18.44580 ? 576 HOH   A O   1 
HETATM 4036 O  O   . HOH   P 6 .   ? 46.60300  1.72300   2.61500   1.000 44.00609 ? 577 HOH   A O   1 
HETATM 4037 O  O   . HOH   P 6 .   ? 29.57500  -11.96400 -15.55800 1.000 26.11820 ? 578 HOH   A O   1 
HETATM 4038 O  O   . HOH   P 6 .   ? 2.97800   -11.94700 1.92400   1.000 55.02991 ? 579 HOH   A O   1 
HETATM 4039 O  O   . HOH   P 6 .   ? 26.06200  19.04100  -4.43700  1.000 18.51803 ? 580 HOH   A O   1 
HETATM 4040 O  O   . HOH   P 6 .   ? 2.51300   -9.04600  0.87400   1.000 48.38431 ? 581 HOH   A O   1 
HETATM 4041 O  O   . HOH   P 6 .   ? 15.54900  -13.11900 -13.81800 1.000 25.55193 ? 582 HOH   A O   1 
HETATM 4042 O  O   . HOH   P 6 .   ? 22.559    -19.584   -5.608    1.000 21.06810 ? 583 HOH   A O   1 
HETATM 4043 O  O   . HOH   P 6 .   ? 9.08000   -19.85400 -6.15000  1.000 35.51427 ? 584 HOH   A O   1 
HETATM 4044 O  O   . HOH   P 6 .   ? 16.24200  16.57400  -0.71100  1.000 30.48645 ? 585 HOH   A O   1 
HETATM 4045 O  O   . HOH   P 6 .   ? 42.84600  2.58600   -3.34500  1.000 38.86244 ? 586 HOH   A O   1 
HETATM 4046 O  O   . HOH   P 6 .   ? 35.85000  12.35400  -6.49400  1.000 30.43477 ? 587 HOH   A O   1 
HETATM 4047 O  O   . HOH   P 6 .   ? 39.01800  -3.26700  -11.63000 1.000 39.24496 ? 588 HOH   A O   1 
HETATM 4048 O  O   . HOH   P 6 .   ? 32.03400  8.32500   -15.08100 1.000 42.14053 ? 589 HOH   A O   1 
HETATM 4049 O  O   . HOH   P 6 .   ? 3.86300   -20.64800 -4.43800  1.000 44.62614 ? 590 HOH   A O   1 
HETATM 4050 O  O   . HOH   P 6 .   ? 12.72800  0.25000   -12.27100 1.000 36.70634 ? 591 HOH   A O   1 
HETATM 4051 O  O   . HOH   P 6 .   ? 37.704    -14.989   -9.729    1.000 33.22977 ? 592 HOH   A O   1 
HETATM 4052 O  O   . HOH   P 6 .   ? 27.43800  4.61200   22.16700  1.000 35.01516 ? 593 HOH   A O   1 
HETATM 4053 O  O   . HOH   P 6 .   ? 26.60900  -18.02400 6.27900   1.000 30.15418 ? 594 HOH   A O   1 
HETATM 4054 O  O   . HOH   P 6 .   ? 28.76400  18.40200  -5.39100  1.000 35.47440 ? 595 HOH   A O   1 
HETATM 4055 O  O   . HOH   P 6 .   ? 25.45900  11.25900  19.10100  1.000 33.63992 ? 596 HOH   A O   1 
HETATM 4056 O  O   . HOH   P 6 .   ? 45.55000  4.87600   -0.76800  1.000 39.11623 ? 597 HOH   A O   1 
HETATM 4057 O  O   . HOH   P 6 .   ? 11.02800  -18.65100 -7.29800  1.000 38.89381 ? 598 HOH   A O   1 
HETATM 4058 O  O   . HOH   P 6 .   ? 44.65400  -4.98000  -1.82300  1.000 33.73598 ? 599 HOH   A O   1 
HETATM 4059 O  O   . HOH   P 6 .   ? 26.00800  -11.46300 11.84100  1.000 21.88031 ? 600 HOH   A O   1 
HETATM 4060 O  O   . HOH   P 6 .   ? 45.92600  1.48700   5.25800   1.000 43.65415 ? 601 HOH   A O   1 
HETATM 4061 O  O   . HOH   P 6 .   ? 42.29100  2.41700   -7.34200  1.000 35.92836 ? 602 HOH   A O   1 
HETATM 4062 O  O   . HOH   P 6 .   ? 15.68500  -18.95600 -12.87900 1.000 42.96552 ? 603 HOH   A O   1 
HETATM 4063 O  O   . HOH   P 6 .   ? 20.18600  9.82000   -9.11600  1.000 20.24809 ? 604 HOH   A O   1 
HETATM 4064 O  O   . HOH   P 6 .   ? 30.77800  17.12800  16.25300  1.000 33.63762 ? 605 HOH   A O   1 
HETATM 4065 O  O   . HOH   P 6 .   ? 1.186     -11.194   0.476     1.000 49.41127 ? 606 HOH   A O   1 
HETATM 4066 O  O   . HOH   P 6 .   ? 30.72700  7.74700   21.13400  1.000 30.13629 ? 607 HOH   A O   1 
HETATM 4067 O  O   . HOH   P 6 .   ? 37.806    -6.190    -15.113   1.000 37.33427 ? 608 HOH   A O   1 
HETATM 4068 O  O   . HOH   P 6 .   ? 43.05400  0.52900   -8.66000  1.000 38.85294 ? 609 HOH   A O   1 
HETATM 4069 O  O   . HOH   P 6 .   ? 39.44200  13.45800  12.36100  1.000 37.01797 ? 610 HOH   A O   1 
HETATM 4070 O  O   . HOH   P 6 .   ? 13.02400  16.15300  9.49400   1.000 32.78751 ? 611 HOH   A O   1 
HETATM 4071 O  O   . HOH   P 6 .   ? 36.14100  -4.06700  -15.14200 1.000 38.22973 ? 612 HOH   A O   1 
HETATM 4072 O  O   . HOH   P 6 .   ? 15.246    -22.302   4.343     1.000 41.06749 ? 613 HOH   A O   1 
HETATM 4073 O  O   . HOH   P 6 .   ? 34.50100  -1.10900  -15.45400 1.000 40.35931 ? 614 HOH   A O   1 
HETATM 4074 O  O   . HOH   P 6 .   ? 23.08400  -7.21500  -17.22800 1.000 30.41652 ? 615 HOH   A O   1 
HETATM 4075 O  O   . HOH   P 6 .   ? 13.01900  -21.33200 -4.02100  1.000 35.47258 ? 616 HOH   A O   1 
HETATM 4076 O  O   . HOH   P 6 .   ? 44.60600  2.25400   0.42200   1.000 38.12249 ? 617 HOH   A O   1 
HETATM 4077 O  O   . HOH   P 6 .   ? 30.517    -14.842   -15.553   1.000 32.32182 ? 618 HOH   A O   1 
HETATM 4078 O  O   . HOH   P 6 .   ? 15.30400  16.80000  -3.06400  1.000 34.14684 ? 619 HOH   A O   1 
HETATM 4079 O  O   . HOH   P 6 .   ? 9.80900   -16.83000 0.62400   1.000 39.47408 ? 620 HOH   A O   1 
HETATM 4080 O  O   . HOH   P 6 .   ? 18.28700  19.43000  2.77200   1.000 37.39169 ? 621 HOH   A O   1 
