data_9JML
# 
_entry.id   9JML 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JML         pdb_00009jml 10.2210/pdb9jml/pdb 
WWPDB D_1300051305 ?            ?                   
# 
_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       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9JML 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              liyaoyao@sdu.edu.cn 
_pdbx_contact_author.name_first         Yaoyao 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8762-9615 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.'  1 0000-0002-8762-9615 
'Zhu, D.' 2 0000-0002-2949-9410 
'Xie, X.' 3 0000-0002-5118-6111 
'Li, F.'  4 0009-0009-0724-7915 
'Lu, M.'  5 0009-0000-1359-6323 
# 
_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            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                19253 
_citation.page_last                 19261 
_citation.title                     
;Structural Basis for Medium-Chain Dehydrogenase/Reductase-Catalyzed Reductive Cyclization in Polycyclic Tetramate Macrolactam Biosynthesis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.5c04971 
_citation.pdbx_database_id_PubMed   40406958 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xie, X.'  1  0000-0002-5118-6111 
primary 'Li, F.'   2  ?                   
primary 'Mu, Y.'   3  ?                   
primary 'Lu, M.'   4  ?                   
primary 'Luo, J.'  5  ?                   
primary 'Wang, H.' 6  0000-0002-1779-0286 
primary 'Shen, Y.' 7  0000-0002-3881-0135 
primary 'Du, L.'   8  0000-0003-4048-1008 
primary 'Zhu, D.'  9  0000-0002-2949-9410 
primary 'Li, Y.'   10 0000-0002-8762-9615 
# 
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 'NADP-dependent oxidoreductase' 38943.332 2   ? ? ? ? 
2 non-polymer syn 
;(1Z,3Z,5Z,7S,8R,9S,10S,11R,13R,15R,16Z,18Z,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
494.622   2   ? ? ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
4 water       nat water 18.015    598 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Oxidoreductase,zinc-binding dehydrogenase family protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;LGSMKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGP
NAPFRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVR
PGDTVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDS
IGGSVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELV
AHETVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LGSMKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGP
NAPFRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVR
PGDTVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDS
IGGSVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELV
AHETVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(1Z,3Z,5Z,7S,8R,9S,10S,11R,13R,15R,16Z,18Z,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
A1EDK 
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP   
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   GLY n 
1 3   SER n 
1 4   MET n 
1 5   LYS n 
1 6   THR n 
1 7   GLU n 
1 8   ARG n 
1 9   TRP n 
1 10  VAL n 
1 11  VAL n 
1 12  ARG n 
1 13  GLU n 
1 14  HIS n 
1 15  VAL n 
1 16  GLU n 
1 17  GLY n 
1 18  VAL n 
1 19  PRO n 
1 20  ASP n 
1 21  ALA n 
1 22  ALA n 
1 23  ARG n 
1 24  ILE n 
1 25  TYR n 
1 26  GLU n 
1 27  LYS n 
1 28  VAL n 
1 29  GLU n 
1 30  THR n 
1 31  GLU n 
1 32  LEU n 
1 33  ASN n 
1 34  THR n 
1 35  ARG n 
1 36  LEU n 
1 37  GLY n 
1 38  GLU n 
1 39  GLU n 
1 40  GLN n 
1 41  MET n 
1 42  LEU n 
1 43  LEU n 
1 44  LYS n 
1 45  THR n 
1 46  LEU n 
1 47  TYR n 
1 48  VAL n 
1 49  SER n 
1 50  VAL n 
1 51  ASP n 
1 52  PRO n 
1 53  TYR n 
1 54  LEU n 
1 55  GLN n 
1 56  GLY n 
1 57  ILE n 
1 58  CYS n 
1 59  LEU n 
1 60  ASP n 
1 61  THR n 
1 62  PRO n 
1 63  ILE n 
1 64  GLY n 
1 65  ASP n 
1 66  HIS n 
1 67  MET n 
1 68  GLY n 
1 69  ALA n 
1 70  ASP n 
1 71  SER n 
1 72  ILE n 
1 73  MET n 
1 74  GLN n 
1 75  VAL n 
1 76  LEU n 
1 77  ASP n 
1 78  ALA n 
1 79  GLY n 
1 80  PRO n 
1 81  ASN n 
1 82  ALA n 
1 83  PRO n 
1 84  PHE n 
1 85  ARG n 
1 86  PRO n 
1 87  GLY n 
1 88  ASP n 
1 89  LEU n 
1 90  VAL n 
1 91  GLN n 
1 92  GLY n 
1 93  PHE n 
1 94  GLY n 
1 95  GLY n 
1 96  TRP n 
1 97  ARG n 
1 98  THR n 
1 99  HIS n 
1 100 LEU n 
1 101 VAL n 
1 102 SER n 
1 103 ASP n 
1 104 GLY n 
1 105 LYS n 
1 106 PRO n 
1 107 LYS n 
1 108 LEU n 
1 109 TRP n 
1 110 GLN n 
1 111 THR n 
1 112 GLY n 
1 113 THR n 
1 114 PHE n 
1 115 PRO n 
1 116 MET n 
1 117 VAL n 
1 118 PHE n 
1 119 PRO n 
1 120 ALA n 
1 121 TYR n 
1 122 ARG n 
1 123 LYS n 
1 124 LEU n 
1 125 ASP n 
1 126 LEU n 
1 127 ARG n 
1 128 HIS n 
1 129 TYR n 
1 130 ASP n 
1 131 ASP n 
1 132 ALA n 
1 133 LEU n 
1 134 PRO n 
1 135 LEU n 
1 136 SER n 
1 137 THR n 
1 138 ALA n 
1 139 LEU n 
1 140 GLY n 
1 141 VAL n 
1 142 MET n 
1 143 GLY n 
1 144 GLY n 
1 145 PRO n 
1 146 GLY n 
1 147 MET n 
1 148 THR n 
1 149 ALA n 
1 150 TRP n 
1 151 GLY n 
1 152 THR n 
1 153 MET n 
1 154 THR n 
1 155 LYS n 
1 156 PHE n 
1 157 MET n 
1 158 GLN n 
1 159 VAL n 
1 160 ARG n 
1 161 PRO n 
1 162 GLY n 
1 163 ASP n 
1 164 THR n 
1 165 VAL n 
1 166 VAL n 
1 167 VAL n 
1 168 SER n 
1 169 GLY n 
1 170 ALA n 
1 171 SER n 
1 172 GLY n 
1 173 MET n 
1 174 ILE n 
1 175 GLY n 
1 176 THR n 
1 177 LEU n 
1 178 VAL n 
1 179 GLY n 
1 180 GLN n 
1 181 MET n 
1 182 ALA n 
1 183 LYS n 
1 184 ARG n 
1 185 ALA n 
1 186 GLY n 
1 187 ALA n 
1 188 ARG n 
1 189 VAL n 
1 190 VAL n 
1 191 GLY n 
1 192 THR n 
1 193 ALA n 
1 194 GLY n 
1 195 SER n 
1 196 ALA n 
1 197 GLY n 
1 198 LYS n 
1 199 ALA n 
1 200 ARG n 
1 201 TYR n 
1 202 LEU n 
1 203 SER n 
1 204 GLN n 
1 205 LEU n 
1 206 GLY n 
1 207 PHE n 
1 208 ASP n 
1 209 ALA n 
1 210 VAL n 
1 211 ILE n 
1 212 ASP n 
1 213 TYR n 
1 214 LYS n 
1 215 LEU n 
1 216 ALA n 
1 217 ASP n 
1 218 ASP n 
1 219 ALA n 
1 220 ASP n 
1 221 LYS n 
1 222 MET n 
1 223 ARG n 
1 224 GLU n 
1 225 ALA n 
1 226 LEU n 
1 227 ARG n 
1 228 GLU n 
1 229 ALA n 
1 230 ALA n 
1 231 PRO n 
1 232 ASP n 
1 233 GLY n 
1 234 VAL n 
1 235 ASP n 
1 236 LYS n 
1 237 TYR n 
1 238 PHE n 
1 239 ASP n 
1 240 SER n 
1 241 ILE n 
1 242 GLY n 
1 243 GLY n 
1 244 SER n 
1 245 VAL n 
1 246 THR n 
1 247 ASP n 
1 248 ALA n 
1 249 VAL n 
1 250 PHE n 
1 251 SER n 
1 252 MET n 
1 253 LEU n 
1 254 ASN n 
1 255 VAL n 
1 256 GLY n 
1 257 SER n 
1 258 GLN n 
1 259 VAL n 
1 260 ALA n 
1 261 VAL n 
1 262 CYS n 
1 263 TRP n 
1 264 GLN n 
1 265 TRP n 
1 266 ALA n 
1 267 THR n 
1 268 GLN n 
1 269 VAL n 
1 270 GLN n 
1 271 ARG n 
1 272 ASP n 
1 273 TYR n 
1 274 HIS n 
1 275 GLY n 
1 276 PRO n 
1 277 ARG n 
1 278 LEU n 
1 279 LEU n 
1 280 PRO n 
1 281 TYR n 
1 282 ILE n 
1 283 MET n 
1 284 PHE n 
1 285 PRO n 
1 286 ARG n 
1 287 ALA n 
1 288 THR n 
1 289 ILE n 
1 290 ARG n 
1 291 GLY n 
1 292 ILE n 
1 293 PHE n 
1 294 SER n 
1 295 LEU n 
1 296 GLU n 
1 297 TRP n 
1 298 PHE n 
1 299 THR n 
1 300 GLU n 
1 301 GLN n 
1 302 ASN n 
1 303 TRP n 
1 304 SER n 
1 305 ALA n 
1 306 LEU n 
1 307 HIS n 
1 308 GLU n 
1 309 GLU n 
1 310 LEU n 
1 311 GLY n 
1 312 GLY n 
1 313 LEU n 
1 314 VAL n 
1 315 ARG n 
1 316 ARG n 
1 317 GLN n 
1 318 GLU n 
1 319 LEU n 
1 320 VAL n 
1 321 ALA n 
1 322 HIS n 
1 323 GLU n 
1 324 THR n 
1 325 VAL n 
1 326 GLN n 
1 327 ASP n 
1 328 GLY n 
1 329 PHE n 
1 330 GLU n 
1 331 HIS n 
1 332 ILE n 
1 333 PRO n 
1 334 ALA n 
1 335 ALA n 
1 336 TYR n 
1 337 GLN n 
1 338 THR n 
1 339 LEU n 
1 340 PHE n 
1 341 SER n 
1 342 ALA n 
1 343 SER n 
1 344 GLU n 
1 345 SER n 
1 346 ASN n 
1 347 ARG n 
1 348 GLY n 
1 349 LYS n 
1 350 VAL n 
1 351 LEU n 
1 352 VAL n 
1 353 ARG n 
1 354 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   354 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GLE_3219 
_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      'Lysobacter enzymogenes' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     69 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EDK non-polymer         . 
;(1Z,3Z,5Z,7S,8R,9S,10S,11R,13R,15R,16Z,18Z,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
?                                            'C29 H38 N2 O5'     494.622 
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  
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 
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PHE   'L-peptide linking' y PHENYLALANINE ?                                            'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                                            'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                                            'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                                            'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                                            'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                                            'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                                            'C5 H11 N O2'       117.146 
# 
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   LEU 1   -2  -2  LEU LEU A . n 
A 1 2   GLY 2   -1  -1  GLY GLY A . n 
A 1 3   SER 3   0   0   SER SER A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   LYS 5   2   2   LYS LYS A . n 
A 1 6   THR 6   3   3   THR THR A . n 
A 1 7   GLU 7   4   4   GLU GLU A . n 
A 1 8   ARG 8   5   5   ARG ARG A . n 
A 1 9   TRP 9   6   6   TRP TRP A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  ARG 12  9   9   ARG ARG A . n 
A 1 13  GLU 13  10  10  GLU GLU A . n 
A 1 14  HIS 14  11  11  HIS HIS A . n 
A 1 15  VAL 15  12  12  VAL VAL A . n 
A 1 16  GLU 16  13  13  GLU GLU A . n 
A 1 17  GLY 17  14  14  GLY GLY A . n 
A 1 18  VAL 18  15  15  VAL VAL A . n 
A 1 19  PRO 19  16  16  PRO PRO A . n 
A 1 20  ASP 20  17  17  ASP ASP A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  ALA 22  19  19  ALA ALA A . n 
A 1 23  ARG 23  20  20  ARG ARG A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  TYR 25  22  22  TYR TYR A . n 
A 1 26  GLU 26  23  23  GLU GLU A . n 
A 1 27  LYS 27  24  24  LYS LYS A . n 
A 1 28  VAL 28  25  25  VAL VAL A . n 
A 1 29  GLU 29  26  26  GLU GLU A . n 
A 1 30  THR 30  27  27  THR THR A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  LEU 32  29  29  LEU LEU A . n 
A 1 33  ASN 33  30  30  ASN ASN A . n 
A 1 34  THR 34  31  31  THR THR A . n 
A 1 35  ARG 35  32  32  ARG ARG A . n 
A 1 36  LEU 36  33  33  LEU LEU A . n 
A 1 37  GLY 37  34  34  GLY GLY A . n 
A 1 38  GLU 38  35  35  GLU GLU A . n 
A 1 39  GLU 39  36  36  GLU GLU A . n 
A 1 40  GLN 40  37  37  GLN GLN A . n 
A 1 41  MET 41  38  38  MET MET A . n 
A 1 42  LEU 42  39  39  LEU LEU A . n 
A 1 43  LEU 43  40  40  LEU LEU A . n 
A 1 44  LYS 44  41  41  LYS LYS A . n 
A 1 45  THR 45  42  42  THR THR A . n 
A 1 46  LEU 46  43  43  LEU LEU A . n 
A 1 47  TYR 47  44  44  TYR TYR A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  SER 49  46  46  SER SER A . n 
A 1 50  VAL 50  47  47  VAL VAL A . n 
A 1 51  ASP 51  48  48  ASP ASP A . n 
A 1 52  PRO 52  49  49  PRO PRO A . n 
A 1 53  TYR 53  50  50  TYR TYR A . n 
A 1 54  LEU 54  51  51  LEU LEU A . n 
A 1 55  GLN 55  52  52  GLN GLN A . n 
A 1 56  GLY 56  53  53  GLY GLY A . n 
A 1 57  ILE 57  54  54  ILE ILE A . n 
A 1 58  CYS 58  55  55  CYS CYS A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  PRO 62  59  59  PRO PRO A . n 
A 1 63  ILE 63  60  60  ILE ILE A . n 
A 1 64  GLY 64  61  61  GLY GLY A . n 
A 1 65  ASP 65  62  62  ASP ASP A . n 
A 1 66  HIS 66  63  63  HIS HIS A . n 
A 1 67  MET 67  64  64  MET MET A . n 
A 1 68  GLY 68  65  65  GLY GLY A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  ASP 70  67  67  ASP ASP A . n 
A 1 71  SER 71  68  68  SER SER A . n 
A 1 72  ILE 72  69  69  ILE ILE A . n 
A 1 73  MET 73  70  70  MET MET A . n 
A 1 74  GLN 74  71  71  GLN GLN A . n 
A 1 75  VAL 75  72  72  VAL VAL A . n 
A 1 76  LEU 76  73  73  LEU LEU A . n 
A 1 77  ASP 77  74  74  ASP ASP A . n 
A 1 78  ALA 78  75  75  ALA ALA A . n 
A 1 79  GLY 79  76  76  GLY GLY A . n 
A 1 80  PRO 80  77  77  PRO PRO A . n 
A 1 81  ASN 81  78  78  ASN ASN A . n 
A 1 82  ALA 82  79  79  ALA ALA A . n 
A 1 83  PRO 83  80  80  PRO PRO A . n 
A 1 84  PHE 84  81  81  PHE PHE A . n 
A 1 85  ARG 85  82  82  ARG ARG A . n 
A 1 86  PRO 86  83  83  PRO PRO A . n 
A 1 87  GLY 87  84  84  GLY GLY A . n 
A 1 88  ASP 88  85  85  ASP ASP A . n 
A 1 89  LEU 89  86  86  LEU LEU A . n 
A 1 90  VAL 90  87  87  VAL VAL A . n 
A 1 91  GLN 91  88  88  GLN GLN A . n 
A 1 92  GLY 92  89  89  GLY GLY A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLY 94  91  91  GLY GLY A . n 
A 1 95  GLY 95  92  92  GLY GLY A . n 
A 1 96  TRP 96  93  93  TRP TRP A . n 
A 1 97  ARG 97  94  94  ARG ARG A . n 
A 1 98  THR 98  95  95  THR THR A . n 
A 1 99  HIS 99  96  96  HIS HIS A . n 
A 1 100 LEU 100 97  97  LEU LEU A . n 
A 1 101 VAL 101 98  98  VAL VAL A . n 
A 1 102 SER 102 99  99  SER SER A . n 
A 1 103 ASP 103 100 100 ASP ASP A . n 
A 1 104 GLY 104 101 101 GLY GLY A . n 
A 1 105 LYS 105 102 102 LYS LYS A . n 
A 1 106 PRO 106 103 103 PRO PRO A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 LEU 108 105 105 LEU LEU A . n 
A 1 109 TRP 109 106 106 TRP TRP A . n 
A 1 110 GLN 110 107 107 GLN GLN A . n 
A 1 111 THR 111 108 108 THR THR A . n 
A 1 112 GLY 112 109 109 GLY GLY A . n 
A 1 113 THR 113 110 110 THR THR A . n 
A 1 114 PHE 114 111 111 PHE PHE A . n 
A 1 115 PRO 115 112 112 PRO PRO A . n 
A 1 116 MET 116 113 113 MET MET A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 PHE 118 115 115 PHE PHE A . n 
A 1 119 PRO 119 116 116 PRO PRO A . n 
A 1 120 ALA 120 117 117 ALA ALA A . n 
A 1 121 TYR 121 118 118 TYR TYR A . n 
A 1 122 ARG 122 119 119 ARG ARG A . n 
A 1 123 LYS 123 120 120 LYS LYS A . n 
A 1 124 LEU 124 121 121 LEU LEU A . n 
A 1 125 ASP 125 122 122 ASP ASP A . n 
A 1 126 LEU 126 123 123 LEU LEU A . n 
A 1 127 ARG 127 124 124 ARG ARG A . n 
A 1 128 HIS 128 125 125 HIS HIS A . n 
A 1 129 TYR 129 126 126 TYR TYR A . n 
A 1 130 ASP 130 127 127 ASP ASP A . n 
A 1 131 ASP 131 128 128 ASP ASP A . n 
A 1 132 ALA 132 129 129 ALA ALA A . n 
A 1 133 LEU 133 130 130 LEU LEU A . n 
A 1 134 PRO 134 131 131 PRO PRO A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 SER 136 133 133 SER SER A . n 
A 1 137 THR 137 134 134 THR THR A . n 
A 1 138 ALA 138 135 135 ALA ALA A . n 
A 1 139 LEU 139 136 136 LEU LEU A . n 
A 1 140 GLY 140 137 137 GLY GLY A . n 
A 1 141 VAL 141 138 138 VAL VAL A . n 
A 1 142 MET 142 139 139 MET MET A . n 
A 1 143 GLY 143 140 140 GLY GLY A . n 
A 1 144 GLY 144 141 141 GLY GLY A . n 
A 1 145 PRO 145 142 142 PRO PRO A . n 
A 1 146 GLY 146 143 143 GLY GLY A . n 
A 1 147 MET 147 144 144 MET MET A . n 
A 1 148 THR 148 145 145 THR THR A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 TRP 150 147 147 TRP TRP A . n 
A 1 151 GLY 151 148 148 GLY GLY A . n 
A 1 152 THR 152 149 149 THR THR A . n 
A 1 153 MET 153 150 150 MET MET A . n 
A 1 154 THR 154 151 151 THR THR A . n 
A 1 155 LYS 155 152 152 LYS LYS A . n 
A 1 156 PHE 156 153 153 PHE PHE A . n 
A 1 157 MET 157 154 154 MET MET A . n 
A 1 158 GLN 158 155 155 GLN GLN A . n 
A 1 159 VAL 159 156 156 VAL VAL A . n 
A 1 160 ARG 160 157 157 ARG ARG A . n 
A 1 161 PRO 161 158 158 PRO PRO A . n 
A 1 162 GLY 162 159 159 GLY GLY A . n 
A 1 163 ASP 163 160 160 ASP ASP A . n 
A 1 164 THR 164 161 161 THR THR A . n 
A 1 165 VAL 165 162 162 VAL VAL A . n 
A 1 166 VAL 166 163 163 VAL VAL A . n 
A 1 167 VAL 167 164 164 VAL VAL A . n 
A 1 168 SER 168 165 165 SER SER A . n 
A 1 169 GLY 169 166 166 GLY GLY A . n 
A 1 170 ALA 170 167 167 ALA ALA A . n 
A 1 171 SER 171 168 168 SER SER A . n 
A 1 172 GLY 172 169 169 GLY GLY A . n 
A 1 173 MET 173 170 170 MET MET A . n 
A 1 174 ILE 174 171 171 ILE ILE A . n 
A 1 175 GLY 175 172 172 GLY GLY A . n 
A 1 176 THR 176 173 173 THR THR A . n 
A 1 177 LEU 177 174 174 LEU LEU A . n 
A 1 178 VAL 178 175 175 VAL VAL A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 GLN 180 177 177 GLN GLN A . n 
A 1 181 MET 181 178 178 MET MET A . n 
A 1 182 ALA 182 179 179 ALA ALA A . n 
A 1 183 LYS 183 180 180 LYS LYS A . n 
A 1 184 ARG 184 181 181 ARG ARG A . n 
A 1 185 ALA 185 182 182 ALA ALA A . n 
A 1 186 GLY 186 183 183 GLY GLY A . n 
A 1 187 ALA 187 184 184 ALA ALA A . n 
A 1 188 ARG 188 185 185 ARG ARG A . n 
A 1 189 VAL 189 186 186 VAL VAL A . n 
A 1 190 VAL 190 187 187 VAL VAL A . n 
A 1 191 GLY 191 188 188 GLY GLY A . n 
A 1 192 THR 192 189 189 THR THR A . n 
A 1 193 ALA 193 190 190 ALA ALA A . n 
A 1 194 GLY 194 191 191 GLY GLY A . n 
A 1 195 SER 195 192 192 SER SER A . n 
A 1 196 ALA 196 193 193 ALA ALA A . n 
A 1 197 GLY 197 194 194 GLY GLY A . n 
A 1 198 LYS 198 195 195 LYS LYS A . n 
A 1 199 ALA 199 196 196 ALA ALA A . n 
A 1 200 ARG 200 197 197 ARG ARG A . n 
A 1 201 TYR 201 198 198 TYR TYR A . n 
A 1 202 LEU 202 199 199 LEU LEU A . n 
A 1 203 SER 203 200 200 SER SER A . n 
A 1 204 GLN 204 201 201 GLN GLN A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 GLY 206 203 203 GLY GLY A . n 
A 1 207 PHE 207 204 204 PHE PHE A . n 
A 1 208 ASP 208 205 205 ASP ASP A . n 
A 1 209 ALA 209 206 206 ALA ALA A . n 
A 1 210 VAL 210 207 207 VAL VAL A . n 
A 1 211 ILE 211 208 208 ILE ILE A . n 
A 1 212 ASP 212 209 209 ASP ASP A . n 
A 1 213 TYR 213 210 210 TYR TYR A . n 
A 1 214 LYS 214 211 211 LYS LYS A . n 
A 1 215 LEU 215 212 212 LEU LEU A . n 
A 1 216 ALA 216 213 213 ALA ALA A . n 
A 1 217 ASP 217 214 214 ASP ASP A . n 
A 1 218 ASP 218 215 215 ASP ASP A . n 
A 1 219 ALA 219 216 216 ALA ALA A . n 
A 1 220 ASP 220 217 217 ASP ASP A . n 
A 1 221 LYS 221 218 218 LYS LYS A . n 
A 1 222 MET 222 219 219 MET MET A . n 
A 1 223 ARG 223 220 220 ARG ARG A . n 
A 1 224 GLU 224 221 221 GLU GLU A . n 
A 1 225 ALA 225 222 222 ALA ALA A . n 
A 1 226 LEU 226 223 223 LEU LEU A . n 
A 1 227 ARG 227 224 224 ARG ARG A . n 
A 1 228 GLU 228 225 225 GLU GLU A . n 
A 1 229 ALA 229 226 226 ALA ALA A . n 
A 1 230 ALA 230 227 227 ALA ALA A . n 
A 1 231 PRO 231 228 228 PRO PRO A . n 
A 1 232 ASP 232 229 229 ASP ASP A . n 
A 1 233 GLY 233 230 230 GLY GLY A . n 
A 1 234 VAL 234 231 231 VAL VAL A . n 
A 1 235 ASP 235 232 232 ASP ASP A . n 
A 1 236 LYS 236 233 233 LYS LYS A . n 
A 1 237 TYR 237 234 234 TYR TYR A . n 
A 1 238 PHE 238 235 235 PHE PHE A . n 
A 1 239 ASP 239 236 236 ASP ASP A . n 
A 1 240 SER 240 237 237 SER SER A . n 
A 1 241 ILE 241 238 238 ILE ILE A . n 
A 1 242 GLY 242 239 239 GLY GLY A . n 
A 1 243 GLY 243 240 240 GLY GLY A . n 
A 1 244 SER 244 241 241 SER SER A . n 
A 1 245 VAL 245 242 242 VAL VAL A . n 
A 1 246 THR 246 243 243 THR THR A . n 
A 1 247 ASP 247 244 244 ASP ASP A . n 
A 1 248 ALA 248 245 245 ALA ALA A . n 
A 1 249 VAL 249 246 246 VAL VAL A . n 
A 1 250 PHE 250 247 247 PHE PHE A . n 
A 1 251 SER 251 248 248 SER SER A . n 
A 1 252 MET 252 249 249 MET MET A . n 
A 1 253 LEU 253 250 250 LEU LEU A . n 
A 1 254 ASN 254 251 251 ASN ASN A . n 
A 1 255 VAL 255 252 252 VAL VAL A . n 
A 1 256 GLY 256 253 253 GLY GLY A . n 
A 1 257 SER 257 254 254 SER SER A . n 
A 1 258 GLN 258 255 255 GLN GLN A . n 
A 1 259 VAL 259 256 256 VAL VAL A . n 
A 1 260 ALA 260 257 257 ALA ALA A . n 
A 1 261 VAL 261 258 258 VAL VAL A . n 
A 1 262 CYS 262 259 259 CYS CYS A . n 
A 1 263 TRP 263 260 260 TRP TRP A . n 
A 1 264 GLN 264 261 261 GLN GLN A . n 
A 1 265 TRP 265 262 262 TRP TRP A . n 
A 1 266 ALA 266 263 263 ALA ALA A . n 
A 1 267 THR 267 264 264 THR THR A . n 
A 1 268 GLN 268 265 265 GLN GLN A . n 
A 1 269 VAL 269 266 266 VAL VAL A . n 
A 1 270 GLN 270 267 267 GLN GLN A . n 
A 1 271 ARG 271 268 268 ARG ARG A . n 
A 1 272 ASP 272 269 269 ASP ASP A . n 
A 1 273 TYR 273 270 270 TYR TYR A . n 
A 1 274 HIS 274 271 271 HIS HIS A . n 
A 1 275 GLY 275 272 272 GLY GLY A . n 
A 1 276 PRO 276 273 273 PRO PRO A . n 
A 1 277 ARG 277 274 274 ARG ARG A . n 
A 1 278 LEU 278 275 275 LEU LEU A . n 
A 1 279 LEU 279 276 276 LEU LEU A . n 
A 1 280 PRO 280 277 277 PRO PRO A . n 
A 1 281 TYR 281 278 278 TYR TYR A . n 
A 1 282 ILE 282 279 279 ILE ILE A . n 
A 1 283 MET 283 280 280 MET MET A . n 
A 1 284 PHE 284 281 281 PHE PHE A . n 
A 1 285 PRO 285 282 282 PRO PRO A . n 
A 1 286 ARG 286 283 283 ARG ARG A . n 
A 1 287 ALA 287 284 284 ALA ALA A . n 
A 1 288 THR 288 285 285 THR THR A . n 
A 1 289 ILE 289 286 286 ILE ILE A . n 
A 1 290 ARG 290 287 287 ARG ARG A . n 
A 1 291 GLY 291 288 288 GLY GLY A . n 
A 1 292 ILE 292 289 289 ILE ILE A . n 
A 1 293 PHE 293 290 290 PHE PHE A . n 
A 1 294 SER 294 291 291 SER SER A . n 
A 1 295 LEU 295 292 292 LEU LEU A . n 
A 1 296 GLU 296 293 293 GLU GLU A . n 
A 1 297 TRP 297 294 294 TRP TRP A . n 
A 1 298 PHE 298 295 295 PHE PHE A . n 
A 1 299 THR 299 296 296 THR THR A . n 
A 1 300 GLU 300 297 297 GLU GLU A . n 
A 1 301 GLN 301 298 298 GLN GLN A . n 
A 1 302 ASN 302 299 299 ASN ASN A . n 
A 1 303 TRP 303 300 300 TRP TRP A . n 
A 1 304 SER 304 301 301 SER SER A . n 
A 1 305 ALA 305 302 302 ALA ALA A . n 
A 1 306 LEU 306 303 303 LEU LEU A . n 
A 1 307 HIS 307 304 304 HIS HIS A . n 
A 1 308 GLU 308 305 305 GLU GLU A . n 
A 1 309 GLU 309 306 306 GLU GLU A . n 
A 1 310 LEU 310 307 307 LEU LEU A . n 
A 1 311 GLY 311 308 308 GLY GLY A . n 
A 1 312 GLY 312 309 309 GLY GLY A . n 
A 1 313 LEU 313 310 310 LEU LEU A . n 
A 1 314 VAL 314 311 311 VAL VAL A . n 
A 1 315 ARG 315 312 312 ARG ARG A . n 
A 1 316 ARG 316 313 313 ARG ARG A . n 
A 1 317 GLN 317 314 314 GLN GLN A . n 
A 1 318 GLU 318 315 315 GLU GLU A . n 
A 1 319 LEU 319 316 316 LEU LEU A . n 
A 1 320 VAL 320 317 317 VAL VAL A . n 
A 1 321 ALA 321 318 318 ALA ALA A . n 
A 1 322 HIS 322 319 319 HIS HIS A . n 
A 1 323 GLU 323 320 320 GLU GLU A . n 
A 1 324 THR 324 321 321 THR THR A . n 
A 1 325 VAL 325 322 322 VAL VAL A . n 
A 1 326 GLN 326 323 323 GLN GLN A . n 
A 1 327 ASP 327 324 324 ASP ASP A . n 
A 1 328 GLY 328 325 325 GLY GLY A . n 
A 1 329 PHE 329 326 326 PHE PHE A . n 
A 1 330 GLU 330 327 327 GLU GLU A . n 
A 1 331 HIS 331 328 328 HIS HIS A . n 
A 1 332 ILE 332 329 329 ILE ILE A . n 
A 1 333 PRO 333 330 330 PRO PRO A . n 
A 1 334 ALA 334 331 331 ALA ALA A . n 
A 1 335 ALA 335 332 332 ALA ALA A . n 
A 1 336 TYR 336 333 333 TYR TYR A . n 
A 1 337 GLN 337 334 334 GLN GLN A . n 
A 1 338 THR 338 335 335 THR THR A . n 
A 1 339 LEU 339 336 336 LEU LEU A . n 
A 1 340 PHE 340 337 337 PHE PHE A . n 
A 1 341 SER 341 338 338 SER SER A . n 
A 1 342 ALA 342 339 339 ALA ALA A . n 
A 1 343 SER 343 340 340 SER SER A . n 
A 1 344 GLU 344 341 341 GLU GLU A . n 
A 1 345 SER 345 342 342 SER SER A . n 
A 1 346 ASN 346 343 343 ASN ASN A . n 
A 1 347 ARG 347 344 344 ARG ARG A . n 
A 1 348 GLY 348 345 345 GLY GLY A . n 
A 1 349 LYS 349 346 346 LYS LYS A . n 
A 1 350 VAL 350 347 347 VAL VAL A . n 
