data_9JU4
# 
_entry.id   9JU4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JU4         pdb_00009ju4 10.2210/pdb9ju4/pdb 
WWPDB D_1300052253 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JU4 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              stanaka1@kpu.ac.jp 
_pdbx_contact_author.name_first         Shun-ichi 
_pdbx_contact_author.name_last          Tanaka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4270-0374 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanaka, S.-i.' 1 0000-0003-4270-0374 
'Amesaka, H.'   2 0000-0003-1688-7796 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70018 
_citation.page_last                 e70018 
_citation.title                     
'Heat-sterilizable antibody mimics designed on the cold shock protein scaffold from hyperthermophile Thermotoga maritima.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70018 
_citation.pdbx_database_id_PubMed   39724358 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Amesaka, H.'   1  0000-0003-1688-7796 
primary 'Tachibana, M.' 2  ?                   
primary 'Hara, M.'      3  ?                   
primary 'Toya, S.'      4  ?                   
primary 'Nakagawa, H.'  5  ?                   
primary 'Matsumura, H.' 6  0000-0003-0361-3796 
primary 'Hirata, A.'    7  0000-0003-3928-5018 
primary 'Fujihashi, M.' 8  0000-0002-6882-9697 
primary 'Takano, K.'    9  0000-0002-7548-7314 
primary 'Tanaka, S.I.'  10 0000-0003-4270-0374 
# 
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 'Alpha/beta hydrolase fold-3 domain protein'                          34338.973 1   ? ? ? ? 
2 polymer     man 'The Thermotoga maritima cold shock protein mutant binding to AacEst' 7377.190  1   ? ? ? ? 
3 non-polymer syn 'phenylmethanesulfonic acid'                                          172.202   1   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                               106.120   1   ? ? ? ? 
5 non-polymer syn GLYCEROL                                                              92.094    1   ? ? ? ? 
6 water       nat water                                                                 18.015    176 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MPLDPVIQQVLDQLNRMPAPDYKHLSAQQFRSQQSLFPPVKKEPVAEVREFDMDLPGRTLKVRMYRPEGVEPPYPALVYY
HGGGWVVGDLETHDPVCRVLAKDGRAVVFSVDYRLAPEHKFPAAVEDAYDALQWIAERAADFHLDPARIAVGGDSAGGNL
AAVTSILAKERGGPAIAFQLLIYPSTGYDPAHPPASIEENAEGYLLTGGMMLWFRDQYLNSLEELTHPWFSPVLYPDLSG
LPPAYIATAQYDPLRDVGKLYAEALNKAGVKVEIENFEDLIHGFAQFYSLSPGATKALVRIAEKLRDALA
;
;MPLDPVIQQVLDQLNRMPAPDYKHLSAQQFRSQQSLFPPVKKEPVAEVREFDMDLPGRTLKVRMYRPEGVEPPYPALVYY
HGGGWVVGDLETHDPVCRVLAKDGRAVVFSVDYRLAPEHKFPAAVEDAYDALQWIAERAADFHLDPARIAVGGDSAGGNL
AAVTSILAKERGGPAIAFQLLIYPSTGYDPAHPPASIEENAEGYLLTGGMMLWFRDQYLNSLEELTHPWFSPVLYPDLSG
LPPAYIATAQYDPLRDVGKLYAEALNKAGVKVEIENFEDLIHGFAQFYSLSPGATKALVRIAEKLRDALA
;
A ? 
2 'polypeptide(L)' no no RGKVKWFHDYYGYGFITKDEGGDVFVNADAIDMEGFKTLKEGQVVEFEIDSTVANAPQAAHVKVVE 
RGKVKWFHDYYGYGFITKDEGGDVFVNADAIDMEGFKTLKEGQVVEFEIDSTVANAPQAAHVKVVE B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'phenylmethanesulfonic acid' PMS 
4 'DI(HYDROXYETHYL)ETHER'      PEG 
5 GLYCEROL                     GOL 
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   PRO n 
1 3   LEU n 
1 4   ASP n 
1 5   PRO n 
1 6   VAL n 
1 7   ILE n 
1 8   GLN n 
1 9   GLN n 
1 10  VAL n 
1 11  LEU n 
1 12  ASP n 
1 13  GLN n 
1 14  LEU n 
1 15  ASN n 
1 16  ARG n 
1 17  MET n 
1 18  PRO n 
1 19  ALA n 
1 20  PRO n 
1 21  ASP n 
1 22  TYR n 
1 23  LYS n 
1 24  HIS n 
1 25  LEU n 
1 26  SER n 
1 27  ALA n 
1 28  GLN n 
1 29  GLN n 
1 30  PHE n 
1 31  ARG n 
1 32  SER n 
1 33  GLN n 
1 34  GLN n 
1 35  SER n 
1 36  LEU n 
1 37  PHE n 
1 38  PRO n 
1 39  PRO n 
1 40  VAL n 
1 41  LYS n 
1 42  LYS n 
1 43  GLU n 
1 44  PRO n 
1 45  VAL n 
1 46  ALA n 
1 47  GLU n 
1 48  VAL n 
1 49  ARG n 
1 50  GLU n 
1 51  PHE n 
1 52  ASP n 
1 53  MET n 
1 54  ASP n 
1 55  LEU n 
1 56  PRO n 
1 57  GLY n 
1 58  ARG n 
1 59  THR n 
1 60  LEU n 
1 61  LYS n 
1 62  VAL n 
1 63  ARG n 
1 64  MET n 
1 65  TYR n 
1 66  ARG n 
1 67  PRO n 
1 68  GLU n 
1 69  GLY n 
1 70  VAL n 
1 71  GLU n 
1 72  PRO n 
1 73  PRO n 
1 74  TYR n 
1 75  PRO n 
1 76  ALA n 
1 77  LEU n 
1 78  VAL n 
1 79  TYR n 
1 80  TYR n 
1 81  HIS n 
1 82  GLY n 
1 83  GLY n 
1 84  GLY n 
1 85  TRP n 
1 86  VAL n 
1 87  VAL n 
1 88  GLY n 
1 89  ASP n 
1 90  LEU n 
1 91  GLU n 
1 92  THR n 
1 93  HIS n 
1 94  ASP n 
1 95  PRO n 
1 96  VAL n 
1 97  CYS n 
1 98  ARG n 
1 99  VAL n 
1 100 LEU n 
1 101 ALA n 
1 102 LYS n 
1 103 ASP n 
1 104 GLY n 
1 105 ARG n 
1 106 ALA n 
1 107 VAL n 
1 108 VAL n 
1 109 PHE n 
1 110 SER n 
1 111 VAL n 
1 112 ASP n 
1 113 TYR n 
1 114 ARG n 
1 115 LEU n 
1 116 ALA n 
1 117 PRO n 
1 118 GLU n 
1 119 HIS n 
1 120 LYS n 
1 121 PHE n 
1 122 PRO n 
1 123 ALA n 
1 124 ALA n 
1 125 VAL n 
1 126 GLU n 
1 127 ASP n 
1 128 ALA n 
1 129 TYR n 
1 130 ASP n 
1 131 ALA n 
1 132 LEU n 
1 133 GLN n 
1 134 TRP n 
1 135 ILE n 
1 136 ALA n 
1 137 GLU n 
1 138 ARG n 
1 139 ALA n 
1 140 ALA n 
1 141 ASP n 
1 142 PHE n 
1 143 HIS n 
1 144 LEU n 
1 145 ASP n 
1 146 PRO n 
1 147 ALA n 
1 148 ARG n 
1 149 ILE n 
1 150 ALA n 
1 151 VAL n 
1 152 GLY n 
1 153 GLY n 
1 154 ASP n 
1 155 SER n 
1 156 ALA n 
1 157 GLY n 
1 158 GLY n 
1 159 ASN n 
1 160 LEU n 
1 161 ALA n 
1 162 ALA n 
1 163 VAL n 
1 164 THR n 
1 165 SER n 
1 166 ILE n 
1 167 LEU n 
1 168 ALA n 
1 169 LYS n 
1 170 GLU n 
1 171 ARG n 
1 172 GLY n 
1 173 GLY n 
1 174 PRO n 
1 175 ALA n 
1 176 ILE n 
1 177 ALA n 
1 178 PHE n 
1 179 GLN n 
1 180 LEU n 
1 181 LEU n 
1 182 ILE n 
1 183 TYR n 
1 184 PRO n 
1 185 SER n 
1 186 THR n 
1 187 GLY n 
1 188 TYR n 
1 189 ASP n 
1 190 PRO n 
1 191 ALA n 
1 192 HIS n 
1 193 PRO n 
1 194 PRO n 
1 195 ALA n 
1 196 SER n 
1 197 ILE n 
1 198 GLU n 
1 199 GLU n 
1 200 ASN n 
1 201 ALA n 
1 202 GLU n 
1 203 GLY n 
1 204 TYR n 
1 205 LEU n 
1 206 LEU n 
1 207 THR n 
1 208 GLY n 
1 209 GLY n 
1 210 MET n 
1 211 MET n 
1 212 LEU n 
1 213 TRP n 
1 214 PHE n 
1 215 ARG n 
1 216 ASP n 
1 217 GLN n 
1 218 TYR n 
1 219 LEU n 
1 220 ASN n 
1 221 SER n 
1 222 LEU n 
1 223 GLU n 
1 224 GLU n 
1 225 LEU n 
1 226 THR n 
1 227 HIS n 
1 228 PRO n 
1 229 TRP n 
1 230 PHE n 
1 231 SER n 
1 232 PRO n 
1 233 VAL n 
1 234 LEU n 
1 235 TYR n 
1 236 PRO n 
1 237 ASP n 
1 238 LEU n 
1 239 SER n 
1 240 GLY n 
1 241 LEU n 
1 242 PRO n 
1 243 PRO n 
1 244 ALA n 
1 245 TYR n 
1 246 ILE n 
1 247 ALA n 
1 248 THR n 
1 249 ALA n 
1 250 GLN n 
1 251 TYR n 
1 252 ASP n 
1 253 PRO n 
1 254 LEU n 
1 255 ARG n 
1 256 ASP n 
1 257 VAL n 
1 258 GLY n 
1 259 LYS n 
1 260 LEU n 
1 261 TYR n 
1 262 ALA n 
1 263 GLU n 
1 264 ALA n 
1 265 LEU n 
1 266 ASN n 
1 267 LYS n 
1 268 ALA n 
1 269 GLY n 
1 270 VAL n 
1 271 LYS n 
1 272 VAL n 
1 273 GLU n 
1 274 ILE n 
1 275 GLU n 
1 276 ASN n 
1 277 PHE n 
1 278 GLU n 
1 279 ASP n 
1 280 LEU n 
1 281 ILE n 
1 282 HIS n 
1 283 GLY n 
1 284 PHE n 
1 285 ALA n 
1 286 GLN n 
1 287 PHE n 
1 288 TYR n 
1 289 SER n 
1 290 LEU n 
1 291 SER n 
1 292 PRO n 
1 293 GLY n 
1 294 ALA n 
1 295 THR n 
1 296 LYS n 
1 297 ALA n 
1 298 LEU n 
1 299 VAL n 
1 300 ARG n 
1 301 ILE n 
1 302 ALA n 
1 303 GLU n 
1 304 LYS n 
1 305 LEU n 
1 306 ARG n 
1 307 ASP n 
1 308 ALA n 
1 309 LEU n 
1 310 ALA n 
2 1   ARG n 
2 2   GLY n 
2 3   LYS n 
2 4   VAL n 
2 5   LYS n 
2 6   TRP n 
2 7   PHE n 
2 8   HIS n 
2 9   ASP n 
2 10  TYR n 
2 11  TYR n 
2 12  GLY n 
2 13  TYR n 
2 14  GLY n 
2 15  PHE n 
2 16  ILE n 
2 17  THR n 
2 18  LYS n 
2 19  ASP n 
2 20  GLU n 
2 21  GLY n 
2 22  GLY n 
2 23  ASP n 
2 24  VAL n 
2 25  PHE n 
2 26  VAL n 
2 27  ASN n 
2 28  ALA n 
2 29  ASP n 
2 30  ALA n 
2 31  ILE n 
2 32  ASP n 
2 33  MET n 
2 34  GLU n 
2 35  GLY n 
2 36  PHE n 
2 37  LYS n 
2 38  THR n 
2 39  LEU n 
2 40  LYS n 
2 41  GLU n 
2 42  GLY n 
2 43  GLN n 
2 44  VAL n 
2 45  VAL n 
2 46  GLU n 
2 47  PHE n 
2 48  GLU n 
2 49  ILE n 
2 50  ASP n 
2 51  SER n 
2 52  THR n 
2 53  VAL n 
2 54  ALA n 
2 55  ASN n 
2 56  ALA n 
2 57  PRO n 
2 58  GLN n 
2 59  ALA n 
2 60  ALA n 
2 61  HIS n 
2 62  VAL n 
2 63  LYS n 
2 64  VAL n 
2 65  VAL n 
2 66  GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 310 ? ? Aaci_2875 ? ? ? ? ? ? 'Alicyclobacillus acidocaldarius' 405212 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 66  ? ? ?         ? ? ? ? ? ? 'Thermotoga maritima'             2336   ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                      ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                     ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                   ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'              ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                     ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                    ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'              ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                      ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                     'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                    ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                        ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                   ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                      ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                       ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                   ?                               'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'      ?                               'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE                ?                               'C9 H11 N O2'    165.189 
PMS non-polymer         . 'phenylmethanesulfonic acid' ?                               'C7 H8 O3 S'     172.202 
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 
# 
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   1   1   MET MET A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  MET 53  53  53  MET MET A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  MET 64  64  64  MET MET A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  TRP 85  85  85  TRP TRP A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  CYS 97  97  97  CYS CYS A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 GLN 179 179 179 GLN GLN A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 TYR 183 183 183 TYR TYR A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 MET 211 211 211 MET MET A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 TRP 213 213 213 TRP TRP A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 HIS 227 227 227 HIS HIS A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 TRP 229 229 229 TRP TRP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 LYS 271 271 271 LYS LYS A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 HIS 282 282 282 HIS HIS A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 PHE 287 287 287 PHE PHE A . n 
A 1 288 TYR 288 288 288 TYR TYR A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
B 2 1   ARG 1   2   2   ARG ARG B . n 
B 2 2   GLY 2   3   3   GLY GLY B . n 
B 2 3   LYS 3   4   4   LYS LYS B . n 
B 2 4   VAL 4   5   5   VAL VAL B . n 
B 2 5   LYS 5   6   6   LYS LYS B . n 
B 2 6   TRP 6   7   7   TRP TRP B . n 
B 2 7   PHE 7   8   8   PHE PHE B . n 
B 2 8   HIS 8   9   9   HIS HIS B . n 
B 2 9   ASP 9   10  10  ASP ASP B . n 
B 2 10  TYR 10  11  11  TYR TYR B . n 
B 2 11  TYR 11  12  12  TYR TYR B . n 
B 2 12  GLY 12  13  13  GLY GLY B . n 
B 2 13  TYR 13  14  14  TYR TYR B . n 
B 2 14  GLY 14  15  15  GLY GLY B . n 
B 2 15  PHE 15  16  16  PHE PHE B . n 
B 2 16  ILE 16  17  17  ILE ILE B . n 
B 2 17  THR 17  18  18  THR THR B . n 
B 2 18  LYS 18  19  ?   ?   ?   B . n 
B 2 19  ASP 19  20  ?   ?   ?   B . n 
B 2 20  GLU 20  21  ?   ?   ?   B . n 
B 2 21  GLY 21  22  ?   ?   ?   B . n 
B 2 22  GLY 22  23  ?   ?   ?   B . n 
B 2 23  ASP 23  24  24  ASP ASP B . n 
B 2 24  VAL 24  25  25  VAL VAL B . n 
B 2 25  PHE 25  26  26  PHE PHE B . n 
B 2 26  VAL 26  27  27  VAL VAL B . n 
B 2 27  ASN 27  28  28  ASN ASN B . n 
B 2 28  ALA 28  29  29  ALA ALA B . n 
B 2 29  ASP 29  30  30  ASP ASP B . n 
B 2 30  ALA 30  31  31  ALA ALA B . n 
B 2 31  ILE 31  32  32  ILE ILE B . n 
B 2 32  ASP 32  33  33  ASP ASP B . n 
B 2 33  MET 33  34  ?   ?   ?   B . n 
B 2 34  GLU 34  35  ?   ?   ?   B . n 
B 2 35  GLY 35  36  ?   ?   ?   B . n 
B 2 36  PHE 36  37  ?   ?   ?   B . n 
B 2 37  LYS 37  38  38  LYS LYS B . n 
B 2 38  THR 38  39  39  THR THR B . n 
B 2 39  LEU 39  40  40  LEU LEU B . n 
B 2 40  LYS 40  41  41  LYS LYS B . n 
B 2 41  GLU 41  42  42  GLU GLU B . n 
B 2 42  GLY 42  43  43  GLY GLY B . n 
B 2 43  GLN 43  44  44  GLN GLN B . n 
B 2 44  VAL 44  45  45  VAL VAL B . n 
B 2 45  VAL 45  46  46  VAL VAL B . n 
B 2 46  GLU 46  47  47  GLU GLU B . n 
B 2 47  PHE 47  48  48  PHE PHE B . n 
B 2 48  GLU 48  49  49  GLU GLU B . n 
B 2 49  ILE 49  50  50  ILE ILE B . n 
B 2 50  ASP 50  51  51  ASP ASP B . n 
B 2 51  SER 51  52  52  SER SER B . n 
B 2 52  THR 52  53  53  THR THR B . n 
B 2 53  VAL 53  54  ?   ?   ?   B . n 
B 2 54  ALA 54  55  ?   ?   ?   B . n 
B 2 55  ASN 55  56  ?   ?   ?   B . n 
B 2 56  ALA 56  57  57  ALA ALA B . n 
B 2 57  PRO 57  58  58  PRO PRO B . n 
B 2 58  GLN 58  59  59  GLN GLN B . n 
B 2 59  ALA 59  60  60  ALA ALA B . n 
B 2 60  ALA 60  61  61  ALA ALA B . n 
B 2 61  HIS 61  62  62  HIS HIS B . n 
B 2 62  VAL 62  63  63  VAL VAL B . n 
B 2 63  LYS 63  64  64  LYS LYS B . n 
B 2 64  VAL 64  65  ?   ?   ?   B . n 
B 2 65  VAL 65  66  ?   ?   ?   B . n 
B 2 66  GLU 66  67  ?   ?   ?   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 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PEG ? ? PEG ? ? 'SUBJECT OF INVESTIGATION' ? 
3 PMS ? ? PMS ? ? '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 3 PMS 1   401 1   PMS PMS A . 
D 4 PEG 1   402 1   PEG PEG A . 
E 5 GOL 1   403 1   GOL GOL A . 
F 6 HOH 1   501 171 HOH HOH A . 
F 6 HOH 2   502 153 HOH HOH A . 
F 6 HOH 3   503 122 HOH HOH A . 
F 6 HOH 4   504 140 HOH HOH A . 
F 6 HOH 5   505 111 HOH HOH A . 
F 6 HOH 6   506 160 HOH HOH A . 
F 6 HOH 7   507 74  HOH HOH A . 
F 6 HOH 8   508 161 HOH HOH A . 
F 6 HOH 9   509 165 HOH HOH A . 
F 6 HOH 10  510 119 HOH HOH A . 
F 6 HOH 11  511 72  HOH HOH A . 
F 6 HOH 12  512 112 HOH HOH A . 
F 6 HOH 13  513 51  HOH HOH A . 
F 6 HOH 14  514 98  HOH HOH A . 
F 6 HOH 15  515 9   HOH HOH A . 
F 6 HOH 16  516 114 HOH HOH A . 
F 6 HOH 17  517 123 HOH HOH A . 
F 6 HOH 18  518 24  HOH HOH A . 
F 6 HOH 19  519 121 HOH HOH A . 
F 6 HOH 20  520 30  HOH HOH A . 
F 6 HOH 21  521 134 HOH HOH A . 
F 6 HOH 22  522 154 HOH HOH A . 
F 6 HOH 23  523 35  HOH HOH A . 
F 6 HOH 24  524 151 HOH HOH A . 
F 6 HOH 25  525 82  HOH HOH A . 
F 6 HOH 26  526 18  HOH HOH A . 
F 6 HOH 27  527 94  HOH HOH A . 
F 6 HOH 28  528 22  HOH HOH A . 
F 6 HOH 29  529 70  HOH HOH A . 
F 6 HOH 30  530 79  HOH HOH A . 
F 6 HOH 31  531 39  HOH HOH A . 
F 6 HOH 32  532 100 HOH HOH A . 
F 6 HOH 33  533 13  HOH HOH A . 
F 6 HOH 34  534 10  HOH HOH A . 
F 6 HOH 35  535 73  HOH HOH A . 
F 6 HOH 36  536 26  HOH HOH A . 
F 6 HOH 37  537 7   HOH HOH A . 
F 6 HOH 38  538 90  HOH HOH A . 
F 6 HOH 39  539 36  HOH HOH A . 
F 6 HOH 40  540 48  HOH HOH A . 
F 6 HOH 41  541 46  HOH HOH A . 
F 6 HOH 42  542 65  HOH HOH A . 
F 6 HOH 43  543 52  HOH HOH A . 
F 6 HOH 44  544 60  HOH HOH A . 
F 6 HOH 45  545 31  HOH HOH A . 
F 6 HOH 46  546 174 HOH HOH A . 
F 6 HOH 47  547 130 HOH HOH A . 
F 6 HOH 48  548 163 HOH HOH A . 
F 6 HOH 49  549 2   HOH HOH A . 
F 6 HOH 50  550 61  HOH HOH A . 
F 6 HOH 51  551 77  HOH HOH A . 
F 6 HOH 52  552 11  HOH HOH A . 
F 6 HOH 53  553 81  HOH HOH A . 
F 6 HOH 54  554 20  HOH HOH A . 
F 6 HOH 55  555 5   HOH HOH A . 
F 6 HOH 56  556 28  HOH HOH A . 
F 6 HOH 57  557 91  HOH HOH A . 
F 6 HOH 58  558 47  HOH HOH A . 
F 6 HOH 59  559 38  HOH HOH A . 
F 6 HOH 60  560 99  HOH HOH A . 
F 6 HOH 61  561 102 HOH HOH A . 
F 6 HOH 62  562 50  HOH HOH A . 
F 6 HOH 63  563 69  HOH HOH A . 
F 6 HOH 64  564 8   HOH HOH A . 
F 6 HOH 65  565 173 HOH HOH A . 
F 6 HOH 66  566 6   HOH HOH A . 
F 6 HOH 67  567 71  HOH HOH A . 
F 6 HOH 68  568 3   HOH HOH A . 
F 6 HOH 69  569 55  HOH HOH A . 
F 6 HOH 70  570 88  HOH HOH A . 
F 6 HOH 71  571 1   HOH HOH A . 
F 6 HOH 72  572 107 HOH HOH A . 
F 6 HOH 73  573 103 HOH HOH A . 
F 6 HOH 74  574 128 HOH HOH A . 
F 6 HOH 75  575 56  HOH HOH A . 
F 6 HOH 76  576 17  HOH HOH A . 
F 6 HOH 77  577 58  HOH HOH A . 
F 6 HOH 78  578 78  HOH HOH A . 
F 6 HOH 79  579 19  HOH HOH A . 
F 6 HOH 80  580 162 HOH HOH A . 
F 6 HOH 81  581 86  HOH HOH A . 
F 6 HOH 82  582 43  HOH HOH A . 
F 6 HOH 83  583 40  HOH HOH A . 
F 6 HOH 84  584 44  HOH HOH A . 
F 6 HOH 85  585 92  HOH HOH A . 
F 6 HOH 86  586 4   HOH HOH A . 
F 6 HOH 87  587 16  HOH HOH A . 
F 6 HOH 88  588 12  HOH HOH A . 
F 6 HOH 89  589 67  HOH HOH A . 
F 6 HOH 90  590 142 HOH HOH A . 
F 6 HOH 91  591 95  HOH HOH A . 
F 6 HOH 92  592 131 HOH HOH A . 
F 6 HOH 93  593 29  HOH HOH A . 
F 6 HOH 94  594 66  HOH HOH A . 
F 6 HOH 95  595 85  HOH HOH A . 
F 6 HOH 96  596 15  HOH HOH A . 
F 6 HOH 97  597 75  HOH HOH A . 
F 6 HOH 98  598 49  HOH HOH A . 
F 6 HOH 99  599 129 HOH HOH A . 
F 6 HOH 100 600 59  HOH HOH A . 
F 6 HOH 101 601 115 HOH HOH A . 
F 6 HOH 102 602 138 HOH HOH A . 
F 6 HOH 103 603 104 HOH HOH A . 
F 6 HOH 104 604 152 HOH HOH A . 
F 6 HOH 105 605 101 HOH HOH A . 
F 6 HOH 106 606 132 HOH HOH A . 
F 6 HOH 107 607 37  HOH HOH A . 
F 6 HOH 108 608 42  HOH HOH A . 
F 6 HOH 109 609 57  HOH HOH A . 
F 6 HOH 110 610 144 HOH HOH A . 
F 6 HOH 111 611 135 HOH HOH A . 
F 6 HOH 112 612 124 HOH HOH A . 
F 6 HOH 113 613 87  HOH HOH A . 
F 6 HOH 114 614 27  HOH HOH A . 
F 6 HOH 115 615 136 HOH HOH A . 
F 6 HOH 116 616 113 HOH HOH A . 
F 6 HOH 117 617 63  HOH HOH A . 
F 6 HOH 118 618 62  HOH HOH A . 
F 6 HOH 119 619 64  HOH HOH A . 
F 6 HOH 120 620 54  HOH HOH A . 
F 6 HOH 121 621 45  HOH HOH A . 
F 6 HOH 122 622 21  HOH HOH A . 
F 6 HOH 123 623 32  HOH HOH A . 
F 6 HOH 124 624 167 HOH HOH A . 
F 6 HOH 125 625 120 HOH HOH A . 
F 6 HOH 126 626 105 HOH HOH A . 
F 6 HOH 127 627 68  HOH HOH A . 
F 6 HOH 128 628 150 HOH HOH A . 
F 6 HOH 129 629 159 HOH HOH A . 
F 6 HOH 130 630 41  HOH HOH A . 
F 6 HOH 131 631 108 HOH HOH A . 
F 6 HOH 132 632 109 HOH HOH A . 
F 6 HOH 133 633 141 HOH HOH A . 
F 6 HOH 134 634 80  HOH HOH A . 
F 6 HOH 135 635 133 HOH HOH A . 
F 6 HOH 136 636 14  HOH HOH A . 
F 6 HOH 137 637 117 HOH HOH A . 
F 6 HOH 138 638 118 HOH HOH A . 
F 6 HOH 139 639 164 HOH HOH A . 
F 6 HOH 140 640 149 HOH HOH A . 
F 6 HOH 141 641 127 HOH HOH A . 
F 6 HOH 142 642 116 HOH HOH A . 
F 6 HOH 143 643 145 HOH HOH A . 
F 6 HOH 144 644 23  HOH HOH A . 
F 6 HOH 145 645 143 HOH HOH A . 
F 6 HOH 146 646 170 HOH HOH A . 
F 6 HOH 147 647 97  HOH HOH A . 
F 6 HOH 148 648 110 HOH HOH A . 
F 6 HOH 149 649 106 HOH HOH A . 
F 6 HOH 150 650 125 HOH HOH A . 
F 6 HOH 151 651 168 HOH HOH A . 
F 6 HOH 152 652 148 HOH HOH A . 
F 6 HOH 153 653 172 HOH HOH A . 
F 6 HOH 154 654 25  HOH HOH A . 
F 6 HOH 155 655 137 HOH HOH A . 
F 6 HOH 156 656 166 HOH HOH A . 
F 6 HOH 157 657 157 HOH HOH A . 
F 6 HOH 158 658 84  HOH HOH A . 
F 6 HOH 159 659 76  HOH HOH A . 
F 6 HOH 160 660 158 HOH HOH A . 
F 6 HOH 161 661 156 HOH HOH A . 
F 6 HOH 162 662 93  HOH HOH A . 
F 6 HOH 163 663 83  HOH HOH A . 
F 6 HOH 164 664 155 HOH HOH A . 
F 6 HOH 165 665 34  HOH HOH A . 
F 6 HOH 166 666 96  HOH HOH A . 
F 6 HOH 167 667 146 HOH HOH A . 
F 6 HOH 168 668 139 HOH HOH A . 
F 6 HOH 169 669 176 HOH HOH A . 
F 6 HOH 170 670 33  HOH HOH A . 
F 6 HOH 171 671 126 HOH HOH A . 
F 6 HOH 172 672 89  HOH HOH A . 
F 6 HOH 173 673 175 HOH HOH A . 
F 6 HOH 174 674 147 HOH HOH A . 
F 6 HOH 175 675 169 HOH HOH A . 
F 6 HOH 176 676 53  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.17.1_3660: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.99 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JU4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.820 
_cell.length_a_esd                 ? 
_cell.length_b                     46.650 
_cell.length_b_esd                 ? 
_cell.length_c                     101.260 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9JU4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9JU4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.59 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.43 
_exptl_crystal.description                  'Needle-like crystals' 
_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              5.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M sodium citrate, pH 5.0, and 20% (W/V) PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 EIGER 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         2024-07-20 
_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   1.0 
_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                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JU4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               46.65 
_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                                     28793 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.38 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.13 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.52 
_reflns_shell.d_res_low                                     1.61 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10348 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.54 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JU4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             46.65 
_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                     28793 
_refine.ls_number_reflns_R_free                  886 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.66 
_refine.ls_percent_reflns_R_free                 3.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1707 
_refine.ls_R_factor_R_free                       0.2070 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1695 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.29 
_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                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2839 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             176 
_refine_hist.number_atoms_total               3038 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        46.65 
# 
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' ? 0.008 ? 2939 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.873 ? 3995 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.288 ? 400  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055 ? 424  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 524  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.13  . . 146 4653 100.00 . . . . 0.1709 . . . . . . . . . . . 0.2041 
'X-RAY DIFFRACTION' 2.13 2.29  . . 145 4618 99.00  . . . . 0.1774 . . . . . . . . . . . 0.2008 
'X-RAY DIFFRACTION' 2.29 2.52  . . 140 4649 99.00  . . . . 0.1777 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 2.52 2.88  . . 152 4644 99.00  . . . . 0.1823 . . . . . . . . . . . 0.2188 
'X-RAY DIFFRACTION' 2.88 3.63  . . 148 4669 99.00  . . . . 0.1736 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 3.63 46.65 . . 155 4674 97.00  . . . . 0.1568 . . . . . . . . . . . 0.1999 
# 
_struct.entry_id                     9JU4 
_struct.title                        
'Crystal structure of the Thermotoga maritima cold shock protein mutant Est#13 in complex with AacEst' 
_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        9JU4 
_struct_keywords.text            
'Antibody-mimics, Cold shock protein, Refolding, Heat sterilization, Freeze-drying, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP C8WUR3_ALIAD C8WUR3 ? 1 
;MPLDPVIQQVLDQLNRMPAPDYKHLSAQQFRSQQSLFPPVKKEPVAEVREFDMDLPGRTLKVRMYRPEGVEPPYPALVYY
HGGGWVVGDLETHDPVCRVLAKDGRAVVFSVDYRLAPEHKFPAAVEDAYDALQWIAERAADFHLDPARIAVGGDSAGGNL
AAVTSILAKERGGPAIAFQLLIYPSTGYDPAHPPASIEENAEGYLLTGGMMLWFRDQYLNSLEELTHPWFSPVLYPDLSG
LPPAYIATAQYDPLRDVGKLYAEALNKAGVKVEIENFEDLIHGFAQFYSLSPGATKALVRIAEKLRDALA
;
1 
2 PDB 9JU4         9JU4   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JU4 A 1 ? 310 ? C8WUR3 1 ? 310 ? 1 310 
2 2 9JU4 B 1 ? 66  ? 9JU4   2 ? 67  ? 2 67  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2310  ? 
1 MORE         -0    ? 
1 'SSA (A^2)'  15120 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_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 ASP A 4   ? ASN A 15  ? ASP A 4   ASN A 15  1 ? 12 
HELX_P HELX_P2  AA2 SER A 26  ? GLN A 33  ? SER A 26  GLN A 33  1 ? 8  
HELX_P HELX_P3  AA3 HIS A 93  ? ARG A 105 ? HIS A 93  ARG A 105 1 ? 13 
HELX_P HELX_P4  AA4 PRO A 122 ? ARG A 138 ? PRO A 122 ARG A 138 1 ? 17 
HELX_P HELX_P5  AA5 SER A 155 ? ARG A 171 ? SER A 155 ARG A 171 1 ? 17 
HELX_P HELX_P6  AA6 PRO A 194 ? ASN A 200 ? PRO A 194 ASN A 200 1 ? 7  
HELX_P HELX_P7  AA7 THR A 207 ? LEU A 219 ? THR A 207 LEU A 219 1 ? 13 
HELX_P HELX_P8  AA8 SER A 221 ? HIS A 227 ? SER A 221 HIS A 227 5 ? 7  
HELX_P HELX_P9  AA9 SER A 231 ? TYR A 235 ? SER A 231 TYR A 235 5 ? 5  
HELX_P HELX_P10 AB1 LEU A 254 ? ALA A 268 ? LEU A 254 ALA A 268 1 ? 15 
HELX_P HELX_P11 AB2 GLY A 283 ? TYR A 288 ? GLY A 283 TYR A 288 5 ? 6  
HELX_P HELX_P12 AB3 SER A 291 ? ALA A 310 ? SER A 291 ALA A 310 1 ? 20 
HELX_P HELX_P13 AB4 ASP B 29  ? ILE B 31  ? ASP B 30  ILE B 32  5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           SER 
_struct_conn.ptnr1_label_seq_id            155 
_struct_conn.ptnr1_label_atom_id           OG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           C 
_struct_conn.ptnr2_label_comp_id           PMS 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           S 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            SER 
_struct_conn.ptnr1_auth_seq_id             155 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            PMS 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.475 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      PMS 
_pdbx_modification_feature.label_asym_id                      C 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     SER 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      155 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       PMS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      SER 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       155 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               S 
_pdbx_modification_feature.modified_residue_id_linking_atom   OG 
_pdbx_modification_feature.modified_residue_id                SER 
_pdbx_modification_feature.ref_pcm_id                         2 
_pdbx_modification_feature.ref_comp_id                        PMS 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 72  A . ? PRO 72  A PRO 73  A ? PRO 73  A 1 -5.15 
2 ALA 116 A . ? ALA 116 A PRO 117 A ? PRO 117 A 1 1.27  
3 PHE 121 A . ? PHE 121 A PRO 122 A ? PRO 122 A 1 3.03  
4 GLY 173 A . ? GLY 173 A PRO 174 A ? PRO 174 A 1 0.58  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 47  ? LEU A 55  ? GLU A 47  LEU A 55  
AA1 2 ARG A 58  ? ARG A 66  ? ARG A 58  ARG A 66  
AA1 3 VAL A 107 ? VAL A 111 ? VAL A 107 VAL A 111 
AA1 4 TYR A 74  ? TYR A 80  ? TYR A 74  TYR A 80  
AA1 5 LEU A 144 ? ASP A 154 ? LEU A 144 ASP A 154 
AA1 6 GLN A 179 ? ILE A 182 ? GLN A 179 ILE A 182 
AA1 7 ALA A 244 ? ALA A 249 ? ALA A 244 ALA A 249 
AA1 8 VAL A 272 ? PHE A 277 ? VAL A 272 PHE A 277 
AA2 1 GLY B 2   ? HIS B 8   ? GLY B 3   HIS B 9   
AA2 2 TYR B 13  ? THR B 17  ? TYR B 14  THR B 18  
AA2 3 VAL B 24  ? ASN B 27  ? VAL B 25  ASN B 28  
AA2 4 GLN B 58  ? LYS B 63  ? GLN B 59  LYS B 64  
AA2 5 VAL B 44  ? ASP B 50  ? VAL B 45  ASP B 51  
AA2 6 GLY B 2   ? HIS B 8   ? GLY B 3   HIS B 9   
# 
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 MET A 53  ? N MET A 53  O LEU A 60  ? O LEU A 60  
AA1 2 3 N ARG A 63  ? N ARG A 63  O SER A 110 ? O SER A 110 
AA1 3 4 O PHE A 109 ? O PHE A 109 N TYR A 79  ? N TYR A 79  
AA1 4 5 N ALA A 76  ? N ALA A 76  O ALA A 150 ? O ALA A 150 
AA1 5 6 N GLY A 153 ? N GLY A 153 O ILE A 182 ? O ILE A 182 
AA1 6 7 N LEU A 181 ? N LEU A 181 O TYR A 245 ? O TYR A 245 
AA1 7 8 N THR A 248 ? N THR A 248 O PHE A 277 ? O PHE A 277 
AA2 1 2 N HIS B 8   ? N HIS B 9   O TYR B 13  ? O TYR B 14  
AA2 2 3 N ILE B 16  ? N ILE B 17  O VAL B 24  ? O VAL B 25  
AA2 3 4 N PHE B 25  ? N PHE B 26  O ALA B 59  ? O ALA B 60  
AA2 4 5 O ALA B 60  ? O ALA B 61  N GLU B 48  ? N GLU B 49  
AA2 5 6 O VAL B 45  ? O VAL B 46  N GLY B 2   ? N GLY B 3   
# 
_pdbx_entry_details.entry_id                   9JU4 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 89  ? ? -163.17 -169.34 
2  1 SER A 155 ? ? 59.84   -119.77 
3  1 PHE A 178 ? ? -171.24 145.77  
4  1 TYR A 183 ? ? 27.22   65.85   
5  1 SER A 185 ? ? -102.64 78.21   
6  1 LEU A 205 ? ? 76.25   -68.19  
7  1 SER A 231 ? ? -117.00 78.94   
8  1 SER A 289 ? ? 65.21   -17.56  
9  1 SER B 52  ? ? -95.39  33.20   
10 1 HIS B 62  ? ? 41.66   73.23   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     621 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 B LYS 19 ? B LYS 18 
2  1 Y 1 B ASP 20 ? B ASP 19 
3  1 Y 1 B GLU 21 ? B GLU 20 
4  1 Y 1 B GLY 22 ? B GLY 21 
5  1 Y 1 B GLY 23 ? B GLY 22 
6  1 Y 1 B MET 34 ? B MET 33 
7  1 Y 1 B GLU 35 ? B GLU 34 
8  1 Y 1 B GLY 36 ? B GLY 35 
9  1 Y 1 B PHE 37 ? B PHE 36 
10 1 Y 1 B VAL 54 ? B VAL 53 
11 1 Y 1 B ALA 55 ? B ALA 54 
12 1 Y 1 B ASN 56 ? B ASN 55 
13 1 Y 1 B VAL 65 ? B VAL 64 
14 1 Y 1 B VAL 66 ? B VAL 65 
15 1 Y 1 B GLU 67 ? B GLU 66 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PEG C1   C N N 264 
PEG O1   O N N 265 
PEG C2   C N N 266 
PEG O2   O N N 267 
PEG C3   C N N 268 
PEG C4   C N N 269 
PEG O4   O N N 270 
PEG H11  H N N 271 
PEG H12  H N N 272 
PEG HO1  H N N 273 
PEG H21  H N N 274 
PEG H22  H N N 275 
PEG H31  H N N 276 
PEG H32  H N N 277 
PEG H41  H N N 278 
PEG H42  H N N 279 
PEG HO4  H N N 280 
PHE N    N N N 281 
PHE CA   C N S 282 
PHE C    C N N 283 
PHE O    O N N 284 
PHE CB   C N N 285 
PHE CG   C Y N 286 
PHE CD1  C Y N 287 
PHE CD2  C Y N 288 
PHE CE1  C Y N 289 
PHE CE2  C Y N 290 
PHE CZ   C Y N 291 
PHE OXT  O N N 292 
PHE H    H N N 293 
PHE H2   H N N 294 
PHE HA   H N N 295 
PHE HB2  H N N 296 
PHE HB3  H N N 297 
PHE HD1  H N N 298 
PHE HD2  H N N 299 
PHE HE1  H N N 300 
PHE HE2  H N N 301 
PHE HZ   H N N 302 
PHE HXT  H N N 303 
PMS C    C N N 304 
PMS S    S N N 305 
PMS C1   C Y N 306 
PMS C2   C Y N 307 
PMS C3   C Y N 308 
PMS C4   C Y N 309 
PMS C5   C Y N 310 
PMS C6   C Y N 311 
PMS O3S  O N N 312 
PMS O2S  O N N 313 
PMS O1S  O N N 314 
PMS H2A  H N N 315 
PMS H1   H N N 316 
PMS H2   H N N 317 
PMS H3   H N N 318 
PMS H4   H N N 319 
PMS H5   H N N 320 
PMS H6   H N N 321 
PMS HO3S H N N 322 
PRO N    N N N 323 
PRO CA   C N S 324 
PRO C    C N N 325 
PRO O    O N N 326 
PRO CB   C N N 327 
PRO CG   C N N 328 
PRO CD   C N N 329 
PRO OXT  O N N 330 
PRO H    H N N 331 
PRO HA   H N N 332 
PRO HB2  H N N 333 
PRO HB3  H N N 334 
PRO HG2  H N N 335 
PRO HG3  H N N 336 
PRO HD2  H N N 337 
PRO HD3  H N N 338 
PRO HXT  H N N 339 
SER N    N N N 340 
SER CA   C N S 341 
SER C    C N N 342 
SER O    O N N 343 
SER CB   C N N 344 
SER OG   O N N 345 
SER OXT  O N N 346 
SER H    H N N 347 
SER H2   H N N 348 
SER HA   H N N 349 
SER HB2  H N N 350 
SER HB3  H N N 351 
SER HG   H N N 352 
SER HXT  H N N 353 
THR N    N N N 354 
THR CA   C N S 355 
THR C    C N N 356 
THR O    O N N 357 
THR CB   C N R 358 
THR OG1  O N N 359 
THR CG2  C N N 360 
THR OXT  O N N 361 
THR H    H N N 362 
THR H2   H N N 363 
THR HA   H N N 364 
THR HB   H N N 365 
THR HG1  H N N 366 
THR HG21 H N N 367 
THR HG22 H N N 368 
THR HG23 H N N 369 
THR HXT  H N N 370 
TRP N    N N N 371 
TRP CA   C N S 372 
TRP C    C N N 373 
TRP O    O N N 374 
TRP CB   C N N 375 
TRP CG   C Y N 376 
TRP CD1  C Y N 377 
TRP CD2  C Y N 378 
TRP NE1  N Y N 379 
TRP CE2  C Y N 380 
TRP CE3  C Y N 381 
TRP CZ2  C Y N 382 
TRP CZ3  C Y N 383 
TRP CH2  C Y N 384 
TRP OXT  O N N 385 
TRP H    H N N 386 
TRP H2   H N N 387 
TRP HA   H N N 388 
TRP HB2  H N N 389 
TRP HB3  H N N 390 
TRP HD1  H N N 391 
TRP HE1  H N N 392 
TRP HE3  H N N 393 
TRP HZ2  H N N 394 
TRP HZ3  H N N 395 
TRP HH2  H N N 396 
TRP HXT  H N N 397 
TYR N    N N N 398 
TYR CA   C N S 399 
TYR C    C N N 400 
TYR O    O N N 401 
TYR CB   C N N 402 
TYR CG   C Y N 403 
TYR CD1  C Y N 404 
TYR CD2  C Y N 405 
TYR CE1  C Y N 406 
TYR CE2  C Y N 407 
TYR CZ   C Y N 408 
TYR OH   O N N 409 
TYR OXT  O N N 410 
TYR H    H N N 411 
TYR H2   H N N 412 
TYR HA   H N N 413 
TYR HB2  H N N 414 
TYR HB3  H N N 415 
TYR HD1  H N N 416 
TYR HD2  H N N 417 
TYR HE1  H N N 418 
TYR HE2  H N N 419 
TYR HH   H N N 420 
TYR HXT  H N N 421 
VAL N    N N N 422 
VAL CA   C N S 423 
VAL C    C N N 424 
VAL O    O N N 425 
VAL CB   C N N 426 
VAL CG1  C N N 427 
VAL CG2  C N N 428 
VAL OXT  O N N 429 
VAL H    H N N 430 
VAL H2   H N N 431 
VAL HA   H N N 432 
VAL HB   H N N 433 
VAL HG11 H N N 434 
VAL HG12 H N N 435 
VAL HG13 H N N 436 
VAL HG21 H N N 437 
VAL HG22 H N N 438 
VAL HG23 H N N 439 
VAL HXT  H N N 440 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PEG C1  O1   sing N N 250 
PEG C1  C2   sing N N 251 
PEG C1  H11  sing N N 252 
PEG C1  H12  sing N N 253 
PEG O1  HO1  sing N N 254 
PEG C2  O2   sing N N 255 
PEG C2  H21  sing N N 256 
PEG C2  H22  sing N N 257 
PEG O2  C3   sing N N 258 
PEG C3  C4   sing N N 259 
PEG C3  H31  sing N N 260 
PEG C3  H32  sing N N 261 
PEG C4  O4   sing N N 262 
PEG C4  H41  sing N N 263 
PEG C4  H42  sing N N 264 
PEG O4  HO4  sing N N 265 
PHE N   CA   sing N N 266 
PHE N   H    sing N N 267 
PHE N   H2   sing N N 268 
PHE CA  C    sing N N 269 
PHE CA  CB   sing N N 270 
PHE CA  HA   sing N N 271 
PHE C   O    doub N N 272 
PHE C   OXT  sing N N 273 
PHE CB  CG   sing N N 274 
PHE CB  HB2  sing N N 275 
PHE CB  HB3  sing N N 276 
PHE CG  CD1  doub Y N 277 
PHE CG  CD2  sing Y N 278 
PHE CD1 CE1  sing Y N 279 
PHE CD1 HD1  sing N N 280 
PHE CD2 CE2  doub Y N 281 
PHE CD2 HD2  sing N N 282 
PHE CE1 CZ   doub Y N 283 
PHE CE1 HE1  sing N N 284 
PHE CE2 CZ   sing Y N 285 
PHE CE2 HE2  sing N N 286 
PHE CZ  HZ   sing N N 287 
PHE OXT HXT  sing N N 288 
PMS C   C1   sing N N 289 
PMS C   S    sing N N 290 
PMS C   H2A  sing N N 291 
PMS C   H1   sing N N 292 
PMS O2S S    doub N N 293 
PMS S   O1S  doub N N 294 
PMS S   O3S  sing N N 295 
PMS C6  C1   doub Y N 296 
PMS C1  C2   sing Y N 297 
PMS C2  C3   doub Y N 298 
PMS C2  H2   sing N N 299 
PMS C4  C3   sing Y N 300 
PMS C3  H3   sing N N 301 
PMS C5  C4   doub Y N 302 
PMS C4  H4   sing N N 303 
PMS C6  C5   sing Y N 304 
PMS C5  H5   sing N N 305 
PMS C6  H6   sing N N 306 
PMS O3S HO3S sing N N 307 
PRO N   CA   sing N N 308 
PRO N   CD   sing N N 309 
PRO N   H    sing N N 310 
PRO CA  C    sing N N 311 
PRO CA  CB   sing N N 312 
PRO CA  HA   sing N N 313 
PRO C   O    doub N N 314 
PRO C   OXT  sing N N 315 
PRO CB  CG   sing N N 316 
PRO CB  HB2  sing N N 317 
PRO CB  HB3  sing N N 318 
PRO CG  CD   sing N N 319 
PRO CG  HG2  sing N N 320 
PRO CG  HG3  sing N N 321 
PRO CD  HD2  sing N N 322 
PRO CD  HD3  sing N N 323 
PRO OXT HXT  sing N N 324 
SER N   CA   sing N N 325 
SER N   H    sing N N 326 
SER N   H2   sing N N 327 
SER CA  C    sing N N 328 
SER CA  CB   sing N N 329 
SER CA  HA   sing N N 330 
SER C   O    doub N N 331 
SER C   OXT  sing N N 332 
SER CB  OG   sing N N 333 
SER CB  HB2  sing N N 334 
SER CB  HB3  sing N N 335 
SER OG  HG   sing N N 336 
SER OXT HXT  sing N N 337 
THR N   CA   sing N N 338 
THR N   H    sing N N 339 
THR N   H2   sing N N 340 
THR CA  C    sing N N 341 
THR CA  CB   sing N N 342 
THR CA  HA   sing N N 343 
THR C   O    doub N N 344 
THR C   OXT  sing N N 345 
THR CB  OG1  sing N N 346 
THR CB  CG2  sing N N 347 
THR CB  HB   sing N N 348 
THR OG1 HG1  sing N N 349 
THR CG2 HG21 sing N N 350 
THR CG2 HG22 sing N N 351 
THR CG2 HG23 sing N N 352 
THR OXT HXT  sing N N 353 
TRP N   CA   sing N N 354 
TRP N   H    sing N N 355 
TRP N   H2   sing N N 356 
TRP CA  C    sing N N 357 
TRP CA  CB   sing N N 358 
TRP CA  HA   sing N N 359 
TRP C   O    doub N N 360 
TRP C   OXT  sing N N 361 
TRP CB  CG   sing N N 362 
TRP CB  HB2  sing N N 363 
TRP CB  HB3  sing N N 364 
TRP CG  CD1  doub Y N 365 
TRP CG  CD2  sing Y N 366 
TRP CD1 NE1  sing Y N 367 
TRP CD1 HD1  sing N N 368 
TRP CD2 CE2  doub Y N 369 
TRP CD2 CE3  sing Y N 370 
TRP NE1 CE2  sing Y N 371 
TRP NE1 HE1  sing N N 372 
TRP CE2 CZ2  sing Y N 373 
TRP CE3 CZ3  doub Y N 374 
TRP CE3 HE3  sing N N 375 
TRP CZ2 CH2  doub Y N 376 
TRP CZ2 HZ2  sing N N 377 
TRP CZ3 CH2  sing Y N 378 
TRP CZ3 HZ3  sing N N 379 
TRP CH2 HH2  sing N N 380 
TRP OXT HXT  sing N N 381 
TYR N   CA   sing N N 382 
TYR N   H    sing N N 383 
TYR N   H2   sing N N 384 
TYR CA  C    sing N N 385 
TYR CA  CB   sing N N 386 
TYR CA  HA   sing N N 387 
TYR C   O    doub N N 388 
TYR C   OXT  sing N N 389 
TYR CB  CG   sing N N 390 
TYR CB  HB2  sing N N 391 
TYR CB  HB3  sing N N 392 
TYR CG  CD1  doub Y N 393 
TYR CG  CD2  sing Y N 394 
TYR CD1 CE1  sing Y N 395 
TYR CD1 HD1  sing N N 396 
TYR CD2 CE2  doub Y N 397 
TYR CD2 HD2  sing N N 398 
TYR CE1 CZ   doub Y N 399 
TYR CE1 HE1  sing N N 400 
TYR CE2 CZ   sing Y N 401 
TYR CE2 HE2  sing N N 402 
TYR CZ  OH   sing N N 403 
TYR OH  HH   sing N N 404 
TYR OXT HXT  sing N N 405 
VAL N   CA   sing N N 406 
VAL N   H    sing N N 407 
VAL N   H2   sing N N 408 
VAL CA  C    sing N N 409 
VAL CA  CB   sing N N 410 
VAL CA  HA   sing N N 411 
VAL C   O    doub N N 412 
VAL C   OXT  sing N N 413 
VAL CB  CG1  sing N N 414 
VAL CB  CG2  sing N N 415 
VAL CB  HB   sing N N 416 
VAL CG1 HG11 sing N N 417 
VAL CG1 HG12 sing N N 418 
VAL CG1 HG13 sing N N 419 
VAL CG2 HG21 sing N N 420 
VAL CG2 HG22 sing N N 421 
VAL CG2 HG23 sing N N 422 