HETATM 4081 O  O   . HOH   P 6 .   ? 31.65400  10.14800  20.75300  1.000 41.73590 ? 622 HOH   A O   1 
HETATM 4082 O  O   . HOH   P 6 .   ? 10.50200  4.46500   -3.20900  1.000 34.58655 ? 623 HOH   A O   1 
HETATM 4083 O  O   . HOH   P 6 .   ? 36.71500  -0.68300  -11.15500 1.000 39.31162 ? 624 HOH   A O   1 
HETATM 4084 O  O   . HOH   P 6 .   ? 15.26900  7.22100   14.74300  1.000 36.27391 ? 625 HOH   A O   1 
HETATM 4085 O  O   . HOH   P 6 .   ? 19.821    10.744    -18.546   1.000 35.89658 ? 626 HOH   A O   1 
HETATM 4086 O  O   . HOH   P 6 .   ? 45.70600  2.01100   -4.07600  1.000 44.50151 ? 627 HOH   A O   1 
HETATM 4087 O  O   . HOH   P 6 .   ? 29.73100  10.06200  -15.76500 1.000 38.32799 ? 628 HOH   A O   1 
HETATM 4088 O  O   . HOH   P 6 .   ? 13.72200  -11.30500 -13.15500 1.000 19.82470 ? 629 HOH   A O   1 
HETATM 4089 O  O   . HOH   P 6 .   ? 21.80800  13.80000  15.19200  1.000 36.93305 ? 630 HOH   A O   1 
HETATM 4090 O  O   . HOH   P 6 .   ? 17.96400  17.28700  -6.71100  1.000 37.00766 ? 631 HOH   A O   1 
HETATM 4091 O  O   . HOH   P 6 .   ? 8.61300   7.47300   -0.61300  1.000 34.64768 ? 632 HOH   A O   1 
HETATM 4092 O  O   . HOH   P 6 .   ? 22.94400  11.82300  19.60300  1.000 44.88450 ? 633 HOH   A O   1 
HETATM 4093 O  O   . HOH   P 6 .   ? 24.92000  -2.61000  -16.76200 1.000 27.51893 ? 634 HOH   A O   1 
HETATM 4094 O  O   . HOH   P 6 .   ? 21.36000  13.20300  -11.71800 1.000 29.36951 ? 635 HOH   A O   1 
HETATM 4095 O  O   . HOH   P 6 .   ? 35.90700  -8.05900  16.12400  1.000 40.29713 ? 636 HOH   A O   1 
HETATM 4096 O  O   . HOH   P 6 .   ? 8.98600   -19.71600 -0.02400  1.000 46.82639 ? 637 HOH   A O   1 
HETATM 4097 O  O   . HOH   P 6 .   ? 32.24100  15.48700  -6.30900  1.000 41.02519 ? 638 HOH   A O   1 
HETATM 4098 O  O   . HOH   P 6 .   ? 26.88400  9.80000   21.68600  1.000 36.19768 ? 639 HOH   A O   1 
HETATM 4099 O  O   . HOH   P 6 .   ? 9.65500   15.60400  -3.14500  1.000 37.89928 ? 640 HOH   A O   1 
HETATM 4100 O  O   . HOH   P 6 .   ? 32.31600  5.57400   21.68900  1.000 33.67828 ? 641 HOH   A O   1 
HETATM 4101 O  O   . HOH   P 6 .   ? 21.72300  21.16200  -4.27100  1.000 34.20252 ? 642 HOH   A O   1 
HETATM 4102 O  O   . HOH   P 6 .   ? 26.443    -14.328   12.008    1.000 41.44243 ? 643 HOH   A O   1 
HETATM 4103 O  O   . HOH   P 6 .   ? 26.61400  15.73600  16.72600  1.000 31.65063 ? 644 HOH   A O   1 
HETATM 4104 O  O   . HOH   P 6 .   ? 30.50600  12.77300  17.09400  1.000 33.01534 ? 645 HOH   A O   1 
HETATM 4105 O  O   . HOH   P 6 .   ? 32.01400  -15.83500 -10.10300 1.000 32.63101 ? 646 HOH   A O   1 
HETATM 4106 O  O   . HOH   P 6 .   ? 43.57700  -8.61600  -0.43300  1.000 44.76181 ? 647 HOH   A O   1 
HETATM 4107 O  O   . HOH   P 6 .   ? 9.418     3.260     -9.451    1.000 41.08115 ? 648 HOH   A O   1 
HETATM 4108 O  O   . HOH   P 6 .   ? 8.677     4.299     -7.578    1.000 41.36021 ? 649 HOH   A O   1 
HETATM 4109 O  O   . HOH   P 6 .   ? 34.59300  13.03600  15.22000  1.000 35.78203 ? 650 HOH   A O   1 
HETATM 4110 O  O   . HOH   P 6 .   ? 27.18300  13.36300  18.84100  1.000 37.68406 ? 651 HOH   A O   1 
HETATM 4111 O  O   . HOH   Q 6 .   ? 5.44600   6.75600   10.84200  1.000 41.12737 ? 401 HOH   B O   1 
HETATM 4112 O  O   . HOH   Q 6 .   ? -6.049    30.059    39.215    1.000 29.96677 ? 402 HOH   B O   1 
HETATM 4113 O  O   . HOH   Q 6 .   ? 10.98800  11.86500  35.98200  1.000 23.40158 ? 403 HOH   B O   1 
HETATM 4114 O  O   . HOH   Q 6 .   ? 11.74600  37.28400  36.80500  1.000 24.35500 ? 404 HOH   B O   1 
HETATM 4115 O  O   . HOH   Q 6 .   ? -18.53800 21.08400  19.96700  1.000 45.68479 ? 405 HOH   B O   1 
HETATM 4116 O  O   . HOH   Q 6 .   ? 20.38600  10.62500  33.22100  1.000 29.17151 ? 406 HOH   B O   1 
HETATM 4117 O  O   . HOH   Q 6 .   ? 11.58100  38.15200  20.54300  1.000 37.30540 ? 407 HOH   B O   1 
HETATM 4118 O  O   . HOH   Q 6 .   ? 17.76500  31.13600  32.32000  1.000 35.98236 ? 408 HOH   B O   1 
HETATM 4119 O  O   . HOH   Q 6 .   ? -5.595    30.878    28.636    1.000 31.70643 ? 409 HOH   B O   1 
HETATM 4120 O  O   . HOH   Q 6 .   ? -5.98200  9.81100   35.12600  1.000 29.34089 ? 410 HOH   B O   1 
HETATM 4121 O  O   . HOH   Q 6 .   ? -8.08500  12.84000  38.65100  1.000 41.46478 ? 411 HOH   B O   1 
HETATM 4122 O  O   . HOH   Q 6 .   ? -3.70100  13.16900  42.26300  1.000 39.20599 ? 412 HOH   B O   1 
HETATM 4123 O  O   . HOH   Q 6 .   ? 10.565    9.915     39.809    1.000 35.56288 ? 413 HOH   B O   1 
HETATM 4124 O  O   . HOH   Q 6 .   ? -8.72300  27.32300  40.53400  1.000 32.42312 ? 414 HOH   B O   1 
HETATM 4125 O  O   . HOH   Q 6 .   ? 14.38600  35.96100  33.41900  1.000 35.40697 ? 415 HOH   B O   1 