A 1 351 LEU 351 348 348 LEU LEU A . n 
A 1 352 VAL 352 349 349 VAL VAL A . n 
A 1 353 ARG 353 350 350 ARG ARG A . n 
A 1 354 VAL 354 351 351 VAL VAL A . n 
B 1 1   LEU 1   -2  -2  LEU LEU B . n 
B 1 2   GLY 2   -1  -1  GLY GLY B . n 
B 1 3   SER 3   0   0   SER SER B . n 
B 1 4   MET 4   1   1   MET MET B . n 
B 1 5   LYS 5   2   2   LYS LYS B . n 
B 1 6   THR 6   3   3   THR THR B . n 
B 1 7   GLU 7   4   4   GLU GLU B . n 
B 1 8   ARG 8   5   5   ARG ARG B . n 
B 1 9   TRP 9   6   6   TRP TRP B . n 
B 1 10  VAL 10  7   7   VAL VAL B . n 
B 1 11  VAL 11  8   8   VAL VAL B . n 
B 1 12  ARG 12  9   9   ARG ARG B . n 
B 1 13  GLU 13  10  10  GLU GLU B . n 
B 1 14  HIS 14  11  11  HIS HIS B . n 
B 1 15  VAL 15  12  12  VAL VAL B . n 
B 1 16  GLU 16  13  13  GLU GLU B . n 
B 1 17  GLY 17  14  14  GLY GLY B . n 
B 1 18  VAL 18  15  15  VAL VAL B . n 
B 1 19  PRO 19  16  16  PRO PRO B . n 
B 1 20  ASP 20  17  17  ASP ASP B . n 
B 1 21  ALA 21  18  18  ALA ALA B . n 
B 1 22  ALA 22  19  19  ALA ALA B . n 
B 1 23  ARG 23  20  20  ARG ARG B . n 
B 1 24  ILE 24  21  21  ILE ILE B . n 
B 1 25  TYR 25  22  22  TYR TYR B . n 
B 1 26  GLU 26  23  23  GLU GLU B . n 
B 1 27  LYS 27  24  24  LYS LYS B . n 
B 1 28  VAL 28  25  25  VAL VAL B . n 
B 1 29  GLU 29  26  26  GLU GLU B . n 
B 1 30  THR 30  27  27  THR THR B . n 
B 1 31  GLU 31  28  28  GLU GLU B . n 
B 1 32  LEU 32  29  29  LEU LEU B . n 
B 1 33  ASN 33  30  30  ASN ASN B . n 
B 1 34  THR 34  31  31  THR THR B . n 
B 1 35  ARG 35  32  32  ARG ARG B . n 
B 1 36  LEU 36  33  33  LEU LEU B . n 
B 1 37  GLY 37  34  34  GLY GLY B . n 
B 1 38  GLU 38  35  35  GLU GLU B . n 
B 1 39  GLU 39  36  36  GLU GLU B . n 
B 1 40  GLN 40  37  37  GLN GLN B . n 
B 1 41  MET 41  38  38  MET MET B . n 
B 1 42  LEU 42  39  39  LEU LEU B . n 
B 1 43  LEU 43  40  40  LEU LEU B . n 
B 1 44  LYS 44  41  41  LYS LYS B . n 
B 1 45  THR 45  42  42  THR THR B . n 
B 1 46  LEU 46  43  43  LEU LEU B . n 
B 1 47  TYR 47  44  44  TYR TYR B . n 
B 1 48  VAL 48  45  45  VAL VAL B . n 
B 1 49  SER 49  46  46  SER SER B . n 
B 1 50  VAL 50  47  47  VAL VAL B . n 
B 1 51  ASP 51  48  48  ASP ASP B . n 
B 1 52  PRO 52  49  49  PRO PRO B . n 
B 1 53  TYR 53  50  50  TYR TYR B . n 
B 1 54  LEU 54  51  51  LEU LEU B . n 
B 1 55  GLN 55  52  52  GLN GLN B . n 
B 1 56  GLY 56  53  53  GLY GLY B . n 
B 1 57  ILE 57  54  54  ILE ILE B . n 
B 1 58  CYS 58  55  55  CYS CYS B . n 
B 1 59  LEU 59  56  56  LEU LEU B . n 
B 1 60  ASP 60  57  57  ASP ASP B . n 
B 1 61  THR 61  58  58  THR THR B . n 
B 1 62  PRO 62  59  59  PRO PRO B . n 
B 1 63  ILE 63  60  60  ILE ILE B . n 
B 1 64  GLY 64  61  61  GLY GLY B . n 
B 1 65  ASP 65  62  62  ASP ASP B . n 
B 1 66  HIS 66  63  63  HIS HIS B . n 
B 1 67  MET 67  64  64  MET MET B . n 
B 1 68  GLY 68  65  65  GLY GLY B . n 
B 1 69  ALA 69  66  66  ALA ALA B . n 
B 1 70  ASP 70  67  67  ASP ASP B . n 
B 1 71  SER 71  68  68  SER SER B . n 
B 1 72  ILE 72  69  69  ILE ILE B . n 
B 1 73  MET 73  70  70  MET MET B . n 
B 1 74  GLN 74  71  71  GLN GLN B . n 
B 1 75  VAL 75  72  72  VAL VAL B . n 
B 1 76  LEU 76  73  73  LEU LEU B . n 
B 1 77  ASP 77  74  74  ASP ASP B . n 
B 1 78  ALA 78  75  75  ALA ALA B . n 
B 1 79  GLY 79  76  76  GLY GLY B . n 
B 1 80  PRO 80  77  77  PRO PRO B . n 
B 1 81  ASN 81  78  78  ASN ASN B . n 
B 1 82  ALA 82  79  79  ALA ALA B . n 
B 1 83  PRO 83  80  80  PRO PRO B . n 
B 1 84  PHE 84  81  81  PHE PHE B . n 
B 1 85  ARG 85  82  82  ARG ARG B . n 
B 1 86  PRO 86  83  83  PRO PRO B . n 
B 1 87  GLY 87  84  84  GLY GLY B . n 
B 1 88  ASP 88  85  85  ASP ASP B . n 
B 1 89  LEU 89  86  86  LEU LEU B . n 
B 1 90  VAL 90  87  87  VAL VAL B . n 
B 1 91  GLN 91  88  88  GLN GLN B . n 
B 1 92  GLY 92  89  89  GLY GLY B . n 
B 1 93  PHE 93  90  90  PHE PHE B . n 
B 1 94  GLY 94  91  91  GLY GLY B . n 
B 1 95  GLY 95  92  92  GLY GLY B . n 
B 1 96  TRP 96  93  93  TRP TRP B . n 
B 1 97  ARG 97  94  94  ARG ARG B . n 
B 1 98  THR 98  95  95  THR THR B . n 
B 1 99  HIS 99  96  96  HIS HIS B . n 
B 1 100 LEU 100 97  97  LEU LEU B . n 
B 1 101 VAL 101 98  98  VAL VAL B . n 
B 1 102 SER 102 99  99  SER SER B . n 
B 1 103 ASP 103 100 100 ASP ASP B . n 
B 1 104 GLY 104 101 101 GLY GLY B . n 
B 1 105 LYS 105 102 102 LYS LYS B . n 
B 1 106 PRO 106 103 103 PRO PRO B . n 
B 1 107 LYS 107 104 104 LYS LYS B . n 
B 1 108 LEU 108 105 105 LEU LEU B . n 
B 1 109 TRP 109 106 106 TRP TRP B . n 
B 1 110 GLN 110 107 107 GLN GLN B . n 
B 1 111 THR 111 108 108 THR THR B . n 
B 1 112 GLY 112 109 109 GLY GLY B . n 
B 1 113 THR 113 110 110 THR THR B . n 
B 1 114 PHE 114 111 111 PHE PHE B . n 
B 1 115 PRO 115 112 112 PRO PRO B . n 
B 1 116 MET 116 113 113 MET MET B . n 
B 1 117 VAL 117 114 114 VAL VAL B . n 
B 1 118 PHE 118 115 115 PHE PHE B . n 
B 1 119 PRO 119 116 116 PRO PRO B . n 
B 1 120 ALA 120 117 117 ALA ALA B . n 
B 1 121 TYR 121 118 118 TYR TYR B . n 
B 1 122 ARG 122 119 119 ARG ARG B . n 
B 1 123 LYS 123 120 120 LYS LYS B . n 
B 1 124 LEU 124 121 121 LEU LEU B . n 
B 1 125 ASP 125 122 122 ASP ASP B . n 
B 1 126 LEU 126 123 123 LEU LEU B . n 
B 1 127 ARG 127 124 124 ARG ARG B . n 
B 1 128 HIS 128 125 125 HIS HIS B . n 
B 1 129 TYR 129 126 126 TYR TYR B . n 
B 1 130 ASP 130 127 127 ASP ASP B . n 
B 1 131 ASP 131 128 128 ASP ASP B . n 
B 1 132 ALA 132 129 129 ALA ALA B . n 
B 1 133 LEU 133 130 130 LEU LEU B . n 
B 1 134 PRO 134 131 131 PRO PRO B . n 
B 1 135 LEU 135 132 132 LEU LEU B . n 
B 1 136 SER 136 133 133 SER SER B . n 
B 1 137 THR 137 134 134 THR THR B . n 
B 1 138 ALA 138 135 135 ALA ALA B . n 
B 1 139 LEU 139 136 136 LEU LEU B . n 
B 1 140 GLY 140 137 137 GLY GLY B . n 
B 1 141 VAL 141 138 138 VAL VAL B . n 
B 1 142 MET 142 139 139 MET MET B . n 
B 1 143 GLY 143 140 140 GLY GLY B . n 
B 1 144 GLY 144 141 141 GLY GLY B . n 
B 1 145 PRO 145 142 142 PRO PRO B . n 
B 1 146 GLY 146 143 143 GLY GLY B . n 
B 1 147 MET 147 144 144 MET MET B . n 
B 1 148 THR 148 145 145 THR THR B . n 
B 1 149 ALA 149 146 146 ALA ALA B . n 
B 1 150 TRP 150 147 147 TRP TRP B . n 
B 1 151 GLY 151 148 148 GLY GLY B . n 
B 1 152 THR 152 149 149 THR THR B . n 
B 1 153 MET 153 150 150 MET MET B . n 
B 1 154 THR 154 151 151 THR THR B . n 
B 1 155 LYS 155 152 152 LYS LYS B . n 
B 1 156 PHE 156 153 153 PHE PHE B . n 
B 1 157 MET 157 154 154 MET MET B . n 
B 1 158 GLN 158 155 155 GLN GLN B . n 
B 1 159 VAL 159 156 156 VAL VAL B . n 
B 1 160 ARG 160 157 157 ARG ARG B . n 
B 1 161 PRO 161 158 158 PRO PRO B . n 
B 1 162 GLY 162 159 159 GLY GLY B . n 
B 1 163 ASP 163 160 160 ASP ASP B . n 
B 1 164 THR 164 161 161 THR THR B . n 
B 1 165 VAL 165 162 162 VAL VAL B . n 
B 1 166 VAL 166 163 163 VAL VAL B . n 
B 1 167 VAL 167 164 164 VAL VAL B . n 
B 1 168 SER 168 165 165 SER SER B . n 
B 1 169 GLY 169 166 166 GLY GLY B . n 
B 1 170 ALA 170 167 167 ALA ALA B . n 
B 1 171 SER 171 168 168 SER SER B . n 
B 1 172 GLY 172 169 169 GLY GLY B . n 
B 1 173 MET 173 170 170 MET MET B . n 
B 1 174 ILE 174 171 171 ILE ILE B . n 
B 1 175 GLY 175 172 172 GLY GLY B . n 
B 1 176 THR 176 173 173 THR THR B . n 
B 1 177 LEU 177 174 174 LEU LEU B . n 
B 1 178 VAL 178 175 175 VAL VAL B . n 
B 1 179 GLY 179 176 176 GLY GLY B . n 
B 1 180 GLN 180 177 177 GLN GLN B . n 
B 1 181 MET 181 178 178 MET MET B . n 
B 1 182 ALA 182 179 179 ALA ALA B . n 
B 1 183 LYS 183 180 180 LYS LYS B . n 
B 1 184 ARG 184 181 181 ARG ARG B . n 
B 1 185 ALA 185 182 182 ALA ALA B . n 
B 1 186 GLY 186 183 183 GLY GLY B . n 
B 1 187 ALA 187 184 184 ALA ALA B . n 
B 1 188 ARG 188 185 185 ARG ARG B . n 
B 1 189 VAL 189 186 186 VAL VAL B . n 
B 1 190 VAL 190 187 187 VAL VAL B . n 
B 1 191 GLY 191 188 188 GLY GLY B . n 
B 1 192 THR 192 189 189 THR THR B . n 
B 1 193 ALA 193 190 190 ALA ALA B . n 
B 1 194 GLY 194 191 191 GLY GLY B . n 
B 1 195 SER 195 192 192 SER SER B . n 
B 1 196 ALA 196 193 193 ALA ALA B . n 
B 1 197 GLY 197 194 194 GLY GLY B . n 
B 1 198 LYS 198 195 195 LYS LYS B . n 
B 1 199 ALA 199 196 196 ALA ALA B . n 
B 1 200 ARG 200 197 197 ARG ARG B . n 
B 1 201 TYR 201 198 198 TYR TYR B . n 
B 1 202 LEU 202 199 199 LEU LEU B . n 
B 1 203 SER 203 200 200 SER SER B . n 
B 1 204 GLN 204 201 201 GLN GLN B . n 
B 1 205 LEU 205 202 202 LEU LEU B . n 
B 1 206 GLY 206 203 203 GLY GLY B . n 
B 1 207 PHE 207 204 204 PHE PHE B . n 
B 1 208 ASP 208 205 205 ASP ASP B . n 
B 1 209 ALA 209 206 206 ALA ALA B . n 
B 1 210 VAL 210 207 207 VAL VAL B . n 
B 1 211 ILE 211 208 208 ILE ILE B . n 
B 1 212 ASP 212 209 209 ASP ASP B . n 
B 1 213 TYR 213 210 210 TYR TYR B . n 
B 1 214 LYS 214 211 211 LYS LYS B . n 
B 1 215 LEU 215 212 212 LEU LEU B . n 
B 1 216 ALA 216 213 213 ALA ALA B . n 
B 1 217 ASP 217 214 214 ASP ASP B . n 
B 1 218 ASP 218 215 215 ASP ASP B . n 
B 1 219 ALA 219 216 216 ALA ALA B . n 
B 1 220 ASP 220 217 217 ASP ASP B . n 
B 1 221 LYS 221 218 218 LYS LYS B . n 
B 1 222 MET 222 219 219 MET MET B . n 
B 1 223 ARG 223 220 220 ARG ARG B . n 
B 1 224 GLU 224 221 221 GLU GLU B . n 
B 1 225 ALA 225 222 222 ALA ALA B . n 
B 1 226 LEU 226 223 223 LEU LEU B . n 
B 1 227 ARG 227 224 224 ARG ARG B . n 
B 1 228 GLU 228 225 225 GLU GLU B . n 
B 1 229 ALA 229 226 226 ALA ALA B . n 
B 1 230 ALA 230 227 227 ALA ALA B . n 
B 1 231 PRO 231 228 228 PRO PRO B . n 
B 1 232 ASP 232 229 229 ASP ASP B . n 
B 1 233 GLY 233 230 230 GLY GLY B . n 
B 1 234 VAL 234 231 231 VAL VAL B . n 
B 1 235 ASP 235 232 232 ASP ASP B . n 
B 1 236 LYS 236 233 233 LYS LYS B . n 
B 1 237 TYR 237 234 234 TYR TYR B . n 
B 1 238 PHE 238 235 235 PHE PHE B . n 
B 1 239 ASP 239 236 236 ASP ASP B . n 
B 1 240 SER 240 237 237 SER SER B . n 
B 1 241 ILE 241 238 238 ILE ILE B . n 
B 1 242 GLY 242 239 239 GLY GLY B . n 
B 1 243 GLY 243 240 240 GLY GLY B . n 
B 1 244 SER 244 241 241 SER SER B . n 
B 1 245 VAL 245 242 242 VAL VAL B . n 
B 1 246 THR 246 243 243 THR THR B . n 
B 1 247 ASP 247 244 244 ASP ASP B . n 
B 1 248 ALA 248 245 245 ALA ALA B . n 
B 1 249 VAL 249 246 246 VAL VAL B . n 
B 1 250 PHE 250 247 247 PHE PHE B . n 
B 1 251 SER 251 248 248 SER SER B . n 
B 1 252 MET 252 249 249 MET MET B . n 
B 1 253 LEU 253 250 250 LEU LEU B . n 
B 1 254 ASN 254 251 251 ASN ASN B . n 
B 1 255 VAL 255 252 252 VAL VAL B . n 
B 1 256 GLY 256 253 253 GLY GLY B . n 
B 1 257 SER 257 254 254 SER SER B . n 
B 1 258 GLN 258 255 255 GLN GLN B . n 
B 1 259 VAL 259 256 256 VAL VAL B . n 
B 1 260 ALA 260 257 257 ALA ALA B . n 
B 1 261 VAL 261 258 258 VAL VAL B . n 
B 1 262 CYS 262 259 259 CYS CYS B . n 
B 1 263 TRP 263 260 260 TRP TRP B . n 
B 1 264 GLN 264 261 261 GLN GLN B . n 
B 1 265 TRP 265 262 262 TRP TRP B . n 
B 1 266 ALA 266 263 263 ALA ALA B . n 
B 1 267 THR 267 264 264 THR THR B . n 
B 1 268 GLN 268 265 265 GLN GLN B . n 
B 1 269 VAL 269 266 266 VAL VAL B . n 
B 1 270 GLN 270 267 267 GLN GLN B . n 
B 1 271 ARG 271 268 268 ARG ARG B . n 
B 1 272 ASP 272 269 269 ASP ASP B . n 
B 1 273 TYR 273 270 270 TYR TYR B . n 
B 1 274 HIS 274 271 271 HIS HIS B . n 
B 1 275 GLY 275 272 272 GLY GLY B . n 
B 1 276 PRO 276 273 273 PRO PRO B . n 
B 1 277 ARG 277 274 274 ARG ARG B . n 
B 1 278 LEU 278 275 275 LEU LEU B . n 
B 1 279 LEU 279 276 276 LEU LEU B . n 
B 1 280 PRO 280 277 277 PRO PRO B . n 
B 1 281 TYR 281 278 278 TYR TYR B . n 
B 1 282 ILE 282 279 279 ILE ILE B . n 
B 1 283 MET 283 280 280 MET MET B . n 
B 1 284 PHE 284 281 281 PHE PHE B . n 
B 1 285 PRO 285 282 282 PRO PRO B . n 
B 1 286 ARG 286 283 283 ARG ARG B . n 
B 1 287 ALA 287 284 284 ALA ALA B . n 
B 1 288 THR 288 285 285 THR THR B . n 
B 1 289 ILE 289 286 286 ILE ILE B . n 
B 1 290 ARG 290 287 287 ARG ARG B . n 
B 1 291 GLY 291 288 288 GLY GLY B . n 
B 1 292 ILE 292 289 289 ILE ILE B . n 
B 1 293 PHE 293 290 290 PHE PHE B . n 
B 1 294 SER 294 291 291 SER SER B . n 
B 1 295 LEU 295 292 292 LEU LEU B . n 
B 1 296 GLU 296 293 293 GLU GLU B . n 
B 1 297 TRP 297 294 294 TRP TRP B . n 
B 1 298 PHE 298 295 295 PHE PHE B . n 
B 1 299 THR 299 296 296 THR THR B . n 
B 1 300 GLU 300 297 297 GLU GLU B . n 
B 1 301 GLN 301 298 298 GLN GLN B . n 
B 1 302 ASN 302 299 299 ASN ASN B . n 
B 1 303 TRP 303 300 300 TRP TRP B . n 
B 1 304 SER 304 301 301 SER SER B . n 
B 1 305 ALA 305 302 302 ALA ALA B . n 
B 1 306 LEU 306 303 303 LEU LEU B . n 
B 1 307 HIS 307 304 304 HIS HIS B . n 
B 1 308 GLU 308 305 305 GLU GLU B . n 
B 1 309 GLU 309 306 306 GLU GLU B . n 
B 1 310 LEU 310 307 307 LEU LEU B . n 
B 1 311 GLY 311 308 308 GLY GLY B . n 
B 1 312 GLY 312 309 309 GLY GLY B . n 
B 1 313 LEU 313 310 310 LEU LEU B . n 
B 1 314 VAL 314 311 311 VAL VAL B . n 
B 1 315 ARG 315 312 312 ARG ARG B . n 
B 1 316 ARG 316 313 313 ARG ARG B . n 
B 1 317 GLN 317 314 314 GLN GLN B . n 
B 1 318 GLU 318 315 315 GLU GLU B . n 
B 1 319 LEU 319 316 316 LEU LEU B . n 
B 1 320 VAL 320 317 317 VAL VAL B . n 
B 1 321 ALA 321 318 318 ALA ALA B . n 
B 1 322 HIS 322 319 319 HIS HIS B . n 
B 1 323 GLU 323 320 320 GLU GLU B . n 
B 1 324 THR 324 321 321 THR THR B . n 
B 1 325 VAL 325 322 322 VAL VAL B . n 
B 1 326 GLN 326 323 323 GLN GLN B . n 
B 1 327 ASP 327 324 324 ASP ASP B . n 
B 1 328 GLY 328 325 325 GLY GLY B . n 
B 1 329 PHE 329 326 326 PHE PHE B . n 
B 1 330 GLU 330 327 327 GLU GLU B . n 
B 1 331 HIS 331 328 328 HIS HIS B . n 
B 1 332 ILE 332 329 329 ILE ILE B . n 
B 1 333 PRO 333 330 330 PRO PRO B . n 
B 1 334 ALA 334 331 331 ALA ALA B . n 
B 1 335 ALA 335 332 332 ALA ALA B . n 
B 1 336 TYR 336 333 333 TYR TYR B . n 
B 1 337 GLN 337 334 334 GLN GLN B . n 
B 1 338 THR 338 335 335 THR THR B . n 
B 1 339 LEU 339 336 336 LEU LEU B . n 
B 1 340 PHE 340 337 337 PHE PHE B . n 
B 1 341 SER 341 338 338 SER SER B . n 
B 1 342 ALA 342 339 339 ALA ALA B . n 
B 1 343 SER 343 340 340 SER SER B . n 
B 1 344 GLU 344 341 341 GLU GLU B . n 
B 1 345 SER 345 342 342 SER SER B . n 
B 1 346 ASN 346 343 343 ASN ASN B . n 
B 1 347 ARG 347 344 344 ARG ARG B . n 
B 1 348 GLY 348 345 345 GLY GLY B . n 
B 1 349 LYS 349 346 346 LYS LYS B . n 
B 1 350 VAL 350 347 347 VAL VAL B . n 
B 1 351 LEU 351 348 348 LEU LEU B . n 
B 1 352 VAL 352 349 349 VAL VAL B . n 
B 1 353 ARG 353 350 350 ARG ARG B . n 
B 1 354 VAL 354 351 351 VAL VAL B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1EDK 1   401 502 A1EDK YYL A . 
D 3 NAP   1   402 501 NAP   NAP A . 
E 2 A1EDK 1   401 502 A1EDK YYL B . 
F 3 NAP   1   402 501 NAP   NAP B . 
G 4 HOH   1   501 471 HOH   HOH A . 
G 4 HOH   2   502 358 HOH   HOH A . 
G 4 HOH   3   503 392 HOH   HOH A . 
G 4 HOH   4   504 311 HOH   HOH A . 
G 4 HOH   5   505 411 HOH   HOH A . 
G 4 HOH   6   506 271 HOH   HOH A . 
G 4 HOH   7   507 22  HOH   HOH A . 
G 4 HOH   8   508 310 HOH   HOH A . 
G 4 HOH   9   509 452 HOH   HOH A . 
G 4 HOH   10  510 320 HOH   HOH A . 
G 4 HOH   11  511 89  HOH   HOH A . 
G 4 HOH   12  512 99  HOH   HOH A . 
G 4 HOH   13  513 410 HOH   HOH A . 
G 4 HOH   14  514 159 HOH   HOH A . 
G 4 HOH   15  515 400 HOH   HOH A . 
G 4 HOH   16  516 4   HOH   HOH A . 
G 4 HOH   17  517 499 HOH   HOH A . 
G 4 HOH   18  518 360 HOH   HOH A . 
G 4 HOH   19  519 200 HOH   HOH A . 
G 4 HOH   20  520 264 HOH   HOH A . 
G 4 HOH   21  521 176 HOH   HOH A . 
G 4 HOH   22  522 217 HOH   HOH A . 
G 4 HOH   23  523 531 HOH   HOH A . 
G 4 HOH   24  524 135 HOH   HOH A . 
G 4 HOH   25  525 7   HOH   HOH A . 
G 4 HOH   26  526 8   HOH   HOH A . 
G 4 HOH   27  527 238 HOH   HOH A . 
G 4 HOH   28  528 386 HOH   HOH A . 
G 4 HOH   29  529 248 HOH   HOH A . 
G 4 HOH   30  530 26  HOH   HOH A . 
G 4 HOH   31  531 252 HOH   HOH A . 
G 4 HOH   32  532 393 HOH   HOH A . 
G 4 HOH   33  533 480 HOH   HOH A . 
G 4 HOH   34  534 39  HOH   HOH A . 
G 4 HOH   35  535 88  HOH   HOH A . 
G 4 HOH   36  536 372 HOH   HOH A . 
G 4 HOH   37  537 15  HOH   HOH A . 
G 4 HOH   38  538 1   HOH   HOH A . 
G 4 HOH   39  539 423 HOH   HOH A . 
G 4 HOH   40  540 216 HOH   HOH A . 
G 4 HOH   41  541 60  HOH   HOH A . 
G 4 HOH   42  542 546 HOH   HOH A . 
G 4 HOH   43  543 102 HOH   HOH A . 
G 4 HOH   44  544 475 HOH   HOH A . 
G 4 HOH   45  545 113 HOH   HOH A . 
G 4 HOH   46  546 332 HOH   HOH A . 
G 4 HOH   47  547 413 HOH   HOH A . 
G 4 HOH   48  548 142 HOH   HOH A . 
G 4 HOH   49  549 600 HOH   HOH A . 
G 4 HOH   50  550 390 HOH   HOH A . 
G 4 HOH   51  551 127 HOH   HOH A . 
G 4 HOH   52  552 76  HOH   HOH A . 
G 4 HOH   53  553 2   HOH   HOH A . 
G 4 HOH   54  554 80  HOH   HOH A . 
G 4 HOH   55  555 322 HOH   HOH A . 
G 4 HOH   56  556 82  HOH   HOH A . 
G 4 HOH   57  557 243 HOH   HOH A . 
G 4 HOH   58  558 245 HOH   HOH A . 
G 4 HOH   59  559 40  HOH   HOH A . 
G 4 HOH   60  560 169 HOH   HOH A . 
G 4 HOH   61  561 379 HOH   HOH A . 
G 4 HOH   62  562 314 HOH   HOH A . 
G 4 HOH   63  563 145 HOH   HOH A . 
G 4 HOH   64  564 369 HOH   HOH A . 
G 4 HOH   65  565 574 HOH   HOH A . 
G 4 HOH   66  566 37  HOH   HOH A . 
G 4 HOH   67  567 150 HOH   HOH A . 
G 4 HOH   68  568 449 HOH   HOH A . 
G 4 HOH   69  569 308 HOH   HOH A . 
G 4 HOH   70  570 168 HOH   HOH A . 
G 4 HOH   71  571 301 HOH   HOH A . 
G 4 HOH   72  572 363 HOH   HOH A . 
G 4 HOH   73  573 466 HOH   HOH A . 
G 4 HOH   74  574 501 HOH   HOH A . 
G 4 HOH   75  575 193 HOH   HOH A . 
G 4 HOH   76  576 241 HOH   HOH A . 
G 4 HOH   77  577 436 HOH   HOH A . 
G 4 HOH   78  578 28  HOH   HOH A . 
G 4 HOH   79  579 277 HOH   HOH A . 
G 4 HOH   80  580 542 HOH   HOH A . 
G 4 HOH   81  581 109 HOH   HOH A . 
G 4 HOH   82  582 406 HOH   HOH A . 
G 4 HOH   83  583 244 HOH   HOH A . 
G 4 HOH   84  584 171 HOH   HOH A . 
G 4 HOH   85  585 236 HOH   HOH A . 
G 4 HOH   86  586 178 HOH   HOH A . 
G 4 HOH   87  587 27  HOH   HOH A . 
G 4 HOH   88  588 364 HOH   HOH A . 
G 4 HOH   89  589 218 HOH   HOH A . 
G 4 HOH   90  590 227 HOH   HOH A . 
G 4 HOH   91  591 208 HOH   HOH A . 
G 4 HOH   92  592 214 HOH   HOH A . 
G 4 HOH   93  593 119 HOH   HOH A . 
G 4 HOH   94  594 128 HOH   HOH A . 
G 4 HOH   95  595 282 HOH   HOH A . 
G 4 HOH   96  596 53  HOH   HOH A . 
G 4 HOH   97  597 84  HOH   HOH A . 
G 4 HOH   98  598 383 HOH   HOH A . 
G 4 HOH   99  599 152 HOH   HOH A . 
G 4 HOH   100 600 114 HOH   HOH A . 
G 4 HOH   101 601 328 HOH   HOH A . 
G 4 HOH   102 602 562 HOH   HOH A . 
G 4 HOH   103 603 179 HOH   HOH A . 
G 4 HOH   104 604 70  HOH   HOH A . 
G 4 HOH   105 605 72  HOH   HOH A . 
G 4 HOH   106 606 16  HOH   HOH A . 
G 4 HOH   107 607 189 HOH   HOH A . 
G 4 HOH   108 608 260 HOH   HOH A . 
G 4 HOH   109 609 324 HOH   HOH A . 
G 4 HOH   110 610 94  HOH   HOH A . 
G 4 HOH   111 611 599 HOH   HOH A . 
G 4 HOH   112 612 479 HOH   HOH A . 
G 4 HOH   113 613 384 HOH   HOH A . 
G 4 HOH   114 614 195 HOH   HOH A . 
G 4 HOH   115 615 496 HOH   HOH A . 
G 4 HOH   116 616 293 HOH   HOH A . 
G 4 HOH   117 617 235 HOH   HOH A . 
G 4 HOH   118 618 233 HOH   HOH A . 
G 4 HOH   119 619 103 HOH   HOH A . 
G 4 HOH   120 620 303 HOH   HOH A . 
G 4 HOH   121 621 86  HOH   HOH A . 
G 4 HOH   122 622 25  HOH   HOH A . 
G 4 HOH   123 623 550 HOH   HOH A . 
G 4 HOH   124 624 106 HOH   HOH A . 
G 4 HOH   125 625 299 HOH   HOH A . 
G 4 HOH   126 626 231 HOH   HOH A . 
G 4 HOH   127 627 35  HOH   HOH A . 
G 4 HOH   128 628 337 HOH   HOH A . 
G 4 HOH   129 629 258 HOH   HOH A . 
G 4 HOH   130 630 304 HOH   HOH A . 
G 4 HOH   131 631 416 HOH   HOH A . 
G 4 HOH   132 632 78  HOH   HOH A . 
G 4 HOH   133 633 117 HOH   HOH A . 
G 4 HOH   134 634 333 HOH   HOH A . 
G 4 HOH   135 635 491 HOH   HOH A . 
G 4 HOH   136 636 421 HOH   HOH A . 
G 4 HOH   137 637 346 HOH   HOH A . 
G 4 HOH   138 638 505 HOH   HOH A . 
G 4 HOH   139 639 126 HOH   HOH A . 
G 4 HOH   140 640 335 HOH   HOH A . 
G 4 HOH   141 641 506 HOH   HOH A . 
G 4 HOH   142 642 154 HOH   HOH A . 
G 4 HOH   143 643 440 HOH   HOH A . 
G 4 HOH   144 644 438 HOH   HOH A . 
G 4 HOH   145 645 83  HOH   HOH A . 
G 4 HOH   146 646 151 HOH   HOH A . 
G 4 HOH   147 647 426 HOH   HOH A . 
G 4 HOH   148 648 305 HOH   HOH A . 
G 4 HOH   149 649 50  HOH   HOH A . 
G 4 HOH   150 650 367 HOH   HOH A . 
G 4 HOH   151 651 289 HOH   HOH A . 
G 4 HOH   152 652 256 HOH   HOH A . 
G 4 HOH   153 653 543 HOH   HOH A . 
G 4 HOH   154 654 148 HOH   HOH A . 
G 4 HOH   155 655 107 HOH   HOH A . 
G 4 HOH   156 656 300 HOH   HOH A . 
G 4 HOH   157 657 140 HOH   HOH A . 
G 4 HOH   158 658 530 HOH   HOH A . 
G 4 HOH   159 659 232 HOH   HOH A . 
G 4 HOH   160 660 272 HOH   HOH A . 
G 4 HOH   161 661 460 HOH   HOH A . 
G 4 HOH   162 662 444 HOH   HOH A . 
G 4 HOH   163 663 158 HOH   HOH A . 
G 4 HOH   164 664 164 HOH   HOH A . 
G 4 HOH   165 665 323 HOH   HOH A . 
G 4 HOH   166 666 476 HOH   HOH A . 
G 4 HOH   167 667 165 HOH   HOH A . 
G 4 HOH   168 668 532 HOH   HOH A . 
G 4 HOH   169 669 382 HOH   HOH A . 
G 4 HOH   170 670 197 HOH   HOH A . 
G 4 HOH   171 671 224 HOH   HOH A . 
G 4 HOH   172 672 30  HOH   HOH A . 
G 4 HOH   173 673 564 HOH   HOH A . 
G 4 HOH   174 674 385 HOH   HOH A . 
G 4 HOH   175 675 280 HOH   HOH A . 
G 4 HOH   176 676 352 HOH   HOH A . 
G 4 HOH   177 677 279 HOH   HOH A . 
G 4 HOH   178 678 202 HOH   HOH A . 
G 4 HOH   179 679 77  HOH   HOH A . 
G 4 HOH   180 680 342 HOH   HOH A . 
G 4 HOH   181 681 98  HOH   HOH A . 
G 4 HOH   182 682 265 HOH   HOH A . 
G 4 HOH   183 683 510 HOH   HOH A . 
G 4 HOH   184 684 87  HOH   HOH A . 
G 4 HOH   185 685 91  HOH   HOH A . 
G 4 HOH   186 686 203 HOH   HOH A . 
G 4 HOH   187 687 450 HOH   HOH A . 
G 4 HOH   188 688 157 HOH   HOH A . 
G 4 HOH   189 689 469 HOH   HOH A . 
G 4 HOH   190 690 365 HOH   HOH A . 
G 4 HOH   191 691 486 HOH   HOH A . 
G 4 HOH   192 692 551 HOH   HOH A . 
G 4 HOH   193 693 309 HOH   HOH A . 
G 4 HOH   194 694 459 HOH   HOH A . 
G 4 HOH   195 695 420 HOH   HOH A . 
G 4 HOH   196 696 194 HOH   HOH A . 
G 4 HOH   197 697 104 HOH   HOH A . 
G 4 HOH   198 698 366 HOH   HOH A . 
G 4 HOH   199 699 134 HOH   HOH A . 
G 4 HOH   200 700 527 HOH   HOH A . 
G 4 HOH   201 701 108 HOH   HOH A . 
G 4 HOH   202 702 348 HOH   HOH A . 
G 4 HOH   203 703 138 HOH   HOH A . 
G 4 HOH   204 704 143 HOH   HOH A . 
G 4 HOH   205 705 378 HOH   HOH A . 
G 4 HOH   206 706 63  HOH   HOH A . 
G 4 HOH   207 707 185 HOH   HOH A . 
G 4 HOH   208 708 520 HOH   HOH A . 
G 4 HOH   209 709 149 HOH   HOH A . 
G 4 HOH   210 710 572 HOH   HOH A . 
G 4 HOH   211 711 97  HOH   HOH A . 
G 4 HOH   212 712 122 HOH   HOH A . 
G 4 HOH   213 713 514 HOH   HOH A . 
G 4 HOH   214 714 206 HOH   HOH A . 
G 4 HOH   215 715 284 HOH   HOH A . 
G 4 HOH   216 716 261 HOH   HOH A . 
G 4 HOH   217 717 187 HOH   HOH A . 
G 4 HOH   218 718 67  HOH   HOH A . 
G 4 HOH   219 719 192 HOH   HOH A . 
G 4 HOH   220 720 344 HOH   HOH A . 
G 4 HOH   221 721 567 HOH   HOH A . 
G 4 HOH   222 722 111 HOH   HOH A . 
G 4 HOH   223 723 563 HOH   HOH A . 
G 4 HOH   224 724 432 HOH   HOH A . 
G 4 HOH   225 725 173 HOH   HOH A . 
G 4 HOH   226 726 580 HOH   HOH A . 
G 4 HOH   227 727 228 HOH   HOH A . 
G 4 HOH   228 728 415 HOH   HOH A . 