VAL OXT HXT  sing N N 423 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan 21K05386 1 
'Japan Society for the Promotion of Science (JSPS)' Japan 23H04559 2 
'Japan Society for the Promotion of Science (JSPS)' Japan 24K08717 3 
'Japan Society for the Promotion of Science (JSPS)' Japan 23KJ1820 4 
# 
_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   1EVQ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JU4 
_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]   0.021825 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001524 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021436 
_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]   0.009900 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 24.711  -21.024 17.050 1.00 45.10 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 24.192  -19.998 16.150 1.00 43.98 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 24.468  -18.597 16.694 1.00 46.18 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 24.474  -18.391 17.909 1.00 46.20 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 22.683  -20.186 15.927 1.00 41.24 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 22.254  -21.599 15.561 1.00 39.64 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 20.451  -21.732 15.407 1.00 57.20 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 20.252  -21.881 13.631 1.00 56.87 ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 2   ? 24.703  -17.636 15.808 1.00 46.21 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 24.803  -16.239 16.233 1.00 43.26 ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 23.407  -15.685 16.496 1.00 39.95 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 22.395  -16.333 16.235 1.00 40.55 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 25.458  -15.552 15.032 1.00 48.14 ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 24.964  -16.332 13.863 1.00 44.63 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 24.857  -17.773 14.346 1.00 46.43 ? 2   PRO A CD  1 
ATOM   16   N N   . LEU A 1 3   ? 23.378  -14.457 17.006 1.00 37.87 ? 3   LEU A N   1 
ATOM   17   C CA  . LEU A 1 3   ? 22.126  -13.760 17.256 1.00 36.16 ? 3   LEU A CA  1 
ATOM   18   C C   . LEU A 1 3   ? 21.285  -13.683 15.992 1.00 41.37 ? 3   LEU A C   1 
ATOM   19   O O   . LEU A 1 3   ? 21.800  -13.428 14.898 1.00 34.44 ? 3   LEU A O   1 
ATOM   20   C CB  . LEU A 1 3   ? 22.411  -12.351 17.756 1.00 35.94 ? 3   LEU A CB  1 
ATOM   21   C CG  . LEU A 1 3   ? 22.402  -12.162 19.259 1.00 37.68 ? 3   LEU A CG  1 
ATOM   22   C CD1 . LEU A 1 3   ? 22.541  -10.686 19.566 1.00 40.52 ? 3   LEU A CD1 1 
ATOM   23   C CD2 . LEU A 1 3   ? 21.117  -12.739 19.835 1.00 32.30 ? 3   LEU A CD2 1 
ATOM   24   N N   . ASP A 1 4   ? 19.989  -13.911 16.147 1.00 36.26 ? 4   ASP A N   1 
ATOM   25   C CA  . ASP A 1 4   ? 19.067  -13.723 15.040 1.00 34.54 ? 4   ASP A CA  1 
ATOM   26   C C   . ASP A 1 4   ? 19.255  -12.326 14.446 1.00 32.01 ? 4   ASP A C   1 
ATOM   27   O O   . ASP A 1 4   ? 19.394  -11.342 15.190 1.00 29.63 ? 4   ASP A O   1 
ATOM   28   C CB  . ASP A 1 4   ? 17.625  -13.928 15.519 1.00 35.51 ? 4   ASP A CB  1 
ATOM   29   C CG  . ASP A 1 4   ? 16.599  -13.579 14.466 1.00 32.65 ? 4   ASP A CG  1 
ATOM   30   O OD1 . ASP A 1 4   ? 16.195  -12.400 14.399 1.00 35.64 ? 4   ASP A OD1 1 
ATOM   31   O OD2 . ASP A 1 4   ? 16.188  -14.485 13.713 1.00 35.87 ? 4   ASP A OD2 1 
ATOM   32   N N   . PRO A 1 5   ? 19.276  -12.200 13.118 1.00 35.82 ? 5   PRO A N   1 
ATOM   33   C CA  . PRO A 1 5   ? 19.692  -10.921 12.513 1.00 35.35 ? 5   PRO A CA  1 
ATOM   34   C C   . PRO A 1 5   ? 18.790  -9.746  12.846 1.00 37.29 ? 5   PRO A C   1 
ATOM   35   O O   . PRO A 1 5   ? 19.291  -8.631  13.044 1.00 32.28 ? 5   PRO A O   1 
ATOM   36   C CB  . PRO A 1 5   ? 19.694  -11.239 11.010 1.00 40.49 ? 5   PRO A CB  1 
ATOM   37   C CG  . PRO A 1 5   ? 18.864  -12.481 10.864 1.00 43.54 ? 5   PRO A CG  1 
ATOM   38   C CD  . PRO A 1 5   ? 19.090  -13.259 12.116 1.00 38.21 ? 5   PRO A CD  1 
ATOM   39   N N   . VAL A 1 6   ? 17.472  -9.950  12.910 1.00 33.49 ? 6   VAL A N   1 
ATOM   40   C CA  . VAL A 1 6   ? 16.580  -8.844  13.247 1.00 32.13 ? 6   VAL A CA  1 
ATOM   41   C C   . VAL A 1 6   ? 16.778  -8.423  14.697 1.00 32.30 ? 6   VAL A C   1 
ATOM   42   O O   . VAL A 1 6   ? 16.837  -7.228  15.015 1.00 31.41 ? 6   VAL A O   1 
ATOM   43   C CB  . VAL A 1 6   ? 15.118  -9.239  12.973 1.00 36.06 ? 6   VAL A CB  1 
ATOM   44   C CG1 . VAL A 1 6   ? 14.199  -8.041  13.168 1.00 37.82 ? 6   VAL A CG1 1 
ATOM   45   C CG2 . VAL A 1 6   ? 14.986  -9.811  11.575 1.00 40.71 ? 6   VAL A CG2 1 
ATOM   46   N N   . ILE A 1 7   ? 16.871  -9.398  15.602 1.00 32.63 ? 7   ILE A N   1 
ATOM   47   C CA  . ILE A 1 7   ? 17.149  -9.094  17.003 1.00 29.15 ? 7   ILE A CA  1 
ATOM   48   C C   . ILE A 1 7   ? 18.465  -8.329  17.141 1.00 30.86 ? 7   ILE A C   1 
ATOM   49   O O   . ILE A 1 7   ? 18.556  -7.348  17.892 1.00 29.84 ? 7   ILE A O   1 
ATOM   50   C CB  . ILE A 1 7   ? 17.143  -10.401 17.819 1.00 34.61 ? 7   ILE A CB  1 
ATOM   51   C CG1 . ILE A 1 7   ? 15.729  -11.008 17.787 1.00 32.92 ? 7   ILE A CG1 1 
ATOM   52   C CG2 . ILE A 1 7   ? 17.629  -10.145 19.237 1.00 30.65 ? 7   ILE A CG2 1 
ATOM   53   C CD1 . ILE A 1 7   ? 15.606  -12.371 18.431 1.00 35.25 ? 7   ILE A CD1 1 
ATOM   54   N N   . GLN A 1 8   ? 19.496  -8.750  16.400 1.00 32.47 ? 8   GLN A N   1 
ATOM   55   C CA  . GLN A 1 8   ? 20.783  -8.049  16.427 1.00 31.86 ? 8   GLN A CA  1 
ATOM   56   C C   . GLN A 1 8   ? 20.627  -6.572  16.091 1.00 33.33 ? 8   GLN A C   1 
ATOM   57   O O   . GLN A 1 8   ? 21.277  -5.712  16.701 1.00 35.13 ? 8   GLN A O   1 
ATOM   58   C CB  . GLN A 1 8   ? 21.754  -8.703  15.446 1.00 35.86 ? 8   GLN A CB  1 
ATOM   59   C CG  . GLN A 1 8   ? 23.147  -8.081  15.460 1.00 37.58 ? 8   GLN A CG  1 
ATOM   60   C CD  . GLN A 1 8   ? 23.938  -8.510  16.674 1.00 41.77 ? 8   GLN A CD  1 
ATOM   61   O OE1 . GLN A 1 8   ? 24.406  -9.648  16.750 1.00 44.48 ? 8   GLN A OE1 1 
ATOM   62   N NE2 . GLN A 1 8   ? 24.079  -7.608  17.640 1.00 40.05 ? 8   GLN A NE2 1 
ATOM   63   N N   . GLN A 1 9   ? 19.781  -6.258  15.107 1.00 34.60 ? 9   GLN A N   1 
ATOM   64   C CA  . GLN A 1 9   ? 19.604  -4.868  14.699 1.00 35.29 ? 9   GLN A CA  1 
ATOM   65   C C   . GLN A 1 9   ? 18.978  -4.051  15.818 1.00 37.17 ? 9   GLN A C   1 
ATOM   66   O O   . GLN A 1 9   ? 19.379  -2.906  16.066 1.00 33.62 ? 9   GLN A O   1 
ATOM   67   C CB  . GLN A 1 9   ? 18.746  -4.806  13.432 1.00 38.23 ? 9   GLN A CB  1 
ATOM   68   C CG  . GLN A 1 9   ? 19.394  -5.457  12.212 1.00 39.84 ? 9   GLN A CG  1 
ATOM   69   C CD  . GLN A 1 9   ? 18.455  -5.550  11.017 1.00 48.75 ? 9   GLN A CD  1 
ATOM   70   O OE1 . GLN A 1 9   ? 17.255  -5.784  11.169 1.00 46.78 ? 9   GLN A OE1 1 
ATOM   71   N NE2 . GLN A 1 9   ? 19.004  -5.372  9.818  1.00 51.66 ? 9   GLN A NE2 1 
ATOM   72   N N   . VAL A 1 10  ? 18.000  -4.632  16.518 1.00 32.23 ? 10  VAL A N   1 
ATOM   73   C CA  . VAL A 1 10  ? 17.365  -3.935  17.631 1.00 37.44 ? 10  VAL A CA  1 
ATOM   74   C C   . VAL A 1 10  ? 18.371  -3.700  18.750 1.00 31.91 ? 10  VAL A C   1 
ATOM   75   O O   . VAL A 1 10  ? 18.486  -2.590  19.283 1.00 37.15 ? 10  VAL A O   1 
ATOM   76   C CB  . VAL A 1 10  ? 16.138  -4.729  18.120 1.00 34.95 ? 10  VAL A CB  1 
ATOM   77   C CG1 . VAL A 1 10  ? 15.550  -4.089  19.371 1.00 40.31 ? 10  VAL A CG1 1 
ATOM   78   C CG2 . VAL A 1 10  ? 15.092  -4.801  17.020 1.00 33.25 ? 10  VAL A CG2 1 
ATOM   79   N N   . LEU A 1 11  ? 19.125  -4.741  19.110 1.00 34.73 ? 11  LEU A N   1 
ATOM   80   C CA  . LEU A 1 11  ? 20.072  -4.638  20.214 1.00 36.92 ? 11  LEU A CA  1 
ATOM   81   C C   . LEU A 1 11  ? 21.154  -3.608  19.927 1.00 38.62 ? 11  LEU A C   1 
ATOM   82   O O   . LEU A 1 11  ? 21.517  -2.820  20.808 1.00 40.09 ? 11  LEU A O   1 
ATOM   83   C CB  . LEU A 1 11  ? 20.713  -6.000  20.486 1.00 33.36 ? 11  LEU A CB  1 
ATOM   84   C CG  . LEU A 1 11  ? 19.868  -7.062  21.183 1.00 36.72 ? 11  LEU A CG  1 
ATOM   85   C CD1 . LEU A 1 11  ? 20.724  -8.279  21.463 1.00 32.24 ? 11  LEU A CD1 1 
ATOM   86   C CD2 . LEU A 1 11  ? 19.239  -6.514  22.464 1.00 31.41 ? 11  LEU A CD2 1 
ATOM   87   N N   . ASP A 1 12  ? 21.691  -3.607  18.704 1.00 38.17 ? 12  ASP A N   1 
ATOM   88   C CA  . ASP A 1 12  ? 22.735  -2.646  18.359 1.00 38.29 ? 12  ASP A CA  1 
ATOM   89   C C   . ASP A 1 12  ? 22.266  -1.216  18.585 1.00 44.53 ? 12  ASP A C   1 
ATOM   90   O O   . ASP A 1 12  ? 23.033  -0.377  19.068 1.00 49.61 ? 12  ASP A O   1 
ATOM   91   C CB  . ASP A 1 12  ? 23.183  -2.858  16.909 1.00 38.27 ? 12  ASP A CB  1 
ATOM   92   C CG  . ASP A 1 12  ? 24.004  -4.123  16.740 1.00 37.28 ? 12  ASP A CG  1 
ATOM   93   O OD1 . ASP A 1 12  ? 24.416  -4.696  17.768 1.00 40.03 ? 12  ASP A OD1 1 
ATOM   94   O OD2 . ASP A 1 12  ? 24.221  -4.567  15.591 1.00 39.78 ? 12  ASP A OD2 1 
ATOM   95   N N   . GLN A 1 13  ? 21.003  -0.924  18.275 1.00 38.86 ? 13  GLN A N   1 
ATOM   96   C CA  . GLN A 1 13  ? 20.482  0.419   18.498 1.00 41.21 ? 13  GLN A CA  1 
ATOM   97   C C   . GLN A 1 13  ? 20.128  0.649   19.965 1.00 47.22 ? 13  GLN A C   1 
ATOM   98   O O   . GLN A 1 13  ? 20.313  1.757   20.485 1.00 45.34 ? 13  GLN A O   1 
ATOM   99   C CB  . GLN A 1 13  ? 19.264  0.661   17.603 1.00 38.88 ? 13  GLN A CB  1 
ATOM   100  C CG  . GLN A 1 13  ? 18.757  2.096   17.599 1.00 45.36 ? 13  GLN A CG  1 
ATOM   101  C CD  . GLN A 1 13  ? 19.827  3.112   17.214 1.00 46.95 ? 13  GLN A CD  1 
ATOM   102  O OE1 . GLN A 1 13  ? 20.743  2.812   16.448 1.00 46.59 ? 13  GLN A OE1 1 
ATOM   103  N NE2 . GLN A 1 13  ? 19.710  4.322   17.746 1.00 46.20 ? 13  GLN A NE2 1 
ATOM   104  N N   . LEU A 1 14  ? 19.612  -0.382  20.644 1.00 47.05 ? 14  LEU A N   1 
ATOM   105  C CA  . LEU A 1 14  ? 19.305  -0.256  22.066 1.00 43.60 ? 14  LEU A CA  1 
ATOM   106  C C   . LEU A 1 14  ? 20.554  0.078   22.871 1.00 41.91 ? 14  LEU A C   1 
ATOM   107  O O   . LEU A 1 14  ? 20.542  0.976   23.718 1.00 46.61 ? 14  LEU A O   1 
ATOM   108  C CB  . LEU A 1 14  ? 18.673  -1.549  22.583 1.00 43.01 ? 14  LEU A CB  1 
ATOM   109  C CG  . LEU A 1 14  ? 17.146  -1.562  22.618 1.00 50.06 ? 14  LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 14  ? 16.621  -2.974  22.823 1.00 49.63 ? 14  LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 14  ? 16.653  -0.640  23.718 1.00 53.93 ? 14  LEU A CD2 1 
ATOM   112  N N   . ASN A 1 15  ? 21.644  -0.634  22.614 1.00 36.02 ? 15  ASN A N   1 
ATOM   113  C CA  . ASN A 1 15  ? 22.839  -0.513  23.433 1.00 40.11 ? 15  ASN A CA  1 
ATOM   114  C C   . ASN A 1 15  ? 23.634  0.757   23.151 1.00 49.07 ? 15  ASN A C   1 
ATOM   115  O O   . ASN A 1 15  ? 24.681  0.958   23.776 1.00 46.34 ? 15  ASN A O   1 
ATOM   116  C CB  . ASN A 1 15  ? 23.723  -1.750  23.241 1.00 41.47 ? 15  ASN A CB  1 
ATOM   117  C CG  . ASN A 1 15  ? 23.045  -3.031  23.724 1.00 35.14 ? 15  ASN A CG  1 
ATOM   118  O OD1 . ASN A 1 15  ? 22.201  -2.998  24.615 1.00 35.76 ? 15  ASN A OD1 1 
ATOM   119  N ND2 . ASN A 1 15  ? 23.416  -4.156  23.138 1.00 29.96 ? 15  ASN A ND2 1 
ATOM   120  N N   . ARG A 1 16  ? 23.165  1.617   22.240 1.00 49.18 ? 16  ARG A N   1 
ATOM   121  C CA  . ARG A 1 16  ? 23.795  2.915   22.019 1.00 50.22 ? 16  ARG A CA  1 
ATOM   122  C C   . ARG A 1 16  ? 23.472  3.917   23.113 1.00 56.00 ? 16  ARG A C   1 
ATOM   123  O O   . ARG A 1 16  ? 24.277  4.821   23.361 1.00 57.67 ? 16  ARG A O   1 
ATOM   124  C CB  . ARG A 1 16  ? 23.367  3.493   20.671 1.00 47.78 ? 16  ARG A CB  1 
ATOM   125  C CG  . ARG A 1 16  ? 23.833  2.652   19.535 1.00 49.02 ? 16  ARG A CG  1 
ATOM   126  C CD  . ARG A 1 16  ? 23.769  3.363   18.192 1.00 53.82 ? 16  ARG A CD  1 
ATOM   127  N NE  . ARG A 1 16  ? 24.010  2.459   17.063 1.00 59.91 ? 16  ARG A NE  1 
ATOM   128  C CZ  . ARG A 1 16  ? 24.993  1.558   16.963 1.00 61.84 ? 16  ARG A CZ  1 
ATOM   129  N NH1 . ARG A 1 16  ? 25.914  1.412   17.911 1.00 65.86 ? 16  ARG A NH1 1 
ATOM   130  N NH2 . ARG A 1 16  ? 25.073  0.808   15.869 1.00 57.18 ? 16  ARG A NH2 1 
ATOM   131  N N   . MET A 1 17  ? 22.321  3.788   23.754 1.00 50.71 ? 17  MET A N   1 
ATOM   132  C CA  . MET A 1 17  ? 22.089  4.700   24.856 1.00 58.28 ? 17  MET A CA  1 
ATOM   133  C C   . MET A 1 17  ? 22.546  4.059   26.162 1.00 58.61 ? 17  MET A C   1 
ATOM   134  O O   . MET A 1 17  ? 22.557  2.830   26.288 1.00 56.10 ? 17  MET A O   1 
ATOM   135  C CB  . MET A 1 17  ? 20.609  5.074   24.941 1.00 58.09 ? 17  MET A CB  1 
ATOM   136  C CG  . MET A 1 17  ? 20.069  5.766   23.689 1.00 63.65 ? 17  MET A CG  1 
ATOM   137  S SD  . MET A 1 17  ? 20.849  7.359   23.337 1.00 81.22 ? 17  MET A SD  1 
ATOM   138  C CE  . MET A 1 17  ? 20.664  8.201   24.909 1.00 63.97 ? 17  MET A CE  1 
ATOM   139  N N   . PRO A 1 18  ? 22.958  4.856   27.144 1.00 60.10 ? 18  PRO A N   1 
ATOM   140  C CA  . PRO A 1 18  ? 23.471  4.274   28.386 1.00 53.35 ? 18  PRO A CA  1 
ATOM   141  C C   . PRO A 1 18  ? 22.355  3.639   29.199 1.00 49.94 ? 18  PRO A C   1 
ATOM   142  O O   . PRO A 1 18  ? 21.169  3.926   29.020 1.00 44.56 ? 18  PRO A O   1 
ATOM   143  C CB  . PRO A 1 18  ? 24.083  5.473   29.114 1.00 52.94 ? 18  PRO A CB  1 
ATOM   144  C CG  . PRO A 1 18  ? 23.288  6.635   28.622 1.00 59.91 ? 18  PRO A CG  1 
ATOM   145  C CD  . PRO A 1 18  ? 22.960  6.329   27.185 1.00 59.26 ? 18  PRO A CD  1 
ATOM   146  N N   . ALA A 1 19  ? 22.760  2.750   30.103 1.00 51.52 ? 19  ALA A N   1 
ATOM   147  C CA  . ALA A 1 19  ? 21.797  2.049   30.934 1.00 46.48 ? 19  ALA A CA  1 
ATOM   148  C C   . ALA A 1 19  ? 21.060  3.042   31.829 1.00 42.93 ? 19  ALA A C   1 
ATOM   149  O O   . ALA A 1 19  ? 21.610  4.087   32.196 1.00 43.51 ? 19  ALA A O   1 
ATOM   150  C CB  . ALA A 1 19  ? 22.496  0.989   31.784 1.00 46.70 ? 19  ALA A CB  1 
ATOM   151  N N   . PRO A 1 20  ? 19.809  2.751   32.178 1.00 40.39 ? 20  PRO A N   1 
ATOM   152  C CA  . PRO A 1 20  ? 19.067  3.637   33.080 1.00 35.32 ? 20  PRO A CA  1 
ATOM   153  C C   . PRO A 1 20  ? 19.719  3.719   34.450 1.00 33.87 ? 20  PRO A C   1 
ATOM   154  O O   . PRO A 1 20  ? 20.515  2.870   34.849 1.00 35.01 ? 20  PRO A O   1 
ATOM   155  C CB  . PRO A 1 20  ? 17.683  2.980   33.177 1.00 38.03 ? 20  PRO A CB  1 
ATOM   156  C CG  . PRO A 1 20  ? 17.606  2.033   32.025 1.00 37.08 ? 20  PRO A CG  1 
ATOM   157  C CD  . PRO A 1 20  ? 19.000  1.607   31.722 1.00 41.83 ? 20  PRO A CD  1 
ATOM   158  N N   . ASP A 1 21  ? 19.350  4.760   35.181 1.00 34.96 ? 21  ASP A N   1 
ATOM   159  C CA  . ASP A 1 21  ? 19.789  4.953   36.560 1.00 37.49 ? 21  ASP A CA  1 
ATOM   160  C C   . ASP A 1 21  ? 18.807  4.197   37.446 1.00 33.97 ? 21  ASP A C   1 
ATOM   161  O O   . ASP A 1 21  ? 17.792  4.741   37.890 1.00 32.48 ? 21  ASP A O   1 
ATOM   162  C CB  . ASP A 1 21  ? 19.836  6.439   36.895 1.00 38.04 ? 21  ASP A CB  1 
ATOM   163  C CG  . ASP A 1 21  ? 20.217  6.700   38.332 1.00 42.52 ? 21  ASP A CG  1 
ATOM   164  O OD1 . ASP A 1 21  ? 20.859  5.815   38.934 1.00 44.93 ? 21  ASP A OD1 1 
ATOM   165  O OD2 . ASP A 1 21  ? 19.877  7.788   38.857 1.00 47.81 ? 21  ASP A OD2 1 
ATOM   166  N N   . TYR A 1 22  ? 19.110  2.918   37.708 1.00 32.24 ? 22  TYR A N   1 
ATOM   167  C CA  . TYR A 1 22  ? 18.154  2.062   38.404 1.00 31.09 ? 22  TYR A CA  1 
ATOM   168  C C   . TYR A 1 22  ? 17.918  2.481   39.851 1.00 36.68 ? 22  TYR A C   1 
ATOM   169  O O   . TYR A 1 22  ? 16.856  2.165   40.397 1.00 30.09 ? 22  TYR A O   1 
ATOM   170  C CB  . TYR A 1 22  ? 18.605  0.597   38.343 1.00 28.89 ? 22  TYR A CB  1 
ATOM   171  C CG  . TYR A 1 22  ? 18.438  0.028   36.954 1.00 30.30 ? 22  TYR A CG  1 
ATOM   172  C CD1 . TYR A 1 22  ? 17.181  -0.027  36.373 1.00 29.28 ? 22  TYR A CD1 1 
ATOM   173  C CD2 . TYR A 1 22  ? 19.529  -0.418  36.213 1.00 30.38 ? 22  TYR A CD2 1 
ATOM   174  C CE1 . TYR A 1 22  ? 17.003  -0.512  35.115 1.00 32.56 ? 22  TYR A CE1 1 
ATOM   175  C CE2 . TYR A 1 22  ? 19.359  -0.923  34.923 1.00 31.72 ? 22  TYR A CE2 1 
ATOM   176  C CZ  . TYR A 1 22  ? 18.074  -0.970  34.390 1.00 32.34 ? 22  TYR A CZ  1 
ATOM   177  O OH  . TYR A 1 22  ? 17.824  -1.442  33.129 1.00 35.95 ? 22  TYR A OH  1 
ATOM   178  N N   . LYS A 1 23  ? 18.852  3.197   40.490 1.00 29.22 ? 23  LYS A N   1 
ATOM   179  C CA  . LYS A 1 23  ? 18.590  3.584   41.876 1.00 32.66 ? 23  LYS A CA  1 
ATOM   180  C C   . LYS A 1 23  ? 17.494  4.644   41.995 1.00 34.23 ? 23  LYS A C   1 
ATOM   181  O O   . LYS A 1 23  ? 16.910  4.792   43.075 1.00 33.83 ? 23  LYS A O   1 
ATOM   182  C CB  . LYS A 1 23  ? 19.870  4.069   42.567 1.00 38.36 ? 23  LYS A CB  1 
ATOM   183  C CG  . LYS A 1 23  ? 20.728  4.978   41.735 1.00 45.38 ? 23  LYS A CG  1 
ATOM   184  C CD  . LYS A 1 23  ? 22.204  4.948   42.169 1.00 51.35 ? 23  LYS A CD  1 
ATOM   185  C CE  . LYS A 1 23  ? 22.899  6.285   41.890 1.00 49.86 ? 23  LYS A CE  1 
ATOM   186  N NZ  . LYS A 1 23  ? 22.596  6.832   40.532 1.00 53.85 ? 23  LYS A NZ  1 
ATOM   187  N N   . HIS A 1 24  ? 17.191  5.376   40.922 1.00 25.73 ? 24  HIS A N   1 
ATOM   188  C CA  . HIS A 1 24  ? 16.141  6.382   40.958 1.00 28.67 ? 24  HIS A CA  1 
ATOM   189  C C   . HIS A 1 24  ? 14.990  6.113   40.000 1.00 27.29 ? 24  HIS A C   1 
ATOM   190  O O   . HIS A 1 24  ? 13.984  6.830   40.065 1.00 32.88 ? 24  HIS A O   1 
ATOM   191  C CB  . HIS A 1 24  ? 16.729  7.772   40.670 1.00 34.14 ? 24  HIS A CB  1 
ATOM   192  C CG  . HIS A 1 24  ? 17.847  8.155   41.591 1.00 35.05 ? 24  HIS A CG  1 
ATOM   193  N ND1 . HIS A 1 24  ? 19.133  8.380   41.150 1.00 38.08 ? 24  HIS A ND1 1 
ATOM   194  C CD2 . HIS A 1 24  ? 17.878  8.340   42.930 1.00 34.97 ? 24  HIS A CD2 1 
ATOM   195  C CE1 . HIS A 1 24  ? 19.911  8.699   42.168 1.00 37.42 ? 24  HIS A CE1 1 
ATOM   196  N NE2 . HIS A 1 24  ? 19.173  8.680   43.262 1.00 35.69 ? 24  HIS A NE2 1 
ATOM   197  N N   . LEU A 1 25  ? 15.104  5.105   39.143 1.00 26.69 ? 25  LEU A N   1 
ATOM   198  C CA  . LEU A 1 25  ? 14.023  4.734   38.243 1.00 26.21 ? 25  LEU A CA  1 
ATOM   199  C C   . LEU A 1 25  ? 12.781  4.345   39.034 1.00 26.11 ? 25  LEU A C   1 
ATOM   200  O O   . LEU A 1 25  ? 12.831  3.481   39.915 1.00 25.05 ? 25  LEU A O   1 
ATOM   201  C CB  . LEU A 1 25  ? 14.466  3.569   37.358 1.00 25.91 ? 25  LEU A CB  1 
ATOM   202  C CG  . LEU A 1 25  ? 13.437  3.060   36.347 1.00 25.96 ? 25  LEU A CG  1 
ATOM   203  C CD1 . LEU A 1 25  ? 13.153  4.131   35.299 1.00 29.05 ? 25  LEU A CD1 1 
ATOM   204  C CD2 . LEU A 1 25  ? 13.933  1.768   35.702 1.00 21.67 ? 25  LEU A CD2 1 
ATOM   205  N N   . SER A 1 26  ? 11.653  4.969   38.719 1.00 23.84 ? 26  SER A N   1 
ATOM   206  C CA  . SER A 1 26  ? 10.406  4.585   39.362 1.00 25.62 ? 26  SER A CA  1 
ATOM   207  C C   . SER A 1 26  ? 9.568   3.714   38.431 1.00 24.33 ? 26  SER A C   1 
ATOM   208  O O   . SER A 1 26  ? 9.760   3.703   37.213 1.00 23.49 ? 26  SER A O   1 
ATOM   209  C CB  . SER A 1 26  ? 9.617   5.824   39.780 1.00 30.36 ? 26  SER A CB  1 
ATOM   210  O OG  . SER A 1 26  ? 9.050   6.429   38.635 1.00 29.24 ? 26  SER A OG  1 
ATOM   211  N N   . ALA A 1 27  ? 8.623   2.977   39.021 1.00 22.56 ? 27  ALA A N   1 
ATOM   212  C CA  . ALA A 1 27  ? 7.749   2.138   38.203 1.00 28.65 ? 27  ALA A CA  1 
ATOM   213  C C   . ALA A 1 27  ? 6.887   2.986   37.272 1.00 30.82 ? 27  ALA A C   1 
ATOM   214  O O   . ALA A 1 27  ? 6.769   2.697   36.072 1.00 29.11 ? 27  ALA A O   1 
ATOM   215  C CB  . ALA A 1 27  ? 6.874   1.264   39.100 1.00 27.05 ? 27  ALA A CB  1 
ATOM   216  N N   . GLN A 1 28  ? 6.292   4.052   37.812 1.00 32.99 ? 28  GLN A N   1 
ATOM   217  C CA  . GLN A 1 28  ? 5.480   4.960   37.005 1.00 40.60 ? 28  GLN A CA  1 
ATOM   218  C C   . GLN A 1 28  ? 6.301   5.569   35.877 1.00 36.44 ? 28  GLN A C   1 
ATOM   219  O O   . GLN A 1 28  ? 5.774   5.830   34.794 1.00 45.62 ? 28  GLN A O   1 
ATOM   220  C CB  . GLN A 1 28  ? 4.871   6.057   37.896 1.00 42.30 ? 28  GLN A CB  1 
ATOM   221  C CG  . GLN A 1 28  ? 4.410   5.592   39.291 1.00 43.27 ? 28  GLN A CG  1 
ATOM   222  C CD  . GLN A 1 28  ? 5.581   5.301   40.231 1.00 42.46 ? 28  GLN A CD  1 
ATOM   223  O OE1 . GLN A 1 28  ? 6.726   5.419   39.833 1.00 46.60 ? 28  GLN A OE1 1 
ATOM   224  N NE2 . GLN A 1 28  ? 5.293   4.904   41.465 1.00 50.26 ? 28  GLN A NE2 1 
ATOM   225  N N   . GLN A 1 29  ? 7.601   5.773   36.111 1.00 39.79 ? 29  GLN A N   1 
ATOM   226  C CA  . GLN A 1 29  ? 8.527   6.197   35.067 1.00 36.43 ? 29  GLN A CA  1 
ATOM   227  C C   . GLN A 1 29  ? 8.722   5.104   34.026 1.00 44.35 ? 29  GLN A C   1 
ATOM   228  O O   . GLN A 1 29  ? 8.662   5.358   32.816 1.00 46.21 ? 29  GLN A O   1 
ATOM   229  C CB  . GLN A 1 29  ? 9.874   6.544   35.709 1.00 37.17 ? 29  GLN A CB  1 
ATOM   230  C CG  . GLN A 1 29  ? 10.681  7.621   35.069 1.00 25.91 ? 29  GLN A CG  1 
ATOM   231  C CD  . GLN A 1 29  ? 11.822  8.061   35.967 1.00 28.75 ? 29  GLN A CD  1 
ATOM   232  O OE1 . GLN A 1 29  ? 12.168  7.368   36.934 1.00 25.06 ? 29  GLN A OE1 1 
ATOM   233  N NE2 . GLN A 1 29  ? 12.426  9.208   35.653 1.00 32.64 ? 29  GLN A NE2 1 
ATOM   234  N N   . PHE A 1 30  ? 9.011   3.885   34.486 1.00 36.99 ? 30  PHE A N   1 
ATOM   235  C CA  . PHE A 1 30  ? 9.285   2.778   33.580 1.00 37.06 ? 30  PHE A CA  1 
ATOM   236  C C   . PHE A 1 30  ? 8.063   2.434   32.727 1.00 33.45 ? 30  PHE A C   1 
ATOM   237  O O   . PHE A 1 30  ? 8.201   2.105   31.545 1.00 37.30 ? 30  PHE A O   1 
ATOM   238  C CB  . PHE A 1 30  ? 9.750   1.569   34.394 1.00 28.23 ? 30  PHE A CB  1 
ATOM   239  C CG  . PHE A 1 30  ? 10.149  0.400   33.562 1.00 33.72 ? 30  PHE A CG  1 
ATOM   240  C CD1 . PHE A 1 30  ? 11.266  0.462   32.756 1.00 33.22 ? 30  PHE A CD1 1 
ATOM   241  C CD2 . PHE A 1 30  ? 9.406   -0.766  33.588 1.00 30.99 ? 30  PHE A CD2 1 
ATOM   242  C CE1 . PHE A 1 30  ? 11.636  -0.613  31.989 1.00 40.42 ? 30  PHE A CE1 1 
ATOM   243  C CE2 . PHE A 1 30  ? 9.770   -1.843  32.820 1.00 31.52 ? 30  PHE A CE2 1 
ATOM   244  C CZ  . PHE A 1 30  ? 10.883  -1.772  32.020 1.00 34.99 ? 30  PHE A CZ  1 
ATOM   245  N N   . ARG A 1 31  ? 6.861   2.505   33.306 1.00 36.03 ? 31  ARG A N   1 
ATOM   246  C CA  . ARG A 1 31  ? 5.641   2.219   32.548 1.00 37.55 ? 31  ARG A CA  1 
ATOM   247  C C   . ARG A 1 31  ? 5.279   3.344   31.582 1.00 43.69 ? 31  ARG A C   1 
ATOM   248  O O   . ARG A 1 31  ? 4.657   3.092   30.545 1.00 45.06 ? 31  ARG A O   1 
ATOM   249  C CB  . ARG A 1 31  ? 4.474   1.970   33.497 1.00 37.64 ? 31  ARG A CB  1 
ATOM   250  C CG  . ARG A 1 31  ? 4.647   0.782   34.402 1.00 27.94 ? 31  ARG A CG  1 
ATOM   251  C CD  . ARG A 1 31  ? 3.457   0.657   35.287 1.00 34.18 ? 31  ARG A CD  1 
ATOM   252  N NE  . ARG A 1 31  ? 3.523   -0.476  36.210 1.00 28.66 ? 31  ARG A NE  1 
ATOM   253  C CZ  . ARG A 1 31  ? 3.258   -0.363  37.505 1.00 28.75 ? 31  ARG A CZ  1 
ATOM   254  N NH1 . ARG A 1 31  ? 2.945   0.828   38.001 1.00 27.88 ? 31  ARG A NH1 1 
ATOM   255  N NH2 . ARG A 1 31  ? 3.303   -1.424  38.300 1.00 23.42 ? 31  ARG A NH2 1 
ATOM   256  N N   . SER A 1 32  ? 5.645   4.582   31.914 1.00 49.06 ? 32  SER A N   1 
ATOM   257  C CA  . SER A 1 32  ? 5.484   5.709   31.001 1.00 48.95 ? 32  SER A CA  1 
ATOM   258  C C   . SER A 1 32  ? 6.370   5.595   29.770 1.00 48.56 ? 32  SER A C   1 
ATOM   259  O O   . SER A 1 32  ? 6.137   6.307   28.787 1.00 53.18 ? 32  SER A O   1 
ATOM   260  C CB  . SER A 1 32  ? 5.812   7.011   31.723 1.00 48.61 ? 32  SER A CB  1 
ATOM   261  O OG  . SER A 1 32  ? 7.220   7.196   31.738 1.00 46.43 ? 32  SER A OG  1 
ATOM   262  N N   . GLN A 1 33  ? 7.392   4.746   29.808 1.00 47.98 ? 33  GLN A N   1 
ATOM   263  C CA  . GLN A 1 33  ? 8.226   4.541   28.637 1.00 47.28 ? 33  GLN A CA  1 
ATOM   264  C C   . GLN A 1 33  ? 7.414   3.928   27.509 1.00 49.91 ? 33  GLN A C   1 
ATOM   265  O O   . GLN A 1 33  ? 6.398   3.265   27.731 1.00 53.96 ? 33  GLN A O   1 
ATOM   266  C CB  . GLN A 1 33  ? 9.406   3.617   28.954 1.00 45.61 ? 33  GLN A CB  1 
ATOM   267  C CG  . GLN A 1 33  ? 10.342  4.104   30.035 1.00 49.77 ? 33  GLN A CG  1 
ATOM   268  C CD  . GLN A 1 33  ? 11.673  3.345   30.050 1.00 48.71 ? 33  GLN A CD  1 
ATOM   269  O OE1 . GLN A 1 33  ? 11.793  2.251   29.487 1.00 52.34 ? 33  GLN A OE1 1 
ATOM   270  N NE2 . GLN A 1 33  ? 12.671  3.925   30.699 1.00 52.31 ? 33  GLN A NE2 1 
ATOM   271  N N   . GLN A 1 34  ? 7.872   4.165   26.286 1.00 50.65 ? 34  GLN A N   1 
ATOM   272  C CA  . GLN A 1 34  ? 7.431   3.362   25.158 1.00 53.96 ? 34  GLN A CA  1 
ATOM   273  C C   . GLN A 1 34  ? 8.094   1.993   25.245 1.00 53.48 ? 34  GLN A C   1 
ATOM   274  O O   . GLN A 1 34  ? 9.285   1.883   25.554 1.00 52.00 ? 34  GLN A O   1 
ATOM   275  C CB  . GLN A 1 34  ? 7.791   4.059   23.847 1.00 53.88 ? 34  GLN A CB  1 
ATOM   276  C CG  . GLN A 1 34  ? 7.023   3.597   22.620 1.00 57.10 ? 34  GLN A CG  1 
ATOM   277  C CD  . GLN A 1 34  ? 7.679   4.076   21.339 1.00 55.25 ? 34  GLN A CD  1 
ATOM   278  O OE1 . GLN A 1 34  ? 8.572   4.920   21.373 1.00 56.98 ? 34  GLN A OE1 1 
ATOM   279  N NE2 . GLN A 1 34  ? 7.240   3.542   20.204 1.00 56.88 ? 34  GLN A NE2 1 
ATOM   280  N N   . SER A 1 35  ? 7.316   0.942   25.004 1.00 52.54 ? 35  SER A N   1 
ATOM   281  C CA  . SER A 1 35  ? 7.849   -0.403  25.162 1.00 51.74 ? 35  SER A CA  1 
ATOM   282  C C   . SER A 1 35  ? 8.821   -0.739  24.036 1.00 54.37 ? 35  SER A C   1 
ATOM   283  O O   . SER A 1 35  ? 8.659   -0.309  22.888 1.00 51.35 ? 35  SER A O   1 
ATOM   284  C CB  . SER A 1 35  ? 6.726   -1.436  25.194 1.00 50.74 ? 35  SER A CB  1 
ATOM   285  O OG  . SER A 1 35  ? 7.270   -2.747  25.160 1.00 51.59 ? 35  SER A OG  1 
ATOM   286  N N   . LEU A 1 36  ? 9.840   -1.529  24.379 1.00 50.69 ? 36  LEU A N   1 
ATOM   287  C CA  . LEU A 1 36  ? 10.822  -1.954  23.388 1.00 48.18 ? 36  LEU A CA  1 
ATOM   288  C C   . LEU A 1 36  ? 10.197  -2.778  22.271 1.00 50.63 ? 36  LEU A C   1 
ATOM   289  O O   . LEU A 1 36  ? 10.782  -2.881  21.187 1.00 50.00 ? 36  LEU A O   1 
ATOM   290  C CB  . LEU A 1 36  ? 11.928  -2.755  24.073 1.00 49.83 ? 36  LEU A CB  1 
ATOM   291  C CG  . LEU A 1 36  ? 12.471  -2.101  25.345 1.00 47.85 ? 36  LEU A CG  1 
ATOM   292  C CD1 . LEU A 1 36  ? 13.407  -3.036  26.071 1.00 52.88 ? 36  LEU A CD1 1 
ATOM   293  C CD2 . LEU A 1 36  ? 13.182  -0.799  25.005 1.00 49.81 ? 36  LEU A CD2 1 
ATOM   294  N N   . PHE A 1 37  ? 9.020   -3.357  22.503 1.00 47.16 ? 37  PHE A N   1 
ATOM   295  C CA  . PHE A 1 37  ? 8.514   -4.259  21.478 1.00 48.99 ? 37  PHE A CA  1 
ATOM   296  C C   . PHE A 1 37  ? 7.416   -3.590  20.666 1.00 48.12 ? 37  PHE A C   1 
ATOM   297  O O   . PHE A 1 37  ? 6.535   -2.935  21.233 1.00 50.19 ? 37  PHE A O   1 
ATOM   298  C CB  . PHE A 1 37  ? 7.966   -5.544  22.107 1.00 41.20 ? 37  PHE A CB  1 
ATOM   299  C CG  . PHE A 1 37  ? 8.893   -6.171  23.113 1.00 43.24 ? 37  PHE A CG  1 
ATOM   300  C CD1 . PHE A 1 37  ? 8.851   -5.791  24.451 1.00 41.77 ? 37  PHE A CD1 1 
ATOM   301  C CD2 . PHE A 1 37  ? 9.806   -7.143  22.723 1.00 39.03 ? 37  PHE A CD2 1 
ATOM   302  C CE1 . PHE A 1 37  ? 9.703   -6.369  25.383 1.00 45.05 ? 37  PHE A CE1 1 
ATOM   303  C CE2 . PHE A 1 37  ? 10.660  -7.733  23.652 1.00 39.55 ? 37  PHE A CE2 1 
ATOM   304  C CZ  . PHE A 1 37  ? 10.607  -7.346  24.984 1.00 39.37 ? 37  PHE A CZ  1 
ATOM   305  N N   . PRO A 1 38  ? 7.444   -3.737  19.346 1.00 46.95 ? 38  PRO A N   1 
ATOM   306  C CA  . PRO A 1 38  ? 6.360   -3.213  18.518 1.00 47.96 ? 38  PRO A CA  1 
ATOM   307  C C   . PRO A 1 38  ? 5.214   -4.204  18.446 1.00 49.01 ? 38  PRO A C   1 
ATOM   308  O O   . PRO A 1 38  ? 5.392   -5.393  18.753 1.00 44.22 ? 38  PRO A O   1 
ATOM   309  C CB  . PRO A 1 38  ? 7.021   -3.031  17.146 1.00 48.40 ? 38  PRO A CB  1 
ATOM   310  C CG  . PRO A 1 38  ? 8.117   -4.031  17.125 1.00 49.48 ? 38  PRO A CG  1 
ATOM   311  C CD  . PRO A 1 38  ? 8.505   -4.367  18.544 1.00 46.57 ? 38  PRO A CD  1 
ATOM   312  N N   . PRO A 1 39  ? 4.020   -3.751  18.055 1.00 51.46 ? 39  PRO A N   1 
ATOM   313  C CA  . PRO A 1 39  ? 2.896   -4.684  17.880 1.00 48.81 ? 39  PRO A CA  1 
ATOM   314  C C   . PRO A 1 39  ? 3.149   -5.624  16.709 1.00 50.53 ? 39  PRO A C   1 
ATOM   315  O O   . PRO A 1 39  ? 3.552   -5.198  15.623 1.00 54.73 ? 39  PRO A O   1 
ATOM   316  C CB  . PRO A 1 39  ? 1.699   -3.760  17.618 1.00 51.74 ? 39  PRO A CB  1 
ATOM   317  C CG  . PRO A 1 39  ? 2.120   -2.415  18.168 1.00 53.97 ? 39  PRO A CG  1 
ATOM   318  C CD  . PRO A 1 39  ? 3.601   -2.343  17.929 1.00 53.19 ? 39  PRO A CD  1 
ATOM   319  N N   . VAL A 1 40  ? 2.908   -6.912  16.940 1.00 39.79 ? 40  VAL A N   1 
ATOM   320  C CA  . VAL A 1 40  ? 3.228   -7.935  15.955 1.00 32.22 ? 40  VAL A CA  1 
ATOM   321  C C   . VAL A 1 40  ? 1.953   -8.613  15.467 1.00 36.71 ? 40  VAL A C   1 
ATOM   322  O O   . VAL A 1 40  ? 0.855   -8.317  15.952 1.00 38.02 ? 40  VAL A O   1 
ATOM   323  C CB  . VAL A 1 40  ? 4.222   -8.944  16.555 1.00 35.85 ? 40  VAL A CB  1 
ATOM   324  C CG1 . VAL A 1 40  ? 5.462   -8.210  17.039 1.00 36.76 ? 40  VAL A CG1 1 
ATOM   325  C CG2 . VAL A 1 40  ? 3.586   -9.687  17.720 1.00 35.85 ? 40  VAL A CG2 1 
ATOM   326  N N   . LYS A 1 41  ? 2.098   -9.532  14.513 1.00 34.01 ? 41  LYS A N   1 
ATOM   327  C CA  . LYS A 1 41  ? 0.954   -10.196 13.899 1.00 35.39 ? 41  LYS A CA  1 
ATOM   328  C C   . LYS A 1 41  ? 0.094   -10.929 14.926 1.00 33.77 ? 41  LYS A C   1 
ATOM   329  O O   . LYS A 1 41  ? 0.607   -11.689 15.754 1.00 27.63 ? 41  LYS A O   1 
ATOM   330  C CB  . LYS A 1 41  ? 1.441   -11.195 12.853 1.00 28.72 ? 41  LYS A CB  1 
ATOM   331  C CG  . LYS A 1 41  ? 0.324   -11.818 12.044 1.00 38.24 ? 41  LYS A CG  1 
ATOM   332  C CD  . LYS A 1 41  ? 0.740   -13.179 11.501 1.00 39.46 ? 41  LYS A CD  1 
ATOM   333  C CE  . LYS A 1 41  ? 0.050   -13.496 10.176 1.00 43.48 ? 41  LYS A CE  1 
ATOM   334  N NZ  . LYS A 1 41  ? 0.389   -12.504 9.111  1.00 50.09 ? 41  LYS A NZ  1 
ATOM   335  N N   . LYS A 1 42  ? -1.226  -10.740 14.834 1.00 29.25 ? 42  LYS A N   1 
ATOM   336  C CA  . LYS A 1 42  ? -2.191  -11.490 15.635 1.00 30.10 ? 42  LYS A CA  1 
ATOM   337  C C   . LYS A 1 42  ? -2.743  -12.619 14.774 1.00 28.91 ? 42  LYS A C   1 
ATOM   338  O O   . LYS A 1 42  ? -3.458  -12.368 13.801 1.00 30.34 ? 42  LYS A O   1 
ATOM   339  C CB  . LYS A 1 42  ? -3.312  -10.576 16.129 1.00 29.37 ? 42  LYS A CB  1 
ATOM   340  C CG  . LYS A 1 42  ? -2.860  -9.610  17.209 1.00 28.62 ? 42  LYS A CG  1 
ATOM   341  C CD  . LYS A 1 42  ? -3.912  -8.577  17.549 1.00 31.45 ? 42  LYS A CD  1 
ATOM   342  C CE  . LYS A 1 42  ? -3.472  -7.732  18.741 1.00 34.79 ? 42  LYS A CE  1 
ATOM   343  N NZ  . LYS A 1 42  ? -4.582  -6.904  19.278 1.00 37.95 ? 42  LYS A NZ  1 
ATOM   344  N N   . GLU A 1 43  ? -2.411  -13.856 15.119 1.00 26.84 ? 43  GLU A N   1 
ATOM   345  C CA  . GLU A 1 43  ? -2.944  -14.982 14.375 1.00 26.77 ? 43  GLU A CA  1 
ATOM   346  C C   . GLU A 1 43  ? -4.444  -15.115 14.647 1.00 34.43 ? 43  GLU A C   1 
ATOM   347  O O   . GLU A 1 43  ? -4.915  -14.791 15.743 1.00 27.76 ? 43  GLU A O   1 
ATOM   348  C CB  . GLU A 1 43  ? -2.228  -16.274 14.759 1.00 27.54 ? 43  GLU A CB  1 
ATOM   349  C CG  . GLU A 1 43  ? -0.740  -16.312 14.397 1.00 29.60 ? 43  GLU A CG  1 
ATOM   350  C CD  . GLU A 1 43  ? -0.481  -16.336 12.890 1.00 36.89 ? 43  GLU A CD  1 
ATOM   351  O OE1 . GLU A 1 43  ? -1.431  -16.579 12.116 1.00 38.26 ? 43  GLU A OE1 1 
ATOM   352  O OE2 . GLU A 1 43  ? 0.685   -16.121 12.487 1.00 35.48 ? 43  GLU A OE2 1 
ATOM   353  N N   . PRO A 1 44  ? -5.222  -15.562 13.660 1.00 35.79 ? 44  PRO A N   1 
ATOM   354  C CA  . PRO A 1 44  ? -6.677  -15.645 13.851 1.00 30.67 ? 44  PRO A CA  1 
ATOM   355  C C   . PRO A 1 44  ? -7.061  -16.840 14.709 1.00 26.82 ? 44  PRO A C   1 
ATOM   356  O O   . PRO A 1 44  ? -6.443  -17.904 14.646 1.00 31.09 ? 44  PRO A O   1 
ATOM   357  C CB  . PRO A 1 44  ? -7.223  -15.796 12.422 1.00 37.03 ? 44  PRO A CB  1 
ATOM   358  C CG  . PRO A 1 44  ? -6.051  -15.527 11.503 1.00 42.59 ? 44  PRO A CG  1 
ATOM   359  C CD  . PRO A 1 44  ? -4.829  -15.898 12.282 1.00 37.79 ? 44  PRO A CD  1 
ATOM   360  N N   . VAL A 1 45  ? -8.087  -16.643 15.539 1.00 30.34 ? 45  VAL A N   1 
ATOM   361  C CA  . VAL A 1 45  ? -8.671  -17.702 16.351 1.00 28.16 ? 45  VAL A CA  1 
ATOM   362  C C   . VAL A 1 45  ? -10.190 -17.641 16.185 1.00 27.32 ? 45  VAL A C   1 
ATOM   363  O O   . VAL A 1 45  ? -10.732 -16.705 15.602 1.00 30.93 ? 45  VAL A O   1 
ATOM   364  C CB  . VAL A 1 45  ? -8.257  -17.576 17.834 1.00 28.02 ? 45  VAL A CB  1 
ATOM   365  C CG1 . VAL A 1 45  ? -6.723  -17.701 17.967 1.00 26.03 ? 45  VAL A CG1 1 
ATOM   366  C CG2 . VAL A 1 45  ? -8.702  -16.241 18.363 1.00 24.62 ? 45  VAL A CG2 1 
ATOM   367  N N   . ALA A 1 46  ? -10.882 -18.663 16.699 1.00 27.44 ? 46  ALA A N   1 
ATOM   368  C CA  . ALA A 1 46  ? -12.338 -18.698 16.548 1.00 30.18 ? 46  ALA A CA  1 
ATOM   369  C C   . ALA A 1 46  ? -13.003 -17.574 17.340 1.00 31.13 ? 46  ALA A C   1 
ATOM   370  O O   . ALA A 1 46  ? -13.906 -16.898 16.834 1.00 30.34 ? 46  ALA A O   1 
ATOM   371  C CB  . ALA A 1 46  ? -12.880 -20.063 16.978 1.00 29.51 ? 46  ALA A CB  1 
ATOM   372  N N   . GLU A 1 47  ? -12.541 -17.325 18.565 1.00 24.71 ? 47  GLU A N   1 
ATOM   373  C CA  . GLU A 1 47  ? -13.185 -16.345 19.422 1.00 26.83 ? 47  GLU A CA  1 
ATOM   374  C C   . GLU A 1 47  ? -12.211 -15.859 20.489 1.00 24.05 ? 47  GLU A C   1 
ATOM   375  O O   . GLU A 1 47  ? -11.399 -16.634 20.995 1.00 22.02 ? 47  GLU A O   1 
ATOM   376  C CB  . GLU A 1 47  ? -14.428 -16.963 20.077 1.00 29.31 ? 47  GLU A CB  1 
ATOM   377  C CG  . GLU A 1 47  ? -15.189 -16.036 20.979 1.00 36.83 ? 47  GLU A CG  1 
ATOM   378  C CD  . GLU A 1 47  ? -16.443 -16.699 21.535 1.00 44.04 ? 47  GLU A CD  1 
ATOM   379  O OE1 . GLU A 1 47  ? -16.319 -17.780 22.162 1.00 45.32 ? 47  GLU A OE1 1 
ATOM   380  O OE2 . GLU A 1 47  ? -17.542 -16.140 21.327 1.00 46.31 ? 47  GLU A OE2 1 
ATOM   381  N N   . VAL A 1 48  ? -12.304 -14.576 20.822 1.00 21.73 ? 48  VAL A N   1 
ATOM   382  C CA  . VAL A 1 48  ? -11.580 -13.984 21.944 1.00 26.40 ? 48  VAL A CA  1 
ATOM   383  C C   . VAL A 1 48  ? -12.609 -13.276 22.809 1.00 25.74 ? 48  VAL A C   1 
ATOM   384  O O   . VAL A 1 48  ? -13.348 -12.422 22.312 1.00 32.75 ? 48  VAL A O   1 
ATOM   385  C CB  . VAL A 1 48  ? -10.492 -12.991 21.490 1.00 26.03 ? 48  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 48  ? -9.812  -12.349 22.702 1.00 25.01 ? 48  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 48  ? -9.462  -13.680 20.605 1.00 21.56 ? 48  VAL A CG2 1 
ATOM   388  N N   . ARG A 1 49  ? -12.665 -13.633 24.090 1.00 22.78 ? 49  ARG A N   1 
ATOM   389  C CA  . ARG A 1 49  ? -13.601 -13.039 25.041 1.00 28.31 ? 49  ARG A CA  1 
ATOM   390  C C   . ARG A 1 49  ? -12.821 -12.434 26.198 1.00 26.69 ? 49  ARG A C   1 
ATOM   391  O O   . ARG A 1 49  ? -11.999 -13.115 26.817 1.00 27.10 ? 49  ARG A O   1 
ATOM   392  C CB  . ARG A 1 49  ? -14.577 -14.079 25.584 1.00 28.46 ? 49  ARG A CB  1 
ATOM   393  C CG  . ARG A 1 49  ? -15.244 -14.964 24.544 1.00 37.32 ? 49  ARG A CG  1 
ATOM   394  C CD  . ARG A 1 49  ? -16.537 -14.330 24.022 1.00 34.65 ? 49  ARG A CD  1 
ATOM   395  N NE  . ARG A 1 49  ? -17.151 -13.446 25.004 1.00 38.22 ? 49  ARG A NE  1 
ATOM   396  C CZ  . ARG A 1 49  ? -18.192 -13.777 25.764 1.00 35.19 ? 49  ARG A CZ  1 
ATOM   397  N NH1 . ARG A 1 49  ? -18.753 -14.981 25.664 1.00 27.63 ? 49  ARG A NH1 1 
ATOM   398  N NH2 . ARG A 1 49  ? -18.668 -12.895 26.626 1.00 31.86 ? 49  ARG A NH2 1 
ATOM   399  N N   . GLU A 1 50  ? -13.071 -11.166 26.497 1.00 20.97 ? 50  GLU A N   1 
ATOM   400  C CA  . GLU A 1 50  ? -12.468 -10.534 27.660 1.00 19.83 ? 50  GLU A CA  1 
ATOM   401  C C   . GLU A 1 50  ? -13.526 -10.328 28.729 1.00 22.76 ? 50  GLU A C   1 
ATOM   402  O O   . GLU A 1 50  ? -14.650 -9.915  28.424 1.00 21.82 ? 50  GLU A O   1 
ATOM   403  C CB  . GLU A 1 50  ? -11.833 -9.188  27.302 1.00 22.54 ? 50  GLU A CB  1 
ATOM   404  C CG  . GLU A 1 50  ? -11.050 -8.595  28.455 1.00 27.97 ? 50  GLU A CG  1 
ATOM   405  C CD  . GLU A 1 50  ? -10.145 -7.466  28.015 1.00 35.54 ? 50  GLU A CD  1 
ATOM   406  O OE1 . GLU A 1 50  ? -9.635  -7.523  26.875 1.00 35.29 ? 50  GLU A OE1 1 
ATOM   407  O OE2 . GLU A 1 50  ? -9.949  -6.530  28.817 1.00 37.88 ? 50  GLU A OE2 1 
ATOM   408  N N   . PHE A 1 51  ? -13.172 -10.602 29.981 1.00 19.25 ? 51  PHE A N   1 
ATOM   409  C CA  . PHE A 1 51  ? -14.149 -10.432 31.057 1.00 21.26 ? 51  PHE A CA  1 
ATOM   410  C C   . PHE A 1 51  ? -13.420 -10.218 32.377 1.00 21.11 ? 51  PHE A C   1 
ATOM   411  O O   . PHE A 1 51  ? -12.202 -10.388 32.477 1.00 22.31 ? 51  PHE A O   1 
ATOM   412  C CB  . PHE A 1 51  ? -15.110 -11.637 31.142 1.00 19.72 ? 51  PHE A CB  1 
ATOM   413  C CG  . PHE A 1 51  ? -14.422 -12.954 31.466 1.00 20.09 ? 51  PHE A CG  1 
ATOM   414  C CD1 . PHE A 1 51  ? -13.924 -13.763 30.455 1.00 20.60 ? 51  PHE A CD1 1 
ATOM   415  C CD2 . PHE A 1 51  ? -14.287 -13.379 32.784 1.00 19.58 ? 51  PHE A CD2 1 
ATOM   416  C CE1 . PHE A 1 51  ? -13.294 -14.973 30.750 1.00 21.22 ? 51  PHE A CE1 1 
ATOM   417  C CE2 . PHE A 1 51  ? -13.655 -14.590 33.094 1.00 19.64 ? 51  PHE A CE2 1 
ATOM   418  C CZ  . PHE A 1 51  ? -13.163 -15.383 32.078 1.00 23.83 ? 51  PHE A CZ  1 
ATOM   419  N N   . ASP A 1 52  ? -14.187 -9.829  33.392 1.00 21.41 ? 52  ASP A N   1 
ATOM   420  C CA  . ASP A 1 52  ? -13.669 -9.582  34.731 1.00 21.52 ? 52  ASP A CA  1 
ATOM   421  C C   . ASP A 1 52  ? -13.910 -10.806 35.603 1.00 26.22 ? 52  ASP A C   1 
ATOM   422  O O   . ASP A 1 52  ? -15.042 -11.285 35.704 1.00 23.61 ? 52  ASP A O   1 
ATOM   423  C CB  . ASP A 1 52  ? -14.349 -8.364  35.363 1.00 24.15 ? 52  ASP A CB  1 
ATOM   424  C CG  . ASP A 1 52  ? -13.769 -7.044  34.874 1.00 32.27 ? 52  ASP A CG  1 
ATOM   425  O OD1 . ASP A 1 52  ? -12.653 -7.046  34.316 1.00 27.77 ? 52  ASP A OD1 1 
ATOM   426  O OD2 . ASP A 1 52  ? -14.437 -6.009  35.049 1.00 38.98 ? 52  ASP A OD2 1 
ATOM   427  N N   . MET A 1 53  ? -12.852 -11.295 36.239 1.00 19.17 ? 53  MET A N   1 