HETATM 4126 O  O   . HOH   Q 6 .   ? -4.84500  13.26300  39.69900  1.000 34.62567 ? 416 HOH   B O   1 
HETATM 4127 O  O   . HOH   Q 6 .   ? -17.00900 7.47600   11.03600  1.000 27.63331 ? 417 HOH   B O   1 
HETATM 4128 O  O   . HOH   Q 6 .   ? -7.96700  0.65800   30.01300  1.000 40.84352 ? 418 HOH   B O   1 
HETATM 4129 O  O   . HOH   Q 6 .   ? 14.65400  9.17500   11.12000  1.000 35.19932 ? 419 HOH   B O   1 
HETATM 4130 O  O   . HOH   Q 6 .   ? 18.74800  17.80200  34.21200  1.000 29.46895 ? 420 HOH   B O   1 
HETATM 4131 O  O   . HOH   Q 6 .   ? 2.19200   7.72100   12.70200  1.000 28.02338 ? 421 HOH   B O   1 
HETATM 4132 O  O   . HOH   Q 6 .   ? -11.31100 9.39800   5.87300   1.000 37.30015 ? 422 HOH   B O   1 
HETATM 4133 O  O   . HOH   Q 6 .   ? 5.68100   -0.18000  21.49400  1.000 27.39171 ? 423 HOH   B O   1 
HETATM 4134 O  O   . HOH   Q 6 .   ? 5.16500   37.88800  21.19400  1.000 24.75403 ? 424 HOH   B O   1 
HETATM 4135 O  O   . HOH   Q 6 .   ? 20.67400  20.22700  34.96700  1.000 33.44611 ? 425 HOH   B O   1 
HETATM 4136 O  O   . HOH   Q 6 .   ? -2.17300  3.48600   40.51400  1.000 25.81914 ? 426 HOH   B O   1 
HETATM 4137 O  O   . HOH   Q 6 .   ? -16.89300 27.78500  40.68500  1.000 25.27806 ? 427 HOH   B O   1 
HETATM 4138 O  O   . HOH   Q 6 .   ? 19.49900  7.95200   31.65300  1.000 25.07452 ? 428 HOH   B O   1 
HETATM 4139 O  O   . HOH   Q 6 .   ? 9.74900   11.54100  30.69200  1.000 17.98153 ? 429 HOH   B O   1 
HETATM 4140 O  O   . HOH   Q 6 .   ? 16.98300  34.58800  32.88500  1.000 34.19759 ? 430 HOH   B O   1 
HETATM 4141 O  O   . HOH   Q 6 .   ? 17.88300  26.30300  36.15000  1.000 16.42416 ? 431 HOH   B O   1 
HETATM 4142 O  O   . HOH   Q 6 .   ? 19.06600  7.86400   27.28700  1.000 26.98711 ? 432 HOH   B O   1 
HETATM 4143 O  O   . HOH   Q 6 .   ? -17.76400 16.33100  17.47000  1.000 35.67126 ? 433 HOH   B O   1 
HETATM 4144 O  O   . HOH   Q 6 .   ? -15.78400 21.97000  18.34600  1.000 38.74779 ? 434 HOH   B O   1 
HETATM 4145 O  O   . HOH   Q 6 .   ? 18.06500  8.81100   23.08100  1.000 29.06519 ? 435 HOH   B O   1 
HETATM 4146 O  O   . HOH   Q 6 .   ? 0.77800   28.03200  9.19200   1.000 40.08010 ? 436 HOH   B O   1 
HETATM 4147 O  O   . HOH   Q 6 .   ? -8.40800  14.55800  6.42200   1.000 28.48347 ? 437 HOH   B O   1 
HETATM 4148 O  O   . HOH   Q 6 .   ? 22.08500  14.92100  30.28200  1.000 35.70578 ? 438 HOH   B O   1 
HETATM 4149 O  O   . HOH   Q 6 .   ? 2.91900   24.88400  35.97600  1.000 19.88942 ? 439 HOH   B O   1 
HETATM 4150 O  O   . HOH   Q 6 .   ? 3.40800   20.72800  7.88000   1.000 29.91246 ? 440 HOH   B O   1 
HETATM 4151 O  O   . HOH   Q 6 .   ? -3.85900  32.82300  16.49400  1.000 42.54575 ? 441 HOH   B O   1 
HETATM 4152 O  O   . HOH   Q 6 .   ? -5.27700  9.35000   43.11500  1.000 31.55390 ? 442 HOH   B O   1 
HETATM 4153 O  O   . HOH   Q 6 .   ? 14.40800  12.75400  15.56900  1.000 29.65580 ? 443 HOH   B O   1 
HETATM 4154 O  O   . HOH   Q 6 .   ? 12.67000  33.01800  24.44600  1.000 21.24514 ? 444 HOH   B O   1 
HETATM 4155 O  O   . HOH   Q 6 .   ? 16.80300  6.21700   28.36400  1.000 26.69977 ? 445 HOH   B O   1 
HETATM 4156 O  O   . HOH   Q 6 .   ? 16.53200  19.40000  41.59000  1.000 31.92351 ? 446 HOH   B O   1 
HETATM 4157 O  O   . HOH   Q 6 .   ? -10.46300 9.95700   33.33000  1.000 41.10623 ? 447 HOH   B O   1 
HETATM 4158 O  O   . HOH   Q 6 .   ? -7.34500  36.23500  16.46100  1.000 48.25583 ? 448 HOH   B O   1 
HETATM 4159 O  O   . HOH   Q 6 .   ? -5.60500  18.57600  27.85700  1.000 21.20424 ? 449 HOH   B O   1 
HETATM 4160 O  O   . HOH   Q 6 .   ? 8.03900   19.88400  43.60600  1.000 24.65502 ? 450 HOH   B O   1 
HETATM 4161 O  O   . HOH   Q 6 .   ? -11.08800 9.83900   13.35800  1.000 25.98518 ? 451 HOH   B O   1 
HETATM 4162 O  O   . HOH   Q 6 .   ? -0.04900  24.30300  34.57100  1.000 21.69929 ? 452 HOH   B O   1 
HETATM 4163 O  O   . HOH   Q 6 .   ? -2.26500  31.98400  38.34700  1.000 36.01987 ? 453 HOH   B O   1 
HETATM 4164 O  O   . HOH   Q 6 .   ? 21.83100  9.96100   26.48200  1.000 31.06280 ? 454 HOH   B O   1 
HETATM 4165 O  O   . HOH   Q 6 .   ? 11.90200  26.85300  10.98500  1.000 22.42608 ? 455 HOH   B O   1 
HETATM 4166 O  O   . HOH   Q 6 .   ? -5.88600  31.97300  43.30600  1.000 37.89163 ? 456 HOH   B O   1 
HETATM 4167 O  O   . HOH   Q 6 .   ? -3.60000  1.64200   17.04300  1.000 27.53642 ? 457 HOH   B O   1 
HETATM 4168 O  O   . HOH   Q 6 .   ? 1.86400   1.41100   18.24200  1.000 22.13857 ? 458 HOH   B O   1 
HETATM 4169 O  O   . HOH   Q 6 .   ? 5.41500   -0.34300  28.72900  1.000 18.76421 ? 459 HOH   B O   1 
HETATM 4170 O  O   . HOH   Q 6 .   ? 1.32200   21.71200  38.58000  1.000 22.81033 ? 460 HOH   B O   1 