G 4 HOH   229 729 204 HOH   HOH A . 
G 4 HOH   230 730 573 HOH   HOH A . 
G 4 HOH   231 731 515 HOH   HOH A . 
G 4 HOH   232 732 263 HOH   HOH A . 
G 4 HOH   233 733 242 HOH   HOH A . 
G 4 HOH   234 734 503 HOH   HOH A . 
G 4 HOH   235 735 556 HOH   HOH A . 
G 4 HOH   236 736 319 HOH   HOH A . 
G 4 HOH   237 737 330 HOH   HOH A . 
G 4 HOH   238 738 552 HOH   HOH A . 
G 4 HOH   239 739 481 HOH   HOH A . 
G 4 HOH   240 740 404 HOH   HOH A . 
G 4 HOH   241 741 571 HOH   HOH A . 
G 4 HOH   242 742 508 HOH   HOH A . 
G 4 HOH   243 743 395 HOH   HOH A . 
G 4 HOH   244 744 569 HOH   HOH A . 
G 4 HOH   245 745 502 HOH   HOH A . 
G 4 HOH   246 746 188 HOH   HOH A . 
G 4 HOH   247 747 575 HOH   HOH A . 
G 4 HOH   248 748 447 HOH   HOH A . 
G 4 HOH   249 749 403 HOH   HOH A . 
G 4 HOH   250 750 545 HOH   HOH A . 
G 4 HOH   251 751 461 HOH   HOH A . 
G 4 HOH   252 752 489 HOH   HOH A . 
G 4 HOH   253 753 518 HOH   HOH A . 
G 4 HOH   254 754 397 HOH   HOH A . 
G 4 HOH   255 755 419 HOH   HOH A . 
G 4 HOH   256 756 470 HOH   HOH A . 
G 4 HOH   257 757 321 HOH   HOH A . 
G 4 HOH   258 758 361 HOH   HOH A . 
G 4 HOH   259 759 540 HOH   HOH A . 
G 4 HOH   260 760 389 HOH   HOH A . 
G 4 HOH   261 761 205 HOH   HOH A . 
G 4 HOH   262 762 463 HOH   HOH A . 
G 4 HOH   263 763 273 HOH   HOH A . 
G 4 HOH   264 764 112 HOH   HOH A . 
G 4 HOH   265 765 307 HOH   HOH A . 
G 4 HOH   266 766 596 HOH   HOH A . 
G 4 HOH   267 767 132 HOH   HOH A . 
G 4 HOH   268 768 570 HOH   HOH A . 
G 4 HOH   269 769 394 HOH   HOH A . 
G 4 HOH   270 770 519 HOH   HOH A . 
G 4 HOH   271 771 156 HOH   HOH A . 
G 4 HOH   272 772 482 HOH   HOH A . 
G 4 HOH   273 773 370 HOH   HOH A . 
G 4 HOH   274 774 561 HOH   HOH A . 
G 4 HOH   275 775 207 HOH   HOH A . 
G 4 HOH   276 776 513 HOH   HOH A . 
G 4 HOH   277 777 251 HOH   HOH A . 
G 4 HOH   278 778 246 HOH   HOH A . 
G 4 HOH   279 779 597 HOH   HOH A . 
G 4 HOH   280 780 288 HOH   HOH A . 
G 4 HOH   281 781 494 HOH   HOH A . 
G 4 HOH   282 782 181 HOH   HOH A . 
G 4 HOH   283 783 566 HOH   HOH A . 
G 4 HOH   284 784 297 HOH   HOH A . 
G 4 HOH   285 785 539 HOH   HOH A . 
G 4 HOH   286 786 85  HOH   HOH A . 
G 4 HOH   287 787 341 HOH   HOH A . 
G 4 HOH   288 788 522 HOH   HOH A . 
G 4 HOH   289 789 458 HOH   HOH A . 
G 4 HOH   290 790 254 HOH   HOH A . 
G 4 HOH   291 791 454 HOH   HOH A . 
G 4 HOH   292 792 504 HOH   HOH A . 
G 4 HOH   293 793 317 HOH   HOH A . 
G 4 HOH   294 794 115 HOH   HOH A . 
G 4 HOH   295 795 275 HOH   HOH A . 
G 4 HOH   296 796 237 HOH   HOH A . 
G 4 HOH   297 797 430 HOH   HOH A . 
G 4 HOH   298 798 559 HOH   HOH A . 
G 4 HOH   299 799 298 HOH   HOH A . 
G 4 HOH   300 800 498 HOH   HOH A . 
G 4 HOH   301 801 509 HOH   HOH A . 
G 4 HOH   302 802 357 HOH   HOH A . 
G 4 HOH   303 803 124 HOH   HOH A . 
G 4 HOH   304 804 191 HOH   HOH A . 
G 4 HOH   305 805 576 HOH   HOH A . 
G 4 HOH   306 806 354 HOH   HOH A . 
G 4 HOH   307 807 453 HOH   HOH A . 
G 4 HOH   308 808 331 HOH   HOH A . 
H 4 HOH   1   501 234 HOH   HOH B . 
H 4 HOH   2   502 535 HOH   HOH B . 
H 4 HOH   3   503 398 HOH   HOH B . 
H 4 HOH   4   504 226 HOH   HOH B . 
H 4 HOH   5   505 29  HOH   HOH B . 
H 4 HOH   6   506 130 HOH   HOH B . 
H 4 HOH   7   507 255 HOH   HOH B . 
H 4 HOH   8   508 73  HOH   HOH B . 
H 4 HOH   9   509 240 HOH   HOH B . 
H 4 HOH   10  510 161 HOH   HOH B . 
H 4 HOH   11  511 230 HOH   HOH B . 
H 4 HOH   12  512 239 HOH   HOH B . 
H 4 HOH   13  513 587 HOH   HOH B . 
H 4 HOH   14  514 81  HOH   HOH B . 
H 4 HOH   15  515 283 HOH   HOH B . 
H 4 HOH   16  516 136 HOH   HOH B . 
H 4 HOH   17  517 141 HOH   HOH B . 
H 4 HOH   18  518 42  HOH   HOH B . 
H 4 HOH   19  519 329 HOH   HOH B . 
H 4 HOH   20  520 316 HOH   HOH B . 
H 4 HOH   21  521 318 HOH   HOH B . 
H 4 HOH   22  522 375 HOH   HOH B . 
H 4 HOH   23  523 511 HOH   HOH B . 
H 4 HOH   24  524 199 HOH   HOH B . 
H 4 HOH   25  525 11  HOH   HOH B . 
H 4 HOH   26  526 594 HOH   HOH B . 
H 4 HOH   27  527 294 HOH   HOH B . 
H 4 HOH   28  528 215 HOH   HOH B . 
H 4 HOH   29  529 223 HOH   HOH B . 
H 4 HOH   30  530 5   HOH   HOH B . 
H 4 HOH   31  531 180 HOH   HOH B . 
H 4 HOH   32  532 51  HOH   HOH B . 
H 4 HOH   33  533 435 HOH   HOH B . 
H 4 HOH   34  534 133 HOH   HOH B . 
H 4 HOH   35  535 57  HOH   HOH B . 
H 4 HOH   36  536 44  HOH   HOH B . 
H 4 HOH   37  537 33  HOH   HOH B . 
H 4 HOH   38  538 36  HOH   HOH B . 
H 4 HOH   39  539 507 HOH   HOH B . 
H 4 HOH   40  540 49  HOH   HOH B . 
H 4 HOH   41  541 536 HOH   HOH B . 
H 4 HOH   42  542 490 HOH   HOH B . 
H 4 HOH   43  543 259 HOH   HOH B . 
H 4 HOH   44  544 327 HOH   HOH B . 
H 4 HOH   45  545 414 HOH   HOH B . 
H 4 HOH   46  546 439 HOH   HOH B . 
H 4 HOH   47  547 222 HOH   HOH B . 
H 4 HOH   48  548 174 HOH   HOH B . 
H 4 HOH   49  549 500 HOH   HOH B . 
H 4 HOH   50  550 95  HOH   HOH B . 
H 4 HOH   51  551 6   HOH   HOH B . 
H 4 HOH   52  552 210 HOH   HOH B . 
H 4 HOH   53  553 474 HOH   HOH B . 
H 4 HOH   54  554 457 HOH   HOH B . 
H 4 HOH   55  555 595 HOH   HOH B . 
H 4 HOH   56  556 183 HOH   HOH B . 
H 4 HOH   57  557 262 HOH   HOH B . 
H 4 HOH   58  558 162 HOH   HOH B . 
H 4 HOH   59  559 45  HOH   HOH B . 
H 4 HOH   60  560 355 HOH   HOH B . 
H 4 HOH   61  561 47  HOH   HOH B . 
H 4 HOH   62  562 312 HOH   HOH B . 
H 4 HOH   63  563 483 HOH   HOH B . 
H 4 HOH   64  564 198 HOH   HOH B . 
H 4 HOH   65  565 448 HOH   HOH B . 
H 4 HOH   66  566 71  HOH   HOH B . 
H 4 HOH   67  567 38  HOH   HOH B . 
H 4 HOH   68  568 345 HOH   HOH B . 
H 4 HOH   69  569 418 HOH   HOH B . 
H 4 HOH   70  570 583 HOH   HOH B . 
H 4 HOH   71  571 13  HOH   HOH B . 
H 4 HOH   72  572 462 HOH   HOH B . 
H 4 HOH   73  573 412 HOH   HOH B . 
H 4 HOH   74  574 23  HOH   HOH B . 
H 4 HOH   75  575 105 HOH   HOH B . 
H 4 HOH   76  576 177 HOH   HOH B . 
H 4 HOH   77  577 59  HOH   HOH B . 
H 4 HOH   78  578 75  HOH   HOH B . 
H 4 HOH   79  579 160 HOH   HOH B . 
H 4 HOH   80  580 359 HOH   HOH B . 
H 4 HOH   81  581 268 HOH   HOH B . 
H 4 HOH   82  582 229 HOH   HOH B . 
H 4 HOH   83  583 46  HOH   HOH B . 
H 4 HOH   84  584 196 HOH   HOH B . 
H 4 HOH   85  585 549 HOH   HOH B . 
H 4 HOH   86  586 266 HOH   HOH B . 
H 4 HOH   87  587 281 HOH   HOH B . 
H 4 HOH   88  588 48  HOH   HOH B . 
H 4 HOH   89  589 166 HOH   HOH B . 
H 4 HOH   90  590 424 HOH   HOH B . 
H 4 HOH   91  591 3   HOH   HOH B . 
H 4 HOH   92  592 65  HOH   HOH B . 
H 4 HOH   93  593 274 HOH   HOH B . 
H 4 HOH   94  594 100 HOH   HOH B . 
H 4 HOH   95  595 69  HOH   HOH B . 
H 4 HOH   96  596 144 HOH   HOH B . 
H 4 HOH   97  597 10  HOH   HOH B . 
H 4 HOH   98  598 353 HOH   HOH B . 
H 4 HOH   99  599 175 HOH   HOH B . 
H 4 HOH   100 600 20  HOH   HOH B . 
H 4 HOH   101 601 446 HOH   HOH B . 
H 4 HOH   102 602 249 HOH   HOH B . 
H 4 HOH   103 603 468 HOH   HOH B . 
H 4 HOH   104 604 326 HOH   HOH B . 
H 4 HOH   105 605 285 HOH   HOH B . 
H 4 HOH   106 606 325 HOH   HOH B . 
H 4 HOH   107 607 334 HOH   HOH B . 
H 4 HOH   108 608 534 HOH   HOH B . 
H 4 HOH   109 609 17  HOH   HOH B . 
H 4 HOH   110 610 12  HOH   HOH B . 
H 4 HOH   111 611 116 HOH   HOH B . 
H 4 HOH   112 612 407 HOH   HOH B . 
H 4 HOH   113 613 592 HOH   HOH B . 
H 4 HOH   114 614 120 HOH   HOH B . 
H 4 HOH   115 615 66  HOH   HOH B . 
H 4 HOH   116 616 32  HOH   HOH B . 
H 4 HOH   117 617 21  HOH   HOH B . 
H 4 HOH   118 618 380 HOH   HOH B . 
H 4 HOH   119 619 163 HOH   HOH B . 
H 4 HOH   120 620 467 HOH   HOH B . 
H 4 HOH   121 621 529 HOH   HOH B . 
H 4 HOH   122 622 590 HOH   HOH B . 
H 4 HOH   123 623 125 HOH   HOH B . 
H 4 HOH   124 624 338 HOH   HOH B . 
H 4 HOH   125 625 55  HOH   HOH B . 
H 4 HOH   126 626 131 HOH   HOH B . 
H 4 HOH   127 627 488 HOH   HOH B . 
H 4 HOH   128 628 347 HOH   HOH B . 
H 4 HOH   129 629 528 HOH   HOH B . 
H 4 HOH   130 630 9   HOH   HOH B . 
H 4 HOH   131 631 356 HOH   HOH B . 
H 4 HOH   132 632 14  HOH   HOH B . 
H 4 HOH   133 633 291 HOH   HOH B . 
H 4 HOH   134 634 225 HOH   HOH B . 
H 4 HOH   135 635 54  HOH   HOH B . 
H 4 HOH   136 636 61  HOH   HOH B . 
H 4 HOH   137 637 495 HOH   HOH B . 
H 4 HOH   138 638 68  HOH   HOH B . 
H 4 HOH   139 639 41  HOH   HOH B . 
H 4 HOH   140 640 170 HOH   HOH B . 
H 4 HOH   141 641 64  HOH   HOH B . 
H 4 HOH   142 642 371 HOH   HOH B . 
H 4 HOH   143 643 581 HOH   HOH B . 
H 4 HOH   144 644 270 HOH   HOH B . 
H 4 HOH   145 645 110 HOH   HOH B . 
H 4 HOH   146 646 220 HOH   HOH B . 
H 4 HOH   147 647 373 HOH   HOH B . 
H 4 HOH   148 648 544 HOH   HOH B . 
H 4 HOH   149 649 139 HOH   HOH B . 
H 4 HOH   150 650 212 HOH   HOH B . 
H 4 HOH   151 651 442 HOH   HOH B . 
H 4 HOH   152 652 96  HOH   HOH B . 
H 4 HOH   153 653 278 HOH   HOH B . 
H 4 HOH   154 654 190 HOH   HOH B . 
H 4 HOH   155 655 560 HOH   HOH B . 
H 4 HOH   156 656 155 HOH   HOH B . 
H 4 HOH   157 657 137 HOH   HOH B . 
H 4 HOH   158 658 315 HOH   HOH B . 
H 4 HOH   159 659 118 HOH   HOH B . 
H 4 HOH   160 660 90  HOH   HOH B . 
H 4 HOH   161 661 589 HOH   HOH B . 
H 4 HOH   162 662 290 HOH   HOH B . 
H 4 HOH   163 663 302 HOH   HOH B . 
H 4 HOH   164 664 123 HOH   HOH B . 
H 4 HOH   165 665 541 HOH   HOH B . 
H 4 HOH   166 666 58  HOH   HOH B . 
H 4 HOH   167 667 537 HOH   HOH B . 
H 4 HOH   168 668 286 HOH   HOH B . 
H 4 HOH   169 669 101 HOH   HOH B . 
H 4 HOH   170 670 336 HOH   HOH B . 
H 4 HOH   171 671 350 HOH   HOH B . 
H 4 HOH   172 672 247 HOH   HOH B . 
H 4 HOH   173 673 147 HOH   HOH B . 
H 4 HOH   174 674 167 HOH   HOH B . 
H 4 HOH   175 675 52  HOH   HOH B . 
H 4 HOH   176 676 257 HOH   HOH B . 
H 4 HOH   177 677 598 HOH   HOH B . 
H 4 HOH   178 678 287 HOH   HOH B . 
H 4 HOH   179 679 497 HOH   HOH B . 
H 4 HOH   180 680 425 HOH   HOH B . 
H 4 HOH   181 681 250 HOH   HOH B . 
H 4 HOH   182 682 374 HOH   HOH B . 
H 4 HOH   183 683 428 HOH   HOH B . 
H 4 HOH   184 684 417 HOH   HOH B . 
H 4 HOH   185 685 24  HOH   HOH B . 
H 4 HOH   186 686 34  HOH   HOH B . 
H 4 HOH   187 687 478 HOH   HOH B . 
H 4 HOH   188 688 451 HOH   HOH B . 
H 4 HOH   189 689 18  HOH   HOH B . 
H 4 HOH   190 690 547 HOH   HOH B . 
H 4 HOH   191 691 526 HOH   HOH B . 
H 4 HOH   192 692 351 HOH   HOH B . 
H 4 HOH   193 693 186 HOH   HOH B . 
H 4 HOH   194 694 405 HOH   HOH B . 
H 4 HOH   195 695 79  HOH   HOH B . 
H 4 HOH   196 696 184 HOH   HOH B . 
H 4 HOH   197 697 343 HOH   HOH B . 
H 4 HOH   198 698 433 HOH   HOH B . 
H 4 HOH   199 699 292 HOH   HOH B . 
H 4 HOH   200 700 129 HOH   HOH B . 
H 4 HOH   201 701 368 HOH   HOH B . 
H 4 HOH   202 702 56  HOH   HOH B . 
H 4 HOH   203 703 533 HOH   HOH B . 
H 4 HOH   204 704 92  HOH   HOH B . 
H 4 HOH   205 705 523 HOH   HOH B . 
H 4 HOH   206 706 267 HOH   HOH B . 
H 4 HOH   207 707 443 HOH   HOH B . 
H 4 HOH   208 708 209 HOH   HOH B . 
H 4 HOH   209 709 121 HOH   HOH B . 
H 4 HOH   210 710 431 HOH   HOH B . 
H 4 HOH   211 711 391 HOH   HOH B . 
H 4 HOH   212 712 388 HOH   HOH B . 
H 4 HOH   213 713 565 HOH   HOH B . 
H 4 HOH   214 714 516 HOH   HOH B . 
H 4 HOH   215 715 74  HOH   HOH B . 
H 4 HOH   216 716 306 HOH   HOH B . 
H 4 HOH   217 717 456 HOH   HOH B . 
H 4 HOH   218 718 577 HOH   HOH B . 
H 4 HOH   219 719 473 HOH   HOH B . 
H 4 HOH   220 720 422 HOH   HOH B . 
H 4 HOH   221 721 487 HOH   HOH B . 
H 4 HOH   222 722 492 HOH   HOH B . 
H 4 HOH   223 723 588 HOH   HOH B . 
H 4 HOH   224 724 172 HOH   HOH B . 
H 4 HOH   225 725 591 HOH   HOH B . 
H 4 HOH   226 726 399 HOH   HOH B . 
H 4 HOH   227 727 19  HOH   HOH B . 
H 4 HOH   228 728 525 HOH   HOH B . 
H 4 HOH   229 729 219 HOH   HOH B . 
H 4 HOH   230 730 548 HOH   HOH B . 
H 4 HOH   231 731 477 HOH   HOH B . 
H 4 HOH   232 732 295 HOH   HOH B . 
H 4 HOH   233 733 441 HOH   HOH B . 
H 4 HOH   234 734 408 HOH   HOH B . 
H 4 HOH   235 735 396 HOH   HOH B . 
H 4 HOH   236 736 493 HOH   HOH B . 
H 4 HOH   237 737 381 HOH   HOH B . 
H 4 HOH   238 738 582 HOH   HOH B . 
H 4 HOH   239 739 253 HOH   HOH B . 
H 4 HOH   240 740 554 HOH   HOH B . 
H 4 HOH   241 741 593 HOH   HOH B . 
H 4 HOH   242 742 558 HOH   HOH B . 
H 4 HOH   243 743 579 HOH   HOH B . 
H 4 HOH   244 744 586 HOH   HOH B . 
H 4 HOH   245 745 213 HOH   HOH B . 
H 4 HOH   246 746 553 HOH   HOH B . 
H 4 HOH   247 747 93  HOH   HOH B . 
H 4 HOH   248 748 401 HOH   HOH B . 
H 4 HOH   249 749 512 HOH   HOH B . 
H 4 HOH   250 750 339 HOH   HOH B . 
H 4 HOH   251 751 43  HOH   HOH B . 
H 4 HOH   252 752 517 HOH   HOH B . 
H 4 HOH   253 753 182 HOH   HOH B . 
H 4 HOH   254 754 276 HOH   HOH B . 
H 4 HOH   255 755 484 HOH   HOH B . 
H 4 HOH   256 756 377 HOH   HOH B . 
H 4 HOH   257 757 585 HOH   HOH B . 
H 4 HOH   258 758 201 HOH   HOH B . 
H 4 HOH   259 759 62  HOH   HOH B . 
H 4 HOH   260 760 578 HOH   HOH B . 
H 4 HOH   261 761 409 HOH   HOH B . 
H 4 HOH   262 762 472 HOH   HOH B . 
H 4 HOH   263 763 153 HOH   HOH B . 
H 4 HOH   264 764 427 HOH   HOH B . 
H 4 HOH   265 765 429 HOH   HOH B . 
H 4 HOH   266 766 584 HOH   HOH B . 
H 4 HOH   267 767 349 HOH   HOH B . 
H 4 HOH   268 768 568 HOH   HOH B . 
H 4 HOH   269 769 31  HOH   HOH B . 
H 4 HOH   270 770 146 HOH   HOH B . 
H 4 HOH   271 771 557 HOH   HOH B . 
H 4 HOH   272 772 296 HOH   HOH B . 
H 4 HOH   273 773 434 HOH   HOH B . 
H 4 HOH   274 774 211 HOH   HOH B . 
H 4 HOH   275 775 437 HOH   HOH B . 
H 4 HOH   276 776 269 HOH   HOH B . 
H 4 HOH   277 777 445 HOH   HOH B . 
H 4 HOH   278 778 521 HOH   HOH B . 
H 4 HOH   279 779 402 HOH   HOH B . 
H 4 HOH   280 780 524 HOH   HOH B . 
H 4 HOH   281 781 221 HOH   HOH B . 
H 4 HOH   282 782 313 HOH   HOH B . 
H 4 HOH   283 783 376 HOH   HOH B . 
H 4 HOH   284 784 387 HOH   HOH B . 
H 4 HOH   285 785 464 HOH   HOH B . 
H 4 HOH   286 786 485 HOH   HOH B . 
H 4 HOH   287 787 555 HOH   HOH B . 
H 4 HOH   288 788 455 HOH   HOH B . 
H 4 HOH   289 789 340 HOH   HOH B . 
H 4 HOH   290 790 362 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(???)' 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .       2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .       3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .       4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .       5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JML 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.993 
_cell.length_a_esd                 ? 
_cell.length_b                     86.993 
_cell.length_b_esd                 ? 
_cell.length_c                     225.878 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9JML 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9JML 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.17 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;PEG3350,sodium chloride,bis-tris
hydrochloride
;
_exptl_crystal_grow.pdbx_pH_range   8.25-9.0 
_exptl_crystal_grow.temp            277.15 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-16 
_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                    Si111 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JML 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.02 
_reflns.d_resolution_low                               81.18 
_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                                     57683 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.9 
_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                                    2.02 
_reflns_shell.d_res_low                                     2.13 
_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                             8037 
_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                                  0.824 
_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                                 9JML 
_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                            2.02 
_refine.ls_d_res_low                             59.35 
_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                     57565 
_refine.ls_number_reflns_R_free                  2834 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1835 
_refine.ls_R_factor_R_free                       0.2231 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1814 
_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             1.10 
_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                 22.45 
_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                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.02 
_refine_hist.d_res_low                        59.35 
_refine_hist.number_atoms_solvent             598 
_refine_hist.number_atoms_total               6238 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5568 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 5782 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.910  ? 7866 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 20.070 ? 2232 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 858  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1004 ? 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' 2.02 2.05  . . 135 2494 93.00  . . . . 0.2324 . . . . . . . . . . . 0.3127 
'X-RAY DIFFRACTION' 2.05 2.09  . . 139 2630 98.00  . . . . 0.2239 . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 2.09 2.13  . . 133 2717 100.00 . . . . 0.2073 . . . . . . . . . . . 0.2406 
'X-RAY DIFFRACTION' 2.13 2.18  . . 140 2706 100.00 . . . . 0.2005 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 2.18 2.22  . . 119 2708 100.00 . . . . 0.1968 . . . . . . . . . . . 0.2628 
'X-RAY DIFFRACTION' 2.22 2.27  . . 142 2708 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2559 
'X-RAY DIFFRACTION' 2.27 2.33  . . 130 2719 100.00 . . . . 0.2018 . . . . . . . . . . . 0.2631 
'X-RAY DIFFRACTION' 2.33 2.39  . . 128 2723 100.00 . . . . 0.2044 . . . . . . . . . . . 0.2560 
'X-RAY DIFFRACTION' 2.39 2.47  . . 138 2736 100.00 . . . . 0.2100 . . . . . . . . . . . 0.2734 
'X-RAY DIFFRACTION' 2.47 2.54  . . 151 2702 100.00 . . . . 0.2061 . . . . . . . . . . . 0.2759 
'X-RAY DIFFRACTION' 2.54 2.64  . . 131 2760 100.00 . . . . 0.2045 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 2.64 2.74  . . 142 2721 100.00 . . . . 0.1996 . . . . . . . . . . . 0.2462 
'X-RAY DIFFRACTION' 2.74 2.87  . . 162 2713 100.00 . . . . 0.1940 . . . . . . . . . . . 0.2578 
'X-RAY DIFFRACTION' 2.87 3.02  . . 116 2769 100.00 . . . . 0.2068 . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 3.02 3.21  . . 154 2746 100.00 . . . . 0.1983 . . . . . . . . . . . 0.2603 
'X-RAY DIFFRACTION' 3.21 3.45  . . 154 2748 100.00 . . . . 0.1754 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 3.45 3.80  . . 142 2789 100.00 . . . . 0.1737 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 3.80 4.35  . . 146 2810 100.00 . . . . 0.1461 . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 4.35 5.48  . . 165 2832 100.00 . . . . 0.1434 . . . . . . . . . . . 0.1777 
'X-RAY DIFFRACTION' 5.48 59.35 . . 167 3000 99.00  . . . . 0.1702 . . . . . . . . . . . 0.1893 
# 
_struct.entry_id                     9JML 
_struct.title                        'NADP-dependent oxidoreductase complexed with NADP and substrate 1' 
_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        9JML 
_struct_keywords.text            'alcohol dehydrogenase, complex, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    C3PTT2_LYSEN 
_struct_ref.pdbx_db_accession          C3PTT2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGPNAP
FRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVRPGD
TVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDSIGG
SVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELVAHE
TVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JML A 4 ? 354 ? C3PTT2 1 ? 351 ? 1 351 
2 1 9JML B 4 ? 354 ? C3PTT2 1 ? 351 ? 1 351 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JML LEU A 1 ? UNP C3PTT2 ? ? 'expression tag' -2 1 
1 9JML GLY A 2 ? UNP C3PTT2 ? ? 'expression tag' -1 2 
1 9JML SER A 3 ? UNP C3PTT2 ? ? 'expression tag' 0  3 
2 9JML LEU B 1 ? UNP C3PTT2 ? ? 'expression tag' -2 4 
2 9JML GLY B 2 ? UNP C3PTT2 ? ? 'expression tag' -1 5 
2 9JML SER B 3 ? UNP C3PTT2 ? ? 'expression tag' 0  6 
# 
_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)' 6060  ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  27360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 20  ? ILE A 24  ? ASP A 17  ILE A 21  1 ? 5  
HELX_P HELX_P2  AA2 TYR A 53  ? ASP A 60  ? TYR A 50  ASP A 57  1 ? 8  
HELX_P HELX_P3  AA3 ASP A 125 ? TYR A 129 ? ASP A 122 TYR A 126 5 ? 5  
HELX_P HELX_P4  AA4 PRO A 134 ? GLY A 140 ? PRO A 131 GLY A 137 5 ? 7  
HELX_P HELX_P5  AA5 GLY A 143 ? PHE A 156 ? GLY A 140 PHE A 153 1 ? 14 
HELX_P HELX_P6  AA6 GLY A 172 ? ALA A 185 ? GLY A 169 ALA A 182 1 ? 14 
HELX_P HELX_P7  AA7 SER A 195 ? LEU A 205 ? SER A 192 LEU A 202 1 ? 11 
HELX_P HELX_P8  AA8 ASP A 218 ? ALA A 230 ? ASP A 215 ALA A 227 1 ? 13 
HELX_P HELX_P9  AA9 GLY A 242 ? SER A 251 ? GLY A 239 SER A 248 1 ? 10 
HELX_P HELX_P10 AB1 GLN A 264 ? VAL A 269 ? GLN A 261 VAL A 266 1 ? 6  
HELX_P HELX_P11 AB2 LEU A 278 ? ILE A 282 ? LEU A 275 ILE A 279 5 ? 5  
HELX_P HELX_P12 AB3 PHE A 293 ? PHE A 298 ? PHE A 290 PHE A 295 5 ? 6  
HELX_P HELX_P13 AB4 THR A 299 ? ARG A 316 ? THR A 296 ARG A 313 1 ? 18 
HELX_P HELX_P14 AB5 HIS A 331 ? ALA A 342 ? HIS A 328 ALA A 339 1 ? 12 
HELX_P HELX_P15 AB6 ASP B 20  ? ILE B 24  ? ASP B 17  ILE B 21  1 ? 5  
HELX_P HELX_P16 AB7 TYR B 53  ? ASP B 60  ? TYR B 50  ASP B 57  1 ? 8  
HELX_P HELX_P17 AB8 ASP B 125 ? TYR B 129 ? ASP B 122 TYR B 126 5 ? 5  
HELX_P HELX_P18 AB9 PRO B 134 ? GLY B 140 ? PRO B 131 GLY B 137 5 ? 7  
HELX_P HELX_P19 AC1 GLY B 143 ? PHE B 156 ? GLY B 140 PHE B 153 1 ? 14 
HELX_P HELX_P20 AC2 GLY B 172 ? ALA B 185 ? GLY B 169 ALA B 182 1 ? 14 
HELX_P HELX_P21 AC3 SER B 195 ? GLN B 204 ? SER B 192 GLN B 201 1 ? 10 
HELX_P HELX_P22 AC4 ASP B 218 ? ALA B 230 ? ASP B 215 ALA B 227 1 ? 13 
HELX_P HELX_P23 AC5 GLY B 242 ? SER B 251 ? GLY B 239 SER B 248 1 ? 10 
HELX_P HELX_P24 AC6 GLN B 264 ? VAL B 269 ? GLN B 261 VAL B 266 1 ? 6  
HELX_P HELX_P25 AC7 LEU B 278 ? ILE B 282 ? LEU B 275 ILE B 279 5 ? 5  
HELX_P HELX_P26 AC8 PHE B 293 ? PHE B 298 ? PHE B 290 PHE B 295 5 ? 6  
HELX_P HELX_P27 AC9 THR B 299 ? ARG B 316 ? THR B 296 ARG B 313 1 ? 18 
HELX_P HELX_P28 AD1 HIS B 331 ? ALA B 342 ? HIS B 328 ALA B 339 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 5  ? 
AA3 ? 4  ? 
AA4 ? 2  ? 
AA5 ? 12 ? 
AA6 ? 2  ? 
AA7 ? 2  ? 
AA8 ? 5  ? 
AA9 ? 4  ? 
AB1 ? 2  ? 