ATOM   428  C CA  . MET A 1 53  ? -12.929 -12.390 37.200 1.00 22.03 ? 53  MET A CA  1 
ATOM   429  C C   . MET A 1 53  ? -12.960 -11.790 38.604 1.00 21.98 ? 53  MET A C   1 
ATOM   430  O O   . MET A 1 53  ? -11.999 -11.136 39.019 1.00 19.14 ? 53  MET A O   1 
ATOM   431  C CB  . MET A 1 53  ? -11.730 -13.333 37.032 1.00 19.17 ? 53  MET A CB  1 
ATOM   432  C CG  . MET A 1 53  ? -11.634 -14.439 38.073 1.00 23.93 ? 53  MET A CG  1 
ATOM   433  S SD  . MET A 1 53  ? -10.036 -15.291 38.023 1.00 22.36 ? 53  MET A SD  1 
ATOM   434  C CE  . MET A 1 53  ? -10.079 -16.027 36.406 1.00 18.24 ? 53  MET A CE  1 
ATOM   435  N N   . ASP A 1 54  ? -14.061 -11.999 39.324 1.00 23.36 ? 54  ASP A N   1 
ATOM   436  C CA  . ASP A 1 54  ? -14.255 -11.400 40.642 1.00 21.17 ? 54  ASP A CA  1 
ATOM   437  C C   . ASP A 1 54  ? -13.700 -12.349 41.700 1.00 24.51 ? 54  ASP A C   1 
ATOM   438  O O   . ASP A 1 54  ? -14.185 -13.475 41.864 1.00 25.95 ? 54  ASP A O   1 
ATOM   439  C CB  . ASP A 1 54  ? -15.735 -11.093 40.880 1.00 27.04 ? 54  ASP A CB  1 
ATOM   440  C CG  . ASP A 1 54  ? -16.295 -10.091 39.875 1.00 31.53 ? 54  ASP A CG  1 
ATOM   441  O OD1 . ASP A 1 54  ? -15.558 -9.172  39.450 1.00 29.51 ? 54  ASP A OD1 1 
ATOM   442  O OD2 . ASP A 1 54  ? -17.476 -10.223 39.494 1.00 37.26 ? 54  ASP A OD2 1 
ATOM   443  N N   . LEU A 1 55  ? -12.660 -11.912 42.388 1.00 23.73 ? 55  LEU A N   1 
ATOM   444  C CA  . LEU A 1 55  ? -12.047 -12.633 43.486 1.00 20.38 ? 55  LEU A CA  1 
ATOM   445  C C   . LEU A 1 55  ? -12.228 -11.818 44.761 1.00 23.01 ? 55  LEU A C   1 
ATOM   446  O O   . LEU A 1 55  ? -12.540 -10.624 44.693 1.00 25.30 ? 55  LEU A O   1 
ATOM   447  C CB  . LEU A 1 55  ? -10.547 -12.846 43.218 1.00 22.04 ? 55  LEU A CB  1 
ATOM   448  C CG  . LEU A 1 55  ? -10.226 -13.721 42.008 1.00 21.13 ? 55  LEU A CG  1 
ATOM   449  C CD1 . LEU A 1 55  ? -8.724  -13.838 41.861 1.00 20.00 ? 55  LEU A CD1 1 
ATOM   450  C CD2 . LEU A 1 55  ? -10.891 -15.097 42.155 1.00 20.40 ? 55  LEU A CD2 1 
ATOM   451  N N   . PRO A 1 56  ? -12.027 -12.425 45.951 1.00 28.81 ? 56  PRO A N   1 
ATOM   452  C CA  . PRO A 1 56  ? -12.140 -11.639 47.193 1.00 25.80 ? 56  PRO A CA  1 
ATOM   453  C C   . PRO A 1 56  ? -11.147 -10.487 47.234 1.00 28.87 ? 56  PRO A C   1 
ATOM   454  O O   . PRO A 1 56  ? -9.931  -10.705 47.224 1.00 25.89 ? 56  PRO A O   1 
ATOM   455  C CB  . PRO A 1 56  ? -11.849 -12.662 48.297 1.00 27.03 ? 56  PRO A CB  1 
ATOM   456  C CG  . PRO A 1 56  ? -12.042 -14.009 47.660 1.00 33.67 ? 56  PRO A CG  1 
ATOM   457  C CD  . PRO A 1 56  ? -11.692 -13.840 46.216 1.00 26.23 ? 56  PRO A CD  1 
ATOM   458  N N   . GLY A 1 57  ? -11.659 -9.257  47.235 1.00 31.38 ? 57  GLY A N   1 
ATOM   459  C CA  . GLY A 1 57  ? -10.839 -8.071  47.364 1.00 28.82 ? 57  GLY A CA  1 
ATOM   460  C C   . GLY A 1 57  ? -10.307 -7.488  46.073 1.00 33.40 ? 57  GLY A C   1 
ATOM   461  O O   . GLY A 1 57  ? -9.744  -6.386  46.100 1.00 34.37 ? 57  GLY A O   1 
ATOM   462  N N   . ARG A 1 58  ? -10.436 -8.184  44.944 1.00 25.50 ? 58  ARG A N   1 
ATOM   463  C CA  . ARG A 1 58  ? -9.882  -7.639  43.715 1.00 24.50 ? 58  ARG A CA  1 
ATOM   464  C C   . ARG A 1 58  ? -10.519 -8.341  42.528 1.00 21.42 ? 58  ARG A C   1 
ATOM   465  O O   . ARG A 1 58  ? -10.966 -9.482  42.628 1.00 25.07 ? 58  ARG A O   1 
ATOM   466  C CB  . ARG A 1 58  ? -8.347  -7.776  43.671 1.00 25.40 ? 58  ARG A CB  1 
ATOM   467  C CG  . ARG A 1 58  ? -7.821  -9.182  43.313 1.00 20.47 ? 58  ARG A CG  1 
ATOM   468  C CD  . ARG A 1 58  ? -7.894  -10.145 44.506 1.00 21.04 ? 58  ARG A CD  1 
ATOM   469  N NE  . ARG A 1 58  ? -6.970  -11.275 44.342 1.00 21.67 ? 58  ARG A NE  1 
ATOM   470  C CZ  . ARG A 1 58  ? -7.035  -12.407 45.035 1.00 22.22 ? 58  ARG A CZ  1 
ATOM   471  N NH1 . ARG A 1 58  ? -7.986  -12.576 45.955 1.00 22.55 ? 58  ARG A NH1 1 
ATOM   472  N NH2 . ARG A 1 58  ? -6.153  -13.377 44.811 1.00 19.85 ? 58  ARG A NH2 1 
ATOM   473  N N   . THR A 1 59  ? -10.565 -7.630  41.413 1.00 19.70 ? 59  THR A N   1 
ATOM   474  C CA  . THR A 1 59  ? -11.067 -8.141  40.148 1.00 21.52 ? 59  THR A CA  1 
ATOM   475  C C   . THR A 1 59  ? -9.912  -8.242  39.161 1.00 23.39 ? 59  THR A C   1 
ATOM   476  O O   . THR A 1 59  ? -9.129  -7.300  39.027 1.00 23.54 ? 59  THR A O   1 
ATOM   477  C CB  . THR A 1 59  ? -12.147 -7.202  39.611 1.00 28.58 ? 59  THR A CB  1 
ATOM   478  O OG1 . THR A 1 59  ? -13.294 -7.282  40.465 1.00 29.76 ? 59  THR A OG1 1 
ATOM   479  C CG2 . THR A 1 59  ? -12.529 -7.581  38.217 1.00 27.12 ? 59  THR A CG2 1 
ATOM   480  N N   . LEU A 1 60  ? -9.803  -9.374  38.473 1.00 21.07 ? 60  LEU A N   1 
ATOM   481  C CA  . LEU A 1 60  ? -8.741  -9.593  37.500 1.00 19.69 ? 60  LEU A CA  1 
ATOM   482  C C   . LEU A 1 60  ? -9.342  -9.700  36.110 1.00 22.28 ? 60  LEU A C   1 
ATOM   483  O O   . LEU A 1 60  ? -10.282 -10.476 35.895 1.00 19.88 ? 60  LEU A O   1 
ATOM   484  C CB  . LEU A 1 60  ? -7.957  -10.867 37.810 1.00 19.12 ? 60  LEU A CB  1 
ATOM   485  C CG  . LEU A 1 60  ? -7.387  -11.096 39.207 1.00 21.47 ? 60  LEU A CG  1 
ATOM   486  C CD1 . LEU A 1 60  ? -6.647  -12.461 39.231 1.00 19.96 ? 60  LEU A CD1 1 
ATOM   487  C CD2 . LEU A 1 60  ? -6.475  -9.948  39.677 1.00 17.95 ? 60  LEU A CD2 1 
ATOM   488  N N   . LYS A 1 61  ? -8.796  -8.938  35.169 1.00 18.66 ? 61  LYS A N   1 
ATOM   489  C CA  . LYS A 1 61  ? -9.198  -9.092  33.777 1.00 18.19 ? 61  LYS A CA  1 
ATOM   490  C C   . LYS A 1 61  ? -8.641  -10.389 33.202 1.00 20.54 ? 61  LYS A C   1 
ATOM   491  O O   . LYS A 1 61  ? -7.525  -10.810 33.540 1.00 18.90 ? 61  LYS A O   1 
ATOM   492  C CB  . LYS A 1 61  ? -8.732  -7.891  32.953 1.00 24.01 ? 61  LYS A CB  1 
ATOM   493  C CG  . LYS A 1 61  ? -9.431  -6.602  33.363 1.00 31.48 ? 61  LYS A CG  1 
ATOM   494  C CD  . LYS A 1 61  ? -8.986  -5.401  32.542 1.00 37.11 ? 61  LYS A CD  1 
ATOM   495  C CE  . LYS A 1 61  ? -10.054 -4.306  32.610 1.00 44.45 ? 61  LYS A CE  1 
ATOM   496  N NZ  . LYS A 1 61  ? -10.911 -4.422  33.845 1.00 48.16 ? 61  LYS A NZ  1 
ATOM   497  N N   . VAL A 1 62  ? -9.439  -11.037 32.342 1.00 17.53 ? 62  VAL A N   1 
ATOM   498  C CA  . VAL A 1 62  ? -9.060  -12.286 31.692 1.00 19.11 ? 62  VAL A CA  1 
ATOM   499  C C   . VAL A 1 62  ? -9.391  -12.198 30.213 1.00 21.38 ? 62  VAL A C   1 
ATOM   500  O O   . VAL A 1 62  ? -10.456 -11.703 29.831 1.00 18.90 ? 62  VAL A O   1 
ATOM   501  C CB  . VAL A 1 62  ? -9.774  -13.507 32.315 1.00 20.23 ? 62  VAL A CB  1 
ATOM   502  C CG1 . VAL A 1 62  ? -9.393  -14.782 31.569 1.00 18.28 ? 62  VAL A CG1 1 
ATOM   503  C CG2 . VAL A 1 62  ? -9.447  -13.619 33.797 1.00 21.23 ? 62  VAL A CG2 1 
ATOM   504  N N   . ARG A 1 63  ? -8.492  -12.694 29.374 1.00 17.82 ? 63  ARG A N   1 
ATOM   505  C CA  . ARG A 1 63  ? -8.808  -12.895 27.967 1.00 17.35 ? 63  ARG A CA  1 
ATOM   506  C C   . ARG A 1 63  ? -8.774  -14.380 27.663 1.00 20.79 ? 63  ARG A C   1 
ATOM   507  O O   . ARG A 1 63  ? -7.769  -15.050 27.945 1.00 19.70 ? 63  ARG A O   1 
ATOM   508  C CB  . ARG A 1 63  ? -7.834  -12.137 27.063 1.00 19.72 ? 63  ARG A CB  1 
ATOM   509  C CG  . ARG A 1 63  ? -8.479  -11.012 26.333 1.00 28.74 ? 63  ARG A CG  1 
ATOM   510  C CD  . ARG A 1 63  ? -7.500  -10.268 25.457 1.00 21.83 ? 63  ARG A CD  1 
ATOM   511  N NE  . ARG A 1 63  ? -7.585  -8.843  25.720 1.00 27.49 ? 63  ARG A NE  1 
ATOM   512  C CZ  . ARG A 1 63  ? -6.903  -7.922  25.057 1.00 28.30 ? 63  ARG A CZ  1 
ATOM   513  N NH1 . ARG A 1 63  ? -6.081  -8.290  24.086 1.00 21.49 ? 63  ARG A NH1 1 
ATOM   514  N NH2 . ARG A 1 63  ? -7.049  -6.644  25.369 1.00 30.98 ? 63  ARG A NH2 1 
ATOM   515  N N   . MET A 1 64  ? -9.871  -14.890 27.103 1.00 16.31 ? 64  MET A N   1 
ATOM   516  C CA  . MET A 1 64  ? -9.999  -16.299 26.744 1.00 18.48 ? 64  MET A CA  1 
ATOM   517  C C   . MET A 1 64  ? -9.935  -16.427 25.228 1.00 19.22 ? 64  MET A C   1 
ATOM   518  O O   . MET A 1 64  ? -10.702 -15.766 24.519 1.00 22.31 ? 64  MET A O   1 
ATOM   519  C CB  . MET A 1 64  ? -11.316 -16.886 27.268 1.00 17.76 ? 64  MET A CB  1 
ATOM   520  C CG  . MET A 1 64  ? -11.529 -18.390 26.947 1.00 21.54 ? 64  MET A CG  1 
ATOM   521  S SD  . MET A 1 64  ? -13.198 -18.976 27.434 1.00 32.38 ? 64  MET A SD  1 
ATOM   522  C CE  . MET A 1 64  ? -14.206 -18.095 26.246 1.00 31.92 ? 64  MET A CE  1 
ATOM   523  N N   . TYR A 1 65  ? -9.045  -17.289 24.740 1.00 18.64 ? 65  TYR A N   1 
ATOM   524  C CA  . TYR A 1 65  ? -8.803  -17.488 23.312 1.00 21.44 ? 65  TYR A CA  1 
ATOM   525  C C   . TYR A 1 65  ? -9.237  -18.893 22.927 1.00 22.80 ? 65  TYR A C   1 
ATOM   526  O O   . TYR A 1 65  ? -8.614  -19.867 23.354 1.00 23.16 ? 65  TYR A O   1 
ATOM   527  C CB  . TYR A 1 65  ? -7.317  -17.324 22.974 1.00 18.76 ? 65  TYR A CB  1 
ATOM   528  C CG  . TYR A 1 65  ? -6.724  -15.998 23.355 1.00 21.48 ? 65  TYR A CG  1 
ATOM   529  C CD1 . TYR A 1 65  ? -6.375  -15.725 24.676 1.00 18.92 ? 65  TYR A CD1 1 
ATOM   530  C CD2 . TYR A 1 65  ? -6.497  -15.019 22.389 1.00 20.57 ? 65  TYR A CD2 1 
ATOM   531  C CE1 . TYR A 1 65  ? -5.830  -14.513 25.028 1.00 18.94 ? 65  TYR A CE1 1 
ATOM   532  C CE2 . TYR A 1 65  ? -5.944  -13.808 22.724 1.00 19.70 ? 65  TYR A CE2 1 
ATOM   533  C CZ  . TYR A 1 65  ? -5.612  -13.561 24.048 1.00 22.73 ? 65  TYR A CZ  1 
ATOM   534  O OH  . TYR A 1 65  ? -5.081  -12.353 24.397 1.00 22.25 ? 65  TYR A OH  1 
ATOM   535  N N   . ARG A 1 66  ? -10.266 -19.010 22.083 1.00 21.60 ? 66  ARG A N   1 
ATOM   536  C CA  . ARG A 1 66  ? -10.658 -20.332 21.589 1.00 19.59 ? 66  ARG A CA  1 
ATOM   537  C C   . ARG A 1 66  ? -10.182 -20.485 20.154 1.00 27.13 ? 66  ARG A C   1 
ATOM   538  O O   . ARG A 1 66  ? -10.590 -19.688 19.295 1.00 25.27 ? 66  ARG A O   1 
ATOM   539  C CB  . ARG A 1 66  ? -12.181 -20.534 21.663 1.00 21.97 ? 66  ARG A CB  1 
ATOM   540  C CG  . ARG A 1 66  ? -12.622 -21.972 21.322 1.00 27.56 ? 66  ARG A CG  1 
ATOM   541  C CD  . ARG A 1 66  ? -14.130 -22.193 21.519 1.00 28.31 ? 66  ARG A CD  1 
ATOM   542  N NE  . ARG A 1 66  ? -14.914 -21.121 20.917 1.00 33.92 ? 66  ARG A NE  1 
ATOM   543  C CZ  . ARG A 1 66  ? -15.328 -21.107 19.652 1.00 36.13 ? 66  ARG A CZ  1 
ATOM   544  N NH1 . ARG A 1 66  ? -15.047 -22.122 18.841 1.00 41.96 ? 66  ARG A NH1 1 
ATOM   545  N NH2 . ARG A 1 66  ? -16.032 -20.078 19.200 1.00 36.90 ? 66  ARG A NH2 1 
ATOM   546  N N   . PRO A 1 67  ? -9.354  -21.479 19.840 1.00 25.99 ? 67  PRO A N   1 
ATOM   547  C CA  . PRO A 1 67  ? -8.830  -21.612 18.479 1.00 29.39 ? 67  PRO A CA  1 
ATOM   548  C C   . PRO A 1 67  ? -9.836  -22.276 17.546 1.00 34.26 ? 67  PRO A C   1 
ATOM   549  O O   . PRO A 1 67  ? -10.770 -22.955 17.972 1.00 32.13 ? 67  PRO A O   1 
ATOM   550  C CB  . PRO A 1 67  ? -7.605  -22.509 18.672 1.00 27.77 ? 67  PRO A CB  1 
ATOM   551  C CG  . PRO A 1 67  ? -8.017  -23.424 19.785 1.00 28.60 ? 67  PRO A CG  1 
ATOM   552  C CD  . PRO A 1 67  ? -8.890  -22.571 20.718 1.00 24.70 ? 67  PRO A CD  1 
ATOM   553  N N   . GLU A 1 68  ? -9.596  -22.099 16.247 1.00 37.68 ? 68  GLU A N   1 
ATOM   554  C CA  . GLU A 1 68  ? -10.418 -22.745 15.228 1.00 38.79 ? 68  GLU A CA  1 
ATOM   555  C C   . GLU A 1 68  ? -10.227 -24.259 15.239 1.00 42.07 ? 68  GLU A C   1 
ATOM   556  O O   . GLU A 1 68  ? -9.151  -24.776 15.558 1.00 38.57 ? 68  GLU A O   1 
ATOM   557  C CB  . GLU A 1 68  ? -10.072 -22.207 13.836 1.00 39.33 ? 68  GLU A CB  1 
ATOM   558  C CG  . GLU A 1 68  ? -10.843 -20.972 13.426 1.00 44.82 ? 68  GLU A CG  1 
ATOM   559  C CD  . GLU A 1 68  ? -10.012 -20.012 12.587 1.00 51.90 ? 68  GLU A CD  1 
ATOM   560  O OE1 . GLU A 1 68  ? -10.271 -18.787 12.651 1.00 54.71 ? 68  GLU A OE1 1 
ATOM   561  O OE2 . GLU A 1 68  ? -9.101  -20.481 11.866 1.00 57.52 ? 68  GLU A OE2 1 
ATOM   562  N N   . GLY A 1 69  ? -11.293 -24.969 14.881 1.00 44.78 ? 69  GLY A N   1 
ATOM   563  C CA  . GLY A 1 69  ? -11.181 -26.381 14.569 1.00 44.70 ? 69  GLY A CA  1 
ATOM   564  C C   . GLY A 1 69  ? -10.830 -27.286 15.724 1.00 47.49 ? 69  GLY A C   1 
ATOM   565  O O   . GLY A 1 69  ? -10.199 -28.329 15.515 1.00 45.44 ? 69  GLY A O   1 
ATOM   566  N N   . VAL A 1 70  ? -11.207 -26.916 16.943 1.00 43.41 ? 70  VAL A N   1 
ATOM   567  C CA  . VAL A 1 70  ? -11.093 -27.801 18.094 1.00 40.67 ? 70  VAL A CA  1 
ATOM   568  C C   . VAL A 1 70  ? -12.494 -28.028 18.636 1.00 38.15 ? 70  VAL A C   1 
ATOM   569  O O   . VAL A 1 70  ? -13.350 -27.141 18.555 1.00 39.12 ? 70  VAL A O   1 
ATOM   570  C CB  . VAL A 1 70  ? -10.156 -27.234 19.182 1.00 39.59 ? 70  VAL A CB  1 
ATOM   571  C CG1 . VAL A 1 70  ? -8.785  -26.940 18.602 1.00 39.37 ? 70  VAL A CG1 1 
ATOM   572  C CG2 . VAL A 1 70  ? -10.758 -25.975 19.808 1.00 42.59 ? 70  VAL A CG2 1 
ATOM   573  N N   . GLU A 1 71  ? -12.739 -29.228 19.152 1.00 40.13 ? 71  GLU A N   1 
ATOM   574  C CA  . GLU A 1 71  ? -14.069 -29.561 19.634 1.00 43.12 ? 71  GLU A CA  1 
ATOM   575  C C   . GLU A 1 71  ? -14.020 -29.883 21.123 1.00 35.53 ? 71  GLU A C   1 
ATOM   576  O O   . GLU A 1 71  ? -12.991 -30.356 21.621 1.00 33.38 ? 71  GLU A O   1 
ATOM   577  C CB  . GLU A 1 71  ? -14.655 -30.755 18.864 1.00 45.72 ? 71  GLU A CB  1 
ATOM   578  C CG  . GLU A 1 71  ? -14.029 -32.090 19.231 1.00 50.57 ? 71  GLU A CG  1 
ATOM   579  C CD  . GLU A 1 71  ? -13.863 -33.010 18.039 1.00 61.42 ? 71  GLU A CD  1 
ATOM   580  O OE1 . GLU A 1 71  ? -14.858 -33.231 17.313 1.00 65.76 ? 71  GLU A OE1 1 
ATOM   581  O OE2 . GLU A 1 71  ? -12.732 -33.504 17.829 1.00 62.20 ? 71  GLU A OE2 1 
ATOM   582  N N   . PRO A 1 72  ? -15.105 -29.629 21.858 1.00 36.75 ? 72  PRO A N   1 
ATOM   583  C CA  . PRO A 1 72  ? -15.111 -29.907 23.303 1.00 27.86 ? 72  PRO A CA  1 
ATOM   584  C C   . PRO A 1 72  ? -15.040 -31.399 23.553 1.00 31.62 ? 72  PRO A C   1 
ATOM   585  O O   . PRO A 1 72  ? -15.382 -32.193 22.666 1.00 34.26 ? 72  PRO A O   1 
ATOM   586  C CB  . PRO A 1 72  ? -16.461 -29.335 23.779 1.00 32.24 ? 72  PRO A CB  1 
ATOM   587  C CG  . PRO A 1 72  ? -17.019 -28.561 22.624 1.00 34.71 ? 72  PRO A CG  1 
ATOM   588  C CD  . PRO A 1 72  ? -16.401 -29.106 21.386 1.00 37.35 ? 72  PRO A CD  1 
ATOM   589  N N   . PRO A 1 73  ? -14.605 -31.829 24.752 1.00 32.06 ? 73  PRO A N   1 
ATOM   590  C CA  . PRO A 1 73  ? -14.082 -30.978 25.831 1.00 27.07 ? 73  PRO A CA  1 
ATOM   591  C C   . PRO A 1 73  ? -12.682 -30.460 25.493 1.00 31.56 ? 73  PRO A C   1 
ATOM   592  O O   . PRO A 1 73  ? -11.832 -31.236 25.038 1.00 32.06 ? 73  PRO A O   1 
ATOM   593  C CB  . PRO A 1 73  ? -14.050 -31.911 27.042 1.00 26.28 ? 73  PRO A CB  1 
ATOM   594  C CG  . PRO A 1 73  ? -14.897 -33.091 26.655 1.00 35.09 ? 73  PRO A CG  1 
ATOM   595  C CD  . PRO A 1 73  ? -14.771 -33.224 25.185 1.00 32.97 ? 73  PRO A CD  1 
ATOM   596  N N   . TYR A 1 74  ? -12.454 -29.162 25.702 1.00 23.95 ? 74  TYR A N   1 
ATOM   597  C CA  . TYR A 1 74  ? -11.211 -28.563 25.231 1.00 25.27 ? 74  TYR A CA  1 
ATOM   598  C C   . TYR A 1 74  ? -10.088 -28.772 26.246 1.00 23.34 ? 74  TYR A C   1 
ATOM   599  O O   . TYR A 1 74  ? -10.320 -28.706 27.457 1.00 20.01 ? 74  TYR A O   1 
ATOM   600  C CB  . TYR A 1 74  ? -11.372 -27.065 25.005 1.00 25.68 ? 74  TYR A CB  1 
ATOM   601  C CG  . TYR A 1 74  ? -12.535 -26.625 24.152 1.00 26.23 ? 74  TYR A CG  1 
ATOM   602  C CD1 . TYR A 1 74  ? -12.564 -26.889 22.789 1.00 32.25 ? 74  TYR A CD1 1 
ATOM   603  C CD2 . TYR A 1 74  ? -13.575 -25.894 24.700 1.00 28.20 ? 74  TYR A CD2 1 
ATOM   604  C CE1 . TYR A 1 74  ? -13.619 -26.461 22.002 1.00 29.57 ? 74  TYR A CE1 1 
ATOM   605  C CE2 . TYR A 1 74  ? -14.630 -25.460 23.924 1.00 28.13 ? 74  TYR A CE2 1 
ATOM   606  C CZ  . TYR A 1 74  ? -14.645 -25.752 22.576 1.00 32.12 ? 74  TYR A CZ  1 
ATOM   607  O OH  . TYR A 1 74  ? -15.697 -25.324 21.809 1.00 37.22 ? 74  TYR A OH  1 
ATOM   608  N N   . PRO A 1 75  ? -8.862  -28.992 25.783 1.00 25.58 ? 75  PRO A N   1 
ATOM   609  C CA  . PRO A 1 75  ? -7.705  -28.745 26.645 1.00 25.31 ? 75  PRO A CA  1 
ATOM   610  C C   . PRO A 1 75  ? -7.523  -27.243 26.803 1.00 23.68 ? 75  PRO A C   1 
ATOM   611  O O   . PRO A 1 75  ? -7.993  -26.448 25.980 1.00 20.22 ? 75  PRO A O   1 
ATOM   612  C CB  . PRO A 1 75  ? -6.545  -29.385 25.881 1.00 26.96 ? 75  PRO A CB  1 
ATOM   613  C CG  . PRO A 1 75  ? -6.934  -29.230 24.441 1.00 28.98 ? 75  PRO A CG  1 
ATOM   614  C CD  . PRO A 1 75  ? -8.470  -29.308 24.399 1.00 21.73 ? 75  PRO A CD  1 
ATOM   615  N N   . ALA A 1 76  ? -6.862  -26.847 27.892 1.00 18.94 ? 76  ALA A N   1 
ATOM   616  C CA  . ALA A 1 76  ? -6.734  -25.427 28.190 1.00 18.64 ? 76  ALA A CA  1 
ATOM   617  C C   . ALA A 1 76  ? -5.377  -25.129 28.819 1.00 16.85 ? 76  ALA A C   1 
ATOM   618  O O   . ALA A 1 76  ? -4.726  -26.002 29.402 1.00 18.77 ? 76  ALA A O   1 
ATOM   619  C CB  . ALA A 1 76  ? -7.840  -24.918 29.117 1.00 16.50 ? 76  ALA A CB  1 
ATOM   620  N N   . LEU A 1 77  ? -4.970  -23.865 28.676 1.00 16.25 ? 77  LEU A N   1 
ATOM   621  C CA  . LEU A 1 77  ? -3.749  -23.324 29.266 1.00 14.72 ? 77  LEU A CA  1 
ATOM   622  C C   . LEU A 1 77  ? -4.114  -22.046 30.007 1.00 15.84 ? 77  LEU A C   1 
ATOM   623  O O   . LEU A 1 77  ? -4.655  -21.121 29.397 1.00 17.49 ? 77  LEU A O   1 
ATOM   624  C CB  . LEU A 1 77  ? -2.705  -23.024 28.177 1.00 15.32 ? 77  LEU A CB  1 
ATOM   625  C CG  . LEU A 1 77  ? -1.479  -22.235 28.631 1.00 18.06 ? 77  LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 77  ? -0.628  -23.122 29.518 1.00 14.19 ? 77  LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 77  ? -0.658  -21.705 27.434 1.00 20.10 ? 77  LEU A CD2 1 
ATOM   628  N N   . VAL A 1 78  ? -3.854  -21.999 31.313 1.00 14.93 ? 78  VAL A N   1 
ATOM   629  C CA  . VAL A 1 78  ? -3.938  -20.747 32.065 1.00 13.22 ? 78  VAL A CA  1 
ATOM   630  C C   . VAL A 1 78  ? -2.569  -20.085 31.986 1.00 16.49 ? 78  VAL A C   1 
ATOM   631  O O   . VAL A 1 78  ? -1.568  -20.659 32.438 1.00 14.81 ? 78  VAL A O   1 
ATOM   632  C CB  . VAL A 1 78  ? -4.358  -20.984 33.522 1.00 14.34 ? 78  VAL A CB  1 
ATOM   633  C CG1 . VAL A 1 78  ? -4.554  -19.645 34.227 1.00 16.21 ? 78  VAL A CG1 1 
ATOM   634  C CG2 . VAL A 1 78  ? -5.663  -21.822 33.589 1.00 17.01 ? 78  VAL A CG2 1 
ATOM   635  N N   . TYR A 1 79  ? -2.525  -18.885 31.405 1.00 16.21 ? 79  TYR A N   1 
ATOM   636  C CA  . TYR A 1 79  ? -1.287  -18.236 30.991 1.00 15.66 ? 79  TYR A CA  1 
ATOM   637  C C   . TYR A 1 79  ? -1.076  -16.946 31.771 1.00 15.74 ? 79  TYR A C   1 
ATOM   638  O O   . TYR A 1 79  ? -2.000  -16.137 31.912 1.00 15.49 ? 79  TYR A O   1 
ATOM   639  C CB  . TYR A 1 79  ? -1.310  -17.934 29.484 1.00 16.09 ? 79  TYR A CB  1 
ATOM   640  C CG  . TYR A 1 79  ? 0.035   -17.459 28.962 1.00 20.42 ? 79  TYR A CG  1 
ATOM   641  C CD1 . TYR A 1 79  ? 1.007   -18.373 28.601 1.00 18.07 ? 79  TYR A CD1 1 
ATOM   642  C CD2 . TYR A 1 79  ? 0.333   -16.103 28.858 1.00 22.68 ? 79  TYR A CD2 1 
ATOM   643  C CE1 . TYR A 1 79  ? 2.250   -17.958 28.131 1.00 24.74 ? 79  TYR A CE1 1 
ATOM   644  C CE2 . TYR A 1 79  ? 1.580   -15.679 28.398 1.00 20.54 ? 79  TYR A CE2 1 
ATOM   645  C CZ  . TYR A 1 79  ? 2.525   -16.614 28.034 1.00 22.65 ? 79  TYR A CZ  1 
ATOM   646  O OH  . TYR A 1 79  ? 3.775   -16.224 27.577 1.00 27.14 ? 79  TYR A OH  1 
ATOM   647  N N   . TYR A 1 80  ? 0.149   -16.750 32.265 1.00 13.71 ? 80  TYR A N   1 
ATOM   648  C CA  . TYR A 1 80  ? 0.530   -15.559 33.004 1.00 14.52 ? 80  TYR A CA  1 
ATOM   649  C C   . TYR A 1 80  ? 1.606   -14.829 32.212 1.00 15.11 ? 80  TYR A C   1 
ATOM   650  O O   . TYR A 1 80  ? 2.683   -15.384 31.975 1.00 14.46 ? 80  TYR A O   1 
ATOM   651  C CB  . TYR A 1 80  ? 1.035   -15.928 34.402 1.00 13.08 ? 80  TYR A CB  1 
ATOM   652  C CG  . TYR A 1 80  ? 0.089   -16.891 35.119 1.00 16.11 ? 80  TYR A CG  1 
ATOM   653  C CD1 . TYR A 1 80  ? -1.150  -16.470 35.591 1.00 14.11 ? 80  TYR A CD1 1 
ATOM   654  C CD2 . TYR A 1 80  ? 0.450   -18.222 35.313 1.00 14.94 ? 80  TYR A CD2 1 
ATOM   655  C CE1 . TYR A 1 80  ? -2.028  -17.375 36.241 1.00 15.63 ? 80  TYR A CE1 1 
ATOM   656  C CE2 . TYR A 1 80  ? -0.397  -19.120 35.959 1.00 16.61 ? 80  TYR A CE2 1 
ATOM   657  C CZ  . TYR A 1 80  ? -1.632  -18.690 36.419 1.00 15.18 ? 80  TYR A CZ  1 
ATOM   658  O OH  . TYR A 1 80  ? -2.438  -19.605 37.064 1.00 15.82 ? 80  TYR A OH  1 
ATOM   659  N N   . HIS A 1 81  ? 1.312   -13.600 31.801 1.00 17.37 ? 81  HIS A N   1 
ATOM   660  C CA  . HIS A 1 81  ? 2.260   -12.826 31.005 1.00 16.79 ? 81  HIS A CA  1 
ATOM   661  C C   . HIS A 1 81  ? 3.504   -12.458 31.822 1.00 15.44 ? 81  HIS A C   1 
ATOM   662  O O   . HIS A 1 81  ? 3.486   -12.406 33.059 1.00 16.52 ? 81  HIS A O   1 
ATOM   663  C CB  . HIS A 1 81  ? 1.602   -11.542 30.491 1.00 16.35 ? 81  HIS A CB  1 
ATOM   664  C CG  . HIS A 1 81  ? 1.288   -10.549 31.576 1.00 17.67 ? 81  HIS A CG  1 
ATOM   665  N ND1 . HIS A 1 81  ? 2.238   -9.702  32.110 1.00 16.91 ? 81  HIS A ND1 1 
ATOM   666  C CD2 . HIS A 1 81  ? 0.134   -10.270 32.224 1.00 17.00 ? 81  HIS A CD2 1 
ATOM   667  C CE1 . HIS A 1 81  ? 1.685   -8.954  33.046 1.00 14.90 ? 81  HIS A CE1 1 
ATOM   668  N NE2 . HIS A 1 81  ? 0.409   -9.280  33.138 1.00 16.98 ? 81  HIS A NE2 1 
ATOM   669  N N   . GLY A 1 82  ? 4.586   -12.157 31.100 1.00 17.01 ? 82  GLY A N   1 
ATOM   670  C CA  . GLY A 1 82  ? 5.806   -11.663 31.708 1.00 16.91 ? 82  GLY A CA  1 
ATOM   671  C C   . GLY A 1 82  ? 5.823   -10.147 31.871 1.00 20.49 ? 82  GLY A C   1 
ATOM   672  O O   . GLY A 1 82  ? 4.847   -9.442  31.616 1.00 19.48 ? 82  GLY A O   1 
ATOM   673  N N   . GLY A 1 83  ? 6.965   -9.649  32.333 1.00 18.37 ? 83  GLY A N   1 
ATOM   674  C CA  . GLY A 1 83  ? 7.111   -8.228  32.588 1.00 18.84 ? 83  GLY A CA  1 
ATOM   675  C C   . GLY A 1 83  ? 7.681   -7.918  33.958 1.00 19.14 ? 83  GLY A C   1 
ATOM   676  O O   . GLY A 1 83  ? 7.392   -6.861  34.526 1.00 17.36 ? 83  GLY A O   1 
ATOM   677  N N   . GLY A 1 84  ? 8.470   -8.838  34.514 1.00 15.06 ? 84  GLY A N   1 
ATOM   678  C CA  . GLY A 1 84  ? 9.201   -8.551  35.742 1.00 15.70 ? 84  GLY A CA  1 
ATOM   679  C C   . GLY A 1 84  ? 8.351   -8.278  36.959 1.00 18.42 ? 84  GLY A C   1 
ATOM   680  O O   . GLY A 1 84  ? 8.820   -7.625  37.898 1.00 16.32 ? 84  GLY A O   1 
ATOM   681  N N   . TRP A 1 85  ? 7.096   -8.738  36.959 1.00 15.01 ? 85  TRP A N   1 
ATOM   682  C CA  . TRP A 1 85  ? 6.103   -8.507  38.006 1.00 18.60 ? 85  TRP A CA  1 
ATOM   683  C C   . TRP A 1 85  ? 5.671   -7.047  38.111 1.00 19.00 ? 85  TRP A C   1 
ATOM   684  O O   . TRP A 1 85  ? 4.959   -6.689  39.061 1.00 19.88 ? 85  TRP A O   1 
ATOM   685  C CB  . TRP A 1 85  ? 6.591   -9.000  39.375 1.00 17.44 ? 85  TRP A CB  1 
ATOM   686  C CG  . TRP A 1 85  ? 7.035   -10.457 39.385 1.00 17.98 ? 85  TRP A CG  1 
ATOM   687  C CD1 . TRP A 1 85  ? 6.226   -11.574 39.401 1.00 19.46 ? 85  TRP A CD1 1 
ATOM   688  C CD2 . TRP A 1 85  ? 8.376   -10.936 39.393 1.00 18.34 ? 85  TRP A CD2 1 
ATOM   689  N NE1 . TRP A 1 85  ? 6.995   -12.714 39.425 1.00 18.43 ? 85  TRP A NE1 1 
ATOM   690  C CE2 . TRP A 1 85  ? 8.318   -12.351 39.417 1.00 19.84 ? 85  TRP A CE2 1 
ATOM   691  C CE3 . TRP A 1 85  ? 9.634   -10.307 39.387 1.00 18.42 ? 85  TRP A CE3 1 
ATOM   692  C CZ2 . TRP A 1 85  ? 9.466   -13.144 39.427 1.00 20.03 ? 85  TRP A CZ2 1 
ATOM   693  C CZ3 . TRP A 1 85  ? 10.767  -11.096 39.410 1.00 24.66 ? 85  TRP A CZ3 1 
ATOM   694  C CH2 . TRP A 1 85  ? 10.676  -12.501 39.425 1.00 23.47 ? 85  TRP A CH2 1 
ATOM   695  N N   . VAL A 1 86  ? 6.019   -6.209  37.132 1.00 17.63 ? 86  VAL A N   1 
ATOM   696  C CA  . VAL A 1 86  ? 5.815   -4.761  37.219 1.00 18.06 ? 86  VAL A CA  1 
ATOM   697  C C   . VAL A 1 86  ? 5.038   -4.237  36.014 1.00 16.46 ? 86  VAL A C   1 
ATOM   698  O O   . VAL A 1 86  ? 4.239   -3.309  36.149 1.00 19.67 ? 86  VAL A O   1 
ATOM   699  C CB  . VAL A 1 86  ? 7.171   -4.024  37.345 1.00 20.91 ? 86  VAL A CB  1 
ATOM   700  C CG1 . VAL A 1 86  ? 6.967   -2.505  37.338 1.00 21.42 ? 86  VAL A CG1 1 
ATOM   701  C CG2 . VAL A 1 86  ? 7.878   -4.437  38.634 1.00 16.72 ? 86  VAL A CG2 1 
ATOM   702  N N   . VAL A 1 87  ? 5.294   -4.791  34.826 1.00 18.71 ? 87  VAL A N   1 
ATOM   703  C CA  . VAL A 1 87  ? 4.634   -4.342  33.602 1.00 22.07 ? 87  VAL A CA  1 
ATOM   704  C C   . VAL A 1 87  ? 3.988   -5.518  32.876 1.00 25.52 ? 87  VAL A C   1 
ATOM   705  O O   . VAL A 1 87  ? 3.936   -6.644  33.397 1.00 19.63 ? 87  VAL A O   1 
ATOM   706  C CB  . VAL A 1 87  ? 5.623   -3.598  32.669 1.00 24.17 ? 87  VAL A CB  1 
ATOM   707  C CG1 . VAL A 1 87  ? 6.245   -2.400  33.398 1.00 22.80 ? 87  VAL A CG1 1 
ATOM   708  C CG2 . VAL A 1 87  ? 6.728   -4.524  32.155 1.00 23.21 ? 87  VAL A CG2 1 
ATOM   709  N N   . GLY A 1 88  ? 3.507   -5.265  31.662 1.00 22.57 ? 88  GLY A N   1 
ATOM   710  C CA  . GLY A 1 88  ? 2.822   -6.249  30.845 1.00 21.09 ? 88  GLY A CA  1 
ATOM   711  C C   . GLY A 1 88  ? 1.341   -6.297  31.164 1.00 20.44 ? 88  GLY A C   1 
ATOM   712  O O   . GLY A 1 88  ? 0.896   -5.924  32.248 1.00 23.99 ? 88  GLY A O   1 
ATOM   713  N N   . ASP A 1 89  ? 0.558   -6.740  30.189 1.00 23.19 ? 89  ASP A N   1 
ATOM   714  C CA  . ASP A 1 89  ? -0.883  -6.865  30.391 1.00 23.35 ? 89  ASP A CA  1 
ATOM   715  C C   . ASP A 1 89  ? -1.444  -7.766  29.297 1.00 22.50 ? 89  ASP A C   1 
ATOM   716  O O   . ASP A 1 89  ? -0.693  -8.378  28.529 1.00 22.16 ? 89  ASP A O   1 
ATOM   717  C CB  . ASP A 1 89  ? -1.563  -5.483  30.439 1.00 26.32 ? 89  ASP A CB  1 
ATOM   718  C CG  . ASP A 1 89  ? -1.399  -4.669  29.139 1.00 29.20 ? 89  ASP A CG  1 
ATOM   719  O OD1 . ASP A 1 89  ? -1.149  -5.236  28.059 1.00 24.98 ? 89  ASP A OD1 1 
ATOM   720  O OD2 . ASP A 1 89  ? -1.531  -3.430  29.202 1.00 34.63 ? 89  ASP A OD2 1 
ATOM   721  N N   . LEU A 1 90  ? -2.780  -7.814  29.195 1.00 22.41 ? 90  LEU A N   1 
ATOM   722  C CA  . LEU A 1 90  ? -3.411  -8.693  28.218 1.00 22.90 ? 90  LEU A CA  1 
ATOM   723  C C   . LEU A 1 90  ? -3.021  -8.317  26.799 1.00 21.41 ? 90  LEU A C   1 
ATOM   724  O O   . LEU A 1 90  ? -2.848  -9.195  25.948 1.00 23.79 ? 90  LEU A O   1 
ATOM   725  C CB  . LEU A 1 90  ? -4.940  -8.666  28.369 1.00 22.56 ? 90  LEU A CB  1 
ATOM   726  C CG  . LEU A 1 90  ? -5.436  -9.112  29.745 1.00 26.39 ? 90  LEU A CG  1 
ATOM   727  C CD1 . LEU A 1 90  ? -6.949  -9.099  29.774 1.00 27.61 ? 90  LEU A CD1 1 
ATOM   728  C CD2 . LEU A 1 90  ? -4.915  -10.490 30.087 1.00 25.05 ? 90  LEU A CD2 1 
ATOM   729  N N   . GLU A 1 91  ? -2.861  -7.022  26.517 1.00 24.10 ? 91  GLU A N   1 
ATOM   730  C CA  . GLU A 1 91  ? -2.567  -6.652  25.130 1.00 24.64 ? 91  GLU A CA  1 
ATOM   731  C C   . GLU A 1 91  ? -1.101  -6.900  24.763 1.00 24.06 ? 91  GLU A C   1 
ATOM   732  O O   . GLU A 1 91  ? -0.812  -7.334  23.638 1.00 21.66 ? 91  GLU A O   1 
ATOM   733  C CB  . GLU A 1 91  ? -2.961  -5.196  24.876 1.00 27.30 ? 91  GLU A CB  1 
ATOM   734  C CG  . GLU A 1 91  ? -2.839  -4.757  23.404 1.00 33.28 ? 91  GLU A CG  1 
ATOM   735  C CD  . GLU A 1 91  ? -3.790  -5.496  22.458 1.00 38.76 ? 91  GLU A CD  1 
ATOM   736  O OE1 . GLU A 1 91  ? -3.471  -5.592  21.257 1.00 38.89 ? 91  GLU A OE1 1 
ATOM   737  O OE2 . GLU A 1 91  ? -4.858  -5.974  22.907 1.00 37.03 ? 91  GLU A OE2 1 
ATOM   738  N N   . THR A 1 92  ? -0.156  -6.656  25.682 1.00 21.40 ? 92  THR A N   1 
ATOM   739  C CA  . THR A 1 92  ? 1.243   -6.878  25.315 1.00 23.55 ? 92  THR A CA  1 
ATOM   740  C C   . THR A 1 92  ? 1.486   -8.321  24.905 1.00 25.74 ? 92  THR A C   1 
ATOM   741  O O   . THR A 1 92  ? 2.315   -8.584  24.033 1.00 23.38 ? 92  THR A O   1 
ATOM   742  C CB  . THR A 1 92  ? 2.203   -6.507  26.455 1.00 24.14 ? 92  THR A CB  1 
ATOM   743  O OG1 . THR A 1 92  ? 1.919   -7.297  27.618 1.00 22.88 ? 92  THR A OG1 1 
ATOM   744  C CG2 . THR A 1 92  ? 2.107   -5.031  26.797 1.00 27.70 ? 92  THR A CG2 1 
ATOM   745  N N   . HIS A 1 93  ? 0.776   -9.272  25.508 1.00 21.01 ? 93  HIS A N   1 
ATOM   746  C CA  . HIS A 1 93  ? 1.007   -10.678 25.226 1.00 21.64 ? 93  HIS A CA  1 
ATOM   747  C C   . HIS A 1 93  ? -0.110  -11.298 24.407 1.00 21.53 ? 93  HIS A C   1 
ATOM   748  O O   . HIS A 1 93  ? -0.147  -12.524 24.241 1.00 21.69 ? 93  HIS A O   1 
ATOM   749  C CB  . HIS A 1 93  ? 1.230   -11.438 26.539 1.00 20.08 ? 93  HIS A CB  1 
ATOM   750  C CG  . HIS A 1 93  ? 2.578   -11.173 27.132 1.00 23.56 ? 93  HIS A CG  1 
ATOM   751  N ND1 . HIS A 1 93  ? 2.934   -9.938  27.635 1.00 23.22 ? 93  HIS A ND1 1 
ATOM   752  C CD2 . HIS A 1 93  ? 3.672   -11.964 27.264 1.00 23.21 ? 93  HIS A CD2 1 
ATOM   753  C CE1 . HIS A 1 93  ? 4.185   -9.986  28.065 1.00 22.18 ? 93  HIS A CE1 1 
ATOM   754  N NE2 . HIS A 1 93  ? 4.652   -11.205 27.857 1.00 24.46 ? 93  HIS A NE2 1 
ATOM   755  N N   . ASP A 1 94  ? -1.009  -10.482 23.872 1.00 19.73 ? 94  ASP A N   1 
ATOM   756  C CA  . ASP A 1 94  ? -2.090  -11.024 23.052 1.00 20.16 ? 94  ASP A CA  1 
ATOM   757  C C   . ASP A 1 94  ? -1.576  -11.820 21.856 1.00 21.21 ? 94  ASP A C   1 
ATOM   758  O O   . ASP A 1 94  ? -2.066  -12.941 21.634 1.00 19.10 ? 94  ASP A O   1 
ATOM   759  C CB  . ASP A 1 94  ? -3.015  -9.875  22.642 1.00 21.94 ? 94  ASP A CB  1 
ATOM   760  C CG  . ASP A 1 94  ? -4.228  -10.349 21.874 1.00 25.20 ? 94  ASP A CG  1 
ATOM   761  O OD1 . ASP A 1 94  ? -4.115  -10.513 20.647 1.00 26.40 ? 94  ASP A OD1 1 
ATOM   762  O OD2 . ASP A 1 94  ? -5.286  -10.560 22.504 1.00 24.52 ? 94  ASP A OD2 1 
ATOM   763  N N   . PRO A 1 95  ? -0.604  -11.341 21.065 1.00 25.19 ? 95  PRO A N   1 
ATOM   764  C CA  . PRO A 1 95  ? -0.115  -12.176 19.954 1.00 21.52 ? 95  PRO A CA  1 
ATOM   765  C C   . PRO A 1 95  ? 0.513   -13.490 20.402 1.00 21.78 ? 95  PRO A C   1 
ATOM   766  O O   . PRO A 1 95  ? 0.413   -14.490 19.680 1.00 20.82 ? 95  PRO A O   1 
ATOM   767  C CB  . PRO A 1 95  ? 0.911   -11.264 19.260 1.00 22.35 ? 95  PRO A CB  1 
ATOM   768  C CG  . PRO A 1 95  ? 0.486   -9.892  19.607 1.00 28.88 ? 95  PRO A CG  1 
ATOM   769  C CD  . PRO A 1 95  ? -0.015  -9.993  21.020 1.00 24.73 ? 95  PRO A CD  1 
ATOM   770  N N   . VAL A 1 96  ? 1.151   -13.527 21.575 1.00 21.60 ? 96  VAL A N   1 
ATOM   771  C CA  . VAL A 1 96  ? 1.709   -14.779 22.084 1.00 17.52 ? 96  VAL A CA  1 
ATOM   772  C C   . VAL A 1 96  ? 0.599   -15.795 22.359 1.00 19.13 ? 96  VAL A C   1 
ATOM   773  O O   . VAL A 1 96  ? 0.686   -16.970 21.971 1.00 19.06 ? 96  VAL A O   1 
ATOM   774  C CB  . VAL A 1 96  ? 2.553   -14.505 23.347 1.00 19.16 ? 96  VAL A CB  1 
ATOM   775  C CG1 . VAL A 1 96  ? 3.217   -15.778 23.828 1.00 22.94 ? 96  VAL A CG1 1 
ATOM   776  C CG2 . VAL A 1 96  ? 3.615   -13.460 23.061 1.00 25.18 ? 96  VAL A CG2 1 
ATOM   777  N N   . CYS A 1 97  ? -0.437  -15.370 23.087 1.00 19.55 ? 97  CYS A N   1 
ATOM   778  C CA  . CYS A 1 97  ? -1.547  -16.265 23.402 1.00 21.17 ? 97  CYS A CA  1 
ATOM   779  C C   . CYS A 1 97  ? -2.220  -16.810 22.149 1.00 19.40 ? 97  CYS A C   1 
ATOM   780  O O   . CYS A 1 97  ? -2.626  -17.982 22.115 1.00 20.37 ? 97  CYS A O   1 
ATOM   781  C CB  . CYS A 1 97  ? -2.553  -15.522 24.283 1.00 20.68 ? 97  CYS A CB  1 
ATOM   782  S SG  . CYS A 1 97  ? -1.863  -15.255 25.962 1.00 23.09 ? 97  CYS A SG  1 
ATOM   783  N N   . ARG A 1 98  ? -2.357  -15.974 21.113 1.00 19.50 ? 98  ARG A N   1 
ATOM   784  C CA  . ARG A 1 98  ? -3.015  -16.428 19.889 1.00 20.78 ? 98  ARG A CA  1 
ATOM   785  C C   . ARG A 1 98  ? -2.236  -17.560 19.228 1.00 19.42 ? 98  ARG A C   1 
ATOM   786  O O   . ARG A 1 98  ? -2.823  -18.550 18.767 1.00 22.14 ? 98  ARG A O   1 
ATOM   787  C CB  . ARG A 1 98  ? -3.194  -15.256 18.921 1.00 21.12 ? 98  ARG A CB  1 
ATOM   788  C CG  . ARG A 1 98  ? -4.257  -14.256 19.365 1.00 24.59 ? 98  ARG A CG  1 
ATOM   789  C CD  . ARG A 1 98  ? -4.211  -12.980 18.532 1.00 24.91 ? 98  ARG A CD  1 
ATOM   790  N NE  . ARG A 1 98  ? -5.368  -12.114 18.802 1.00 23.61 ? 98  ARG A NE  1 
ATOM   791  C CZ  . ARG A 1 98  ? -6.526  -12.199 18.148 1.00 23.54 ? 98  ARG A CZ  1 
ATOM   792  N NH1 . ARG A 1 98  ? -6.696  -13.115 17.199 1.00 21.88 ? 98  ARG A NH1 1 
ATOM   793  N NH2 . ARG A 1 98  ? -7.515  -11.374 18.447 1.00 24.95 ? 98  ARG A NH2 1 
ATOM   794  N N   . VAL A 1 99  ? -0.908  -17.448 19.199 1.00 20.55 ? 99  VAL A N   1 
ATOM   795  C CA  . VAL A 1 99  ? -0.083  -18.531 18.667 1.00 19.48 ? 99  VAL A CA  1 
ATOM   796  C C   . VAL A 1 99  ? -0.207  -19.773 19.543 1.00 21.61 ? 99  VAL A C   1 
ATOM   797  O O   . VAL A 1 99  ? -0.337  -20.902 19.044 1.00 20.33 ? 99  VAL A O   1 
ATOM   798  C CB  . VAL A 1 99  ? 1.384   -18.075 18.543 1.00 21.03 ? 99  VAL A CB  1 
ATOM   799  C CG1 . VAL A 1 99  ? 2.285   -19.279 18.264 1.00 20.15 ? 99  VAL A CG1 1 
ATOM   800  C CG2 . VAL A 1 99  ? 1.534   -16.995 17.450 1.00 24.05 ? 99  VAL A CG2 1 
ATOM   801  N N   . LEU A 1 100 ? -0.179  -19.586 20.865 1.00 21.09 ? 100 LEU A N   1 
ATOM   802  C CA  . LEU A 1 100 ? -0.304  -20.731 21.759 1.00 18.95 ? 100 LEU A CA  1 
ATOM   803  C C   . LEU A 1 100 ? -1.653  -21.419 21.574 1.00 18.17 ? 100 LEU A C   1 
ATOM   804  O O   . LEU A 1 100 ? -1.738  -22.651 21.590 1.00 23.88 ? 100 LEU A O   1 
ATOM   805  C CB  . LEU A 1 100 ? -0.109  -20.282 23.208 1.00 19.67 ? 100 LEU A CB  1 
ATOM   806  C CG  . LEU A 1 100 ? 1.313   -19.816 23.560 1.00 20.93 ? 100 LEU A CG  1 
ATOM   807  C CD1 . LEU A 1 100 ? 1.396   -19.370 25.003 1.00 19.77 ? 100 LEU A CD1 1 
ATOM   808  C CD2 . LEU A 1 100 ? 2.343   -20.936 23.265 1.00 17.51 ? 100 LEU A CD2 1 
ATOM   809  N N   . ALA A 1 101 ? -2.718  -20.643 21.397 1.00 20.83 ? 101 ALA A N   1 
ATOM   810  C CA  . ALA A 1 101 ? -4.030  -21.247 21.172 1.00 18.96 ? 101 ALA A CA  1 
ATOM   811  C C   . ALA A 1 101 ? -4.104  -21.912 19.797 1.00 21.19 ? 101 ALA A C   1 
ATOM   812  O O   . ALA A 1 101 ? -4.477  -23.087 19.679 1.00 24.78 ? 101 ALA A O   1 
ATOM   813  C CB  . ALA A 1 101 ? -5.120  -20.186 21.314 1.00 19.83 ? 101 ALA A CB  1 
ATOM   814  N N   . LYS A 1 102 ? -3.758  -21.167 18.747 1.00 23.73 ? 102 LYS A N   1 
ATOM   815  C CA  . LYS A 1 102 ? -3.928  -21.666 17.384 1.00 27.22 ? 102 LYS A CA  1 
ATOM   816  C C   . LYS A 1 102 ? -3.052  -22.890 17.125 1.00 25.70 ? 102 LYS A C   1 
ATOM   817  O O   . LYS A 1 102 ? -3.534  -23.931 16.658 1.00 25.87 ? 102 LYS A O   1 
ATOM   818  C CB  . LYS A 1 102 ? -3.616  -20.553 16.382 1.00 23.98 ? 102 LYS A CB  1 
ATOM   819  C CG  . LYS A 1 102 ? -3.590  -21.015 14.925 1.00 32.02 ? 102 LYS A CG  1 
ATOM   820  C CD  . LYS A 1 102 ? -3.280  -19.858 13.997 1.00 34.65 ? 102 LYS A CD  1 
ATOM   821  C CE  . LYS A 1 102 ? -3.323  -20.289 12.531 1.00 39.47 ? 102 LYS A CE  1 
ATOM   822  N NZ  . LYS A 1 102 ? -2.218  -21.236 12.216 1.00 44.56 ? 102 LYS A NZ  1 
ATOM   823  N N   . ASP A 1 103 ? -1.764  -22.794 17.433 1.00 24.33 ? 103 ASP A N   1 
ATOM   824  C CA  . ASP A 1 103 ? -0.871  -23.917 17.184 1.00 26.27 ? 103 ASP A CA  1 
ATOM   825  C C   . ASP A 1 103 ? -0.827  -24.908 18.337 1.00 31.11 ? 103 ASP A C   1 
ATOM   826  O O   . ASP A 1 103 ? -0.510  -26.082 18.113 1.00 30.37 ? 103 ASP A O   1 
ATOM   827  C CB  . ASP A 1 103 ? 0.539   -23.409 16.875 1.00 29.05 ? 103 ASP A CB  1 
ATOM   828  C CG  . ASP A 1 103 ? 0.582   -22.551 15.622 1.00 34.50 ? 103 ASP A CG  1 
ATOM   829  O OD1 . ASP A 1 103 ? -0.283  -22.740 14.739 1.00 36.48 ? 103 ASP A OD1 1 
ATOM   830  O OD2 . ASP A 1 103 ? 1.470   -21.687 15.518 1.00 35.18 ? 103 ASP A OD2 1 
ATOM   831  N N   . GLY A 1 104 ? -1.154  -24.481 19.561 1.00 25.94 ? 104 GLY A N   1 
ATOM   832  C CA  . GLY A 1 104 ? -1.270  -25.452 20.637 1.00 23.92 ? 104 GLY A CA  1 
ATOM   833  C C   . GLY A 1 104 ? -2.573  -26.227 20.659 1.00 26.77 ? 104 GLY A C   1 
ATOM   834  O O   . GLY A 1 104 ? -2.654  -27.255 21.340 1.00 21.31 ? 104 GLY A O   1 
ATOM   835  N N   . ARG A 1 105 ? -3.587  -25.761 19.922 1.00 26.68 ? 105 ARG A N   1 
ATOM   836  C CA  . ARG A 1 105 ? -4.891  -26.435 19.846 1.00 28.49 ? 105 ARG A CA  1 
ATOM   837  C C   . ARG A 1 105 ? -5.572  -26.463 21.211 1.00 25.09 ? 105 ARG A C   1 
ATOM   838  O O   . ARG A 1 105 ? -6.151  -27.473 21.610 1.00 28.76 ? 105 ARG A O   1 
ATOM   839  C CB  . ARG A 1 105 ? -4.754  -27.857 19.292 1.00 28.50 ? 105 ARG A CB  1 
ATOM   840  C CG  . ARG A 1 105 ? -3.999  -27.934 17.985 1.00 32.44 ? 105 ARG A CG  1 
ATOM   841  C CD  . ARG A 1 105 ? -4.922  -27.691 16.810 1.00 45.11 ? 105 ARG A CD  1 
ATOM   842  N NE  . ARG A 1 105 ? -4.977  -26.287 16.448 1.00 43.88 ? 105 ARG A NE  1 
ATOM   843  C CZ  . ARG A 1 105 ? -5.997  -25.716 15.810 1.00 46.32 ? 105 ARG A CZ  1 
ATOM   844  N NH1 . ARG A 1 105 ? -7.066  -26.437 15.469 1.00 48.59 ? 105 ARG A NH1 1 
ATOM   845  N NH2 . ARG A 1 105 ? -5.947  -24.418 15.518 1.00 39.82 ? 105 ARG A NH2 1 
ATOM   846  N N   . ALA A 1 106 ? -5.496  -25.348 21.937 1.00 21.87 ? 106 ALA A N   1 
ATOM   847  C CA  . ALA A 1 106 ? -5.987  -25.279 23.308 1.00 22.60 ? 106 ALA A CA  1 
ATOM   848  C C   . ALA A 1 106 ? -6.659  -23.935 23.544 1.00 19.59 ? 106 ALA A C   1 
ATOM   849  O O   . ALA A 1 106 ? -6.297  -22.926 22.930 1.00 19.68 ? 106 ALA A O   1 
ATOM   850  C CB  . ALA A 1 106 ? -4.846  -25.465 24.325 1.00 20.92 ? 106 ALA A CB  1 
ATOM   851  N N   . VAL A 1 107 ? -7.647  -23.930 24.441 1.00 20.70 ? 107 VAL A N   1 
ATOM   852  C CA  . VAL A 1 107 ? -8.207  -22.675 24.915 1.00 18.61 ? 107 VAL A CA  1 
ATOM   853  C C   . VAL A 1 107 ? -7.207  -22.045 25.869 1.00 18.94 ? 107 VAL A C   1 
ATOM   854  O O   . VAL A 1 107 ? -6.755  -22.690 26.822 1.00 22.28 ? 107 VAL A O   1 
ATOM   855  C CB  . VAL A 1 107 ? -9.558  -22.908 25.608 1.00 18.32 ? 107 VAL A CB  1 
ATOM   856  C CG1 . VAL A 1 107 ? -10.067 -21.598 26.201 1.00 17.69 ? 107 VAL A CG1 1 
ATOM   857  C CG2 . VAL A 1 107 ? -10.578 -23.461 24.613 1.00 21.53 ? 107 VAL A CG2 1 
ATOM   858  N N   . VAL A 1 108 ? -6.864  -20.784 25.635 1.00 15.43 ? 108 VAL A N   1 
ATOM   859  C CA  . VAL A 1 108 ? -5.912  -20.074 26.492 1.00 15.30 ? 108 VAL A CA  1 
ATOM   860  C C   . VAL A 1 108 ? -6.666  -19.019 27.280 1.00 16.02 ? 108 VAL A C   1 
ATOM   861  O O   . VAL A 1 108 ? -7.447  -18.247 26.709 1.00 18.31 ? 108 VAL A O   1 
ATOM   862  C CB  . VAL A 1 108 ? -4.777  -19.425 25.685 1.00 17.58 ? 108 VAL A CB  1 