HETATM 4171 O  O   . HOH   Q 6 .   ? 16.17700  20.95500  15.81300  1.000 20.28586 ? 461 HOH   B O   1 
HETATM 4172 O  O   . HOH   Q 6 .   ? 3.55800   18.46700  29.34000  1.000 12.37380 ? 462 HOH   B O   1 
HETATM 4173 O  O   . HOH   Q 6 .   ? 8.64000   24.68900  8.46600   1.000 36.30616 ? 463 HOH   B O   1 
HETATM 4174 O  O   . HOH   Q 6 .   ? 1.21100   25.93200  29.88600  1.000 15.51310 ? 464 HOH   B O   1 
HETATM 4175 O  O   . HOH   Q 6 .   ? -3.33900  4.14300   38.10200  1.000 29.21352 ? 465 HOH   B O   1 
HETATM 4176 O  O   . HOH   Q 6 .   ? 6.08700   19.39400  28.73400  1.000 12.59756 ? 466 HOH   B O   1 
HETATM 4177 O  O   . HOH   Q 6 .   ? 16.01000  14.24400  35.32000  1.000 34.07626 ? 467 HOH   B O   1 
HETATM 4178 O  O   . HOH   Q 6 .   ? 12.11900  22.38800  11.35300  1.000 23.86460 ? 468 HOH   B O   1 
HETATM 4179 O  O   . HOH   Q 6 .   ? 21.25400  13.50000  27.07000  1.000 25.75980 ? 469 HOH   B O   1 
HETATM 4180 O  O   . HOH   Q 6 .   ? -0.55900  30.76900  36.62200  1.000 24.49740 ? 470 HOH   B O   1 
HETATM 4181 O  O   . HOH   Q 6 .   ? 15.96200  29.77600  30.67700  1.000 23.85304 ? 471 HOH   B O   1 
HETATM 4182 O  O   . HOH   Q 6 .   ? 21.37900  26.13100  19.14100  1.000 32.86577 ? 472 HOH   B O   1 
HETATM 4183 O  O   . HOH   Q 6 .   ? 10.64400  22.81100  43.01500  1.000 26.98802 ? 473 HOH   B O   1 
HETATM 4184 O  O   . HOH   Q 6 .   ? -14.11700 20.90900  27.29000  1.000 31.70124 ? 474 HOH   B O   1 
HETATM 4185 O  O   . HOH   Q 6 .   ? -6.51400  5.66800   7.07300   1.000 36.39277 ? 475 HOH   B O   1 
HETATM 4186 O  O   . HOH   Q 6 .   ? -10.35300 7.49800   30.13000  1.000 21.57744 ? 476 HOH   B O   1 
HETATM 4187 O  O   . HOH   Q 6 .   ? 9.55800   37.79900  42.60700  1.000 29.30988 ? 477 HOH   B O   1 
HETATM 4188 O  O   . HOH   Q 6 .   ? 0.15000   28.47600  30.08200  1.000 16.83486 ? 478 HOH   B O   1 
HETATM 4189 O  O   . HOH   Q 6 .   ? 10.02500  12.54600  40.15000  1.000 32.04345 ? 479 HOH   B O   1 
HETATM 4190 O  O   . HOH   Q 6 .   ? 14.46900  29.06600  39.36900  1.000 19.64429 ? 480 HOH   B O   1 
HETATM 4191 O  O   . HOH   Q 6 .   ? 7.92700   32.80400  15.62300  1.000 28.11742 ? 481 HOH   B O   1 
HETATM 4192 O  O   . HOH   Q 6 .   ? 12.97800  6.82900   28.14100  1.000 17.09607 ? 482 HOH   B O   1 
HETATM 4193 O  O   . HOH   Q 6 .   ? 7.34300   15.88600  38.92600  1.000 16.32240 ? 483 HOH   B O   1 
HETATM 4194 O  O   . HOH   Q 6 .   ? 20.48200  22.87700  17.77400  1.000 36.28603 ? 484 HOH   B O   1 
HETATM 4195 O  O   . HOH   Q 6 .   ? 0.14900   17.56900  41.41700  1.000 41.87960 ? 485 HOH   B O   1 
HETATM 4196 O  O   . HOH   Q 6 .   ? 4.66900   16.01600  9.21600   1.000 39.76740 ? 486 HOH   B O   1 
HETATM 4197 O  O   . HOH   Q 6 .   ? 14.17700  4.49800   29.21300  1.000 25.57350 ? 487 HOH   B O   1 
HETATM 4198 O  O   . HOH   Q 6 .   ? -17.93700 13.11100  25.42100  1.000 31.78275 ? 488 HOH   B O   1 
HETATM 4199 O  O   . HOH   Q 6 .   ? 14.81800  31.31500  24.50600  1.000 27.81976 ? 489 HOH   B O   1 
HETATM 4200 O  O   . HOH   Q 6 .   ? 18.27800  24.37800  14.29600  1.000 22.46198 ? 490 HOH   B O   1 
HETATM 4201 O  O   . HOH   Q 6 .   ? -13.22600 22.91000  16.19500  1.000 34.23380 ? 491 HOH   B O   1 
HETATM 4202 O  O   . HOH   Q 6 .   ? 20.75200  17.47200  23.35400  1.000 29.81057 ? 492 HOH   B O   1 
HETATM 4203 O  O   . HOH   Q 6 .   ? -15.83100 9.39900   20.65100  1.000 25.68663 ? 493 HOH   B O   1 
HETATM 4204 O  O   . HOH   Q 6 .   ? 6.08300   10.66900  28.84100  1.000 11.94740 ? 494 HOH   B O   1 
HETATM 4205 O  O   . HOH   Q 6 .   ? -9.46800  1.15200   28.34400  1.000 31.06503 ? 495 HOH   B O   1 
HETATM 4206 O  O   . HOH   Q 6 .   ? 16.27900  31.06900  17.89000  1.000 23.94982 ? 496 HOH   B O   1 
HETATM 4207 O  O   . HOH   Q 6 .   ? 2.35100   25.39500  43.70100  1.000 29.77330 ? 497 HOH   B O   1 
HETATM 4208 O  O   . HOH   Q 6 .   ? 1.93300   5.07700   11.92600  1.000 39.18840 ? 498 HOH   B O   1 
HETATM 4209 O  O   . HOH   Q 6 .   ? 1.51700   34.47300  22.20500  1.000 18.53924 ? 499 HOH   B O   1 
HETATM 4210 O  O   . HOH   Q 6 .   ? -3.12900  1.78700   24.47400  1.000 15.14576 ? 500 HOH   B O   1 
HETATM 4211 O  O   . HOH   Q 6 .   ? -14.033   8.916     8.343     1.000 38.14251 ? 501 HOH   B O   1 
HETATM 4212 O  O   . HOH   Q 6 .   ? 15.66700  18.24000  15.81000  1.000 26.09014 ? 502 HOH   B O   1 
HETATM 4213 O  O   . HOH   Q 6 .   ? 18.839    20.642    41.078    1.000 37.15713 ? 503 HOH   B O   1 
HETATM 4214 O  O   . HOH   Q 6 .   ? -6.82700  28.77900  24.54500  1.000 25.68351 ? 504 HOH   B O   1 
HETATM 4215 O  O   . HOH   Q 6 .   ? 7.42800   16.45000  10.56300  1.000 18.21183 ? 505 HOH   B O   1 