# 
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 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? parallel      
AA4 1  2  ? anti-parallel 
AA5 1  2  ? parallel      
AA5 2  3  ? parallel      
AA5 3  4  ? parallel      
AA5 4  5  ? parallel      
AA5 5  6  ? parallel      
AA5 6  7  ? anti-parallel 
AA5 7  8  ? parallel      
AA5 8  9  ? parallel      
AA5 9  10 ? parallel      
AA5 10 11 ? parallel      
AA5 11 12 ? parallel      
AA6 1  2  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA8 1  2  ? anti-parallel 
AA8 2  3  ? anti-parallel 
AA8 3  4  ? anti-parallel 
AA8 4  5  ? anti-parallel 
AA9 1  2  ? anti-parallel 
AA9 2  3  ? anti-parallel 
AA9 3  4  ? parallel      
AB1 1  2  ? 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  SER A 3   ? VAL A 11  ? SER A 0   VAL A 8   
AA1 2  TYR A 25  ? ASN A 33  ? TYR A 22  ASN A 30  
AA2 1  HIS A 99  ? SER A 102 ? HIS A 96  SER A 99  
AA2 2  MET A 41  ? SER A 49  ? MET A 38  SER A 46  
AA2 3  SER A 71  ? ALA A 78  ? SER A 68  ALA A 75  
AA2 4  LEU A 89  ? GLY A 92  ? LEU A 86  GLY A 89  
AA2 5  ARG A 122 ? LEU A 124 ? ARG A 119 LEU A 121 
AA3 1  HIS A 99  ? SER A 102 ? HIS A 96  SER A 99  
AA3 2  MET A 41  ? SER A 49  ? MET A 38  SER A 46  
AA3 3  LYS A 349 ? ARG A 353 ? LYS A 346 ARG A 350 
AA3 4  GLU A 323 ? ASP A 327 ? GLU A 320 ASP A 324 
AA4 1  LYS A 107 ? LEU A 108 ? LYS A 104 LEU A 105 
AA4 2  VAL A 117 ? PHE A 118 ? VAL A 114 PHE A 115 
AA5 1  ALA A 209 ? ASP A 212 ? ALA A 206 ASP A 209 
AA5 2  ARG A 188 ? ALA A 193 ? ARG A 185 ALA A 190 
AA5 3  THR A 164 ? VAL A 167 ? THR A 161 VAL A 164 
AA5 4  VAL A 234 ? ASP A 239 ? VAL A 231 ASP A 236 
AA5 5  LEU A 253 ? VAL A 261 ? LEU A 250 VAL A 258 
AA5 6  THR A 288 ? GLY A 291 ? THR A 285 GLY A 288 
AA5 7  THR B 288 ? GLY B 291 ? THR B 285 GLY B 288 
AA5 8  LEU B 253 ? VAL B 261 ? LEU B 250 VAL B 258 
AA5 9  VAL B 234 ? ASP B 239 ? VAL B 231 ASP B 236 
AA5 10 THR B 164 ? VAL B 167 ? THR B 161 VAL B 164 
AA5 11 ARG B 188 ? ALA B 193 ? ARG B 185 ALA B 190 
AA5 12 ALA B 209 ? ASP B 212 ? ALA B 206 ASP B 209 
AA6 1  HIS A 274 ? PRO A 276 ? HIS A 271 PRO A 273 
AA6 2  HIS B 274 ? PRO B 276 ? HIS B 271 PRO B 273 
AA7 1  SER B 3   ? VAL B 11  ? SER B 0   VAL B 8   
AA7 2  TYR B 25  ? ASN B 33  ? TYR B 22  ASN B 30  
AA8 1  HIS B 99  ? SER B 102 ? HIS B 96  SER B 99  
AA8 2  MET B 41  ? SER B 49  ? MET B 38  SER B 46  
AA8 3  SER B 71  ? ALA B 78  ? SER B 68  ALA B 75  
AA8 4  LEU B 89  ? GLY B 92  ? LEU B 86  GLY B 89  
AA8 5  ARG B 122 ? LEU B 124 ? ARG B 119 LEU B 121 
AA9 1  HIS B 99  ? SER B 102 ? HIS B 96  SER B 99  
AA9 2  MET B 41  ? SER B 49  ? MET B 38  SER B 46  
AA9 3  LYS B 349 ? ARG B 353 ? LYS B 346 ARG B 350 
AA9 4  GLU B 323 ? ASP B 327 ? GLU B 320 ASP B 324 
AB1 1  LYS B 107 ? LEU B 108 ? LYS B 104 LEU B 105 
AB1 2  VAL B 117 ? PHE B 118 ? VAL B 114 PHE B 115 
# 
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 THR A 6   ? N THR A 3   O THR A 30  ? O THR A 27  
AA2 1  2  O LEU A 100 ? O LEU A 97  N LEU A 43  ? N LEU A 40  
AA2 2  3  N LEU A 42  ? N LEU A 39  O LEU A 76  ? O LEU A 73  
AA2 3  4  N MET A 73  ? N MET A 70  O VAL A 90  ? O VAL A 87  
AA2 4  5  N GLN A 91  ? N GLN A 88  O ARG A 122 ? O ARG A 119 
AA3 1  2  O LEU A 100 ? O LEU A 97  N LEU A 43  ? N LEU A 40  
AA3 2  3  N VAL A 48  ? N VAL A 45  O VAL A 352 ? O VAL A 349 
AA3 3  4  O LYS A 349 ? O LYS A 346 N THR A 324 ? N THR A 321 
AA4 1  2  N LYS A 107 ? N LYS A 104 O PHE A 118 ? O PHE A 115 
AA5 1  2  O ILE A 211 ? O ILE A 208 N GLY A 191 ? N GLY A 188 
AA5 2  3  O ARG A 188 ? O ARG A 185 N VAL A 165 ? N VAL A 162 
AA5 3  4  N VAL A 166 ? N VAL A 163 O PHE A 238 ? O PHE A 235 
AA5 4  5  N ASP A 239 ? N ASP A 236 O ALA A 260 ? O ALA A 257 
AA5 5  6  N VAL A 259 ? N VAL A 256 O THR A 288 ? O THR A 285 
AA5 6  7  N ILE A 289 ? N ILE A 286 O ILE B 289 ? O ILE B 286 
AA5 7  8  O THR B 288 ? O THR B 285 N VAL B 259 ? N VAL B 256 
AA5 8  9  O ALA B 260 ? O ALA B 257 N ASP B 239 ? N ASP B 236 
AA5 9  10 O LYS B 236 ? O LYS B 233 N VAL B 166 ? N VAL B 163 
AA5 10 11 N VAL B 165 ? N VAL B 162 O ARG B 188 ? O ARG B 185 
AA5 11 12 N GLY B 191 ? N GLY B 188 O ILE B 211 ? O ILE B 208 
AA6 1  2  N GLY A 275 ? N GLY A 272 O GLY B 275 ? O GLY B 272 
AA7 1  2  N THR B 6   ? N THR B 3   O THR B 30  ? O THR B 27  
AA8 1  2  O SER B 102 ? O SER B 99  N MET B 41  ? N MET B 38  
AA8 2  3  N LEU B 46  ? N LEU B 43  O ILE B 72  ? O ILE B 69  
AA8 3  4  N MET B 73  ? N MET B 70  O VAL B 90  ? O VAL B 87  
AA8 4  5  N GLN B 91  ? N GLN B 88  O ARG B 122 ? O ARG B 119 
AA9 1  2  O SER B 102 ? O SER B 99  N MET B 41  ? N MET B 38  
AA9 2  3  N VAL B 48  ? N VAL B 45  O VAL B 352 ? O VAL B 349 
AA9 3  4  O ARG B 353 ? O ARG B 350 N GLN B 326 ? N GLN B 323 
AB1 1  2  N LYS B 107 ? N LYS B 104 O PHE B 118 ? O PHE B 115 
# 
_pdbx_entry_details.entry_id                   9JML 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 66  ? ? -178.05 149.19 
2 1 PHE A 153 ? ? -128.73 -65.03 
3 1 MET A 249 ? ? -143.14 31.97  
4 1 ALA A 339 ? ? -155.68 70.62  
5 1 PHE B 153 ? ? -132.81 -66.38 
6 1 MET B 249 ? ? -140.20 30.65  
7 1 GLN B 314 ? ? 59.36   16.09  
8 1 ALA B 339 ? ? -156.96 56.52  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       790 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.26 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1EDK C8   C N R 1   
A1EDK C5   C N N 2   
A1EDK C6   C N S 3   
A1EDK N1   N N N 4   
A1EDK C2   C N N 5   
A1EDK C4   C N S 6   
A1EDK C21  C N N 7   
A1EDK C23  C N N 8   
A1EDK C24  C N N 9   
A1EDK C25  C N N 10  
A1EDK C27  C N N 11  
A1EDK C29  C N N 12  
A1EDK C1   C N N 13  
A1EDK C10  C N N 14  
A1EDK C11  C N N 15  
A1EDK C12  C N N 16  
A1EDK C13  C N N 17  
A1EDK C14  C N N 18  
A1EDK C15  C N N 19  
A1EDK C16  C N N 20  
A1EDK C17  C N S 21  
A1EDK C18  C N N 22  
A1EDK C19  C N N 23  
A1EDK C20  C N N 24  
A1EDK C22  C N N 25  
A1EDK C26  C N S 26  
A1EDK C28  C N R 27  
A1EDK C3   C N R 28  
A1EDK C7   C N R 29  
A1EDK C9   C N N 30  
A1EDK N2   N N N 31  
A1EDK O1   O N N 32  
A1EDK O2   O N N 33  
A1EDK O3   O N N 34  
A1EDK O4   O N N 35  
A1EDK O5   O N N 36  
A1EDK H1   H N N 37  
A1EDK H3   H N N 38  
A1EDK H4   H N N 39  
A1EDK H2   H N N 40  
A1EDK H5   H N N 41  
A1EDK H6   H N N 42  
A1EDK H7   H N N 43  
A1EDK H8   H N N 44  
A1EDK H9   H N N 45  
A1EDK H10  H N N 46  
A1EDK H12  H N N 47  
A1EDK H13  H N N 48  
A1EDK H15  H N N 49  
A1EDK H14  H N N 50  
A1EDK H16  H N N 51  
A1EDK H17  H N N 52  
A1EDK H20  H N N 53  
A1EDK H18  H N N 54  
A1EDK H19  H N N 55  
A1EDK H21  H N N 56  
A1EDK H22  H N N 57  
A1EDK H23  H N N 58  
A1EDK H25  H N N 59  
A1EDK H24  H N N 60  
A1EDK H27  H N N 61  
A1EDK H26  H N N 62  
A1EDK H29  H N N 63  
A1EDK H28  H N N 64  
A1EDK H30  H N N 65  
A1EDK H32  H N N 66  
A1EDK H33  H N N 67  
A1EDK H34  H N N 68  
A1EDK H35  H N N 69  
A1EDK H36  H N N 70  
A1EDK H37  H N N 71  
A1EDK H38  H N N 72  
A1EDK H39  H N N 73  
A1EDK H40  H N N 74  
ALA   N    N N N 75  
ALA   CA   C N S 76  
ALA   C    C N N 77  
ALA   O    O N N 78  
ALA   CB   C N N 79  
ALA   OXT  O N N 80  
ALA   H    H N N 81  
ALA   H2   H N N 82  
ALA   HA   H N N 83  
ALA   HB1  H N N 84  
ALA   HB2  H N N 85  
ALA   HB3  H N N 86  
ALA   HXT  H N N 87  
ARG   N    N N N 88  
ARG   CA   C N S 89  
ARG   C    C N N 90  
ARG   O    O N N 91  
ARG   CB   C N N 92  
ARG   CG   C N N 93  
ARG   CD   C N N 94  
ARG   NE   N N N 95  
ARG   CZ   C N N 96  
ARG   NH1  N N N 97  
ARG   NH2  N N N 98  
ARG   OXT  O N N 99  
ARG   H    H N N 100 
ARG   H2   H N N 101 
ARG   HA   H N N 102 
ARG   HB2  H N N 103 
ARG   HB3  H N N 104 
ARG   HG2  H N N 105 
ARG   HG3  H N N 106 
ARG   HD2  H N N 107 
ARG   HD3  H N N 108 
ARG   HE   H N N 109 
ARG   HH11 H N N 110 
ARG   HH12 H N N 111 
ARG   HH21 H N N 112 
ARG   HH22 H N N 113 
ARG   HXT  H N N 114 
ASN   N    N N N 115 
ASN   CA   C N S 116 
ASN   C    C N N 117 
ASN   O    O N N 118 
ASN   CB   C N N 119 
ASN   CG   C N N 120 
ASN   OD1  O N N 121 
ASN   ND2  N N N 122 
ASN   OXT  O N N 123 
ASN   H    H N N 124 
ASN   H2   H N N 125 
ASN   HA   H N N 126 
ASN   HB2  H N N 127 
ASN   HB3  H N N 128 
ASN   HD21 H N N 129 
ASN   HD22 H N N 130 
ASN   HXT  H N N 131 
ASP   N    N N N 132 
ASP   CA   C N S 133 
ASP   C    C N N 134 
ASP   O    O N N 135 
ASP   CB   C N N 136 
ASP   CG   C N N 137 
ASP   OD1  O N N 138 
ASP   OD2  O N N 139 
ASP   OXT  O N N 140 
ASP   H    H N N 141 
ASP   H2   H N N 142 
ASP   HA   H N N 143 
ASP   HB2  H N N 144 
ASP   HB3  H N N 145 
ASP   HD2  H N N 146 
ASP   HXT  H N N 147 
CYS   N    N N N 148 
CYS   CA   C N R 149 
CYS   C    C N N 150 
CYS   O    O N N 151 
CYS   CB   C N N 152 
CYS   SG   S N N 153 
CYS   OXT  O N N 154 
CYS   H    H N N 155 
CYS   H2   H N N 156 
CYS   HA   H N N 157 
CYS   HB2  H N N 158 
CYS   HB3  H N N 159 
CYS   HG   H N N 160 
CYS   HXT  H N N 161 
GLN   N    N N N 162 
GLN   CA   C N S 163 
GLN   C    C N N 164 
GLN   O    O N N 165 
GLN   CB   C N N 166 
GLN   CG   C N N 167 
GLN   CD   C N N 168 
GLN   OE1  O N N 169 
GLN   NE2  N N N 170 
GLN   OXT  O N N 171 
GLN   H    H N N 172 
GLN   H2   H N N 173 
GLN   HA   H N N 174 
GLN   HB2  H N N 175 
GLN   HB3  H N N 176 
GLN   HG2  H N N 177 
GLN   HG3  H N N 178 
GLN   HE21 H N N 179 
GLN   HE22 H N N 180 
GLN   HXT  H N N 181 
GLU   N    N N N 182 
GLU   CA   C N S 183 
GLU   C    C N N 184 
GLU   O    O N N 185 
GLU   CB   C N N 186 
GLU   CG   C N N 187 
GLU   CD   C N N 188 
GLU   OE1  O N N 189 
GLU   OE2  O N N 190 
GLU   OXT  O N N 191 
GLU   H    H N N 192 
GLU   H2   H N N 193 
GLU   HA   H N N 194 
GLU   HB2  H N N 195 
GLU   HB3  H N N 196 
GLU   HG2  H N N 197 
GLU   HG3  H N N 198 
GLU   HE2  H N N 199 
GLU   HXT  H N N 200 
GLY   N    N N N 201 
GLY   CA   C N N 202 
GLY   C    C N N 203 
GLY   O    O N N 204 
GLY   OXT  O N N 205 
GLY   H    H N N 206 
GLY   H2   H N N 207 
GLY   HA2  H N N 208 
GLY   HA3  H N N 209 
GLY   HXT  H N N 210 
HIS   N    N N N 211 
HIS   CA   C N S 212 
HIS   C    C N N 213 
HIS   O    O N N 214 
HIS   CB   C N N 215 
HIS   CG   C Y N 216 
HIS   ND1  N Y N 217 
HIS   CD2  C Y N 218 
HIS   CE1  C Y N 219 
HIS   NE2  N Y N 220 
HIS   OXT  O N N 221 
HIS   H    H N N 222 
HIS   H2   H N N 223 
HIS   HA   H N N 224 
HIS   HB2  H N N 225 
HIS   HB3  H N N 226 
HIS   HD1  H N N 227 
HIS   HD2  H N N 228 
HIS   HE1  H N N 229 
HIS   HE2  H N N 230 
HIS   HXT  H N N 231 
HOH   O    O N N 232 
HOH   H1   H N N 233 
HOH   H2   H N N 234 
ILE   N    N N N 235 
ILE   CA   C N S 236 
ILE   C    C N N 237 
ILE   O    O N N 238 
ILE   CB   C N S 239 
ILE   CG1  C N N 240 
ILE   CG2  C N N 241 
ILE   CD1  C N N 242 
ILE   OXT  O N N 243 
ILE   H    H N N 244 
ILE   H2   H N N 245 
ILE   HA   H N N 246 
ILE   HB   H N N 247 
ILE   HG12 H N N 248 
ILE   HG13 H N N 249 
ILE   HG21 H N N 250 
ILE   HG22 H N N 251 
ILE   HG23 H N N 252 
ILE   HD11 H N N 253 
ILE   HD12 H N N 254 
ILE   HD13 H N N 255 
ILE   HXT  H N N 256 
LEU   N    N N N 257 
LEU   CA   C N S 258 
LEU   C    C N N 259 
LEU   O    O N N 260 
LEU   CB   C N N 261 
LEU   CG   C N N 262 
LEU   CD1  C N N 263 
LEU   CD2  C N N 264 
LEU   OXT  O N N 265 
LEU   H    H N N 266 
LEU   H2   H N N 267 
LEU   HA   H N N 268 
LEU   HB2  H N N 269 
LEU   HB3  H N N 270 
LEU   HG   H N N 271 
LEU   HD11 H N N 272 
LEU   HD12 H N N 273 
LEU   HD13 H N N 274 
LEU   HD21 H N N 275 
LEU   HD22 H N N 276 
LEU   HD23 H N N 277 
LEU   HXT  H N N 278 
LYS   N    N N N 279 
LYS   CA   C N S 280 
LYS   C    C N N 281 
LYS   O    O N N 282 
LYS   CB   C N N 283 
LYS   CG   C N N 284 
LYS   CD   C N N 285 
LYS   CE   C N N 286 
LYS   NZ   N N N 287 
LYS   OXT  O N N 288 
LYS   H    H N N 289 
LYS   H2   H N N 290 
LYS   HA   H N N 291 
LYS   HB2  H N N 292 
LYS   HB3  H N N 293 
LYS   HG2  H N N 294 
LYS   HG3  H N N 295 
LYS   HD2  H N N 296 
LYS   HD3  H N N 297 
LYS   HE2  H N N 298 
LYS   HE3  H N N 299 
LYS   HZ1  H N N 300 
LYS   HZ2  H N N 301 
LYS   HZ3  H N N 302 
LYS   HXT  H N N 303 
MET   N    N N N 304 
MET   CA   C N S 305 
MET   C    C N N 306 
MET   O    O N N 307 
MET   CB   C N N 308 
MET   CG   C N N 309 
MET   SD   S N N 310 
MET   CE   C N N 311 
MET   OXT  O N N 312 
MET   H    H N N 313 
MET   H2   H N N 314 
MET   HA   H N N 315 
MET   HB2  H N N 316 
MET   HB3  H N N 317 
MET   HG2  H N N 318 
MET   HG3  H N N 319 
MET   HE1  H N N 320 
MET   HE2  H N N 321 
MET   HE3  H N N 322 
MET   HXT  H N N 323 
NAP   PA   P N R 324 
NAP   O1A  O N N 325 
NAP   O2A  O N N 326 
NAP   O5B  O N N 327 
NAP   C5B  C N N 328 
NAP   C4B  C N R 329 
NAP   O4B  O N N 330 
NAP   C3B  C N R 331 
NAP   O3B  O N N 332 
NAP   C2B  C N R 333 
NAP   O2B  O N N 334 
NAP   C1B  C N R 335 
NAP   N9A  N Y N 336 
NAP   C8A  C Y N 337 
NAP   N7A  N Y N 338 
NAP   C5A  C Y N 339 
NAP   C6A  C Y N 340 
NAP   N6A  N N N 341 
NAP   N1A  N Y N 342 
NAP   C2A  C Y N 343 
NAP   N3A  N Y N 344 
NAP   C4A  C Y N 345 
NAP   O3   O N N 346 
NAP   PN   P N N 347 
NAP   O1N  O N N 348 
NAP   O2N  O N N 349 
NAP   O5D  O N N 350 
NAP   C5D  C N N 351 
NAP   C4D  C N R 352 
NAP   O4D  O N N 353 
NAP   C3D  C N S 354 
NAP   O3D  O N N 355 
NAP   C2D  C N R 356 
NAP   O2D  O N N 357 
NAP   C1D  C N R 358 
NAP   N1N  N Y N 359 
NAP   C2N  C Y N 360 
NAP   C3N  C Y N 361 
NAP   C7N  C N N 362 
NAP   O7N  O N N 363 
NAP   N7N  N N N 364 
NAP   C4N  C Y N 365 
NAP   C5N  C Y N 366 
NAP   C6N  C Y N 367 
NAP   P2B  P N N 368 
NAP   O1X  O N N 369 
NAP   O2X  O N N 370 
NAP   O3X  O N N 371 
NAP   HOA2 H N N 372 
NAP   H51A H N N 373 
NAP   H52A H N N 374 
NAP   H4B  H N N 375 
NAP   H3B  H N N 376 
NAP   HO3A H N N 377 
NAP   H2B  H N N 378 
NAP   H1B  H N N 379 
NAP   H8A  H N N 380 
NAP   H61A H N N 381 
NAP   H62A H N N 382 
NAP   H2A  H N N 383 
NAP   H51N H N N 384 
NAP   H52N H N N 385 
NAP   H4D  H N N 386 
NAP   H3D  H N N 387 
NAP   HO3N H N N 388 
NAP   H2D  H N N 389 
NAP   HO2N H N N 390 
NAP   H1D  H N N 391 
NAP   H2N  H N N 392 
NAP   H71N H N N 393 
NAP   H72N H N N 394 
NAP   H4N  H N N 395 
NAP   H5N  H N N 396 
NAP   H6N  H N N 397 
NAP   HOP2 H N N 398 
NAP   HOP3 H N N 399 
PHE   N    N N N 400 
PHE   CA   C N S 401 
PHE   C    C N N 402 
PHE   O    O N N 403 
PHE   CB   C N N 404 
PHE   CG   C Y N 405 
PHE   CD1  C Y N 406 
PHE   CD2  C Y N 407 
PHE   CE1  C Y N 408 
PHE   CE2  C Y N 409 
PHE   CZ   C Y N 410 
PHE   OXT  O N N 411 
PHE   H    H N N 412 
PHE   H2   H N N 413 
PHE   HA   H N N 414 
PHE   HB2  H N N 415 
PHE   HB3  H N N 416 
PHE   HD1  H N N 417 
PHE   HD2  H N N 418 
PHE   HE1  H N N 419 
PHE   HE2  H N N 420 
PHE   HZ   H N N 421 
PHE   HXT  H N N 422 
PRO   N    N N N 423 
PRO   CA   C N S 424 
PRO   C    C N N 425 
PRO   O    O N N 426 
PRO   CB   C N N 427 
PRO   CG   C N N 428 
PRO   CD   C N N 429 
PRO   OXT  O N N 430 
PRO   H    H N N 431 
PRO   HA   H N N 432 
PRO   HB2  H N N 433 
PRO   HB3  H N N 434 
PRO   HG2  H N N 435 
PRO   HG3  H N N 436 
PRO   HD2  H N N 437 
PRO   HD3  H N N 438 
PRO   HXT  H N N 439 
SER   N    N N N 440 
SER   CA   C N S 441 
SER   C    C N N 442 
SER   O    O N N 443 
SER   CB   C N N 444 
SER   OG   O N N 445 
SER   OXT  O N N 446 
SER   H    H N N 447 
SER   H2   H N N 448 
SER   HA   H N N 449 
SER   HB2  H N N 450 
SER   HB3  H N N 451 
SER   HG   H N N 452 
SER   HXT  H N N 453 
THR   N    N N N 454 
THR   CA   C N S 455 
THR   C    C N N 456 
THR   O    O N N 457 
THR   CB   C N R 458 
THR   OG1  O N N 459 
THR   CG2  C N N 460 
THR   OXT  O N N 461 
THR   H    H N N 462 
THR   H2   H N N 463 
THR   HA   H N N 464 
THR   HB   H N N 465 
THR   HG1  H N N 466 
THR   HG21 H N N 467 
THR   HG22 H N N 468 
THR   HG23 H N N 469 
THR   HXT  H N N 470 
TRP   N    N N N 471 
TRP   CA   C N S 472 
TRP   C    C N N 473 
TRP   O    O N N 474 
TRP   CB   C N N 475 
TRP   CG   C Y N 476 
TRP   CD1  C Y N 477 
TRP   CD2  C Y N 478 
TRP   NE1  N Y N 479 
TRP   CE2  C Y N 480 
TRP   CE3  C Y N 481 
TRP   CZ2  C Y N 482 
TRP   CZ3  C Y N 483 
TRP   CH2  C Y N 484 
TRP   OXT  O N N 485 
TRP   H    H N N 486 
TRP   H2   H N N 487 
TRP   HA   H N N 488 
TRP   HB2  H N N 489 
TRP   HB3  H N N 490 
TRP   HD1  H N N 491 
TRP   HE1  H N N 492 
TRP   HE3  H N N 493 
TRP   HZ2  H N N 494 
TRP   HZ3  H N N 495 
TRP   HH2  H N N 496 
TRP   HXT  H N N 497 
TYR   N    N N N 498 
TYR   CA   C N S 499 
TYR   C    C N N 500 
TYR   O    O N N 501 
TYR   CB   C N N 502 
TYR   CG   C Y N 503 
TYR   CD1  C Y N 504 
TYR   CD2  C Y N 505 
TYR   CE1  C Y N 506 
TYR   CE2  C Y N 507 
TYR   CZ   C Y N 508 
TYR   OH   O N N 509 
TYR   OXT  O N N 510 
TYR   H    H N N 511 
TYR   H2   H N N 512 
TYR   HA   H N N 513 
TYR   HB2  H N N 514 
TYR   HB3  H N N 515 
TYR   HD1  H N N 516 
TYR   HD2  H N N 517 
TYR   HE1  H N N 518 
TYR   HE2  H N N 519 
TYR   HH   H N N 520 
TYR   HXT  H N N 521 
VAL   N    N N N 522 
VAL   CA   C N S 523 
VAL   C    C N N 524 
VAL   O    O N N 525 
VAL   CB   C N N 526 
VAL   CG1  C N N 527 
VAL   CG2  C N N 528 
VAL   OXT  O N N 529 
VAL   H    H N N 530 
VAL   H2   H N N 531 
VAL   HA   H N N 532 
VAL   HB   H N N 533 
VAL   HG11 H N N 534 
VAL   HG12 H N N 535 
VAL   HG13 H N N 536 
VAL   HG21 H N N 537 
VAL   HG22 H N N 538 
VAL   HG23 H N N 539 
VAL   HXT  H N N 540 
# 
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 
A1EDK O1  C20  doub N N 1   
A1EDK O2  C21  sing N N 2   
A1EDK C20 N2   sing N N 3   
A1EDK C20 C19  sing N N 4   
A1EDK C21 C19  doub N Z 5   
A1EDK C21 C22  sing N N 6   
A1EDK N2  C17  sing N N 7   
A1EDK C19 C18  sing N N 8   
A1EDK C23 C22  doub N E 9   
A1EDK C23 C24  sing N N 10  
A1EDK O3  C26  sing N N 11  
A1EDK C25 C24  doub N E 12  
A1EDK C25 C26  sing N N 13  
A1EDK C17 C18  sing N N 14  
A1EDK C17 C16  sing N N 15  
A1EDK C18 O4   doub N N 16  
A1EDK C26 C7   sing N N 17  
A1EDK C16 C15  sing N N 18  
A1EDK C15 C14  sing N N 19  
A1EDK C7  C8   sing N N 20  
A1EDK C7  C6   sing N N 21  
A1EDK C9  C10  doub N E 22  
A1EDK C9  C8   sing N N 23  
A1EDK C5  C4   sing N N 24  
A1EDK C10 C11  sing N N 25  
A1EDK C11 C12  doub N E 26  
A1EDK C8  C27  sing N N 27  
A1EDK C4  C6   sing N N 28  
A1EDK C4  C3   sing N N 29  
A1EDK C12 C13  sing N N 30  
A1EDK C6  C28  sing N N 31  
A1EDK O5  C13  doub N N 32  
A1EDK C13 N1   sing N N 33  
A1EDK C14 N1   sing N N 34  
A1EDK C27 C28  sing N N 35  
A1EDK C3  C2   sing N N 36  
A1EDK C3  C29  sing N N 37  
A1EDK C2  C1   sing N N 38  
A1EDK C28 C29  sing N N 39  
A1EDK C8  H1   sing N N 40  
A1EDK C5  H3   sing N N 41  
A1EDK C5  H4   sing N N 42  
A1EDK C5  H2   sing N N 43  
A1EDK C6  H5   sing N N 44  
A1EDK N1  H6   sing N N 45  
A1EDK C2  H7   sing N N 46  
A1EDK C2  H8   sing N N 47  
A1EDK C4  H9   sing N N 48  
A1EDK C23 H10  sing N N 49  
A1EDK C24 H12  sing N N 50  
A1EDK C25 H13  sing N N 51  
A1EDK C27 H15  sing N N 52  
A1EDK C27 H14  sing N N 53  
A1EDK C29 H16  sing N N 54  
A1EDK C29 H17  sing N N 55  
A1EDK C1  H20  sing N N 56  
A1EDK C1  H18  sing N N 57  
A1EDK C1  H19  sing N N 58  
A1EDK C10 H21  sing N N 59  
A1EDK C11 H22  sing N N 60  
A1EDK C12 H23  sing N N 61  
A1EDK C14 H25  sing N N 62  
A1EDK C14 H24  sing N N 63  
A1EDK C15 H27  sing N N 64  
A1EDK C15 H26  sing N N 65  
A1EDK C16 H29  sing N N 66  
A1EDK C16 H28  sing N N 67  
A1EDK C17 H30  sing N N 68  
A1EDK C22 H32  sing N N 69  
A1EDK C26 H33  sing N N 70  
A1EDK C28 H34  sing N N 71  
A1EDK C3  H35  sing N N 72  
A1EDK C7  H36  sing N N 73  
A1EDK C9  H37  sing N N 74  
A1EDK N2  H38  sing N N 75  
A1EDK O2  H39  sing N N 76  
A1EDK O3  H40  sing N N 77  
ALA   N   CA   sing N N 78  
ALA   N   H    sing N N 79  
ALA   N   H2   sing N N 80  
ALA   CA  C    sing N N 81  
ALA   CA  CB   sing N N 82  
ALA   CA  HA   sing N N 83  
ALA   C   O    doub N N 84  
ALA   C   OXT  sing N N 85  
ALA   CB  HB1  sing N N 86  
ALA   CB  HB2  sing N N 87  
ALA   CB  HB3  sing N N 88  
ALA   OXT HXT  sing N N 89  
ARG   N   CA   sing N N 90  
ARG   N   H    sing N N 91  
ARG   N   H2   sing N N 92  
ARG   CA  C    sing N N 93  
ARG   CA  CB   sing N N 94  
ARG   CA  HA   sing N N 95  
ARG   C   O    doub N N 96  
ARG   C   OXT  sing N N 97  
ARG   CB  CG   sing N N 98  
ARG   CB  HB2  sing N N 99  
ARG   CB  HB3  sing N N 100 
ARG   CG  CD   sing N N 101 
ARG   CG  HG2  sing N N 102 
ARG   CG  HG3  sing N N 103 
ARG   CD  NE   sing N N 104 
ARG   CD  HD2  sing N N 105 
ARG   CD  HD3  sing N N 106 
ARG   NE  CZ   sing N N 107 
ARG   NE  HE   sing N N 108 
ARG   CZ  NH1  sing N N 109 
ARG   CZ  NH2  doub N N 110 
ARG   NH1 HH11 sing N N 111 
ARG   NH1 HH12 sing N N 112 
ARG   NH2 HH21 sing N N 113 
ARG   NH2 HH22 sing N N 114 
ARG   OXT HXT  sing N N 115 
ASN   N   CA   sing N N 116 
ASN   N   H    sing N N 117 
ASN   N   H2   sing N N 118 
ASN   CA  C    sing N N 119 
ASN   CA  CB   sing N N 120 
ASN   CA  HA   sing N N 121 
ASN   C   O    doub N N 122 
ASN   C   OXT  sing N N 123 
ASN   CB  CG   sing N N 124 
ASN   CB  HB2  sing N N 125 
ASN   CB  HB3  sing N N 126 
ASN   CG  OD1  doub N N 127 
ASN   CG  ND2  sing N N 128 
ASN   ND2 HD21 sing N N 129 
ASN   ND2 HD22 sing N N 130 
ASN   OXT HXT  sing N N 131 
ASP   N   CA   sing N N 132 
ASP   N   H    sing N N 133 
ASP   N   H2   sing N N 134 
ASP   CA  C    sing N N 135 
ASP   CA  CB   sing N N 136 
ASP   CA  HA   sing N N 137 
ASP   C   O    doub N N 138 
ASP   C   OXT  sing N N 139 
ASP   CB  CG   sing N N 140 
ASP   CB  HB2  sing N N 141 
ASP   CB  HB3  sing N N 142 
ASP   CG  OD1  doub N N 143 
ASP   CG  OD2  sing N N 144 
ASP   OD2 HD2  sing N N 145 
ASP   OXT HXT  sing N N 146 
CYS   N   CA   sing N N 147 
CYS   N   H    sing N N 148 
CYS   N   H2   sing N N 149 
CYS   CA  C    sing N N 150 
CYS   CA  CB   sing N N 151 
CYS   CA  HA   sing N N 152 
CYS   C   O    doub N N 153 
CYS   C   OXT  sing N N 154 
CYS   CB  SG   sing N N 155 
CYS   CB  HB2  sing N N 156 
CYS   CB  HB3  sing N N 157 
CYS   SG  HG   sing N N 158 
CYS   OXT HXT  sing N N 159 
GLN   N   CA   sing N N 160 
GLN   N   H    sing N N 161 
GLN   N   H2   sing N N 162 
GLN   CA  C    sing N N 163 
GLN   CA  CB   sing N N 164 
GLN   CA  HA   sing N N 165 
GLN   C   O    doub N N 166 
GLN   C   OXT  sing N N 167 
GLN   CB  CG   sing N N 168 
GLN   CB  HB2  sing N N 169 
GLN   CB  HB3  sing N N 170 
GLN   CG  CD   sing N N 171 
GLN   CG  HG2  sing N N 172 
GLN   CG  HG3  sing N N 173 
GLN   CD  OE1  doub N N 174 
GLN   CD  NE2  sing N N 175 
GLN   NE2 HE21 sing N N 176 
GLN   NE2 HE22 sing N N 177 
GLN   OXT HXT  sing N N 178 
GLU   N   CA   sing N N 179 
GLU   N   H    sing N N 180 
GLU   N   H2   sing N N 181 
GLU   CA  C    sing N N 182 
GLU   CA  CB   sing N N 183 
GLU   CA  HA   sing N N 184 
GLU   C   O    doub N N 185 
GLU   C   OXT  sing N N 186 
GLU   CB  CG   sing N N 187 
GLU   CB  HB2  sing N N 188 
GLU   CB  HB3  sing N N 189 
GLU   CG  CD   sing N N 190 
GLU   CG  HG2  sing N N 191 
GLU   CG  HG3  sing N N 192 
GLU   CD  OE1  doub N N 193 
GLU   CD  OE2  sing N N 194 
GLU   OE2 HE2  sing N N 195 