ATOM   863  C CG1 . VAL A 1 108 ? -3.787  -18.699 26.646 1.00 17.81 ? 108 VAL A CG1 1 
ATOM   864  C CG2 . VAL A 1 108 ? -4.063  -20.484 24.848 1.00 17.70 ? 108 VAL A CG2 1 
ATOM   865  N N   . PHE A 1 109 ? -6.441  -18.999 28.593 1.00 14.34 ? 109 PHE A N   1 
ATOM   866  C CA  . PHE A 1 109 ? -6.954  -17.969 29.494 1.00 16.16 ? 109 PHE A CA  1 
ATOM   867  C C   . PHE A 1 109 ? -5.765  -17.136 29.947 1.00 16.78 ? 109 PHE A C   1 
ATOM   868  O O   . PHE A 1 109 ? -4.965  -17.604 30.767 1.00 15.91 ? 109 PHE A O   1 
ATOM   869  C CB  . PHE A 1 109 ? -7.619  -18.593 30.714 1.00 13.78 ? 109 PHE A CB  1 
ATOM   870  C CG  . PHE A 1 109 ? -8.843  -19.361 30.409 1.00 15.87 ? 109 PHE A CG  1 
ATOM   871  C CD1 . PHE A 1 109 ? -8.763  -20.664 29.953 1.00 14.86 ? 109 PHE A CD1 1 
ATOM   872  C CD2 . PHE A 1 109 ? -10.094 -18.798 30.633 1.00 18.00 ? 109 PHE A CD2 1 
ATOM   873  C CE1 . PHE A 1 109 ? -9.919  -21.399 29.693 1.00 16.56 ? 109 PHE A CE1 1 
ATOM   874  C CE2 . PHE A 1 109 ? -11.253 -19.527 30.387 1.00 18.13 ? 109 PHE A CE2 1 
ATOM   875  C CZ  . PHE A 1 109 ? -11.166 -20.819 29.908 1.00 17.52 ? 109 PHE A CZ  1 
ATOM   876  N N   . SER A 1 110 ? -5.650  -15.917 29.422 1.00 17.14 ? 110 SER A N   1 
ATOM   877  C CA  . SER A 1 110 ? -4.578  -15.002 29.806 1.00 17.72 ? 110 SER A CA  1 
ATOM   878  C C   . SER A 1 110 ? -5.046  -14.152 30.983 1.00 18.61 ? 110 SER A C   1 
ATOM   879  O O   . SER A 1 110 ? -6.076  -13.479 30.890 1.00 19.35 ? 110 SER A O   1 
ATOM   880  C CB  . SER A 1 110 ? -4.190  -14.117 28.621 1.00 18.57 ? 110 SER A CB  1 
ATOM   881  O OG  . SER A 1 110 ? -3.038  -13.346 28.928 1.00 20.88 ? 110 SER A OG  1 
ATOM   882  N N   . VAL A 1 111 ? -4.301  -14.182 32.086 1.00 17.76 ? 111 VAL A N   1 
ATOM   883  C CA  . VAL A 1 111 ? -4.758  -13.645 33.368 1.00 16.55 ? 111 VAL A CA  1 
ATOM   884  C C   . VAL A 1 111 ? -3.975  -12.382 33.695 1.00 17.86 ? 111 VAL A C   1 
ATOM   885  O O   . VAL A 1 111 ? -2.739  -12.399 33.706 1.00 18.19 ? 111 VAL A O   1 
ATOM   886  C CB  . VAL A 1 111 ? -4.594  -14.678 34.497 1.00 17.52 ? 111 VAL A CB  1 
ATOM   887  C CG1 . VAL A 1 111 ? -4.879  -14.033 35.852 1.00 17.15 ? 111 VAL A CG1 1 
ATOM   888  C CG2 . VAL A 1 111 ? -5.516  -15.862 34.260 1.00 16.47 ? 111 VAL A CG2 1 
ATOM   889  N N   . ASP A 1 112 ? -4.697  -11.301 34.001 1.00 17.93 ? 112 ASP A N   1 
ATOM   890  C CA  . ASP A 1 112 ? -4.109  -10.013 34.400 1.00 20.01 ? 112 ASP A CA  1 
ATOM   891  C C   . ASP A 1 112 ? -3.935  -9.973  35.915 1.00 21.82 ? 112 ASP A C   1 
ATOM   892  O O   . ASP A 1 112 ? -4.772  -9.453  36.653 1.00 23.41 ? 112 ASP A O   1 
ATOM   893  C CB  . ASP A 1 112 ? -4.992  -8.855  33.952 1.00 23.51 ? 112 ASP A CB  1 
ATOM   894  C CG  . ASP A 1 112 ? -4.232  -7.780  33.219 1.00 32.91 ? 112 ASP A CG  1 
ATOM   895  O OD1 . ASP A 1 112 ? -3.096  -8.037  32.752 1.00 38.22 ? 112 ASP A OD1 1 
ATOM   896  O OD2 . ASP A 1 112 ? -4.787  -6.666  33.126 1.00 41.80 ? 112 ASP A OD2 1 
ATOM   897  N N   . TYR A 1 113 ? -2.804  -10.501 36.384 1.00 18.10 ? 113 TYR A N   1 
ATOM   898  C CA  . TYR A 1 113 ? -2.545  -10.501 37.813 1.00 17.87 ? 113 TYR A CA  1 
ATOM   899  C C   . TYR A 1 113 ? -2.085  -9.116  38.281 1.00 13.58 ? 113 TYR A C   1 
ATOM   900  O O   . TYR A 1 113 ? -1.666  -8.275  37.489 1.00 23.12 ? 113 TYR A O   1 
ATOM   901  C CB  . TYR A 1 113 ? -1.497  -11.562 38.154 1.00 17.53 ? 113 TYR A CB  1 
ATOM   902  C CG  . TYR A 1 113 ? -0.216  -11.414 37.370 1.00 15.18 ? 113 TYR A CG  1 
ATOM   903  C CD1 . TYR A 1 113 ? 0.836   -10.642 37.872 1.00 16.21 ? 113 TYR A CD1 1 
ATOM   904  C CD2 . TYR A 1 113 ? -0.047  -12.058 36.143 1.00 15.76 ? 113 TYR A CD2 1 
ATOM   905  C CE1 . TYR A 1 113 ? 2.031   -10.506 37.174 1.00 17.02 ? 113 TYR A CE1 1 
ATOM   906  C CE2 . TYR A 1 113 ? 1.142   -11.924 35.418 1.00 14.76 ? 113 TYR A CE2 1 
ATOM   907  C CZ  . TYR A 1 113 ? 2.175   -11.143 35.943 1.00 15.23 ? 113 TYR A CZ  1 
ATOM   908  O OH  . TYR A 1 113 ? 3.354   -10.998 35.252 1.00 17.24 ? 113 TYR A OH  1 
ATOM   909  N N   . ARG A 1 114 ? -2.180  -8.884  39.591 1.00 19.07 ? 114 ARG A N   1 
ATOM   910  C CA  . ARG A 1 114 ? -1.823  -7.584  40.151 1.00 19.06 ? 114 ARG A CA  1 
ATOM   911  C C   . ARG A 1 114 ? -0.313  -7.367  40.074 1.00 19.31 ? 114 ARG A C   1 
ATOM   912  O O   . ARG A 1 114 ? 0.479   -8.305  40.221 1.00 17.35 ? 114 ARG A O   1 
ATOM   913  C CB  . ARG A 1 114 ? -2.308  -7.471  41.602 1.00 16.18 ? 114 ARG A CB  1 
ATOM   914  C CG  . ARG A 1 114 ? -3.855  -7.235  41.713 1.00 17.41 ? 114 ARG A CG  1 
ATOM   915  C CD  . ARG A 1 114 ? -4.355  -7.416  43.157 1.00 19.41 ? 114 ARG A CD  1 
ATOM   916  N NE  . ARG A 1 114 ? -4.013  -8.731  43.705 1.00 16.93 ? 114 ARG A NE  1 
ATOM   917  C CZ  . ARG A 1 114 ? -4.116  -9.048  44.994 1.00 21.97 ? 114 ARG A CZ  1 
ATOM   918  N NH1 . ARG A 1 114 ? -4.555  -8.142  45.855 1.00 24.55 ? 114 ARG A NH1 1 
ATOM   919  N NH2 . ARG A 1 114 ? -3.784  -10.259 45.427 1.00 20.55 ? 114 ARG A NH2 1 
ATOM   920  N N   . LEU A 1 115 ? 0.077   -6.113  39.854 1.00 17.61 ? 115 LEU A N   1 
ATOM   921  C CA  . LEU A 1 115 ? 1.457   -5.737  39.562 1.00 19.55 ? 115 LEU A CA  1 
ATOM   922  C C   . LEU A 1 115 ? 2.086   -4.991  40.734 1.00 20.90 ? 115 LEU A C   1 
ATOM   923  O O   . LEU A 1 115 ? 1.403   -4.287  41.483 1.00 20.11 ? 115 LEU A O   1 
ATOM   924  C CB  . LEU A 1 115 ? 1.526   -4.868  38.299 1.00 20.38 ? 115 LEU A CB  1 
ATOM   925  C CG  . LEU A 1 115 ? 0.998   -5.530  37.022 1.00 23.39 ? 115 LEU A CG  1 
ATOM   926  C CD1 . LEU A 1 115 ? 0.926   -4.548  35.854 1.00 23.48 ? 115 LEU A CD1 1 
ATOM   927  C CD2 . LEU A 1 115 ? 1.843   -6.729  36.649 1.00 20.93 ? 115 LEU A CD2 1 
ATOM   928  N N   . ALA A 1 116 ? 3.405   -5.185  40.904 1.00 19.85 ? 116 ALA A N   1 
ATOM   929  C CA  . ALA A 1 116 ? 4.222   -4.453  41.860 1.00 18.09 ? 116 ALA A CA  1 
ATOM   930  C C   . ALA A 1 116 ? 4.668   -3.121  41.256 1.00 21.50 ? 116 ALA A C   1 
ATOM   931  O O   . ALA A 1 116 ? 4.732   -2.981  40.032 1.00 18.55 ? 116 ALA A O   1 
ATOM   932  C CB  . ALA A 1 116 ? 5.455   -5.287  42.235 1.00 17.18 ? 116 ALA A CB  1 
ATOM   933  N N   . PRO A 1 117 ? 5.046   -2.131  42.091 1.00 20.07 ? 117 PRO A N   1 
ATOM   934  C CA  . PRO A 1 117 ? 5.131   -2.115  43.553 1.00 20.81 ? 117 PRO A CA  1 
ATOM   935  C C   . PRO A 1 117 ? 3.803   -1.816  44.226 1.00 19.12 ? 117 PRO A C   1 
ATOM   936  O O   . PRO A 1 117 ? 3.734   -1.882  45.451 1.00 21.37 ? 117 PRO A O   1 
ATOM   937  C CB  . PRO A 1 117 ? 6.135   -0.986  43.829 1.00 24.13 ? 117 PRO A CB  1 
ATOM   938  C CG  . PRO A 1 117 ? 5.872   -0.020  42.724 1.00 22.33 ? 117 PRO A CG  1 
ATOM   939  C CD  . PRO A 1 117 ? 5.602   -0.890  41.512 1.00 24.29 ? 117 PRO A CD  1 
ATOM   940  N N   . GLU A 1 118 ? 2.765   -1.499  43.445 1.00 22.05 ? 118 GLU A N   1 
ATOM   941  C CA  . GLU A 1 118 ? 1.461   -1.235  44.046 1.00 24.38 ? 118 GLU A CA  1 
ATOM   942  C C   . GLU A 1 118 ? 0.971   -2.440  44.843 1.00 26.58 ? 118 GLU A C   1 
ATOM   943  O O   . GLU A 1 118 ? 0.465   -2.287  45.959 1.00 20.36 ? 118 GLU A O   1 
ATOM   944  C CB  . GLU A 1 118 ? 0.449   -0.843  42.964 1.00 25.81 ? 118 GLU A CB  1 
ATOM   945  C CG  . GLU A 1 118 ? 0.736   0.523   42.303 1.00 31.05 ? 118 GLU A CG  1 
ATOM   946  C CD  . GLU A 1 118 ? 1.755   0.456   41.157 1.00 33.92 ? 118 GLU A CD  1 
ATOM   947  O OE1 . GLU A 1 118 ? 2.194   -0.656  40.782 1.00 30.01 ? 118 GLU A OE1 1 
ATOM   948  O OE2 . GLU A 1 118 ? 2.123   1.531   40.623 1.00 34.23 ? 118 GLU A OE2 1 
ATOM   949  N N   . HIS A 1 119 ? 1.149   -3.648  44.303 1.00 19.96 ? 119 HIS A N   1 
ATOM   950  C CA  . HIS A 1 119 ? 0.790   -4.891  44.988 1.00 21.53 ? 119 HIS A CA  1 
ATOM   951  C C   . HIS A 1 119 ? 2.038   -5.773  45.037 1.00 20.23 ? 119 HIS A C   1 
ATOM   952  O O   . HIS A 1 119 ? 2.365   -6.460  44.067 1.00 16.85 ? 119 HIS A O   1 
ATOM   953  C CB  . HIS A 1 119 ? -0.386  -5.562  44.278 1.00 18.09 ? 119 HIS A CB  1 
ATOM   954  C CG  . HIS A 1 119 ? -1.534  -4.624  44.056 1.00 20.50 ? 119 HIS A CG  1 
ATOM   955  N ND1 . HIS A 1 119 ? -2.445  -4.322  45.047 1.00 22.81 ? 119 HIS A ND1 1 
ATOM   956  C CD2 . HIS A 1 119 ? -1.870  -3.861  42.990 1.00 21.43 ? 119 HIS A CD2 1 
ATOM   957  C CE1 . HIS A 1 119 ? -3.319  -3.440  44.586 1.00 24.69 ? 119 HIS A CE1 1 
ATOM   958  N NE2 . HIS A 1 119 ? -2.988  -3.139  43.342 1.00 24.91 ? 119 HIS A NE2 1 
ATOM   959  N N   . LYS A 1 120 ? 2.742   -5.730  46.159 1.00 19.64 ? 120 LYS A N   1 
ATOM   960  C CA  . LYS A 1 120 ? 4.007   -6.426  46.284 1.00 22.06 ? 120 LYS A CA  1 
ATOM   961  C C   . LYS A 1 120 ? 3.771   -7.919  46.484 1.00 21.85 ? 120 LYS A C   1 
ATOM   962  O O   . LYS A 1 120 ? 2.645   -8.372  46.704 1.00 18.13 ? 120 LYS A O   1 
ATOM   963  C CB  . LYS A 1 120 ? 4.823   -5.843  47.433 1.00 22.19 ? 120 LYS A CB  1 
ATOM   964  C CG  . LYS A 1 120 ? 5.530   -4.535  47.051 1.00 27.34 ? 120 LYS A CG  1 
ATOM   965  C CD  . LYS A 1 120 ? 6.699   -4.242  47.961 1.00 26.06 ? 120 LYS A CD  1 
ATOM   966  C CE  . LYS A 1 120 ? 7.400   -2.955  47.543 1.00 27.96 ? 120 LYS A CE  1 
ATOM   967  N NZ  . LYS A 1 120 ? 8.647   -3.299  46.836 1.00 22.46 ? 120 LYS A NZ  1 
ATOM   968  N N   . PHE A 1 121 ? 4.853   -8.676  46.343 1.00 18.83 ? 121 PHE A N   1 
ATOM   969  C CA  . PHE A 1 121 ? 4.867   -10.093 46.677 1.00 17.95 ? 121 PHE A CA  1 
ATOM   970  C C   . PHE A 1 121 ? 4.146   -10.313 48.008 1.00 21.36 ? 121 PHE A C   1 
ATOM   971  O O   . PHE A 1 121 ? 4.352   -9.542  48.950 1.00 18.28 ? 121 PHE A O   1 
ATOM   972  C CB  . PHE A 1 121 ? 6.331   -10.544 46.766 1.00 16.54 ? 121 PHE A CB  1 
ATOM   973  C CG  . PHE A 1 121 ? 6.533   -11.942 47.277 1.00 17.74 ? 121 PHE A CG  1 
ATOM   974  C CD1 . PHE A 1 121 ? 6.467   -13.025 46.409 1.00 15.08 ? 121 PHE A CD1 1 
ATOM   975  C CD2 . PHE A 1 121 ? 6.805   -12.173 48.627 1.00 23.14 ? 121 PHE A CD2 1 
ATOM   976  C CE1 . PHE A 1 121 ? 6.671   -14.328 46.880 1.00 18.05 ? 121 PHE A CE1 1 
ATOM   977  C CE2 . PHE A 1 121 ? 7.001   -13.470 49.108 1.00 26.35 ? 121 PHE A CE2 1 
ATOM   978  C CZ  . PHE A 1 121 ? 6.929   -14.549 48.228 1.00 20.57 ? 121 PHE A CZ  1 
ATOM   979  N N   . PRO A 1 122 ? 3.295   -11.346 48.134 1.00 18.99 ? 122 PRO A N   1 
ATOM   980  C CA  . PRO A 1 122 ? 2.954   -12.397 47.184 1.00 18.44 ? 122 PRO A CA  1 
ATOM   981  C C   . PRO A 1 122 ? 1.621   -12.179 46.461 1.00 18.86 ? 122 PRO A C   1 
ATOM   982  O O   . PRO A 1 122 ? 0.964   -13.183 46.164 1.00 18.76 ? 122 PRO A O   1 
ATOM   983  C CB  . PRO A 1 122 ? 2.860   -13.623 48.088 1.00 22.07 ? 122 PRO A CB  1 
ATOM   984  C CG  . PRO A 1 122 ? 2.162   -13.052 49.315 1.00 21.62 ? 122 PRO A CG  1 
ATOM   985  C CD  . PRO A 1 122 ? 2.645   -11.599 49.437 1.00 21.46 ? 122 PRO A CD  1 
ATOM   986  N N   . ALA A 1 123 ? 1.232   -10.924 46.181 1.00 18.82 ? 123 ALA A N   1 
ATOM   987  C CA  . ALA A 1 123 ? -0.063  -10.667 45.546 1.00 17.82 ? 123 ALA A CA  1 
ATOM   988  C C   . ALA A 1 123 ? -0.208  -11.421 44.224 1.00 18.02 ? 123 ALA A C   1 
ATOM   989  O O   . ALA A 1 123 ? -1.223  -12.082 43.992 1.00 18.57 ? 123 ALA A O   1 
ATOM   990  C CB  . ALA A 1 123 ? -0.268  -9.162  45.320 1.00 16.86 ? 123 ALA A CB  1 
ATOM   991  N N   . ALA A 1 124 ? 0.785   -11.311 43.331 1.00 16.63 ? 124 ALA A N   1 
ATOM   992  C CA  . ALA A 1 124 ? 0.705   -11.982 42.030 1.00 17.13 ? 124 ALA A CA  1 
ATOM   993  C C   . ALA A 1 124 ? 0.595   -13.497 42.172 1.00 16.88 ? 124 ALA A C   1 
ATOM   994  O O   . ALA A 1 124 ? -0.101  -14.149 41.387 1.00 16.23 ? 124 ALA A O   1 
ATOM   995  C CB  . ALA A 1 124 ? 1.926   -11.640 41.178 1.00 18.04 ? 124 ALA A CB  1 
ATOM   996  N N   . VAL A 1 125 ? 1.304   -14.075 43.143 1.00 14.34 ? 125 VAL A N   1 
ATOM   997  C CA  . VAL A 1 125 ? 1.248   -15.518 43.379 1.00 16.43 ? 125 VAL A CA  1 
ATOM   998  C C   . VAL A 1 125 ? -0.161  -15.939 43.790 1.00 15.28 ? 125 VAL A C   1 
ATOM   999  O O   . VAL A 1 125 ? -0.711  -16.918 43.277 1.00 15.42 ? 125 VAL A O   1 
ATOM   1000 C CB  . VAL A 1 125 ? 2.273   -15.921 44.452 1.00 18.09 ? 125 VAL A CB  1 
ATOM   1001 C CG1 . VAL A 1 125 ? 2.027   -17.375 44.901 1.00 17.90 ? 125 VAL A CG1 1 
ATOM   1002 C CG2 . VAL A 1 125 ? 3.678   -15.714 43.923 1.00 16.33 ? 125 VAL A CG2 1 
ATOM   1003 N N   . GLU A 1 126 ? -0.748  -15.219 44.741 1.00 16.51 ? 126 GLU A N   1 
ATOM   1004 C CA  . GLU A 1 126 ? -2.119  -15.500 45.146 1.00 18.68 ? 126 GLU A CA  1 
ATOM   1005 C C   . GLU A 1 126 ? -3.076  -15.350 43.969 1.00 19.05 ? 126 GLU A C   1 
ATOM   1006 O O   . GLU A 1 126 ? -3.963  -16.185 43.780 1.00 18.01 ? 126 GLU A O   1 
ATOM   1007 C CB  . GLU A 1 126 ? -2.525  -14.575 46.295 1.00 22.27 ? 126 GLU A CB  1 
ATOM   1008 C CG  . GLU A 1 126 ? -1.742  -14.787 47.589 1.00 30.14 ? 126 GLU A CG  1 
ATOM   1009 C CD  . GLU A 1 126 ? -2.095  -16.099 48.295 1.00 39.80 ? 126 GLU A CD  1 
ATOM   1010 O OE1 . GLU A 1 126 ? -1.251  -16.594 49.076 1.00 43.85 ? 126 GLU A OE1 1 
ATOM   1011 O OE2 . GLU A 1 126 ? -3.207  -16.640 48.073 1.00 42.26 ? 126 GLU A OE2 1 
ATOM   1012 N N   . ASP A 1 127 ? -2.897  -14.301 43.154 1.00 16.44 ? 127 ASP A N   1 
ATOM   1013 C CA  . ASP A 1 127 ? -3.740  -14.127 41.971 1.00 16.07 ? 127 ASP A CA  1 
ATOM   1014 C C   . ASP A 1 127 ? -3.599  -15.290 41.001 1.00 16.80 ? 127 ASP A C   1 
ATOM   1015 O O   . ASP A 1 127 ? -4.597  -15.770 40.438 1.00 16.27 ? 127 ASP A O   1 
ATOM   1016 C CB  . ASP A 1 127 ? -3.390  -12.816 41.265 1.00 15.04 ? 127 ASP A CB  1 
ATOM   1017 C CG  . ASP A 1 127 ? -3.841  -11.602 42.048 1.00 21.23 ? 127 ASP A CG  1 
ATOM   1018 O OD1 . ASP A 1 127 ? -4.609  -11.759 43.036 1.00 19.96 ? 127 ASP A OD1 1 
ATOM   1019 O OD2 . ASP A 1 127 ? -3.434  -10.493 41.676 1.00 17.35 ? 127 ASP A OD2 1 
ATOM   1020 N N   . ALA A 1 128 ? -2.363  -15.735 40.775 1.00 13.98 ? 128 ALA A N   1 
ATOM   1021 C CA  . ALA A 1 128 ? -2.102  -16.781 39.790 1.00 17.00 ? 128 ALA A CA  1 
ATOM   1022 C C   . ALA A 1 128 ? -2.770  -18.087 40.200 1.00 18.40 ? 128 ALA A C   1 
ATOM   1023 O O   . ALA A 1 128 ? -3.413  -18.758 39.378 1.00 15.53 ? 128 ALA A O   1 
ATOM   1024 C CB  . ALA A 1 128 ? -0.585  -16.968 39.625 1.00 14.30 ? 128 ALA A CB  1 
ATOM   1025 N N   . TYR A 1 129 ? -2.642  -18.456 41.478 1.00 15.36 ? 129 TYR A N   1 
ATOM   1026 C CA  . TYR A 1 129 ? -3.306  -19.668 41.951 1.00 17.31 ? 129 TYR A CA  1 
ATOM   1027 C C   . TYR A 1 129 ? -4.822  -19.489 41.993 1.00 16.13 ? 129 TYR A C   1 
ATOM   1028 O O   . TYR A 1 129 ? -5.572  -20.383 41.578 1.00 16.19 ? 129 TYR A O   1 
ATOM   1029 C CB  . TYR A 1 129 ? -2.795  -20.081 43.338 1.00 18.38 ? 129 TYR A CB  1 
ATOM   1030 C CG  . TYR A 1 129 ? -3.545  -21.312 43.842 1.00 17.93 ? 129 TYR A CG  1 
ATOM   1031 C CD1 . TYR A 1 129 ? -3.149  -22.587 43.466 1.00 22.59 ? 129 TYR A CD1 1 
ATOM   1032 C CD2 . TYR A 1 129 ? -4.678  -21.188 44.649 1.00 21.33 ? 129 TYR A CD2 1 
ATOM   1033 C CE1 . TYR A 1 129 ? -3.851  -23.718 43.893 1.00 20.53 ? 129 TYR A CE1 1 
ATOM   1034 C CE2 . TYR A 1 129 ? -5.387  -22.313 45.085 1.00 21.83 ? 129 TYR A CE2 1 
ATOM   1035 C CZ  . TYR A 1 129 ? -4.966  -23.568 44.707 1.00 21.88 ? 129 TYR A CZ  1 
ATOM   1036 O OH  . TYR A 1 129 ? -5.667  -24.683 45.126 1.00 22.44 ? 129 TYR A OH  1 
ATOM   1037 N N   . ASP A 1 130 ? -5.297  -18.355 42.525 1.00 15.27 ? 130 ASP A N   1 
ATOM   1038 C CA  . ASP A 1 130 ? -6.739  -18.167 42.665 1.00 17.67 ? 130 ASP A CA  1 
ATOM   1039 C C   . ASP A 1 130 ? -7.433  -18.112 41.313 1.00 17.62 ? 130 ASP A C   1 
ATOM   1040 O O   . ASP A 1 130 ? -8.581  -18.555 41.187 1.00 13.97 ? 130 ASP A O   1 
ATOM   1041 C CB  . ASP A 1 130 ? -7.035  -16.893 43.458 1.00 17.34 ? 130 ASP A CB  1 
ATOM   1042 C CG  . ASP A 1 130 ? -6.679  -17.030 44.917 1.00 21.93 ? 130 ASP A CG  1 
ATOM   1043 O OD1 . ASP A 1 130 ? -6.383  -18.168 45.357 1.00 22.31 ? 130 ASP A OD1 1 
ATOM   1044 O OD2 . ASP A 1 130 ? -6.673  -16.005 45.618 1.00 26.86 ? 130 ASP A OD2 1 
ATOM   1045 N N   . ALA A 1 131 ? -6.756  -17.572 40.292 1.00 13.07 ? 131 ALA A N   1 
ATOM   1046 C CA  . ALA A 1 131 ? -7.322  -17.561 38.946 1.00 15.47 ? 131 ALA A CA  1 
ATOM   1047 C C   . ALA A 1 131 ? -7.362  -18.961 38.338 1.00 13.51 ? 131 ALA A C   1 
ATOM   1048 O O   . ALA A 1 131 ? -8.349  -19.328 37.686 1.00 14.04 ? 131 ALA A O   1 
ATOM   1049 C CB  . ALA A 1 131 ? -6.530  -16.610 38.046 1.00 15.81 ? 131 ALA A CB  1 
ATOM   1050 N N   . LEU A 1 132 ? -6.303  -19.766 38.528 1.00 13.58 ? 132 LEU A N   1 
ATOM   1051 C CA  . LEU A 1 132 ? -6.376  -21.152 38.068 1.00 13.29 ? 132 LEU A CA  1 
ATOM   1052 C C   . LEU A 1 132 ? -7.514  -21.896 38.755 1.00 16.44 ? 132 LEU A C   1 
ATOM   1053 O O   . LEU A 1 132 ? -8.260  -22.651 38.113 1.00 14.32 ? 132 LEU A O   1 
ATOM   1054 C CB  . LEU A 1 132 ? -5.061  -21.884 38.334 1.00 16.50 ? 132 LEU A CB  1 
ATOM   1055 C CG  . LEU A 1 132 ? -5.146  -23.410 38.198 1.00 17.57 ? 132 LEU A CG  1 
ATOM   1056 C CD1 . LEU A 1 132 ? -5.316  -23.847 36.724 1.00 14.90 ? 132 LEU A CD1 1 
ATOM   1057 C CD2 . LEU A 1 132 ? -3.890  -24.062 38.809 1.00 18.26 ? 132 LEU A CD2 1 
ATOM   1058 N N   . GLN A 1 133 ? -7.655  -21.705 40.065 1.00 13.34 ? 133 GLN A N   1 
ATOM   1059 C CA  . GLN A 1 133 ? -8.740  -22.371 40.782 1.00 15.23 ? 133 GLN A CA  1 
ATOM   1060 C C   . GLN A 1 133 ? -10.105 -21.908 40.269 1.00 17.15 ? 133 GLN A C   1 
ATOM   1061 O O   . GLN A 1 133 ? -11.030 -22.720 40.103 1.00 18.97 ? 133 GLN A O   1 
ATOM   1062 C CB  . GLN A 1 133 ? -8.604  -22.092 42.273 1.00 15.58 ? 133 GLN A CB  1 
ATOM   1063 C CG  . GLN A 1 133 ? -9.706  -22.720 43.128 1.00 24.09 ? 133 GLN A CG  1 
ATOM   1064 C CD  . GLN A 1 133 ? -9.509  -22.397 44.585 1.00 32.17 ? 133 GLN A CD  1 
ATOM   1065 O OE1 . GLN A 1 133 ? -9.522  -21.225 44.975 1.00 35.83 ? 133 GLN A OE1 1 
ATOM   1066 N NE2 . GLN A 1 133 ? -9.273  -23.424 45.397 1.00 33.33 ? 133 GLN A NE2 1 
ATOM   1067 N N   . TRP A 1 134 ? -10.245 -20.606 40.000 1.00 14.69 ? 134 TRP A N   1 
ATOM   1068 C CA  . TRP A 1 134 ? -11.524 -20.073 39.518 1.00 17.19 ? 134 TRP A CA  1 
ATOM   1069 C C   . TRP A 1 134 ? -11.933 -20.738 38.210 1.00 17.16 ? 134 TRP A C   1 
ATOM   1070 O O   . TRP A 1 134 ? -13.096 -21.123 38.026 1.00 16.56 ? 134 TRP A O   1 
ATOM   1071 C CB  . TRP A 1 134 ? -11.416 -18.549 39.341 1.00 15.45 ? 134 TRP A CB  1 
ATOM   1072 C CG  . TRP A 1 134 ? -12.733 -17.844 39.075 1.00 17.57 ? 134 TRP A CG  1 
ATOM   1073 C CD1 . TRP A 1 134 ? -13.539 -17.232 39.996 1.00 18.04 ? 134 TRP A CD1 1 
ATOM   1074 C CD2 . TRP A 1 134 ? -13.380 -17.683 37.807 1.00 17.45 ? 134 TRP A CD2 1 
ATOM   1075 N NE1 . TRP A 1 134 ? -14.649 -16.710 39.380 1.00 20.82 ? 134 TRP A NE1 1 
ATOM   1076 C CE2 . TRP A 1 134 ? -14.578 -16.972 38.037 1.00 20.50 ? 134 TRP A CE2 1 
ATOM   1077 C CE3 . TRP A 1 134 ? -13.058 -18.064 36.494 1.00 17.88 ? 134 TRP A CE3 1 
ATOM   1078 C CZ2 . TRP A 1 134 ? -15.469 -16.640 37.000 1.00 20.89 ? 134 TRP A CZ2 1 
ATOM   1079 C CZ3 . TRP A 1 134 ? -13.937 -17.723 35.463 1.00 19.14 ? 134 TRP A CZ3 1 
ATOM   1080 C CH2 . TRP A 1 134 ? -15.130 -17.029 35.728 1.00 18.25 ? 134 TRP A CH2 1 
ATOM   1081 N N   . ILE A 1 135 ? -10.976 -20.901 37.300 1.00 14.61 ? 135 ILE A N   1 
ATOM   1082 C CA  . ILE A 1 135 ? -11.255 -21.468 35.984 1.00 14.39 ? 135 ILE A CA  1 
ATOM   1083 C C   . ILE A 1 135 ? -11.500 -22.971 36.084 1.00 17.87 ? 135 ILE A C   1 
ATOM   1084 O O   . ILE A 1 135 ? -12.451 -23.504 35.489 1.00 17.25 ? 135 ILE A O   1 
ATOM   1085 C CB  . ILE A 1 135 ? -10.090 -21.139 35.029 1.00 13.93 ? 135 ILE A CB  1 
ATOM   1086 C CG1 . ILE A 1 135 ? -10.048 -19.631 34.749 1.00 14.89 ? 135 ILE A CG1 1 
ATOM   1087 C CG2 . ILE A 1 135 ? -10.200 -21.949 33.732 1.00 17.78 ? 135 ILE A CG2 1 
ATOM   1088 C CD1 . ILE A 1 135 ? -8.692  -19.163 34.189 1.00 16.41 ? 135 ILE A CD1 1 
ATOM   1089 N N   . ALA A 1 136 ? -10.639 -23.678 36.833 1.00 15.76 ? 136 ALA A N   1 
ATOM   1090 C CA  . ALA A 1 136 ? -10.742 -25.134 36.928 1.00 17.18 ? 136 ALA A CA  1 
ATOM   1091 C C   . ALA A 1 136 ? -12.054 -25.554 37.571 1.00 18.89 ? 136 ALA A C   1 
ATOM   1092 O O   . ALA A 1 136 ? -12.671 -26.537 37.154 1.00 19.23 ? 136 ALA A O   1 
ATOM   1093 C CB  . ALA A 1 136 ? -9.568  -25.694 37.728 1.00 18.24 ? 136 ALA A CB  1 
ATOM   1094 N N   . GLU A 1 137 ? -12.494 -24.823 38.591 1.00 16.94 ? 137 GLU A N   1 
ATOM   1095 C CA  . GLU A 1 137 ? -13.790 -25.107 39.187 1.00 21.55 ? 137 GLU A CA  1 
ATOM   1096 C C   . GLU A 1 137 ? -14.939 -24.881 38.208 1.00 21.10 ? 137 GLU A C   1 
ATOM   1097 O O   . GLU A 1 137 ? -16.026 -25.422 38.417 1.00 20.77 ? 137 GLU A O   1 
ATOM   1098 C CB  . GLU A 1 137 ? -13.991 -24.254 40.438 1.00 22.21 ? 137 GLU A CB  1 
ATOM   1099 C CG  . GLU A 1 137 ? -13.087 -24.648 41.597 1.00 24.30 ? 137 GLU A CG  1 
ATOM   1100 C CD  . GLU A 1 137 ? -13.312 -23.757 42.808 1.00 32.84 ? 137 GLU A CD  1 
ATOM   1101 O OE1 . GLU A 1 137 ? -14.071 -22.775 42.675 1.00 37.69 ? 137 GLU A OE1 1 
ATOM   1102 O OE2 . GLU A 1 137 ? -12.733 -24.027 43.883 1.00 37.89 ? 137 GLU A OE2 1 
ATOM   1103 N N   . ARG A 1 138 ? -14.727 -24.107 37.145 1.00 19.82 ? 138 ARG A N   1 
ATOM   1104 C CA  . ARG A 1 138 ? -15.754 -23.851 36.141 1.00 19.35 ? 138 ARG A CA  1 
ATOM   1105 C C   . ARG A 1 138 ? -15.487 -24.594 34.837 1.00 19.27 ? 138 ARG A C   1 
ATOM   1106 O O   . ARG A 1 138 ? -16.017 -24.211 33.789 1.00 19.83 ? 138 ARG A O   1 
ATOM   1107 C CB  . ARG A 1 138 ? -15.879 -22.342 35.912 1.00 18.29 ? 138 ARG A CB  1 
ATOM   1108 C CG  . ARG A 1 138 ? -16.544 -21.647 37.141 1.00 17.22 ? 138 ARG A CG  1 
ATOM   1109 C CD  . ARG A 1 138 ? -16.347 -20.130 37.188 1.00 16.70 ? 138 ARG A CD  1 
ATOM   1110 N NE  . ARG A 1 138 ? -16.993 -19.587 38.388 1.00 16.55 ? 138 ARG A NE  1 
ATOM   1111 C CZ  . ARG A 1 138 ? -16.478 -19.627 39.615 1.00 21.60 ? 138 ARG A CZ  1 
ATOM   1112 N NH1 . ARG A 1 138 ? -15.266 -20.158 39.826 1.00 16.10 ? 138 ARG A NH1 1 
ATOM   1113 N NH2 . ARG A 1 138 ? -17.180 -19.135 40.639 1.00 19.50 ? 138 ARG A NH2 1 
ATOM   1114 N N   . ALA A 1 139 ? -14.685 -25.665 34.891 1.00 18.50 ? 139 ALA A N   1 
ATOM   1115 C CA  . ALA A 1 139 ? -14.330 -26.413 33.687 1.00 21.99 ? 139 ALA A CA  1 
ATOM   1116 C C   . ALA A 1 139 ? -15.560 -26.798 32.875 1.00 20.88 ? 139 ALA A C   1 
ATOM   1117 O O   . ALA A 1 139 ? -15.559 -26.681 31.646 1.00 22.61 ? 139 ALA A O   1 
ATOM   1118 C CB  . ALA A 1 139 ? -13.538 -27.671 34.062 1.00 19.60 ? 139 ALA A CB  1 
ATOM   1119 N N   . ALA A 1 140 ? -16.620 -27.267 33.542 1.00 19.33 ? 140 ALA A N   1 
ATOM   1120 C CA  . ALA A 1 140 ? -17.801 -27.709 32.800 1.00 24.30 ? 140 ALA A CA  1 
ATOM   1121 C C   . ALA A 1 140 ? -18.497 -26.535 32.115 1.00 24.20 ? 140 ALA A C   1 
ATOM   1122 O O   . ALA A 1 140 ? -18.999 -26.669 30.990 1.00 27.14 ? 140 ALA A O   1 
ATOM   1123 C CB  . ALA A 1 140 ? -18.771 -28.442 33.732 1.00 23.82 ? 140 ALA A CB  1 
ATOM   1124 N N   . ASP A 1 141 ? -18.530 -25.377 32.777 1.00 19.73 ? 141 ASP A N   1 
ATOM   1125 C CA  . ASP A 1 141 ? -19.134 -24.186 32.186 1.00 21.34 ? 141 ASP A CA  1 
ATOM   1126 C C   . ASP A 1 141 ? -18.372 -23.759 30.940 1.00 22.92 ? 141 ASP A C   1 
ATOM   1127 O O   . ASP A 1 141 ? -18.963 -23.264 29.974 1.00 21.53 ? 141 ASP A O   1 
ATOM   1128 C CB  . ASP A 1 141 ? -19.138 -23.031 33.201 1.00 18.52 ? 141 ASP A CB  1 
ATOM   1129 C CG  . ASP A 1 141 ? -20.170 -23.207 34.321 1.00 28.58 ? 141 ASP A CG  1 
ATOM   1130 O OD1 . ASP A 1 141 ? -21.135 -23.987 34.143 1.00 24.54 ? 141 ASP A OD1 1 
ATOM   1131 O OD2 . ASP A 1 141 ? -20.010 -22.545 35.388 1.00 24.19 ? 141 ASP A OD2 1 
ATOM   1132 N N   . PHE A 1 142 ? -17.049 -23.903 30.963 1.00 20.70 ? 142 PHE A N   1 
ATOM   1133 C CA  . PHE A 1 142 ? -16.205 -23.509 29.846 1.00 21.45 ? 142 PHE A CA  1 
ATOM   1134 C C   . PHE A 1 142 ? -15.979 -24.640 28.843 1.00 23.62 ? 142 PHE A C   1 
ATOM   1135 O O   . PHE A 1 142 ? -15.222 -24.452 27.885 1.00 24.62 ? 142 PHE A O   1 
ATOM   1136 C CB  . PHE A 1 142 ? -14.854 -23.000 30.376 1.00 19.93 ? 142 PHE A CB  1 
ATOM   1137 C CG  . PHE A 1 142 ? -14.904 -21.605 30.977 1.00 18.05 ? 142 PHE A CG  1 
ATOM   1138 C CD1 . PHE A 1 142 ? -15.258 -20.513 30.200 1.00 20.36 ? 142 PHE A CD1 1 
ATOM   1139 C CD2 . PHE A 1 142 ? -14.561 -21.393 32.311 1.00 19.04 ? 142 PHE A CD2 1 
ATOM   1140 C CE1 . PHE A 1 142 ? -15.280 -19.222 30.745 1.00 22.81 ? 142 PHE A CE1 1 
ATOM   1141 C CE2 . PHE A 1 142 ? -14.583 -20.110 32.867 1.00 19.28 ? 142 PHE A CE2 1 
ATOM   1142 C CZ  . PHE A 1 142 ? -14.936 -19.023 32.076 1.00 19.73 ? 142 PHE A CZ  1 
ATOM   1143 N N   . HIS A 1 143 ? -16.596 -25.804 29.056 1.00 21.23 ? 143 HIS A N   1 
ATOM   1144 C CA  . HIS A 1 143 ? -16.406 -26.993 28.213 1.00 22.50 ? 143 HIS A CA  1 
ATOM   1145 C C   . HIS A 1 143 ? -14.954 -27.453 28.179 1.00 25.34 ? 143 HIS A C   1 
ATOM   1146 O O   . HIS A 1 143 ? -14.456 -27.865 27.130 1.00 22.07 ? 143 HIS A O   1 
ATOM   1147 C CB  . HIS A 1 143 ? -16.905 -26.746 26.791 1.00 21.73 ? 143 HIS A CB  1 
ATOM   1148 C CG  . HIS A 1 143 ? -18.252 -26.110 26.748 1.00 32.24 ? 143 HIS A CG  1 
ATOM   1149 N ND1 . HIS A 1 143 ? -19.381 -26.751 27.204 1.00 30.88 ? 143 HIS A ND1 1 
ATOM   1150 C CD2 . HIS A 1 143 ? -18.648 -24.876 26.356 1.00 34.15 ? 143 HIS A CD2 1 
ATOM   1151 C CE1 . HIS A 1 143 ? -20.422 -25.949 27.070 1.00 33.14 ? 143 HIS A CE1 1 
ATOM   1152 N NE2 . HIS A 1 143 ? -20.004 -24.805 26.558 1.00 35.05 ? 143 HIS A NE2 1 
ATOM   1153 N N   . LEU A 1 144 ? -14.262 -27.383 29.317 1.00 21.59 ? 144 LEU A N   1 
ATOM   1154 C CA  . LEU A 1 144 ? -12.876 -27.834 29.366 1.00 21.88 ? 144 LEU A CA  1 
ATOM   1155 C C   . LEU A 1 144 ? -12.797 -29.262 29.888 1.00 23.99 ? 144 LEU A C   1 
ATOM   1156 O O   . LEU A 1 144 ? -13.631 -29.705 30.681 1.00 21.81 ? 144 LEU A O   1 
ATOM   1157 C CB  . LEU A 1 144 ? -12.013 -26.936 30.258 1.00 19.62 ? 144 LEU A CB  1 
ATOM   1158 C CG  . LEU A 1 144 ? -12.152 -25.423 30.094 1.00 19.95 ? 144 LEU A CG  1 
ATOM   1159 C CD1 . LEU A 1 144 ? -11.250 -24.724 31.105 1.00 17.56 ? 144 LEU A CD1 1 
ATOM   1160 C CD2 . LEU A 1 144 ? -11.850 -24.992 28.670 1.00 20.21 ? 144 LEU A CD2 1 
ATOM   1161 N N   . ASP A 1 145 ? -11.773 -29.973 29.444 1.00 22.53 ? 145 ASP A N   1 
ATOM   1162 C CA  . ASP A 1 145 ? -11.431 -31.246 30.058 1.00 22.77 ? 145 ASP A CA  1 
ATOM   1163 C C   . ASP A 1 145 ? -10.629 -30.989 31.329 1.00 22.63 ? 145 ASP A C   1 
ATOM   1164 O O   . ASP A 1 145 ? -9.466  -30.561 31.243 1.00 24.07 ? 145 ASP A O   1 
ATOM   1165 C CB  . ASP A 1 145 ? -10.621 -32.102 29.076 1.00 24.18 ? 145 ASP A CB  1 
ATOM   1166 C CG  . ASP A 1 145 ? -10.267 -33.479 29.634 1.00 23.61 ? 145 ASP A CG  1 
ATOM   1167 O OD1 . ASP A 1 145 ? -10.442 -33.736 30.846 1.00 28.26 ? 145 ASP A OD1 1 
ATOM   1168 O OD2 . ASP A 1 145 ? -9.820  -34.324 28.842 1.00 30.02 ? 145 ASP A OD2 1 
ATOM   1169 N N   . PRO A 1 146 ? -11.170 -31.297 32.513 1.00 24.83 ? 146 PRO A N   1 
ATOM   1170 C CA  . PRO A 1 146 ? -10.428 -31.005 33.754 1.00 25.77 ? 146 PRO A CA  1 
ATOM   1171 C C   . PRO A 1 146 ? -9.116  -31.760 33.872 1.00 24.91 ? 146 PRO A C   1 
ATOM   1172 O O   . PRO A 1 146 ? -8.275  -31.375 34.695 1.00 25.14 ? 146 PRO A O   1 
ATOM   1173 C CB  . PRO A 1 146 ? -11.406 -31.417 34.867 1.00 28.02 ? 146 PRO A CB  1 
ATOM   1174 C CG  . PRO A 1 146 ? -12.738 -31.574 34.200 1.00 28.47 ? 146 PRO A CG  1 
ATOM   1175 C CD  . PRO A 1 146 ? -12.462 -31.957 32.779 1.00 24.98 ? 146 PRO A CD  1 
ATOM   1176 N N   . ALA A 1 147 ? -8.907  -32.810 33.079 1.00 23.81 ? 147 ALA A N   1 
ATOM   1177 C CA  . ALA A 1 147 ? -7.659  -33.558 33.115 1.00 28.36 ? 147 ALA A CA  1 
ATOM   1178 C C   . ALA A 1 147 ? -6.606  -33.007 32.160 1.00 26.05 ? 147 ALA A C   1 
ATOM   1179 O O   . ALA A 1 147 ? -5.498  -33.554 32.101 1.00 23.67 ? 147 ALA A O   1 
ATOM   1180 C CB  . ALA A 1 147 ? -7.914  -35.040 32.798 1.00 28.27 ? 147 ALA A CB  1 
ATOM   1181 N N   . ARG A 1 148 ? -6.921  -31.958 31.404 1.00 23.66 ? 148 ARG A N   1 
ATOM   1182 C CA  . ARG A 1 148 ? -6.017  -31.390 30.407 1.00 21.64 ? 148 ARG A CA  1 
ATOM   1183 C C   . ARG A 1 148 ? -5.976  -29.872 30.519 1.00 24.06 ? 148 ARG A C   1 
ATOM   1184 O O   . ARG A 1 148 ? -6.069  -29.146 29.525 1.00 19.56 ? 148 ARG A O   1 
ATOM   1185 C CB  . ARG A 1 148 ? -6.426  -31.805 28.997 1.00 25.56 ? 148 ARG A CB  1 
ATOM   1186 C CG  . ARG A 1 148 ? -6.308  -33.315 28.764 1.00 30.64 ? 148 ARG A CG  1 
ATOM   1187 C CD  . ARG A 1 148 ? -6.412  -33.669 27.293 1.00 35.03 ? 148 ARG A CD  1 
ATOM   1188 N NE  . ARG A 1 148 ? -7.775  -33.478 26.831 1.00 38.25 ? 148 ARG A NE  1 
ATOM   1189 C CZ  . ARG A 1 148 ? -8.110  -33.173 25.583 1.00 38.03 ? 148 ARG A CZ  1 
ATOM   1190 N NH1 . ARG A 1 148 ? -7.171  -33.035 24.659 1.00 31.73 ? 148 ARG A NH1 1 
ATOM   1191 N NH2 . ARG A 1 148 ? -9.393  -33.022 25.265 1.00 31.96 ? 148 ARG A NH2 1 
ATOM   1192 N N   . ILE A 1 149 ? -5.826  -29.374 31.743 1.00 21.46 ? 149 ILE A N   1 
ATOM   1193 C CA  . ILE A 1 149 ? -5.626  -27.950 32.005 1.00 18.25 ? 149 ILE A CA  1 
ATOM   1194 C C   . ILE A 1 149 ? -4.172  -27.748 32.400 1.00 20.21 ? 149 ILE A C   1 
ATOM   1195 O O   . ILE A 1 149 ? -3.692  -28.330 33.384 1.00 19.55 ? 149 ILE A O   1 
ATOM   1196 C CB  . ILE A 1 149 ? -6.574  -27.425 33.091 1.00 18.56 ? 149 ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 149 ? -8.036  -27.586 32.636 1.00 19.28 ? 149 ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 149 ? -6.273  -25.951 33.397 1.00 15.75 ? 149 ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 149 ? -9.058  -27.061 33.666 1.00 18.33 ? 149 ILE A CD1 1 
ATOM   1200 N N   . ALA A 1 150 ? -3.468  -26.939 31.631 1.00 16.38 ? 150 ALA A N   1 
ATOM   1201 C CA  . ALA A 1 150 ? -2.076  -26.644 31.919 1.00 18.28 ? 150 ALA A CA  1 
ATOM   1202 C C   . ALA A 1 150 ? -1.952  -25.231 32.475 1.00 20.02 ? 150 ALA A C   1 
ATOM   1203 O O   . ALA A 1 150 ? -2.881  -24.417 32.381 1.00 15.49 ? 150 ALA A O   1 
ATOM   1204 C CB  . ALA A 1 150 ? -1.232  -26.801 30.657 1.00 17.08 ? 150 ALA A CB  1 
ATOM   1205 N N   . VAL A 1 151 ? -0.788  -24.951 33.066 1.00 15.76 ? 151 VAL A N   1 
ATOM   1206 C CA  . VAL A 1 151 ? -0.386  -23.590 33.411 1.00 15.17 ? 151 VAL A CA  1 
ATOM   1207 C C   . VAL A 1 151 ? 0.866   -23.248 32.623 1.00 16.78 ? 151 VAL A C   1 
ATOM   1208 O O   . VAL A 1 151 ? 1.648   -24.127 32.240 1.00 17.45 ? 151 VAL A O   1 
ATOM   1209 C CB  . VAL A 1 151 ? -0.131  -23.395 34.931 1.00 18.65 ? 151 VAL A CB  1 
ATOM   1210 C CG1 . VAL A 1 151 ? -1.411  -23.651 35.726 1.00 18.84 ? 151 VAL A CG1 1 
ATOM   1211 C CG2 . VAL A 1 151 ? 1.029   -24.294 35.420 1.00 14.30 ? 151 VAL A CG2 1 
ATOM   1212 N N   . GLY A 1 152 ? 1.071   -21.957 32.400 1.00 16.48 ? 152 GLY A N   1 
ATOM   1213 C CA  . GLY A 1 152 ? 2.259   -21.545 31.667 1.00 12.56 ? 152 GLY A CA  1 
ATOM   1214 C C   . GLY A 1 152 ? 2.449   -20.045 31.723 1.00 12.89 ? 152 GLY A C   1 
ATOM   1215 O O   . GLY A 1 152 ? 1.588   -19.298 32.193 1.00 15.09 ? 152 GLY A O   1 
ATOM   1216 N N   . GLY A 1 153 ? 3.600   -19.607 31.230 1.00 14.05 ? 153 GLY A N   1 
ATOM   1217 C CA  . GLY A 1 153 ? 3.855   -18.188 31.166 1.00 16.43 ? 153 GLY A CA  1 
ATOM   1218 C C   . GLY A 1 153 ? 5.288   -17.933 30.773 1.00 15.69 ? 153 GLY A C   1 
ATOM   1219 O O   . GLY A 1 153 ? 6.113   -18.848 30.688 1.00 15.23 ? 153 GLY A O   1 
ATOM   1220 N N   . ASP A 1 154 ? 5.573   -16.662 30.527 1.00 14.63 ? 154 ASP A N   1 
ATOM   1221 C CA  . ASP A 1 154 ? 6.914   -16.244 30.116 1.00 18.36 ? 154 ASP A CA  1 
ATOM   1222 C C   . ASP A 1 154 ? 7.558   -15.361 31.181 1.00 18.42 ? 154 ASP A C   1 
ATOM   1223 O O   . ASP A 1 154 ? 6.893   -14.507 31.772 1.00 16.47 ? 154 ASP A O   1 
ATOM   1224 C CB  . ASP A 1 154 ? 6.853   -15.503 28.775 1.00 20.38 ? 154 ASP A CB  1 
ATOM   1225 C CG  . ASP A 1 154 ? 6.055   -14.204 28.853 1.00 23.09 ? 154 ASP A CG  1 
ATOM   1226 O OD1 . ASP A 1 154 ? 4.807   -14.246 29.024 1.00 20.42 ? 154 ASP A OD1 1 
ATOM   1227 O OD2 . ASP A 1 154 ? 6.685   -13.131 28.732 1.00 23.50 ? 154 ASP A OD2 1 
ATOM   1228 N N   . SER A 1 155 ? 8.859   -15.570 31.430 1.00 19.88 ? 155 SER A N   1 
ATOM   1229 C CA  . SER A 1 155 ? 9.673   -14.704 32.301 1.00 19.87 ? 155 SER A CA  1 
ATOM   1230 C C   . SER A 1 155 ? 9.072   -14.694 33.706 1.00 21.21 ? 155 SER A C   1 
ATOM   1231 O O   . SER A 1 155 ? 9.000   -15.767 34.332 1.00 18.36 ? 155 SER A O   1 
ATOM   1232 C CB  . SER A 1 155 ? 9.816   -13.330 31.630 1.00 21.31 ? 155 SER A CB  1 
ATOM   1233 O OG  . SER A 1 155 ? 10.752  -12.491 32.323 1.00 34.81 ? 155 SER A OG  1 
ATOM   1234 N N   . ALA A 1 156 ? 8.651   -13.538 34.249 1.00 17.26 ? 156 ALA A N   1 
ATOM   1235 C CA  . ALA A 1 156 ? 7.975   -13.527 35.549 1.00 17.34 ? 156 ALA A CA  1 
ATOM   1236 C C   . ALA A 1 156 ? 6.690   -14.357 35.528 1.00 18.33 ? 156 ALA A C   1 
ATOM   1237 O O   . ALA A 1 156 ? 6.262   -14.878 36.571 1.00 16.53 ? 156 ALA A O   1 
ATOM   1238 C CB  . ALA A 1 156 ? 7.660   -12.091 35.959 1.00 17.93 ? 156 ALA A CB  1 
ATOM   1239 N N   . GLY A 1 157 ? 6.039   -14.461 34.368 1.00 17.65 ? 157 GLY A N   1 
ATOM   1240 C CA  . GLY A 1 157 ? 4.843   -15.293 34.275 1.00 14.98 ? 157 GLY A CA  1 
ATOM   1241 C C   . GLY A 1 157 ? 5.148   -16.776 34.345 1.00 16.10 ? 157 GLY A C   1 
ATOM   1242 O O   . GLY A 1 157 ? 4.308   -17.569 34.790 1.00 15.70 ? 157 GLY A O   1 
ATOM   1243 N N   . GLY A 1 158 ? 6.334   -17.174 33.886 1.00 16.52 ? 158 GLY A N   1 
ATOM   1244 C CA  . GLY A 1 158 ? 6.771   -18.550 34.069 1.00 15.84 ? 158 GLY A CA  1 
ATOM   1245 C C   . GLY A 1 158 ? 7.083   -18.850 35.521 1.00 16.32 ? 158 GLY A C   1 
ATOM   1246 O O   . GLY A 1 158 ? 6.760   -19.926 36.028 1.00 17.15 ? 158 GLY A O   1 
ATOM   1247 N N   . ASN A 1 159 ? 7.711   -17.899 36.208 1.00 16.51 ? 159 ASN A N   1 
ATOM   1248 C CA  . ASN A 1 159 ? 7.798   -17.967 37.660 1.00 15.75 ? 159 ASN A CA  1 
ATOM   1249 C C   . ASN A 1 159 ? 6.424   -18.238 38.278 1.00 15.52 ? 159 ASN A C   1 
ATOM   1250 O O   . ASN A 1 159 ? 6.250   -19.189 39.051 1.00 14.97 ? 159 ASN A O   1 
ATOM   1251 C CB  . ASN A 1 159 ? 8.408   -16.660 38.182 1.00 15.52 ? 159 ASN A CB  1 
ATOM   1252 C CG  . ASN A 1 159 ? 8.301   -16.531 39.684 1.00 19.80 ? 159 ASN A CG  1 
ATOM   1253 O OD1 . ASN A 1 159 ? 7.297   -16.030 40.210 1.00 18.80 ? 159 ASN A OD1 1 
ATOM   1254 N ND2 . ASN A 1 159 ? 9.339   -16.983 40.390 1.00 17.30 ? 159 ASN A ND2 1 
ATOM   1255 N N   . LEU A 1 160 ? 5.424   -17.429 37.925 1.00 13.51 ? 160 LEU A N   1 
ATOM   1256 C CA  . LEU A 1 160 ? 4.100   -17.601 38.526 1.00 15.43 ? 160 LEU A CA  1 
ATOM   1257 C C   . LEU A 1 160 ? 3.489   -18.962 38.190 1.00 16.65 ? 160 LEU A C   1 
ATOM   1258 O O   . LEU A 1 160 ? 2.827   -19.573 39.037 1.00 16.11 ? 160 LEU A O   1 
ATOM   1259 C CB  . LEU A 1 160 ? 3.157   -16.469 38.082 1.00 15.24 ? 160 LEU A CB  1 
ATOM   1260 C CG  . LEU A 1 160 ? 3.526   -15.070 38.600 1.00 15.51 ? 160 LEU A CG  1 
ATOM   1261 C CD1 . LEU A 1 160 ? 2.628   -13.990 38.012 1.00 16.89 ? 160 LEU A CD1 1 
ATOM   1262 C CD2 . LEU A 1 160 ? 3.468   -15.042 40.126 1.00 16.46 ? 160 LEU A CD2 1 
ATOM   1263 N N   . ALA A 1 161 ? 3.684   -19.456 36.959 1.00 13.45 ? 161 ALA A N   1 
ATOM   1264 C CA  . ALA A 1 161 ? 3.162   -20.783 36.628 1.00 13.17 ? 161 ALA A CA  1 
ATOM   1265 C C   . ALA A 1 161 ? 3.850   -21.864 37.442 1.00 15.50 ? 161 ALA A C   1 
ATOM   1266 O O   . ALA A 1 161 ? 3.195   -22.802 37.925 1.00 14.34 ? 161 ALA A O   1 
ATOM   1267 C CB  . ALA A 1 161 ? 3.318   -21.082 35.137 1.00 15.95 ? 161 ALA A CB  1 
ATOM   1268 N N   . ALA A 1 162 ? 5.180   -21.774 37.585 1.00 14.84 ? 162 ALA A N   1 
ATOM   1269 C CA  . ALA A 1 162 ? 5.896   -22.760 38.387 1.00 14.96 ? 162 ALA A CA  1 
ATOM   1270 C C   . ALA A 1 162 ? 5.447   -22.722 39.846 1.00 15.64 ? 162 ALA A C   1 
ATOM   1271 O O   . ALA A 1 162 ? 5.300   -23.771 40.487 1.00 15.14 ? 162 ALA A O   1 
ATOM   1272 C CB  . ALA A 1 162 ? 7.415   -22.520 38.286 1.00 15.05 ? 162 ALA A CB  1 
ATOM   1273 N N   . VAL A 1 163 ? 5.260   -21.523 40.405 1.00 13.31 ? 163 VAL A N   1 
ATOM   1274 C CA  . VAL A 1 163 ? 4.837   -21.434 41.806 1.00 14.95 ? 163 VAL A CA  1 
ATOM   1275 C C   . VAL A 1 163 ? 3.398   -21.903 41.962 1.00 16.39 ? 163 VAL A C   1 
ATOM   1276 O O   . VAL A 1 163 ? 3.056   -22.560 42.954 1.00 17.51 ? 163 VAL A O   1 
ATOM   1277 C CB  . VAL A 1 163 ? 5.021   -20.004 42.339 1.00 14.85 ? 163 VAL A CB  1 
ATOM   1278 C CG1 . VAL A 1 163 ? 4.373   -19.863 43.729 1.00 14.19 ? 163 VAL A CG1 1 
ATOM   1279 C CG2 . VAL A 1 163 ? 6.541   -19.676 42.419 1.00 12.49 ? 163 VAL A CG2 1 
ATOM   1280 N N   . THR A 1 164 ? 2.530   -21.555 41.004 1.00 13.41 ? 164 THR A N   1 
ATOM   1281 C CA  . THR A 1 164 ? 1.147   -22.040 41.030 1.00 14.85 ? 164 THR A CA  1 
ATOM   1282 C C   . THR A 1 164 ? 1.098   -23.565 41.106 1.00 16.17 ? 164 THR A C   1 
ATOM   1283 O O   . THR A 1 164 ? 0.304   -24.127 41.870 1.00 15.76 ? 164 THR A O   1 
ATOM   1284 C CB  . THR A 1 164 ? 0.385   -21.536 39.796 1.00 15.88 ? 164 THR A CB  1 
ATOM   1285 O OG1 . THR A 1 164 ? 0.263   -20.108 39.855 1.00 15.91 ? 164 THR A OG1 1 
ATOM   1286 C CG2 . THR A 1 164 ? -1.038  -22.135 39.724 1.00 15.88 ? 164 THR A CG2 1 
ATOM   1287 N N   . SER A 1 165 ? 1.956   -24.254 40.337 1.00 15.86 ? 165 SER A N   1 
ATOM   1288 C CA  . SER A 1 165 ? 1.986   -25.721 40.385 1.00 17.81 ? 165 SER A CA  1 
ATOM   1289 C C   . SER A 1 165 ? 2.364   -26.230 41.774 1.00 19.26 ? 165 SER A C   1 
ATOM   1290 O O   . SER A 1 165 ? 1.846   -27.259 42.234 1.00 20.69 ? 165 SER A O   1 
ATOM   1291 C CB  . SER A 1 165 ? 2.975   -26.261 39.346 1.00 17.80 ? 165 SER A CB  1 
ATOM   1292 O OG  . SER A 1 165 ? 2.599   -25.864 38.035 1.00 17.74 ? 165 SER A OG  1 
ATOM   1293 N N   . ILE A 1 166 ? 3.274   -25.525 42.451 1.00 14.52 ? 166 ILE A N   1 
ATOM   1294 C CA  . ILE A 1 166 ? 3.644   -25.874 43.824 1.00 18.86 ? 166 ILE A CA  1 
ATOM   1295 C C   . ILE A 1 166 ? 2.462   -25.681 44.783 1.00 19.13 ? 166 ILE A C   1 
ATOM   1296 O O   . ILE A 1 166 ? 2.198   -26.531 45.644 1.00 18.54 ? 166 ILE A O   1 
ATOM   1297 C CB  . ILE A 1 166 ? 4.878   -25.058 44.263 1.00 17.28 ? 166 ILE A CB  1 