HETATM 4216 O  O   . HOH   Q 6 .   ? -5.65000  26.39100  25.55000  1.000 19.07113 ? 506 HOH   B O   1 
HETATM 4217 O  O   . HOH   Q 6 .   ? 17.84300  15.65500  17.78000  1.000 27.18011 ? 507 HOH   B O   1 
HETATM 4218 O  O   . HOH   Q 6 .   ? -20.20700 25.32100  21.83000  1.000 49.45844 ? 508 HOH   B O   1 
HETATM 4219 O  O   . HOH   Q 6 .   ? 0.80600   33.22600  24.56500  1.000 16.09512 ? 509 HOH   B O   1 
HETATM 4220 O  O   . HOH   Q 6 .   ? 12.29100  11.19900  30.92800  1.000 24.92330 ? 510 HOH   B O   1 
HETATM 4221 O  O   . HOH   Q 6 .   ? -1.18100  34.46100  26.10400  1.000 18.47241 ? 511 HOH   B O   1 
HETATM 4222 O  O   . HOH   Q 6 .   ? 20.96900  27.71300  33.67300  1.000 34.95068 ? 512 HOH   B O   1 
HETATM 4223 O  O   . HOH   Q 6 .   ? 13.20600  6.44400   17.17500  1.000 36.19123 ? 513 HOH   B O   1 
HETATM 4224 O  O   . HOH   Q 6 .   ? -0.48000  32.66200  41.28000  1.000 39.86175 ? 514 HOH   B O   1 
HETATM 4225 O  O   . HOH   Q 6 .   ? 18.69300  27.16900  40.18400  1.000 18.79968 ? 515 HOH   B O   1 
HETATM 4226 O  O   . HOH   Q 6 .   ? 6.571     27.643    49.552    1.000 43.25008 ? 516 HOH   B O   1 
HETATM 4227 O  O   . HOH   Q 6 .   ? 13.05400  30.58100  15.07600  1.000 24.84645 ? 517 HOH   B O   1 
HETATM 4228 O  O   . HOH   Q 6 .   ? 12.89900  35.92200  23.74300  1.000 22.01061 ? 518 HOH   B O   1 
HETATM 4229 O  O   . HOH   Q 6 .   ? -9.24600  19.08000  8.58000   1.000 40.41815 ? 519 HOH   B O   1 
HETATM 4230 O  O   . HOH   Q 6 .   ? 9.83800   31.64600  17.13400  1.000 23.78176 ? 520 HOH   B O   1 
HETATM 4231 O  O   . HOH   Q 6 .   ? -17.80700 12.39100  14.86300  1.000 25.08111 ? 521 HOH   B O   1 
HETATM 4232 O  O   . HOH   Q 6 .   ? -13.37000 4.89800   23.69900  1.000 27.48192 ? 522 HOH   B O   1 
HETATM 4233 O  O   . HOH   Q 6 .   ? 10.95500  6.23700   19.49100  1.000 35.25291 ? 523 HOH   B O   1 
HETATM 4234 O  O   . HOH   Q 6 .   ? 10.56900  -1.31700  26.70400  1.000 33.39054 ? 524 HOH   B O   1 
HETATM 4235 O  O   . HOH   Q 6 .   ? -17.10900 16.06300  20.02200  1.000 34.18006 ? 525 HOH   B O   1 
HETATM 4236 O  O   . HOH   Q 6 .   ? 21.11300  23.73100  36.25800  1.000 36.41962 ? 526 HOH   B O   1 
HETATM 4237 O  O   . HOH   Q 6 .   ? -11.36500 9.65400   15.97500  1.000 21.99909 ? 527 HOH   B O   1 
HETATM 4238 O  O   . HOH   Q 6 .   ? -10.10400 22.61500  12.59500  1.000 39.68016 ? 528 HOH   B O   1 
HETATM 4239 O  O   . HOH   Q 6 .   ? -6.97800  19.40200  25.24200  1.000 19.50526 ? 529 HOH   B O   1 
HETATM 4240 O  O   . HOH   Q 6 .   ? -4.93900  34.34500  27.14400  1.000 34.37777 ? 530 HOH   B O   1 
HETATM 4241 O  O   . HOH   Q 6 .   ? -13.35900 15.21000  30.64400  1.000 26.37028 ? 531 HOH   B O   1 
HETATM 4242 O  O   . HOH   Q 6 .   ? 10.48200  36.55700  25.49300  1.000 25.32487 ? 532 HOH   B O   1 
HETATM 4243 O  O   . HOH   Q 6 .   ? -0.06800  25.34700  36.70500  1.000 31.36227 ? 533 HOH   B O   1 
HETATM 4244 O  O   . HOH   Q 6 .   ? 7.35500   2.42800   33.50500  1.000 34.21683 ? 534 HOH   B O   1 
HETATM 4245 O  O   . HOH   Q 6 .   ? -19.01100 15.75600  25.56000  1.000 40.48248 ? 535 HOH   B O   1 
HETATM 4246 O  O   . HOH   Q 6 .   ? 19.43900  20.75700  17.58700  1.000 34.20087 ? 536 HOH   B O   1 
HETATM 4247 O  O   . HOH   Q 6 .   ? 5.66700   2.88000   17.72700  1.000 25.13324 ? 537 HOH   B O   1 
HETATM 4248 O  O   . HOH   Q 6 .   ? 3.82500   20.64000  38.98800  1.000 19.11086 ? 538 HOH   B O   1 
HETATM 4249 O  O   . HOH   Q 6 .   ? 19.24200  13.84900  33.22500  1.000 30.39433 ? 539 HOH   B O   1 
HETATM 4250 O  O   . HOH   Q 6 .   ? -6.755    27.779    42.951    1.000 36.91894 ? 540 HOH   B O   1 
HETATM 4251 O  O   . HOH   Q 6 .   ? 6.63700   5.75900   13.05000  1.000 30.26026 ? 541 HOH   B O   1 
HETATM 4252 O  O   . HOH   Q 6 .   ? 1.59100   25.05300  32.38700  1.000 18.53830 ? 542 HOH   B O   1 
HETATM 4253 O  O   . HOH   Q 6 .   ? -0.43200  5.59900   6.53300   1.000 37.40452 ? 543 HOH   B O   1 
HETATM 4254 O  O   . HOH   Q 6 .   ? 12.64700  34.57400  21.26200  1.000 41.32796 ? 544 HOH   B O   1 
HETATM 4255 O  O   . HOH   Q 6 .   ? 5.02000   3.35900   40.09700  1.000 41.96066 ? 545 HOH   B O   1 
HETATM 4256 O  O   . HOH   Q 6 .   ? 19.82000  21.23100  23.92300  1.000 33.43536 ? 546 HOH   B O   1 
HETATM 4257 O  O   . HOH   Q 6 .   ? 14.72000  32.78300  20.90900  1.000 33.38158 ? 547 HOH   B O   1 
HETATM 4258 O  O   . HOH   Q 6 .   ? -4.76700  3.07300   32.91100  1.000 26.06453 ? 548 HOH   B O   1 
HETATM 4259 O  O   . HOH   Q 6 .   ? 1.381     40.927    35.957    1.000 30.80538 ? 549 HOH   B O   1 
HETATM 4260 O  O   . HOH   Q 6 .   ? 8.05100   2.93900   21.93900  1.000 39.09460 ? 550 HOH   B O   1 