GLU   OXT HXT  sing N N 196 
GLY   N   CA   sing N N 197 
GLY   N   H    sing N N 198 
GLY   N   H2   sing N N 199 
GLY   CA  C    sing N N 200 
GLY   CA  HA2  sing N N 201 
GLY   CA  HA3  sing N N 202 
GLY   C   O    doub N N 203 
GLY   C   OXT  sing N N 204 
GLY   OXT HXT  sing N N 205 
HIS   N   CA   sing N N 206 
HIS   N   H    sing N N 207 
HIS   N   H2   sing N N 208 
HIS   CA  C    sing N N 209 
HIS   CA  CB   sing N N 210 
HIS   CA  HA   sing N N 211 
HIS   C   O    doub N N 212 
HIS   C   OXT  sing N N 213 
HIS   CB  CG   sing N N 214 
HIS   CB  HB2  sing N N 215 
HIS   CB  HB3  sing N N 216 
HIS   CG  ND1  sing Y N 217 
HIS   CG  CD2  doub Y N 218 
HIS   ND1 CE1  doub Y N 219 
HIS   ND1 HD1  sing N N 220 
HIS   CD2 NE2  sing Y N 221 
HIS   CD2 HD2  sing N N 222 
HIS   CE1 NE2  sing Y N 223 
HIS   CE1 HE1  sing N N 224 
HIS   NE2 HE2  sing N N 225 
HIS   OXT HXT  sing N N 226 
HOH   O   H1   sing N N 227 
HOH   O   H2   sing N N 228 
ILE   N   CA   sing N N 229 
ILE   N   H    sing N N 230 
ILE   N   H2   sing N N 231 
ILE   CA  C    sing N N 232 
ILE   CA  CB   sing N N 233 
ILE   CA  HA   sing N N 234 
ILE   C   O    doub N N 235 
ILE   C   OXT  sing N N 236 
ILE   CB  CG1  sing N N 237 
ILE   CB  CG2  sing N N 238 
ILE   CB  HB   sing N N 239 
ILE   CG1 CD1  sing N N 240 
ILE   CG1 HG12 sing N N 241 
ILE   CG1 HG13 sing N N 242 
ILE   CG2 HG21 sing N N 243 
ILE   CG2 HG22 sing N N 244 
ILE   CG2 HG23 sing N N 245 
ILE   CD1 HD11 sing N N 246 
ILE   CD1 HD12 sing N N 247 
ILE   CD1 HD13 sing N N 248 
ILE   OXT HXT  sing N N 249 
LEU   N   CA   sing N N 250 
LEU   N   H    sing N N 251 
LEU   N   H2   sing N N 252 
LEU   CA  C    sing N N 253 
LEU   CA  CB   sing N N 254 
LEU   CA  HA   sing N N 255 
LEU   C   O    doub N N 256 
LEU   C   OXT  sing N N 257 
LEU   CB  CG   sing N N 258 
LEU   CB  HB2  sing N N 259 
LEU   CB  HB3  sing N N 260 
LEU   CG  CD1  sing N N 261 
LEU   CG  CD2  sing N N 262 
LEU   CG  HG   sing N N 263 
LEU   CD1 HD11 sing N N 264 
LEU   CD1 HD12 sing N N 265 
LEU   CD1 HD13 sing N N 266 
LEU   CD2 HD21 sing N N 267 
LEU   CD2 HD22 sing N N 268 
LEU   CD2 HD23 sing N N 269 
LEU   OXT HXT  sing N N 270 
LYS   N   CA   sing N N 271 
LYS   N   H    sing N N 272 
LYS   N   H2   sing N N 273 
LYS   CA  C    sing N N 274 
LYS   CA  CB   sing N N 275 
LYS   CA  HA   sing N N 276 
LYS   C   O    doub N N 277 
LYS   C   OXT  sing N N 278 
LYS   CB  CG   sing N N 279 
LYS   CB  HB2  sing N N 280 
LYS   CB  HB3  sing N N 281 
LYS   CG  CD   sing N N 282 
LYS   CG  HG2  sing N N 283 
LYS   CG  HG3  sing N N 284 
LYS   CD  CE   sing N N 285 
LYS   CD  HD2  sing N N 286 
LYS   CD  HD3  sing N N 287 
LYS   CE  NZ   sing N N 288 
LYS   CE  HE2  sing N N 289 
LYS   CE  HE3  sing N N 290 
LYS   NZ  HZ1  sing N N 291 
LYS   NZ  HZ2  sing N N 292 
LYS   NZ  HZ3  sing N N 293 
LYS   OXT HXT  sing N N 294 
MET   N   CA   sing N N 295 
MET   N   H    sing N N 296 
MET   N   H2   sing N N 297 
MET   CA  C    sing N N 298 
MET   CA  CB   sing N N 299 
MET   CA  HA   sing N N 300 
MET   C   O    doub N N 301 
MET   C   OXT  sing N N 302 
MET   CB  CG   sing N N 303 
MET   CB  HB2  sing N N 304 
MET   CB  HB3  sing N N 305 
MET   CG  SD   sing N N 306 
MET   CG  HG2  sing N N 307 
MET   CG  HG3  sing N N 308 
MET   SD  CE   sing N N 309 
MET   CE  HE1  sing N N 310 
MET   CE  HE2  sing N N 311 
MET   CE  HE3  sing N N 312 
MET   OXT HXT  sing N N 313 
NAP   PA  O1A  doub N N 314 
NAP   PA  O2A  sing N N 315 
NAP   PA  O5B  sing N N 316 
NAP   PA  O3   sing N N 317 
NAP   O2A HOA2 sing N N 318 
NAP   O5B C5B  sing N N 319 
NAP   C5B C4B  sing N N 320 
NAP   C5B H51A sing N N 321 
NAP   C5B H52A sing N N 322 
NAP   C4B O4B  sing N N 323 
NAP   C4B C3B  sing N N 324 
NAP   C4B H4B  sing N N 325 
NAP   O4B C1B  sing N N 326 
NAP   C3B O3B  sing N N 327 
NAP   C3B C2B  sing N N 328 
NAP   C3B H3B  sing N N 329 
NAP   O3B HO3A sing N N 330 
NAP   C2B O2B  sing N N 331 
NAP   C2B C1B  sing N N 332 
NAP   C2B H2B  sing N N 333 
NAP   O2B P2B  sing N N 334 
NAP   C1B N9A  sing N N 335 
NAP   C1B H1B  sing N N 336 
NAP   N9A C8A  sing Y N 337 
NAP   N9A C4A  sing Y N 338 
NAP   C8A N7A  doub Y N 339 
NAP   C8A H8A  sing N N 340 
NAP   N7A C5A  sing Y N 341 
NAP   C5A C6A  sing Y N 342 
NAP   C5A C4A  doub Y N 343 
NAP   C6A N6A  sing N N 344 
NAP   C6A N1A  doub Y N 345 
NAP   N6A H61A sing N N 346 
NAP   N6A H62A sing N N 347 
NAP   N1A C2A  sing Y N 348 
NAP   C2A N3A  doub Y N 349 
NAP   C2A H2A  sing N N 350 
NAP   N3A C4A  sing Y N 351 
NAP   O3  PN   sing N N 352 
NAP   PN  O1N  doub N N 353 
NAP   PN  O2N  sing N N 354 
NAP   PN  O5D  sing N N 355 
NAP   O5D C5D  sing N N 356 
NAP   C5D C4D  sing N N 357 
NAP   C5D H51N sing N N 358 
NAP   C5D H52N sing N N 359 
NAP   C4D O4D  sing N N 360 
NAP   C4D C3D  sing N N 361 
NAP   C4D H4D  sing N N 362 
NAP   O4D C1D  sing N N 363 
NAP   C3D O3D  sing N N 364 
NAP   C3D C2D  sing N N 365 
NAP   C3D H3D  sing N N 366 
NAP   O3D HO3N sing N N 367 
NAP   C2D O2D  sing N N 368 
NAP   C2D C1D  sing N N 369 
NAP   C2D H2D  sing N N 370 
NAP   O2D HO2N sing N N 371 
NAP   C1D N1N  sing N N 372 
NAP   C1D H1D  sing N N 373 
NAP   N1N C2N  sing Y N 374 
NAP   N1N C6N  doub Y N 375 
NAP   C2N C3N  doub Y N 376 
NAP   C2N H2N  sing N N 377 
NAP   C3N C7N  sing N N 378 
NAP   C3N C4N  sing Y N 379 
NAP   C7N O7N  doub N N 380 
NAP   C7N N7N  sing N N 381 
NAP   N7N H71N sing N N 382 
NAP   N7N H72N sing N N 383 
NAP   C4N C5N  doub Y N 384 
NAP   C4N H4N  sing N N 385 
NAP   C5N C6N  sing Y N 386 
NAP   C5N H5N  sing N N 387 
NAP   C6N H6N  sing N N 388 
NAP   P2B O1X  doub N N 389 
NAP   P2B O2X  sing N N 390 
NAP   P2B O3X  sing N N 391 
NAP   O2X HOP2 sing N N 392 
NAP   O3X HOP3 sing N N 393 
PHE   N   CA   sing N N 394 
PHE   N   H    sing N N 395 
PHE   N   H2   sing N N 396 
PHE   CA  C    sing N N 397 
PHE   CA  CB   sing N N 398 
PHE   CA  HA   sing N N 399 
PHE   C   O    doub N N 400 
PHE   C   OXT  sing N N 401 
PHE   CB  CG   sing N N 402 
PHE   CB  HB2  sing N N 403 
PHE   CB  HB3  sing N N 404 
PHE   CG  CD1  doub Y N 405 
PHE   CG  CD2  sing Y N 406 
PHE   CD1 CE1  sing Y N 407 
PHE   CD1 HD1  sing N N 408 
PHE   CD2 CE2  doub Y N 409 
PHE   CD2 HD2  sing N N 410 
PHE   CE1 CZ   doub Y N 411 
PHE   CE1 HE1  sing N N 412 
PHE   CE2 CZ   sing Y N 413 
PHE   CE2 HE2  sing N N 414 
PHE   CZ  HZ   sing N N 415 
PHE   OXT HXT  sing N N 416 
PRO   N   CA   sing N N 417 
PRO   N   CD   sing N N 418 
PRO   N   H    sing N N 419 
PRO   CA  C    sing N N 420 
PRO   CA  CB   sing N N 421 
PRO   CA  HA   sing N N 422 
PRO   C   O    doub N N 423 
PRO   C   OXT  sing N N 424 
PRO   CB  CG   sing N N 425 
PRO   CB  HB2  sing N N 426 
PRO   CB  HB3  sing N N 427 
PRO   CG  CD   sing N N 428 
PRO   CG  HG2  sing N N 429 
PRO   CG  HG3  sing N N 430 
PRO   CD  HD2  sing N N 431 
PRO   CD  HD3  sing N N 432 
PRO   OXT HXT  sing N N 433 
SER   N   CA   sing N N 434 
SER   N   H    sing N N 435 
SER   N   H2   sing N N 436 
SER   CA  C    sing N N 437 
SER   CA  CB   sing N N 438 
SER   CA  HA   sing N N 439 
SER   C   O    doub N N 440 
SER   C   OXT  sing N N 441 
SER   CB  OG   sing N N 442 
SER   CB  HB2  sing N N 443 
SER   CB  HB3  sing N N 444 
SER   OG  HG   sing N N 445 
SER   OXT HXT  sing N N 446 
THR   N   CA   sing N N 447 
THR   N   H    sing N N 448 
THR   N   H2   sing N N 449 
THR   CA  C    sing N N 450 
THR   CA  CB   sing N N 451 
THR   CA  HA   sing N N 452 
THR   C   O    doub N N 453 
THR   C   OXT  sing N N 454 
THR   CB  OG1  sing N N 455 
THR   CB  CG2  sing N N 456 
THR   CB  HB   sing N N 457 
THR   OG1 HG1  sing N N 458 
THR   CG2 HG21 sing N N 459 
THR   CG2 HG22 sing N N 460 
THR   CG2 HG23 sing N N 461 
THR   OXT HXT  sing N N 462 
TRP   N   CA   sing N N 463 
TRP   N   H    sing N N 464 
TRP   N   H2   sing N N 465 
TRP   CA  C    sing N N 466 
TRP   CA  CB   sing N N 467 
TRP   CA  HA   sing N N 468 
TRP   C   O    doub N N 469 
TRP   C   OXT  sing N N 470 
TRP   CB  CG   sing N N 471 
TRP   CB  HB2  sing N N 472 
TRP   CB  HB3  sing N N 473 
TRP   CG  CD1  doub Y N 474 
TRP   CG  CD2  sing Y N 475 
TRP   CD1 NE1  sing Y N 476 
TRP   CD1 HD1  sing N N 477 
TRP   CD2 CE2  doub Y N 478 
TRP   CD2 CE3  sing Y N 479 
TRP   NE1 CE2  sing Y N 480 
TRP   NE1 HE1  sing N N 481 
TRP   CE2 CZ2  sing Y N 482 
TRP   CE3 CZ3  doub Y N 483 
TRP   CE3 HE3  sing N N 484 
TRP   CZ2 CH2  doub Y N 485 
TRP   CZ2 HZ2  sing N N 486 
TRP   CZ3 CH2  sing Y N 487 
TRP   CZ3 HZ3  sing N N 488 
TRP   CH2 HH2  sing N N 489 
TRP   OXT HXT  sing N N 490 
TYR   N   CA   sing N N 491 
TYR   N   H    sing N N 492 
TYR   N   H2   sing N N 493 
TYR   CA  C    sing N N 494 
TYR   CA  CB   sing N N 495 
TYR   CA  HA   sing N N 496 
TYR   C   O    doub N N 497 
TYR   C   OXT  sing N N 498 
TYR   CB  CG   sing N N 499 
TYR   CB  HB2  sing N N 500 
TYR   CB  HB3  sing N N 501 
TYR   CG  CD1  doub Y N 502 
TYR   CG  CD2  sing Y N 503 
TYR   CD1 CE1  sing Y N 504 
TYR   CD1 HD1  sing N N 505 
TYR   CD2 CE2  doub Y N 506 
TYR   CD2 HD2  sing N N 507 
TYR   CE1 CZ   doub Y N 508 
TYR   CE1 HE1  sing N N 509 
TYR   CE2 CZ   sing Y N 510 
TYR   CE2 HE2  sing N N 511 
TYR   CZ  OH   sing N N 512 
TYR   OH  HH   sing N N 513 
TYR   OXT HXT  sing N N 514 
VAL   N   CA   sing N N 515 
VAL   N   H    sing N N 516 
VAL   N   H2   sing N N 517 
VAL   CA  C    sing N N 518 
VAL   CA  CB   sing N N 519 
VAL   CA  HA   sing N N 520 
VAL   C   O    doub N N 521 
VAL   C   OXT  sing N N 522 
VAL   CB  CG1  sing N N 523 
VAL   CB  CG2  sing N N 524 
VAL   CB  HB   sing N N 525 
VAL   CG1 HG11 sing N N 526 
VAL   CG1 HG12 sing N N 527 
VAL   CG1 HG13 sing N N 528 
VAL   CG2 HG21 sing N N 529 
VAL   CG2 HG22 sing N N 530 
VAL   CG2 HG23 sing N N 531 
VAL   OXT HXT  sing N N 532 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82173702 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2J3H 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JML 
_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]   0.011495 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011495 
_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]   0.004427 
_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 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU   A 1 1   ? -15.420 -0.564  49.548  1.00 76.12 ? -2  LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 1   ? -14.321 -0.525  48.587  1.00 77.33 ? -2  LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 1   ? -13.612 0.832   48.609  1.00 80.66 ? -2  LEU   A C   1 
ATOM   4    O O   . LEU   A 1 1   ? -13.289 1.353   49.684  1.00 82.10 ? -2  LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 1   ? -14.832 -0.854  47.178  1.00 75.39 ? -2  LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 1   ? -14.916 -2.348  46.843  1.00 77.56 ? -2  LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 1   ? -16.360 -2.846  46.848  1.00 70.62 ? -2  LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 1   ? -14.240 -2.636  45.511  1.00 67.44 ? -2  LEU   A CD2 1 
ATOM   9    N N   . GLY   A 1 2   ? -13.366 1.423   47.428  1.00 68.17 ? -1  GLY   A N   1 
ATOM   10   C CA  . GLY   A 1 2   ? -12.545 2.609   47.333  1.00 53.18 ? -1  GLY   A CA  1 
ATOM   11   C C   . GLY   A 1 2   ? -13.145 3.673   46.427  1.00 48.04 ? -1  GLY   A C   1 
ATOM   12   O O   . GLY   A 1 2   ? -14.117 3.450   45.699  1.00 44.01 ? -1  GLY   A O   1 
ATOM   13   N N   . SER   A 1 3   ? -12.532 4.849   46.500  1.00 43.93 ? 0   SER   A N   1 
ATOM   14   C CA  . SER   A 1 3   ? -12.874 5.975   45.649  1.00 39.00 ? 0   SER   A CA  1 
ATOM   15   C C   . SER   A 1 3   ? -11.607 6.792   45.474  1.00 44.88 ? 0   SER   A C   1 
ATOM   16   O O   . SER   A 1 3   ? -10.599 6.567   46.159  1.00 38.60 ? 0   SER   A O   1 
ATOM   17   C CB  . SER   A 1 3   ? -14.002 6.816   46.250  1.00 43.05 ? 0   SER   A CB  1 
ATOM   18   O OG  . SER   A 1 3   ? -13.494 7.712   47.223  1.00 46.90 ? 0   SER   A OG  1 
ATOM   19   N N   . MET   A 1 4   ? -11.646 7.742   44.545  1.00 36.69 ? 1   MET   A N   1 
ATOM   20   C CA  . MET   A 1 4   ? -10.485 8.591   44.344  1.00 36.69 ? 1   MET   A CA  1 
ATOM   21   C C   . MET   A 1 4   ? -10.936 10.015  44.046  1.00 34.70 ? 1   MET   A C   1 
ATOM   22   O O   . MET   A 1 4   ? -12.085 10.262  43.672  1.00 36.38 ? 1   MET   A O   1 
ATOM   23   C CB  . MET   A 1 4   ? -9.586  8.059   43.220  1.00 35.84 ? 1   MET   A CB  1 
ATOM   24   C CG  . MET   A 1 4   ? -10.159 8.204   41.822  1.00 33.98 ? 1   MET   A CG  1 
ATOM   25   S SD  . MET   A 1 4   ? -9.159  7.283   40.642  1.00 34.96 ? 1   MET   A SD  1 
ATOM   26   C CE  . MET   A 1 4   ? -7.671  8.217   40.541  1.00 29.12 ? 1   MET   A CE  1 
ATOM   27   N N   . LYS   A 1 5   ? -10.013 10.953  44.250  1.00 40.33 ? 2   LYS   A N   1 
ATOM   28   C CA  . LYS   A 1 5   ? -10.231 12.337  43.866  1.00 39.82 ? 2   LYS   A CA  1 
ATOM   29   C C   . LYS   A 1 5   ? -9.974  12.493  42.371  1.00 36.34 ? 2   LYS   A C   1 
ATOM   30   O O   . LYS   A 1 5   ? -8.948  12.034  41.866  1.00 33.43 ? 2   LYS   A O   1 
ATOM   31   C CB  . LYS   A 1 5   ? -9.303  13.258  44.652  1.00 39.77 ? 2   LYS   A CB  1 
ATOM   32   C CG  . LYS   A 1 5   ? -9.464  13.150  46.166  1.00 47.07 ? 2   LYS   A CG  1 
ATOM   33   C CD  . LYS   A 1 5   ? -10.899 13.443  46.578  1.00 52.19 ? 2   LYS   A CD  1 
ATOM   34   C CE  . LYS   A 1 5   ? -11.611 12.180  47.043  1.00 50.30 ? 2   LYS   A CE  1 
ATOM   35   N NZ  . LYS   A 1 5   ? -13.056 12.206  46.713  1.00 51.00 ? 2   LYS   A NZ  1 
ATOM   36   N N   . THR   A 1 6   ? -10.912 13.126  41.670  1.00 33.52 ? 3   THR   A N   1 
ATOM   37   C CA  . THR   A 1 6   ? -10.768 13.439  40.255  1.00 33.54 ? 3   THR   A CA  1 
ATOM   38   C C   . THR   A 1 6   ? -11.236 14.868  40.028  1.00 37.93 ? 3   THR   A C   1 
ATOM   39   O O   . THR   A 1 6   ? -11.982 15.427  40.837  1.00 37.27 ? 3   THR   A O   1 
ATOM   40   C CB  . THR   A 1 6   ? -11.593 12.500  39.371  1.00 32.49 ? 3   THR   A CB  1 
ATOM   41   O OG1 . THR   A 1 6   ? -12.981 12.828  39.510  1.00 30.95 ? 3   THR   A OG1 1 
ATOM   42   C CG2 . THR   A 1 6   ? -11.364 11.052  39.756  1.00 32.38 ? 3   THR   A CG2 1 
ATOM   43   N N   . GLU   A 1 7   ? -10.809 15.462  38.913  1.00 31.43 ? 4   GLU   A N   1 
ATOM   44   C CA  . GLU   A 1 7   ? -11.306 16.779  38.525  1.00 32.50 ? 4   GLU   A CA  1 
ATOM   45   C C   . GLU   A 1 7   ? -12.056 16.705  37.201  1.00 31.17 ? 4   GLU   A C   1 
ATOM   46   O O   . GLU   A 1 7   ? -11.695 15.934  36.307  1.00 29.00 ? 4   GLU   A O   1 
ATOM   47   C CB  . GLU   A 1 7   ? -10.166 17.795  38.428  1.00 35.11 ? 4   GLU   A CB  1 
ATOM   48   C CG  . GLU   A 1 7   ? -9.624  18.243  39.769  1.00 39.45 ? 4   GLU   A CG  1 
ATOM   49   C CD  . GLU   A 1 7   ? -8.469  19.205  39.613  1.00 44.64 ? 4   GLU   A CD  1 
ATOM   50   O OE1 . GLU   A 1 7   ? -7.709  19.068  38.631  1.00 48.84 ? 4   GLU   A OE1 1 
ATOM   51   O OE2 . GLU   A 1 7   ? -8.320  20.097  40.467  1.00 53.45 ? 4   GLU   A OE2 1 
ATOM   52   N N   . ARG   A 1 8   ? -13.104 17.505  37.080  1.00 33.52 ? 5   ARG   A N   1 
ATOM   53   C CA  . ARG   A 1 8   ? -13.887 17.562  35.857  1.00 32.98 ? 5   ARG   A CA  1 
ATOM   54   C C   . ARG   A 1 8   ? -14.128 19.021  35.496  1.00 35.71 ? 5   ARG   A C   1 
ATOM   55   O O   . ARG   A 1 8   ? -14.237 19.880  36.377  1.00 34.12 ? 5   ARG   A O   1 
ATOM   56   C CB  . ARG   A 1 8   ? -15.223 16.803  36.016  1.00 32.67 ? 5   ARG   A CB  1 
ATOM   57   C CG  . ARG   A 1 8   ? -15.063 15.339  36.460  1.00 32.00 ? 5   ARG   A CG  1 
ATOM   58   C CD  . ARG   A 1 8   ? -16.407 14.608  36.465  1.00 35.36 ? 5   ARG   A CD  1 
ATOM   59   N NE  . ARG   A 1 8   ? -17.350 15.255  37.373  1.00 34.48 ? 5   ARG   A NE  1 
ATOM   60   C CZ  . ARG   A 1 8   ? -18.638 15.419  37.117  1.00 33.19 ? 5   ARG   A CZ  1 
ATOM   61   N NH1 . ARG   A 1 8   ? -19.186 14.946  36.012  1.00 31.70 ? 5   ARG   A NH1 1 
ATOM   62   N NH2 . ARG   A 1 8   ? -19.394 16.087  37.988  1.00 35.90 ? 5   ARG   A NH2 1 
ATOM   63   N N   . TRP   A 1 9   ? -14.151 19.307  34.193  1.00 32.51 ? 6   TRP   A N   1 
ATOM   64   C CA  . TRP   A 1 9   ? -14.727 20.550  33.692  1.00 31.58 ? 6   TRP   A CA  1 
ATOM   65   C C   . TRP   A 1 9   ? -16.174 20.271  33.317  1.00 28.12 ? 6   TRP   A C   1 
ATOM   66   O O   . TRP   A 1 9   ? -16.439 19.434  32.451  1.00 34.30 ? 6   TRP   A O   1 
ATOM   67   C CB  . TRP   A 1 9   ? -13.958 21.074  32.482  1.00 30.89 ? 6   TRP   A CB  1 
ATOM   68   C CG  . TRP   A 1 9   ? -12.619 21.659  32.784  1.00 28.74 ? 6   TRP   A CG  1 
ATOM   69   C CD1 . TRP   A 1 9   ? -11.408 21.061  32.618  1.00 28.92 ? 6   TRP   A CD1 1 
ATOM   70   C CD2 . TRP   A 1 9   ? -12.356 22.976  33.283  1.00 31.17 ? 6   TRP   A CD2 1 
ATOM   71   N NE1 . TRP   A 1 9   ? -10.391 21.929  32.984  1.00 29.82 ? 6   TRP   A NE1 1 
ATOM   72   C CE2 . TRP   A 1 9   ? -10.953 23.106  33.407  1.00 30.81 ? 6   TRP   A CE2 1 
ATOM   73   C CE3 . TRP   A 1 9   ? -13.171 24.055  33.661  1.00 33.76 ? 6   TRP   A CE3 1 
ATOM   74   C CZ2 . TRP   A 1 9   ? -10.349 24.273  33.879  1.00 30.32 ? 6   TRP   A CZ2 1 
ATOM   75   C CZ3 . TRP   A 1 9   ? -12.567 25.212  34.127  1.00 29.46 ? 6   TRP   A CZ3 1 
ATOM   76   C CH2 . TRP   A 1 9   ? -11.172 25.311  34.233  1.00 31.04 ? 6   TRP   A CH2 1 
ATOM   77   N N   . VAL   A 1 10  ? -17.110 20.948  33.975  1.00 31.36 ? 7   VAL   A N   1 
ATOM   78   C CA  . VAL   A 1 10  ? -18.530 20.722  33.746  1.00 31.98 ? 7   VAL   A CA  1 
ATOM   79   C C   . VAL   A 1 10  ? -19.126 21.968  33.107  1.00 34.01 ? 7   VAL   A C   1 
ATOM   80   O O   . VAL   A 1 10  ? -18.549 23.059  33.142  1.00 33.00 ? 7   VAL   A O   1 
ATOM   81   C CB  . VAL   A 1 10  ? -19.281 20.364  35.046  1.00 35.45 ? 7   VAL   A CB  1 
ATOM   82   C CG1 . VAL   A 1 10  ? -18.778 19.035  35.606  1.00 32.56 ? 7   VAL   A CG1 1 
ATOM   83   C CG2 . VAL   A 1 10  ? -19.122 21.484  36.069  1.00 34.62 ? 7   VAL   A CG2 1 
ATOM   84   N N   . VAL   A 1 11  ? -20.309 21.799  32.529  1.00 34.61 ? 8   VAL   A N   1 
ATOM   85   C CA  . VAL   A 1 11  ? -20.975 22.880  31.812  1.00 36.66 ? 8   VAL   A CA  1 
ATOM   86   C C   . VAL   A 1 11  ? -21.806 23.671  32.815  1.00 40.06 ? 8   VAL   A C   1 
ATOM   87   O O   . VAL   A 1 11  ? -22.819 23.184  33.331  1.00 36.01 ? 8   VAL   A O   1 
ATOM   88   C CB  . VAL   A 1 11  ? -21.843 22.356  30.661  1.00 36.85 ? 8   VAL   A CB  1 
ATOM   89   C CG1 . VAL   A 1 11  ? -22.523 23.525  29.964  1.00 38.06 ? 8   VAL   A CG1 1 
ATOM   90   C CG2 . VAL   A 1 11  ? -20.987 21.569  29.678  1.00 34.87 ? 8   VAL   A CG2 1 
ATOM   91   N N   . ARG   A 1 12  ? -21.373 24.898  33.075  1.00 36.81 ? 9   ARG   A N   1 
ATOM   92   C CA  . ARG   A 1 12  ? -22.036 25.797  34.011  1.00 43.12 ? 9   ARG   A CA  1 
ATOM   93   C C   . ARG   A 1 12  ? -23.157 26.606  33.364  1.00 45.87 ? 9   ARG   A C   1 
ATOM   94   O O   . ARG   A 1 12  ? -24.145 26.929  34.036  1.00 40.46 ? 9   ARG   A O   1 
ATOM   95   C CB  . ARG   A 1 12  ? -20.980 26.722  34.636  1.00 43.21 ? 9   ARG   A CB  1 
ATOM   96   C CG  . ARG   A 1 12  ? -21.491 27.979  35.304  1.00 47.84 ? 9   ARG   A CG  1 
ATOM   97   C CD  . ARG   A 1 12  ? -20.416 28.573  36.211  1.00 48.98 ? 9   ARG   A CD  1 
ATOM   98   N NE  . ARG   A 1 12  ? -19.231 29.025  35.488  1.00 45.46 ? 9   ARG   A NE  1 
ATOM   99   C CZ  . ARG   A 1 12  ? -18.113 29.439  36.072  1.00 50.23 ? 9   ARG   A CZ  1 
ATOM   100  N NH1 . ARG   A 1 12  ? -17.977 29.430  37.391  1.00 54.65 ? 9   ARG   A NH1 1 
ATOM   101  N NH2 . ARG   A 1 12  ? -17.101 29.864  35.318  1.00 45.17 ? 9   ARG   A NH2 1 
ATOM   102  N N   . GLU   A 1 13  ? -23.046 26.922  32.071  1.00 39.49 ? 10  GLU   A N   1 
ATOM   103  C CA  . GLU   A 1 13  ? -23.999 27.821  31.438  1.00 36.53 ? 10  GLU   A CA  1 
ATOM   104  C C   . GLU   A 1 13  ? -23.981 27.602  29.928  1.00 40.38 ? 10  GLU   A C   1 
ATOM   105  O O   . GLU   A 1 13  ? -22.923 27.342  29.347  1.00 34.96 ? 10  GLU   A O   1 
ATOM   106  C CB  . GLU   A 1 13  ? -23.667 29.280  31.776  1.00 40.38 ? 10  GLU   A CB  1 
ATOM   107  C CG  . GLU   A 1 13  ? -24.686 30.291  31.291  1.00 42.63 ? 10  GLU   A CG  1 
ATOM   108  C CD  . GLU   A 1 13  ? -24.223 31.723  31.494  1.00 44.56 ? 10  GLU   A CD  1 
ATOM   109  O OE1 . GLU   A 1 13  ? -23.133 31.926  32.074  1.00 45.66 ? 10  GLU   A OE1 1 
ATOM   110  O OE2 . GLU   A 1 13  ? -24.940 32.648  31.060  1.00 49.60 ? 10  GLU   A OE2 1 
ATOM   111  N N   . HIS   A 1 14  ? -25.153 27.716  29.313  1.00 37.54 ? 11  HIS   A N   1 
ATOM   112  C CA  . HIS   A 1 14  ? -25.326 27.593  27.873  1.00 35.29 ? 11  HIS   A CA  1 
ATOM   113  C C   . HIS   A 1 14  ? -25.403 28.984  27.252  1.00 43.82 ? 11  HIS   A C   1 
ATOM   114  O O   . HIS   A 1 14  ? -26.304 29.768  27.578  1.00 41.85 ? 11  HIS   A O   1 
ATOM   115  C CB  . HIS   A 1 14  ? -26.589 26.803  27.549  1.00 35.44 ? 11  HIS   A CB  1 
ATOM   116  C CG  . HIS   A 1 14  ? -26.470 25.338  27.825  1.00 37.35 ? 11  HIS   A CG  1 
ATOM   117  N ND1 . HIS   A 1 14  ? -27.547 24.558  28.193  1.00 36.93 ? 11  HIS   A ND1 1 
ATOM   118  C CD2 . HIS   A 1 14  ? -25.403 24.504  27.768  1.00 29.57 ? 11  HIS   A CD2 1 
ATOM   119  C CE1 . HIS   A 1 14  ? -27.150 23.307  28.351  1.00 37.18 ? 11  HIS   A CE1 1 
ATOM   120  N NE2 . HIS   A 1 14  ? -25.855 23.247  28.093  1.00 34.21 ? 11  HIS   A NE2 1 
ATOM   121  N N   . VAL   A 1 15  ? -24.450 29.285  26.374  1.00 33.31 ? 12  VAL   A N   1 
ATOM   122  C CA  . VAL   A 1 15  ? -24.423 30.511  25.587  1.00 38.51 ? 12  VAL   A CA  1 
ATOM   123  C C   . VAL   A 1 15  ? -24.177 30.117  24.143  1.00 40.31 ? 12  VAL   A C   1 
ATOM   124  O O   . VAL   A 1 15  ? -23.313 29.278  23.864  1.00 40.24 ? 12  VAL   A O   1 
ATOM   125  C CB  . VAL   A 1 15  ? -23.321 31.486  26.053  1.00 39.56 ? 12  VAL   A CB  1 
ATOM   126  C CG1 . VAL   A 1 15  ? -23.607 32.896  25.540  1.00 40.41 ? 12  VAL   A CG1 1 
ATOM   127  C CG2 . VAL   A 1 15  ? -23.164 31.448  27.554  1.00 41.40 ? 12  VAL   A CG2 1 
ATOM   128  N N   . GLU   A 1 16  ? -24.922 30.721  23.224  1.00 38.71 ? 13  GLU   A N   1 
ATOM   129  C CA  . GLU   A 1 16  ? -24.730 30.401  21.819  1.00 36.40 ? 13  GLU   A CA  1 
ATOM   130  C C   . GLU   A 1 16  ? -23.601 31.243  21.233  1.00 34.93 ? 13  GLU   A C   1 
ATOM   131  O O   . GLU   A 1 16  ? -23.001 32.087  21.907  1.00 33.75 ? 13  GLU   A O   1 
ATOM   132  C CB  . GLU   A 1 16  ? -26.039 30.597  21.073  1.00 39.39 ? 13  GLU   A CB  1 
ATOM   133  C CG  . GLU   A 1 16  ? -27.157 29.989  21.860  1.00 40.20 ? 13  GLU   A CG  1 
ATOM   134  C CD  . GLU   A 1 16  ? -28.251 29.456  20.998  1.00 47.06 ? 13  GLU   A CD  1 
ATOM   135  O OE1 . GLU   A 1 16  ? -28.433 29.992  19.889  1.00 55.73 ? 13  GLU   A OE1 1 
ATOM   136  O OE2 . GLU   A 1 16  ? -28.931 28.502  21.431  1.00 55.20 ? 13  GLU   A OE2 1 
ATOM   137  N N   . GLY   A 1 17  ? -23.291 30.992  19.959  1.00 38.22 ? 14  GLY   A N   1 