ATOM   1298 C CG1 . ILE A 1 166 ? 6.137   -25.594 43.550 1.00 17.44 ? 166 ILE A CG1 1 
ATOM   1299 C CG2 . ILE A 1 166 ? 5.059   -25.122 45.785 1.00 22.80 ? 166 ILE A CG2 1 
ATOM   1300 C CD1 . ILE A 1 166 ? 7.400   -24.724 43.741 1.00 20.15 ? 166 ILE A CD1 1 
ATOM   1301 N N   . LEU A 1 167 ? 1.753   -24.554 44.673 1.00 18.55 ? 167 LEU A N   1 
ATOM   1302 C CA  . LEU A 1 167 ? 0.617   -24.316 45.565 1.00 19.99 ? 167 LEU A CA  1 
ATOM   1303 C C   . LEU A 1 167 ? -0.486  -25.340 45.333 1.00 22.66 ? 167 LEU A C   1 
ATOM   1304 O O   . LEU A 1 167 ? -1.136  -25.796 46.285 1.00 20.31 ? 167 LEU A O   1 
ATOM   1305 C CB  . LEU A 1 167 ? 0.074   -22.899 45.371 1.00 17.00 ? 167 LEU A CB  1 
ATOM   1306 C CG  . LEU A 1 167 ? 0.972   -21.798 45.958 1.00 26.55 ? 167 LEU A CG  1 
ATOM   1307 C CD1 . LEU A 1 167 ? 0.262   -20.459 45.920 1.00 24.43 ? 167 LEU A CD1 1 
ATOM   1308 C CD2 . LEU A 1 167 ? 1.344   -22.171 47.374 1.00 34.99 ? 167 LEU A CD2 1 
ATOM   1309 N N   . ALA A 1 168 ? -0.701  -25.721 44.074 1.00 19.19 ? 168 ALA A N   1 
ATOM   1310 C CA  . ALA A 1 168 ? -1.697  -26.737 43.761 1.00 20.20 ? 168 ALA A CA  1 
ATOM   1311 C C   . ALA A 1 168 ? -1.293  -28.102 44.313 1.00 25.92 ? 168 ALA A C   1 
ATOM   1312 O O   . ALA A 1 168 ? -2.147  -28.868 44.779 1.00 22.22 ? 168 ALA A O   1 
ATOM   1313 C CB  . ALA A 1 168 ? -1.917  -26.800 42.254 1.00 19.06 ? 168 ALA A CB  1 
ATOM   1314 N N   . LYS A 1 169 ? 0.002   -28.422 44.296 1.00 21.18 ? 169 LYS A N   1 
ATOM   1315 C CA  . LYS A 1 169 ? 0.444   -29.649 44.953 1.00 20.21 ? 169 LYS A CA  1 
ATOM   1316 C C   . LYS A 1 169 ? 0.135   -29.610 46.443 1.00 23.83 ? 169 LYS A C   1 
ATOM   1317 O O   . LYS A 1 169 ? -0.382  -30.583 47.005 1.00 27.30 ? 169 LYS A O   1 
ATOM   1318 C CB  . LYS A 1 169 ? 1.943   -29.874 44.730 1.00 20.59 ? 169 LYS A CB  1 
ATOM   1319 C CG  . LYS A 1 169 ? 2.452   -31.194 45.356 1.00 24.95 ? 169 LYS A CG  1 
ATOM   1320 C CD  . LYS A 1 169 ? 3.981   -31.282 45.334 1.00 33.83 ? 169 LYS A CD  1 
ATOM   1321 C CE  . LYS A 1 169 ? 4.507   -32.029 46.553 1.00 31.05 ? 169 LYS A CE  1 
ATOM   1322 N NZ  . LYS A 1 169 ? 5.949   -32.374 46.391 1.00 29.52 ? 169 LYS A NZ  1 
ATOM   1323 N N   . GLU A 1 170 ? 0.438   -28.489 47.098 1.00 21.85 ? 170 GLU A N   1 
ATOM   1324 C CA  . GLU A 1 170 ? 0.230   -28.380 48.537 1.00 23.75 ? 170 GLU A CA  1 
ATOM   1325 C C   . GLU A 1 170 ? -1.249  -28.478 48.897 1.00 31.87 ? 170 GLU A C   1 
ATOM   1326 O O   . GLU A 1 170 ? -1.611  -29.043 49.935 1.00 24.55 ? 170 GLU A O   1 
ATOM   1327 C CB  . GLU A 1 170 ? 0.796   -27.058 49.040 1.00 21.08 ? 170 GLU A CB  1 
ATOM   1328 C CG  . GLU A 1 170 ? 2.333   -26.978 49.021 1.00 25.11 ? 170 GLU A CG  1 
ATOM   1329 C CD  . GLU A 1 170 ? 2.826   -25.676 49.603 1.00 26.40 ? 170 GLU A CD  1 
ATOM   1330 O OE1 . GLU A 1 170 ? 2.017   -24.730 49.693 1.00 30.42 ? 170 GLU A OE1 1 
ATOM   1331 O OE2 . GLU A 1 170 ? 4.018   -25.587 49.973 1.00 32.71 ? 170 GLU A OE2 1 
ATOM   1332 N N   . ARG A 1 171 ? -2.113  -27.913 48.065 1.00 27.21 ? 171 ARG A N   1 
ATOM   1333 C CA  . ARG A 1 171 ? -3.527  -27.794 48.384 1.00 23.60 ? 171 ARG A CA  1 
ATOM   1334 C C   . ARG A 1 171 ? -4.372  -28.876 47.735 1.00 27.06 ? 171 ARG A C   1 
ATOM   1335 O O   . ARG A 1 171 ? -5.603  -28.794 47.770 1.00 31.86 ? 171 ARG A O   1 
ATOM   1336 C CB  . ARG A 1 171 ? -4.019  -26.402 47.983 1.00 26.16 ? 171 ARG A CB  1 
ATOM   1337 C CG  . ARG A 1 171 ? -3.265  -25.306 48.706 1.00 24.92 ? 171 ARG A CG  1 
ATOM   1338 C CD  . ARG A 1 171 ? -3.505  -23.939 48.112 1.00 27.66 ? 171 ARG A CD  1 
ATOM   1339 N NE  . ARG A 1 171 ? -2.623  -22.947 48.720 1.00 25.37 ? 171 ARG A NE  1 
ATOM   1340 C CZ  . ARG A 1 171 ? -2.779  -21.635 48.589 1.00 28.01 ? 171 ARG A CZ  1 
ATOM   1341 N NH1 . ARG A 1 171 ? -3.789  -21.149 47.874 1.00 33.56 ? 171 ARG A NH1 1 
ATOM   1342 N NH2 . ARG A 1 171 ? -1.939  -20.806 49.182 1.00 32.62 ? 171 ARG A NH2 1 
ATOM   1343 N N   . GLY A 1 172 ? -3.746  -29.882 47.138 1.00 27.85 ? 172 GLY A N   1 
ATOM   1344 C CA  . GLY A 1 172 ? -4.503  -30.985 46.586 1.00 33.33 ? 172 GLY A CA  1 
ATOM   1345 C C   . GLY A 1 172 ? -5.302  -30.633 45.359 1.00 33.97 ? 172 GLY A C   1 
ATOM   1346 O O   . GLY A 1 172 ? -6.208  -31.382 44.987 1.00 30.42 ? 172 GLY A O   1 
ATOM   1347 N N   . GLY A 1 173 ? -4.993  -29.511 44.717 1.00 25.63 ? 173 GLY A N   1 
ATOM   1348 C CA  . GLY A 1 173 ? -5.654  -29.146 43.493 1.00 23.88 ? 173 GLY A CA  1 
ATOM   1349 C C   . GLY A 1 173 ? -5.629  -27.654 43.238 1.00 22.07 ? 173 GLY A C   1 
ATOM   1350 O O   . GLY A 1 173 ? -5.192  -26.857 44.079 1.00 22.03 ? 173 GLY A O   1 
ATOM   1351 N N   . PRO A 1 174 ? -6.124  -27.243 42.063 1.00 23.21 ? 174 PRO A N   1 
ATOM   1352 C CA  . PRO A 1 174 ? -6.684  -28.159 41.051 1.00 18.12 ? 174 PRO A CA  1 
ATOM   1353 C C   . PRO A 1 174 ? -5.644  -28.964 40.281 1.00 21.34 ? 174 PRO A C   1 
ATOM   1354 O O   . PRO A 1 174 ? -4.453  -28.647 40.302 1.00 21.72 ? 174 PRO A O   1 
ATOM   1355 C CB  . PRO A 1 174 ? -7.439  -27.225 40.096 1.00 22.81 ? 174 PRO A CB  1 
ATOM   1356 C CG  . PRO A 1 174 ? -6.779  -25.874 40.265 1.00 24.89 ? 174 PRO A CG  1 
ATOM   1357 C CD  . PRO A 1 174 ? -6.247  -25.820 41.689 1.00 21.22 ? 174 PRO A CD  1 
ATOM   1358 N N   . ALA A 1 175 ? -6.113  -30.010 39.607 1.00 14.78 ? 175 ALA A N   1 
ATOM   1359 C CA  . ALA A 1 175 ? -5.244  -30.852 38.803 1.00 22.42 ? 175 ALA A CA  1 
ATOM   1360 C C   . ALA A 1 175 ? -4.642  -30.058 37.645 1.00 20.67 ? 175 ALA A C   1 
ATOM   1361 O O   . ALA A 1 175 ? -5.363  -29.437 36.861 1.00 18.92 ? 175 ALA A O   1 
ATOM   1362 C CB  . ALA A 1 175 ? -6.037  -32.050 38.275 1.00 22.15 ? 175 ALA A CB  1 
ATOM   1363 N N   . ILE A 1 176 ? -3.316  -30.079 37.544 1.00 18.38 ? 176 ILE A N   1 
ATOM   1364 C CA  . ILE A 1 176 ? -2.585  -29.446 36.448 1.00 18.89 ? 176 ILE A CA  1 
ATOM   1365 C C   . ILE A 1 176 ? -1.905  -30.543 35.649 1.00 19.91 ? 176 ILE A C   1 
ATOM   1366 O O   . ILE A 1 176 ? -1.154  -31.349 36.213 1.00 19.79 ? 176 ILE A O   1 
ATOM   1367 C CB  . ILE A 1 176 ? -1.543  -28.433 36.959 1.00 18.06 ? 176 ILE A CB  1 
ATOM   1368 C CG1 . ILE A 1 176 ? -2.232  -27.305 37.733 1.00 18.89 ? 176 ILE A CG1 1 
ATOM   1369 C CG2 . ILE A 1 176 ? -0.717  -27.884 35.782 1.00 19.39 ? 176 ILE A CG2 1 
ATOM   1370 C CD1 . ILE A 1 176 ? -1.264  -26.473 38.628 1.00 17.20 ? 176 ILE A CD1 1 
ATOM   1371 N N   . ALA A 1 177 ? -2.136  -30.556 34.339 1.00 20.19 ? 177 ALA A N   1 
ATOM   1372 C CA  . ALA A 1 177 ? -1.590  -31.616 33.496 1.00 21.76 ? 177 ALA A CA  1 
ATOM   1373 C C   . ALA A 1 177 ? -0.177  -31.337 32.996 1.00 21.37 ? 177 ALA A C   1 
ATOM   1374 O O   . ALA A 1 177 ? 0.515   -32.276 32.583 1.00 17.21 ? 177 ALA A O   1 
ATOM   1375 C CB  . ALA A 1 177 ? -2.495  -31.842 32.282 1.00 22.35 ? 177 ALA A CB  1 
ATOM   1376 N N   . PHE A 1 178 ? 0.262   -30.082 33.001 1.00 20.06 ? 178 PHE A N   1 
ATOM   1377 C CA  . PHE A 1 178 ? 1.463   -29.701 32.267 1.00 18.27 ? 178 PHE A CA  1 
ATOM   1378 C C   . PHE A 1 178 ? 1.818   -28.263 32.649 1.00 20.68 ? 178 PHE A C   1 
ATOM   1379 O O   . PHE A 1 178 ? 0.927   -27.463 32.944 1.00 16.27 ? 178 PHE A O   1 
ATOM   1380 C CB  . PHE A 1 178 ? 1.192   -29.856 30.759 1.00 20.33 ? 178 PHE A CB  1 
ATOM   1381 C CG  . PHE A 1 178 ? 2.339   -29.491 29.862 1.00 20.18 ? 178 PHE A CG  1 
ATOM   1382 C CD1 . PHE A 1 178 ? 3.507   -30.235 29.853 1.00 24.21 ? 178 PHE A CD1 1 
ATOM   1383 C CD2 . PHE A 1 178 ? 2.222   -28.424 28.984 1.00 22.23 ? 178 PHE A CD2 1 
ATOM   1384 C CE1 . PHE A 1 178 ? 4.554   -29.891 28.999 1.00 23.92 ? 178 PHE A CE1 1 
ATOM   1385 C CE2 . PHE A 1 178 ? 3.251   -28.080 28.140 1.00 21.87 ? 178 PHE A CE2 1 
ATOM   1386 C CZ  . PHE A 1 178 ? 4.422   -28.815 28.148 1.00 23.32 ? 178 PHE A CZ  1 
ATOM   1387 N N   . GLN A 1 179 ? 3.121   -27.954 32.701 1.00 18.77 ? 179 GLN A N   1 
ATOM   1388 C CA  . GLN A 1 179 ? 3.598   -26.585 32.907 1.00 18.06 ? 179 GLN A CA  1 
ATOM   1389 C C   . GLN A 1 179 ? 4.449   -26.163 31.724 1.00 17.72 ? 179 GLN A C   1 
ATOM   1390 O O   . GLN A 1 179 ? 5.452   -26.819 31.419 1.00 18.49 ? 179 GLN A O   1 
ATOM   1391 C CB  . GLN A 1 179 ? 4.477   -26.401 34.148 1.00 20.41 ? 179 GLN A CB  1 
ATOM   1392 C CG  . GLN A 1 179 ? 4.371   -27.375 35.272 1.00 30.09 ? 179 GLN A CG  1 
ATOM   1393 C CD  . GLN A 1 179 ? 5.439   -27.120 36.341 1.00 24.56 ? 179 GLN A CD  1 
ATOM   1394 O OE1 . GLN A 1 179 ? 5.626   -25.983 36.802 1.00 22.59 ? 179 GLN A OE1 1 
ATOM   1395 N NE2 . GLN A 1 179 ? 6.101   -28.183 36.776 1.00 20.76 ? 179 GLN A NE2 1 
ATOM   1396 N N   . LEU A 1 180 ? 4.102   -25.033 31.119 1.00 15.66 ? 180 LEU A N   1 
ATOM   1397 C CA  . LEU A 1 180 ? 4.798   -24.508 29.943 1.00 17.01 ? 180 LEU A CA  1 
ATOM   1398 C C   . LEU A 1 180 ? 5.561   -23.274 30.395 1.00 18.11 ? 180 LEU A C   1 
ATOM   1399 O O   . LEU A 1 180 ? 4.972   -22.205 30.567 1.00 18.67 ? 180 LEU A O   1 
ATOM   1400 C CB  . LEU A 1 180 ? 3.804   -24.170 28.828 1.00 18.12 ? 180 LEU A CB  1 
ATOM   1401 C CG  . LEU A 1 180 ? 4.354   -23.610 27.515 1.00 21.66 ? 180 LEU A CG  1 
ATOM   1402 C CD1 . LEU A 1 180 ? 5.009   -24.753 26.777 1.00 21.41 ? 180 LEU A CD1 1 
ATOM   1403 C CD2 . LEU A 1 180 ? 3.243   -23.028 26.673 1.00 19.96 ? 180 LEU A CD2 1 
ATOM   1404 N N   . LEU A 1 181 ? 6.869   -23.410 30.595 1.00 16.78 ? 181 LEU A N   1 
ATOM   1405 C CA  . LEU A 1 181 ? 7.674   -22.346 31.191 1.00 16.66 ? 181 LEU A CA  1 
ATOM   1406 C C   . LEU A 1 181 ? 8.592   -21.769 30.118 1.00 17.00 ? 181 LEU A C   1 
ATOM   1407 O O   . LEU A 1 181 ? 9.539   -22.433 29.694 1.00 18.29 ? 181 LEU A O   1 
ATOM   1408 C CB  . LEU A 1 181 ? 8.466   -22.885 32.383 1.00 16.00 ? 181 LEU A CB  1 
ATOM   1409 C CG  . LEU A 1 181 ? 7.656   -23.691 33.410 1.00 18.24 ? 181 LEU A CG  1 
ATOM   1410 C CD1 . LEU A 1 181 ? 8.576   -24.100 34.548 1.00 18.99 ? 181 LEU A CD1 1 
ATOM   1411 C CD2 . LEU A 1 181 ? 6.452   -22.896 33.955 1.00 13.38 ? 181 LEU A CD2 1 
ATOM   1412 N N   . ILE A 1 182 ? 8.296   -20.545 29.671 1.00 15.54 ? 182 ILE A N   1 
ATOM   1413 C CA  . ILE A 1 182 ? 9.019   -19.887 28.581 1.00 17.20 ? 182 ILE A CA  1 
ATOM   1414 C C   . ILE A 1 182 ? 10.002  -18.893 29.191 1.00 16.51 ? 182 ILE A C   1 
ATOM   1415 O O   . ILE A 1 182 ? 9.588   -17.920 29.825 1.00 17.31 ? 182 ILE A O   1 
ATOM   1416 C CB  . ILE A 1 182 ? 8.047   -19.183 27.615 1.00 17.14 ? 182 ILE A CB  1 
ATOM   1417 C CG1 . ILE A 1 182 ? 7.075   -20.188 26.983 1.00 18.68 ? 182 ILE A CG1 1 
ATOM   1418 C CG2 . ILE A 1 182 ? 8.823   -18.409 26.559 1.00 16.51 ? 182 ILE A CG2 1 
ATOM   1419 C CD1 . ILE A 1 182 ? 5.893   -19.515 26.250 1.00 18.00 ? 182 ILE A CD1 1 
ATOM   1420 N N   . TYR A 1 183 ? 11.312  -19.125 28.983 1.00 16.59 ? 183 TYR A N   1 
ATOM   1421 C CA  . TYR A 1 183 ? 12.423  -18.442 29.654 1.00 16.07 ? 183 TYR A CA  1 
ATOM   1422 C C   . TYR A 1 183 ? 11.994  -17.947 31.034 1.00 16.01 ? 183 TYR A C   1 
ATOM   1423 O O   . TYR A 1 183 ? 11.938  -16.734 31.275 1.00 15.98 ? 183 TYR A O   1 
ATOM   1424 C CB  . TYR A 1 183 ? 13.016  -17.292 28.803 1.00 18.55 ? 183 TYR A CB  1 
ATOM   1425 C CG  . TYR A 1 183 ? 12.063  -16.532 27.864 1.00 18.76 ? 183 TYR A CG  1 
ATOM   1426 C CD1 . TYR A 1 183 ? 11.233  -15.521 28.346 1.00 17.83 ? 183 TYR A CD1 1 
ATOM   1427 C CD2 . TYR A 1 183 ? 12.057  -16.780 26.489 1.00 22.22 ? 183 TYR A CD2 1 
ATOM   1428 C CE1 . TYR A 1 183 ? 10.367  -14.813 27.488 1.00 17.57 ? 183 TYR A CE1 1 
ATOM   1429 C CE2 . TYR A 1 183 ? 11.207  -16.076 25.624 1.00 20.37 ? 183 TYR A CE2 1 
ATOM   1430 C CZ  . TYR A 1 183 ? 10.361  -15.112 26.132 1.00 19.77 ? 183 TYR A CZ  1 
ATOM   1431 O OH  . TYR A 1 183 ? 9.528   -14.425 25.280 1.00 21.90 ? 183 TYR A OH  1 
ATOM   1432 N N   . PRO A 1 184 ? 11.690  -18.858 31.960 1.00 17.18 ? 184 PRO A N   1 
ATOM   1433 C CA  . PRO A 1 184 ? 11.122  -18.459 33.251 1.00 16.96 ? 184 PRO A CA  1 
ATOM   1434 C C   . PRO A 1 184 ? 12.193  -17.986 34.223 1.00 18.77 ? 184 PRO A C   1 
ATOM   1435 O O   . PRO A 1 184 ? 13.371  -18.321 34.113 1.00 16.46 ? 184 PRO A O   1 
ATOM   1436 C CB  . PRO A 1 184 ? 10.487  -19.759 33.755 1.00 18.26 ? 184 PRO A CB  1 
ATOM   1437 C CG  . PRO A 1 184 ? 11.478  -20.824 33.250 1.00 17.62 ? 184 PRO A CG  1 
ATOM   1438 C CD  . PRO A 1 184 ? 11.851  -20.325 31.857 1.00 14.41 ? 184 PRO A CD  1 
ATOM   1439 N N   . SER A 1 185 ? 11.745  -17.205 35.203 1.00 17.09 ? 185 SER A N   1 
ATOM   1440 C CA  . SER A 1 185 ? 12.606  -16.748 36.287 1.00 17.05 ? 185 SER A CA  1 
ATOM   1441 C C   . SER A 1 185 ? 12.313  -17.576 37.533 1.00 19.00 ? 185 SER A C   1 
ATOM   1442 O O   . SER A 1 185 ? 11.610  -17.145 38.451 1.00 19.64 ? 185 SER A O   1 
ATOM   1443 C CB  . SER A 1 185 ? 12.380  -15.272 36.542 1.00 20.57 ? 185 SER A CB  1 
ATOM   1444 O OG  . SER A 1 185 ? 13.276  -14.817 37.538 1.00 29.54 ? 185 SER A OG  1 
ATOM   1445 N N   . THR A 1 186 ? 12.853  -18.792 37.555 1.00 17.13 ? 186 THR A N   1 
ATOM   1446 C CA  . THR A 1 186 ? 12.548  -19.724 38.638 1.00 16.78 ? 186 THR A CA  1 
ATOM   1447 C C   . THR A 1 186 ? 13.530  -19.662 39.811 1.00 19.05 ? 186 THR A C   1 
ATOM   1448 O O   . THR A 1 186 ? 13.393  -20.450 40.749 1.00 16.10 ? 186 THR A O   1 
ATOM   1449 C CB  . THR A 1 186 ? 12.488  -21.150 38.079 1.00 16.37 ? 186 THR A CB  1 
ATOM   1450 O OG1 . THR A 1 186 ? 13.544  -21.319 37.128 1.00 16.31 ? 186 THR A OG1 1 
ATOM   1451 C CG2 . THR A 1 186 ? 11.155  -21.357 37.361 1.00 17.15 ? 186 THR A CG2 1 
ATOM   1452 N N   . GLY A 1 187 ? 14.526  -18.779 39.786 1.00 16.25 ? 187 GLY A N   1 
ATOM   1453 C CA  . GLY A 1 187 ? 15.307  -18.514 40.975 1.00 15.77 ? 187 GLY A CA  1 
ATOM   1454 C C   . GLY A 1 187 ? 16.595  -19.328 41.036 1.00 16.21 ? 187 GLY A C   1 
ATOM   1455 O O   . GLY A 1 187 ? 16.877  -20.189 40.198 1.00 16.50 ? 187 GLY A O   1 
ATOM   1456 N N   . TYR A 1 188 ? 17.386  -19.036 42.063 1.00 16.28 ? 188 TYR A N   1 
ATOM   1457 C CA  . TYR A 1 188 ? 18.671  -19.692 42.293 1.00 17.58 ? 188 TYR A CA  1 
ATOM   1458 C C   . TYR A 1 188 ? 19.190  -19.240 43.653 1.00 22.63 ? 188 TYR A C   1 
ATOM   1459 O O   . TYR A 1 188 ? 18.727  -18.238 44.211 1.00 16.61 ? 188 TYR A O   1 
ATOM   1460 C CB  . TYR A 1 188 ? 19.687  -19.368 41.192 1.00 19.41 ? 188 TYR A CB  1 
ATOM   1461 C CG  . TYR A 1 188 ? 19.929  -17.887 40.981 1.00 17.45 ? 188 TYR A CG  1 
ATOM   1462 C CD1 . TYR A 1 188 ? 19.105  -17.144 40.133 1.00 19.92 ? 188 TYR A CD1 1 
ATOM   1463 C CD2 . TYR A 1 188 ? 20.980  -17.227 41.628 1.00 17.84 ? 188 TYR A CD2 1 
ATOM   1464 C CE1 . TYR A 1 188 ? 19.312  -15.784 39.932 1.00 20.76 ? 188 TYR A CE1 1 
ATOM   1465 C CE2 . TYR A 1 188 ? 21.204  -15.858 41.423 1.00 22.60 ? 188 TYR A CE2 1 
ATOM   1466 C CZ  . TYR A 1 188 ? 20.368  -15.148 40.572 1.00 24.84 ? 188 TYR A CZ  1 
ATOM   1467 O OH  . TYR A 1 188 ? 20.551  -13.798 40.368 1.00 26.55 ? 188 TYR A OH  1 
ATOM   1468 N N   . ASP A 1 189 ? 20.147  -19.994 44.178 1.00 20.30 ? 189 ASP A N   1 
ATOM   1469 C CA  . ASP A 1 189 ? 20.858  -19.600 45.404 1.00 23.63 ? 189 ASP A CA  1 
ATOM   1470 C C   . ASP A 1 189 ? 21.699  -18.363 45.114 1.00 21.55 ? 189 ASP A C   1 
ATOM   1471 O O   . ASP A 1 189 ? 22.638  -18.440 44.307 1.00 24.09 ? 189 ASP A O   1 
ATOM   1472 C CB  . ASP A 1 189 ? 21.735  -20.756 45.895 1.00 26.91 ? 189 ASP A CB  1 
ATOM   1473 C CG  . ASP A 1 189 ? 22.453  -20.453 47.220 1.00 31.36 ? 189 ASP A CG  1 
ATOM   1474 O OD1 . ASP A 1 189 ? 22.349  -19.328 47.760 1.00 27.71 ? 189 ASP A OD1 1 
ATOM   1475 O OD2 . ASP A 1 189 ? 23.117  -21.370 47.735 1.00 37.70 ? 189 ASP A OD2 1 
ATOM   1476 N N   . PRO A 1 190 ? 21.412  -17.215 45.737 1.00 21.07 ? 190 PRO A N   1 
ATOM   1477 C CA  . PRO A 1 190 ? 22.165  -15.996 45.397 1.00 23.96 ? 190 PRO A CA  1 
ATOM   1478 C C   . PRO A 1 190 ? 23.658  -16.119 45.668 1.00 23.61 ? 190 PRO A C   1 
ATOM   1479 O O   . PRO A 1 190 ? 24.432  -15.332 45.121 1.00 25.04 ? 190 PRO A O   1 
ATOM   1480 C CB  . PRO A 1 190 ? 21.518  -14.914 46.278 1.00 27.12 ? 190 PRO A CB  1 
ATOM   1481 C CG  . PRO A 1 190 ? 20.189  -15.506 46.737 1.00 29.27 ? 190 PRO A CG  1 
ATOM   1482 C CD  . PRO A 1 190 ? 20.430  -16.984 46.817 1.00 25.20 ? 190 PRO A CD  1 
ATOM   1483 N N   . ALA A 1 191 ? 24.083  -17.084 46.477 1.00 22.53 ? 191 ALA A N   1 
ATOM   1484 C CA  . ALA A 1 191 ? 25.509  -17.304 46.693 1.00 32.41 ? 191 ALA A CA  1 
ATOM   1485 C C   . ALA A 1 191 ? 26.162  -18.075 45.559 1.00 30.69 ? 191 ALA A C   1 
ATOM   1486 O O   . ALA A 1 191 ? 27.389  -18.120 45.480 1.00 33.40 ? 191 ALA A O   1 
ATOM   1487 C CB  . ALA A 1 191 ? 25.742  -18.058 47.999 1.00 28.79 ? 191 ALA A CB  1 
ATOM   1488 N N   . HIS A 1 192 ? 25.390  -18.695 44.677 1.00 25.28 ? 192 HIS A N   1 
ATOM   1489 C CA  . HIS A 1 192 ? 25.947  -19.461 43.559 1.00 27.21 ? 192 HIS A CA  1 
ATOM   1490 C C   . HIS A 1 192 ? 25.130  -19.170 42.305 1.00 22.12 ? 192 HIS A C   1 
ATOM   1491 O O   . HIS A 1 192 ? 24.379  -20.017 41.809 1.00 21.38 ? 192 HIS A O   1 
ATOM   1492 C CB  . HIS A 1 192 ? 26.001  -20.957 43.890 1.00 34.20 ? 192 HIS A CB  1 
ATOM   1493 C CG  . HIS A 1 192 ? 26.620  -21.239 45.217 1.00 45.24 ? 192 HIS A CG  1 
ATOM   1494 N ND1 . HIS A 1 192 ? 27.941  -21.527 45.376 1.00 51.60 ? 192 HIS A ND1 1 
ATOM   1495 C CD2 . HIS A 1 192 ? 26.102  -21.225 46.458 1.00 45.23 ? 192 HIS A CD2 1 
ATOM   1496 C CE1 . HIS A 1 192 ? 28.223  -21.658 46.657 1.00 50.36 ? 192 HIS A CE1 1 
ATOM   1497 N NE2 . HIS A 1 192 ? 27.110  -21.538 47.332 1.00 47.44 ? 192 HIS A NE2 1 
ATOM   1498 N N   . PRO A 1 193 ? 25.277  -17.975 41.748 1.00 20.82 ? 193 PRO A N   1 
ATOM   1499 C CA  . PRO A 1 193 ? 24.513  -17.622 40.537 1.00 22.00 ? 193 PRO A CA  1 
ATOM   1500 C C   . PRO A 1 193 ? 24.932  -18.505 39.375 1.00 20.71 ? 193 PRO A C   1 
ATOM   1501 O O   . PRO A 1 193 ? 26.130  -18.766 39.187 1.00 20.88 ? 193 PRO A O   1 
ATOM   1502 C CB  . PRO A 1 193 ? 24.877  -16.145 40.289 1.00 22.28 ? 193 PRO A CB  1 
ATOM   1503 C CG  . PRO A 1 193 ? 26.113  -15.900 41.125 1.00 24.78 ? 193 PRO A CG  1 
ATOM   1504 C CD  . PRO A 1 193 ? 26.179  -16.897 42.190 1.00 24.21 ? 193 PRO A CD  1 
ATOM   1505 N N   . PRO A 1 194 ? 23.972  -19.006 38.602 1.00 18.30 ? 194 PRO A N   1 
ATOM   1506 C CA  . PRO A 1 194 ? 24.320  -19.776 37.407 1.00 19.86 ? 194 PRO A CA  1 
ATOM   1507 C C   . PRO A 1 194 ? 25.066  -18.888 36.420 1.00 19.73 ? 194 PRO A C   1 
ATOM   1508 O O   . PRO A 1 194 ? 24.924  -17.664 36.423 1.00 17.16 ? 194 PRO A O   1 
ATOM   1509 C CB  . PRO A 1 194 ? 22.956  -20.214 36.858 1.00 18.82 ? 194 PRO A CB  1 
ATOM   1510 C CG  . PRO A 1 194 ? 22.016  -20.143 38.046 1.00 19.13 ? 194 PRO A CG  1 
ATOM   1511 C CD  . PRO A 1 194 ? 22.513  -18.943 38.812 1.00 19.52 ? 194 PRO A CD  1 
ATOM   1512 N N   . ALA A 1 195 ? 25.875  -19.524 35.567 1.00 16.59 ? 195 ALA A N   1 
ATOM   1513 C CA  . ALA A 1 195 ? 26.825  -18.775 34.745 1.00 17.98 ? 195 ALA A CA  1 
ATOM   1514 C C   . ALA A 1 195 ? 26.151  -17.657 33.955 1.00 19.38 ? 195 ALA A C   1 
ATOM   1515 O O   . ALA A 1 195 ? 26.655  -16.532 33.913 1.00 19.19 ? 195 ALA A O   1 
ATOM   1516 C CB  . ALA A 1 195 ? 27.565  -19.726 33.802 1.00 19.10 ? 195 ALA A CB  1 
ATOM   1517 N N   . SER A 1 196 ? 25.001  -17.942 33.329 1.00 16.68 ? 196 SER A N   1 
ATOM   1518 C CA  . SER A 1 196 ? 24.392  -16.965 32.424 1.00 17.28 ? 196 SER A CA  1 
ATOM   1519 C C   . SER A 1 196 ? 24.041  -15.672 33.135 1.00 15.77 ? 196 SER A C   1 
ATOM   1520 O O   . SER A 1 196 ? 23.965  -14.625 32.491 1.00 16.79 ? 196 SER A O   1 
ATOM   1521 C CB  . SER A 1 196 ? 23.119  -17.528 31.782 1.00 17.29 ? 196 SER A CB  1 
ATOM   1522 O OG  . SER A 1 196 ? 22.186  -17.836 32.809 1.00 17.95 ? 196 SER A OG  1 
ATOM   1523 N N   . ILE A 1 197 ? 23.783  -15.732 34.448 1.00 16.38 ? 197 ILE A N   1 
ATOM   1524 C CA  . ILE A 1 197 ? 23.413  -14.534 35.191 1.00 18.01 ? 197 ILE A CA  1 
ATOM   1525 C C   . ILE A 1 197 ? 24.500  -13.473 35.060 1.00 20.63 ? 197 ILE A C   1 
ATOM   1526 O O   . ILE A 1 197 ? 24.212  -12.275 34.949 1.00 20.67 ? 197 ILE A O   1 
ATOM   1527 C CB  . ILE A 1 197 ? 23.137  -14.880 36.669 1.00 16.80 ? 197 ILE A CB  1 
ATOM   1528 C CG1 . ILE A 1 197 ? 21.804  -15.642 36.829 1.00 18.99 ? 197 ILE A CG1 1 
ATOM   1529 C CG2 . ILE A 1 197 ? 23.169  -13.604 37.512 1.00 19.57 ? 197 ILE A CG2 1 
ATOM   1530 C CD1 . ILE A 1 197 ? 20.557  -14.797 36.613 1.00 17.96 ? 197 ILE A CD1 1 
ATOM   1531 N N   . GLU A 1 198 ? 25.762  -13.898 35.050 1.00 18.53 ? 198 GLU A N   1 
ATOM   1532 C CA  . GLU A 1 198 ? 26.891  -12.992 34.883 1.00 21.25 ? 198 GLU A CA  1 
ATOM   1533 C C   . GLU A 1 198 ? 27.395  -12.941 33.448 1.00 18.20 ? 198 GLU A C   1 
ATOM   1534 O O   . GLU A 1 198 ? 27.696  -11.860 32.947 1.00 20.80 ? 198 GLU A O   1 
ATOM   1535 C CB  . GLU A 1 198 ? 28.012  -13.397 35.853 1.00 20.11 ? 198 GLU A CB  1 
ATOM   1536 C CG  . GLU A 1 198 ? 27.543  -13.162 37.287 1.00 21.09 ? 198 GLU A CG  1 
ATOM   1537 C CD  . GLU A 1 198 ? 28.490  -13.657 38.359 1.00 24.68 ? 198 GLU A CD  1 
ATOM   1538 O OE1 . GLU A 1 198 ? 29.713  -13.615 38.158 1.00 24.51 ? 198 GLU A OE1 1 
ATOM   1539 O OE2 . GLU A 1 198 ? 27.996  -14.079 39.427 1.00 28.87 ? 198 GLU A OE2 1 
ATOM   1540 N N   . GLU A 1 199 ? 27.419  -14.074 32.745 1.00 18.79 ? 199 GLU A N   1 
ATOM   1541 C CA  . GLU A 1 199 ? 27.847  -14.067 31.344 1.00 21.08 ? 199 GLU A CA  1 
ATOM   1542 C C   . GLU A 1 199 ? 26.967  -13.159 30.492 1.00 24.24 ? 199 GLU A C   1 
ATOM   1543 O O   . GLU A 1 199 ? 27.473  -12.389 29.668 1.00 21.26 ? 199 GLU A O   1 
ATOM   1544 C CB  . GLU A 1 199 ? 27.828  -15.496 30.789 1.00 21.26 ? 199 GLU A CB  1 
ATOM   1545 C CG  . GLU A 1 199 ? 28.281  -15.630 29.341 1.00 22.24 ? 199 GLU A CG  1 
ATOM   1546 C CD  . GLU A 1 199 ? 28.077  -17.036 28.797 1.00 27.10 ? 199 GLU A CD  1 
ATOM   1547 O OE1 . GLU A 1 199 ? 27.142  -17.713 29.269 1.00 24.76 ? 199 GLU A OE1 1 
ATOM   1548 O OE2 . GLU A 1 199 ? 28.863  -17.473 27.919 1.00 30.74 ? 199 GLU A OE2 1 
ATOM   1549 N N   . ASN A 1 200 ? 25.643  -13.212 30.690 1.00 17.29 ? 200 ASN A N   1 
ATOM   1550 C CA  . ASN A 1 200 ? 24.709  -12.490 29.837 1.00 20.88 ? 200 ASN A CA  1 
ATOM   1551 C C   . ASN A 1 200 ? 24.109  -11.274 30.532 1.00 20.91 ? 200 ASN A C   1 
ATOM   1552 O O   . ASN A 1 200 ? 23.018  -10.827 30.167 1.00 21.01 ? 200 ASN A O   1 
ATOM   1553 C CB  . ASN A 1 200 ? 23.598  -13.424 29.352 1.00 21.19 ? 200 ASN A CB  1 
ATOM   1554 C CG  . ASN A 1 200 ? 24.115  -14.541 28.464 1.00 25.50 ? 200 ASN A CG  1 
ATOM   1555 O OD1 . ASN A 1 200 ? 25.140  -14.392 27.800 1.00 23.69 ? 200 ASN A OD1 1 
ATOM   1556 N ND2 . ASN A 1 200 ? 23.413  -15.681 28.461 1.00 19.53 ? 200 ASN A ND2 1 
ATOM   1557 N N   . ALA A 1 201 ? 24.817  -10.710 31.515 1.00 17.42 ? 201 ALA A N   1 
ATOM   1558 C CA  . ALA A 1 201 ? 24.235  -9.664  32.358 1.00 19.30 ? 201 ALA A CA  1 
ATOM   1559 C C   . ALA A 1 201 ? 24.077  -8.329  31.638 1.00 22.89 ? 201 ALA A C   1 
ATOM   1560 O O   . ALA A 1 201 ? 23.320  -7.477  32.110 1.00 20.35 ? 201 ALA A O   1 
ATOM   1561 C CB  . ALA A 1 201 ? 25.095  -9.435  33.605 1.00 22.81 ? 201 ALA A CB  1 
ATOM   1562 N N   . GLU A 1 202 ? 24.803  -8.109  30.547 1.00 22.02 ? 202 GLU A N   1 
ATOM   1563 C CA  . GLU A 1 202 ? 24.749  -6.854  29.820 1.00 26.82 ? 202 GLU A CA  1 
ATOM   1564 C C   . GLU A 1 202 ? 24.628  -7.138  28.333 1.00 22.92 ? 202 GLU A C   1 
ATOM   1565 O O   . GLU A 1 202 ? 25.155  -8.128  27.827 1.00 26.46 ? 202 GLU A O   1 
ATOM   1566 C CB  . GLU A 1 202 ? 26.005  -5.973  30.083 1.00 30.22 ? 202 GLU A CB  1 
ATOM   1567 C CG  . GLU A 1 202 ? 26.191  -5.575  31.546 1.00 30.25 ? 202 GLU A CG  1 
ATOM   1568 C CD  . GLU A 1 202 ? 25.026  -4.756  32.084 1.00 40.29 ? 202 GLU A CD  1 
ATOM   1569 O OE1 . GLU A 1 202 ? 24.702  -4.902  33.287 1.00 47.67 ? 202 GLU A OE1 1 
ATOM   1570 O OE2 . GLU A 1 202 ? 24.428  -3.970  31.309 1.00 40.70 ? 202 GLU A OE2 1 
ATOM   1571 N N   . GLY A 1 203 ? 23.920  -6.264  27.637 1.00 25.70 ? 203 GLY A N   1 
ATOM   1572 C CA  . GLY A 1 203 ? 23.943  -6.261  26.192 1.00 28.30 ? 203 GLY A CA  1 
ATOM   1573 C C   . GLY A 1 203 ? 22.771  -6.933  25.515 1.00 29.34 ? 203 GLY A C   1 
ATOM   1574 O O   . GLY A 1 203 ? 22.633  -6.793  24.292 1.00 26.30 ? 203 GLY A O   1 
ATOM   1575 N N   . TYR A 1 204 ? 21.920  -7.656  26.255 1.00 24.87 ? 204 TYR A N   1 
ATOM   1576 C CA  . TYR A 1 204 ? 20.892  -8.478  25.624 1.00 23.33 ? 204 TYR A CA  1 
ATOM   1577 C C   . TYR A 1 204 ? 19.496  -8.149  26.136 1.00 22.64 ? 204 TYR A C   1 
ATOM   1578 O O   . TYR A 1 204 ? 18.695  -9.045  26.409 1.00 21.83 ? 204 TYR A O   1 
ATOM   1579 C CB  . TYR A 1 204 ? 21.189  -9.963  25.811 1.00 24.96 ? 204 TYR A CB  1 
ATOM   1580 C CG  . TYR A 1 204 ? 22.526  -10.345 25.250 1.00 28.53 ? 204 TYR A CG  1 
ATOM   1581 C CD1 . TYR A 1 204 ? 22.744  -10.364 23.877 1.00 29.58 ? 204 TYR A CD1 1 
ATOM   1582 C CD2 . TYR A 1 204 ? 23.580  -10.671 26.087 1.00 33.21 ? 204 TYR A CD2 1 
ATOM   1583 C CE1 . TYR A 1 204 ? 23.977  -10.703 23.352 1.00 31.85 ? 204 TYR A CE1 1 
ATOM   1584 C CE2 . TYR A 1 204 ? 24.819  -11.018 25.575 1.00 31.43 ? 204 TYR A CE2 1 
ATOM   1585 C CZ  . TYR A 1 204 ? 25.013  -11.032 24.208 1.00 35.94 ? 204 TYR A CZ  1 
ATOM   1586 O OH  . TYR A 1 204 ? 26.252  -11.375 23.707 1.00 41.31 ? 204 TYR A OH  1 
ATOM   1587 N N   . LEU A 1 205 ? 19.202  -6.854  26.261 1.00 20.75 ? 205 LEU A N   1 
ATOM   1588 C CA  . LEU A 1 205 ? 17.869  -6.328  26.562 1.00 25.44 ? 205 LEU A CA  1 
ATOM   1589 C C   . LEU A 1 205 ? 17.520  -6.510  28.034 1.00 25.55 ? 205 LEU A C   1 
ATOM   1590 O O   . LEU A 1 205 ? 17.404  -5.518  28.760 1.00 24.92 ? 205 LEU A O   1 
ATOM   1591 C CB  . LEU A 1 205 ? 16.807  -6.970  25.663 1.00 27.01 ? 205 LEU A CB  1 
ATOM   1592 C CG  . LEU A 1 205 ? 15.505  -6.177  25.479 1.00 36.22 ? 205 LEU A CG  1 
ATOM   1593 C CD1 . LEU A 1 205 ? 14.807  -6.612  24.204 1.00 37.79 ? 205 LEU A CD1 1 
ATOM   1594 C CD2 . LEU A 1 205 ? 14.586  -6.354  26.677 1.00 35.05 ? 205 LEU A CD2 1 
ATOM   1595 N N   . LEU A 1 206 ? 17.327  -7.752  28.491 1.00 19.29 ? 206 LEU A N   1 
ATOM   1596 C CA  . LEU A 1 206 ? 17.222  -7.999  29.927 1.00 20.60 ? 206 LEU A CA  1 
ATOM   1597 C C   . LEU A 1 206 ? 18.622  -8.004  30.526 1.00 19.63 ? 206 LEU A C   1 
ATOM   1598 O O   . LEU A 1 206 ? 19.456  -8.833  30.147 1.00 22.06 ? 206 LEU A O   1 
ATOM   1599 C CB  . LEU A 1 206 ? 16.522  -9.327  30.218 1.00 19.83 ? 206 LEU A CB  1 
ATOM   1600 C CG  . LEU A 1 206 ? 16.357  -9.601  31.719 1.00 19.88 ? 206 LEU A CG  1 
ATOM   1601 C CD1 . LEU A 1 206 ? 15.395  -8.568  32.334 1.00 23.74 ? 206 LEU A CD1 1 
ATOM   1602 C CD2 . LEU A 1 206 ? 15.862  -11.026 31.954 1.00 23.37 ? 206 LEU A CD2 1 
ATOM   1603 N N   . THR A 1 207 ? 18.876  -7.089  31.455 1.00 20.13 ? 207 THR A N   1 
ATOM   1604 C CA  . THR A 1 207 ? 20.190  -6.894  32.049 1.00 25.41 ? 207 THR A CA  1 
ATOM   1605 C C   . THR A 1 207 ? 20.155  -7.211  33.539 1.00 24.63 ? 207 THR A C   1 
ATOM   1606 O O   . THR A 1 207 ? 19.092  -7.240  34.168 1.00 22.28 ? 207 THR A O   1 
ATOM   1607 C CB  . THR A 1 207 ? 20.684  -5.449  31.865 1.00 26.46 ? 207 THR A CB  1 
ATOM   1608 O OG1 . THR A 1 207 ? 19.819  -4.557  32.584 1.00 25.31 ? 207 THR A OG1 1 
ATOM   1609 C CG2 . THR A 1 207 ? 20.717  -5.063  30.390 1.00 25.04 ? 207 THR A CG2 1 
ATOM   1610 N N   . GLY A 1 208 ? 21.348  -7.412  34.102 1.00 21.76 ? 208 GLY A N   1 
ATOM   1611 C CA  . GLY A 1 208 ? 21.458  -7.628  35.537 1.00 21.49 ? 208 GLY A CA  1 
ATOM   1612 C C   . GLY A 1 208 ? 20.892  -6.486  36.363 1.00 25.17 ? 208 GLY A C   1 
ATOM   1613 O O   . GLY A 1 208 ? 20.215  -6.714  37.369 1.00 21.88 ? 208 GLY A O   1 
ATOM   1614 N N   . GLY A 1 209 ? 21.151  -5.239  35.951 1.00 18.56 ? 209 GLY A N   1 
ATOM   1615 C CA  . GLY A 1 209 ? 20.577  -4.112  36.670 1.00 22.31 ? 209 GLY A CA  1 
ATOM   1616 C C   . GLY A 1 209 ? 19.058  -4.084  36.598 1.00 22.54 ? 209 GLY A C   1 
ATOM   1617 O O   . GLY A 1 209 ? 18.379  -3.800  37.593 1.00 21.44 ? 209 GLY A O   1 
ATOM   1618 N N   . MET A 1 210 ? 18.507  -4.392  35.423 1.00 20.24 ? 210 MET A N   1 
ATOM   1619 C CA  . MET A 1 210 ? 17.057  -4.475  35.282 1.00 23.90 ? 210 MET A CA  1 
ATOM   1620 C C   . MET A 1 210 ? 16.480  -5.554  36.198 1.00 20.84 ? 210 MET A C   1 
ATOM   1621 O O   . MET A 1 210 ? 15.455  -5.339  36.856 1.00 21.30 ? 210 MET A O   1 
ATOM   1622 C CB  . MET A 1 210 ? 16.697  -4.757  33.820 1.00 23.62 ? 210 MET A CB  1 
ATOM   1623 C CG  . MET A 1 210 ? 15.207  -4.686  33.496 1.00 32.32 ? 210 MET A CG  1 
ATOM   1624 S SD  . MET A 1 210 ? 14.745  -3.067  32.859 1.00 66.47 ? 210 MET A SD  1 
ATOM   1625 C CE  . MET A 1 210 ? 14.314  -2.241  34.385 1.00 32.64 ? 210 MET A CE  1 
ATOM   1626 N N   . MET A 1 211 ? 17.127  -6.718  36.257 1.00 18.61 ? 211 MET A N   1 
ATOM   1627 C CA  . MET A 1 211 ? 16.637  -7.814  37.089 1.00 20.64 ? 211 MET A CA  1 
ATOM   1628 C C   . MET A 1 211 ? 16.592  -7.396  38.549 1.00 21.67 ? 211 MET A C   1 
ATOM   1629 O O   . MET A 1 211 ? 15.597  -7.625  39.233 1.00 19.70 ? 211 MET A O   1 
ATOM   1630 C CB  . MET A 1 211 ? 17.522  -9.051  36.893 1.00 19.98 ? 211 MET A CB  1 
ATOM   1631 C CG  . MET A 1 211 ? 17.360  -9.701  35.510 1.00 22.69 ? 211 MET A CG  1 
ATOM   1632 S SD  . MET A 1 211 ? 18.406  -11.168 35.320 1.00 28.18 ? 211 MET A SD  1 
ATOM   1633 C CE  . MET A 1 211 ? 17.808  -12.194 36.650 1.00 29.39 ? 211 MET A CE  1 
ATOM   1634 N N   . LEU A 1 212 ? 17.656  -6.747  39.039 1.00 20.15 ? 212 LEU A N   1 
ATOM   1635 C CA  . LEU A 1 212 ? 17.655  -6.287  40.425 1.00 22.84 ? 212 LEU A CA  1 
ATOM   1636 C C   . LEU A 1 212 ? 16.576  -5.234  40.668 1.00 19.76 ? 212 LEU A C   1 
ATOM   1637 O O   . LEU A 1 212 ? 15.988  -5.179  41.754 1.00 20.70 ? 212 LEU A O   1 
ATOM   1638 C CB  . LEU A 1 212 ? 19.030  -5.736  40.799 1.00 25.21 ? 212 LEU A CB  1 
ATOM   1639 C CG  . LEU A 1 212 ? 20.148  -6.784  40.887 1.00 31.87 ? 212 LEU A CG  1 
ATOM   1640 C CD1 . LEU A 1 212 ? 21.522  -6.153  40.704 1.00 40.28 ? 212 LEU A CD1 1 
ATOM   1641 C CD2 . LEU A 1 212 ? 20.076  -7.564  42.197 1.00 41.95 ? 212 LEU A CD2 1 
ATOM   1642 N N   . TRP A 1 213 ? 16.324  -4.377  39.677 1.00 19.44 ? 213 TRP A N   1 
ATOM   1643 C CA  . TRP A 1 213 ? 15.282  -3.358  39.820 1.00 21.72 ? 213 TRP A CA  1 
ATOM   1644 C C   . TRP A 1 213 ? 13.901  -4.000  39.926 1.00 19.58 ? 213 TRP A C   1 
ATOM   1645 O O   . TRP A 1 213 ? 13.109  -3.643  40.806 1.00 19.41 ? 213 TRP A O   1 
ATOM   1646 C CB  . TRP A 1 213 ? 15.330  -2.380  38.646 1.00 17.74 ? 213 TRP A CB  1 
ATOM   1647 C CG  . TRP A 1 213 ? 14.313  -1.252  38.751 1.00 23.43 ? 213 TRP A CG  1 
ATOM   1648 C CD1 . TRP A 1 213 ? 14.470  -0.051  39.400 1.00 25.05 ? 213 TRP A CD1 1 
ATOM   1649 C CD2 . TRP A 1 213 ? 12.994  -1.231  38.187 1.00 20.86 ? 213 TRP A CD2 1 
ATOM   1650 N NE1 . TRP A 1 213 ? 13.320  0.711   39.270 1.00 22.42 ? 213 TRP A NE1 1 
ATOM   1651 C CE2 . TRP A 1 213 ? 12.408  0.011   38.525 1.00 23.19 ? 213 TRP A CE2 1 
ATOM   1652 C CE3 . TRP A 1 213 ? 12.248  -2.146  37.427 1.00 21.48 ? 213 TRP A CE3 1 
ATOM   1653 C CZ2 . TRP A 1 213 ? 11.113  0.358   38.133 1.00 22.96 ? 213 TRP A CZ2 1 
ATOM   1654 C CZ3 . TRP A 1 213 ? 10.977  -1.788  37.022 1.00 22.29 ? 213 TRP A CZ3 1 
ATOM   1655 C CH2 . TRP A 1 213 ? 10.422  -0.550  37.381 1.00 24.67 ? 213 TRP A CH2 1 
ATOM   1656 N N   . PHE A 1 214 ? 13.597  -4.964  39.047 1.00 18.29 ? 214 PHE A N   1 
ATOM   1657 C CA  . PHE A 1 214 ? 12.302  -5.658  39.142 1.00 18.14 ? 214 PHE A CA  1 
ATOM   1658 C C   . PHE A 1 214 ? 12.122  -6.277  40.515 1.00 19.40 ? 214 PHE A C   1 
ATOM   1659 O O   . PHE A 1 214 ? 11.048  -6.201  41.122 1.00 19.49 ? 214 PHE A O   1 
ATOM   1660 C CB  . PHE A 1 214 ? 12.196  -6.768  38.100 1.00 19.32 ? 214 PHE A CB  1 
ATOM   1661 C CG  . PHE A 1 214 ? 11.930  -6.304  36.702 1.00 20.70 ? 214 PHE A CG  1 
ATOM   1662 C CD1 . PHE A 1 214 ? 10.942  -5.368  36.427 1.00 22.82 ? 214 PHE A CD1 1 
ATOM   1663 C CD2 . PHE A 1 214 ? 12.619  -6.883  35.648 1.00 21.96 ? 214 PHE A CD2 1 
ATOM   1664 C CE1 . PHE A 1 214 ? 10.682  -4.979  35.121 1.00 21.55 ? 214 PHE A CE1 1 
ATOM   1665 C CE2 . PHE A 1 214 ? 12.373  -6.502  34.341 1.00 25.04 ? 214 PHE A CE2 1 
ATOM   1666 C CZ  . PHE A 1 214 ? 11.406  -5.546  34.078 1.00 26.35 ? 214 PHE A CZ  1 
ATOM   1667 N N   . ARG A 1 215 ? 13.171  -6.926  41.004 1.00 21.80 ? 215 ARG A N   1 
ATOM   1668 C CA  . ARG A 1 215 ? 13.117  -7.615  42.282 1.00 22.23 ? 215 ARG A CA  1 
ATOM   1669 C C   . ARG A 1 215 ? 12.890  -6.647  43.433 1.00 21.96 ? 215 ARG A C   1 
ATOM   1670 O O   . ARG A 1 215 ? 12.135  -6.947  44.368 1.00 21.72 ? 215 ARG A O   1 
ATOM   1671 C CB  . ARG A 1 215 ? 14.427  -8.368  42.459 1.00 24.57 ? 215 ARG A CB  1 
ATOM   1672 C CG  . ARG A 1 215 ? 14.460  -9.433  43.471 1.00 30.69 ? 215 ARG A CG  1 
ATOM   1673 C CD  . ARG A 1 215 ? 15.912  -9.796  43.631 1.00 39.73 ? 215 ARG A CD  1 
ATOM   1674 N NE  . ARG A 1 215 ? 16.680  -8.693  44.210 1.00 38.92 ? 215 ARG A NE  1 
ATOM   1675 C CZ  . ARG A 1 215 ? 17.972  -8.760  44.522 1.00 44.57 ? 215 ARG A CZ  1 
ATOM   1676 N NH1 . ARG A 1 215 ? 18.652  -9.885  44.314 1.00 40.47 ? 215 ARG A NH1 1 
ATOM   1677 N NH2 . ARG A 1 215 ? 18.582  -7.699  45.041 1.00 43.61 ? 215 ARG A NH2 1 
ATOM   1678 N N   . ASP A 1 216 ? 13.554  -5.487  43.391 1.00 18.13 ? 216 ASP A N   1 
ATOM   1679 C CA  . ASP A 1 216 ? 13.324  -4.450  44.396 1.00 20.61 ? 216 ASP A CA  1 
ATOM   1680 C C   . ASP A 1 216 ? 11.887  -3.940  44.360 1.00 19.29 ? 216 ASP A C   1 
ATOM   1681 O O   . ASP A 1 216 ? 11.308  -3.613  45.407 1.00 21.81 ? 216 ASP A O   1 
ATOM   1682 C CB  . ASP A 1 216 ? 14.298  -3.292  44.172 1.00 23.89 ? 216 ASP A CB  1 
ATOM   1683 C CG  . ASP A 1 216 ? 15.734  -3.655  44.529 1.00 33.90 ? 216 ASP A CG  1 
ATOM   1684 O OD1 . ASP A 1 216 ? 15.948  -4.704  45.179 1.00 35.51 ? 216 ASP A OD1 1 
ATOM   1685 O OD2 . ASP A 1 216 ? 16.643  -2.890  44.144 1.00 36.32 ? 216 ASP A OD2 1 
ATOM   1686 N N   . GLN A 1 217 ? 11.297  -3.845  43.167 1.00 17.76 ? 217 GLN A N   1 
ATOM   1687 C CA  . GLN A 1 217 ? 9.899   -3.414  43.079 1.00 20.04 ? 217 GLN A CA  1 
ATOM   1688 C C   . GLN A 1 217 ? 8.954   -4.476  43.632 1.00 21.67 ? 217 GLN A C   1 
ATOM   1689 O O   . GLN A 1 217 ? 7.957   -4.155  44.295 1.00 18.82 ? 217 GLN A O   1 
ATOM   1690 C CB  . GLN A 1 217 ? 9.540   -3.105  41.627 1.00 20.70 ? 217 GLN A CB  1 
ATOM   1691 C CG  . GLN A 1 217 ? 10.403  -2.048  40.973 1.00 25.01 ? 217 GLN A CG  1 
ATOM   1692 C CD  . GLN A 1 217 ? 10.292  -0.705  41.673 1.00 26.08 ? 217 GLN A CD  1 
ATOM   1693 O OE1 . GLN A 1 217 ? 9.194   -0.225  41.946 1.00 26.12 ? 217 GLN A OE1 1 
ATOM   1694 N NE2 . GLN A 1 217 ? 11.429  -0.103  41.978 1.00 29.91 ? 217 GLN A NE2 1 
ATOM   1695 N N   . TYR A 1 218 ? 9.266   -5.748  43.379 1.00 21.30 ? 218 TYR A N   1 
ATOM   1696 C CA  . TYR A 1 218 ? 8.354   -6.857  43.656 1.00 18.81 ? 218 TYR A CA  1 
ATOM   1697 C C   . TYR A 1 218 ? 8.407   -7.269  45.119 1.00 17.67 ? 218 TYR A C   1 
ATOM   1698 O O   . TYR A 1 218 ? 7.363   -7.423  45.769 1.00 15.18 ? 218 TYR A O   1 
ATOM   1699 C CB  . TYR A 1 218 ? 8.723   -8.039  42.742 1.00 18.83 ? 218 TYR A CB  1 
ATOM   1700 C CG  . TYR A 1 218 ? 7.848   -9.281  42.824 1.00 18.36 ? 218 TYR A CG  1 
ATOM   1701 C CD1 . TYR A 1 218 ? 6.461   -9.191  42.842 1.00 18.84 ? 218 TYR A CD1 1 
ATOM   1702 C CD2 . TYR A 1 218 ? 8.420   -10.550 42.807 1.00 15.30 ? 218 TYR A CD2 1 
ATOM   1703 C CE1 . TYR A 1 218 ? 5.665   -10.340 42.885 1.00 20.07 ? 218 TYR A CE1 1 
ATOM   1704 C CE2 . TYR A 1 218 ? 7.629   -11.701 42.847 1.00 16.76 ? 218 TYR A CE2 1 
ATOM   1705 C CZ  . TYR A 1 218 ? 6.262   -11.588 42.879 1.00 18.74 ? 218 TYR A CZ  1 
ATOM   1706 O OH  . TYR A 1 218 ? 5.482   -12.734 42.911 1.00 16.56 ? 218 TYR A OH  1 
ATOM   1707 N N   . LEU A 1 219 ? 9.613   -7.440  45.653 1.00 16.59 ? 219 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 219 ? 9.803   -8.029  46.971 1.00 19.83 ? 219 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 219 ? 9.662   -6.981  48.069 1.00 22.07 ? 219 LEU A C   1 
ATOM   1710 O O   . LEU A 1 219 ? 9.880   -5.789  47.857 1.00 20.07 ? 219 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 219 ? 11.180  -8.706  47.073 1.00 21.64 ? 219 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 219 ? 11.409  -9.911  46.147 1.00 19.17 ? 219 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 219 ? 12.762  -10.589 46.427 1.00 22.77 ? 219 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 219 ? 10.264  -10.930 46.242 1.00 16.95 ? 219 LEU A CD2 1 
ATOM   1715 N N   . ASN A 1 220 ? 9.286   -7.446  49.259 1.00 21.10 ? 220 ASN A N   1 
ATOM   1716 C CA  . ASN A 1 220 ? 9.233   -6.558  50.412 1.00 25.70 ? 220 ASN A CA  1 
ATOM   1717 C C   . ASN A 1 220 ? 10.613  -6.321  51.000 1.00 28.46 ? 220 ASN A C   1 
ATOM   1718 O O   . ASN A 1 220 ? 10.875  -5.241  51.534 1.00 29.88 ? 220 ASN A O   1 
ATOM   1719 C CB  . ASN A 1 220 ? 8.295   -7.136  51.477 1.00 27.31 ? 220 ASN A CB  1 
ATOM   1720 C CG  . ASN A 1 220 ? 6.893   -7.354  50.946 1.00 27.65 ? 220 ASN A CG  1 
ATOM   1721 O OD1 . ASN A 1 220 ? 6.174   -6.397  50.664 1.00 27.65 ? 220 ASN A OD1 1 
ATOM   1722 N ND2 . ASN A 1 220 ? 6.504   -8.615  50.790 1.00 27.61 ? 220 ASN A ND2 1 
ATOM   1723 N N   . SER A 1 221 ? 11.496  -7.313  50.920 1.00 25.86 ? 221 SER A N   1 
ATOM   1724 C CA  . SER A 1 221 ? 12.870  -7.170  51.373 1.00 31.11 ? 221 SER A CA  1 
ATOM   1725 C C   . SER A 1 221 ? 13.684  -8.258  50.696 1.00 31.84 ? 221 SER A C   1 
ATOM   1726 O O   . SER A 1 221 ? 13.136  -9.232  50.171 1.00 24.73 ? 221 SER A O   1 
ATOM   1727 C CB  . SER A 1 221 ? 12.975  -7.260  52.901 1.00 33.08 ? 221 SER A CB  1 
ATOM   1728 O OG  . SER A 1 221 ? 13.076  -8.604  53.331 1.00 35.09 ? 221 SER A OG  1 
ATOM   1729 N N   . LEU A 1 222 ? 15.007  -8.087  50.712 1.00 27.26 ? 222 LEU A N   1 
ATOM   1730 C CA  . LEU A 1 222 ? 15.862  -9.058  50.049 1.00 30.68 ? 222 LEU A CA  1 
ATOM   1731 C C   . LEU A 1 222 ? 16.001  -10.345 50.842 1.00 29.69 ? 222 LEU A C   1 
ATOM   1732 O O   . LEU A 1 222 ? 16.597  -11.304 50.337 1.00 27.82 ? 222 LEU A O   1 