HETATM 4261 O  O   . HOH   Q 6 .   ? 21.41000  24.41200  27.04400  1.000 30.02457 ? 551 HOH   B O   1 
HETATM 4262 O  O   . HOH   Q 6 .   ? -17.88500 10.94400  10.23900  1.000 23.06861 ? 552 HOH   B O   1 
HETATM 4263 O  O   . HOH   Q 6 .   ? 3.22800   10.50600  41.46900  1.000 25.67435 ? 553 HOH   B O   1 
HETATM 4264 O  O   . HOH   Q 6 .   ? -1.07400  0.48300   31.44300  1.000 30.24593 ? 554 HOH   B O   1 
HETATM 4265 O  O   . HOH   Q 6 .   ? 6.42000   -0.58000  25.14500  1.000 22.60614 ? 555 HOH   B O   1 
HETATM 4266 O  O   . HOH   Q 6 .   ? 7.45900   0.45400   23.25300  1.000 31.43991 ? 556 HOH   B O   1 
HETATM 4267 O  O   . HOH   Q 6 .   ? -13.021   19.923    8.419     1.000 43.97364 ? 557 HOH   B O   1 
HETATM 4268 O  O   . HOH   Q 6 .   ? 12.20800  39.43500  29.27500  1.000 24.23327 ? 558 HOH   B O   1 
HETATM 4269 O  O   . HOH   Q 6 .   ? 16.77600  17.95400  35.02100  1.000 30.13964 ? 559 HOH   B O   1 
HETATM 4270 O  O   . HOH   Q 6 .   ? 1.81400   17.00800  44.85100  1.000 47.18947 ? 560 HOH   B O   1 
HETATM 4271 O  O   . HOH   Q 6 .   ? 15.38500  8.17000   17.23100  1.000 29.06314 ? 561 HOH   B O   1 
HETATM 4272 O  O   . HOH   Q 6 .   ? 8.51600   5.74300   42.23700  1.000 38.90650 ? 562 HOH   B O   1 
HETATM 4273 O  O   . HOH   Q 6 .   ? 7.58600   38.08300  35.40000  1.000 39.83493 ? 563 HOH   B O   1 
HETATM 4274 O  O   . HOH   Q 6 .   ? 19.04200  30.75100  34.47200  1.000 27.80101 ? 564 HOH   B O   1 
HETATM 4275 O  O   . HOH   Q 6 .   ? -6.24700  13.09600  2.47400   1.000 38.69809 ? 565 HOH   B O   1 
HETATM 4276 O  O   . HOH   Q 6 .   ? 20.75300  24.43300  29.62100  1.000 28.22560 ? 566 HOH   B O   1 
HETATM 4277 O  O   . HOH   Q 6 .   ? -11.61300 20.24200  41.19400  1.000 38.85226 ? 567 HOH   B O   1 
HETATM 4278 O  O   . HOH   Q 6 .   ? 23.43200  12.51900  28.59300  1.000 35.99352 ? 568 HOH   B O   1 
HETATM 4279 O  O   . HOH   Q 6 .   ? -8.45600  16.38400  36.88400  1.000 37.71410 ? 569 HOH   B O   1 
HETATM 4280 O  O   . HOH   Q 6 .   ? 6.55500   36.20900  18.46500  1.000 42.38458 ? 570 HOH   B O   1 
HETATM 4281 O  O   . HOH   Q 6 .   ? 10.71300  3.56200   22.31100  1.000 29.30720 ? 571 HOH   B O   1 
HETATM 4282 O  O   . HOH   Q 6 .   ? 16.04000  3.79500   27.35800  1.000 36.63673 ? 572 HOH   B O   1 
HETATM 4283 O  O   . HOH   Q 6 .   ? 0.45700   7.43100   14.78900  1.000 21.75089 ? 573 HOH   B O   1 
HETATM 4284 O  O   . HOH   Q 6 .   ? 9.78100   6.61400   14.17000  1.000 25.61736 ? 574 HOH   B O   1 
HETATM 4285 O  O   . HOH   Q 6 .   ? -22.15091 21.24000  25.72555  0.50  47.04809 ? 575 HOH   B O   1 
HETATM 4286 O  O   . HOH   Q 6 .   ? 5.70800   34.17000  39.26400  1.000 35.58514 ? 576 HOH   B O   1 
HETATM 4287 O  O   . HOH   Q 6 .   ? 19.27200  11.29500  22.08800  1.000 36.75903 ? 577 HOH   B O   1 
HETATM 4288 O  O   . HOH   Q 6 .   ? -14.36300 23.00600  39.98300  1.000 36.75194 ? 578 HOH   B O   1 
HETATM 4289 O  O   . HOH   Q 6 .   ? -0.63400  8.17600   25.96400  1.000 15.62036 ? 579 HOH   B O   1 
HETATM 4290 O  O   . HOH   Q 6 .   ? -14.71900 12.44800  32.41800  1.000 34.02871 ? 580 HOH   B O   1 
HETATM 4291 O  O   . HOH   Q 6 .   ? 10.91500  37.38300  49.29400  1.000 46.43531 ? 581 HOH   B O   1 
HETATM 4292 O  O   . HOH   Q 6 .   ? 16.70700  15.55100  14.36700  1.000 42.66361 ? 582 HOH   B O   1 
HETATM 4293 O  O   . HOH   Q 6 .   ? 5.74400   28.97400  49.30700  1.000 46.09059 ? 583 HOH   B O   1 
HETATM 4294 O  O   . HOH   Q 6 .   ? 7.28900   23.19900  44.20100  1.000 40.34259 ? 584 HOH   B O   1 
HETATM 4295 O  O   . HOH   Q 6 .   ? 16.69200  17.93100  38.04300  1.000 29.04315 ? 585 HOH   B O   1 
HETATM 4296 O  O   . HOH   Q 6 .   ? -11.91700 10.97600  33.65000  1.000 43.00144 ? 586 HOH   B O   1 
HETATM 4297 O  O   . HOH   Q 6 .   ? 9.19700   34.71800  19.23800  1.000 26.77104 ? 587 HOH   B O   1 
HETATM 4298 O  O   . HOH   Q 6 .   ? -7.54600  8.00600   37.38100  1.000 32.51199 ? 588 HOH   B O   1 
HETATM 4299 O  O   . HOH   Q 6 .   ? 15.85600  30.19300  26.79200  1.000 29.99580 ? 589 HOH   B O   1 
HETATM 4300 O  O   . HOH   Q 6 .   ? 7.08700   9.86700   9.78400   1.000 29.50949 ? 590 HOH   B O   1 
HETATM 4301 O  O   . HOH   Q 6 .   ? 14.28500  37.14700  35.51100  1.000 32.78042 ? 591 HOH   B O   1 
HETATM 4302 O  O   . HOH   Q 6 .   ? 1.56500   5.85600   8.85400   1.000 37.27273 ? 592 HOH   B O   1 
HETATM 4303 O  O   . HOH   Q 6 .   ? -9.04500  20.66900  9.49600   1.000 40.79173 ? 593 HOH   B O   1 
HETATM 4304 O  O   . HOH   Q 6 .   ? -2.79100  14.74800  38.25200  1.000 21.44111 ? 594 HOH   B O   1 
HETATM 4305 O  O   . HOH   Q 6 .   ? -16.89200 18.75300  20.81900  1.000 32.51970 ? 595 HOH   B O   1 