ATOM   138  C CA  . GLY   A 1 17  ? -22.265 31.769  19.290  1.00 28.60 ? 14  GLY   A CA  1 
ATOM   139  C C   . GLY   A 1 17  ? -20.872 31.398  19.759  1.00 31.67 ? 14  GLY   A C   1 
ATOM   140  O O   . GLY   A 1 17  ? -20.584 30.258  20.128  1.00 33.28 ? 14  GLY   A O   1 
ATOM   141  N N   . VAL   A 1 18  ? -19.984 32.381  19.716  1.00 33.47 ? 15  VAL   A N   1 
ATOM   142  C CA  . VAL   A 1 18  ? -18.595 32.167  20.101  1.00 32.02 ? 15  VAL   A CA  1 
ATOM   143  C C   . VAL   A 1 18  ? -18.541 31.917  21.601  1.00 36.90 ? 15  VAL   A C   1 
ATOM   144  O O   . VAL   A 1 18  ? -18.979 32.764  22.387  1.00 34.21 ? 15  VAL   A O   1 
ATOM   145  C CB  . VAL   A 1 18  ? -17.712 33.355  19.709  1.00 30.98 ? 15  VAL   A CB  1 
ATOM   146  C CG1 . VAL   A 1 18  ? -16.319 33.172  20.303  1.00 31.60 ? 15  VAL   A CG1 1 
ATOM   147  C CG2 . VAL   A 1 18  ? -17.653 33.479  18.189  1.00 35.20 ? 15  VAL   A CG2 1 
ATOM   148  N N   . PRO   A 1 19  ? -18.021 30.781  22.045  1.00 37.89 ? 16  PRO   A N   1 
ATOM   149  C CA  . PRO   A 1 19  ? -18.062 30.479  23.479  1.00 39.63 ? 16  PRO   A CA  1 
ATOM   150  C C   . PRO   A 1 19  ? -17.128 31.376  24.275  1.00 39.86 ? 16  PRO   A C   1 
ATOM   151  O O   . PRO   A 1 19  ? -16.039 31.748  23.821  1.00 36.43 ? 16  PRO   A O   1 
ATOM   152  C CB  . PRO   A 1 19  ? -17.630 29.009  23.548  1.00 34.81 ? 16  PRO   A CB  1 
ATOM   153  C CG  . PRO   A 1 19  ? -16.824 28.791  22.298  1.00 39.68 ? 16  PRO   A CG  1 
ATOM   154  C CD  . PRO   A 1 19  ? -17.441 29.684  21.249  1.00 34.99 ? 16  PRO   A CD  1 
ATOM   155  N N   . ASP   A 1 20  ? -17.590 31.741  25.471  1.00 35.38 ? 17  ASP   A N   1 
ATOM   156  C CA  . ASP   A 1 20  ? -16.756 32.330  26.519  1.00 36.55 ? 17  ASP   A CA  1 
ATOM   157  C C   . ASP   A 1 20  ? -16.381 31.170  27.444  1.00 38.78 ? 17  ASP   A C   1 
ATOM   158  O O   . ASP   A 1 20  ? -17.119 30.818  28.367  1.00 36.32 ? 17  ASP   A O   1 
ATOM   159  C CB  . ASP   A 1 20  ? -17.502 33.446  27.252  1.00 34.30 ? 17  ASP   A CB  1 
ATOM   160  C CG  . ASP   A 1 20  ? -16.634 34.169  28.273  1.00 44.04 ? 17  ASP   A CG  1 
ATOM   161  O OD1 . ASP   A 1 20  ? -15.441 33.810  28.423  1.00 46.12 ? 17  ASP   A OD1 1 
ATOM   162  O OD2 . ASP   A 1 20  ? -17.149 35.102  28.933  1.00 43.55 ? 17  ASP   A OD2 1 
ATOM   163  N N   . ALA   A 1 21  ? -15.227 30.555  27.168  1.00 35.16 ? 18  ALA   A N   1 
ATOM   164  C CA  . ALA   A 1 21  ? -14.860 29.327  27.865  1.00 37.72 ? 18  ALA   A CA  1 
ATOM   165  C C   . ALA   A 1 21  ? -14.743 29.558  29.367  1.00 40.12 ? 18  ALA   A C   1 
ATOM   166  O O   . ALA   A 1 21  ? -15.239 28.753  30.163  1.00 36.34 ? 18  ALA   A O   1 
ATOM   167  C CB  . ALA   A 1 21  ? -13.553 28.777  27.295  1.00 32.75 ? 18  ALA   A CB  1 
ATOM   168  N N   . ALA   A 1 22  ? -14.098 30.661  29.768  1.00 37.12 ? 19  ALA   A N   1 
ATOM   169  C CA  . ALA   A 1 22  ? -13.961 30.986  31.183  1.00 41.96 ? 19  ALA   A CA  1 
ATOM   170  C C   . ALA   A 1 22  ? -15.308 31.032  31.889  1.00 40.20 ? 19  ALA   A C   1 
ATOM   171  O O   . ALA   A 1 22  ? -15.400 30.723  33.083  1.00 40.22 ? 19  ALA   A O   1 
ATOM   172  C CB  . ALA   A 1 22  ? -13.232 32.325  31.337  1.00 44.41 ? 19  ALA   A CB  1 
ATOM   173  N N   . ARG   A 1 23  ? -16.364 31.388  31.166  1.00 42.19 ? 20  ARG   A N   1 
ATOM   174  C CA  . ARG   A 1 23  ? -17.691 31.545  31.748  1.00 38.45 ? 20  ARG   A CA  1 
ATOM   175  C C   . ARG   A 1 23  ? -18.532 30.282  31.636  1.00 42.44 ? 20  ARG   A C   1 
ATOM   176  O O   . ARG   A 1 23  ? -19.294 29.963  32.559  1.00 41.17 ? 20  ARG   A O   1 
ATOM   177  C CB  . ARG   A 1 23  ? -18.403 32.716  31.067  1.00 37.60 ? 20  ARG   A CB  1 
ATOM   178  C CG  . ARG   A 1 23  ? -19.901 32.750  31.250  1.00 35.62 ? 20  ARG   A CG  1 
ATOM   179  C CD  . ARG   A 1 23  ? -20.480 33.959  30.516  1.00 41.44 ? 20  ARG   A CD  1 
ATOM   180  N NE  . ARG   A 1 23  ? -21.936 34.008  30.586  1.00 39.35 ? 20  ARG   A NE  1 
ATOM   181  C CZ  . ARG   A 1 23  ? -22.686 34.852  29.889  1.00 41.55 ? 20  ARG   A CZ  1 
ATOM   182  N NH1 . ARG   A 1 23  ? -22.147 35.725  29.052  1.00 43.11 ? 20  ARG   A NH1 1 
ATOM   183  N NH2 . ARG   A 1 23  ? -24.009 34.821  30.036  1.00 37.17 ? 20  ARG   A NH2 1 
ATOM   184  N N   . ILE   A 1 24  ? -18.405 29.550  30.523  1.00 39.25 ? 21  ILE   A N   1 
ATOM   185  C CA  . ILE   A 1 24  ? -19.262 28.390  30.289  1.00 35.26 ? 21  ILE   A CA  1 
ATOM   186  C C   . ILE   A 1 24  ? -18.862 27.205  31.163  1.00 33.10 ? 21  ILE   A C   1 
ATOM   187  O O   . ILE   A 1 24  ? -19.710 26.377  31.515  1.00 36.83 ? 21  ILE   A O   1 
ATOM   188  C CB  . ILE   A 1 24  ? -19.234 28.009  28.799  1.00 37.03 ? 21  ILE   A CB  1 
ATOM   189  C CG1 . ILE   A 1 24  ? -20.027 29.028  27.974  1.00 41.66 ? 21  ILE   A CG1 1 
ATOM   190  C CG2 . ILE   A 1 24  ? -19.786 26.596  28.611  1.00 30.96 ? 21  ILE   A CG2 1 
ATOM   191  C CD1 . ILE   A 1 24  ? -19.370 29.404  26.653  1.00 44.55 ? 21  ILE   A CD1 1 
ATOM   192  N N   . TYR   A 1 25  ? -17.583 27.089  31.519  1.00 34.05 ? 22  TYR   A N   1 
ATOM   193  C CA  . TYR   A 1 25  ? -17.064 25.904  32.186  1.00 34.79 ? 22  TYR   A CA  1 
ATOM   194  C C   . TYR   A 1 25  ? -16.562 26.226  33.589  1.00 32.50 ? 22  TYR   A C   1 
ATOM   195  O O   . TYR   A 1 25  ? -16.024 27.305  33.850  1.00 35.84 ? 22  TYR   A O   1 
ATOM   196  C CB  . TYR   A 1 25  ? -15.922 25.265  31.374  1.00 33.54 ? 22  TYR   A CB  1 
ATOM   197  C CG  . TYR   A 1 25  ? -16.351 24.866  29.985  1.00 32.71 ? 22  TYR   A CG  1 
ATOM   198  C CD1 . TYR   A 1 25  ? -17.252 23.819  29.795  1.00 32.58 ? 22  TYR   A CD1 1 
ATOM   199  C CD2 . TYR   A 1 25  ? -15.887 25.549  28.867  1.00 33.77 ? 22  TYR   A CD2 1 
ATOM   200  C CE1 . TYR   A 1 25  ? -17.659 23.445  28.534  1.00 30.98 ? 22  TYR   A CE1 1 
ATOM   201  C CE2 . TYR   A 1 25  ? -16.299 25.183  27.594  1.00 30.58 ? 22  TYR   A CE2 1 
ATOM   202  C CZ  . TYR   A 1 25  ? -17.187 24.136  27.435  1.00 31.25 ? 22  TYR   A CZ  1 
ATOM   203  O OH  . TYR   A 1 25  ? -17.602 23.759  26.169  1.00 36.45 ? 22  TYR   A OH  1 
ATOM   204  N N   . GLU   A 1 26  ? -16.700 25.246  34.477  1.00 39.13 ? 23  GLU   A N   1 
ATOM   205  C CA  . GLU   A 1 26  ? -16.178 25.359  35.830  1.00 38.35 ? 23  GLU   A CA  1 
ATOM   206  C C   . GLU   A 1 26  ? -15.474 24.057  36.198  1.00 37.16 ? 23  GLU   A C   1 
ATOM   207  O O   . GLU   A 1 26  ? -16.011 22.983  35.970  1.00 35.44 ? 23  GLU   A O   1 
ATOM   208  C CB  . GLU   A 1 26  ? -17.292 25.628  36.812  1.00 39.93 ? 23  GLU   A CB  1 
ATOM   209  C CG  . GLU   A 1 26  ? -16.884 25.470  38.260  1.00 45.81 ? 23  GLU   A CG  1 
ATOM   210  C CD  . GLU   A 1 26  ? -18.026 25.742  39.209  1.00 50.58 ? 23  GLU   A CD  1 
ATOM   211  O OE1 . GLU   A 1 26  ? -19.101 26.160  38.742  1.00 50.25 ? 23  GLU   A OE1 1 
ATOM   212  O OE2 . GLU   A 1 26  ? -17.846 25.533  40.421  1.00 58.01 ? 23  GLU   A OE2 1 
ATOM   213  N N   . LYS   A 1 27  ? -14.279 24.145  36.754  1.00 30.80 ? 24  LYS   A N   1 
ATOM   214  C CA  . LYS   A 1 27  ? -13.508 22.968  37.151  1.00 32.88 ? 24  LYS   A CA  1 
ATOM   215  C C   . LYS   A 1 27  ? -13.923 22.547  38.556  1.00 38.25 ? 24  LYS   A C   1 
ATOM   216  O O   . LYS   A 1 27  ? -13.804 23.340  39.499  1.00 38.12 ? 24  LYS   A O   1 
ATOM   217  C CB  . LYS   A 1 27  ? -12.007 23.242  37.121  1.00 31.99 ? 24  LYS   A CB  1 
ATOM   218  C CG  . LYS   A 1 27  ? -11.168 22.003  37.425  1.00 36.56 ? 24  LYS   A CG  1 
ATOM   219  C CD  . LYS   A 1 27  ? -9.674  22.316  37.395  1.00 42.07 ? 24  LYS   A CD  1 
ATOM   220  C CE  . LYS   A 1 27  ? -9.244  23.122  38.619  1.00 43.56 ? 24  LYS   A CE  1 
ATOM   221  N NZ  . LYS   A 1 27  ? -7.813  23.526  38.516  1.00 50.19 ? 24  LYS   A NZ  1 
ATOM   222  N N   . VAL   A 1 28  ? -14.395 21.305  38.695  1.00 35.90 ? 25  VAL   A N   1 
ATOM   223  C CA  . VAL   A 1 28  ? -14.899 20.788  39.961  1.00 39.08 ? 25  VAL   A CA  1 
ATOM   224  C C   . VAL   A 1 28  ? -14.087 19.565  40.377  1.00 42.36 ? 25  VAL   A C   1 
ATOM   225  O O   . VAL   A 1 28  ? -13.468 18.882  39.556  1.00 36.61 ? 25  VAL   A O   1 
ATOM   226  C CB  . VAL   A 1 28  ? -16.392 20.426  39.883  1.00 36.69 ? 25  VAL   A CB  1 
ATOM   227  C CG1 . VAL   A 1 28  ? -17.172 21.555  39.221  1.00 43.48 ? 25  VAL   A CG1 1 
ATOM   228  C CG2 . VAL   A 1 28  ? -16.581 19.104  39.135  1.00 33.32 ? 25  VAL   A CG2 1 
ATOM   229  N N   . GLU   A 1 29  ? -14.104 19.295  41.682  1.00 39.62 ? 26  GLU   A N   1 
ATOM   230  C CA  . GLU   A 1 29  ? -13.534 18.079  42.249  1.00 39.94 ? 26  GLU   A CA  1 
ATOM   231  C C   . GLU   A 1 29  ? -14.642 17.046  42.404  1.00 40.07 ? 26  GLU   A C   1 
ATOM   232  O O   . GLU   A 1 29  ? -15.727 17.365  42.900  1.00 40.17 ? 26  GLU   A O   1 
ATOM   233  C CB  . GLU   A 1 29  ? -12.873 18.374  43.594  1.00 47.14 ? 26  GLU   A CB  1 
ATOM   234  C CG  . GLU   A 1 29  ? -12.102 17.214  44.185  1.00 50.90 ? 26  GLU   A CG  1 
ATOM   235  C CD  . GLU   A 1 29  ? -11.443 17.582  45.503  1.00 58.65 ? 26  GLU   A CD  1 
ATOM   236  O OE1 . GLU   A 1 29  ? -11.121 18.781  45.691  1.00 58.32 ? 26  GLU   A OE1 1 
ATOM   237  O OE2 . GLU   A 1 29  ? -11.263 16.675  46.349  1.00 58.51 ? 26  GLU   A OE2 1 
ATOM   238  N N   . THR   A 1 30  ? -14.387 15.819  41.956  1.00 39.24 ? 27  THR   A N   1 
ATOM   239  C CA  . THR   A 1 30  ? -15.420 14.792  41.937  1.00 36.31 ? 27  THR   A CA  1 
ATOM   240  C C   . THR   A 1 30  ? -14.855 13.506  42.515  1.00 40.75 ? 27  THR   A C   1 
ATOM   241  O O   . THR   A 1 30  ? -13.815 13.020  42.057  1.00 39.47 ? 27  THR   A O   1 
ATOM   242  C CB  . THR   A 1 30  ? -15.950 14.558  40.514  1.00 36.70 ? 27  THR   A CB  1 
ATOM   243  O OG1 . THR   A 1 30  ? -16.482 15.782  39.999  1.00 37.05 ? 27  THR   A OG1 1 
ATOM   244  C CG2 . THR   A 1 30  ? -17.055 13.509  40.507  1.00 35.04 ? 27  THR   A CG2 1 
ATOM   245  N N   . GLU   A 1 31  ? -15.529 12.969  43.530  1.00 37.13 ? 28  GLU   A N   1 
ATOM   246  C CA  . GLU   A 1 31  ? -15.152 11.681  44.094  1.00 39.62 ? 28  GLU   A CA  1 
ATOM   247  C C   . GLU   A 1 31  ? -15.651 10.575  43.180  1.00 38.70 ? 28  GLU   A C   1 
ATOM   248  O O   . GLU   A 1 31  ? -16.855 10.486  42.913  1.00 40.28 ? 28  GLU   A O   1 
ATOM   249  C CB  . GLU   A 1 31  ? -15.738 11.522  45.495  1.00 46.95 ? 28  GLU   A CB  1 
ATOM   250  C CG  . GLU   A 1 31  ? -15.469 10.159  46.112  1.00 47.72 ? 28  GLU   A CG  1 
ATOM   251  C CD  . GLU   A 1 31  ? -15.944 10.075  47.549  1.00 57.29 ? 28  GLU   A CD  1 
ATOM   252  O OE1 . GLU   A 1 31  ? -15.210 10.549  48.446  1.00 57.37 ? 28  GLU   A OE1 1 
ATOM   253  O OE2 . GLU   A 1 31  ? -17.058 9.547   47.775  1.00 63.32 ? 28  GLU   A OE2 1 
ATOM   254  N N   . LEU   A 1 32  ? -14.738 9.729   42.710  1.00 36.89 ? 29  LEU   A N   1 
ATOM   255  C CA  . LEU   A 1 32  ? -15.049 8.699   41.721  1.00 39.39 ? 29  LEU   A CA  1 
ATOM   256  C C   . LEU   A 1 32  ? -14.980 7.323   42.374  1.00 34.29 ? 29  LEU   A C   1 
ATOM   257  O O   . LEU   A 1 32  ? -13.938 6.939   42.916  1.00 36.80 ? 29  LEU   A O   1 
ATOM   258  C CB  . LEU   A 1 32  ? -14.087 8.771   40.532  1.00 31.25 ? 29  LEU   A CB  1 
ATOM   259  C CG  . LEU   A 1 32  ? -14.234 7.692   39.459  1.00 35.28 ? 29  LEU   A CG  1 
ATOM   260  C CD1 . LEU   A 1 32  ? -15.649 7.684   38.895  1.00 35.27 ? 29  LEU   A CD1 1 
ATOM   261  C CD2 . LEU   A 1 32  ? -13.211 7.911   38.338  1.00 33.74 ? 29  LEU   A CD2 1 
ATOM   262  N N   . ASN   A 1 33  ? -16.074 6.574   42.288  1.00 36.37 ? 30  ASN   A N   1 
ATOM   263  C CA  . ASN   A 1 33  ? -16.091 5.204   42.777  1.00 37.89 ? 30  ASN   A CA  1 
ATOM   264  C C   . ASN   A 1 33  ? -15.151 4.348   41.940  1.00 40.35 ? 30  ASN   A C   1 
ATOM   265  O O   . ASN   A 1 33  ? -15.327 4.237   40.724  1.00 41.95 ? 30  ASN   A O   1 
ATOM   266  C CB  . ASN   A 1 33  ? -17.510 4.645   42.717  1.00 41.99 ? 30  ASN   A CB  1 
ATOM   267  C CG  . ASN   A 1 33  ? -17.562 3.165   43.047  1.00 47.28 ? 30  ASN   A CG  1 
ATOM   268  O OD1 . ASN   A 1 33  ? -16.640 2.629   43.664  1.00 45.93 ? 30  ASN   A OD1 1 
ATOM   269  N ND2 . ASN   A 1 33  ? -18.637 2.495   42.634  1.00 50.03 ? 30  ASN   A ND2 1 
ATOM   270  N N   . THR   A 1 34  ? -14.175 3.711   42.583  1.00 36.11 ? 31  THR   A N   1 
ATOM   271  C CA  . THR   A 1 34  ? -13.208 2.896   41.867  1.00 39.83 ? 31  THR   A CA  1 
ATOM   272  C C   . THR   A 1 34  ? -13.554 1.407   41.881  1.00 41.45 ? 31  THR   A C   1 
ATOM   273  O O   . THR   A 1 34  ? -12.714 0.577   41.508  1.00 36.80 ? 31  THR   A O   1 
ATOM   274  C CB  . THR   A 1 34  ? -11.801 3.136   42.424  1.00 41.98 ? 31  THR   A CB  1 
ATOM   275  O OG1 . THR   A 1 34  ? -11.790 2.911   43.834  1.00 41.28 ? 31  THR   A OG1 1 
ATOM   276  C CG2 . THR   A 1 34  ? -11.374 4.577   42.149  1.00 39.38 ? 31  THR   A CG2 1 
ATOM   277  N N   . ARG   A 1 35  ? -14.769 1.051   42.288  1.00 40.22 ? 32  ARG   A N   1 
ATOM   278  C CA  . ARG   A 1 35  ? -15.235 -0.328  42.246  1.00 40.33 ? 32  ARG   A CA  1 
ATOM   279  C C   . ARG   A 1 35  ? -15.814 -0.615  40.866  1.00 38.27 ? 32  ARG   A C   1 
ATOM   280  O O   . ARG   A 1 35  ? -16.735 0.075   40.417  1.00 42.09 ? 32  ARG   A O   1 
ATOM   281  C CB  . ARG   A 1 35  ? -16.278 -0.576  43.334  1.00 48.65 ? 32  ARG   A CB  1 
ATOM   282  C CG  . ARG   A 1 35  ? -17.352 -1.552  42.910  1.00 57.04 ? 32  ARG   A CG  1 
ATOM   283  C CD  . ARG   A 1 35  ? -18.309 -1.867  44.046  1.00 67.07 ? 32  ARG   A CD  1 
ATOM   284  N NE  . ARG   A 1 35  ? -19.187 -2.971  43.679  1.00 74.32 ? 32  ARG   A NE  1 
ATOM   285  C CZ  . ARG   A 1 35  ? -18.797 -4.236  43.586  1.00 78.26 ? 32  ARG   A CZ  1 
ATOM   286  N NH1 . ARG   A 1 35  ? -17.545 -4.595  43.836  1.00 70.28 ? 32  ARG   A NH1 1 
ATOM   287  N NH2 . ARG   A 1 35  ? -19.682 -5.163  43.229  1.00 79.98 ? 32  ARG   A NH2 1 
ATOM   288  N N   . LEU   A 1 36  ? -15.286 -1.635  40.201  1.00 35.74 ? 33  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 36  ? -15.527 -1.847  38.781  1.00 33.17 ? 33  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 36  ? -16.487 -3.009  38.551  1.00 35.87 ? 33  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 36  ? -16.320 -4.083  39.138  1.00 34.18 ? 33  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 36  ? -14.207 -2.118  38.054  1.00 30.25 ? 33  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 36  ? -13.138 -1.022  38.163  1.00 29.22 ? 33  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 36  ? -11.943 -1.403  37.310  1.00 28.38 ? 33  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 36  ? -13.717 0.303   37.719  1.00 30.34 ? 33  LEU   A CD2 1 
ATOM   296  N N   . GLY   A 1 37  ? -17.467 -2.797  37.670  1.00 32.26 ? 34  GLY   A N   1 
ATOM   297  C CA  . GLY   A 1 37  ? -18.248 -3.891  37.139  1.00 30.66 ? 34  GLY   A CA  1 
ATOM   298  C C   . GLY   A 1 37  ? -17.404 -4.813  36.275  1.00 35.24 ? 34  GLY   A C   1 
ATOM   299  O O   . GLY   A 1 37  ? -16.242 -4.543  35.975  1.00 33.61 ? 34  GLY   A O   1 
ATOM   300  N N   . GLU   A 1 38  ? -18.010 -5.932  35.870  1.00 32.23 ? 35  GLU   A N   1 
ATOM   301  C CA  . GLU   A 1 38  ? -17.265 -6.996  35.197  1.00 34.57 ? 35  GLU   A CA  1 
ATOM   302  C C   . GLU   A 1 38  ? -16.458 -6.484  34.004  1.00 32.86 ? 35  GLU   A C   1 
ATOM   303  O O   . GLU   A 1 38  ? -15.324 -6.919  33.780  1.00 32.04 ? 35  GLU   A O   1 
ATOM   304  C CB  . GLU   A 1 38  ? -18.224 -8.097  34.735  1.00 35.46 ? 35  GLU   A CB  1 
ATOM   305  C CG  . GLU   A 1 38  ? -18.787 -8.934  35.870  1.00 40.81 ? 35  GLU   A CG  1 
ATOM   306  C CD  . GLU   A 1 38  ? -19.820 -8.194  36.696  1.00 39.94 ? 35  GLU   A CD  1 
ATOM   307  O OE1 . GLU   A 1 38  ? -20.487 -7.286  36.153  1.00 42.81 ? 35  GLU   A OE1 1 
ATOM   308  O OE2 . GLU   A 1 38  ? -19.971 -8.531  37.890  1.00 47.74 ? 35  GLU   A OE2 1 
ATOM   309  N N   . GLU   A 1 39  ? -17.034 -5.574  33.225  1.00 30.36 ? 36  GLU   A N   1 
ATOM   310  C CA  . GLU   A 1 39  ? -16.442 -5.099  31.984  1.00 32.11 ? 36  GLU   A CA  1 
ATOM   311  C C   . GLU   A 1 39  ? -15.905 -3.681  32.068  1.00 34.48 ? 36  GLU   A C   1 
ATOM   312  O O   . GLU   A 1 39  ? -15.417 -3.164  31.057  1.00 31.91 ? 36  GLU   A O   1 
ATOM   313  C CB  . GLU   A 1 39  ? -17.473 -5.160  30.847  1.00 37.10 ? 36  GLU   A CB  1 
ATOM   314  C CG  . GLU   A 1 39  ? -17.844 -6.563  30.421  1.00 36.48 ? 36  GLU   A CG  1 
ATOM   315  C CD  . GLU   A 1 39  ? -18.881 -6.573  29.318  1.00 37.40 ? 36  GLU   A CD  1 
ATOM   316  O OE1 . GLU   A 1 39  ? -20.055 -6.254  29.595  1.00 38.71 ? 36  GLU   A OE1 1 
ATOM   317  O OE2 . GLU   A 1 39  ? -18.509 -6.898  28.173  1.00 36.40 ? 36  GLU   A OE2 1 
ATOM   318  N N   . GLN   A 1 40  ? -15.990 -3.033  33.226  1.00 28.96 ? 37  GLN   A N   1 
ATOM   319  C CA  . GLN   A 1 40  ? -15.616 -1.631  33.294  1.00 31.13 ? 37  GLN   A CA  1 
ATOM   320  C C   . GLN   A 1 40  ? -14.115 -1.476  33.507  1.00 30.15 ? 37  GLN   A C   1 
ATOM   321  O O   . GLN   A 1 40  ? -13.420 -2.386  33.969  1.00 29.81 ? 37  GLN   A O   1 
ATOM   322  C CB  . GLN   A 1 40  ? -16.353 -0.920  34.421  1.00 27.68 ? 37  GLN   A CB  1 
ATOM   323  C CG  . GLN   A 1 40  ? -17.823 -0.755  34.188  1.00 32.73 ? 37  GLN   A CG  1 
ATOM   324  C CD  . GLN   A 1 40  ? -18.479 -0.031  35.338  1.00 31.17 ? 37  GLN   A CD  1 
ATOM   325  O OE1 . GLN   A 1 40  ? -18.107 -0.224  36.491  1.00 31.35 ? 37  GLN   A OE1 1 
ATOM   326  N NE2 . GLN   A 1 40  ? -19.445 0.820   35.028  1.00 31.50 ? 37  GLN   A NE2 1 
ATOM   327  N N   . MET   A 1 41  ? -13.630 -0.284  33.171  1.00 28.53 ? 38  MET   A N   1 
ATOM   328  C CA  . MET   A 1 41  ? -12.238 0.091   33.332  1.00 26.18 ? 38  MET   A CA  1 
ATOM   329  C C   . MET   A 1 41  ? -12.181 1.408   34.085  1.00 27.09 ? 38  MET   A C   1 
ATOM   330  O O   . MET   A 1 41  ? -13.042 2.275   33.896  1.00 26.17 ? 38  MET   A O   1 
ATOM   331  C CB  . MET   A 1 41  ? -11.541 0.220   31.958  1.00 25.79 ? 38  MET   A CB  1 
ATOM   332  C CG  . MET   A 1 41  ? -11.161 -1.104  31.311  1.00 29.33 ? 38  MET   A CG  1 
ATOM   333  S SD  . MET   A 1 41  ? -11.093 -0.916  29.486  1.00 31.35 ? 38  MET   A SD  1 
ATOM   334  C CE  . MET   A 1 41  ? -12.556 -0.008  29.193  1.00 28.93 ? 38  MET   A CE  1 
ATOM   335  N N   . LEU   A 1 42  ? -11.184 1.546   34.952  1.00 25.98 ? 39  LEU   A N   1 
ATOM   336  C CA  . LEU   A 1 42  ? -10.820 2.844   35.516  1.00 25.61 ? 39  LEU   A CA  1 
ATOM   337  C C   . LEU   A 1 42  ? -9.748  3.454   34.615  1.00 24.18 ? 39  LEU   A C   1 
ATOM   338  O O   . LEU   A 1 42  ? -8.700  2.844   34.395  1.00 23.73 ? 39  LEU   A O   1 
ATOM   339  C CB  . LEU   A 1 42  ? -10.303 2.693   36.948  1.00 24.41 ? 39  LEU   A CB  1 
ATOM   340  C CG  . LEU   A 1 42  ? -9.720  3.958   37.579  1.00 27.52 ? 39  LEU   A CG  1 
ATOM   341  C CD1 . LEU   A 1 42  ? -10.798 5.017   37.689  1.00 25.15 ? 39  LEU   A CD1 1 
ATOM   342  C CD2 . LEU   A 1 42  ? -9.082  3.664   38.960  1.00 25.75 ? 39  LEU   A CD2 1 
ATOM   343  N N   . LEU   A 1 43  ? -10.007 4.647   34.097  1.00 23.60 ? 40  LEU   A N   1 
ATOM   344  C CA  . LEU   A 1 43  ? -9.166  5.239   33.062  1.00 26.49 ? 40  LEU   A CA  1 
ATOM   345  C C   . LEU   A 1 43  ? -8.627  6.585   33.513  1.00 23.62 ? 40  LEU   A C   1 
ATOM   346  O O   . LEU   A 1 43  ? -9.325  7.352   34.181  1.00 25.55 ? 40  LEU   A O   1 
ATOM   347  C CB  . LEU   A 1 43  ? -9.949  5.410   31.755  1.00 25.19 ? 40  LEU   A CB  1 
ATOM   348  C CG  . LEU   A 1 43  ? -10.443 4.096   31.157  1.00 24.02 ? 40  LEU   A CG  1 
ATOM   349  C CD1 . LEU   A 1 43  ? -11.966 4.143   30.956  1.00 23.80 ? 40  LEU   A CD1 1 
ATOM   350  C CD2 . LEU   A 1 43  ? -9.730  3.827   29.840  1.00 23.58 ? 40  LEU   A CD2 1 
ATOM   351  N N   . LYS   A 1 44  ? -7.368  6.846   33.162  1.00 25.84 ? 41  LYS   A N   1 
ATOM   352  C CA  . LYS   A 1 44  ? -6.711  8.123   33.392  1.00 25.29 ? 41  LYS   A CA  1 
ATOM   353  C C   . LYS   A 1 44  ? -6.479  8.817   32.051  1.00 21.71 ? 41  LYS   A C   1 
ATOM   354  O O   . LYS   A 1 44  ? -5.896  8.229   31.138  1.00 23.08 ? 41  LYS   A O   1 
ATOM   355  C CB  . LYS   A 1 44  ? -5.378  7.917   34.107  1.00 23.66 ? 41  LYS   A CB  1 
ATOM   356  C CG  . LYS   A 1 44  ? -4.675  9.205   34.454  1.00 29.02 ? 41  LYS   A CG  1 
ATOM   357  C CD  . LYS   A 1 44  ? -3.267  8.949   34.955  1.00 31.82 ? 41  LYS   A CD  1 
ATOM   358  C CE  . LYS   A 1 44  ? -2.648  10.222  35.504  1.00 40.27 ? 41  LYS   A CE  1 
ATOM   359  N NZ  . LYS   A 1 44  ? -1.227  9.996   35.894  1.00 45.89 ? 41  LYS   A NZ  1 
ATOM   360  N N   . THR   A 1 45  ? -6.921  10.065  31.955  1.00 21.60 ? 42  THR   A N   1 
ATOM   361  C CA  . THR   A 1 45  ? -6.767  10.863  30.747  1.00 25.64 ? 42  THR   A CA  1 
ATOM   362  C C   . THR   A 1 45  ? -5.323  11.331  30.578  1.00 29.23 ? 42  THR   A C   1 
ATOM   363  O O   . THR   A 1 45  ? -4.735  11.914  31.494  1.00 25.03 ? 42  THR   A O   1 
ATOM   364  C CB  . THR   A 1 45  ? -7.713  12.053  30.834  1.00 25.48 ? 42  THR   A CB  1 
ATOM   365  O OG1 . THR   A 1 45  ? -9.038  11.560  31.084  1.00 22.78 ? 42  THR   A OG1 1 
ATOM   366  C CG2 . THR   A 1 45  ? -7.699  12.878  29.541  1.00 22.59 ? 42  THR   A CG2 1 
ATOM   367  N N   . LEU   A 1 46  ? -4.736  11.055  29.412  1.00 23.55 ? 43  LEU   A N   1 
ATOM   368  C CA  . LEU   A 1 46  ? -3.391  11.528  29.084  1.00 25.41 ? 43  LEU   A CA  1 
ATOM   369  C C   . LEU   A 1 46  ? -3.404  12.771  28.206  1.00 27.62 ? 43  LEU   A C   1 
ATOM   370  O O   . LEU   A 1 46  ? -2.594  13.676  28.419  1.00 24.37 ? 43  LEU   A O   1 
ATOM   371  C CB  . LEU   A 1 46  ? -2.588  10.430  28.376  1.00 23.60 ? 43  LEU   A CB  1 
ATOM   372  C CG  . LEU   A 1 46  ? -2.408  9.071   29.072  1.00 31.06 ? 43  LEU   A CG  1 
ATOM   373  C CD1 . LEU   A 1 46  ? -1.416  8.210   28.304  1.00 28.06 ? 43  LEU   A CD1 1 
ATOM   374  C CD2 . LEU   A 1 46  ? -1.951  9.258   30.506  1.00 27.62 ? 43  LEU   A CD2 1 
ATOM   375  N N   . TYR   A 1 47  ? -4.293  12.820  27.215  1.00 24.54 ? 44  TYR   A N   1 
ATOM   376  C CA  . TYR   A 1 47  ? -4.463  13.974  26.335  1.00 25.09 ? 44  TYR   A CA  1 
ATOM   377  C C   . TYR   A 1 47  ? -5.946  14.165  26.054  1.00 26.08 ? 44  TYR   A C   1 
ATOM   378  O O   . TYR   A 1 47  ? -6.714  13.196  26.031  1.00 22.27 ? 44  TYR   A O   1 
ATOM   379  C CB  . TYR   A 1 47  ? -3.744  13.816  24.972  1.00 24.15 ? 44  TYR   A CB  1 
ATOM   380  C CG  . TYR   A 1 47  ? -2.270  13.462  25.030  1.00 23.83 ? 44  TYR   A CG  1 
ATOM   381  C CD1 . TYR   A 1 47  ? -1.867  12.155  25.234  1.00 23.65 ? 44  TYR   A CD1 1 
ATOM   382  C CD2 . TYR   A 1 47  ? -1.278  14.434  24.828  1.00 26.53 ? 44  TYR   A CD2 1 
ATOM   383  C CE1 . TYR   A 1 47  ? -0.524  11.807  25.285  1.00 24.34 ? 44  TYR   A CE1 1 
ATOM   384  C CE2 . TYR   A 1 47  ? 0.089   14.087  24.866  1.00 23.56 ? 44  TYR   A CE2 1 
ATOM   385  C CZ  . TYR   A 1 47  ? 0.450   12.770  25.099  1.00 28.04 ? 44  TYR   A CZ  1 