ATOM   1733 C CB  . LEU A 1 222 ? 17.242  -8.456  49.772 1.00 35.05 ? 222 LEU A CB  1 
ATOM   1734 C CG  . LEU A 1 222 ? 17.252  -7.405  48.659 1.00 36.33 ? 222 LEU A CG  1 
ATOM   1735 C CD1 . LEU A 1 222 ? 18.680  -7.119  48.225 1.00 41.29 ? 222 LEU A CD1 1 
ATOM   1736 C CD2 . LEU A 1 222 ? 16.393  -7.834  47.474 1.00 37.28 ? 222 LEU A CD2 1 
ATOM   1737 N N   . GLU A 1 223 ? 15.477  -10.374 52.067 1.00 25.18 ? 223 GLU A N   1 
ATOM   1738 C CA  . GLU A 1 223 ? 15.362  -11.617 52.816 1.00 30.37 ? 223 GLU A CA  1 
ATOM   1739 C C   . GLU A 1 223 ? 14.402  -12.588 52.144 1.00 33.07 ? 223 GLU A C   1 
ATOM   1740 O O   . GLU A 1 223 ? 14.422  -13.785 52.461 1.00 32.35 ? 223 GLU A O   1 
ATOM   1741 C CB  . GLU A 1 223 ? 14.890  -11.327 54.246 1.00 35.25 ? 223 GLU A CB  1 
ATOM   1742 C CG  . GLU A 1 223 ? 16.009  -11.298 55.287 1.00 41.38 ? 223 GLU A CG  1 
ATOM   1743 C CD  . GLU A 1 223 ? 16.598  -9.919  55.465 1.00 50.36 ? 223 GLU A CD  1 
ATOM   1744 O OE1 . GLU A 1 223 ? 16.087  -8.973  54.824 1.00 52.44 ? 223 GLU A OE1 1 
ATOM   1745 O OE2 . GLU A 1 223 ? 17.569  -9.778  56.239 1.00 50.18 ? 223 GLU A OE2 1 
ATOM   1746 N N   . GLU A 1 224 ? 13.562  -12.098 51.227 1.00 23.63 ? 224 GLU A N   1 
ATOM   1747 C CA  . GLU A 1 224 ? 12.633  -12.939 50.479 1.00 26.38 ? 224 GLU A CA  1 
ATOM   1748 C C   . GLU A 1 224 ? 13.281  -13.587 49.267 1.00 23.64 ? 224 GLU A C   1 
ATOM   1749 O O   . GLU A 1 224 ? 12.612  -14.350 48.564 1.00 20.09 ? 224 GLU A O   1 
ATOM   1750 C CB  . GLU A 1 224 ? 11.413  -12.105 50.057 1.00 20.08 ? 224 GLU A CB  1 
ATOM   1751 C CG  . GLU A 1 224 ? 10.498  -11.825 51.232 1.00 24.70 ? 224 GLU A CG  1 
ATOM   1752 C CD  . GLU A 1 224 ? 9.368   -10.862 50.909 1.00 28.60 ? 224 GLU A CD  1 
ATOM   1753 O OE1 . GLU A 1 224 ? 9.473   -10.107 49.910 1.00 23.86 ? 224 GLU A OE1 1 
ATOM   1754 O OE2 . GLU A 1 224 ? 8.371   -10.864 51.665 1.00 28.15 ? 224 GLU A OE2 1 
ATOM   1755 N N   . LEU A 1 225 ? 14.569  -13.311 49.019 1.00 21.86 ? 225 LEU A N   1 
ATOM   1756 C CA  . LEU A 1 225 ? 15.259  -13.864 47.856 1.00 21.34 ? 225 LEU A CA  1 
ATOM   1757 C C   . LEU A 1 225 ? 15.192  -15.382 47.801 1.00 18.78 ? 225 LEU A C   1 
ATOM   1758 O O   . LEU A 1 225 ? 15.202  -15.967 46.712 1.00 21.15 ? 225 LEU A O   1 
ATOM   1759 C CB  . LEU A 1 225 ? 16.731  -13.441 47.871 1.00 26.60 ? 225 LEU A CB  1 
ATOM   1760 C CG  . LEU A 1 225 ? 16.996  -12.078 47.256 1.00 29.25 ? 225 LEU A CG  1 
ATOM   1761 C CD1 . LEU A 1 225 ? 18.491  -11.804 47.180 1.00 30.48 ? 225 LEU A CD1 1 
ATOM   1762 C CD2 . LEU A 1 225 ? 16.357  -12.067 45.898 1.00 27.67 ? 225 LEU A CD2 1 
ATOM   1763 N N   . THR A 1 226 ? 15.177  -16.041 48.953 1.00 19.13 ? 226 THR A N   1 
ATOM   1764 C CA  . THR A 1 226 ? 15.174  -17.498 48.990 1.00 19.24 ? 226 THR A CA  1 
ATOM   1765 C C   . THR A 1 226 ? 13.814  -18.058 49.381 1.00 21.14 ? 226 THR A C   1 
ATOM   1766 O O   . THR A 1 226 ? 13.691  -19.261 49.635 1.00 19.64 ? 226 THR A O   1 
ATOM   1767 C CB  . THR A 1 226 ? 16.249  -17.997 49.956 1.00 20.68 ? 226 THR A CB  1 
ATOM   1768 O OG1 . THR A 1 226 ? 15.993  -17.443 51.254 1.00 23.24 ? 226 THR A OG1 1 
ATOM   1769 C CG2 . THR A 1 226 ? 17.631  -17.572 49.478 1.00 21.79 ? 226 THR A CG2 1 
ATOM   1770 N N   . HIS A 1 227 ? 12.790  -17.221 49.442 1.00 19.50 ? 227 HIS A N   1 
ATOM   1771 C CA  . HIS A 1 227 ? 11.449  -17.726 49.680 1.00 16.90 ? 227 HIS A CA  1 
ATOM   1772 C C   . HIS A 1 227 ? 11.003  -18.548 48.474 1.00 15.91 ? 227 HIS A C   1 
ATOM   1773 O O   . HIS A 1 227 ? 11.090  -18.066 47.333 1.00 17.95 ? 227 HIS A O   1 
ATOM   1774 C CB  . HIS A 1 227 ? 10.500  -16.549 49.938 1.00 19.14 ? 227 HIS A CB  1 
ATOM   1775 C CG  . HIS A 1 227 ? 9.155   -16.940 50.466 1.00 20.52 ? 227 HIS A CG  1 
ATOM   1776 N ND1 . HIS A 1 227 ? 8.296   -17.773 49.782 1.00 19.75 ? 227 HIS A ND1 1 
ATOM   1777 C CD2 . HIS A 1 227 ? 8.498   -16.566 51.593 1.00 23.10 ? 227 HIS A CD2 1 
ATOM   1778 C CE1 . HIS A 1 227 ? 7.173   -17.906 50.470 1.00 26.46 ? 227 HIS A CE1 1 
ATOM   1779 N NE2 . HIS A 1 227 ? 7.269   -17.182 51.571 1.00 24.99 ? 227 HIS A NE2 1 
ATOM   1780 N N   . PRO A 1 228 ? 10.534  -19.784 48.671 1.00 17.11 ? 228 PRO A N   1 
ATOM   1781 C CA  . PRO A 1 228 ? 10.213  -20.638 47.512 1.00 17.12 ? 228 PRO A CA  1 
ATOM   1782 C C   . PRO A 1 228 ? 9.055   -20.130 46.654 1.00 18.78 ? 228 PRO A C   1 
ATOM   1783 O O   . PRO A 1 228 ? 8.968   -20.534 45.488 1.00 16.99 ? 228 PRO A O   1 
ATOM   1784 C CB  . PRO A 1 228 ? 9.882   -22.002 48.149 1.00 21.53 ? 228 PRO A CB  1 
ATOM   1785 C CG  . PRO A 1 228 ? 9.580   -21.699 49.597 1.00 27.62 ? 228 PRO A CG  1 
ATOM   1786 C CD  . PRO A 1 228 ? 10.434  -20.513 49.950 1.00 21.06 ? 228 PRO A CD  1 
ATOM   1787 N N   . TRP A 1 229 ? 8.171   -19.265 47.169 1.00 13.83 ? 229 TRP A N   1 
ATOM   1788 C CA  . TRP A 1 229 ? 7.168   -18.645 46.303 1.00 15.00 ? 229 TRP A CA  1 
ATOM   1789 C C   . TRP A 1 229 ? 7.770   -17.581 45.398 1.00 15.89 ? 229 TRP A C   1 
ATOM   1790 O O   . TRP A 1 229 ? 7.092   -17.108 44.479 1.00 14.22 ? 229 TRP A O   1 
ATOM   1791 C CB  . TRP A 1 229 ? 6.061   -17.995 47.127 1.00 18.30 ? 229 TRP A CB  1 
ATOM   1792 C CG  . TRP A 1 229 ? 5.193   -18.954 47.881 1.00 20.58 ? 229 TRP A CG  1 
ATOM   1793 C CD1 . TRP A 1 229 ? 5.419   -20.290 48.109 1.00 20.82 ? 229 TRP A CD1 1 
ATOM   1794 C CD2 . TRP A 1 229 ? 3.950   -18.640 48.518 1.00 23.12 ? 229 TRP A CD2 1 
ATOM   1795 N NE1 . TRP A 1 229 ? 4.375   -20.822 48.850 1.00 20.61 ? 229 TRP A NE1 1 
ATOM   1796 C CE2 . TRP A 1 229 ? 3.468   -19.826 49.110 1.00 22.28 ? 229 TRP A CE2 1 
ATOM   1797 C CE3 . TRP A 1 229 ? 3.191   -17.466 48.635 1.00 25.29 ? 229 TRP A CE3 1 
ATOM   1798 C CZ2 . TRP A 1 229 ? 2.254   -19.871 49.811 1.00 33.07 ? 229 TRP A CZ2 1 
ATOM   1799 C CZ3 . TRP A 1 229 ? 1.986   -17.517 49.330 1.00 28.82 ? 229 TRP A CZ3 1 
ATOM   1800 C CH2 . TRP A 1 229 ? 1.533   -18.711 49.906 1.00 32.11 ? 229 TRP A CH2 1 
ATOM   1801 N N   . PHE A 1 230 ? 8.994   -17.150 45.681 1.00 14.74 ? 230 PHE A N   1 
ATOM   1802 C CA  . PHE A 1 230 ? 9.738   -16.300 44.761 1.00 17.13 ? 230 PHE A CA  1 
ATOM   1803 C C   . PHE A 1 230 ? 10.751  -17.087 43.942 1.00 14.82 ? 230 PHE A C   1 
ATOM   1804 O O   . PHE A 1 230 ? 10.878  -16.850 42.735 1.00 16.98 ? 230 PHE A O   1 
ATOM   1805 C CB  . PHE A 1 230 ? 10.452  -15.174 45.518 1.00 15.95 ? 230 PHE A CB  1 
ATOM   1806 C CG  . PHE A 1 230 ? 11.338  -14.347 44.636 1.00 15.97 ? 230 PHE A CG  1 
ATOM   1807 C CD1 . PHE A 1 230 ? 10.794  -13.584 43.606 1.00 18.61 ? 230 PHE A CD1 1 
ATOM   1808 C CD2 . PHE A 1 230 ? 12.714  -14.386 44.792 1.00 21.53 ? 230 PHE A CD2 1 
ATOM   1809 C CE1 . PHE A 1 230 ? 11.624  -12.842 42.767 1.00 17.83 ? 230 PHE A CE1 1 
ATOM   1810 C CE2 . PHE A 1 230 ? 13.539  -13.657 43.961 1.00 21.52 ? 230 PHE A CE2 1 
ATOM   1811 C CZ  . PHE A 1 230 ? 12.998  -12.883 42.957 1.00 22.00 ? 230 PHE A CZ  1 
ATOM   1812 N N   . SER A 1 231 ? 11.481  -18.022 44.578 1.00 17.27 ? 231 SER A N   1 
ATOM   1813 C CA  . SER A 1 231 ? 12.480  -18.885 43.934 1.00 13.74 ? 231 SER A CA  1 
ATOM   1814 C C   . SER A 1 231 ? 12.031  -20.338 44.051 1.00 13.25 ? 231 SER A C   1 
ATOM   1815 O O   . SER A 1 231 ? 12.537  -21.079 44.910 1.00 15.38 ? 231 SER A O   1 
ATOM   1816 C CB  . SER A 1 231 ? 13.867  -18.749 44.576 1.00 17.88 ? 231 SER A CB  1 
ATOM   1817 O OG  . SER A 1 231 ? 14.363  -17.418 44.496 1.00 24.95 ? 231 SER A OG  1 
ATOM   1818 N N   . PRO A 1 232 ? 11.094  -20.785 43.209 1.00 15.21 ? 232 PRO A N   1 
ATOM   1819 C CA  . PRO A 1 232 ? 10.574  -22.157 43.346 1.00 16.71 ? 232 PRO A CA  1 
ATOM   1820 C C   . PRO A 1 232 ? 11.639  -23.239 43.218 1.00 16.54 ? 232 PRO A C   1 
ATOM   1821 O O   . PRO A 1 232 ? 11.417  -24.349 43.712 1.00 17.29 ? 232 PRO A O   1 
ATOM   1822 C CB  . PRO A 1 232 ? 9.527   -22.249 42.223 1.00 15.64 ? 232 PRO A CB  1 
ATOM   1823 C CG  . PRO A 1 232 ? 9.966   -21.165 41.215 1.00 16.19 ? 232 PRO A CG  1 
ATOM   1824 C CD  . PRO A 1 232 ? 10.439  -20.053 42.115 1.00 14.85 ? 232 PRO A CD  1 
ATOM   1825 N N   . VAL A 1 233 ? 12.790  -22.959 42.596 1.00 15.69 ? 233 VAL A N   1 
ATOM   1826 C CA  . VAL A 1 233 ? 13.850  -23.966 42.524 1.00 14.35 ? 233 VAL A CA  1 
ATOM   1827 C C   . VAL A 1 233 ? 14.337  -24.373 43.908 1.00 17.19 ? 233 VAL A C   1 
ATOM   1828 O O   . VAL A 1 233 ? 14.873  -25.474 44.076 1.00 17.14 ? 233 VAL A O   1 
ATOM   1829 C CB  . VAL A 1 233 ? 15.026  -23.451 41.651 1.00 16.00 ? 233 VAL A CB  1 
ATOM   1830 C CG1 . VAL A 1 233 ? 15.876  -22.469 42.418 1.00 12.88 ? 233 VAL A CG1 1 
ATOM   1831 C CG2 . VAL A 1 233 ? 15.874  -24.611 41.113 1.00 16.97 ? 233 VAL A CG2 1 
ATOM   1832 N N   . LEU A 1 234 ? 14.145  -23.522 44.917 1.00 14.93 ? 234 LEU A N   1 
ATOM   1833 C CA  . LEU A 1 234 ? 14.551  -23.810 46.283 1.00 16.11 ? 234 LEU A CA  1 
ATOM   1834 C C   . LEU A 1 234 ? 13.468  -24.504 47.104 1.00 21.42 ? 234 LEU A C   1 
ATOM   1835 O O   . LEU A 1 234 ? 13.686  -24.775 48.289 1.00 20.02 ? 234 LEU A O   1 
ATOM   1836 C CB  . LEU A 1 234 ? 14.969  -22.513 46.979 1.00 16.99 ? 234 LEU A CB  1 
ATOM   1837 C CG  . LEU A 1 234 ? 16.098  -21.771 46.244 1.00 18.15 ? 234 LEU A CG  1 
ATOM   1838 C CD1 . LEU A 1 234 ? 16.380  -20.436 46.946 1.00 18.72 ? 234 LEU A CD1 1 
ATOM   1839 C CD2 . LEU A 1 234 ? 17.349  -22.636 46.181 1.00 22.00 ? 234 LEU A CD2 1 
ATOM   1840 N N   . TYR A 1 235 ? 12.319  -24.783 46.522 1.00 19.91 ? 235 TYR A N   1 
ATOM   1841 C CA  . TYR A 1 235 ? 11.271  -25.477 47.256 1.00 20.00 ? 235 TYR A CA  1 
ATOM   1842 C C   . TYR A 1 235 ? 11.776  -26.865 47.646 1.00 21.70 ? 235 TYR A C   1 
ATOM   1843 O O   . TYR A 1 235 ? 12.339  -27.564 46.800 1.00 20.25 ? 235 TYR A O   1 
ATOM   1844 C CB  . TYR A 1 235 ? 10.018  -25.592 46.393 1.00 16.94 ? 235 TYR A CB  1 
ATOM   1845 C CG  . TYR A 1 235 ? 8.847   -26.165 47.130 1.00 20.36 ? 235 TYR A CG  1 
ATOM   1846 C CD1 . TYR A 1 235 ? 8.220   -25.438 48.138 1.00 22.42 ? 235 TYR A CD1 1 
ATOM   1847 C CD2 . TYR A 1 235 ? 8.349   -27.434 46.816 1.00 22.36 ? 235 TYR A CD2 1 
ATOM   1848 C CE1 . TYR A 1 235 ? 7.114   -25.959 48.821 1.00 21.29 ? 235 TYR A CE1 1 
ATOM   1849 C CE2 . TYR A 1 235 ? 7.234   -27.964 47.505 1.00 21.45 ? 235 TYR A CE2 1 
ATOM   1850 C CZ  . TYR A 1 235 ? 6.642   -27.218 48.510 1.00 27.56 ? 235 TYR A CZ  1 
ATOM   1851 O OH  . TYR A 1 235 ? 5.542   -27.701 49.197 1.00 24.74 ? 235 TYR A OH  1 
ATOM   1852 N N   . PRO A 1 236 ? 11.622  -27.285 48.909 1.00 24.95 ? 236 PRO A N   1 
ATOM   1853 C CA  . PRO A 1 236 ? 12.315  -28.504 49.362 1.00 27.73 ? 236 PRO A CA  1 
ATOM   1854 C C   . PRO A 1 236 ? 11.867  -29.781 48.667 1.00 28.51 ? 236 PRO A C   1 
ATOM   1855 O O   . PRO A 1 236 ? 12.681  -30.702 48.535 1.00 32.77 ? 236 PRO A O   1 
ATOM   1856 C CB  . PRO A 1 236 ? 11.995  -28.560 50.865 1.00 30.42 ? 236 PRO A CB  1 
ATOM   1857 C CG  . PRO A 1 236 ? 11.578  -27.180 51.236 1.00 34.74 ? 236 PRO A CG  1 
ATOM   1858 C CD  . PRO A 1 236 ? 10.931  -26.601 50.013 1.00 27.82 ? 236 PRO A CD  1 
ATOM   1859 N N   . ASP A 1 237 ? 10.611  -29.888 48.227 1.00 24.03 ? 237 ASP A N   1 
ATOM   1860 C CA  . ASP A 1 237 ? 10.140  -31.154 47.632 1.00 28.44 ? 237 ASP A CA  1 
ATOM   1861 C C   . ASP A 1 237 ? 9.337   -30.888 46.360 1.00 21.09 ? 237 ASP A C   1 
ATOM   1862 O O   . ASP A 1 237 ? 8.113   -30.722 46.398 1.00 23.09 ? 237 ASP A O   1 
ATOM   1863 C CB  . ASP A 1 237 ? 9.327   -31.974 48.628 1.00 34.05 ? 237 ASP A CB  1 
ATOM   1864 C CG  . ASP A 1 237 ? 8.887   -33.327 48.046 1.00 36.44 ? 237 ASP A CG  1 
ATOM   1865 O OD1 . ASP A 1 237 ? 9.458   -33.759 47.018 1.00 32.77 ? 237 ASP A OD1 1 
ATOM   1866 O OD2 . ASP A 1 237 ? 7.968   -33.949 48.615 1.00 42.87 ? 237 ASP A OD2 1 
ATOM   1867 N N   . LEU A 1 238 ? 10.025  -30.932 45.222 1.00 21.73 ? 238 LEU A N   1 
ATOM   1868 C CA  . LEU A 1 238 ? 9.403   -30.745 43.921 1.00 20.91 ? 238 LEU A CA  1 
ATOM   1869 C C   . LEU A 1 238 ? 8.801   -32.020 43.356 1.00 21.95 ? 238 LEU A C   1 
ATOM   1870 O O   . LEU A 1 238 ? 8.294   -31.994 42.226 1.00 22.12 ? 238 LEU A O   1 
ATOM   1871 C CB  . LEU A 1 238 ? 10.430  -30.198 42.925 1.00 20.40 ? 238 LEU A CB  1 
ATOM   1872 C CG  . LEU A 1 238 ? 11.062  -28.861 43.305 1.00 19.14 ? 238 LEU A CG  1 
ATOM   1873 C CD1 . LEU A 1 238 ? 12.275  -28.607 42.433 1.00 20.02 ? 238 LEU A CD1 1 
ATOM   1874 C CD2 . LEU A 1 238 ? 10.044  -27.741 43.125 1.00 16.42 ? 238 LEU A CD2 1 
ATOM   1875 N N   . SER A 1 239 ? 8.860   -33.133 44.085 1.00 22.27 ? 239 SER A N   1 
ATOM   1876 C CA  . SER A 1 239 ? 8.296   -34.370 43.560 1.00 22.57 ? 239 SER A CA  1 
ATOM   1877 C C   . SER A 1 239 ? 6.786   -34.229 43.391 1.00 20.64 ? 239 SER A C   1 
ATOM   1878 O O   . SER A 1 239 ? 6.119   -33.502 44.134 1.00 25.84 ? 239 SER A O   1 
ATOM   1879 C CB  . SER A 1 239 ? 8.632   -35.544 44.488 1.00 24.63 ? 239 SER A CB  1 
ATOM   1880 O OG  . SER A 1 239 ? 7.976   -35.392 45.728 1.00 32.02 ? 239 SER A OG  1 
ATOM   1881 N N   . GLY A 1 240 ? 6.250   -34.924 42.391 1.00 21.97 ? 240 GLY A N   1 
ATOM   1882 C CA  . GLY A 1 240 ? 4.823   -34.919 42.118 1.00 24.31 ? 240 GLY A CA  1 
ATOM   1883 C C   . GLY A 1 240 ? 4.319   -33.713 41.357 1.00 25.23 ? 240 GLY A C   1 
ATOM   1884 O O   . GLY A 1 240 ? 3.104   -33.572 41.192 1.00 24.23 ? 240 GLY A O   1 
ATOM   1885 N N   . LEU A 1 241 ? 5.204   -32.826 40.890 1.00 22.89 ? 241 LEU A N   1 
ATOM   1886 C CA  . LEU A 1 241 ? 4.731   -31.660 40.158 1.00 23.45 ? 241 LEU A CA  1 
ATOM   1887 C C   . LEU A 1 241 ? 4.353   -32.082 38.741 1.00 20.47 ? 241 LEU A C   1 
ATOM   1888 O O   . LEU A 1 241 ? 4.745   -33.151 38.280 1.00 19.47 ? 241 LEU A O   1 
ATOM   1889 C CB  . LEU A 1 241 ? 5.811   -30.570 40.149 1.00 17.34 ? 241 LEU A CB  1 
ATOM   1890 C CG  . LEU A 1 241 ? 5.988   -29.829 41.478 1.00 21.79 ? 241 LEU A CG  1 
ATOM   1891 C CD1 . LEU A 1 241 ? 7.190   -28.898 41.405 1.00 19.80 ? 241 LEU A CD1 1 
ATOM   1892 C CD2 . LEU A 1 241 ? 4.742   -29.046 41.815 1.00 19.98 ? 241 LEU A CD2 1 
ATOM   1893 N N   . PRO A 1 242 ? 3.572   -31.253 38.027 1.00 22.49 ? 242 PRO A N   1 
ATOM   1894 C CA  . PRO A 1 242 ? 3.193   -31.644 36.665 1.00 19.21 ? 242 PRO A CA  1 
ATOM   1895 C C   . PRO A 1 242 ? 4.428   -31.702 35.756 1.00 21.91 ? 242 PRO A C   1 
ATOM   1896 O O   . PRO A 1 242 ? 5.408   -30.995 35.997 1.00 22.40 ? 242 PRO A O   1 
ATOM   1897 C CB  . PRO A 1 242 ? 2.240   -30.507 36.239 1.00 21.57 ? 242 PRO A CB  1 
ATOM   1898 C CG  . PRO A 1 242 ? 1.780   -29.876 37.531 1.00 20.19 ? 242 PRO A CG  1 
ATOM   1899 C CD  . PRO A 1 242 ? 2.954   -29.988 38.446 1.00 20.90 ? 242 PRO A CD  1 
ATOM   1900 N N   . PRO A 1 243 ? 4.369   -32.544 34.726 1.00 21.38 ? 243 PRO A N   1 
ATOM   1901 C CA  . PRO A 1 243 ? 5.480   -32.554 33.754 1.00 23.09 ? 243 PRO A CA  1 
ATOM   1902 C C   . PRO A 1 243 ? 5.651   -31.186 33.111 1.00 19.14 ? 243 PRO A C   1 
ATOM   1903 O O   . PRO A 1 243 ? 4.698   -30.422 32.957 1.00 19.60 ? 243 PRO A O   1 
ATOM   1904 C CB  . PRO A 1 243 ? 5.046   -33.610 32.729 1.00 24.59 ? 243 PRO A CB  1 
ATOM   1905 C CG  . PRO A 1 243 ? 3.584   -33.822 32.955 1.00 30.09 ? 243 PRO A CG  1 
ATOM   1906 C CD  . PRO A 1 243 ? 3.340   -33.542 34.411 1.00 25.20 ? 243 PRO A CD  1 
ATOM   1907 N N   . ALA A 1 244 ? 6.890   -30.854 32.761 1.00 20.40 ? 244 ALA A N   1 
ATOM   1908 C CA  . ALA A 1 244 ? 7.195   -29.493 32.345 1.00 17.53 ? 244 ALA A CA  1 
ATOM   1909 C C   . ALA A 1 244 ? 7.921   -29.487 31.011 1.00 21.91 ? 244 ALA A C   1 
ATOM   1910 O O   . ALA A 1 244 ? 8.654   -30.426 30.675 1.00 21.27 ? 244 ALA A O   1 
ATOM   1911 C CB  . ALA A 1 244 ? 8.043   -28.755 33.394 1.00 18.00 ? 244 ALA A CB  1 
ATOM   1912 N N   . TYR A 1 245 ? 7.692   -28.419 30.251 1.00 18.45 ? 245 TYR A N   1 
ATOM   1913 C CA  . TYR A 1 245 ? 8.525   -28.042 29.118 1.00 19.46 ? 245 TYR A CA  1 
ATOM   1914 C C   . TYR A 1 245 ? 9.110   -26.668 29.409 1.00 19.26 ? 245 TYR A C   1 
ATOM   1915 O O   . TYR A 1 245 ? 8.372   -25.726 29.702 1.00 16.36 ? 245 TYR A O   1 
ATOM   1916 C CB  . TYR A 1 245 ? 7.740   -28.014 27.801 1.00 19.01 ? 245 TYR A CB  1 
ATOM   1917 C CG  . TYR A 1 245 ? 8.556   -27.440 26.643 1.00 21.48 ? 245 TYR A CG  1 
ATOM   1918 C CD1 . TYR A 1 245 ? 9.423   -28.244 25.911 1.00 23.83 ? 245 TYR A CD1 1 
ATOM   1919 C CD2 . TYR A 1 245 ? 8.477   -26.086 26.314 1.00 20.47 ? 245 TYR A CD2 1 
ATOM   1920 C CE1 . TYR A 1 245 ? 10.187  -27.719 24.875 1.00 25.88 ? 245 TYR A CE1 1 
ATOM   1921 C CE2 . TYR A 1 245 ? 9.225   -25.557 25.283 1.00 21.93 ? 245 TYR A CE2 1 
ATOM   1922 C CZ  . TYR A 1 245 ? 10.072  -26.377 24.562 1.00 25.92 ? 245 TYR A CZ  1 
ATOM   1923 O OH  . TYR A 1 245 ? 10.819  -25.839 23.537 1.00 23.77 ? 245 TYR A OH  1 
ATOM   1924 N N   . ILE A 1 246 ? 10.428  -26.550 29.336 1.00 15.43 ? 246 ILE A N   1 
ATOM   1925 C CA  . ILE A 1 246 ? 11.112  -25.295 29.614 1.00 15.88 ? 246 ILE A CA  1 
ATOM   1926 C C   . ILE A 1 246 ? 11.836  -24.835 28.356 1.00 21.34 ? 246 ILE A C   1 
ATOM   1927 O O   . ILE A 1 246 ? 12.670  -25.571 27.811 1.00 18.25 ? 246 ILE A O   1 
ATOM   1928 C CB  . ILE A 1 246 ? 12.108  -25.441 30.778 1.00 16.95 ? 246 ILE A CB  1 
ATOM   1929 C CG1 . ILE A 1 246 ? 11.363  -25.812 32.072 1.00 17.00 ? 246 ILE A CG1 1 
ATOM   1930 C CG2 . ILE A 1 246 ? 12.947  -24.137 30.940 1.00 16.64 ? 246 ILE A CG2 1 
ATOM   1931 C CD1 . ILE A 1 246 ? 12.318  -26.376 33.178 1.00 19.13 ? 246 ILE A CD1 1 
ATOM   1932 N N   . ALA A 1 247 ? 11.563  -23.605 27.923 1.00 16.40 ? 247 ALA A N   1 
ATOM   1933 C CA  . ALA A 1 247 ? 12.326  -22.999 26.830 1.00 19.03 ? 247 ALA A CA  1 
ATOM   1934 C C   . ALA A 1 247 ? 13.290  -21.964 27.392 1.00 18.61 ? 247 ALA A C   1 
ATOM   1935 O O   . ALA A 1 247 ? 12.880  -21.081 28.149 1.00 17.72 ? 247 ALA A O   1 
ATOM   1936 C CB  . ALA A 1 247 ? 11.399  -22.345 25.800 1.00 18.72 ? 247 ALA A CB  1 
ATOM   1937 N N   . THR A 1 248 ? 14.570  -22.064 27.027 1.00 18.69 ? 248 THR A N   1 
ATOM   1938 C CA  . THR A 1 248 ? 15.531  -21.025 27.373 1.00 17.50 ? 248 THR A CA  1 
ATOM   1939 C C   . THR A 1 248 ? 16.080  -20.399 26.095 1.00 21.65 ? 248 THR A C   1 
ATOM   1940 O O   . THR A 1 248 ? 16.014  -20.991 25.013 1.00 22.35 ? 248 THR A O   1 
ATOM   1941 C CB  . THR A 1 248 ? 16.691  -21.564 28.233 1.00 20.39 ? 248 THR A CB  1 
ATOM   1942 O OG1 . THR A 1 248 ? 17.486  -22.487 27.475 1.00 21.39 ? 248 THR A OG1 1 
ATOM   1943 C CG2 . THR A 1 248 ? 16.157  -22.276 29.471 1.00 18.81 ? 248 THR A CG2 1 
ATOM   1944 N N   . ALA A 1 249 ? 16.625  -19.191 26.231 1.00 19.42 ? 249 ALA A N   1 
ATOM   1945 C CA  . ALA A 1 249 ? 17.289  -18.493 25.134 1.00 19.95 ? 249 ALA A CA  1 
ATOM   1946 C C   . ALA A 1 249 ? 18.789  -18.379 25.413 1.00 21.39 ? 249 ALA A C   1 
ATOM   1947 O O   . ALA A 1 249 ? 19.199  -18.097 26.541 1.00 18.31 ? 249 ALA A O   1 
ATOM   1948 C CB  . ALA A 1 249 ? 16.676  -17.106 24.936 1.00 19.59 ? 249 ALA A CB  1 
ATOM   1949 N N   . GLN A 1 250 ? 19.608  -18.585 24.373 1.00 21.20 ? 250 GLN A N   1 
ATOM   1950 C CA  . GLN A 1 250 ? 21.061  -18.653 24.565 1.00 19.98 ? 250 GLN A CA  1 
ATOM   1951 C C   . GLN A 1 250 ? 21.619  -17.385 25.200 1.00 21.51 ? 250 GLN A C   1 
ATOM   1952 O O   . GLN A 1 250 ? 22.535  -17.447 26.034 1.00 21.00 ? 250 GLN A O   1 
ATOM   1953 C CB  . GLN A 1 250 ? 21.760  -18.916 23.227 1.00 25.09 ? 250 GLN A CB  1 
ATOM   1954 C CG  . GLN A 1 250 ? 23.312  -18.801 23.268 1.00 24.83 ? 250 GLN A CG  1 
ATOM   1955 C CD  . GLN A 1 250 ? 23.983  -19.890 24.103 1.00 24.37 ? 250 GLN A CD  1 
ATOM   1956 O OE1 . GLN A 1 250 ? 23.345  -20.858 24.514 1.00 23.84 ? 250 GLN A OE1 1 
ATOM   1957 N NE2 . GLN A 1 250 ? 25.297  -19.749 24.326 1.00 29.29 ? 250 GLN A NE2 1 
ATOM   1958 N N   . TYR A 1 251 ? 21.110  -16.217 24.809 1.00 19.13 ? 251 TYR A N   1 
ATOM   1959 C CA  . TYR A 1 251 ? 21.701  -14.962 25.252 1.00 22.90 ? 251 TYR A CA  1 
ATOM   1960 C C   . TYR A 1 251 ? 20.913  -14.318 26.392 1.00 23.16 ? 251 TYR A C   1 
ATOM   1961 O O   . TYR A 1 251 ? 20.962  -13.103 26.584 1.00 26.49 ? 251 TYR A O   1 
ATOM   1962 C CB  . TYR A 1 251 ? 21.850  -14.016 24.062 1.00 24.39 ? 251 TYR A CB  1 
ATOM   1963 C CG  . TYR A 1 251 ? 22.806  -14.584 23.049 1.00 24.90 ? 251 TYR A CG  1 
ATOM   1964 C CD1 . TYR A 1 251 ? 24.184  -14.427 23.206 1.00 28.18 ? 251 TYR A CD1 1 
ATOM   1965 C CD2 . TYR A 1 251 ? 22.348  -15.323 21.964 1.00 24.84 ? 251 TYR A CD2 1 
ATOM   1966 C CE1 . TYR A 1 251 ? 25.068  -14.962 22.298 1.00 32.18 ? 251 TYR A CE1 1 
ATOM   1967 C CE2 . TYR A 1 251 ? 23.234  -15.875 21.050 1.00 30.90 ? 251 TYR A CE2 1 
ATOM   1968 C CZ  . TYR A 1 251 ? 24.594  -15.678 21.222 1.00 31.62 ? 251 TYR A CZ  1 
ATOM   1969 O OH  . TYR A 1 251 ? 25.487  -16.212 20.325 1.00 36.72 ? 251 TYR A OH  1 
ATOM   1970 N N   . ASP A 1 252 ? 20.242  -15.098 27.158 1.00 23.80 ? 252 ASP A N   1 
ATOM   1971 C CA  . ASP A 1 252 ? 19.391  -14.663 28.271 1.00 19.24 ? 252 ASP A CA  1 
ATOM   1972 C C   . ASP A 1 252 ? 20.168  -14.824 29.573 1.00 19.14 ? 252 ASP A C   1 
ATOM   1973 O O   . ASP A 1 252 ? 20.755  -15.898 29.791 1.00 18.35 ? 252 ASP A O   1 
ATOM   1974 C CB  . ASP A 1 252 ? 18.135  -15.530 28.269 1.00 16.86 ? 252 ASP A CB  1 
ATOM   1975 C CG  . ASP A 1 252 ? 17.072  -15.105 29.277 1.00 19.05 ? 252 ASP A CG  1 
ATOM   1976 O OD1 . ASP A 1 252 ? 17.272  -14.201 30.129 1.00 17.96 ? 252 ASP A OD1 1 
ATOM   1977 O OD2 . ASP A 1 252 ? 15.992  -15.725 29.199 1.00 20.77 ? 252 ASP A OD2 1 
ATOM   1978 N N   . PRO A 1 253 ? 20.268  -13.795 30.428 1.00 18.85 ? 253 PRO A N   1 
ATOM   1979 C CA  . PRO A 1 253 ? 20.843  -14.018 31.769 1.00 16.20 ? 253 PRO A CA  1 
ATOM   1980 C C   . PRO A 1 253 ? 20.130  -15.119 32.540 1.00 18.59 ? 253 PRO A C   1 
ATOM   1981 O O   . PRO A 1 253 ? 20.747  -15.774 33.392 1.00 17.23 ? 253 PRO A O   1 
ATOM   1982 C CB  . PRO A 1 253 ? 20.685  -12.652 32.456 1.00 17.47 ? 253 PRO A CB  1 
ATOM   1983 C CG  . PRO A 1 253 ? 19.671  -11.918 31.647 1.00 19.98 ? 253 PRO A CG  1 
ATOM   1984 C CD  . PRO A 1 253 ? 19.840  -12.398 30.238 1.00 17.33 ? 253 PRO A CD  1 
ATOM   1985 N N   . LEU A 1 254 ? 18.856  -15.364 32.238 1.00 15.76 ? 254 LEU A N   1 
ATOM   1986 C CA  . LEU A 1 254 ? 18.080  -16.430 32.862 1.00 15.96 ? 254 LEU A CA  1 
ATOM   1987 C C   . LEU A 1 254 ? 18.264  -17.796 32.209 1.00 15.31 ? 254 LEU A C   1 
ATOM   1988 O O   . LEU A 1 254 ? 17.604  -18.752 32.634 1.00 15.43 ? 254 LEU A O   1 
ATOM   1989 C CB  . LEU A 1 254 ? 16.585  -16.062 32.835 1.00 15.77 ? 254 LEU A CB  1 
ATOM   1990 C CG  . LEU A 1 254 ? 16.179  -14.890 33.723 1.00 19.24 ? 254 LEU A CG  1 
ATOM   1991 C CD1 . LEU A 1 254 ? 14.709  -14.536 33.463 1.00 22.45 ? 254 LEU A CD1 1 
ATOM   1992 C CD2 . LEU A 1 254 ? 16.406  -15.241 35.196 1.00 19.65 ? 254 LEU A CD2 1 
ATOM   1993 N N   . ARG A 1 255 ? 19.122  -17.929 31.190 1.00 16.07 ? 255 ARG A N   1 
ATOM   1994 C CA  . ARG A 1 255 ? 19.271  -19.210 30.493 1.00 18.78 ? 255 ARG A CA  1 
ATOM   1995 C C   . ARG A 1 255 ? 19.590  -20.358 31.448 1.00 19.04 ? 255 ARG A C   1 
ATOM   1996 O O   . ARG A 1 255 ? 18.910  -21.393 31.455 1.00 16.80 ? 255 ARG A O   1 
ATOM   1997 C CB  . ARG A 1 255 ? 20.377  -19.109 29.431 1.00 19.18 ? 255 ARG A CB  1 
ATOM   1998 C CG  . ARG A 1 255 ? 20.684  -20.433 28.726 1.00 17.80 ? 255 ARG A CG  1 
ATOM   1999 C CD  . ARG A 1 255 ? 22.042  -20.339 27.995 1.00 21.11 ? 255 ARG A CD  1 
ATOM   2000 N NE  . ARG A 1 255 ? 23.171  -20.323 28.936 1.00 22.64 ? 255 ARG A NE  1 
ATOM   2001 C CZ  . ARG A 1 255 ? 24.328  -19.694 28.732 1.00 25.14 ? 255 ARG A CZ  1 
ATOM   2002 N NH1 . ARG A 1 255 ? 24.533  -19.010 27.606 1.00 21.75 ? 255 ARG A NH1 1 
ATOM   2003 N NH2 . ARG A 1 255 ? 25.287  -19.753 29.658 1.00 22.60 ? 255 ARG A NH2 1 
ATOM   2004 N N   . ASP A 1 256 ? 20.643  -20.210 32.246 1.00 14.86 ? 256 ASP A N   1 
ATOM   2005 C CA  . ASP A 1 256 ? 21.015  -21.301 33.142 1.00 16.46 ? 256 ASP A CA  1 
ATOM   2006 C C   . ASP A 1 256 ? 20.140  -21.367 34.396 1.00 17.75 ? 256 ASP A C   1 
ATOM   2007 O O   . ASP A 1 256 ? 20.231  -22.344 35.149 1.00 14.77 ? 256 ASP A O   1 
ATOM   2008 C CB  . ASP A 1 256 ? 22.488  -21.173 33.522 1.00 19.48 ? 256 ASP A CB  1 
ATOM   2009 C CG  . ASP A 1 256 ? 23.404  -21.189 32.298 1.00 18.75 ? 256 ASP A CG  1 
ATOM   2010 O OD1 . ASP A 1 256 ? 23.067  -21.877 31.302 1.00 21.32 ? 256 ASP A OD1 1 
ATOM   2011 O OD2 . ASP A 1 256 ? 24.449  -20.509 32.325 1.00 19.57 ? 256 ASP A OD2 1 
ATOM   2012 N N   . VAL A 1 257 ? 19.310  -20.351 34.640 1.00 14.10 ? 257 VAL A N   1 
ATOM   2013 C CA  . VAL A 1 257 ? 18.279  -20.451 35.675 1.00 14.46 ? 257 VAL A CA  1 
ATOM   2014 C C   . VAL A 1 257 ? 17.199  -21.438 35.243 1.00 16.60 ? 257 VAL A C   1 
ATOM   2015 O O   . VAL A 1 257 ? 16.763  -22.292 36.028 1.00 15.45 ? 257 VAL A O   1 
ATOM   2016 C CB  . VAL A 1 257 ? 17.696  -19.050 35.967 1.00 15.11 ? 257 VAL A CB  1 
ATOM   2017 C CG1 . VAL A 1 257 ? 16.449  -19.144 36.861 1.00 17.69 ? 257 VAL A CG1 1 
ATOM   2018 C CG2 . VAL A 1 257 ? 18.763  -18.154 36.600 1.00 16.80 ? 257 VAL A CG2 1 
ATOM   2019 N N   . GLY A 1 258 ? 16.758  -21.353 33.987 1.00 17.49 ? 258 GLY A N   1 
ATOM   2020 C CA  . GLY A 1 258 ? 15.821  -22.351 33.486 1.00 19.46 ? 258 GLY A CA  1 
ATOM   2021 C C   . GLY A 1 258 ? 16.411  -23.749 33.486 1.00 18.03 ? 258 GLY A C   1 
ATOM   2022 O O   . GLY A 1 258 ? 15.736  -24.725 33.836 1.00 15.08 ? 258 GLY A O   1 
ATOM   2023 N N   . LYS A 1 259 ? 17.681  -23.866 33.087 1.00 17.14 ? 259 LYS A N   1 
ATOM   2024 C CA  . LYS A 1 259 ? 18.361  -25.158 33.131 1.00 17.59 ? 259 LYS A CA  1 
ATOM   2025 C C   . LYS A 1 259 ? 18.426  -25.703 34.554 1.00 18.80 ? 259 LYS A C   1 
ATOM   2026 O O   . LYS A 1 259 ? 18.271  -26.910 34.771 1.00 17.85 ? 259 LYS A O   1 
ATOM   2027 C CB  . LYS A 1 259 ? 19.768  -25.005 32.539 1.00 21.32 ? 259 LYS A CB  1 
ATOM   2028 C CG  . LYS A 1 259 ? 20.541  -26.277 32.327 1.00 25.80 ? 259 LYS A CG  1 
ATOM   2029 C CD  . LYS A 1 259 ? 21.900  -25.926 31.677 1.00 32.54 ? 259 LYS A CD  1 
ATOM   2030 C CE  . LYS A 1 259 ? 22.607  -27.163 31.143 1.00 33.11 ? 259 LYS A CE  1 
ATOM   2031 N NZ  . LYS A 1 259 ? 23.842  -26.817 30.392 1.00 40.54 ? 259 LYS A NZ  1 
ATOM   2032 N N   . LEU A 1 260 ? 18.644  -24.826 35.539 1.00 15.48 ? 260 LEU A N   1 
ATOM   2033 C CA  . LEU A 1 260 ? 18.676  -25.252 36.936 1.00 17.48 ? 260 LEU A CA  1 
ATOM   2034 C C   . LEU A 1 260 ? 17.328  -25.796 37.387 1.00 18.36 ? 260 LEU A C   1 
ATOM   2035 O O   . LEU A 1 260 ? 17.269  -26.751 38.172 1.00 14.68 ? 260 LEU A O   1 
ATOM   2036 C CB  . LEU A 1 260 ? 19.085  -24.082 37.838 1.00 18.91 ? 260 LEU A CB  1 
ATOM   2037 C CG  . LEU A 1 260 ? 19.303  -24.382 39.325 1.00 18.78 ? 260 LEU A CG  1 
ATOM   2038 C CD1 . LEU A 1 260 ? 20.645  -25.136 39.534 1.00 25.77 ? 260 LEU A CD1 1 
ATOM   2039 C CD2 . LEU A 1 260 ? 19.314  -23.058 40.096 1.00 21.29 ? 260 LEU A CD2 1 
ATOM   2040 N N   . TYR A 1 261 ? 16.229  -25.179 36.939 1.00 16.12 ? 261 TYR A N   1 
ATOM   2041 C CA  . TYR A 1 261 ? 14.917  -25.696 37.313 1.00 16.37 ? 261 TYR A CA  1 
ATOM   2042 C C   . TYR A 1 261 ? 14.666  -27.063 36.680 1.00 17.78 ? 261 TYR A C   1 
ATOM   2043 O O   . TYR A 1 261 ? 14.101  -27.961 37.323 1.00 16.73 ? 261 TYR A O   1 
ATOM   2044 C CB  . TYR A 1 261 ? 13.818  -24.705 36.918 1.00 16.36 ? 261 TYR A CB  1 
ATOM   2045 C CG  . TYR A 1 261 ? 12.552  -24.903 37.741 1.00 16.49 ? 261 TYR A CG  1 
ATOM   2046 C CD1 . TYR A 1 261 ? 12.593  -24.810 39.125 1.00 14.44 ? 261 TYR A CD1 1 
ATOM   2047 C CD2 . TYR A 1 261 ? 11.333  -25.197 37.136 1.00 16.95 ? 261 TYR A CD2 1 
ATOM   2048 C CE1 . TYR A 1 261 ? 11.453  -24.996 39.905 1.00 18.27 ? 261 TYR A CE1 1 
ATOM   2049 C CE2 . TYR A 1 261 ? 10.164  -25.389 37.912 1.00 16.64 ? 261 TYR A CE2 1 
ATOM   2050 C CZ  . TYR A 1 261 ? 10.242  -25.296 39.291 1.00 16.19 ? 261 TYR A CZ  1 
ATOM   2051 O OH  . TYR A 1 261 ? 9.123   -25.478 40.078 1.00 16.14 ? 261 TYR A OH  1 
ATOM   2052 N N   . ALA A 1 262 ? 15.081  -27.243 35.424 1.00 17.30 ? 262 ALA A N   1 
ATOM   2053 C CA  . ALA A 1 262 ? 14.941  -28.547 34.784 1.00 18.30 ? 262 ALA A CA  1 
ATOM   2054 C C   . ALA A 1 262 ? 15.729  -29.607 35.548 1.00 18.53 ? 262 ALA A C   1 
ATOM   2055 O O   . ALA A 1 262 ? 15.223  -30.705 35.813 1.00 21.23 ? 262 ALA A O   1 
ATOM   2056 C CB  . ALA A 1 262 ? 15.404  -28.470 33.323 1.00 18.84 ? 262 ALA A CB  1 
ATOM   2057 N N   . GLU A 1 263 ? 16.967  -29.284 35.933 1.00 18.45 ? 263 GLU A N   1 
ATOM   2058 C CA  . GLU A 1 263 ? 17.764  -30.198 36.750 1.00 19.03 ? 263 GLU A CA  1 
ATOM   2059 C C   . GLU A 1 263 ? 17.043  -30.552 38.041 1.00 21.16 ? 263 GLU A C   1 
ATOM   2060 O O   . GLU A 1 263 ? 16.988  -31.722 38.435 1.00 20.94 ? 263 GLU A O   1 
ATOM   2061 C CB  . GLU A 1 263 ? 19.120  -29.583 37.099 1.00 19.86 ? 263 GLU A CB  1 
ATOM   2062 C CG  . GLU A 1 263 ? 19.992  -29.130 35.962 1.00 31.99 ? 263 GLU A CG  1 
ATOM   2063 C CD  . GLU A 1 263 ? 21.157  -28.262 36.477 1.00 38.00 ? 263 GLU A CD  1 
ATOM   2064 O OE1 . GLU A 1 263 ? 21.658  -28.541 37.597 1.00 41.70 ? 263 GLU A OE1 1 
ATOM   2065 O OE2 . GLU A 1 263 ? 21.542  -27.280 35.797 1.00 38.26 ? 263 GLU A OE2 1 
ATOM   2066 N N   . ALA A 1 264 ? 16.511  -29.544 38.736 1.00 18.79 ? 264 ALA A N   1 
ATOM   2067 C CA  . ALA A 1 264 ? 15.862  -29.793 40.020 1.00 20.16 ? 264 ALA A CA  1 
ATOM   2068 C C   . ALA A 1 264 ? 14.595  -30.625 39.856 1.00 19.74 ? 264 ALA A C   1 
ATOM   2069 O O   . ALA A 1 264 ? 14.307  -31.505 40.688 1.00 20.41 ? 264 ALA A O   1 
ATOM   2070 C CB  . ALA A 1 264 ? 15.551  -28.462 40.716 1.00 22.08 ? 264 ALA A CB  1 
ATOM   2071 N N   . LEU A 1 265 ? 13.821  -30.365 38.797 1.00 18.12 ? 265 LEU A N   1 
ATOM   2072 C CA  . LEU A 1 265 ? 12.617  -31.159 38.551 1.00 19.66 ? 265 LEU A CA  1 
ATOM   2073 C C   . LEU A 1 265 ? 12.991  -32.592 38.220 1.00 26.07 ? 265 LEU A C   1 
ATOM   2074 O O   . LEU A 1 265 ? 12.418  -33.552 38.764 1.00 23.70 ? 265 LEU A O   1 
ATOM   2075 C CB  . LEU A 1 265 ? 11.806  -30.554 37.408 1.00 18.23 ? 265 LEU A CB  1 
ATOM   2076 C CG  . LEU A 1 265 ? 10.994  -29.289 37.724 1.00 18.55 ? 265 LEU A CG  1 
ATOM   2077 C CD1 . LEU A 1 265 ? 10.284  -28.780 36.473 1.00 17.25 ? 265 LEU A CD1 1 
ATOM   2078 C CD2 . LEU A 1 265 ? 9.998   -29.540 38.827 1.00 18.60 ? 265 LEU A CD2 1 
ATOM   2079 N N   . ASN A 1 266 ? 13.959  -32.744 37.319 1.00 20.77 ? 266 ASN A N   1 
ATOM   2080 C CA  . ASN A 1 266 ? 14.431  -34.067 36.956 1.00 22.61 ? 266 ASN A CA  1 
ATOM   2081 C C   . ASN A 1 266 ? 14.908  -34.827 38.188 1.00 26.00 ? 266 ASN A C   1 
ATOM   2082 O O   . ASN A 1 266 ? 14.553  -35.994 38.362 1.00 25.15 ? 266 ASN A O   1 
ATOM   2083 C CB  . ASN A 1 266 ? 15.526  -33.951 35.894 1.00 26.06 ? 266 ASN A CB  1 
ATOM   2084 C CG  . ASN A 1 266 ? 15.874  -35.281 35.283 1.00 33.90 ? 266 ASN A CG  1 
ATOM   2085 O OD1 . ASN A 1 266 ? 15.012  -35.974 34.739 1.00 34.79 ? 266 ASN A OD1 1 
ATOM   2086 N ND2 . ASN A 1 266 ? 17.130  -35.670 35.412 1.00 37.91 ? 266 ASN A ND2 1 
ATOM   2087 N N   . LYS A 1 267 ? 15.648  -34.172 39.100 1.00 25.25 ? 267 LYS A N   1 
ATOM   2088 C CA  . LYS A 1 267 ? 16.158  -34.894 40.271 1.00 25.93 ? 267 LYS A CA  1 
ATOM   2089 C C   . LYS A 1 267 ? 15.059  -35.224 41.261 1.00 28.83 ? 267 LYS A C   1 
ATOM   2090 O O   . LYS A 1 267 ? 15.233  -36.125 42.087 1.00 23.87 ? 267 LYS A O   1 
ATOM   2091 C CB  . LYS A 1 267 ? 17.290  -34.094 40.947 1.00 30.42 ? 267 LYS A CB  1 
ATOM   2092 C CG  . LYS A 1 267 ? 18.203  -34.798 41.911 1.00 44.34 ? 267 LYS A CG  1 
ATOM   2093 C CD  . LYS A 1 267 ? 19.032  -33.808 42.804 1.00 44.74 ? 267 LYS A CD  1 
ATOM   2094 C CE  . LYS A 1 267 ? 20.255  -34.457 43.481 1.00 55.78 ? 267 LYS A CE  1 
ATOM   2095 N NZ  . LYS A 1 267 ? 21.033  -35.281 42.571 1.00 62.36 ? 267 LYS A NZ  1 
ATOM   2096 N N   . ALA A 1 268 ? 13.912  -34.555 41.178 1.00 25.11 ? 268 ALA A N   1 
ATOM   2097 C CA  . ALA A 1 268 ? 12.778  -34.900 42.026 1.00 24.95 ? 268 ALA A CA  1 
ATOM   2098 C C   . ALA A 1 268 ? 11.816  -35.891 41.366 1.00 21.66 ? 268 ALA A C   1 
ATOM   2099 O O   . ALA A 1 268 ? 10.728  -36.128 41.897 1.00 23.02 ? 268 ALA A O   1 
ATOM   2100 C CB  . ALA A 1 268 ? 12.001  -33.636 42.448 1.00 21.94 ? 268 ALA A CB  1 
ATOM   2101 N N   . GLY A 1 269 ? 12.184  -36.463 40.226 1.00 24.25 ? 269 GLY A N   1 
ATOM   2102 C CA  . GLY A 1 269 ? 11.338  -37.443 39.570 1.00 24.65 ? 269 GLY A CA  1 
ATOM   2103 C C   . GLY A 1 269 ? 10.211  -36.876 38.732 1.00 27.89 ? 269 GLY A C   1 
ATOM   2104 O O   . GLY A 1 269 ? 9.227   -37.581 38.479 1.00 21.16 ? 269 GLY A O   1 
ATOM   2105 N N   . VAL A 1 270 ? 10.310  -35.619 38.290 1.00 23.37 ? 270 VAL A N   1 
ATOM   2106 C CA  . VAL A 1 270 ? 9.284   -35.008 37.443 1.00 23.49 ? 270 VAL A CA  1 
ATOM   2107 C C   . VAL A 1 270 ? 9.765   -35.060 36.005 1.00 23.14 ? 270 VAL A C   1 
ATOM   2108 O O   . VAL A 1 270 ? 10.919  -34.721 35.727 1.00 22.95 ? 270 VAL A O   1 
ATOM   2109 C CB  . VAL A 1 270 ? 9.001   -33.554 37.869 1.00 21.13 ? 270 VAL A CB  1 
ATOM   2110 C CG1 . VAL A 1 270 ? 7.970   -32.923 36.939 1.00 21.49 ? 270 VAL A CG1 1 
ATOM   2111 C CG2 . VAL A 1 270 ? 8.549   -33.509 39.322 1.00 20.64 ? 270 VAL A CG2 1 
ATOM   2112 N N   . LYS A 1 271 ? 8.893   -35.466 35.079 1.00 20.98 ? 271 LYS A N   1 
ATOM   2113 C CA  . LYS A 1 271 ? 9.280   -35.425 33.672 1.00 25.20 ? 271 LYS A CA  1 
ATOM   2114 C C   . LYS A 1 271 ? 9.446   -33.985 33.204 1.00 26.22 ? 271 LYS A C   1 
ATOM   2115 O O   . LYS A 1 271 ? 8.541   -33.157 33.359 1.00 22.18 ? 271 LYS A O   1 
ATOM   2116 C CB  . LYS A 1 271 ? 8.260   -36.117 32.768 1.00 27.05 ? 271 LYS A CB  1 
ATOM   2117 C CG  . LYS A 1 271 ? 8.748   -36.066 31.306 1.00 36.25 ? 271 LYS A CG  1 
ATOM   2118 C CD  . LYS A 1 271 ? 8.008   -36.986 30.351 1.00 43.74 ? 271 LYS A CD  1 
ATOM   2119 C CE  . LYS A 1 271 ? 6.560   -36.569 30.155 1.00 47.98 ? 271 LYS A CE  1 
ATOM   2120 N NZ  . LYS A 1 271 ? 5.907   -37.257 28.996 1.00 45.51 ? 271 LYS A NZ  1 
ATOM   2121 N N   . VAL A 1 272 ? 10.579  -33.692 32.583 1.00 24.23 ? 272 VAL A N   1 
ATOM   2122 C CA  . VAL A 1 272 ? 10.843  -32.348 32.096 1.00 23.30 ? 272 VAL A CA  1 
ATOM   2123 C C   . VAL A 1 272 ? 11.621  -32.447 30.796 1.00 27.43 ? 272 VAL A C   1 
ATOM   2124 O O   . VAL A 1 272 ? 12.555  -33.247 30.671 1.00 28.76 ? 272 VAL A O   1 
ATOM   2125 C CB  . VAL A 1 272 ? 11.595  -31.494 33.149 1.00 25.38 ? 272 VAL A CB  1 
ATOM   2126 C CG1 . VAL A 1 272 ? 12.821  -32.236 33.691 1.00 26.64 ? 272 VAL A CG1 1 
ATOM   2127 C CG2 . VAL A 1 272 ? 11.997  -30.130 32.562 1.00 22.26 ? 272 VAL A CG2 1 
ATOM   2128 N N   . GLU A 1 273 ? 11.209  -31.656 29.817 1.00 21.48 ? 273 GLU A N   1 
ATOM   2129 C CA  . GLU A 1 273 ? 11.972  -31.429 28.602 1.00 23.92 ? 273 GLU A CA  1 
ATOM   2130 C C   . GLU A 1 273 ? 12.418  -29.973 28.599 1.00 24.15 ? 273 GLU A C   1 
ATOM   2131 O O   . GLU A 1 273 ? 11.644  -29.076 28.949 1.00 22.19 ? 273 GLU A O   1 
ATOM   2132 C CB  . GLU A 1 273 ? 11.128  -31.761 27.362 1.00 26.33 ? 273 GLU A CB  1 
ATOM   2133 C CG  . GLU A 1 273 ? 11.757  -31.349 26.023 1.00 31.95 ? 273 GLU A CG  1 
ATOM   2134 C CD  . GLU A 1 273 ? 10.861  -31.693 24.836 1.00 37.13 ? 273 GLU A CD  1 
ATOM   2135 O OE1 . GLU A 1 273 ? 9.694   -32.076 25.067 1.00 34.97 ? 273 GLU A OE1 1 
ATOM   2136 O OE2 . GLU A 1 273 ? 11.323  -31.585 23.679 1.00 37.17 ? 273 GLU A OE2 1 
ATOM   2137 N N   . ILE A 1 274 ? 13.684  -29.734 28.276 1.00 20.15 ? 274 ILE A N   1 
ATOM   2138 C CA  . ILE A 1 274 ? 14.190  -28.374 28.155 1.00 20.19 ? 274 ILE A CA  1 
ATOM   2139 C C   . ILE A 1 274 ? 14.851  -28.219 26.795 1.00 24.24 ? 274 ILE A C   1 
ATOM   2140 O O   . ILE A 1 274 ? 15.583  -29.108 26.345 1.00 22.63 ? 274 ILE A O   1 
ATOM   2141 C CB  . ILE A 1 274 ? 15.167  -28.012 29.297 1.00 17.88 ? 274 ILE A CB  1 
ATOM   2142 C CG1 . ILE A 1 274 ? 15.763  -26.620 29.060 1.00 22.85 ? 274 ILE A CG1 1 
ATOM   2143 C CG2 . ILE A 1 274 ? 16.226  -29.113 29.496 1.00 23.19 ? 274 ILE A CG2 1 
ATOM   2144 C CD1 . ILE A 1 274 ? 16.447  -26.021 30.273 1.00 21.83 ? 274 ILE A CD1 1 
ATOM   2145 N N   . GLU A 1 275 ? 14.589  -27.094 26.138 1.00 20.72 ? 275 GLU A N   1 
ATOM   2146 C CA  . GLU A 1 275 ? 15.194  -26.788 24.849 1.00 23.43 ? 275 GLU A CA  1 
ATOM   2147 C C   . GLU A 1 275 ? 15.754  -25.379 24.914 1.00 25.78 ? 275 GLU A C   1 
ATOM   2148 O O   . GLU A 1 275 ? 15.072  -24.453 25.366 1.00 21.67 ? 275 GLU A O   1 
ATOM   2149 C CB  . GLU A 1 275 ? 14.182  -26.932 23.696 1.00 26.78 ? 275 GLU A CB  1 
ATOM   2150 C CG  . GLU A 1 275 ? 13.710  -28.382 23.519 1.00 29.02 ? 275 GLU A CG  1 
ATOM   2151 C CD  . GLU A 1 275 ? 12.869  -28.616 22.264 1.00 38.67 ? 275 GLU A CD  1 
ATOM   2152 O OE1 . GLU A 1 275 ? 12.078  -27.719 21.872 1.00 29.88 ? 275 GLU A OE1 1 
ATOM   2153 O OE2 . GLU A 1 275 ? 12.993  -29.715 21.678 1.00 40.93 ? 275 GLU A OE2 1 
ATOM   2154 N N   . ASN A 1 276 ? 17.007  -25.229 24.497 1.00 20.28 ? 276 ASN A N   1 
ATOM   2155 C CA  . ASN A 1 276 ? 17.666  -23.934 24.440 1.00 18.84 ? 276 ASN A CA  1 
ATOM   2156 C C   . ASN A 1 276 ? 17.661  -23.435 22.998 1.00 26.58 ? 276 ASN A C   1 
ATOM   2157 O O   . ASN A 1 276 ? 18.085  -24.153 22.088 1.00 23.90 ? 276 ASN A O   1 
ATOM   2158 C CB  . ASN A 1 276 ? 19.100  -24.047 24.969 1.00 20.16 ? 276 ASN A CB  1 
ATOM   2159 C CG  . ASN A 1 276 ? 19.794  -22.718 25.028 1.00 24.73 ? 276 ASN A CG  1 
ATOM   2160 O OD1 . ASN A 1 276 ? 19.300  -21.775 25.659 1.00 21.68 ? 276 ASN A OD1 1 
ATOM   2161 N ND2 . ASN A 1 276 ? 20.950  -22.622 24.370 1.00 22.38 ? 276 ASN A ND2 1 
ATOM   2162 N N   . PHE A 1 277 ? 17.184  -22.211 22.787 1.00 24.13 ? 277 PHE A N   1 
ATOM   2163 C CA  . PHE A 1 277 ? 17.118  -21.635 21.445 1.00 26.34 ? 277 PHE A CA  1 
ATOM   2164 C C   . PHE A 1 277 ? 18.371  -20.794 21.216 1.00 26.69 ? 277 PHE A C   1 
ATOM   2165 O O   . PHE A 1 277 ? 18.532  -19.707 21.790 1.00 22.64 ? 277 PHE A O   1 
ATOM   2166 C CB  . PHE A 1 277 ? 15.807  -20.869 21.265 1.00 24.11 ? 277 PHE A CB  1 
ATOM   2167 C CG  . PHE A 1 277 ? 14.612  -21.787 21.232 1.00 24.02 ? 277 PHE A CG  1 