HETATM 4306 O  O   . HOH   Q 6 .   ? -15.19800 17.05500  31.18100  1.000 34.37345 ? 596 HOH   B O   1 
HETATM 4307 O  O   . HOH   Q 6 .   ? 12.97500  37.38200  39.63700  1.000 34.33924 ? 597 HOH   B O   1 
HETATM 4308 O  O   . HOH   Q 6 .   ? 8.22800   5.13900   15.60500  1.000 33.22220 ? 598 HOH   B O   1 
HETATM 4309 O  O   . HOH   Q 6 .   ? 22.70600  9.31100   29.00200  1.000 38.99255 ? 599 HOH   B O   1 
HETATM 4310 O  O   . HOH   Q 6 .   ? -18.98900 17.34400  22.90200  1.000 46.62488 ? 600 HOH   B O   1 
HETATM 4311 O  O   . HOH   Q 6 .   ? 10.31300  13.54500  12.86400  1.000 21.13835 ? 601 HOH   B O   1 
HETATM 4312 O  O   . HOH   Q 6 .   ? 4.12700   35.30300  21.07000  1.000 28.56699 ? 602 HOH   B O   1 
HETATM 4313 O  O   . HOH   Q 6 .   ? 12.22300  11.84200  33.46600  1.000 28.74800 ? 603 HOH   B O   1 
HETATM 4314 O  O   . HOH   Q 6 .   ? -2.462    7.003     45.020    1.000 34.84389 ? 604 HOH   B O   1 
HETATM 4315 O  O   . HOH   Q 6 .   ? 4.28200   33.41400  41.06900  1.000 36.63468 ? 605 HOH   B O   1 
HETATM 4316 O  O   . HOH   Q 6 .   ? -18.17600 24.27200  37.08800  1.000 39.17621 ? 606 HOH   B O   1 
HETATM 4317 O  O   . HOH   Q 6 .   ? -2.12400  31.36100  16.30000  1.000 40.27353 ? 607 HOH   B O   1 
HETATM 4318 O  O   . HOH   Q 6 .   ? 20.78800  7.52300   29.38800  1.000 31.52324 ? 608 HOH   B O   1 
HETATM 4319 O  O   . HOH   Q 6 .   ? 1.62400   32.02300  41.93000  1.000 37.62153 ? 609 HOH   B O   1 
HETATM 4320 O  O   . HOH   Q 6 .   ? -20.58000 19.41200  26.92100  1.000 52.47285 ? 610 HOH   B O   1 
HETATM 4321 O  O   . HOH   Q 6 .   ? 2.69900   16.28700  9.34000   1.000 36.58607 ? 611 HOH   B O   1 
HETATM 4322 O  O   . HOH   Q 6 .   ? 3.74600   1.84500   35.69900  1.000 31.43512 ? 612 HOH   B O   1 
HETATM 4323 O  O   . HOH   Q 6 .   ? 1.77700   24.92700  6.44300   1.000 39.12638 ? 613 HOH   B O   1 
HETATM 4324 O  O   . HOH   Q 6 .   ? -11.12400 7.31400   10.96700  1.000 33.61241 ? 614 HOH   B O   1 
HETATM 4325 O  O   . HOH   Q 6 .   ? 3.88700   32.28000  15.36000  1.000 39.51076 ? 615 HOH   B O   1 
HETATM 4326 O  O   . HOH   Q 6 .   ? -9.39100  12.24700  34.41400  1.000 36.37169 ? 616 HOH   B O   1 
HETATM 4327 O  O   . HOH   Q 6 .   ? 15.30200  31.74700  28.94000  1.000 35.53477 ? 617 HOH   B O   1 
HETATM 4328 O  O   . HOH   Q 6 .   ? 16.67300  33.79100  29.91200  1.000 41.43002 ? 618 HOH   B O   1 
HETATM 4329 O  O   . HOH   Q 6 .   ? 15.19500  4.68300   21.66000  1.000 39.00065 ? 619 HOH   B O   1 
HETATM 4330 O  O   . HOH   Q 6 .   ? -7.089    31.246    26.204    1.000 20.22233 ? 620 HOH   B O   1 
HETATM 4331 O  O   . HOH   Q 6 .   ? -1.27500  36.99900  24.93200  1.000 21.93166 ? 621 HOH   B O   1 
HETATM 4332 O  O   . HOH   Q 6 .   ? 4.04400   23.15300  6.76300   1.000 34.73610 ? 622 HOH   B O   1 
HETATM 4333 O  O   . HOH   Q 6 .   ? -1.22400  15.32400  40.30500  1.000 38.43922 ? 623 HOH   B O   1 
HETATM 4334 O  O   . HOH   Q 6 .   ? -14.31700 2.82300   22.13900  1.000 35.70752 ? 624 HOH   B O   1 
HETATM 4335 O  O   . HOH   Q 6 .   ? -15.81800 9.06800   17.89100  1.000 32.67058 ? 625 HOH   B O   1 
HETATM 4336 O  O   . HOH   Q 6 .   ? -18.44200 12.49200  22.84800  1.000 33.68181 ? 626 HOH   B O   1 
HETATM 4337 O  O   . HOH   Q 6 .   ? 10.17900  38.57700  27.11900  1.000 23.39400 ? 627 HOH   B O   1 
HETATM 4338 O  O   . HOH   Q 6 .   ? 22.58900  22.59700  30.14500  1.000 36.78133 ? 628 HOH   B O   1 
HETATM 4339 O  O   . HOH   Q 6 .   ? 5.58000   34.60500  16.64800  1.000 41.44500 ? 629 HOH   B O   1 
HETATM 4340 O  O   . HOH   Q 6 .   ? 23.84000  22.01400  32.63200  1.000 41.73350 ? 630 HOH   B O   1 
HETATM 4341 O  O   . HOH   Q 6 .   ? 9.88600   4.73300   17.84700  1.000 44.81177 ? 631 HOH   B O   1 
HETATM 4342 O  O   . HOH   Q 6 .   ? -18.41300 12.75100  12.19700  1.000 24.44722 ? 632 HOH   B O   1 
HETATM 4343 O  O   . HOH   Q 6 .   ? 7.62000   12.49000  8.41100   1.000 30.79740 ? 633 HOH   B O   1 
HETATM 4344 O  O   . HOH   Q 6 .   ? 8.11800   7.10200   9.90300   1.000 40.12464 ? 634 HOH   B O   1 
HETATM 4345 O  O   . HOH   Q 6 .   ? 21.83300  22.06100  25.86600  1.000 36.05066 ? 635 HOH   B O   1 
HETATM 4346 O  O   . HOH   Q 6 .   ? -13.45700 8.03000   16.47900  1.000 27.44082 ? 636 HOH   B O   1 
HETATM 4347 O  O   . HOH   Q 6 .   ? 8.68100   37.09400  50.48900  1.000 33.76447 ? 637 HOH   B O   1 
HETATM 4348 O  O   . HOH   Q 6 .   ? 5.94200   1.36100   35.86600  1.000 37.35484 ? 638 HOH   B O   1 
HETATM 4349 O  O   . HOH   Q 6 .   ? -13.98000 6.51500   14.25700  1.000 37.17714 ? 639 HOH   B O   1 
HETATM 4350 O  O   . HOH   Q 6 .   ? -14.874   19.842    8.840     1.000 40.18303 ? 640 HOH   B O   1 