ATOM   386  O OH  . TYR   A 1 47  ? 1.781   12.380  25.159  1.00 31.88 ? 44  TYR   A OH  1 
ATOM   387  N N   . VAL   A 1 48  ? -6.345  15.411  25.822  1.00 24.42 ? 45  VAL   A N   1 
ATOM   388  C CA  . VAL   A 1 48  ? -7.708  15.698  25.397  1.00 23.52 ? 45  VAL   A CA  1 
ATOM   389  C C   . VAL   A 1 48  ? -7.656  16.641  24.207  1.00 26.49 ? 45  VAL   A C   1 
ATOM   390  O O   . VAL   A 1 48  ? -6.735  17.455  24.067  1.00 26.92 ? 45  VAL   A O   1 
ATOM   391  C CB  . VAL   A 1 48  ? -8.615  16.290  26.512  1.00 27.24 ? 45  VAL   A CB  1 
ATOM   392  C CG1 . VAL   A 1 48  ? -8.575  15.419  27.751  1.00 29.35 ? 45  VAL   A CG1 1 
ATOM   393  C CG2 . VAL   A 1 48  ? -8.231  17.709  26.837  1.00 26.83 ? 45  VAL   A CG2 1 
ATOM   394  N N   . SER   A 1 49  ? -8.653  16.504  23.336  1.00 23.12 ? 46  SER   A N   1 
ATOM   395  C CA  . SER   A 1 49  ? -8.812  17.352  22.172  1.00 24.22 ? 46  SER   A CA  1 
ATOM   396  C C   . SER   A 1 49  ? -9.766  18.492  22.489  1.00 25.04 ? 46  SER   A C   1 
ATOM   397  O O   . SER   A 1 49  ? -10.685 18.341  23.291  1.00 24.37 ? 46  SER   A O   1 
ATOM   398  C CB  . SER   A 1 49  ? -9.357  16.544  20.991  1.00 23.78 ? 46  SER   A CB  1 
ATOM   399  O OG  . SER   A 1 49  ? -9.389  17.321  19.809  1.00 25.63 ? 46  SER   A OG  1 
ATOM   400  N N   . VAL   A 1 50  ? -9.535  19.638  21.854  1.00 22.81 ? 47  VAL   A N   1 
ATOM   401  C CA  . VAL   A 1 50  ? -10.517 20.712  21.778  1.00 24.43 ? 47  VAL   A CA  1 
ATOM   402  C C   . VAL   A 1 50  ? -10.815 20.958  20.302  1.00 24.20 ? 47  VAL   A C   1 
ATOM   403  O O   . VAL   A 1 50  ? -9.903  20.920  19.469  1.00 25.80 ? 47  VAL   A O   1 
ATOM   404  C CB  . VAL   A 1 50  ? -10.010 22.001  22.462  1.00 26.05 ? 47  VAL   A CB  1 
ATOM   405  C CG1 . VAL   A 1 50  ? -9.664  21.724  23.928  1.00 29.05 ? 47  VAL   A CG1 1 
ATOM   406  C CG2 . VAL   A 1 50  ? -8.806  22.552  21.711  1.00 26.12 ? 47  VAL   A CG2 1 
ATOM   407  N N   . ASP   A 1 51  ? -12.088 21.192  19.979  1.00 25.80 ? 48  ASP   A N   1 
ATOM   408  C CA  . ASP   A 1 51  ? -12.533 21.243  18.590  1.00 25.98 ? 48  ASP   A CA  1 
ATOM   409  C C   . ASP   A 1 51  ? -13.695 22.210  18.459  1.00 26.54 ? 48  ASP   A C   1 
ATOM   410  O O   . ASP   A 1 51  ? -14.490 22.353  19.399  1.00 27.63 ? 48  ASP   A O   1 
ATOM   411  C CB  . ASP   A 1 51  ? -12.994 19.869  18.080  1.00 24.90 ? 48  ASP   A CB  1 
ATOM   412  C CG  . ASP   A 1 51  ? -11.942 18.800  18.242  1.00 27.85 ? 48  ASP   A CG  1 
ATOM   413  O OD1 . ASP   A 1 51  ? -11.839 18.219  19.355  1.00 25.17 ? 48  ASP   A OD1 1 
ATOM   414  O OD2 . ASP   A 1 51  ? -11.215 18.543  17.252  1.00 26.33 ? 48  ASP   A OD2 1 
ATOM   415  N N   . PRO   A 1 52  ? -13.846 22.854  17.302  1.00 28.54 ? 49  PRO   A N   1 
ATOM   416  C CA  . PRO   A 1 52  ? -15.032 23.692  17.071  1.00 26.56 ? 49  PRO   A CA  1 
ATOM   417  C C   . PRO   A 1 52  ? -16.346 22.968  17.270  1.00 28.34 ? 49  PRO   A C   1 
ATOM   418  O O   . PRO   A 1 52  ? -17.305 23.593  17.751  1.00 28.01 ? 49  PRO   A O   1 
ATOM   419  C CB  . PRO   A 1 52  ? -14.845 24.156  15.617  1.00 28.76 ? 49  PRO   A CB  1 
ATOM   420  C CG  . PRO   A 1 52  ? -13.333 24.264  15.488  1.00 28.86 ? 49  PRO   A CG  1 
ATOM   421  C CD  . PRO   A 1 52  ? -12.822 23.039  16.252  1.00 27.80 ? 49  PRO   A CD  1 
ATOM   422  N N   . TYR   A 1 53  ? -16.436 21.675  16.935  1.00 26.15 ? 50  TYR   A N   1 
ATOM   423  C CA  . TYR   A 1 53  ? -17.708 20.972  17.085  1.00 27.54 ? 50  TYR   A CA  1 
ATOM   424  C C   . TYR   A 1 53  ? -18.100 20.755  18.547  1.00 26.15 ? 50  TYR   A C   1 
ATOM   425  O O   . TYR   A 1 53  ? -19.234 20.332  18.809  1.00 26.85 ? 50  TYR   A O   1 
ATOM   426  C CB  . TYR   A 1 53  ? -17.681 19.625  16.332  1.00 24.60 ? 50  TYR   A CB  1 
ATOM   427  C CG  . TYR   A 1 53  ? -16.675 18.614  16.871  1.00 30.75 ? 50  TYR   A CG  1 
ATOM   428  C CD1 . TYR   A 1 53  ? -16.825 18.041  18.137  1.00 28.83 ? 50  TYR   A CD1 1 
ATOM   429  C CD2 . TYR   A 1 53  ? -15.591 18.216  16.099  1.00 26.19 ? 50  TYR   A CD2 1 
ATOM   430  C CE1 . TYR   A 1 53  ? -15.896 17.128  18.622  1.00 27.70 ? 50  TYR   A CE1 1 
ATOM   431  C CE2 . TYR   A 1 53  ? -14.668 17.303  16.574  1.00 26.11 ? 50  TYR   A CE2 1 
ATOM   432  C CZ  . TYR   A 1 53  ? -14.823 16.761  17.831  1.00 28.67 ? 50  TYR   A CZ  1 
ATOM   433  O OH  . TYR   A 1 53  ? -13.892 15.855  18.294  1.00 26.67 ? 50  TYR   A OH  1 
ATOM   434  N N   . LEU   A 1 54  ? -17.194 20.997  19.504  1.00 27.09 ? 51  LEU   A N   1 
ATOM   435  C CA  . LEU   A 1 54  ? -17.606 20.946  20.907  1.00 26.09 ? 51  LEU   A CA  1 
ATOM   436  C C   . LEU   A 1 54  ? -18.552 22.088  21.254  1.00 31.01 ? 51  LEU   A C   1 
ATOM   437  O O   . LEU   A 1 54  ? -19.297 21.987  22.236  1.00 27.13 ? 51  LEU   A O   1 
ATOM   438  C CB  . LEU   A 1 54  ? -16.389 20.971  21.836  1.00 24.97 ? 51  LEU   A CB  1 
ATOM   439  C CG  . LEU   A 1 54  ? -15.455 19.757  21.725  1.00 26.86 ? 51  LEU   A CG  1 
ATOM   440  C CD1 . LEU   A 1 54  ? -14.279 19.876  22.695  1.00 24.07 ? 51  LEU   A CD1 1 
ATOM   441  C CD2 . LEU   A 1 54  ? -16.226 18.443  21.934  1.00 25.97 ? 51  LEU   A CD2 1 
ATOM   442  N N   . GLN   A 1 55  ? -18.566 23.158  20.449  1.00 28.33 ? 52  GLN   A N   1 
ATOM   443  C CA  . GLN   A 1 55  ? -19.468 24.275  20.716  1.00 30.43 ? 52  GLN   A CA  1 
ATOM   444  C C   . GLN   A 1 55  ? -20.927 23.823  20.715  1.00 28.85 ? 52  GLN   A C   1 
ATOM   445  O O   . GLN   A 1 55  ? -21.716 24.245  21.572  1.00 30.17 ? 52  GLN   A O   1 
ATOM   446  C CB  . GLN   A 1 55  ? -19.232 25.385  19.688  1.00 29.98 ? 52  GLN   A CB  1 
ATOM   447  C CG  . GLN   A 1 55  ? -20.021 26.663  19.941  1.00 31.08 ? 52  GLN   A CG  1 
ATOM   448  C CD  . GLN   A 1 55  ? -21.379 26.642  19.275  1.00 26.74 ? 52  GLN   A CD  1 
ATOM   449  O OE1 . GLN   A 1 55  ? -21.795 25.628  18.710  1.00 27.82 ? 52  GLN   A OE1 1 
ATOM   450  N NE2 . GLN   A 1 55  ? -22.067 27.772  19.316  1.00 32.38 ? 52  GLN   A NE2 1 
ATOM   451  N N   . GLY   A 1 56  ? -21.300 22.947  19.769  1.00 27.22 ? 53  GLY   A N   1 
ATOM   452  C CA  . GLY   A 1 56  ? -22.682 22.485  19.694  1.00 27.62 ? 53  GLY   A CA  1 
ATOM   453  C C   . GLY   A 1 56  ? -22.992 21.325  20.616  1.00 31.74 ? 53  GLY   A C   1 
ATOM   454  O O   . GLY   A 1 56  ? -24.127 21.193  21.091  1.00 29.09 ? 53  GLY   A O   1 
ATOM   455  N N   . ILE   A 1 57  ? -22.018 20.456  20.863  1.00 31.51 ? 54  ILE   A N   1 
ATOM   456  C CA  . ILE   A 1 57  ? -22.197 19.400  21.852  1.00 31.72 ? 54  ILE   A CA  1 
ATOM   457  C C   . ILE   A 1 57  ? -22.404 20.010  23.236  1.00 28.26 ? 54  ILE   A C   1 
ATOM   458  O O   . ILE   A 1 57  ? -23.291 19.589  23.989  1.00 29.57 ? 54  ILE   A O   1 
ATOM   459  C CB  . ILE   A 1 57  ? -20.996 18.436  21.816  1.00 27.94 ? 54  ILE   A CB  1 
ATOM   460  C CG1 . ILE   A 1 57  ? -20.934 17.729  20.458  1.00 30.89 ? 54  ILE   A CG1 1 
ATOM   461  C CG2 . ILE   A 1 57  ? -21.077 17.420  22.976  1.00 31.74 ? 54  ILE   A CG2 1 
ATOM   462  C CD1 . ILE   A 1 57  ? -19.755 16.806  20.311  1.00 26.08 ? 54  ILE   A CD1 1 
ATOM   463  N N   . CYS   A 1 58  ? -21.606 21.029  23.577  1.00 30.28 ? 55  CYS   A N   1 
ATOM   464  C CA  . CYS   A 1 58  ? -21.771 21.744  24.840  1.00 32.38 ? 55  CYS   A CA  1 
ATOM   465  C C   . CYS   A 1 58  ? -23.203 22.223  25.034  1.00 34.12 ? 55  CYS   A C   1 
ATOM   466  O O   . CYS   A 1 58  ? -23.787 22.058  26.113  1.00 30.48 ? 55  CYS   A O   1 
ATOM   467  C CB  . CYS   A 1 58  ? -20.811 22.936  24.892  1.00 34.02 ? 55  CYS   A CB  1 
ATOM   468  S SG  . CYS   A 1 58  ? -20.879 23.908  26.450  1.00 33.41 ? 55  CYS   A SG  1 
ATOM   469  N N   . LEU   A 1 59  ? -23.776 22.851  23.999  1.00 29.87 ? 56  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 59  ? -25.141 23.371  24.085  1.00 34.31 ? 56  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 59  ? -26.172 22.266  24.211  1.00 34.39 ? 56  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 59  ? -27.307 22.546  24.606  1.00 33.72 ? 56  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 59  ? -25.476 24.228  22.858  1.00 31.99 ? 56  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 59  ? -24.779 25.575  22.683  1.00 31.08 ? 56  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 59  ? -25.040 26.093  21.274  1.00 35.61 ? 56  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 59  ? -25.290 26.575  23.713  1.00 37.18 ? 56  LEU   A CD2 1 
ATOM   477  N N   . ASP   A 1 60  ? -25.812 21.032  23.868  1.00 32.19 ? 57  ASP   A N   1 
ATOM   478  C CA  . ASP   A 1 60  ? -26.671 19.874  24.085  1.00 31.60 ? 57  ASP   A CA  1 
ATOM   479  C C   . ASP   A 1 60  ? -26.316 19.122  25.362  1.00 28.98 ? 57  ASP   A C   1 
ATOM   480  O O   . ASP   A 1 60  ? -26.867 18.048  25.616  1.00 32.10 ? 57  ASP   A O   1 
ATOM   481  C CB  . ASP   A 1 60  ? -26.603 18.924  22.891  1.00 33.28 ? 57  ASP   A CB  1 
ATOM   482  C CG  . ASP   A 1 60  ? -27.311 19.478  21.655  1.00 39.37 ? 57  ASP   A CG  1 
ATOM   483  O OD1 . ASP   A 1 60  ? -28.044 20.478  21.775  1.00 36.88 ? 57  ASP   A OD1 1 
ATOM   484  O OD2 . ASP   A 1 60  ? -27.140 18.903  20.562  1.00 37.22 ? 57  ASP   A OD2 1 
ATOM   485  N N   . THR   A 1 61  ? -25.400 19.647  26.153  1.00 29.53 ? 58  THR   A N   1 
ATOM   486  C CA  . THR   A 1 61  ? -24.983 18.960  27.375  1.00 29.59 ? 58  THR   A CA  1 
ATOM   487  C C   . THR   A 1 61  ? -25.779 19.495  28.557  1.00 34.17 ? 58  THR   A C   1 
ATOM   488  O O   . THR   A 1 61  ? -25.810 20.723  28.761  1.00 33.72 ? 58  THR   A O   1 
ATOM   489  C CB  . THR   A 1 61  ? -23.486 19.170  27.618  1.00 34.07 ? 58  THR   A CB  1 
ATOM   490  O OG1 . THR   A 1 61  ? -22.733 18.647  26.506  1.00 28.84 ? 58  THR   A OG1 1 
ATOM   491  C CG2 . THR   A 1 61  ? -23.036 18.491  28.936  1.00 29.46 ? 58  THR   A CG2 1 
ATOM   492  N N   . PRO   A 1 62  ? -26.451 18.653  29.341  1.00 33.59 ? 59  PRO   A N   1 
ATOM   493  C CA  . PRO   A 1 62  ? -27.161 19.161  30.525  1.00 37.10 ? 59  PRO   A CA  1 
ATOM   494  C C   . PRO   A 1 62  ? -26.237 19.946  31.446  1.00 37.11 ? 59  PRO   A C   1 
ATOM   495  O O   . PRO   A 1 62  ? -25.088 19.564  31.686  1.00 34.37 ? 59  PRO   A O   1 
ATOM   496  C CB  . PRO   A 1 62  ? -27.682 17.884  31.193  1.00 34.69 ? 59  PRO   A CB  1 
ATOM   497  C CG  . PRO   A 1 62  ? -27.906 16.954  30.024  1.00 37.88 ? 59  PRO   A CG  1 
ATOM   498  C CD  . PRO   A 1 62  ? -26.742 17.226  29.101  1.00 34.71 ? 59  PRO   A CD  1 
ATOM   499  N N   . ILE   A 1 63  ? -26.749 21.077  31.945  1.00 35.30 ? 60  ILE   A N   1 
ATOM   500  C CA  . ILE   A 1 63  ? -26.011 21.874  32.912  1.00 34.48 ? 60  ILE   A CA  1 
ATOM   501  C C   . ILE   A 1 63  ? -25.571 20.976  34.060  1.00 39.57 ? 60  ILE   A C   1 
ATOM   502  O O   . ILE   A 1 63  ? -26.344 20.150  34.558  1.00 35.95 ? 60  ILE   A O   1 
ATOM   503  C CB  . ILE   A 1 63  ? -26.885 23.037  33.417  1.00 41.71 ? 60  ILE   A CB  1 
ATOM   504  C CG1 . ILE   A 1 63  ? -27.355 23.900  32.243  1.00 38.22 ? 60  ILE   A CG1 1 
ATOM   505  C CG2 . ILE   A 1 63  ? -26.122 23.885  34.421  1.00 36.95 ? 60  ILE   A CG2 1 
ATOM   506  C CD1 . ILE   A 1 63  ? -26.225 24.672  31.592  1.00 37.20 ? 60  ILE   A CD1 1 
ATOM   507  N N   . GLY   A 1 64  ? -24.314 21.123  34.474  1.00 35.40 ? 61  GLY   A N   1 
ATOM   508  C CA  . GLY   A 1 64  ? -23.740 20.280  35.496  1.00 39.53 ? 61  GLY   A CA  1 
ATOM   509  C C   . GLY   A 1 64  ? -23.012 19.042  34.996  1.00 39.34 ? 61  GLY   A C   1 
ATOM   510  O O   . GLY   A 1 64  ? -22.222 18.463  35.754  1.00 37.56 ? 61  GLY   A O   1 
ATOM   511  N N   . ASP   A 1 65  ? -23.251 18.605  33.757  1.00 36.75 ? 62  ASP   A N   1 
ATOM   512  C CA  . ASP   A 1 65  ? -22.526 17.439  33.258  1.00 33.85 ? 62  ASP   A CA  1 
ATOM   513  C C   . ASP   A 1 65  ? -21.139 17.834  32.745  1.00 35.26 ? 62  ASP   A C   1 
ATOM   514  O O   . ASP   A 1 65  ? -20.882 18.983  32.371  1.00 33.94 ? 62  ASP   A O   1 
ATOM   515  C CB  . ASP   A 1 65  ? -23.303 16.741  32.144  1.00 35.07 ? 62  ASP   A CB  1 
ATOM   516  C CG  . ASP   A 1 65  ? -24.510 15.974  32.662  1.00 41.06 ? 62  ASP   A CG  1 
ATOM   517  O OD1 . ASP   A 1 65  ? -24.838 16.104  33.862  1.00 41.13 ? 62  ASP   A OD1 1 
ATOM   518  O OD2 . ASP   A 1 65  ? -25.132 15.237  31.859  1.00 39.59 ? 62  ASP   A OD2 1 
ATOM   519  N N   . HIS   A 1 66  ? -20.236 16.857  32.732  1.00 31.22 ? 63  HIS   A N   1 
ATOM   520  C CA  . HIS   A 1 66  ? -18.902 17.117  32.229  1.00 30.96 ? 63  HIS   A CA  1 
ATOM   521  C C   . HIS   A 1 66  ? -18.967 17.378  30.722  1.00 29.99 ? 63  HIS   A C   1 
ATOM   522  O O   . HIS   A 1 66  ? -19.909 16.972  30.034  1.00 27.92 ? 63  HIS   A O   1 
ATOM   523  C CB  . HIS   A 1 66  ? -17.962 15.940  32.539  1.00 26.85 ? 63  HIS   A CB  1 
ATOM   524  C CG  . HIS   A 1 66  ? -18.114 14.782  31.602  1.00 30.17 ? 63  HIS   A CG  1 
ATOM   525  N ND1 . HIS   A 1 66  ? -19.027 13.769  31.808  1.00 29.21 ? 63  HIS   A ND1 1 
ATOM   526  C CD2 . HIS   A 1 66  ? -17.471 14.479  30.446  1.00 28.69 ? 63  HIS   A CD2 1 
ATOM   527  C CE1 . HIS   A 1 66  ? -18.941 12.892  30.821  1.00 31.14 ? 63  HIS   A CE1 1 
ATOM   528  N NE2 . HIS   A 1 66  ? -18.008 13.303  29.978  1.00 28.65 ? 63  HIS   A NE2 1 
ATOM   529  N N   . MET   A 1 67  ? -17.953 18.081  30.219  1.00 31.59 ? 64  MET   A N   1 
ATOM   530  C CA  . MET   A 1 67  ? -17.848 18.379  28.791  1.00 31.74 ? 64  MET   A CA  1 
ATOM   531  C C   . MET   A 1 67  ? -17.227 17.198  28.053  1.00 28.75 ? 64  MET   A C   1 
ATOM   532  O O   . MET   A 1 67  ? -16.072 16.832  28.315  1.00 25.73 ? 64  MET   A O   1 
ATOM   533  C CB  . MET   A 1 67  ? -17.008 19.633  28.572  1.00 29.01 ? 64  MET   A CB  1 
ATOM   534  C CG  . MET   A 1 67  ? -16.903 20.020  27.097  1.00 26.80 ? 64  MET   A CG  1 
ATOM   535  S SD  . MET   A 1 67  ? -18.431 20.748  26.531  1.00 33.49 ? 64  MET   A SD  1 
ATOM   536  C CE  . MET   A 1 67  ? -19.193 19.494  25.568  1.00 34.55 ? 64  MET   A CE  1 
ATOM   537  N N   . GLY   A 1 68  ? -17.993 16.589  27.146  1.00 25.44 ? 65  GLY   A N   1 
ATOM   538  C CA  . GLY   A 1 68  ? -17.436 15.550  26.303  1.00 28.63 ? 65  GLY   A CA  1 
ATOM   539  C C   . GLY   A 1 68  ? -16.330 16.082  25.407  1.00 28.72 ? 65  GLY   A C   1 
ATOM   540  O O   . GLY   A 1 68  ? -16.235 17.274  25.115  1.00 27.41 ? 65  GLY   A O   1 
ATOM   541  N N   . ALA   A 1 69  ? -15.464 15.168  24.978  1.00 28.20 ? 66  ALA   A N   1 
ATOM   542  C CA  . ALA   A 1 69  ? -14.347 15.501  24.106  1.00 24.49 ? 66  ALA   A CA  1 
ATOM   543  C C   . ALA   A 1 69  ? -13.602 14.219  23.780  1.00 24.63 ? 66  ALA   A C   1 
ATOM   544  O O   . ALA   A 1 69  ? -13.597 13.283  24.590  1.00 23.63 ? 66  ALA   A O   1 
ATOM   545  C CB  . ALA   A 1 69  ? -13.404 16.520  24.752  1.00 24.79 ? 66  ALA   A CB  1 
ATOM   546  N N   . ASP   A 1 70  ? -13.003 14.155  22.595  1.00 22.51 ? 67  ASP   A N   1 
ATOM   547  C CA  . ASP   A 1 70  ? -12.117 13.051  22.239  1.00 23.54 ? 67  ASP   A CA  1 
ATOM   548  C C   . ASP   A 1 70  ? -10.861 13.082  23.111  1.00 22.10 ? 67  ASP   A C   1 
ATOM   549  O O   . ASP   A 1 70  ? -10.262 14.137  23.317  1.00 21.68 ? 67  ASP   A O   1 
ATOM   550  C CB  . ASP   A 1 70  ? -11.722 13.153  20.770  1.00 21.69 ? 67  ASP   A CB  1 
ATOM   551  C CG  . ASP   A 1 70  ? -11.275 11.824  20.194  1.00 28.87 ? 67  ASP   A CG  1 
ATOM   552  O OD1 . ASP   A 1 70  ? -11.459 10.788  20.879  1.00 29.71 ? 67  ASP   A OD1 1 
ATOM   553  O OD2 . ASP   A 1 70  ? -10.757 11.800  19.059  1.00 27.60 ? 67  ASP   A OD2 1 
ATOM   554  N N   . SER   A 1 71  ? -10.437 11.914  23.596  1.00 19.47 ? 68  SER   A N   1 
ATOM   555  C CA  . SER   A 1 71  ? -9.296  11.870  24.499  1.00 22.49 ? 68  SER   A CA  1 
ATOM   556  C C   . SER   A 1 71  ? -8.524  10.575  24.313  1.00 24.00 ? 68  SER   A C   1 
ATOM   557  O O   . SER   A 1 71  ? -9.013  9.608   23.716  1.00 20.15 ? 68  SER   A O   1 
ATOM   558  C CB  . SER   A 1 71  ? -9.734  11.999  25.962  1.00 21.04 ? 68  SER   A CB  1 
ATOM   559  O OG  . SER   A 1 71  ? -10.539 10.890  26.326  1.00 20.49 ? 68  SER   A OG  1 
ATOM   560  N N   . ILE   A 1 72  ? -7.293  10.586  24.824  1.00 18.74 ? 69  ILE   A N   1 
ATOM   561  C CA  . ILE   A 1 72  ? -6.445  9.404   24.933  1.00 20.05 ? 69  ILE   A CA  1 
ATOM   562  C C   . ILE   A 1 72  ? -6.348  9.057   26.412  1.00 23.82 ? 69  ILE   A C   1 
ATOM   563  O O   . ILE   A 1 72  ? -6.059  9.929   27.233  1.00 18.63 ? 69  ILE   A O   1 
ATOM   564  C CB  . ILE   A 1 72  ? -5.046  9.653   24.338  1.00 22.70 ? 69  ILE   A CB  1 
ATOM   565  C CG1 . ILE   A 1 72  ? -5.134  9.948   22.821  1.00 21.14 ? 69  ILE   A CG1 1 
ATOM   566  C CG2 . ILE   A 1 72  ? -4.112  8.465   24.612  1.00 18.93 ? 69  ILE   A CG2 1 
ATOM   567  C CD1 . ILE   A 1 72  ? -3.786  10.374  22.216  1.00 19.60 ? 69  ILE   A CD1 1 
ATOM   568  N N   . MET   A 1 73  ? -6.603  7.793   26.751  1.00 21.08 ? 70  MET   A N   1 
ATOM   569  C CA  . MET   A 1 73  ? -6.738  7.357   28.136  1.00 20.31 ? 70  MET   A CA  1 
ATOM   570  C C   . MET   A 1 73  ? -5.906  6.102   28.352  1.00 24.75 ? 70  MET   A C   1 
ATOM   571  O O   . MET   A 1 73  ? -5.694  5.323   27.417  1.00 22.62 ? 70  MET   A O   1 
ATOM   572  C CB  . MET   A 1 73  ? -8.203  7.063   28.484  1.00 17.84 ? 70  MET   A CB  1 
ATOM   573  C CG  . MET   A 1 73  ? -9.131  8.267   28.341  1.00 18.64 ? 70  MET   A CG  1 
ATOM   574  S SD  . MET   A 1 73  ? -10.858 7.775   28.195  1.00 24.62 ? 70  MET   A SD  1 
ATOM   575  C CE  . MET   A 1 73  ? -10.959 7.229   26.451  1.00 21.91 ? 70  MET   A CE  1 
ATOM   576  N N   . GLN   A 1 74  ? -5.427  5.913   29.591  1.00 21.90 ? 71  GLN   A N   1 
ATOM   577  C CA  . GLN   A 1 74  ? -4.689  4.714   29.957  1.00 22.65 ? 71  GLN   A CA  1 
ATOM   578  C C   . GLN   A 1 74  ? -5.463  3.953   31.021  1.00 20.23 ? 71  GLN   A C   1 
ATOM   579  O O   . GLN   A 1 74  ? -5.936  4.546   31.996  1.00 21.65 ? 71  GLN   A O   1 
ATOM   580  C CB  . GLN   A 1 74  ? -3.274  5.041   30.465  1.00 22.45 ? 71  GLN   A CB  1 
ATOM   581  C CG  . GLN   A 1 74  ? -2.431  3.793   30.695  1.00 23.55 ? 71  GLN   A CG  1 
ATOM   582  C CD  . GLN   A 1 74  ? -0.933  4.081   30.794  1.00 27.56 ? 71  GLN   A CD  1 
ATOM   583  O OE1 . GLN   A 1 74  ? -0.522  5.100   31.334  1.00 26.73 ? 71  GLN   A OE1 1 
ATOM   584  N NE2 . GLN   A 1 74  ? -0.119  3.176   30.265  1.00 24.83 ? 71  GLN   A NE2 1 
ATOM   585  N N   . VAL   A 1 75  ? -5.599  2.641   30.832  1.00 22.53 ? 72  VAL   A N   1 
ATOM   586  C CA  . VAL   A 1 75  ? -6.332  1.828   31.800  1.00 23.08 ? 72  VAL   A CA  1 
ATOM   587  C C   . VAL   A 1 75  ? -5.500  1.708   33.077  1.00 26.34 ? 72  VAL   A C   1 
ATOM   588  O O   . VAL   A 1 75  ? -4.339  1.280   33.044  1.00 24.50 ? 72  VAL   A O   1 
ATOM   589  C CB  . VAL   A 1 75  ? -6.662  0.446   31.231  1.00 25.83 ? 72  VAL   A CB  1 
ATOM   590  C CG1 . VAL   A 1 75  ? -7.463  -0.358  32.262  1.00 25.82 ? 72  VAL   A CG1 1 
ATOM   591  C CG2 . VAL   A 1 75  ? -7.433  0.566   29.904  1.00 25.36 ? 72  VAL   A CG2 1 
ATOM   592  N N   . LEU   A 1 76  ? -6.086  2.101   34.205  1.00 25.66 ? 73  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 76  ? -5.439  1.889   35.498  1.00 27.35 ? 73  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 76  ? -5.868  0.586   36.153  1.00 27.35 ? 73  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 76  ? -5.058  -0.063  36.823  1.00 29.27 ? 73  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 76  ? -5.741  3.054   36.443  1.00 26.79 ? 73  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 76  ? -5.313  4.444   35.982  1.00 28.14 ? 73  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 76  ? -5.774  5.475   37.013  1.00 30.10 ? 73  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 76  ? -3.812  4.504   35.787  1.00 31.63 ? 73  LEU   A CD2 1 
ATOM   600  N N   . ASP   A 1 77  ? -7.113  0.179   35.946  1.00 24.74 ? 74  ASP   A N   1 
ATOM   601  C CA  . ASP   A 1 77  ? -7.671  -1.033  36.530  1.00 30.46 ? 74  ASP   A CA  1 
ATOM   602  C C   . ASP   A 1 77  ? -8.812  -1.476  35.624  1.00 28.77 ? 74  ASP   A C   1 
ATOM   603  O O   . ASP   A 1 77  ? -9.352  -0.676  34.852  1.00 25.80 ? 74  ASP   A O   1 
ATOM   604  C CB  . ASP   A 1 77  ? -8.156  -0.769  37.964  1.00 29.86 ? 74  ASP   A CB  1 
ATOM   605  C CG  . ASP   A 1 77  ? -8.416  -2.050  38.754  1.00 35.72 ? 74  ASP   A CG  1 
ATOM   606  O OD1 . ASP   A 1 77  ? -7.913  -3.125  38.360  1.00 34.48 ? 74  ASP   A OD1 1 
ATOM   607  O OD2 . ASP   A 1 77  ? -9.145  -1.967  39.766  1.00 36.90 ? 74  ASP   A OD2 1 
ATOM   608  N N   . ALA   A 1 78  ? -9.193  -2.747  35.732  1.00 28.13 ? 75  ALA   A N   1 
ATOM   609  C CA  . ALA   A 1 78  ? -10.192 -3.277  34.812  1.00 29.56 ? 75  ALA   A CA  1 
ATOM   610  C C   . ALA   A 1 78  ? -10.920 -4.462  35.430  1.00 31.71 ? 75  ALA   A C   1 
ATOM   611  O O   . ALA   A 1 78  ? -10.305 -5.293  36.094  1.00 31.86 ? 75  ALA   A O   1 
ATOM   612  C CB  . ALA   A 1 78  ? -9.546  -3.714  33.490  1.00 29.74 ? 75  ALA   A CB  1 
ATOM   613  N N   . GLY   A 1 79  ? -12.222 -4.551  35.166  1.00 32.57 ? 76  GLY   A N   1 
ATOM   614  C CA  . GLY   A 1 79  ? -12.986 -5.721  35.526  1.00 31.97 ? 76  GLY   A CA  1 
ATOM   615  C C   . GLY   A 1 79  ? -12.477 -6.958  34.813  1.00 33.84 ? 76  GLY   A C   1 
ATOM   616  O O   . GLY   A 1 79  ? -11.713 -6.878  33.844  1.00 34.72 ? 76  GLY   A O   1 
ATOM   617  N N   . PRO   A 1 80  ? -12.899 -8.135  35.281  1.00 36.88 ? 77  PRO   A N   1 
ATOM   618  C CA  . PRO   A 1 80  ? -12.403 -9.384  34.674  1.00 31.63 ? 77  PRO   A CA  1 
ATOM   619  C C   . PRO   A 1 80  ? -12.715 -9.520  33.193  1.00 34.82 ? 77  PRO   A C   1 
ATOM   620  O O   . PRO   A 1 80  ? -11.947 -10.168 32.470  1.00 36.86 ? 77  PRO   A O   1 
ATOM   621  C CB  . PRO   A 1 80  ? -13.101 -10.476 35.497  1.00 34.13 ? 77  PRO   A CB  1 
ATOM   622  C CG  . PRO   A 1 80  ? -14.266 -9.783  36.163  1.00 36.84 ? 77  PRO   A CG  1 
ATOM   623  C CD  . PRO   A 1 80  ? -13.806 -8.388  36.418  1.00 36.67 ? 77  PRO   A CD  1 
ATOM   624  N N   . ASN   A 1 81  ? -13.820 -8.953  32.712  1.00 29.51 ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 81  ? -14.186 -9.077  31.305  1.00 37.04 ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 81  ? -14.045 -7.762  30.547  1.00 34.55 ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 81  ? -14.661 -7.590  29.491  1.00 33.53 ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 81  ? -15.608 -9.612  31.186  1.00 35.43 ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 81  ? -15.779 -10.920 31.915  1.00 35.85 ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 81  ? -16.443 -10.979 32.946  1.00 36.29 ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 81  ? -15.155 -11.974 31.395  1.00 34.60 ? 78  ASN   A ND2 1 
ATOM   632  N N   . ALA   A 1 82  ? -13.257 -6.829  31.075  1.00 33.57 ? 79  ALA   A N   1 
ATOM   633  C CA  . ALA   A 1 82  ? -13.031 -5.569  30.381  1.00 35.03 ? 79  ALA   A CA  1 