ATOM   2168 C CD1 . PHE A 1 277 ? 14.223  -22.405 20.043 1.00 24.50 ? 277 PHE A CD1 1 
ATOM   2169 C CD2 . PHE A 1 277 ? 13.924  -22.098 22.394 1.00 22.45 ? 277 PHE A CD2 1 
ATOM   2170 C CE1 . PHE A 1 277 ? 13.152  -23.277 20.005 1.00 27.28 ? 277 PHE A CE1 1 
ATOM   2171 C CE2 . PHE A 1 277 ? 12.847  -22.984 22.370 1.00 23.41 ? 277 PHE A CE2 1 
ATOM   2172 C CZ  . PHE A 1 277 ? 12.449  -23.566 21.179 1.00 27.39 ? 277 PHE A CZ  1 
ATOM   2173 N N   . GLU A 1 278 ? 19.269  -21.327 20.381 1.00 25.75 ? 278 GLU A N   1 
ATOM   2174 C CA  . GLU A 1 278 ? 20.659  -20.900 20.353 1.00 29.83 ? 278 GLU A CA  1 
ATOM   2175 C C   . GLU A 1 278 ? 20.842  -19.506 19.775 1.00 28.54 ? 278 GLU A C   1 
ATOM   2176 O O   . GLU A 1 278 ? 21.900  -18.897 19.983 1.00 28.96 ? 278 GLU A O   1 
ATOM   2177 C CB  . GLU A 1 278 ? 21.480  -21.911 19.548 1.00 27.60 ? 278 GLU A CB  1 
ATOM   2178 C CG  . GLU A 1 278 ? 21.426  -23.340 20.097 1.00 32.11 ? 278 GLU A CG  1 
ATOM   2179 C CD  . GLU A 1 278 ? 22.241  -23.512 21.380 1.00 39.16 ? 278 GLU A CD  1 
ATOM   2180 O OE1 . GLU A 1 278 ? 21.961  -24.461 22.157 1.00 40.75 ? 278 GLU A OE1 1 
ATOM   2181 O OE2 . GLU A 1 278 ? 23.164  -22.693 21.611 1.00 39.94 ? 278 GLU A OE2 1 
ATOM   2182 N N   . ASP A 1 279 ? 19.847  -18.980 19.064 1.00 28.91 ? 279 ASP A N   1 
ATOM   2183 C CA  . ASP A 1 279 ? 20.005  -17.707 18.376 1.00 31.72 ? 279 ASP A CA  1 
ATOM   2184 C C   . ASP A 1 279 ? 19.181  -16.583 18.992 1.00 31.54 ? 279 ASP A C   1 
ATOM   2185 O O   . ASP A 1 279 ? 19.088  -15.507 18.393 1.00 30.71 ? 279 ASP A O   1 
ATOM   2186 C CB  . ASP A 1 279 ? 19.660  -17.866 16.890 1.00 36.80 ? 279 ASP A CB  1 
ATOM   2187 C CG  . ASP A 1 279 ? 18.246  -18.409 16.650 1.00 41.77 ? 279 ASP A CG  1 
ATOM   2188 O OD1 . ASP A 1 279 ? 17.664  -19.102 17.528 1.00 37.73 ? 279 ASP A OD1 1 
ATOM   2189 O OD2 . ASP A 1 279 ? 17.717  -18.149 15.550 1.00 44.20 ? 279 ASP A OD2 1 
ATOM   2190 N N   . LEU A 1 280 ? 18.618  -16.776 20.184 1.00 25.90 ? 280 LEU A N   1 
ATOM   2191 C CA  . LEU A 1 280 ? 17.608  -15.851 20.687 1.00 22.91 ? 280 LEU A CA  1 
ATOM   2192 C C   . LEU A 1 280 ? 17.999  -15.267 22.040 1.00 23.67 ? 280 LEU A C   1 
ATOM   2193 O O   . LEU A 1 280 ? 18.939  -15.716 22.700 1.00 23.36 ? 280 LEU A O   1 
ATOM   2194 C CB  . LEU A 1 280 ? 16.241  -16.544 20.778 1.00 21.69 ? 280 LEU A CB  1 
ATOM   2195 C CG  . LEU A 1 280 ? 15.759  -17.068 19.421 1.00 28.91 ? 280 LEU A CG  1 
ATOM   2196 C CD1 . LEU A 1 280 ? 14.415  -17.762 19.533 1.00 23.46 ? 280 LEU A CD1 1 
ATOM   2197 C CD2 . LEU A 1 280 ? 15.675  -15.925 18.432 1.00 28.85 ? 280 LEU A CD2 1 
ATOM   2198 N N   . ILE A 1 281 ? 17.248  -14.235 22.426 1.00 21.41 ? 281 ILE A N   1 
ATOM   2199 C CA  . ILE A 1 281 ? 17.431  -13.493 23.663 1.00 20.70 ? 281 ILE A CA  1 
ATOM   2200 C C   . ILE A 1 281 ? 16.184  -13.693 24.531 1.00 20.81 ? 281 ILE A C   1 
ATOM   2201 O O   . ILE A 1 281 ? 15.180  -14.265 24.097 1.00 22.32 ? 281 ILE A O   1 
ATOM   2202 C CB  . ILE A 1 281 ? 17.651  -11.989 23.422 1.00 23.16 ? 281 ILE A CB  1 
ATOM   2203 C CG1 . ILE A 1 281 ? 16.454  -11.413 22.658 1.00 22.60 ? 281 ILE A CG1 1 
ATOM   2204 C CG2 . ILE A 1 281 ? 19.001  -11.705 22.711 1.00 21.40 ? 281 ILE A CG2 1 
ATOM   2205 C CD1 . ILE A 1 281 ? 16.340  -9.918  22.791 1.00 25.77 ? 281 ILE A CD1 1 
ATOM   2206 N N   . HIS A 1 282 ? 16.254  -13.170 25.756 1.00 20.40 ? 282 HIS A N   1 
ATOM   2207 C CA  . HIS A 1 282 ? 15.078  -13.100 26.619 1.00 20.81 ? 282 HIS A CA  1 
ATOM   2208 C C   . HIS A 1 282 ? 13.963  -12.314 25.947 1.00 22.94 ? 282 HIS A C   1 
ATOM   2209 O O   . HIS A 1 282 ? 14.205  -11.272 25.333 1.00 22.93 ? 282 HIS A O   1 
ATOM   2210 C CB  . HIS A 1 282 ? 15.432  -12.421 27.938 1.00 19.78 ? 282 HIS A CB  1 
ATOM   2211 C CG  . HIS A 1 282 ? 14.340  -12.494 28.949 1.00 19.34 ? 282 HIS A CG  1 
ATOM   2212 N ND1 . HIS A 1 282 ? 14.129  -13.608 29.731 1.00 22.89 ? 282 HIS A ND1 1 
ATOM   2213 C CD2 . HIS A 1 282 ? 13.363  -11.612 29.274 1.00 26.35 ? 282 HIS A CD2 1 
ATOM   2214 C CE1 . HIS A 1 282 ? 13.078  -13.402 30.511 1.00 21.81 ? 282 HIS A CE1 1 
ATOM   2215 N NE2 . HIS A 1 282 ? 12.598  -12.198 30.254 1.00 22.29 ? 282 HIS A NE2 1 
ATOM   2216 N N   . GLY A 1 283 ? 12.729  -12.800 26.092 1.00 22.24 ? 283 GLY A N   1 
ATOM   2217 C CA  . GLY A 1 283 ? 11.587  -12.078 25.569 1.00 21.69 ? 283 GLY A CA  1 
ATOM   2218 C C   . GLY A 1 283 ? 11.331  -12.274 24.094 1.00 24.99 ? 283 GLY A C   1 
ATOM   2219 O O   . GLY A 1 283 ? 10.541  -11.514 23.515 1.00 24.45 ? 283 GLY A O   1 
ATOM   2220 N N   . PHE A 1 284 ? 11.942  -13.291 23.473 1.00 22.02 ? 284 PHE A N   1 
ATOM   2221 C CA  . PHE A 1 284 ? 11.839  -13.449 22.024 1.00 22.21 ? 284 PHE A CA  1 
ATOM   2222 C C   . PHE A 1 284 ? 10.421  -13.738 21.545 1.00 26.38 ? 284 PHE A C   1 
ATOM   2223 O O   . PHE A 1 284 ? 10.137  -13.514 20.362 1.00 26.77 ? 284 PHE A O   1 
ATOM   2224 C CB  . PHE A 1 284 ? 12.803  -14.539 21.509 1.00 21.79 ? 284 PHE A CB  1 
ATOM   2225 C CG  . PHE A 1 284 ? 12.471  -15.961 21.933 1.00 22.21 ? 284 PHE A CG  1 
ATOM   2226 C CD1 . PHE A 1 284 ? 11.395  -16.656 21.381 1.00 19.90 ? 284 PHE A CD1 1 
ATOM   2227 C CD2 . PHE A 1 284 ? 13.300  -16.630 22.825 1.00 18.39 ? 284 PHE A CD2 1 
ATOM   2228 C CE1 . PHE A 1 284 ? 11.128  -17.961 21.760 1.00 23.88 ? 284 PHE A CE1 1 
ATOM   2229 C CE2 . PHE A 1 284 ? 13.044  -17.928 23.200 1.00 20.30 ? 284 PHE A CE2 1 
ATOM   2230 C CZ  . PHE A 1 284 ? 11.953  -18.599 22.673 1.00 22.83 ? 284 PHE A CZ  1 
ATOM   2231 N N   . ALA A 1 285 ? 9.520   -14.221 22.418 1.00 21.10 ? 285 ALA A N   1 
ATOM   2232 C CA  . ALA A 1 285 ? 8.166   -14.509 21.948 1.00 23.14 ? 285 ALA A CA  1 
ATOM   2233 C C   . ALA A 1 285 ? 7.473   -13.247 21.465 1.00 24.69 ? 285 ALA A C   1 
ATOM   2234 O O   . ALA A 1 285 ? 6.611   -13.312 20.583 1.00 28.23 ? 285 ALA A O   1 
ATOM   2235 C CB  . ALA A 1 285 ? 7.328   -15.178 23.045 1.00 20.88 ? 285 ALA A CB  1 
ATOM   2236 N N   . GLN A 1 286 ? 7.854   -12.094 22.007 1.00 21.96 ? 286 GLN A N   1 
ATOM   2237 C CA  . GLN A 1 286 ? 7.256   -10.825 21.635 1.00 25.74 ? 286 GLN A CA  1 
ATOM   2238 C C   . GLN A 1 286 ? 7.826   -10.261 20.343 1.00 29.50 ? 286 GLN A C   1 
ATOM   2239 O O   . GLN A 1 286 ? 7.385   -9.190  19.909 1.00 32.14 ? 286 GLN A O   1 
ATOM   2240 C CB  . GLN A 1 286 ? 7.422   -9.821  22.774 1.00 27.57 ? 286 GLN A CB  1 
ATOM   2241 C CG  . GLN A 1 286 ? 6.597   -10.218 24.006 1.00 31.63 ? 286 GLN A CG  1 
ATOM   2242 C CD  . GLN A 1 286 ? 6.905   -9.368  25.203 1.00 32.36 ? 286 GLN A CD  1 
ATOM   2243 O OE1 . GLN A 1 286 ? 7.632   -9.784  26.110 1.00 32.60 ? 286 GLN A OE1 1 
ATOM   2244 N NE2 . GLN A 1 286 ? 6.368   -8.152  25.211 1.00 30.82 ? 286 GLN A NE2 1 
ATOM   2245 N N   . PHE A 1 287 ? 8.784   -10.952 19.725 1.00 30.35 ? 287 PHE A N   1 
ATOM   2246 C CA  . PHE A 1 287 ? 9.254   -10.619 18.388 1.00 30.26 ? 287 PHE A CA  1 
ATOM   2247 C C   . PHE A 1 287 ? 8.653   -11.532 17.336 1.00 28.69 ? 287 PHE A C   1 
ATOM   2248 O O   . PHE A 1 287 ? 9.134   -11.558 16.199 1.00 31.38 ? 287 PHE A O   1 
ATOM   2249 C CB  . PHE A 1 287 ? 10.786  -10.656 18.339 1.00 27.82 ? 287 PHE A CB  1 
ATOM   2250 C CG  . PHE A 1 287 ? 11.421  -9.465  18.975 1.00 33.09 ? 287 PHE A CG  1 
ATOM   2251 C CD1 . PHE A 1 287 ? 11.286  -8.207  18.404 1.00 39.99 ? 287 PHE A CD1 1 
ATOM   2252 C CD2 . PHE A 1 287 ? 12.122  -9.584  20.163 1.00 36.43 ? 287 PHE A CD2 1 
ATOM   2253 C CE1 . PHE A 1 287 ? 11.854  -7.094  18.995 1.00 41.84 ? 287 PHE A CE1 1 
ATOM   2254 C CE2 . PHE A 1 287 ? 12.695  -8.474  20.756 1.00 40.13 ? 287 PHE A CE2 1 
ATOM   2255 C CZ  . PHE A 1 287 ? 12.562  -7.228  20.170 1.00 44.38 ? 287 PHE A CZ  1 
ATOM   2256 N N   . TYR A 1 288 ? 7.599   -12.273 17.690 1.00 28.62 ? 288 TYR A N   1 
ATOM   2257 C CA  . TYR A 1 288 ? 6.951   -13.173 16.743 1.00 29.59 ? 288 TYR A CA  1 
ATOM   2258 C C   . TYR A 1 288 ? 6.615   -12.439 15.449 1.00 27.64 ? 288 TYR A C   1 
ATOM   2259 O O   . TYR A 1 288 ? 6.287   -11.251 15.465 1.00 28.13 ? 288 TYR A O   1 
ATOM   2260 C CB  . TYR A 1 288 ? 5.684   -13.756 17.368 1.00 27.11 ? 288 TYR A CB  1 
ATOM   2261 C CG  . TYR A 1 288 ? 4.851   -14.600 16.426 1.00 25.96 ? 288 TYR A CG  1 
ATOM   2262 C CD1 . TYR A 1 288 ? 5.207   -15.917 16.149 1.00 24.84 ? 288 TYR A CD1 1 
ATOM   2263 C CD2 . TYR A 1 288 ? 3.711   -14.082 15.816 1.00 26.08 ? 288 TYR A CD2 1 
ATOM   2264 C CE1 . TYR A 1 288 ? 4.460   -16.696 15.299 1.00 24.86 ? 288 TYR A CE1 1 
ATOM   2265 C CE2 . TYR A 1 288 ? 2.951   -14.861 14.952 1.00 26.85 ? 288 TYR A CE2 1 
ATOM   2266 C CZ  . TYR A 1 288 ? 3.334   -16.163 14.700 1.00 26.13 ? 288 TYR A CZ  1 
ATOM   2267 O OH  . TYR A 1 288 ? 2.597   -16.951 13.850 1.00 30.72 ? 288 TYR A OH  1 
ATOM   2268 N N   . SER A 1 289 ? 6.738   -13.154 14.324 1.00 28.50 ? 289 SER A N   1 
ATOM   2269 C CA  . SER A 1 289 ? 6.481   -12.640 12.972 1.00 30.32 ? 289 SER A CA  1 
ATOM   2270 C C   . SER A 1 289 ? 7.448   -11.541 12.528 1.00 37.17 ? 289 SER A C   1 
ATOM   2271 O O   . SER A 1 289 ? 7.548   -11.249 11.331 1.00 39.56 ? 289 SER A O   1 
ATOM   2272 C CB  . SER A 1 289 ? 5.040   -12.131 12.841 1.00 31.06 ? 289 SER A CB  1 
ATOM   2273 O OG  . SER A 1 289 ? 4.944   -10.772 13.233 1.00 30.62 ? 289 SER A OG  1 
ATOM   2274 N N   . LEU A 1 290 ? 8.154   -10.919 13.464 1.00 35.55 ? 290 LEU A N   1 
ATOM   2275 C CA  . LEU A 1 290 ? 9.118   -9.884  13.119 1.00 34.69 ? 290 LEU A CA  1 
ATOM   2276 C C   . LEU A 1 290 ? 10.519  -10.456 12.970 1.00 42.92 ? 290 LEU A C   1 
ATOM   2277 O O   . LEU A 1 290 ? 11.288  -10.010 12.106 1.00 38.20 ? 290 LEU A O   1 
ATOM   2278 C CB  . LEU A 1 290 ? 9.111   -8.794  14.186 1.00 38.95 ? 290 LEU A CB  1 
ATOM   2279 C CG  . LEU A 1 290 ? 8.991   -7.345  13.737 1.00 51.09 ? 290 LEU A CG  1 
ATOM   2280 C CD1 . LEU A 1 290 ? 7.938   -7.173  12.648 1.00 49.71 ? 290 LEU A CD1 1 
ATOM   2281 C CD2 . LEU A 1 290 ? 8.623   -6.530  14.941 1.00 49.63 ? 290 LEU A CD2 1 
ATOM   2282 N N   . SER A 1 291 ? 10.860  -11.435 13.808 1.00 33.71 ? 291 SER A N   1 
ATOM   2283 C CA  . SER A 1 291 ? 12.139  -12.120 13.763 1.00 33.16 ? 291 SER A CA  1 
ATOM   2284 C C   . SER A 1 291 ? 11.914  -13.545 13.294 1.00 33.42 ? 291 SER A C   1 
ATOM   2285 O O   . SER A 1 291 ? 11.125  -14.282 13.910 1.00 33.27 ? 291 SER A O   1 
ATOM   2286 C CB  . SER A 1 291 ? 12.810  -12.111 15.136 1.00 34.00 ? 291 SER A CB  1 
ATOM   2287 O OG  . SER A 1 291 ? 13.718  -13.193 15.263 1.00 33.38 ? 291 SER A OG  1 
ATOM   2288 N N   . PRO A 1 292 ? 12.563  -13.974 12.210 1.00 32.95 ? 292 PRO A N   1 
ATOM   2289 C CA  . PRO A 1 292 ? 12.344  -15.350 11.737 1.00 30.97 ? 292 PRO A CA  1 
ATOM   2290 C C   . PRO A 1 292 ? 12.704  -16.401 12.770 1.00 33.13 ? 292 PRO A C   1 
ATOM   2291 O O   . PRO A 1 292 ? 11.992  -17.409 12.895 1.00 30.62 ? 292 PRO A O   1 
ATOM   2292 C CB  . PRO A 1 292 ? 13.237  -15.432 10.486 1.00 39.75 ? 292 PRO A CB  1 
ATOM   2293 C CG  . PRO A 1 292 ? 14.236  -14.318 10.652 1.00 35.92 ? 292 PRO A CG  1 
ATOM   2294 C CD  . PRO A 1 292 ? 13.488  -13.225 11.344 1.00 38.44 ? 292 PRO A CD  1 
ATOM   2295 N N   . GLY A 1 293 ? 13.788  -16.195 13.523 1.00 33.34 ? 293 GLY A N   1 
ATOM   2296 C CA  . GLY A 1 293 ? 14.122  -17.136 14.580 1.00 32.87 ? 293 GLY A CA  1 
ATOM   2297 C C   . GLY A 1 293 ? 13.082  -17.163 15.691 1.00 25.37 ? 293 GLY A C   1 
ATOM   2298 O O   . GLY A 1 293 ? 12.694  -18.236 16.160 1.00 27.53 ? 293 GLY A O   1 
ATOM   2299 N N   . ALA A 1 294 ? 12.625  -15.990 16.128 1.00 27.26 ? 294 ALA A N   1 
ATOM   2300 C CA  . ALA A 1 294 ? 11.600  -15.945 17.171 1.00 28.89 ? 294 ALA A CA  1 
ATOM   2301 C C   . ALA A 1 294 ? 10.313  -16.609 16.705 1.00 28.94 ? 294 ALA A C   1 
ATOM   2302 O O   . ALA A 1 294 ? 9.699   -17.382 17.452 1.00 28.51 ? 294 ALA A O   1 
ATOM   2303 C CB  . ALA A 1 294 ? 11.341  -14.500 17.593 1.00 27.95 ? 294 ALA A CB  1 
ATOM   2304 N N   . THR A 1 295 ? 9.899   -16.335 15.460 1.00 30.23 ? 295 THR A N   1 
ATOM   2305 C CA  . THR A 1 295 ? 8.702   -16.966 14.906 1.00 28.29 ? 295 THR A CA  1 
ATOM   2306 C C   . THR A 1 295 ? 8.798   -18.481 14.974 1.00 29.50 ? 295 THR A C   1 
ATOM   2307 O O   . THR A 1 295 ? 7.905   -19.150 15.505 1.00 27.79 ? 295 THR A O   1 
ATOM   2308 C CB  . THR A 1 295 ? 8.501   -16.520 13.458 1.00 25.95 ? 295 THR A CB  1 
ATOM   2309 O OG1 . THR A 1 295 ? 8.457   -15.094 13.409 1.00 27.82 ? 295 THR A OG1 1 
ATOM   2310 C CG2 . THR A 1 295 ? 7.211   -17.103 12.897 1.00 26.89 ? 295 THR A CG2 1 
ATOM   2311 N N   . LYS A 1 296 ? 9.887   -19.042 14.442 1.00 26.74 ? 296 LYS A N   1 
ATOM   2312 C CA  . LYS A 1 296 ? 10.059  -20.494 14.452 1.00 29.79 ? 296 LYS A CA  1 
ATOM   2313 C C   . LYS A 1 296 ? 10.047  -21.049 15.870 1.00 25.11 ? 296 LYS A C   1 
ATOM   2314 O O   . LYS A 1 296 ? 9.520   -22.140 16.114 1.00 27.00 ? 296 LYS A O   1 
ATOM   2315 C CB  . LYS A 1 296 ? 11.375  -20.879 13.770 1.00 27.52 ? 296 LYS A CB  1 
ATOM   2316 C CG  . LYS A 1 296 ? 11.242  -21.283 12.312 1.00 38.38 ? 296 LYS A CG  1 
ATOM   2317 C CD  . LYS A 1 296 ? 12.615  -21.508 11.682 1.00 34.72 ? 296 LYS A CD  1 
ATOM   2318 C CE  . LYS A 1 296 ? 12.959  -20.384 10.720 1.00 47.15 ? 296 LYS A CE  1 
ATOM   2319 N NZ  . LYS A 1 296 ? 13.596  -20.880 9.463  1.00 56.58 ? 296 LYS A NZ  1 
ATOM   2320 N N   . ALA A 1 297 ? 10.677  -20.337 16.804 1.00 27.25 ? 297 ALA A N   1 
ATOM   2321 C CA  . ALA A 1 297 ? 10.804  -20.864 18.158 1.00 27.92 ? 297 ALA A CA  1 
ATOM   2322 C C   . ALA A 1 297 ? 9.460   -20.863 18.879 1.00 22.44 ? 297 ALA A C   1 
ATOM   2323 O O   . ALA A 1 297 ? 9.120   -21.830 19.572 1.00 25.91 ? 297 ALA A O   1 
ATOM   2324 C CB  . ALA A 1 297 ? 11.835  -20.049 18.934 1.00 22.30 ? 297 ALA A CB  1 
ATOM   2325 N N   . LEU A 1 298 ? 8.688   -19.784 18.746 1.00 26.39 ? 298 LEU A N   1 
ATOM   2326 C CA  . LEU A 1 298 ? 7.391   -19.748 19.426 1.00 24.73 ? 298 LEU A CA  1 
ATOM   2327 C C   . LEU A 1 298 ? 6.448   -20.803 18.857 1.00 23.08 ? 298 LEU A C   1 
ATOM   2328 O O   . LEU A 1 298 ? 5.722   -21.466 19.603 1.00 23.97 ? 298 LEU A O   1 
ATOM   2329 C CB  . LEU A 1 298 ? 6.771   -18.356 19.322 1.00 22.18 ? 298 LEU A CB  1 
ATOM   2330 C CG  . LEU A 1 298 ? 5.425   -18.213 20.062 1.00 22.53 ? 298 LEU A CG  1 
ATOM   2331 C CD1 . LEU A 1 298 ? 5.590   -18.574 21.541 1.00 21.40 ? 298 LEU A CD1 1 
ATOM   2332 C CD2 . LEU A 1 298 ? 4.860   -16.809 19.896 1.00 18.30 ? 298 LEU A CD2 1 
ATOM   2333 N N   . VAL A 1 299 ? 6.480   -21.014 17.542 1.00 23.89 ? 299 VAL A N   1 
ATOM   2334 C CA  . VAL A 1 299 ? 5.652   -22.063 16.953 1.00 23.68 ? 299 VAL A CA  1 
ATOM   2335 C C   . VAL A 1 299 ? 6.058   -23.432 17.479 1.00 25.84 ? 299 VAL A C   1 
ATOM   2336 O O   . VAL A 1 299 ? 5.200   -24.284 17.749 1.00 24.22 ? 299 VAL A O   1 
ATOM   2337 C CB  . VAL A 1 299 ? 5.701   -21.994 15.412 1.00 25.61 ? 299 VAL A CB  1 
ATOM   2338 C CG1 . VAL A 1 299 ? 4.879   -23.119 14.809 1.00 28.85 ? 299 VAL A CG1 1 
ATOM   2339 C CG2 . VAL A 1 299 ? 5.195   -20.649 14.926 1.00 28.26 ? 299 VAL A CG2 1 
ATOM   2340 N N   . ARG A 1 300 ? 7.365   -23.665 17.662 1.00 25.46 ? 300 ARG A N   1 
ATOM   2341 C CA  . ARG A 1 300 ? 7.787   -24.939 18.243 1.00 25.93 ? 300 ARG A CA  1 
ATOM   2342 C C   . ARG A 1 300 ? 7.315   -25.084 19.688 1.00 22.46 ? 300 ARG A C   1 
ATOM   2343 O O   . ARG A 1 300 ? 6.907   -26.174 20.104 1.00 24.42 ? 300 ARG A O   1 
ATOM   2344 C CB  . ARG A 1 300 ? 9.312   -25.101 18.204 1.00 27.93 ? 300 ARG A CB  1 
ATOM   2345 C CG  . ARG A 1 300 ? 9.747   -26.398 18.923 1.00 30.12 ? 300 ARG A CG  1 
ATOM   2346 C CD  . ARG A 1 300 ? 11.187  -26.806 18.678 1.00 36.25 ? 300 ARG A CD  1 
ATOM   2347 N NE  . ARG A 1 300 ? 11.508  -28.079 19.332 1.00 40.86 ? 300 ARG A NE  1 
ATOM   2348 C CZ  . ARG A 1 300 ? 11.466  -29.267 18.729 1.00 40.86 ? 300 ARG A CZ  1 
ATOM   2349 N NH1 . ARG A 1 300 ? 11.114  -29.352 17.453 1.00 41.05 ? 300 ARG A NH1 1 
ATOM   2350 N NH2 . ARG A 1 300 ? 11.776  -30.371 19.399 1.00 35.09 ? 300 ARG A NH2 1 
ATOM   2351 N N   . ILE A 1 301 ? 7.423   -24.019 20.487 1.00 23.52 ? 301 ILE A N   1 
ATOM   2352 C CA  . ILE A 1 301 ? 6.907   -24.086 21.858 1.00 20.70 ? 301 ILE A CA  1 
ATOM   2353 C C   . ILE A 1 301 ? 5.418   -24.420 21.840 1.00 20.48 ? 301 ILE A C   1 
ATOM   2354 O O   . ILE A 1 301 ? 4.936   -25.251 22.622 1.00 23.14 ? 301 ILE A O   1 
ATOM   2355 C CB  . ILE A 1 301 ? 7.176   -22.760 22.590 1.00 19.85 ? 301 ILE A CB  1 
ATOM   2356 C CG1 . ILE A 1 301 ? 8.682   -22.525 22.799 1.00 18.95 ? 301 ILE A CG1 1 
ATOM   2357 C CG2 . ILE A 1 301 ? 6.383   -22.683 23.929 1.00 22.05 ? 301 ILE A CG2 1 
ATOM   2358 C CD1 . ILE A 1 301 ? 9.001   -21.076 23.020 1.00 20.18 ? 301 ILE A CD1 1 
ATOM   2359 N N   . ALA A 1 302 ? 4.671   -23.792 20.935 1.00 21.12 ? 302 ALA A N   1 
ATOM   2360 C CA  . ALA A 1 302 ? 3.240   -24.076 20.857 1.00 26.35 ? 302 ALA A CA  1 
ATOM   2361 C C   . ALA A 1 302 ? 2.977   -25.528 20.476 1.00 26.03 ? 302 ALA A C   1 
ATOM   2362 O O   . ALA A 1 302 ? 2.016   -26.136 20.958 1.00 27.10 ? 302 ALA A O   1 
ATOM   2363 C CB  . ALA A 1 302 ? 2.561   -23.120 19.874 1.00 23.67 ? 302 ALA A CB  1 
ATOM   2364 N N   . GLU A 1 303 ? 3.814   -26.112 19.611 1.00 26.24 ? 303 GLU A N   1 
ATOM   2365 C CA  . GLU A 1 303 ? 3.591   -27.513 19.259 1.00 25.29 ? 303 GLU A CA  1 
ATOM   2366 C C   . GLU A 1 303 ? 3.949   -28.444 20.409 1.00 24.58 ? 303 GLU A C   1 
ATOM   2367 O O   . GLU A 1 303 ? 3.356   -29.523 20.539 1.00 24.18 ? 303 GLU A O   1 
ATOM   2368 C CB  . GLU A 1 303 ? 4.380   -27.876 18.001 1.00 31.74 ? 303 GLU A CB  1 
ATOM   2369 C CG  . GLU A 1 303 ? 3.825   -27.210 16.760 1.00 33.67 ? 303 GLU A CG  1 
ATOM   2370 C CD  . GLU A 1 303 ? 4.771   -27.284 15.588 1.00 42.55 ? 303 GLU A CD  1 
ATOM   2371 O OE1 . GLU A 1 303 ? 4.454   -26.686 14.542 1.00 44.51 ? 303 GLU A OE1 1 
ATOM   2372 O OE2 . GLU A 1 303 ? 5.825   -27.942 15.714 1.00 43.30 ? 303 GLU A OE2 1 
ATOM   2373 N N   . LYS A 1 304 ? 4.900   -28.045 21.262 1.00 22.95 ? 304 LYS A N   1 
ATOM   2374 C CA  . LYS A 1 304 ? 5.145   -28.815 22.479 1.00 23.55 ? 304 LYS A CA  1 
ATOM   2375 C C   . LYS A 1 304 ? 3.919   -28.815 23.383 1.00 21.76 ? 304 LYS A C   1 
ATOM   2376 O O   . LYS A 1 304 ? 3.583   -29.838 23.995 1.00 22.95 ? 304 LYS A O   1 
ATOM   2377 C CB  . LYS A 1 304 ? 6.356   -28.264 23.229 1.00 23.76 ? 304 LYS A CB  1 
ATOM   2378 C CG  . LYS A 1 304 ? 7.667   -28.518 22.495 1.00 28.33 ? 304 LYS A CG  1 
ATOM   2379 C CD  . LYS A 1 304 ? 7.956   -30.012 22.448 1.00 26.56 ? 304 LYS A CD  1 
ATOM   2380 C CE  . LYS A 1 304 ? 9.204   -30.299 21.611 1.00 39.20 ? 304 LYS A CE  1 
ATOM   2381 N NZ  . LYS A 1 304 ? 9.605   -31.733 21.730 1.00 36.12 ? 304 LYS A NZ  1 
ATOM   2382 N N   . LEU A 1 305 ? 3.240   -27.676 23.488 1.00 22.34 ? 305 LEU A N   1 
ATOM   2383 C CA  . LEU A 1 305 ? 2.008   -27.645 24.269 1.00 19.77 ? 305 LEU A CA  1 
ATOM   2384 C C   . LEU A 1 305 ? 0.944   -28.554 23.654 1.00 25.10 ? 305 LEU A C   1 
ATOM   2385 O O   . LEU A 1 305 ? 0.269   -29.307 24.370 1.00 24.65 ? 305 LEU A O   1 
ATOM   2386 C CB  . LEU A 1 305 ? 1.514   -26.208 24.370 1.00 22.75 ? 305 LEU A CB  1 
ATOM   2387 C CG  . LEU A 1 305 ? 0.105   -26.005 24.912 1.00 23.05 ? 305 LEU A CG  1 
ATOM   2388 C CD1 . LEU A 1 305 ? 0.070   -26.370 26.390 1.00 25.18 ? 305 LEU A CD1 1 
ATOM   2389 C CD2 . LEU A 1 305 ? -0.288  -24.568 24.684 1.00 22.61 ? 305 LEU A CD2 1 
ATOM   2390 N N   . ARG A 1 306 ? 0.797   -28.513 22.326 1.00 25.91 ? 306 ARG A N   1 
ATOM   2391 C CA  . ARG A 1 306 ? -0.179  -29.371 21.644 1.00 27.52 ? 306 ARG A CA  1 
ATOM   2392 C C   . ARG A 1 306 ? 0.060   -30.844 21.963 1.00 27.98 ? 306 ARG A C   1 
ATOM   2393 O O   . ARG A 1 306 ? -0.877  -31.580 22.307 1.00 31.68 ? 306 ARG A O   1 
ATOM   2394 C CB  . ARG A 1 306 ? -0.114  -29.121 20.132 1.00 27.83 ? 306 ARG A CB  1 
ATOM   2395 C CG  . ARG A 1 306 ? -1.061  -29.979 19.276 1.00 30.59 ? 306 ARG A CG  1 
ATOM   2396 C CD  . ARG A 1 306 ? -0.608  -29.987 17.798 1.00 32.59 ? 306 ARG A CD  1 
ATOM   2397 N NE  . ARG A 1 306 ? 0.661   -30.701 17.645 1.00 38.06 ? 306 ARG A NE  1 
ATOM   2398 C CZ  . ARG A 1 306 ? 1.596   -30.419 16.736 1.00 44.49 ? 306 ARG A CZ  1 
ATOM   2399 N NH1 . ARG A 1 306 ? 1.415   -29.435 15.865 1.00 44.79 ? 306 ARG A NH1 1 
ATOM   2400 N NH2 . ARG A 1 306 ? 2.718   -31.130 16.692 1.00 44.50 ? 306 ARG A NH2 1 
ATOM   2401 N N   . ASP A 1 307 ? 1.317   -31.293 21.862 1.00 27.08 ? 307 ASP A N   1 
ATOM   2402 C CA  . ASP A 1 307 ? 1.637   -32.696 22.110 1.00 26.23 ? 307 ASP A CA  1 
ATOM   2403 C C   . ASP A 1 307 ? 1.391   -33.073 23.562 1.00 28.89 ? 307 ASP A C   1 
ATOM   2404 O O   . ASP A 1 307 ? 0.971   -34.196 23.855 1.00 28.41 ? 307 ASP A O   1 
ATOM   2405 C CB  . ASP A 1 307 ? 3.098   -32.989 21.742 1.00 29.43 ? 307 ASP A CB  1 
ATOM   2406 C CG  . ASP A 1 307 ? 3.388   -32.782 20.265 1.00 37.49 ? 307 ASP A CG  1 
ATOM   2407 O OD1 . ASP A 1 307 ? 2.437   -32.775 19.454 1.00 38.98 ? 307 ASP A OD1 1 
ATOM   2408 O OD2 . ASP A 1 307 ? 4.578   -32.627 19.916 1.00 43.19 ? 307 ASP A OD2 1 
ATOM   2409 N N   . ALA A 1 308 ? 1.667   -32.152 24.491 1.00 28.15 ? 308 ALA A N   1 
ATOM   2410 C CA  . ALA A 1 308 ? 1.482   -32.447 25.911 1.00 29.04 ? 308 ALA A CA  1 
ATOM   2411 C C   . ALA A 1 308 ? 0.012   -32.628 26.269 1.00 30.51 ? 308 ALA A C   1 
ATOM   2412 O O   . ALA A 1 308 ? -0.315  -33.434 27.147 1.00 34.11 ? 308 ALA A O   1 
ATOM   2413 C CB  . ALA A 1 308 ? 2.094   -31.330 26.764 1.00 28.07 ? 308 ALA A CB  1 
ATOM   2414 N N   . LEU A 1 309 ? -0.882  -31.885 25.625 1.00 30.33 ? 309 LEU A N   1 
ATOM   2415 C CA  . LEU A 1 309 ? -2.301  -31.935 25.950 1.00 27.79 ? 309 LEU A CA  1 
ATOM   2416 C C   . LEU A 1 309 ? -3.117  -32.777 24.974 1.00 36.76 ? 309 LEU A C   1 
ATOM   2417 O O   . LEU A 1 309 ? -4.349  -32.805 25.086 1.00 38.13 ? 309 LEU A O   1 
ATOM   2418 C CB  . LEU A 1 309 ? -2.879  -30.517 26.007 1.00 29.07 ? 309 LEU A CB  1 
ATOM   2419 C CG  . LEU A 1 309 ? -2.303  -29.606 27.100 1.00 25.22 ? 309 LEU A CG  1 
ATOM   2420 C CD1 . LEU A 1 309 ? -3.072  -28.320 27.209 1.00 24.37 ? 309 LEU A CD1 1 
ATOM   2421 C CD2 . LEU A 1 309 ? -2.275  -30.340 28.418 1.00 23.95 ? 309 LEU A CD2 1 
ATOM   2422 N N   . ALA A 1 310 ? -2.480  -33.452 24.023 1.00 36.73 ? 310 ALA A N   1 
ATOM   2423 C CA  . ALA A 1 310 ? -3.222  -34.305 23.089 1.00 42.60 ? 310 ALA A CA  1 
ATOM   2424 C C   . ALA A 1 310 ? -3.844  -35.486 23.832 1.00 50.05 ? 310 ALA A C   1 
ATOM   2425 O O   . ALA A 1 310 ? -5.069  -35.637 23.889 1.00 53.03 ? 310 ALA A O   1 
ATOM   2426 C CB  . ALA A 1 310 ? -2.322  -34.796 21.977 1.00 35.19 ? 310 ALA A CB  1 
ATOM   2427 O OXT . ALA A 1 310 ? -3.134  -36.313 24.408 1.00 51.45 ? 310 ALA A OXT 1 
ATOM   2428 N N   . ARG B 2 1   ? 9.049   3.568   -1.464 1.00 72.26 ? 2   ARG B N   1 
ATOM   2429 C CA  . ARG B 2 1   ? 8.074   4.206   -0.586 1.00 76.58 ? 2   ARG B CA  1 
ATOM   2430 C C   . ARG B 2 1   ? 7.509   3.206   0.419  1.00 75.32 ? 2   ARG B C   1 
ATOM   2431 O O   . ARG B 2 1   ? 7.386   2.016   0.130  1.00 75.81 ? 2   ARG B O   1 
ATOM   2432 C CB  . ARG B 2 1   ? 6.935   4.858   -1.403 1.00 74.04 ? 2   ARG B CB  1 
ATOM   2433 C CG  . ARG B 2 1   ? 6.048   3.899   -2.227 1.00 76.94 ? 2   ARG B CG  1 
ATOM   2434 C CD  . ARG B 2 1   ? 4.876   3.307   -1.426 1.00 79.53 ? 2   ARG B CD  1 
ATOM   2435 N NE  . ARG B 2 1   ? 4.481   1.993   -1.939 1.00 83.02 ? 2   ARG B NE  1 
ATOM   2436 C CZ  . ARG B 2 1   ? 3.933   1.028   -1.202 1.00 83.13 ? 2   ARG B CZ  1 
ATOM   2437 N NH1 . ARG B 2 1   ? 3.719   1.214   0.092  1.00 79.43 ? 2   ARG B NH1 1 
ATOM   2438 N NH2 . ARG B 2 1   ? 3.615   -0.137  -1.756 1.00 85.14 ? 2   ARG B NH2 1 
ATOM   2439 N N   . GLY B 2 2   ? 7.153   3.703   1.597  1.00 72.48 ? 3   GLY B N   1 
ATOM   2440 C CA  . GLY B 2 2   ? 6.509   2.876   2.599  1.00 70.95 ? 3   GLY B CA  1 
ATOM   2441 C C   . GLY B 2 2   ? 6.013   3.760   3.716  1.00 71.54 ? 3   GLY B C   1 
ATOM   2442 O O   . GLY B 2 2   ? 6.114   4.988   3.657  1.00 72.63 ? 3   GLY B O   1 
ATOM   2443 N N   . LYS B 2 3   ? 5.470   3.126   4.751  1.00 72.71 ? 4   LYS B N   1 
ATOM   2444 C CA  . LYS B 2 3   ? 4.996   3.882   5.902  1.00 74.94 ? 4   LYS B CA  1 
ATOM   2445 C C   . LYS B 2 3   ? 5.462   3.244   7.200  1.00 70.50 ? 4   LYS B C   1 
ATOM   2446 O O   . LYS B 2 3   ? 5.400   2.021   7.363  1.00 71.08 ? 4   LYS B O   1 
ATOM   2447 C CB  . LYS B 2 3   ? 3.464   4.053   5.885  1.00 75.77 ? 4   LYS B CB  1 
ATOM   2448 C CG  . LYS B 2 3   ? 2.623   2.825   6.170  1.00 74.02 ? 4   LYS B CG  1 
ATOM   2449 C CD  . LYS B 2 3   ? 1.238   3.256   6.638  1.00 76.42 ? 4   LYS B CD  1 
ATOM   2450 C CE  . LYS B 2 3   ? 0.667   4.348   5.730  1.00 75.47 ? 4   LYS B CE  1 
ATOM   2451 N NZ  . LYS B 2 3   ? -0.646  4.875   6.203  1.00 78.39 ? 4   LYS B NZ  1 
ATOM   2452 N N   . VAL B 2 4   ? 5.934   4.089   8.111  1.00 70.78 ? 5   VAL B N   1 
ATOM   2453 C CA  . VAL B 2 4   ? 6.501   3.670   9.386  1.00 71.38 ? 5   VAL B CA  1 
ATOM   2454 C C   . VAL B 2 4   ? 5.446   2.971   10.235 1.00 70.39 ? 5   VAL B C   1 
ATOM   2455 O O   . VAL B 2 4   ? 4.558   3.617   10.804 1.00 70.37 ? 5   VAL B O   1 
ATOM   2456 C CB  . VAL B 2 4   ? 7.097   4.878   10.131 1.00 71.33 ? 5   VAL B CB  1 
ATOM   2457 C CG1 . VAL B 2 4   ? 8.054   4.411   11.218 1.00 69.17 ? 5   VAL B CG1 1 
ATOM   2458 C CG2 . VAL B 2 4   ? 7.799   5.814   9.149  1.00 69.88 ? 5   VAL B CG2 1 
ATOM   2459 N N   . LYS B 2 5   ? 5.543   1.642   10.331 1.00 67.44 ? 6   LYS B N   1 
ATOM   2460 C CA  . LYS B 2 5   ? 4.600   0.883   11.149 1.00 65.81 ? 6   LYS B CA  1 
ATOM   2461 C C   . LYS B 2 5   ? 4.811   1.146   12.634 1.00 66.64 ? 6   LYS B C   1 
ATOM   2462 O O   . LYS B 2 5   ? 3.857   1.098   13.421 1.00 68.87 ? 6   LYS B O   1 
ATOM   2463 C CB  . LYS B 2 5   ? 4.735   -0.611  10.857 1.00 65.31 ? 6   LYS B CB  1 
ATOM   2464 C CG  . LYS B 2 5   ? 3.856   -1.492  11.734 1.00 67.43 ? 6   LYS B CG  1 
ATOM   2465 C CD  . LYS B 2 5   ? 4.087   -2.965  11.451 1.00 74.04 ? 6   LYS B CD  1 
ATOM   2466 C CE  . LYS B 2 5   ? 3.119   -3.483  10.400 1.00 71.54 ? 6   LYS B CE  1 
ATOM   2467 N NZ  . LYS B 2 5   ? 3.741   -4.551  9.570  1.00 71.89 ? 6   LYS B NZ  1 
ATOM   2468 N N   . TRP B 2 6   ? 6.050   1.404   13.040 1.00 62.68 ? 7   TRP B N   1 
ATOM   2469 C CA  . TRP B 2 6   ? 6.375   1.615   14.442 1.00 60.78 ? 7   TRP B CA  1 
ATOM   2470 C C   . TRP B 2 6   ? 7.797   2.147   14.516 1.00 59.36 ? 7   TRP B C   1 
ATOM   2471 O O   . TRP B 2 6   ? 8.647   1.765   13.708 1.00 60.30 ? 7   TRP B O   1 
ATOM   2472 C CB  . TRP B 2 6   ? 6.233   0.316   15.251 1.00 55.74 ? 7   TRP B CB  1 
ATOM   2473 C CG  . TRP B 2 6   ? 6.513   0.436   16.726 1.00 51.76 ? 7   TRP B CG  1 
ATOM   2474 C CD1 . TRP B 2 6   ? 5.622   0.764   17.709 1.00 50.06 ? 7   TRP B CD1 1 
ATOM   2475 C CD2 . TRP B 2 6   ? 7.765   0.197   17.385 1.00 52.08 ? 7   TRP B CD2 1 
ATOM   2476 N NE1 . TRP B 2 6   ? 6.245   0.754   18.936 1.00 51.27 ? 7   TRP B NE1 1 
ATOM   2477 C CE2 . TRP B 2 6   ? 7.559   0.406   18.765 1.00 49.63 ? 7   TRP B CE2 1 
ATOM   2478 C CE3 . TRP B 2 6   ? 9.040   -0.175  16.941 1.00 52.12 ? 7   TRP B CE3 1 
ATOM   2479 C CZ2 . TRP B 2 6   ? 8.582   0.263   19.703 1.00 52.46 ? 7   TRP B CZ2 1 
ATOM   2480 C CZ3 . TRP B 2 6   ? 10.054  -0.316  17.873 1.00 49.89 ? 7   TRP B CZ3 1 
ATOM   2481 C CH2 . TRP B 2 6   ? 9.821   -0.096  19.238 1.00 49.11 ? 7   TRP B CH2 1 
ATOM   2482 N N   . PHE B 2 7   ? 8.040   3.040   15.470 1.00 56.76 ? 8   PHE B N   1 
ATOM   2483 C CA  . PHE B 2 7   ? 9.366   3.610   15.661 1.00 55.77 ? 8   PHE B CA  1 
ATOM   2484 C C   . PHE B 2 7   ? 9.509   4.021   17.117 1.00 54.31 ? 8   PHE B C   1 
ATOM   2485 O O   . PHE B 2 7   ? 8.660   4.748   17.642 1.00 56.81 ? 8   PHE B O   1 
ATOM   2486 C CB  . PHE B 2 7   ? 9.599   4.811   14.731 1.00 59.59 ? 8   PHE B CB  1 
ATOM   2487 C CG  . PHE B 2 7   ? 11.034  5.274   14.686 1.00 60.26 ? 8   PHE B CG  1 
ATOM   2488 C CD1 . PHE B 2 7   ? 11.956  4.645   13.862 1.00 58.87 ? 8   PHE B CD1 1 
ATOM   2489 C CD2 . PHE B 2 7   ? 11.462  6.328   15.477 1.00 60.25 ? 8   PHE B CD2 1 
ATOM   2490 C CE1 . PHE B 2 7   ? 13.279  5.065   13.828 1.00 55.27 ? 8   PHE B CE1 1 
ATOM   2491 C CE2 . PHE B 2 7   ? 12.781  6.752   15.445 1.00 59.70 ? 8   PHE B CE2 1 
ATOM   2492 C CZ  . PHE B 2 7   ? 13.689  6.118   14.622 1.00 51.41 ? 8   PHE B CZ  1 
ATOM   2493 N N   . HIS B 2 8   ? 10.568  3.546   17.771 1.00 55.44 ? 9   HIS B N   1 
ATOM   2494 C CA  . HIS B 2 8   ? 10.841  3.931   19.152 1.00 54.63 ? 9   HIS B CA  1 
ATOM   2495 C C   . HIS B 2 8   ? 11.488  5.310   19.155 1.00 56.86 ? 9   HIS B C   1 
ATOM   2496 O O   . HIS B 2 8   ? 12.614  5.481   18.673 1.00 54.60 ? 9   HIS B O   1 
ATOM   2497 C CB  . HIS B 2 8   ? 11.729  2.906   19.849 1.00 52.52 ? 9   HIS B CB  1 
ATOM   2498 C CG  . HIS B 2 8   ? 11.608  2.929   21.342 1.00 56.69 ? 9   HIS B CG  1 
ATOM   2499 N ND1 . HIS B 2 8   ? 12.386  3.741   22.140 1.00 54.21 ? 9   HIS B ND1 1 
ATOM   2500 C CD2 . HIS B 2 8   ? 10.786  2.255   22.181 1.00 55.06 ? 9   HIS B CD2 1 
ATOM   2501 C CE1 . HIS B 2 8   ? 12.055  3.559   23.406 1.00 57.86 ? 9   HIS B CE1 1 
ATOM   2502 N NE2 . HIS B 2 8   ? 11.089  2.659   23.459 1.00 54.98 ? 9   HIS B NE2 1 
ATOM   2503 N N   . ASP B 2 9   ? 10.774  6.290   19.710 1.00 59.16 ? 10  ASP B N   1 
ATOM   2504 C CA  . ASP B 2 9   ? 11.238  7.671   19.674 1.00 59.49 ? 10  ASP B CA  1 
ATOM   2505 C C   . ASP B 2 9   ? 12.481  7.878   20.530 1.00 60.19 ? 10  ASP B C   1 
ATOM   2506 O O   . ASP B 2 9   ? 13.344  8.687   20.173 1.00 60.08 ? 10  ASP B O   1 
ATOM   2507 C CB  . ASP B 2 9   ? 10.113  8.600   20.131 1.00 67.09 ? 10  ASP B CB  1 
ATOM   2508 C CG  . ASP B 2 9   ? 10.269  10.011  19.605 1.00 69.84 ? 10  ASP B CG  1 
ATOM   2509 O OD1 . ASP B 2 9   ? 10.227  10.196  18.369 1.00 69.64 ? 10  ASP B OD1 1 
ATOM   2510 O OD2 . ASP B 2 9   ? 10.421  10.936  20.432 1.00 67.69 ? 10  ASP B OD2 1 
ATOM   2511 N N   . TYR B 2 10  ? 12.599  7.157   21.650 1.00 58.71 ? 11  TYR B N   1 
ATOM   2512 C CA  . TYR B 2 10  ? 13.722  7.389   22.554 1.00 56.78 ? 11  TYR B CA  1 
ATOM   2513 C C   . TYR B 2 10  ? 14.969  6.617   22.134 1.00 57.05 ? 11  TYR B C   1 
ATOM   2514 O O   . TYR B 2 10  ? 16.084  7.143   22.225 1.00 58.81 ? 11  TYR B O   1 
ATOM   2515 C CB  . TYR B 2 10  ? 13.353  7.018   23.996 1.00 60.15 ? 11  TYR B CB  1 
ATOM   2516 C CG  . TYR B 2 10  ? 14.572  7.026   24.893 1.00 63.03 ? 11  TYR B CG  1 
ATOM   2517 C CD1 . TYR B 2 10  ? 15.109  8.223   25.352 1.00 66.09 ? 11  TYR B CD1 1 
ATOM   2518 C CD2 . TYR B 2 10  ? 15.216  5.845   25.240 1.00 61.96 ? 11  TYR B CD2 1 
ATOM   2519 C CE1 . TYR B 2 10  ? 16.241  8.243   26.152 1.00 65.66 ? 11  TYR B CE1 1 
ATOM   2520 C CE2 . TYR B 2 10  ? 16.354  5.856   26.034 1.00 65.26 ? 11  TYR B CE2 1 
ATOM   2521 C CZ  . TYR B 2 10  ? 16.859  7.058   26.489 1.00 65.45 ? 11  TYR B CZ  1 
ATOM   2522 O OH  . TYR B 2 10  ? 17.985  7.076   27.283 1.00 67.47 ? 11  TYR B OH  1 
ATOM   2523 N N   . TYR B 2 11  ? 14.815  5.366   21.708 1.00 53.61 ? 12  TYR B N   1 
ATOM   2524 C CA  . TYR B 2 11  ? 15.967  4.543   21.375 1.00 52.92 ? 12  TYR B CA  1 
ATOM   2525 C C   . TYR B 2 11  ? 16.327  4.597   19.896 1.00 47.34 ? 12  TYR B C   1 
ATOM   2526 O O   . TYR B 2 11  ? 17.408  4.134   19.523 1.00 49.99 ? 12  TYR B O   1 
ATOM   2527 C CB  . TYR B 2 11  ? 15.722  3.088   21.804 1.00 56.16 ? 12  TYR B CB  1 
ATOM   2528 C CG  . TYR B 2 11  ? 16.037  2.822   23.268 1.00 58.57 ? 12  TYR B CG  1 
ATOM   2529 C CD1 . TYR B 2 11  ? 17.345  2.893   23.745 1.00 54.94 ? 12  TYR B CD1 1 
ATOM   2530 C CD2 . TYR B 2 11  ? 15.026  2.499   24.172 1.00 56.56 ? 12  TYR B CD2 1 
ATOM   2531 C CE1 . TYR B 2 11  ? 17.638  2.655   25.079 1.00 56.57 ? 12  TYR B CE1 1 
ATOM   2532 C CE2 . TYR B 2 11  ? 15.308  2.258   25.510 1.00 57.46 ? 12  TYR B CE2 1 
ATOM   2533 C CZ  . TYR B 2 11  ? 16.617  2.339   25.960 1.00 61.69 ? 12  TYR B CZ  1 
ATOM   2534 O OH  . TYR B 2 11  ? 16.903  2.102   27.292 1.00 59.84 ? 12  TYR B OH  1 
ATOM   2535 N N   . GLY B 2 12  ? 15.455  5.146   19.055 1.00 50.32 ? 13  GLY B N   1 
ATOM   2536 C CA  . GLY B 2 12  ? 15.784  5.408   17.667 1.00 49.75 ? 13  GLY B CA  1 
ATOM   2537 C C   . GLY B 2 12  ? 15.897  4.188   16.776 1.00 50.49 ? 13  GLY B C   1 
ATOM   2538 O O   . GLY B 2 12  ? 16.845  4.075   15.997 1.00 44.73 ? 13  GLY B O   1 
ATOM   2539 N N   . TYR B 2 13  ? 14.943  3.265   16.877 1.00 51.22 ? 14  TYR B N   1 
ATOM   2540 C CA  . TYR B 2 13  ? 14.847  2.145   15.951 1.00 50.84 ? 14  TYR B CA  1 
ATOM   2541 C C   . TYR B 2 13  ? 13.378  1.871   15.671 1.00 49.64 ? 14  TYR B C   1 
ATOM   2542 O O   . TYR B 2 13  ? 12.493  2.309   16.406 1.00 52.19 ? 14  TYR B O   1 
ATOM   2543 C CB  . TYR B 2 13  ? 15.535  0.880   16.485 1.00 46.94 ? 14  TYR B CB  1 
ATOM   2544 C CG  . TYR B 2 13  ? 14.852  0.230   17.675 1.00 49.55 ? 14  TYR B CG  1 
ATOM   2545 C CD1 . TYR B 2 13  ? 15.157  0.625   18.970 1.00 45.00 ? 14  TYR B CD1 1 
ATOM   2546 C CD2 . TYR B 2 13  ? 13.921  -0.792  17.502 1.00 49.45 ? 14  TYR B CD2 1 
ATOM   2547 C CE1 . TYR B 2 13  ? 14.550  0.036   20.058 1.00 51.94 ? 14  TYR B CE1 1 
ATOM   2548 C CE2 . TYR B 2 13  ? 13.303  -1.388  18.591 1.00 50.42 ? 14  TYR B CE2 1 
ATOM   2549 C CZ  . TYR B 2 13  ? 13.622  -0.967  19.866 1.00 52.15 ? 14  TYR B CZ  1 
ATOM   2550 O OH  . TYR B 2 13  ? 13.028  -1.544  20.966 1.00 49.83 ? 14  TYR B OH  1 
ATOM   2551 N N   . GLY B 2 14  ? 13.124  1.145   14.593 1.00 49.47 ? 15  GLY B N   1 
ATOM   2552 C CA  . GLY B 2 14  ? 11.751  0.877   14.220 1.00 53.54 ? 15  GLY B CA  1 
ATOM   2553 C C   . GLY B 2 14  ? 11.684  0.041   12.964 1.00 54.81 ? 15  GLY B C   1 
ATOM   2554 O O   . GLY B 2 14  ? 12.684  -0.519  12.507 1.00 49.40 ? 15  GLY B O   1 
ATOM   2555 N N   . PHE B 2 15  ? 10.477  -0.040  12.415 1.00 54.72 ? 16  PHE B N   1 
ATOM   2556 C CA  . PHE B 2 15  ? 10.233  -0.827  11.220 1.00 56.84 ? 16  PHE B CA  1 
ATOM   2557 C C   . PHE B 2 15  ? 9.353   -0.028  10.273 1.00 60.32 ? 16  PHE B C   1 
ATOM   2558 O O   . PHE B 2 15  ? 8.539   0.796   10.699 1.00 61.16 ? 16  PHE B O   1 
ATOM   2559 C CB  . PHE B 2 15  ? 9.590   -2.180  11.559 1.00 57.45 ? 16  PHE B CB  1 
ATOM   2560 C CG  . PHE B 2 15  ? 10.431  -3.031  12.468 1.00 52.12 ? 16  PHE B CG  1 
ATOM   2561 C CD1 . PHE B 2 15  ? 10.339  -2.899  13.846 1.00 50.57 ? 16  PHE B CD1 1 
ATOM   2562 C CD2 . PHE B 2 15  ? 11.333  -3.942  11.946 1.00 51.14 ? 16  PHE B CD2 1 
ATOM   2563 C CE1 . PHE B 2 15  ? 11.124  -3.669  14.682 1.00 50.12 ? 16  PHE B CE1 1 
ATOM   2564 C CE2 . PHE B 2 15  ? 12.116  -4.715  12.776 1.00 47.71 ? 16  PHE B CE2 1 
ATOM   2565 C CZ  . PHE B 2 15  ? 12.012  -4.578  14.146 1.00 49.54 ? 16  PHE B CZ  1 
ATOM   2566 N N   . ILE B 2 16  ? 9.546   -0.272  8.981  1.00 62.44 ? 17  ILE B N   1 
ATOM   2567 C CA  . ILE B 2 16  ? 8.824   0.410   7.915  1.00 65.55 ? 17  ILE B CA  1 
ATOM   2568 C C   . ILE B 2 16  ? 8.153   -0.649  7.054  1.00 66.62 ? 17  ILE B C   1 
ATOM   2569 O O   . ILE B 2 16  ? 8.808   -1.600  6.611  1.00 64.52 ? 17  ILE B O   1 
ATOM   2570 C CB  . ILE B 2 16  ? 9.765   1.286   7.066  1.00 64.13 ? 17  ILE B CB  1 
ATOM   2571 C CG1 . ILE B 2 16  ? 9.988   2.646   7.730  1.00 62.73 ? 17  ILE B CG1 1 
ATOM   2572 C CG2 . ILE B 2 16  ? 9.212   1.462   5.661  1.00 67.69 ? 17  ILE B CG2 1 
ATOM   2573 C CD1 . ILE B 2 16  ? 11.206  3.379   7.207  1.00 56.97 ? 17  ILE B CD1 1 
ATOM   2574 N N   . THR B 2 17  ? 6.852   -0.491  6.826  1.00 69.06 ? 18  THR B N   1 
ATOM   2575 C CA  . THR B 2 17  ? 6.116   -1.420  5.975  1.00 67.07 ? 18  THR B CA  1 
ATOM   2576 C C   . THR B 2 17  ? 6.150   -0.967  4.520  1.00 64.00 ? 18  THR B C   1 
ATOM   2577 O O   . THR B 2 17  ? 5.850   0.185   4.216  1.00 67.21 ? 18  THR B O   1 
ATOM   2578 C CB  . THR B 2 17  ? 4.651   -1.563  6.429  1.00 70.61 ? 18  THR B CB  1 
ATOM   2579 O OG1 . THR B 2 17  ? 4.585   -1.533  7.860  1.00 68.70 ? 18  THR B OG1 1 
ATOM   2580 C CG2 . THR B 2 17  ? 4.066   -2.876  5.926  1.00 68.90 ? 18  THR B CG2 1 
ATOM   2581 N N   . ASP B 2 23  ? 7.978   -5.509  5.834  1.00 65.79 ? 24  ASP B N   1 
ATOM   2582 C CA  . ASP B 2 23  ? 8.625   -4.763  6.910  1.00 62.14 ? 24  ASP B CA  1 
ATOM   2583 C C   . ASP B 2 23  ? 10.143  -4.754  6.737  1.00 63.60 ? 24  ASP B C   1 
ATOM   2584 O O   . ASP B 2 23  ? 10.733  -5.750  6.309  1.00 61.93 ? 24  ASP B O   1 
ATOM   2585 C CB  . ASP B 2 23  ? 8.257   -5.354  8.271  1.00 63.31 ? 24  ASP B CB  1 
ATOM   2586 C CG  . ASP B 2 23  ? 6.852   -4.982  8.709  1.00 71.12 ? 24  ASP B CG  1 
ATOM   2587 O OD1 . ASP B 2 23  ? 6.104   -4.398  7.895  1.00 72.69 ? 24  ASP B OD1 1 
ATOM   2588 O OD2 . ASP B 2 23  ? 6.493   -5.280  9.869  1.00 78.30 ? 24  ASP B OD2 1 
ATOM   2589 N N   . VAL B 2 24  ? 10.768  -3.619  7.056  1.00 63.61 ? 25  VAL B N   1 
ATOM   2590 C CA  . VAL B 2 24  ? 12.216  -3.446  6.966  1.00 60.96 ? 25  VAL B CA  1 
ATOM   2591 C C   . VAL B 2 24  ? 12.678  -2.581  8.136  1.00 58.86 ? 25  VAL B C   1 
ATOM   2592 O O   . VAL B 2 24  ? 11.994  -1.628  8.523  1.00 58.97 ? 25  VAL B O   1 
ATOM   2593 C CB  . VAL B 2 24  ? 12.636  -2.815  5.617  1.00 59.06 ? 25  VAL B CB  1 
ATOM   2594 C CG1 . VAL B 2 24  ? 14.137  -2.775  5.493  1.00 62.91 ? 25  VAL B CG1 1 
ATOM   2595 C CG2 . VAL B 2 24  ? 12.055  -3.586  4.439  1.00 61.24 ? 25  VAL B CG2 1 
ATOM   2596 N N   . PHE B 2 25  ? 13.842  -2.911  8.696  1.00 59.82 ? 26  PHE B N   1 
ATOM   2597 C CA  . PHE B 2 25  ? 14.369  -2.195  9.853  1.00 53.67 ? 26  PHE B CA  1 
ATOM   2598 C C   . PHE B 2 25  ? 14.913  -0.826  9.455  1.00 52.32 ? 26  PHE B C   1 
ATOM   2599 O O   . PHE B 2 25  ? 15.440  -0.634  8.356  1.00 58.48 ? 26  PHE B O   1 
ATOM   2600 C CB  . PHE B 2 25  ? 15.476  -3.018  10.526 1.00 52.43 ? 26  PHE B CB  1 
ATOM   2601 C CG  . PHE B 2 25  ? 16.063  -2.376  11.766 1.00 50.02 ? 26  PHE B CG  1 
ATOM   2602 C CD1 . PHE B 2 25  ? 15.493  -2.590  13.013 1.00 46.22 ? 26  PHE B CD1 1 
ATOM   2603 C CD2 . PHE B 2 25  ? 17.196  -1.583  11.684 1.00 46.52 ? 26  PHE B CD2 1 