HETATM 4351 O  O   . HOH   Q 6 .   ? 22.16100  18.56200  26.86800  1.000 37.20604 ? 641 HOH   B O   1 
HETATM 4352 O  O   . HOH   Q 6 .   ? -18.46700 10.18000  21.19300  1.000 35.68155 ? 642 HOH   B O   1 
HETATM 4353 O  O   . HOH   Q 6 .   ? -0.107    -0.507    33.731    1.000 35.91542 ? 643 HOH   B O   1 
HETATM 4354 O  O   . HOH   Q 6 .   ? -2.19300  0.61600   40.42300  1.000 37.67788 ? 644 HOH   B O   1 
HETATM 4355 O  O   . HOH   Q 6 .   ? -19.45100 14.39300  16.17700  1.000 35.32194 ? 645 HOH   B O   1 
HETATM 4356 O  O   . HOH   Q 6 .   ? 13.36100  17.11200  14.14100  1.000 39.27564 ? 646 HOH   B O   1 
HETATM 4357 O  O   . HOH   Q 6 .   ? 21.068    19.549    41.524    1.000 39.34485 ? 647 HOH   B O   1 
HETATM 4358 O  O   . HOH   Q 6 .   ? 4.332     40.837    35.921    1.000 34.22575 ? 648 HOH   B O   1 
HETATM 4359 O  O   . HOH   Q 6 .   ? 21.28600  34.25000  32.92300  1.000 45.48597 ? 649 HOH   B O   1 
HETATM 4360 O  O   . HOH   Q 6 .   ? 7.32300   14.02700  40.95900  1.000 25.51596 ? 650 HOH   B O   1 
HETATM 4361 O  O   . HOH   Q 6 .   ? 4.85700   12.54500  42.17300  1.000 34.76120 ? 651 HOH   B O   1 
HETATM 4362 O  O   . HOH   Q 6 .   ? -8.828    13.087    4.197     1.000 27.72766 ? 652 HOH   B O   1 
HETATM 4363 O  O   . HOH   Q 6 .   ? 20.49700  10.02100  19.62700  1.000 41.83711 ? 653 HOH   B O   1 
HETATM 4364 O  O   . HOH   Q 6 .   ? 18.59600  28.92200  36.42500  1.000 19.73620 ? 654 HOH   B O   1 
HETATM 4365 O  O   . HOH   Q 6 .   ? -12.36400 5.97500   31.08800  1.000 32.07246 ? 655 HOH   B O   1 
HETATM 4366 O  O   . HOH   Q 6 .   ? 14.73200  15.10700  37.81200  1.000 35.99038 ? 656 HOH   B O   1 
HETATM 4367 O  O   . HOH   Q 6 .   ? -7.656    6.763     4.437     1.000 43.28955 ? 657 HOH   B O   1 
HETATM 4368 O  O   . HOH   Q 6 .   ? 6.746     -2.687    28.993    1.000 23.93803 ? 658 HOH   B O   1 
HETATM 4369 O  O   . HOH   Q 6 .   ? 11.92500  33.31100  17.21500  1.000 37.83880 ? 659 HOH   B O   1 
HETATM 4370 O  O   . HOH   Q 6 .   ? -3.68400  0.48500   33.38700  1.000 35.99821 ? 660 HOH   B O   1 
HETATM 4371 O  O   . HOH   Q 6 .   ? 14.28000  5.11100   19.35600  1.000 37.94257 ? 661 HOH   B O   1 
HETATM 4372 O  O   . HOH   Q 6 .   ? 2.80700   4.27000   9.33000   1.000 46.62765 ? 662 HOH   B O   1 
HETATM 4373 O  O   . HOH   Q 6 .   ? -11.30400 6.23900   13.68000  1.000 39.40863 ? 663 HOH   B O   1 
HETATM 4374 O  O   . HOH   Q 6 .   ? 16.91300  16.81700  42.28700  1.000 36.12303 ? 664 HOH   B O   1 
HETATM 4375 O  O   . HOH   Q 6 .   ? 16.35900  11.09700  14.87600  1.000 43.59531 ? 665 HOH   B O   1 
HETATM 4376 O  O   . HOH   Q 6 .   ? 12.93600  13.85800  13.37100  1.000 33.89733 ? 666 HOH   B O   1 
HETATM 4377 O  O   . HOH   Q 6 .   ? 9.06600   14.79900  9.02500   1.000 30.29892 ? 667 HOH   B O   1 
HETATM 4378 O  O   . HOH   Q 6 .   ? -14.58200 4.20800   25.82700  1.000 37.23070 ? 668 HOH   B O   1 
HETATM 4379 O  O   . HOH   Q 6 .   ? 8.11100   2.85800   18.71900  1.000 40.32894 ? 669 HOH   B O   1 
HETATM 4380 O  O   . HOH   Q 6 .   ? 18.03400  7.03800   21.24000  1.000 36.33625 ? 670 HOH   B O   1 
HETATM 4381 O  O   . HOH   Q 6 .   ? 20.42300  19.54500  25.42000  1.000 28.43575 ? 671 HOH   B O   1 
HETATM 4382 O  O   . HOH   Q 6 .   ? -10.040   10.708    3.962     1.000 31.03790 ? 672 HOH   B O   1 
HETATM 4383 O  O   . HOH   Q 6 .   ? 14.60700  33.12900  18.40800  1.000 38.17383 ? 673 HOH   B O   1 
HETATM 4384 O  O   . HOH   Q 6 .   ? -19.01000 14.68400  21.25400  1.000 37.44914 ? 674 HOH   B O   1 
HETATM 4385 O  O   . HOH   Q 6 .   ? -5.88800  3.03200   8.44000   1.000 43.41132 ? 675 HOH   B O   1 
HETATM 4386 O  O   . HOH   Q 6 .   ? 12.20300  13.66900  41.79300  1.000 35.36027 ? 676 HOH   B O   1 
HETATM 4387 O  O   . HOH   Q 6 .   ? 7.00300   3.17100   41.80800  1.000 42.00562 ? 677 HOH   B O   1 
HETATM 4388 O  O   . HOH   Q 6 .   ? -14.73600 7.01000   22.70300  1.000 34.87476 ? 678 HOH   B O   1 
HETATM 4389 O  O   . HOH   Q 6 .   ? -8.089    9.087     3.018     1.000 37.70696 ? 679 HOH   B O   1 
HETATM 4390 O  O   . HOH   Q 6 .   ? 2.99200   33.06700  13.17200  1.000 47.58699 ? 680 HOH   B O   1 
HETATM 4391 O  O   . HOH   Q 6 .   ? 5.35400   10.52100  43.12100  1.000 36.35186 ? 681 HOH   B O   1 
HETATM 4392 O  O   . HOH   Q 6 .   ? -13.37900 6.25200   18.55600  1.000 38.34917 ? 682 HOH   B O   1 
HETATM 4393 O  O   . HOH   Q 6 .   ? 7.38800   -2.03900  35.77400  1.000 47.98690 ? 683 HOH   B O   1 
HETATM 4394 O  O   . HOH   Q 6 .   ? -16.13600 6.25700   26.89400  1.000 38.18681 ? 684 HOH   B O   1 
HETATM 4395 O  O   . HOH   Q 6 .   ? -17.21100 6.95000   24.50200  1.000 48.84156 ? 685 HOH   B O   1 
# 