ATOM   2604 C CE1 . PHE B 2 25  ? 16.035  -2.015  14.151 1.00 42.71 ? 26  PHE B CE1 1 
ATOM   2605 C CE2 . PHE B 2 25  ? 17.742  -1.001  12.815 1.00 48.12 ? 26  PHE B CE2 1 
ATOM   2606 C CZ  . PHE B 2 25  ? 17.161  -1.216  14.051 1.00 46.12 ? 26  PHE B CZ  1 
ATOM   2607 N N   . VAL B 2 26  ? 14.795  0.128   10.377 1.00 48.60 ? 27  VAL B N   1 
ATOM   2608 C CA  . VAL B 2 26  ? 15.389  1.455   10.220 1.00 51.73 ? 27  VAL B CA  1 
ATOM   2609 C C   . VAL B 2 26  ? 15.775  1.969   11.602 1.00 52.26 ? 27  VAL B C   1 
ATOM   2610 O O   . VAL B 2 26  ? 15.016  1.815   12.564 1.00 50.27 ? 27  VAL B O   1 
ATOM   2611 C CB  . VAL B 2 26  ? 14.421  2.425   9.505  1.00 50.23 ? 27  VAL B CB  1 
ATOM   2612 C CG1 . VAL B 2 26  ? 13.053  2.387   10.159 1.00 51.12 ? 27  VAL B CG1 1 
ATOM   2613 C CG2 . VAL B 2 26  ? 14.972  3.845   9.498  1.00 51.06 ? 27  VAL B CG2 1 
ATOM   2614 N N   . ASN B 2 27  ? 16.970  2.559   11.709 1.00 47.41 ? 28  ASN B N   1 
ATOM   2615 C CA  . ASN B 2 27  ? 17.388  3.240   12.929 1.00 49.67 ? 28  ASN B CA  1 
ATOM   2616 C C   . ASN B 2 27  ? 17.571  4.732   12.653 1.00 53.59 ? 28  ASN B C   1 
ATOM   2617 O O   . ASN B 2 27  ? 17.464  5.195   11.514 1.00 54.01 ? 28  ASN B O   1 
ATOM   2618 C CB  . ASN B 2 27  ? 18.656  2.608   13.524 1.00 49.20 ? 28  ASN B CB  1 
ATOM   2619 C CG  . ASN B 2 27  ? 19.838  2.606   12.566 1.00 53.67 ? 28  ASN B CG  1 
ATOM   2620 O OD1 . ASN B 2 27  ? 19.980  3.487   11.721 1.00 53.16 ? 28  ASN B OD1 1 
ATOM   2621 N ND2 . ASN B 2 27  ? 20.709  1.616   12.717 1.00 48.51 ? 28  ASN B ND2 1 
ATOM   2622 N N   . ALA B 2 28  ? 17.853  5.486   13.720 1.00 50.80 ? 29  ALA B N   1 
ATOM   2623 C CA  . ALA B 2 28  ? 17.849  6.944   13.624 1.00 53.49 ? 29  ALA B CA  1 
ATOM   2624 C C   . ALA B 2 28  ? 18.959  7.467   12.717 1.00 59.31 ? 29  ALA B C   1 
ATOM   2625 O O   . ALA B 2 28  ? 18.794  8.518   12.085 1.00 59.86 ? 29  ALA B O   1 
ATOM   2626 C CB  . ALA B 2 28  ? 17.967  7.563   15.017 1.00 51.42 ? 29  ALA B CB  1 
ATOM   2627 N N   . ASP B 2 29  ? 20.092  6.763   12.643 1.00 55.77 ? 30  ASP B N   1 
ATOM   2628 C CA  . ASP B 2 29  ? 21.177  7.193   11.768 1.00 57.21 ? 30  ASP B CA  1 
ATOM   2629 C C   . ASP B 2 29  ? 20.789  7.128   10.295 1.00 60.76 ? 30  ASP B C   1 
ATOM   2630 O O   . ASP B 2 29  ? 21.377  7.846   9.479  1.00 59.41 ? 30  ASP B O   1 
ATOM   2631 C CB  . ASP B 2 29  ? 22.425  6.343   12.021 1.00 54.83 ? 30  ASP B CB  1 
ATOM   2632 C CG  . ASP B 2 29  ? 23.195  6.779   13.262 1.00 57.91 ? 30  ASP B CG  1 
ATOM   2633 O OD1 . ASP B 2 29  ? 22.777  7.760   13.918 1.00 56.72 ? 30  ASP B OD1 1 
ATOM   2634 O OD2 . ASP B 2 29  ? 24.222  6.137   13.582 1.00 59.83 ? 30  ASP B OD2 1 
ATOM   2635 N N   . ALA B 2 30  ? 19.810  6.294   9.939  1.00 59.27 ? 31  ALA B N   1 
ATOM   2636 C CA  . ALA B 2 30  ? 19.370  6.177   8.556  1.00 61.47 ? 31  ALA B CA  1 
ATOM   2637 C C   . ALA B 2 30  ? 18.523  7.358   8.103  1.00 62.82 ? 31  ALA B C   1 
ATOM   2638 O O   . ALA B 2 30  ? 18.306  7.514   6.897  1.00 66.79 ? 31  ALA B O   1 
ATOM   2639 C CB  . ALA B 2 30  ? 18.587  4.876   8.360  1.00 58.21 ? 31  ALA B CB  1 
ATOM   2640 N N   . ILE B 2 31  ? 18.048  8.186   9.025  1.00 63.06 ? 32  ILE B N   1 
ATOM   2641 C CA  . ILE B 2 31  ? 17.173  9.302   8.681  1.00 66.49 ? 32  ILE B CA  1 
ATOM   2642 C C   . ILE B 2 31  ? 18.013  10.500  8.254  1.00 68.20 ? 32  ILE B C   1 
ATOM   2643 O O   . ILE B 2 31  ? 19.161  10.667  8.679  1.00 67.13 ? 32  ILE B O   1 
ATOM   2644 C CB  . ILE B 2 31  ? 16.249  9.640   9.870  1.00 64.27 ? 32  ILE B CB  1 
ATOM   2645 C CG1 . ILE B 2 31  ? 15.572  8.367   10.388 1.00 64.19 ? 32  ILE B CG1 1 
ATOM   2646 C CG2 . ILE B 2 31  ? 15.192  10.662  9.474  1.00 66.46 ? 32  ILE B CG2 1 
ATOM   2647 C CD1 . ILE B 2 31  ? 14.892  8.541   11.726 1.00 61.80 ? 32  ILE B CD1 1 
ATOM   2648 N N   . ASP B 2 32  ? 17.441  11.336  7.391  1.00 72.66 ? 33  ASP B N   1 
ATOM   2649 C CA  . ASP B 2 32  ? 18.130  12.513  6.875  1.00 70.99 ? 33  ASP B CA  1 
ATOM   2650 C C   . ASP B 2 32  ? 17.315  13.783  7.108  1.00 70.46 ? 33  ASP B C   1 
ATOM   2651 O O   . ASP B 2 32  ? 16.254  13.968  6.512  1.00 73.83 ? 33  ASP B O   1 
ATOM   2652 C CB  . ASP B 2 32  ? 18.428  12.342  5.383  1.00 70.83 ? 33  ASP B CB  1 
ATOM   2653 C CG  . ASP B 2 32  ? 19.553  11.356  5.123  1.00 73.92 ? 33  ASP B CG  1 
ATOM   2654 O OD1 . ASP B 2 32  ? 20.430  11.203  6.000  1.00 71.93 ? 33  ASP B OD1 1 
ATOM   2655 O OD2 . ASP B 2 32  ? 19.565  10.731  4.041  1.00 78.17 ? 33  ASP B OD2 1 
ATOM   2656 N N   . LYS B 2 37  ? 15.159  14.783  15.128 1.00 64.15 ? 38  LYS B N   1 
ATOM   2657 C CA  . LYS B 2 37  ? 15.492  13.527  14.461 1.00 67.85 ? 38  LYS B CA  1 
ATOM   2658 C C   . LYS B 2 37  ? 14.613  12.362  14.914 1.00 69.75 ? 38  LYS B C   1 
ATOM   2659 O O   . LYS B 2 37  ? 14.857  11.773  15.972 1.00 68.87 ? 38  LYS B O   1 
ATOM   2660 C CB  . LYS B 2 37  ? 16.958  13.178  14.705 1.00 71.33 ? 38  LYS B CB  1 
ATOM   2661 C CG  . LYS B 2 37  ? 17.506  12.145  13.744 1.00 68.60 ? 38  LYS B CG  1 
ATOM   2662 C CD  . LYS B 2 37  ? 18.413  12.795  12.723 1.00 61.55 ? 38  LYS B CD  1 
ATOM   2663 C CE  . LYS B 2 37  ? 18.728  11.833  11.593 1.00 65.64 ? 38  LYS B CE  1 
ATOM   2664 N NZ  . LYS B 2 37  ? 20.033  11.142  11.780 1.00 61.26 ? 38  LYS B NZ  1 
ATOM   2665 N N   . THR B 2 38  ? 13.604  12.018  14.114 1.00 71.14 ? 39  THR B N   1 
ATOM   2666 C CA  . THR B 2 38  ? 12.730  10.900  14.445 1.00 71.21 ? 39  THR B CA  1 
ATOM   2667 C C   . THR B 2 38  ? 11.790  10.614  13.284 1.00 73.12 ? 39  THR B C   1 
ATOM   2668 O O   . THR B 2 38  ? 11.520  11.486  12.452 1.00 73.56 ? 39  THR B O   1 
ATOM   2669 C CB  . THR B 2 38  ? 11.907  11.177  15.711 1.00 70.58 ? 39  THR B CB  1 
ATOM   2670 O OG1 . THR B 2 38  ? 11.204  9.989   16.094 1.00 70.14 ? 39  THR B OG1 1 
ATOM   2671 C CG2 . THR B 2 38  ? 10.908  12.295  15.463 1.00 71.75 ? 39  THR B CG2 1 
ATOM   2672 N N   . LEU B 2 39  ? 11.312  9.375   13.241 1.00 72.83 ? 40  LEU B N   1 
ATOM   2673 C CA  . LEU B 2 39  ? 10.142  8.976   12.476 1.00 70.69 ? 40  LEU B CA  1 
ATOM   2674 C C   . LEU B 2 39  ? 8.980   8.746   13.436 1.00 69.02 ? 40  LEU B C   1 
ATOM   2675 O O   . LEU B 2 39  ? 9.170   8.459   14.620 1.00 68.09 ? 40  LEU B O   1 
ATOM   2676 C CB  . LEU B 2 39  ? 10.415  7.702   11.671 1.00 67.69 ? 40  LEU B CB  1 
ATOM   2677 C CG  . LEU B 2 39  ? 11.345  7.805   10.464 1.00 67.28 ? 40  LEU B CG  1 
ATOM   2678 C CD1 . LEU B 2 39  ? 11.568  6.430   9.842  1.00 65.33 ? 40  LEU B CD1 1 
ATOM   2679 C CD2 . LEU B 2 39  ? 10.771  8.776   9.445  1.00 69.54 ? 40  LEU B CD2 1 
ATOM   2680 N N   . LYS B 2 40  ? 7.767   8.884   12.916 1.00 72.38 ? 41  LYS B N   1 
ATOM   2681 C CA  . LYS B 2 40  ? 6.568   8.647   13.706 1.00 72.66 ? 41  LYS B CA  1 
ATOM   2682 C C   . LYS B 2 40  ? 5.646   7.700   12.952 1.00 72.57 ? 41  LYS B C   1 
ATOM   2683 O O   . LYS B 2 40  ? 5.640   7.662   11.718 1.00 72.60 ? 41  LYS B O   1 
ATOM   2684 C CB  . LYS B 2 40  ? 5.839   9.964   14.040 1.00 72.64 ? 41  LYS B CB  1 
ATOM   2685 C CG  . LYS B 2 40  ? 5.154   10.014  15.395 1.00 74.28 ? 41  LYS B CG  1 
ATOM   2686 C CD  . LYS B 2 40  ? 3.931   10.924  15.330 1.00 73.75 ? 41  LYS B CD  1 
ATOM   2687 C CE  . LYS B 2 40  ? 2.859   10.494  16.316 1.00 66.34 ? 41  LYS B CE  1 
ATOM   2688 N NZ  . LYS B 2 40  ? 2.149   9.268   15.841 1.00 66.74 ? 41  LYS B NZ  1 
ATOM   2689 N N   . GLU B 2 41  ? 4.875   6.928   13.715 1.00 75.51 ? 42  GLU B N   1 
ATOM   2690 C CA  . GLU B 2 41  ? 4.032   5.894   13.134 1.00 76.07 ? 42  GLU B CA  1 
ATOM   2691 C C   . GLU B 2 41  ? 2.989   6.503   12.206 1.00 75.36 ? 42  GLU B C   1 
ATOM   2692 O O   . GLU B 2 41  ? 2.219   7.386   12.604 1.00 71.14 ? 42  GLU B O   1 
ATOM   2693 C CB  . GLU B 2 41  ? 3.348   5.096   14.241 1.00 74.34 ? 42  GLU B CB  1 
ATOM   2694 C CG  . GLU B 2 41  ? 2.706   3.816   13.743 1.00 76.03 ? 42  GLU B CG  1 
ATOM   2695 C CD  . GLU B 2 41  ? 1.346   4.036   13.119 1.00 81.94 ? 42  GLU B CD  1 
ATOM   2696 O OE1 . GLU B 2 41  ? 1.222   3.883   11.884 1.00 82.61 ? 42  GLU B OE1 1 
ATOM   2697 O OE2 . GLU B 2 41  ? 0.394   4.342   13.870 1.00 86.11 ? 42  GLU B OE2 1 
ATOM   2698 N N   . GLY B 2 42  ? 2.960   6.018   10.967 1.00 76.10 ? 43  GLY B N   1 
ATOM   2699 C CA  . GLY B 2 42  ? 1.999   6.455   9.976  1.00 76.22 ? 43  GLY B CA  1 
ATOM   2700 C C   . GLY B 2 42  ? 2.575   7.322   8.881  1.00 77.13 ? 43  GLY B C   1 
ATOM   2701 O O   . GLY B 2 42  ? 1.863   7.616   7.911  1.00 77.59 ? 43  GLY B O   1 
ATOM   2702 N N   . GLN B 2 43  ? 3.832   7.740   9.001  1.00 78.26 ? 44  GLN B N   1 
ATOM   2703 C CA  . GLN B 2 43  ? 4.453   8.609   8.012  1.00 77.06 ? 44  GLN B CA  1 
ATOM   2704 C C   . GLN B 2 43  ? 4.813   7.832   6.756  1.00 77.86 ? 44  GLN B C   1 
ATOM   2705 O O   . GLN B 2 43  ? 5.150   6.650   6.814  1.00 80.35 ? 44  GLN B O   1 
ATOM   2706 C CB  . GLN B 2 43  ? 5.719   9.250   8.573  1.00 73.08 ? 44  GLN B CB  1 
ATOM   2707 C CG  . GLN B 2 43  ? 5.504   10.596  9.202  1.00 73.42 ? 44  GLN B CG  1 
ATOM   2708 C CD  . GLN B 2 43  ? 6.595   10.945  10.183 1.00 77.37 ? 44  GLN B CD  1 
ATOM   2709 O OE1 . GLN B 2 43  ? 6.364   11.005  11.384 1.00 77.16 ? 44  GLN B OE1 1 
ATOM   2710 N NE2 . GLN B 2 43  ? 7.797   11.173  9.676  1.00 73.30 ? 44  GLN B NE2 1 
ATOM   2711 N N   . VAL B 2 44  ? 4.769   8.515   5.615  1.00 75.77 ? 45  VAL B N   1 
ATOM   2712 C CA  . VAL B 2 44  ? 5.183   7.934   4.344  1.00 78.61 ? 45  VAL B CA  1 
ATOM   2713 C C   . VAL B 2 44  ? 6.584   8.441   4.022  1.00 78.10 ? 45  VAL B C   1 
ATOM   2714 O O   . VAL B 2 44  ? 6.862   9.643   4.129  1.00 80.40 ? 45  VAL B O   1 
ATOM   2715 C CB  . VAL B 2 44  ? 4.180   8.257   3.220  1.00 79.40 ? 45  VAL B CB  1 
ATOM   2716 C CG1 . VAL B 2 44  ? 4.068   9.765   2.987  1.00 78.71 ? 45  VAL B CG1 1 
ATOM   2717 C CG2 . VAL B 2 44  ? 4.549   7.512   1.938  1.00 77.20 ? 45  VAL B CG2 1 
ATOM   2718 N N   . VAL B 2 45  ? 7.479   7.520   3.656  1.00 77.73 ? 46  VAL B N   1 
ATOM   2719 C CA  . VAL B 2 45  ? 8.901   7.815   3.538  1.00 76.42 ? 46  VAL B CA  1 
ATOM   2720 C C   . VAL B 2 45  ? 9.451   7.232   2.243  1.00 75.63 ? 46  VAL B C   1 
ATOM   2721 O O   . VAL B 2 45  ? 8.841   6.367   1.609  1.00 77.50 ? 46  VAL B O   1 
ATOM   2722 C CB  . VAL B 2 45  ? 9.709   7.270   4.740  1.00 76.33 ? 46  VAL B CB  1 
ATOM   2723 C CG1 . VAL B 2 45  ? 9.150   7.796   6.059  1.00 70.93 ? 46  VAL B CG1 1 
ATOM   2724 C CG2 . VAL B 2 45  ? 9.716   5.744   4.724  1.00 74.66 ? 46  VAL B CG2 1 
ATOM   2725 N N   . GLU B 2 46  ? 10.629  7.719   1.861  1.00 76.43 ? 47  GLU B N   1 
ATOM   2726 C CA  . GLU B 2 46  ? 11.397  7.171   0.753  1.00 77.26 ? 47  GLU B CA  1 
ATOM   2727 C C   . GLU B 2 46  ? 12.773  6.767   1.264  1.00 76.57 ? 47  GLU B C   1 
ATOM   2728 O O   . GLU B 2 46  ? 13.400  7.501   2.035  1.00 76.18 ? 47  GLU B O   1 
ATOM   2729 C CB  . GLU B 2 46  ? 11.527  8.179   -0.397 1.00 80.31 ? 47  GLU B CB  1 
ATOM   2730 C CG  . GLU B 2 46  ? 12.075  7.587   -1.695 1.00 80.76 ? 47  GLU B CG  1 
ATOM   2731 C CD  . GLU B 2 46  ? 11.653  8.375   -2.926 1.00 84.41 ? 47  GLU B CD  1 
ATOM   2732 O OE1 . GLU B 2 46  ? 10.442  8.390   -3.239 1.00 83.85 ? 47  GLU B OE1 1 
ATOM   2733 O OE2 . GLU B 2 46  ? 12.531  8.982   -3.578 1.00 82.87 ? 47  GLU B OE2 1 
ATOM   2734 N N   . PHE B 2 47  ? 13.238  5.599   0.829  1.00 77.70 ? 48  PHE B N   1 
ATOM   2735 C CA  . PHE B 2 47  ? 14.455  5.016   1.372  1.00 76.76 ? 48  PHE B CA  1 
ATOM   2736 C C   . PHE B 2 47  ? 15.083  4.101   0.334  1.00 76.72 ? 48  PHE B C   1 
ATOM   2737 O O   . PHE B 2 47  ? 14.442  3.705   -0.644 1.00 80.70 ? 48  PHE B O   1 
ATOM   2738 C CB  . PHE B 2 47  ? 14.164  4.224   2.652  1.00 76.17 ? 48  PHE B CB  1 
ATOM   2739 C CG  . PHE B 2 47  ? 13.075  3.198   2.489  1.00 75.09 ? 48  PHE B CG  1 
ATOM   2740 C CD1 . PHE B 2 47  ? 13.359  1.934   2.002  1.00 75.48 ? 48  PHE B CD1 1 
ATOM   2741 C CD2 . PHE B 2 47  ? 11.761  3.506   2.806  1.00 75.09 ? 48  PHE B CD2 1 
ATOM   2742 C CE1 . PHE B 2 47  ? 12.352  0.997   1.845  1.00 77.98 ? 48  PHE B CE1 1 
ATOM   2743 C CE2 . PHE B 2 47  ? 10.754  2.568   2.650  1.00 74.48 ? 48  PHE B CE2 1 
ATOM   2744 C CZ  . PHE B 2 47  ? 11.052  1.313   2.171  1.00 74.98 ? 48  PHE B CZ  1 
ATOM   2745 N N   . GLU B 2 48  ? 16.344  3.759   0.565  1.00 74.59 ? 49  GLU B N   1 
ATOM   2746 C CA  . GLU B 2 48  ? 16.988  2.670   -0.150 1.00 76.89 ? 49  GLU B CA  1 
ATOM   2747 C C   . GLU B 2 48  ? 16.961  1.407   0.696  1.00 77.91 ? 49  GLU B C   1 
ATOM   2748 O O   . GLU B 2 48  ? 16.906  1.461   1.928  1.00 77.24 ? 49  GLU B O   1 
ATOM   2749 C CB  . GLU B 2 48  ? 18.434  3.006   -0.497 1.00 74.68 ? 49  GLU B CB  1 
ATOM   2750 C CG  . GLU B 2 48  ? 18.617  4.335   -1.149 1.00 76.75 ? 49  GLU B CG  1 
ATOM   2751 C CD  . GLU B 2 48  ? 20.068  4.664   -1.348 1.00 74.64 ? 49  GLU B CD  1 
ATOM   2752 O OE1 . GLU B 2 48  ? 20.905  3.734   -1.338 1.00 78.64 ? 49  GLU B OE1 1 
ATOM   2753 O OE2 . GLU B 2 48  ? 20.366  5.860   -1.500 1.00 77.66 ? 49  GLU B OE2 1 
ATOM   2754 N N   . ILE B 2 49  ? 17.007  0.265   0.022  1.00 79.18 ? 50  ILE B N   1 
ATOM   2755 C CA  . ILE B 2 49  ? 17.163  -0.998  0.725  1.00 77.89 ? 50  ILE B CA  1 
ATOM   2756 C C   . ILE B 2 49  ? 18.646  -1.259  0.974  1.00 77.01 ? 50  ILE B C   1 
ATOM   2757 O O   . ILE B 2 49  ? 19.528  -0.748  0.279  1.00 78.17 ? 50  ILE B O   1 
ATOM   2758 C CB  . ILE B 2 49  ? 16.494  -2.150  -0.050 1.00 79.15 ? 50  ILE B CB  1 
ATOM   2759 C CG1 . ILE B 2 49  ? 14.997  -1.896  -0.148 1.00 82.37 ? 50  ILE B CG1 1 
ATOM   2760 C CG2 . ILE B 2 49  ? 16.616  -3.467  0.698  1.00 76.47 ? 50  ILE B CG2 1 
ATOM   2761 C CD1 . ILE B 2 49  ? 14.415  -1.416  1.152  1.00 78.36 ? 50  ILE B CD1 1 
ATOM   2762 N N   . ASP B 2 50  ? 18.911  -2.044  2.017  1.00 75.94 ? 51  ASP B N   1 
ATOM   2763 C CA  . ASP B 2 50  ? 20.226  -2.344  2.561  1.00 73.15 ? 51  ASP B CA  1 
ATOM   2764 C C   . ASP B 2 50  ? 20.159  -3.822  2.963  1.00 74.26 ? 51  ASP B C   1 
ATOM   2765 O O   . ASP B 2 50  ? 19.929  -4.179  4.123  1.00 74.60 ? 51  ASP B O   1 
ATOM   2766 C CB  . ASP B 2 50  ? 20.549  -1.425  3.740  1.00 70.94 ? 51  ASP B CB  1 
ATOM   2767 C CG  . ASP B 2 50  ? 21.997  -1.479  4.163  1.00 71.57 ? 51  ASP B CG  1 
ATOM   2768 O OD1 . ASP B 2 50  ? 22.641  -2.534  3.988  1.00 70.32 ? 51  ASP B OD1 1 
ATOM   2769 O OD2 . ASP B 2 50  ? 22.483  -0.452  4.691  1.00 69.07 ? 51  ASP B OD2 1 
ATOM   2770 N N   . SER B 2 51  ? 20.316  -4.696  1.965  1.00 71.00 ? 52  SER B N   1 
ATOM   2771 C CA  . SER B 2 51  ? 20.127  -6.131  2.142  1.00 70.57 ? 52  SER B CA  1 
ATOM   2772 C C   . SER B 2 51  ? 21.438  -6.861  2.419  1.00 69.45 ? 52  SER B C   1 
ATOM   2773 O O   . SER B 2 51  ? 21.606  -8.016  2.012  1.00 73.43 ? 52  SER B O   1 
ATOM   2774 C CB  . SER B 2 51  ? 19.428  -6.730  0.922  1.00 71.93 ? 52  SER B CB  1 
ATOM   2775 O OG  . SER B 2 51  ? 18.090  -6.269  0.829  1.00 69.24 ? 52  SER B OG  1 
ATOM   2776 N N   . THR B 2 52  ? 22.367  -6.209  3.108  1.00 68.93 ? 53  THR B N   1 
ATOM   2777 C CA  . THR B 2 52  ? 23.590  -6.860  3.558  1.00 71.04 ? 53  THR B CA  1 
ATOM   2778 C C   . THR B 2 52  ? 23.272  -7.978  4.548  1.00 70.70 ? 53  THR B C   1 
ATOM   2779 O O   . THR B 2 52  ? 23.526  -9.153  4.274  1.00 70.31 ? 53  THR B O   1 
ATOM   2780 C CB  . THR B 2 52  ? 24.550  -5.853  4.220  1.00 71.43 ? 53  THR B CB  1 
ATOM   2781 O OG1 . THR B 2 52  ? 24.948  -4.867  3.260  1.00 65.40 ? 53  THR B OG1 1 
ATOM   2782 C CG2 . THR B 2 52  ? 25.783  -6.566  4.749  1.00 64.97 ? 53  THR B CG2 1 
ATOM   2783 N N   . ALA B 2 56  ? 16.944  -10.209 6.999  1.00 61.07 ? 57  ALA B N   1 
ATOM   2784 C CA  . ALA B 2 56  ? 16.786  -9.015  7.821  1.00 61.79 ? 57  ALA B CA  1 
ATOM   2785 C C   . ALA B 2 56  ? 17.204  -7.746  7.078  1.00 63.62 ? 57  ALA B C   1 
ATOM   2786 O O   . ALA B 2 56  ? 18.284  -7.205  7.323  1.00 65.17 ? 57  ALA B O   1 
ATOM   2787 C CB  . ALA B 2 56  ? 17.583  -9.152  9.103  1.00 54.93 ? 57  ALA B CB  1 
ATOM   2788 N N   . PRO B 2 57  ? 16.344  -7.260  6.186  1.00 66.93 ? 58  PRO B N   1 
ATOM   2789 C CA  . PRO B 2 57  ? 16.671  -6.045  5.436  1.00 68.71 ? 58  PRO B CA  1 
ATOM   2790 C C   . PRO B 2 57  ? 16.651  -4.817  6.334  1.00 69.19 ? 58  PRO B C   1 
ATOM   2791 O O   . PRO B 2 57  ? 16.028  -4.795  7.400  1.00 64.54 ? 58  PRO B O   1 
ATOM   2792 C CB  . PRO B 2 57  ? 15.569  -5.975  4.376  1.00 68.73 ? 58  PRO B CB  1 
ATOM   2793 C CG  . PRO B 2 57  ? 14.402  -6.646  5.023  1.00 64.88 ? 58  PRO B CG  1 
ATOM   2794 C CD  . PRO B 2 57  ? 14.976  -7.733  5.906  1.00 66.05 ? 58  PRO B CD  1 
ATOM   2795 N N   . GLN B 2 58  ? 17.333  -3.771  5.864  1.00 68.26 ? 59  GLN B N   1 
ATOM   2796 C CA  . GLN B 2 58  ? 17.489  -2.533  6.612  1.00 65.99 ? 59  GLN B CA  1 
ATOM   2797 C C   . GLN B 2 58  ? 17.348  -1.351  5.659  1.00 69.62 ? 59  GLN B C   1 
ATOM   2798 O O   . GLN B 2 58  ? 17.633  -1.466  4.466  1.00 71.39 ? 59  GLN B O   1 
ATOM   2799 C CB  . GLN B 2 58  ? 18.841  -2.518  7.329  1.00 62.57 ? 59  GLN B CB  1 
ATOM   2800 C CG  . GLN B 2 58  ? 19.256  -1.190  7.897  1.00 62.54 ? 59  GLN B CG  1 
ATOM   2801 C CD  . GLN B 2 58  ? 20.192  -1.356  9.059  1.00 60.19 ? 59  GLN B CD  1 
ATOM   2802 O OE1 . GLN B 2 58  ? 20.873  -2.375  9.172  1.00 64.34 ? 59  GLN B OE1 1 
ATOM   2803 N NE2 . GLN B 2 58  ? 20.231  -0.364  9.939  1.00 57.79 ? 59  GLN B NE2 1 
ATOM   2804 N N   . ALA B 2 59  ? 16.880  -0.220  6.182  1.00 67.33 ? 60  ALA B N   1 
ATOM   2805 C CA  . ALA B 2 59  ? 16.692  0.977   5.374  1.00 68.70 ? 60  ALA B CA  1 
ATOM   2806 C C   . ALA B 2 59  ? 17.930  1.871   5.410  1.00 71.16 ? 60  ALA B C   1 
ATOM   2807 O O   . ALA B 2 59  ? 18.764  1.792   6.316  1.00 67.44 ? 60  ALA B O   1 
ATOM   2808 C CB  . ALA B 2 59  ? 15.471  1.764   5.851  1.00 62.58 ? 60  ALA B CB  1 
ATOM   2809 N N   . ALA B 2 60  ? 18.034  2.738   4.401  1.00 72.77 ? 61  ALA B N   1 
ATOM   2810 C CA  . ALA B 2 60  ? 19.127  3.694   4.301  1.00 67.36 ? 61  ALA B CA  1 
ATOM   2811 C C   . ALA B 2 60  ? 18.610  4.981   3.674  1.00 72.79 ? 61  ALA B C   1 
ATOM   2812 O O   . ALA B 2 60  ? 17.694  4.956   2.846  1.00 73.26 ? 61  ALA B O   1 
ATOM   2813 C CB  . ALA B 2 60  ? 20.294  3.142   3.479  1.00 66.81 ? 61  ALA B CB  1 
ATOM   2814 N N   . HIS B 2 61  ? 19.217  6.104   4.078  1.00 70.92 ? 62  HIS B N   1 
ATOM   2815 C CA  . HIS B 2 61  ? 18.845  7.449   3.635  1.00 70.65 ? 62  HIS B CA  1 
ATOM   2816 C C   . HIS B 2 61  ? 17.338  7.640   3.572  1.00 72.83 ? 62  HIS B C   1 
ATOM   2817 O O   . HIS B 2 61  ? 16.756  7.694   2.484  1.00 74.65 ? 62  HIS B O   1 
ATOM   2818 C CB  . HIS B 2 61  ? 19.461  7.758   2.272  1.00 70.46 ? 62  HIS B CB  1 
ATOM   2819 C CG  . HIS B 2 61  ? 20.936  7.532   2.221  1.00 69.51 ? 62  HIS B CG  1 
ATOM   2820 N ND1 . HIS B 2 61  ? 21.486  6.319   1.872  1.00 70.73 ? 62  HIS B ND1 1 
ATOM   2821 C CD2 . HIS B 2 61  ? 21.976  8.354   2.497  1.00 69.07 ? 62  HIS B CD2 1 
ATOM   2822 C CE1 . HIS B 2 61  ? 22.801  6.406   1.923  1.00 69.89 ? 62  HIS B CE1 1 
ATOM   2823 N NE2 . HIS B 2 61  ? 23.125  7.630   2.299  1.00 69.72 ? 62  HIS B NE2 1 
ATOM   2824 N N   . VAL B 2 62  ? 16.708  7.747   4.724  1.00 72.84 ? 63  VAL B N   1 
ATOM   2825 C CA  . VAL B 2 62  ? 15.257  7.816   4.811  1.00 72.54 ? 63  VAL B CA  1 
ATOM   2826 C C   . VAL B 2 62  ? 14.824  9.274   4.723  1.00 75.09 ? 63  VAL B C   1 
ATOM   2827 O O   . VAL B 2 62  ? 15.430  10.159  5.344  1.00 74.73 ? 63  VAL B O   1 
ATOM   2828 C CB  . VAL B 2 62  ? 14.768  7.147   6.109  1.00 70.47 ? 63  VAL B CB  1 
ATOM   2829 C CG1 . VAL B 2 62  ? 13.257  7.275   6.253  1.00 72.96 ? 63  VAL B CG1 1 
ATOM   2830 C CG2 . VAL B 2 62  ? 15.187  5.681   6.128  1.00 67.86 ? 63  VAL B CG2 1 
ATOM   2831 N N   . LYS B 2 63  ? 13.783  9.528   3.932  1.00 78.80 ? 64  LYS B N   1 
ATOM   2832 C CA  . LYS B 2 63  ? 13.285  10.881  3.711  1.00 73.91 ? 64  LYS B CA  1 
ATOM   2833 C C   . LYS B 2 63  ? 11.851  11.017  4.203  1.00 72.10 ? 64  LYS B C   1 
ATOM   2834 O O   . LYS B 2 63  ? 10.965  10.293  3.749  1.00 75.23 ? 64  LYS B O   1 
ATOM   2835 C CB  . LYS B 2 63  ? 13.372  11.242  2.227  1.00 75.47 ? 64  LYS B CB  1 
ATOM   2836 C CG  . LYS B 2 63  ? 14.762  11.064  1.631  1.00 77.86 ? 64  LYS B CG  1 
ATOM   2837 C CD  . LYS B 2 63  ? 14.931  11.860  0.344  1.00 79.46 ? 64  LYS B CD  1 
ATOM   2838 C CE  . LYS B 2 63  ? 14.298  11.139  -0.840 1.00 80.79 ? 64  LYS B CE  1 
ATOM   2839 N NZ  . LYS B 2 63  ? 13.257  11.967  -1.516 1.00 80.36 ? 64  LYS B NZ  1 
HETATM 2840 C C   . PMS C 3 .   ? 11.893  -9.885  33.324 1.00 37.79 ? 401 PMS A C   1 
HETATM 2841 S S   . PMS C 3 .   ? 10.623  -11.030 32.478 1.00 52.78 ? 401 PMS A S   1 
HETATM 2842 C C1  . PMS C 3 .   ? 12.430  -10.634 34.627 1.00 33.72 ? 401 PMS A C1  1 
HETATM 2843 C C2  . PMS C 3 .   ? 11.513  -11.466 35.370 1.00 37.96 ? 401 PMS A C2  1 
HETATM 2844 C C3  . PMS C 3 .   ? 12.005  -12.138 36.550 1.00 41.47 ? 401 PMS A C3  1 
HETATM 2845 C C4  . PMS C 3 .   ? 13.397  -12.018 36.980 1.00 33.04 ? 401 PMS A C4  1 
HETATM 2846 C C5  . PMS C 3 .   ? 14.291  -11.190 36.231 1.00 33.07 ? 401 PMS A C5  1 
HETATM 2847 C C6  . PMS C 3 .   ? 13.811  -10.502 35.049 1.00 40.44 ? 401 PMS A C6  1 
HETATM 2848 O O2S . PMS C 3 .   ? 9.214   -11.012 33.241 1.00 25.48 ? 401 PMS A O2S 1 
HETATM 2849 O O1S . PMS C 3 .   ? 10.186  -10.312 31.127 1.00 44.61 ? 401 PMS A O1S 1 
HETATM 2850 C C1  . PEG D 4 .   ? -5.005  -5.587  30.106 1.00 30.16 ? 402 PEG A C1  1 
HETATM 2851 O O1  . PEG D 4 .   ? -5.416  -4.478  30.983 1.00 43.55 ? 402 PEG A O1  1 
HETATM 2852 C C2  . PEG D 4 .   ? -4.652  -5.035  28.637 1.00 35.64 ? 402 PEG A C2  1 
HETATM 2853 O O2  . PEG D 4 .   ? -5.393  -3.792  28.399 1.00 47.88 ? 402 PEG A O2  1 
HETATM 2854 C C3  . PEG D 4 .   ? -6.453  -3.961  27.400 1.00 50.62 ? 402 PEG A C3  1 
HETATM 2855 C C4  . PEG D 4 .   ? -7.584  -4.903  28.029 1.00 39.78 ? 402 PEG A C4  1 
HETATM 2856 O O4  . PEG D 4 .   ? -8.723  -4.069  28.436 1.00 46.42 ? 402 PEG A O4  1 
HETATM 2857 C C1  . GOL E 5 .   ? 7.350   -19.949 53.275 1.00 41.54 ? 403 GOL A C1  1 
HETATM 2858 O O1  . GOL E 5 .   ? 8.714   -19.540 53.706 1.00 47.91 ? 403 GOL A O1  1 
HETATM 2859 C C2  . GOL E 5 .   ? 7.069   -21.536 53.204 1.00 46.80 ? 403 GOL A C2  1 
HETATM 2860 O O2  . GOL E 5 .   ? 8.244   -22.323 52.794 1.00 50.04 ? 403 GOL A O2  1 
HETATM 2861 C C3  . GOL E 5 .   ? 5.911   -21.753 52.112 1.00 46.99 ? 403 GOL A C3  1 
HETATM 2862 O O3  . GOL E 5 .   ? 5.559   -23.178 51.931 1.00 48.09 ? 403 GOL A O3  1 
HETATM 2863 O O   . HOH F 6 .   ? 22.946  -3.694  34.094 1.00 33.53 ? 501 HOH A O   1 
HETATM 2864 O O   . HOH F 6 .   ? 12.114  5.807   31.961 1.00 46.02 ? 502 HOH A O   1 
HETATM 2865 O O   . HOH F 6 .   ? 16.405  -15.152 51.431 1.00 36.51 ? 503 HOH A O   1 
HETATM 2866 O O   . HOH F 6 .   ? 5.888   -34.863 47.888 1.00 46.26 ? 504 HOH A O   1 
HETATM 2867 O O   . HOH F 6 .   ? 3.432   -12.090 44.059 1.00 27.02 ? 505 HOH A O   1 
HETATM 2868 O O   . HOH F 6 .   ? 17.793  -16.690 13.574 1.00 45.56 ? 506 HOH A O   1 
HETATM 2869 O O   . HOH F 6 .   ? -2.136  -18.047 50.942 1.00 40.31 ? 507 HOH A O   1 
HETATM 2870 O O   . HOH F 6 .   ? -11.025 -30.995 18.564 1.00 48.02 ? 508 HOH A O   1 
HETATM 2871 O O   . HOH F 6 .   ? 4.368   -31.137 14.771 1.00 52.46 ? 509 HOH A O   1 
HETATM 2872 O O   . HOH F 6 .   ? 8.781   -24.664 51.983 1.00 37.83 ? 510 HOH A O   1 
HETATM 2873 O O   . HOH F 6 .   ? 1.183   -31.948 41.544 1.00 33.02 ? 511 HOH A O   1 
HETATM 2874 O O   . HOH F 6 .   ? 15.090  -31.608 43.105 1.00 26.62 ? 512 HOH A O   1 
HETATM 2875 O O   . HOH F 6 .   ? 5.189   -35.661 38.253 1.00 36.21 ? 513 HOH A O   1 
HETATM 2876 O O   . HOH F 6 .   ? -16.003 -30.548 31.152 1.00 30.76 ? 514 HOH A O   1 
HETATM 2877 O O   . HOH F 6 .   ? 16.176  -18.280 29.095 1.00 16.98 ? 515 HOH A O   1 
HETATM 2878 O O   . HOH F 6 .   ? 6.790   -26.010 39.125 1.00 16.63 ? 516 HOH A O   1 
HETATM 2879 O O   . HOH F 6 .   ? 14.611  -27.996 45.665 1.00 35.45 ? 517 HOH A O   1 
HETATM 2880 O O   . HOH F 6 .   ? 23.994  -21.284 50.157 1.00 28.28 ? 518 HOH A O   1 
HETATM 2881 O O   . HOH F 6 .   ? 3.698   -5.748  50.967 1.00 35.19 ? 519 HOH A O   1 
HETATM 2882 O O   . HOH F 6 .   ? -16.184 -14.989 41.264 1.00 20.33 ? 520 HOH A O   1 
HETATM 2883 O O   . HOH F 6 .   ? -1.007  -33.005 46.361 1.00 40.22 ? 521 HOH A O   1 
HETATM 2884 O O   . HOH F 6 .   ? 6.540   3.347   43.121 1.00 45.36 ? 522 HOH A O   1 
HETATM 2885 O O   . HOH F 6 .   ? 27.901  -19.510 26.629 1.00 31.21 ? 523 HOH A O   1 
HETATM 2886 O O   . HOH F 6 .   ? -5.710  -15.924 48.043 1.00 39.16 ? 524 HOH A O   1 
HETATM 2887 O O   . HOH F 6 .   ? -21.665 -22.823 26.234 1.00 33.06 ? 525 HOH A O   1 
HETATM 2888 O O   . HOH F 6 .   ? -21.543 -23.622 29.687 1.00 25.36 ? 526 HOH A O   1 
HETATM 2889 O O   . HOH F 6 .   ? 20.171  -1.826  32.020 1.00 38.09 ? 527 HOH A O   1 
HETATM 2890 O O   . HOH F 6 .   ? 15.273  -16.212 38.519 1.00 22.12 ? 528 HOH A O   1 
HETATM 2891 O O   . HOH F 6 .   ? -8.751  -36.665 29.392 1.00 41.54 ? 529 HOH A O   1 
HETATM 2892 O O   . HOH F 6 .   ? -17.311 -10.029 35.202 1.00 33.73 ? 530 HOH A O   1 
HETATM 2893 O O   . HOH F 6 .   ? -10.183 -18.913 43.267 1.00 23.11 ? 531 HOH A O   1 
HETATM 2894 O O   . HOH F 6 .   ? -3.441  -30.848 22.186 1.00 35.18 ? 532 HOH A O   1 
HETATM 2895 O O   . HOH F 6 .   ? -1.305  -7.908  34.869 1.00 20.77 ? 533 HOH A O   1 
HETATM 2896 O O   . HOH F 6 .   ? 6.995   -14.924 42.664 1.00 15.02 ? 534 HOH A O   1 
HETATM 2897 O O   . HOH F 6 .   ? -0.368  -23.734 50.378 1.00 32.33 ? 535 HOH A O   1 
HETATM 2898 O O   . HOH F 6 .   ? 8.783   2.480   41.644 1.00 29.11 ? 536 HOH A O   1 
HETATM 2899 O O   . HOH F 6 .   ? 15.696  -22.064 38.551 1.00 17.49 ? 537 HOH A O   1 
HETATM 2900 O O   . HOH F 6 .   ? 21.050  -22.228 42.989 1.00 34.49 ? 538 HOH A O   1 
HETATM 2901 O O   . HOH F 6 .   ? -0.416  -13.845 16.999 1.00 25.27 ? 539 HOH A O   1 
HETATM 2902 O O   . HOH F 6 .   ? 7.964   -12.529 26.440 1.00 25.33 ? 540 HOH A O   1 
HETATM 2903 O O   . HOH F 6 .   ? 0.720   -7.607  48.425 1.00 28.47 ? 541 HOH A O   1 
HETATM 2904 O O   . HOH F 6 .   ? 16.086  -25.575 49.221 1.00 36.07 ? 542 HOH A O   1 
HETATM 2905 O O   . HOH F 6 .   ? -7.229  -9.777  20.806 1.00 27.58 ? 543 HOH A O   1 
HETATM 2906 O O   . HOH F 6 .   ? 5.311   -7.695  20.769 1.00 33.64 ? 544 HOH A O   1 
HETATM 2907 O O   . HOH F 6 .   ? -3.149  -11.915 26.643 1.00 21.45 ? 545 HOH A O   1 
HETATM 2908 O O   . HOH F 6 .   ? -21.622 -26.626 33.859 1.00 38.28 ? 546 HOH A O   1 
HETATM 2909 O O   . HOH F 6 .   ? 8.867   -11.941 54.099 1.00 42.29 ? 547 HOH A O   1 
HETATM 2910 O O   . HOH F 6 .   ? -16.517 -7.987  28.793 1.00 39.47 ? 548 HOH A O   1 
HETATM 2911 O O   . HOH F 6 .   ? 0.642   -29.288 40.902 1.00 19.71 ? 549 HOH A O   1 
HETATM 2912 O O   . HOH F 6 .   ? 20.598  -4.431  26.270 1.00 31.01 ? 550 HOH A O   1 
HETATM 2913 O O   . HOH F 6 .   ? -18.356 -17.301 24.296 1.00 40.30 ? 551 HOH A O   1 
HETATM 2914 O O   . HOH F 6 .   ? 21.950  -8.547  29.084 1.00 21.16 ? 552 HOH A O   1 
HETATM 2915 O O   . HOH F 6 .   ? 20.844  -1.201  14.513 1.00 40.94 ? 553 HOH A O   1 
HETATM 2916 O O   . HOH F 6 .   ? -23.374 -24.017 35.714 1.00 23.40 ? 554 HOH A O   1 
HETATM 2917 O O   . HOH F 6 .   ? 2.641   -9.049  43.207 1.00 18.78 ? 555 HOH A O   1 
HETATM 2918 O O   . HOH F 6 .   ? 18.558  -11.801 26.802 1.00 19.65 ? 556 HOH A O   1 
HETATM 2919 O O   . HOH F 6 .   ? 23.949  -11.831 14.285 1.00 34.41 ? 557 HOH A O   1 
HETATM 2920 O O   . HOH F 6 .   ? 19.459  -2.271  39.605 1.00 31.22 ? 558 HOH A O   1 
HETATM 2921 O O   . HOH F 6 .   ? -0.339  -27.337 15.552 1.00 40.03 ? 559 HOH A O   1 
HETATM 2922 O O   . HOH F 6 .   ? 22.985  -22.366 41.445 1.00 35.24 ? 560 HOH A O   1 
HETATM 2923 O O   . HOH F 6 .   ? -14.144 -8.821  43.355 1.00 37.89 ? 561 HOH A O   1 
HETATM 2924 O O   . HOH F 6 .   ? 4.607   -6.969  23.441 1.00 31.37 ? 562 HOH A O   1 
HETATM 2925 O O   . HOH F 6 .   ? 2.565   -8.023  50.414 1.00 31.85 ? 563 HOH A O   1 
HETATM 2926 O O   . HOH F 6 .   ? 16.537  -16.144 43.357 1.00 27.00 ? 564 HOH A O   1 
HETATM 2927 O O   . HOH F 6 .   ? 26.926  -24.222 46.692 1.00 56.93 ? 565 HOH A O   1 
HETATM 2928 O O   . HOH F 6 .   ? 4.966   -8.748  35.056 1.00 17.19 ? 566 HOH A O   1 
HETATM 2929 O O   . HOH F 6 .   ? -7.151  -20.995 15.523 1.00 32.98 ? 567 HOH A O   1 
HETATM 2930 O O   . HOH F 6 .   ? -1.458  -12.797 31.269 1.00 17.57 ? 568 HOH A O   1 
HETATM 2931 O O   . HOH F 6 .   ? 13.228  -23.537 50.746 1.00 33.17 ? 569 HOH A O   1 
HETATM 2932 O O   . HOH F 6 .   ? 1.897   -25.571 14.419 1.00 48.66 ? 570 HOH A O   1 
HETATM 2933 O O   . HOH F 6 .   ? 7.474   -31.478 26.659 1.00 28.50 ? 571 HOH A O   1 
HETATM 2934 O O   . HOH F 6 .   ? 27.541  -9.648  30.220 1.00 29.24 ? 572 HOH A O   1 
HETATM 2935 O O   . HOH F 6 .   ? 8.956   -24.232 14.340 1.00 36.69 ? 573 HOH A O   1 
HETATM 2936 O O   . HOH F 6 .   ? 25.964  -13.594 17.647 1.00 42.08 ? 574 HOH A O   1 
HETATM 2937 O O   . HOH F 6 .   ? -6.721  -6.379  40.125 1.00 26.39 ? 575 HOH A O   1 
HETATM 2938 O O   . HOH F 6 .   ? 3.225   -8.603  40.694 1.00 23.15 ? 576 HOH A O   1 
HETATM 2939 O O   . HOH F 6 .   ? 5.329   -31.909 24.737 1.00 28.69 ? 577 HOH A O   1 
HETATM 2940 O O   . HOH F 6 .   ? -13.208 -24.329 18.265 1.00 42.44 ? 578 HOH A O   1 
HETATM 2941 O O   . HOH F 6 .   ? -2.005  -30.026 40.460 1.00 23.47 ? 579 HOH A O   1 
HETATM 2942 O O   . HOH F 6 .   ? -11.601 -35.734 32.461 1.00 41.76 ? 580 HOH A O   1 
HETATM 2943 O O   . HOH F 6 .   ? -16.764 -8.919  32.700 1.00 31.48 ? 581 HOH A O   1 
HETATM 2944 O O   . HOH F 6 .   ? 12.930  -15.905 41.048 1.00 22.28 ? 582 HOH A O   1 
HETATM 2945 O O   . HOH F 6 .   ? 19.338  -24.213 28.720 1.00 28.49 ? 583 HOH A O   1 
HETATM 2946 O O   . HOH F 6 .   ? 6.881   -3.766  51.400 1.00 35.90 ? 584 HOH A O   1 
HETATM 2947 O O   . HOH F 6 .   ? 23.324  -3.678  28.603 1.00 31.69 ? 585 HOH A O   1 
HETATM 2948 O O   . HOH F 6 .   ? 14.877  -19.282 31.925 1.00 18.18 ? 586 HOH A O   1 
HETATM 2949 O O   . HOH F 6 .   ? -5.511  -30.950 34.291 1.00 19.97 ? 587 HOH A O   1 
HETATM 2950 O O   . HOH F 6 .   ? -8.161  -29.222 36.530 1.00 22.92 ? 588 HOH A O   1 
HETATM 2951 O O   . HOH F 6 .   ? -13.700 -19.970 42.628 1.00 33.37 ? 589 HOH A O   1 
HETATM 2952 O O   . HOH F 6 .   ? 12.301  6.704   42.361 1.00 47.32 ? 590 HOH A O   1 
HETATM 2953 O O   . HOH F 6 .   ? -9.425  -5.416  36.898 1.00 41.44 ? 591 HOH A O   1 
HETATM 2954 O O   . HOH F 6 .   ? 10.309  -9.239  53.822 1.00 43.46 ? 592 HOH A O   1 
HETATM 2955 O O   . HOH F 6 .   ? -1.869  -4.029  39.401 1.00 24.65 ? 593 HOH A O   1 
HETATM 2956 O O   . HOH F 6 .   ? 7.369   -36.936 40.646 1.00 34.48 ? 594 HOH A O   1 
HETATM 2957 O O   . HOH F 6 .   ? 18.450  -27.587 23.655 1.00 28.59 ? 595 HOH A O   1 
HETATM 2958 O O   . HOH F 6 .   ? 2.815   -2.874  30.191 1.00 35.85 ? 596 HOH A O   1 
HETATM 2959 O O   . HOH F 6 .   ? 0.905   -6.198  21.605 1.00 35.03 ? 597 HOH A O   1 
HETATM 2960 O O   . HOH F 6 .   ? -1.828  -5.567  47.585 1.00 35.65 ? 598 HOH A O   1 
HETATM 2961 O O   . HOH F 6 .   ? -2.652  -31.322 43.327 1.00 37.36 ? 599 HOH A O   1 
HETATM 2962 O O   . HOH F 6 .   ? 17.448  -1.285  41.869 1.00 43.17 ? 600 HOH A O   1 
HETATM 2963 O O   . HOH F 6 .   ? 7.547   -32.533 28.999 1.00 31.04 ? 601 HOH A O   1 
HETATM 2964 O O   . HOH F 6 .   ? 11.995  3.377   42.703 1.00 49.01 ? 602 HOH A O   1 
HETATM 2965 O O   . HOH F 6 .   ? 18.687  -33.686 37.114 1.00 34.62 ? 603 HOH A O   1 
HETATM 2966 O O   . HOH F 6 .   ? -18.840 -9.501  37.014 1.00 44.54 ? 604 HOH A O   1 
HETATM 2967 O O   . HOH F 6 .   ? -14.564 -9.457  24.656 1.00 36.26 ? 605 HOH A O   1 
HETATM 2968 O O   . HOH F 6 .   ? 27.413  -24.012 48.867 1.00 41.42 ? 606 HOH A O   1 
HETATM 2969 O O   . HOH F 6 .   ? -16.846 -27.862 36.401 1.00 27.62 ? 607 HOH A O   1 
HETATM 2970 O O   . HOH F 6 .   ? -5.216  -6.888  38.008 1.00 26.84 ? 608 HOH A O   1 
HETATM 2971 O O   . HOH F 6 .   ? -18.603 -25.767 35.685 1.00 29.18 ? 609 HOH A O   1 
HETATM 2972 O O   . HOH F 6 .   ? 21.266  -17.417 13.737 1.00 45.35 ? 610 HOH A O   1 
HETATM 2973 O O   . HOH F 6 .   ? -7.137  -24.193 47.640 1.00 36.10 ? 611 HOH A O   1 
HETATM 2974 O O   . HOH F 6 .   ? -2.246  -8.579  13.093 1.00 37.11 ? 612 HOH A O   1 
HETATM 2975 O O   . HOH F 6 .   ? -14.227 -22.096 26.373 1.00 36.41 ? 613 HOH A O   1 
HETATM 2976 O O   . HOH F 6 .   ? -9.236  -13.711 15.777 1.00 32.51 ? 614 HOH A O   1 
HETATM 2977 O O   . HOH F 6 .   ? 14.252  3.067   42.496 1.00 45.03 ? 615 HOH A O   1 
HETATM 2978 O O   . HOH F 6 .   ? 12.935  -31.482 45.527 1.00 30.23 ? 616 HOH A O   1 
HETATM 2979 O O   . HOH F 6 .   ? 26.567  -11.782 20.771 1.00 45.50 ? 617 HOH A O   1 
HETATM 2980 O O   . HOH F 6 .   ? -9.646  -4.800  41.609 1.00 31.82 ? 618 HOH A O   1 
HETATM 2981 O O   . HOH F 6 .   ? 6.175   -36.412 35.873 1.00 31.64 ? 619 HOH A O   1 
HETATM 2982 O O   . HOH F 6 .   ? 15.229  -32.217 27.674 1.00 28.49 ? 620 HOH A O   1 
HETATM 2983 O O   . HOH F 6 .   ? -3.520  -31.277 50.508 0.50 36.85 ? 621 HOH A O   1 
HETATM 2984 O O   . HOH F 6 .   ? -6.966  -6.664  35.904 1.00 22.94 ? 622 HOH A O   1 
HETATM 2985 O O   . HOH F 6 .   ? 1.856   -4.155  48.567 1.00 26.18 ? 623 HOH A O   1 
HETATM 2986 O O   . HOH F 6 .   ? 14.119  0.558   43.166 1.00 42.98 ? 624 HOH A O   1 
HETATM 2987 O O   . HOH F 6 .   ? -17.635 -13.366 20.141 1.00 53.15 ? 625 HOH A O   1 
HETATM 2988 O O   . HOH F 6 .   ? 24.163  -10.016 36.985 1.00 42.32 ? 626 HOH A O   1 
HETATM 2989 O O   . HOH F 6 .   ? 12.610  -35.947 32.856 1.00 30.97 ? 627 HOH A O   1 
HETATM 2990 O O   . HOH F 6 .   ? -8.127  -14.720 48.117 1.00 37.76 ? 628 HOH A O   1 
HETATM 2991 O O   . HOH F 6 .   ? 3.416   -35.807 30.004 1.00 49.95 ? 629 HOH A O   1 
HETATM 2992 O O   . HOH F 6 .   ? 1.951   3.538   36.964 1.00 40.12 ? 630 HOH A O   1 
HETATM 2993 O O   . HOH F 6 .   ? -20.164 -11.571 40.103 1.00 41.66 ? 631 HOH A O   1 
HETATM 2994 O O   . HOH F 6 .   ? 21.956  2.025   38.439 1.00 45.30 ? 632 HOH A O   1 
HETATM 2995 O O   . HOH F 6 .   ? -11.423 -13.838 16.503 1.00 42.36 ? 633 HOH A O   1 
HETATM 2996 O O   . HOH F 6 .   ? -14.588 -8.590  46.455 1.00 37.07 ? 634 HOH A O   1 
HETATM 2997 O O   . HOH F 6 .   ? -10.192 -11.785 16.879 1.00 43.77 ? 635 HOH A O   1 
HETATM 2998 O O   . HOH F 6 .   ? -0.299  -1.723  39.156 1.00 30.11 ? 636 HOH A O   1 
HETATM 2999 O O   . HOH F 6 .   ? 2.602   -7.087  20.102 1.00 43.20 ? 637 HOH A O   1 
HETATM 3000 O O   . HOH F 6 .   ? 23.493  -13.356 42.777 1.00 42.72 ? 638 HOH A O   1 
HETATM 3001 O O   . HOH F 6 .   ? 10.620  -8.591  9.302  1.00 50.91 ? 639 HOH A O   1 
HETATM 3002 O O   . HOH F 6 .   ? -18.742 -21.861 27.088 1.00 40.60 ? 640 HOH A O   1 
HETATM 3003 O O   . HOH F 6 .   ? 2.006   -1.924  33.738 1.00 38.97 ? 641 HOH A O   1 
HETATM 3004 O O   . HOH F 6 .   ? -6.833  -22.008 48.698 1.00 31.52 ? 642 HOH A O   1 
HETATM 3005 O O   . HOH F 6 .   ? -9.027  -34.093 36.386 1.00 42.81 ? 643 HOH A O   1 
HETATM 3006 O O   . HOH F 6 .   ? -4.278  -33.256 35.150 1.00 24.04 ? 644 HOH A O   1 
HETATM 3007 O O   . HOH F 6 .   ? 25.601  -8.498  20.450 1.00 42.25 ? 645 HOH A O   1 
HETATM 3008 O O   . HOH F 6 .   ? 21.141  -9.767  38.378 1.00 45.74 ? 646 HOH A O   1 
HETATM 3009 O O   . HOH F 6 .   ? 2.504   5.093   35.282 1.00 37.91 ? 647 HOH A O   1 
HETATM 3010 O O   . HOH F 6 .   ? -6.787  -29.852 15.713 1.00 48.62 ? 648 HOH A O   1 
HETATM 3011 O O   . HOH F 6 .   ? 4.747   -33.937 28.844 1.00 41.72 ? 649 HOH A O   1 
HETATM 3012 O O   . HOH F 6 .   ? 4.655   -4.670  23.779 1.00 41.59 ? 650 HOH A O   1 
HETATM 3013 O O   . HOH F 6 .   ? 19.810  -21.556 49.295 1.00 42.49 ? 651 HOH A O   1 
HETATM 3014 O O   . HOH F 6 .   ? -0.131  -0.653  36.591 1.00 40.14 ? 652 HOH A O   1 
HETATM 3015 O O   . HOH F 6 .   ? -16.762 -15.281 43.781 1.00 38.37 ? 653 HOH A O   1 
HETATM 3016 O O   . HOH F 6 .   ? -9.721  -29.764 38.800 1.00 37.35 ? 654 HOH A O   1 
HETATM 3017 O O   . HOH F 6 .   ? 15.400  -33.786 45.041 1.00 39.86 ? 655 HOH A O   1 
HETATM 3018 O O   . HOH F 6 .   ? -12.902 -3.257  37.227 1.00 46.46 ? 656 HOH A O   1 
HETATM 3019 O O   . HOH F 6 .   ? 28.058  -14.675 47.043 1.00 39.51 ? 657 HOH A O   1 
HETATM 3020 O O   . HOH F 6 .   ? 4.632   9.332   33.662 1.00 38.94 ? 658 HOH A O   1 
HETATM 3021 O O   . HOH F 6 .   ? 4.545   -34.219 26.010 1.00 38.39 ? 659 HOH A O   1 
HETATM 3022 O O   . HOH F 6 .   ? 21.162  -22.467 50.892 1.00 35.88 ? 660 HOH A O   1 
HETATM 3023 O O   . HOH F 6 .   ? -16.186 -31.197 33.575 1.00 40.84 ? 661 HOH A O   1 
HETATM 3024 O O   . HOH F 6 .   ? 17.395  -13.314 42.703 1.00 38.78 ? 662 HOH A O   1 
HETATM 3025 O O   . HOH F 6 .   ? -11.157 -27.975 40.635 1.00 34.59 ? 663 HOH A O   1 
HETATM 3026 O O   . HOH F 6 .   ? 8.067   -27.417 52.274 1.00 43.08 ? 664 HOH A O   1 
HETATM 3027 O O   . HOH F 6 .   ? 15.352  -14.904 41.013 1.00 26.39 ? 665 HOH A O   1 
HETATM 3028 O O   . HOH F 6 .   ? 21.950  -24.146 28.003 1.00 35.39 ? 666 HOH A O   1 
HETATM 3029 O O   . HOH F 6 .   ? 1.137   -34.454 47.203 1.00 53.08 ? 667 HOH A O   1 
HETATM 3030 O O   . HOH F 6 .   ? -10.901 -35.704 35.384 1.00 40.96 ? 668 HOH A O   1 
HETATM 3031 O O   . HOH F 6 .   ? 12.596  -37.492 30.355 1.00 57.05 ? 669 HOH A O   1 
HETATM 3032 O O   . HOH F 6 .   ? -6.489  -34.928 36.216 1.00 36.90 ? 670 HOH A O   1 
HETATM 3033 O O   . HOH F 6 .   ? -9.976  -32.460 38.460 1.00 40.49 ? 671 HOH A O   1 
HETATM 3034 O O   . HOH F 6 .   ? -11.161 -17.261 45.224 1.00 38.95 ? 672 HOH A O   1 
HETATM 3035 O O   . HOH F 6 .   ? 28.017  -12.955 44.612 1.00 50.02 ? 673 HOH A O   1 
HETATM 3036 O O   . HOH F 6 .   ? -0.605  -32.973 43.367 1.00 37.36 ? 674 HOH A O   1 
HETATM 3037 O O   . HOH F 6 .   ? 22.200  -1.577  39.207 1.00 48.55 ? 675 HOH A O   1 
HETATM 3038 O O   . HOH F 6 .   ? 19.638  -26.908 28.176 1.00 32.07 ? 676 HOH A O   1 
# 