ATOM   634  C C   . ALA   A 1 82  ? -12.342 -5.832  29.043  1.00 30.82 ? 79  ALA   A C   1 
ATOM   635  O O   . ALA   A 1 82  ? -11.560 -6.775  28.913  1.00 30.22 ? 79  ALA   A O   1 
ATOM   636  C CB  . ALA   A 1 82  ? -12.174 -4.629  31.232  1.00 30.69 ? 79  ALA   A CB  1 
ATOM   637  N N   . PRO   A 1 83  ? -12.604 -5.002  28.035  1.00 30.30 ? 80  PRO   A N   1 
ATOM   638  C CA  . PRO   A 1 83  ? -11.953 -5.209  26.732  1.00 33.07 ? 80  PRO   A CA  1 
ATOM   639  C C   . PRO   A 1 83  ? -10.457 -4.956  26.756  1.00 34.17 ? 80  PRO   A C   1 
ATOM   640  O O   . PRO   A 1 83  ? -9.737  -5.512  25.919  1.00 32.99 ? 80  PRO   A O   1 
ATOM   641  C CB  . PRO   A 1 83  ? -12.675 -4.211  25.818  1.00 31.84 ? 80  PRO   A CB  1 
ATOM   642  C CG  . PRO   A 1 83  ? -13.145 -3.129  26.741  1.00 30.41 ? 80  PRO   A CG  1 
ATOM   643  C CD  . PRO   A 1 83  ? -13.469 -3.810  28.054  1.00 28.33 ? 80  PRO   A CD  1 
ATOM   644  N N   . PHE   A 1 84  ? -9.956  -4.149  27.688  1.00 33.40 ? 81  PHE   A N   1 
ATOM   645  C CA  . PHE   A 1 84  ? -8.540  -3.818  27.722  1.00 32.51 ? 81  PHE   A CA  1 
ATOM   646  C C   . PHE   A 1 84  ? -7.994  -4.020  29.129  1.00 34.50 ? 81  PHE   A C   1 
ATOM   647  O O   . PHE   A 1 84  ? -8.736  -3.989  30.113  1.00 35.15 ? 81  PHE   A O   1 
ATOM   648  C CB  . PHE   A 1 84  ? -8.320  -2.384  27.230  1.00 27.87 ? 81  PHE   A CB  1 
ATOM   649  C CG  . PHE   A 1 84  ? -9.015  -2.108  25.934  1.00 29.03 ? 81  PHE   A CG  1 
ATOM   650  C CD1 . PHE   A 1 84  ? -8.662  -2.807  24.793  1.00 29.37 ? 81  PHE   A CD1 1 
ATOM   651  C CD2 . PHE   A 1 84  ? -10.055 -1.208  25.872  1.00 26.46 ? 81  PHE   A CD2 1 
ATOM   652  C CE1 . PHE   A 1 84  ? -9.319  -2.586  23.596  1.00 30.41 ? 81  PHE   A CE1 1 
ATOM   653  C CE2 . PHE   A 1 84  ? -10.717 -0.983  24.673  1.00 30.52 ? 81  PHE   A CE2 1 
ATOM   654  C CZ  . PHE   A 1 84  ? -10.346 -1.674  23.542  1.00 27.67 ? 81  PHE   A CZ  1 
ATOM   655  N N   . ARG   A 1 85  ? -6.674  -4.248  29.209  1.00 32.03 ? 82  ARG   A N   1 
ATOM   656  C CA  . ARG   A 1 85  ? -5.988  -4.557  30.458  1.00 27.74 ? 82  ARG   A CA  1 
ATOM   657  C C   . ARG   A 1 85  ? -5.295  -3.323  31.013  1.00 34.55 ? 82  ARG   A C   1 
ATOM   658  O O   . ARG   A 1 85  ? -5.078  -2.335  30.300  1.00 30.07 ? 82  ARG   A O   1 
ATOM   659  C CB  . ARG   A 1 85  ? -4.959  -5.676  30.242  1.00 37.48 ? 82  ARG   A CB  1 
ATOM   660  C CG  . ARG   A 1 85  ? -5.516  -6.971  29.617  1.00 44.19 ? 82  ARG   A CG  1 
ATOM   661  C CD  . ARG   A 1 85  ? -6.988  -7.234  30.009  1.00 48.61 ? 82  ARG   A CD  1 
ATOM   662  N NE  . ARG   A 1 85  ? -7.141  -7.600  31.414  1.00 49.77 ? 82  ARG   A NE  1 
ATOM   663  C CZ  . ARG   A 1 85  ? -8.222  -7.349  32.141  1.00 46.85 ? 82  ARG   A CZ  1 
ATOM   664  N NH1 . ARG   A 1 85  ? -9.280  -6.743  31.621  1.00 45.78 ? 82  ARG   A NH1 1 
ATOM   665  N NH2 . ARG   A 1 85  ? -8.236  -7.695  33.424  1.00 47.23 ? 82  ARG   A NH2 1 
ATOM   666  N N   . PRO   A 1 86  ? -4.937  -3.342  32.296  1.00 31.25 ? 83  PRO   A N   1 
ATOM   667  C CA  . PRO   A 1 86  ? -4.201  -2.213  32.870  1.00 29.11 ? 83  PRO   A CA  1 
ATOM   668  C C   . PRO   A 1 86  ? -2.941  -1.883  32.074  1.00 30.19 ? 83  PRO   A C   1 
ATOM   669  O O   . PRO   A 1 86  ? -2.182  -2.765  31.666  1.00 28.27 ? 83  PRO   A O   1 
ATOM   670  C CB  . PRO   A 1 86  ? -3.874  -2.697  34.289  1.00 32.31 ? 83  PRO   A CB  1 
ATOM   671  C CG  . PRO   A 1 86  ? -5.081  -3.566  34.639  1.00 35.07 ? 83  PRO   A CG  1 
ATOM   672  C CD  . PRO   A 1 86  ? -5.445  -4.266  33.332  1.00 37.94 ? 83  PRO   A CD  1 
ATOM   673  N N   . GLY   A 1 87  ? -2.712  -0.584  31.874  1.00 26.11 ? 84  GLY   A N   1 
ATOM   674  C CA  . GLY   A 1 87  ? -1.616  -0.111  31.062  1.00 30.07 ? 84  GLY   A CA  1 
ATOM   675  C C   . GLY   A 1 87  ? -1.960  0.105   29.601  1.00 24.14 ? 84  GLY   A C   1 
ATOM   676  O O   . GLY   A 1 87  ? -1.249  0.849   28.909  1.00 28.21 ? 84  GLY   A O   1 
ATOM   677  N N   . ASP   A 1 88  ? -3.032  -0.506  29.114  1.00 28.16 ? 85  ASP   A N   1 
ATOM   678  C CA  . ASP   A 1 88  ? -3.441  -0.303  27.727  1.00 26.65 ? 85  ASP   A CA  1 
ATOM   679  C C   . ASP   A 1 88  ? -3.838  1.150   27.488  1.00 25.27 ? 85  ASP   A C   1 
ATOM   680  O O   . ASP   A 1 88  ? -4.328  1.838   28.384  1.00 22.82 ? 85  ASP   A O   1 
ATOM   681  C CB  . ASP   A 1 88  ? -4.607  -1.225  27.371  1.00 23.31 ? 85  ASP   A CB  1 
ATOM   682  C CG  . ASP   A 1 88  ? -4.167  -2.668  27.119  1.00 27.53 ? 85  ASP   A CG  1 
ATOM   683  O OD1 . ASP   A 1 88  ? -2.949  -2.939  27.069  1.00 31.02 ? 85  ASP   A OD1 1 
ATOM   684  O OD2 . ASP   A 1 88  ? -5.049  -3.528  26.965  1.00 33.72 ? 85  ASP   A OD2 1 
ATOM   685  N N   . LEU   A 1 89  ? -3.628  1.609   26.253  1.00 22.77 ? 86  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -4.025  2.931   25.807  1.00 20.06 ? 86  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -5.244  2.819   24.893  1.00 22.90 ? 86  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -5.320  1.919   24.054  1.00 21.21 ? 86  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -2.862  3.614   25.072  1.00 21.88 ? 86  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -1.618  3.771   25.958  1.00 23.58 ? 86  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -0.385  4.054   25.129  1.00 25.35 ? 86  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -1.845  4.883   26.974  1.00 25.39 ? 86  LEU   A CD2 1 
ATOM   693  N N   . VAL   A 1 90  ? -6.200  3.729   25.056  1.00 21.01 ? 87  VAL   A N   1 
ATOM   694  C CA  . VAL   A 1 90  ? -7.372  3.755   24.186  1.00 18.83 ? 87  VAL   A CA  1 
ATOM   695  C C   . VAL   A 1 90  ? -7.662  5.190   23.775  1.00 23.21 ? 87  VAL   A C   1 
ATOM   696  O O   . VAL   A 1 90  ? -7.326  6.141   24.487  1.00 21.33 ? 87  VAL   A O   1 
ATOM   697  C CB  . VAL   A 1 90  ? -8.621  3.163   24.867  1.00 21.29 ? 87  VAL   A CB  1 
ATOM   698  C CG1 . VAL   A 1 90  ? -8.416  1.662   25.146  1.00 22.65 ? 87  VAL   A CG1 1 
ATOM   699  C CG2 . VAL   A 1 90  ? -8.917  3.915   26.170  1.00 21.68 ? 87  VAL   A CG2 1 
ATOM   700  N N   . GLN   A 1 91  ? -8.321  5.333   22.629  1.00 20.85 ? 88  GLN   A N   1 
ATOM   701  C CA  . GLN   A 1 91  ? -8.841  6.610   22.170  1.00 19.01 ? 88  GLN   A CA  1 
ATOM   702  C C   . GLN   A 1 91  ? -10.361 6.519   22.158  1.00 23.80 ? 88  GLN   A C   1 
ATOM   703  O O   . GLN   A 1 91  ? -10.924 5.570   21.608  1.00 21.91 ? 88  GLN   A O   1 
ATOM   704  C CB  . GLN   A 1 91  ? -8.303  6.950   20.779  1.00 22.70 ? 88  GLN   A CB  1 
ATOM   705  C CG  . GLN   A 1 91  ? -8.941  8.198   20.152  1.00 22.63 ? 88  GLN   A CG  1 
ATOM   706  C CD  . GLN   A 1 91  ? -10.173 7.833   19.338  1.00 25.93 ? 88  GLN   A CD  1 
ATOM   707  O OE1 . GLN   A 1 91  ? -10.150 6.887   18.537  1.00 29.34 ? 88  GLN   A OE1 1 
ATOM   708  N NE2 . GLN   A 1 91  ? -11.247 8.561   19.543  1.00 24.49 ? 88  GLN   A NE2 1 
ATOM   709  N N   . GLY   A 1 92  ? -11.017 7.487   22.785  1.00 21.67 ? 89  GLY   A N   1 
ATOM   710  C CA  . GLY   A 1 92  ? -12.467 7.501   22.816  1.00 22.44 ? 89  GLY   A CA  1 
ATOM   711  C C   . GLY   A 1 92  ? -12.932 8.806   23.421  1.00 23.14 ? 89  GLY   A C   1 
ATOM   712  O O   . GLY   A 1 92  ? -12.128 9.643   23.838  1.00 22.55 ? 89  GLY   A O   1 
ATOM   713  N N   . PHE   A 1 93  ? -14.254 8.959   23.497  1.00 23.59 ? 90  PHE   A N   1 
ATOM   714  C CA  . PHE   A 1 93  ? -14.864 10.224  23.912  1.00 23.26 ? 90  PHE   A CA  1 
ATOM   715  C C   . PHE   A 1 93  ? -14.939 10.312  25.444  1.00 25.89 ? 90  PHE   A C   1 
ATOM   716  O O   . PHE   A 1 93  ? -16.009 10.383  26.049  1.00 24.07 ? 90  PHE   A O   1 
ATOM   717  C CB  . PHE   A 1 93  ? -16.241 10.370  23.273  1.00 23.62 ? 90  PHE   A CB  1 
ATOM   718  C CG  . PHE   A 1 93  ? -16.660 11.810  23.026  1.00 25.45 ? 90  PHE   A CG  1 
ATOM   719  C CD1 . PHE   A 1 93  ? -15.963 12.607  22.120  1.00 26.02 ? 90  PHE   A CD1 1 
ATOM   720  C CD2 . PHE   A 1 93  ? -17.761 12.348  23.667  1.00 25.85 ? 90  PHE   A CD2 1 
ATOM   721  C CE1 . PHE   A 1 93  ? -16.355 13.924  21.872  1.00 23.90 ? 90  PHE   A CE1 1 
ATOM   722  C CE2 . PHE   A 1 93  ? -18.167 13.662  23.429  1.00 26.24 ? 90  PHE   A CE2 1 
ATOM   723  C CZ  . PHE   A 1 93  ? -17.461 14.454  22.533  1.00 23.84 ? 90  PHE   A CZ  1 
ATOM   724  N N   . GLY   A 1 94  ? -13.756 10.349  26.068  1.00 21.89 ? 91  GLY   A N   1 
ATOM   725  C CA  . GLY   A 1 94  ? -13.686 10.351  27.519  1.00 25.65 ? 91  GLY   A CA  1 
ATOM   726  C C   . GLY   A 1 94  ? -14.015 11.679  28.164  1.00 27.17 ? 91  GLY   A C   1 
ATOM   727  O O   . GLY   A 1 94  ? -14.469 11.706  29.312  1.00 25.48 ? 91  GLY   A O   1 
ATOM   728  N N   . GLY   A 1 95  ? -13.764 12.794  27.470  1.00 22.46 ? 92  GLY   A N   1 
ATOM   729  C CA  . GLY   A 1 95  ? -14.183 14.093  27.964  1.00 24.20 ? 92  GLY   A CA  1 
ATOM   730  C C   . GLY   A 1 95  ? -13.131 14.814  28.791  1.00 25.02 ? 92  GLY   A C   1 
ATOM   731  O O   . GLY   A 1 95  ? -12.017 14.340  29.027  1.00 23.84 ? 92  GLY   A O   1 
ATOM   732  N N   . TRP   A 1 96  ? -13.507 16.011  29.237  1.00 24.10 ? 93  TRP   A N   1 
ATOM   733  C CA  . TRP   A 1 96  ? -12.603 16.868  30.009  1.00 25.87 ? 93  TRP   A CA  1 
ATOM   734  C C   . TRP   A 1 96  ? -12.638 16.446  31.485  1.00 27.64 ? 93  TRP   A C   1 
ATOM   735  O O   . TRP   A 1 96  ? -13.166 17.138  32.357  1.00 30.87 ? 93  TRP   A O   1 
ATOM   736  C CB  . TRP   A 1 96  ? -12.987 18.337  29.842  1.00 25.72 ? 93  TRP   A CB  1 
ATOM   737  C CG  . TRP   A 1 96  ? -12.767 18.909  28.455  1.00 26.65 ? 93  TRP   A CG  1 
ATOM   738  C CD1 . TRP   A 1 96  ? -12.166 18.297  27.390  1.00 26.95 ? 93  TRP   A CD1 1 
ATOM   739  C CD2 . TRP   A 1 96  ? -13.156 20.212  27.998  1.00 28.95 ? 93  TRP   A CD2 1 
ATOM   740  N NE1 . TRP   A 1 96  ? -12.158 19.146  26.293  1.00 24.42 ? 93  TRP   A NE1 1 
ATOM   741  C CE2 . TRP   A 1 96  ? -12.772 20.318  26.642  1.00 27.21 ? 93  TRP   A CE2 1 
ATOM   742  C CE3 . TRP   A 1 96  ? -13.797 21.298  28.602  1.00 28.88 ? 93  TRP   A CE3 1 
ATOM   743  C CZ2 . TRP   A 1 96  ? -12.991 21.478  25.888  1.00 27.61 ? 93  TRP   A CZ2 1 
ATOM   744  C CZ3 . TRP   A 1 96  ? -14.033 22.441  27.845  1.00 30.18 ? 93  TRP   A CZ3 1 
ATOM   745  C CH2 . TRP   A 1 96  ? -13.621 22.526  26.511  1.00 31.13 ? 93  TRP   A CH2 1 
ATOM   746  N N   . ARG   A 1 97  ? -12.043 15.283  31.753  1.00 24.83 ? 94  ARG   A N   1 
ATOM   747  C CA  . ARG   A 1 97  ? -12.022 14.651  33.069  1.00 26.57 ? 94  ARG   A CA  1 
ATOM   748  C C   . ARG   A 1 97  ? -10.656 14.022  33.286  1.00 30.32 ? 94  ARG   A C   1 
ATOM   749  O O   . ARG   A 1 97  ? -10.094 13.420  32.364  1.00 23.75 ? 94  ARG   A O   1 
ATOM   750  C CB  . ARG   A 1 97  ? -13.098 13.562  33.206  1.00 27.31 ? 94  ARG   A CB  1 
ATOM   751  C CG  . ARG   A 1 97  ? -14.529 14.043  33.026  1.00 26.50 ? 94  ARG   A CG  1 
ATOM   752  C CD  . ARG   A 1 97  ? -15.530 12.904  33.184  1.00 27.55 ? 94  ARG   A CD  1 
ATOM   753  N NE  . ARG   A 1 97  ? -15.561 11.981  32.047  1.00 26.95 ? 94  ARG   A NE  1 
ATOM   754  C CZ  . ARG   A 1 97  ? -16.439 10.993  31.924  1.00 29.98 ? 94  ARG   A CZ  1 
ATOM   755  N NH1 . ARG   A 1 97  ? -17.349 10.754  32.861  1.00 28.08 ? 94  ARG   A NH1 1 
ATOM   756  N NH2 . ARG   A 1 97  ? -16.409 10.227  30.840  1.00 27.57 ? 94  ARG   A NH2 1 
ATOM   757  N N   . THR   A 1 98  ? -10.132 14.135  34.515  1.00 24.24 ? 95  THR   A N   1 
ATOM   758  C CA  . THR   A 1 98  ? -8.828  13.540  34.795  1.00 22.81 ? 95  THR   A CA  1 
ATOM   759  C C   . THR   A 1 98  ? -8.912  12.023  34.827  1.00 23.90 ? 95  THR   A C   1 
ATOM   760  O O   . THR   A 1 98  ? -7.945  11.337  34.470  1.00 25.65 ? 95  THR   A O   1 
ATOM   761  C CB  . THR   A 1 98  ? -8.274  14.063  36.125  1.00 31.24 ? 95  THR   A CB  1 
ATOM   762  O OG1 . THR   A 1 98  ? -9.053  13.526  37.215  1.00 28.63 ? 95  THR   A OG1 1 
ATOM   763  C CG2 . THR   A 1 98  ? -8.320  15.583  36.153  1.00 30.20 ? 95  THR   A CG2 1 
ATOM   764  N N   . HIS   A 1 99  ? -10.057 11.488  35.249  1.00 24.53 ? 96  HIS   A N   1 
ATOM   765  C CA  . HIS   A 1 99  ? -10.262 10.056  35.376  1.00 27.31 ? 96  HIS   A CA  1 
ATOM   766  C C   . HIS   A 1 99  ? -11.738 9.795   35.182  1.00 26.17 ? 96  HIS   A C   1 
ATOM   767  O O   . HIS   A 1 99  ? -12.564 10.691  35.368  1.00 27.08 ? 96  HIS   A O   1 
ATOM   768  C CB  . HIS   A 1 99  ? -9.861  9.507   36.754  1.00 27.84 ? 96  HIS   A CB  1 
ATOM   769  C CG  . HIS   A 1 99  ? -8.464  9.839   37.163  1.00 26.36 ? 96  HIS   A CG  1 
ATOM   770  N ND1 . HIS   A 1 99  ? -8.106  11.076  37.645  1.00 27.79 ? 96  HIS   A ND1 1 
ATOM   771  C CD2 . HIS   A 1 99  ? -7.334  9.095   37.154  1.00 25.30 ? 96  HIS   A CD2 1 
ATOM   772  C CE1 . HIS   A 1 99  ? -6.815  11.076  37.929  1.00 27.67 ? 96  HIS   A CE1 1 
ATOM   773  N NE2 . HIS   A 1 99  ? -6.322  9.889   37.632  1.00 26.19 ? 96  HIS   A NE2 1 
ATOM   774  N N   . LEU   A 1 100 ? -12.059 8.543   34.867  1.00 24.10 ? 97  LEU   A N   1 
ATOM   775  C CA  . LEU   A 1 100 ? -13.433 8.156   34.585  1.00 25.88 ? 97  LEU   A CA  1 
ATOM   776  C C   . LEU   A 1 100 ? -13.493 6.637   34.592  1.00 23.96 ? 97  LEU   A C   1 
ATOM   777  O O   . LEU   A 1 100 ? -12.460 5.961   34.551  1.00 24.07 ? 97  LEU   A O   1 
ATOM   778  C CB  . LEU   A 1 100 ? -13.909 8.722   33.224  1.00 25.17 ? 97  LEU   A CB  1 
ATOM   779  C CG  . LEU   A 1 100 ? -13.076 8.248   32.022  1.00 23.97 ? 97  LEU   A CG  1 
ATOM   780  C CD1 . LEU   A 1 100 ? -13.926 7.497   31.006  1.00 26.32 ? 97  LEU   A CD1 1 
ATOM   781  C CD2 . LEU   A 1 100 ? -12.362 9.435   31.354  1.00 21.98 ? 97  LEU   A CD2 1 
ATOM   782  N N   . VAL   A 1 101 ? -14.714 6.116   34.685  1.00 24.03 ? 98  VAL   A N   1 
ATOM   783  C CA  . VAL   A 1 101 ? -14.983 4.688   34.631  1.00 25.95 ? 98  VAL   A CA  1 
ATOM   784  C C   . VAL   A 1 101 ? -15.900 4.454   33.444  1.00 25.63 ? 98  VAL   A C   1 
ATOM   785  O O   . VAL   A 1 101 ? -16.893 5.170   33.277  1.00 26.14 ? 98  VAL   A O   1 
ATOM   786  C CB  . VAL   A 1 101 ? -15.629 4.184   35.937  1.00 27.43 ? 98  VAL   A CB  1 
ATOM   787  C CG1 . VAL   A 1 101 ? -16.139 2.753   35.774  1.00 28.32 ? 98  VAL   A CG1 1 
ATOM   788  C CG2 . VAL   A 1 101 ? -14.627 4.288   37.085  1.00 25.96 ? 98  VAL   A CG2 1 
ATOM   789  N N   . SER   A 1 102 ? -15.565 3.467   32.620  1.00 27.63 ? 99  SER   A N   1 
ATOM   790  C CA  . SER   A 1 102 ? -16.379 3.166   31.452  1.00 28.51 ? 99  SER   A CA  1 
ATOM   791  C C   . SER   A 1 102 ? -16.097 1.741   31.017  1.00 28.67 ? 99  SER   A C   1 
ATOM   792  O O   . SER   A 1 102 ? -15.003 1.212   31.247  1.00 25.65 ? 99  SER   A O   1 
ATOM   793  C CB  . SER   A 1 102 ? -16.088 4.144   30.291  1.00 32.78 ? 99  SER   A CB  1 
ATOM   794  O OG  . SER   A 1 102 ? -16.689 3.697   29.087  1.00 29.44 ? 99  SER   A OG  1 
ATOM   795  N N   . ASP   A 1 103 ? -17.081 1.123   30.373  1.00 26.31 ? 100 ASP   A N   1 
ATOM   796  C CA  . ASP   A 1 103 ? -16.824 -0.174  29.775  1.00 26.96 ? 100 ASP   A CA  1 
ATOM   797  C C   . ASP   A 1 103 ? -16.342 -0.061  28.331  1.00 29.42 ? 100 ASP   A C   1 
ATOM   798  O O   . ASP   A 1 103 ? -16.030 -1.087  27.718  1.00 28.30 ? 100 ASP   A O   1 
ATOM   799  C CB  . ASP   A 1 103 ? -18.063 -1.072  29.853  1.00 33.93 ? 100 ASP   A CB  1 
ATOM   800  C CG  . ASP   A 1 103 ? -19.270 -0.483  29.136  1.00 38.97 ? 100 ASP   A CG  1 
ATOM   801  O OD1 . ASP   A 1 103 ? -19.169 0.646   28.597  1.00 36.37 ? 100 ASP   A OD1 1 
ATOM   802  O OD2 . ASP   A 1 103 ? -20.321 -1.160  29.112  1.00 40.27 ? 100 ASP   A OD2 1 
ATOM   803  N N   . GLY   A 1 104 ? -16.238 1.156   27.792  1.00 30.75 ? 101 GLY   A N   1 
ATOM   804  C CA  . GLY   A 1 104 ? -15.694 1.342   26.455  1.00 30.43 ? 101 GLY   A CA  1 
ATOM   805  C C   . GLY   A 1 104 ? -16.604 0.925   25.323  1.00 29.51 ? 101 GLY   A C   1 
ATOM   806  O O   . GLY   A 1 104 ? -16.154 0.864   24.174  1.00 26.07 ? 101 GLY   A O   1 
ATOM   807  N N   . LYS   A 1 105 ? -17.867 0.628   25.613  1.00 25.57 ? 102 LYS   A N   1 
ATOM   808  C CA  . LYS   A 1 105 ? -18.819 0.241   24.592  1.00 31.11 ? 102 LYS   A CA  1 
ATOM   809  C C   . LYS   A 1 105 ? -19.376 1.470   23.874  1.00 26.80 ? 102 LYS   A C   1 
ATOM   810  O O   . LYS   A 1 105 ? -19.276 2.596   24.373  1.00 22.79 ? 102 LYS   A O   1 
ATOM   811  C CB  . LYS   A 1 105 ? -19.962 -0.568  25.214  1.00 32.27 ? 102 LYS   A CB  1 
ATOM   812  C CG  . LYS   A 1 105 ? -19.584 -1.995  25.644  1.00 32.61 ? 102 LYS   A CG  1 
ATOM   813  C CD  . LYS   A 1 105 ? -20.716 -2.612  26.464  1.00 39.04 ? 102 LYS   A CD  1 
ATOM   814  C CE  . LYS   A 1 105 ? -20.626 -4.124  26.521  1.00 40.04 ? 102 LYS   A CE  1 
ATOM   815  N NZ  . LYS   A 1 105 ? -19.304 -4.618  26.968  1.00 42.35 ? 102 LYS   A NZ  1 
ATOM   816  N N   . PRO   A 1 106 ? -19.944 1.282   22.680  1.00 28.67 ? 103 PRO   A N   1 
ATOM   817  C CA  . PRO   A 1 106 ? -20.590 2.406   21.992  1.00 29.00 ? 103 PRO   A CA  1 
ATOM   818  C C   . PRO   A 1 106 ? -21.710 2.964   22.849  1.00 30.25 ? 103 PRO   A C   1 
ATOM   819  O O   . PRO   A 1 106 ? -22.430 2.220   23.515  1.00 26.26 ? 103 PRO   A O   1 
ATOM   820  C CB  . PRO   A 1 106 ? -21.129 1.777   20.703  1.00 29.06 ? 103 PRO   A CB  1 
ATOM   821  C CG  . PRO   A 1 106 ? -20.255 0.571   20.473  1.00 30.02 ? 103 PRO   A CG  1 
ATOM   822  C CD  . PRO   A 1 106 ? -19.927 0.058   21.863  1.00 27.13 ? 103 PRO   A CD  1 
ATOM   823  N N   . LYS   A 1 107 ? -21.871 4.285   22.820  1.00 30.15 ? 104 LYS   A N   1 
ATOM   824  C CA  . LYS   A 1 107 ? -22.793 4.951   23.737  1.00 28.51 ? 104 LYS   A CA  1 
ATOM   825  C C   . LYS   A 1 107 ? -23.597 5.996   22.979  1.00 33.11 ? 104 LYS   A C   1 
ATOM   826  O O   . LYS   A 1 107 ? -23.019 6.884   22.343  1.00 28.34 ? 104 LYS   A O   1 
ATOM   827  C CB  . LYS   A 1 107 ? -22.029 5.581   24.900  1.00 36.00 ? 104 LYS   A CB  1 
ATOM   828  C CG  . LYS   A 1 107 ? -22.901 6.193   25.978  1.00 43.79 ? 104 LYS   A CG  1 
ATOM   829  C CD  . LYS   A 1 107 ? -22.241 6.050   27.348  1.00 46.32 ? 104 LYS   A CD  1 
ATOM   830  C CE  . LYS   A 1 107 ? -22.817 7.050   28.352  1.00 48.75 ? 104 LYS   A CE  1 
ATOM   831  N NZ  . LYS   A 1 107 ? -24.306 6.930   28.477  1.00 49.39 ? 104 LYS   A NZ  1 
ATOM   832  N N   . LEU   A 1 108 ? -24.927 5.889   23.048  1.00 31.44 ? 105 LEU   A N   1 
ATOM   833  C CA  . LEU   A 1 108 ? -25.786 6.885   22.421  1.00 33.05 ? 105 LEU   A CA  1 
ATOM   834  C C   . LEU   A 1 108 ? -25.592 8.239   23.086  1.00 35.40 ? 105 LEU   A C   1 
ATOM   835  O O   . LEU   A 1 108 ? -25.439 8.334   24.307  1.00 34.38 ? 105 LEU   A O   1 
ATOM   836  C CB  . LEU   A 1 108 ? -27.259 6.460   22.512  1.00 38.25 ? 105 LEU   A CB  1 
ATOM   837  C CG  . LEU   A 1 108 ? -28.291 7.449   21.955  1.00 34.65 ? 105 LEU   A CG  1 
ATOM   838  C CD1 . LEU   A 1 108 ? -28.328 7.375   20.439  1.00 36.46 ? 105 LEU   A CD1 1 
ATOM   839  C CD2 . LEU   A 1 108 ? -29.681 7.193   22.531  1.00 38.41 ? 105 LEU   A CD2 1 
ATOM   840  N N   . TRP   A 1 109 ? -25.584 9.292   22.270  1.00 28.48 ? 106 TRP   A N   1 
ATOM   841  C CA  . TRP   A 1 109 ? -25.592 10.669  22.763  1.00 33.00 ? 106 TRP   A CA  1 
ATOM   842  C C   . TRP   A 1 109 ? -27.055 11.016  22.993  1.00 39.01 ? 106 TRP   A C   1 
ATOM   843  O O   . TRP   A 1 109 ? -27.769 11.387  22.053  1.00 35.45 ? 106 TRP   A O   1 
ATOM   844  C CB  . TRP   A 1 109 ? -24.908 11.611  21.769  1.00 31.04 ? 106 TRP   A CB  1 
ATOM   845  C CG  . TRP   A 1 109 ? -24.776 13.071  22.176  1.00 30.85 ? 106 TRP   A CG  1 
ATOM   846  C CD1 . TRP   A 1 109 ? -24.903 14.162  21.349  1.00 32.66 ? 106 TRP   A CD1 1 
ATOM   847  C CD2 . TRP   A 1 109 ? -24.462 13.598  23.481  1.00 31.17 ? 106 TRP   A CD2 1 
ATOM   848  N NE1 . TRP   A 1 109 ? -24.698 15.321  22.055  1.00 34.69 ? 106 TRP   A NE1 1 
ATOM   849  C CE2 . TRP   A 1 109 ? -24.432 15.007  23.367  1.00 31.00 ? 106 TRP   A CE2 1 
ATOM   850  C CE3 . TRP   A 1 109 ? -24.216 13.018  24.733  1.00 34.14 ? 106 TRP   A CE3 1 
ATOM   851  C CZ2 . TRP   A 1 109 ? -24.153 15.846  24.455  1.00 31.22 ? 106 TRP   A CZ2 1 
ATOM   852  C CZ3 . TRP   A 1 109 ? -23.944 13.862  25.825  1.00 32.21 ? 106 TRP   A CZ3 1 
ATOM   853  C CH2 . TRP   A 1 109 ? -23.924 15.253  25.679  1.00 31.52 ? 106 TRP   A CH2 1 
ATOM   854  N N   . GLN   A 1 110 ? -27.501 10.864  24.246  1.00 39.20 ? 107 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? -28.926 10.904  24.552  1.00 39.56 ? 107 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? -29.533 12.257  24.222  1.00 37.29 ? 107 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? -30.624 12.333  23.647  1.00 43.01 ? 107 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? -29.153 10.574  26.031  1.00 36.31 ? 107 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? -28.991 9.111   26.390  1.00 43.65 ? 107 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? -30.105 8.253   25.808  1.00 55.44 ? 107 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? -29.938 7.048   25.601  1.00 56.51 ? 107 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? -31.252 8.878   25.540  1.00 57.75 ? 107 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? -28.850 13.334  24.589  1.00 35.57 ? 108 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? -29.367 14.681  24.434  1.00 34.96 ? 108 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? -28.965 15.320  23.104  1.00 33.66 ? 108 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? -29.103 16.534  22.949  1.00 34.21 ? 108 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? -28.880 15.550  25.598  1.00 38.63 ? 108 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? -27.460 15.399  25.743  1.00 36.89 ? 108 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? -29.567 15.137  26.906  1.00 36.03 ? 108 THR   A CG2 1 
ATOM   870  N N   . GLY   A 1 112 ? -28.482 14.536  22.144  1.00 35.12 ? 109 GLY   A N   1 
ATOM   871  C CA  . GLY   A 1 112 ? -27.920 15.118  20.930  1.00 35.64 ? 109 GLY   A CA  1 
ATOM   872  C C   . GLY   A 1 112 ? -28.991 15.618  19.972  1.00 37.01 ? 109 GLY   A C   1 
ATOM   873  O O   . GLY   A 1 112 ? -30.056 15.023  19.828  1.00 36.03 ? 109 GLY   A O   1 
ATOM   874  N N   . THR   A 1 113 ? -28.689 16.741  19.315  1.00 36.68 ? 110 THR   A N   1 
ATOM   875  C CA  . THR   A 1 113 ? -29.518 17.198  18.201  1.00 38.53 ? 110 THR   A CA  1 
ATOM   876  C C   . THR   A 1 113 ? -29.781 16.061  17.217  1.00 40.26 ? 110 THR   A C   1 
ATOM   877  O O   . THR   A 1 113 ? -30.903 15.899  16.723  1.00 39.27 ? 110 THR   A O   1 
ATOM   878  C CB  . THR   A 1 113 ? -28.833 18.376  17.502  1.00 43.28 ? 110 THR   A CB  1 
ATOM   879  O OG1 . THR   A 1 113 ? -28.722 19.471  18.421  1.00 42.76 ? 110 THR   A OG1 1 
ATOM   880  C CG2 . THR   A 1 113 ? -29.610 18.816  16.252  1.00 40.26 ? 110 THR   A CG2 1 
ATOM   881  N N   . PHE   A 1 114 ? -28.744 15.252  16.923  1.00 39.17 ? 111 PHE   A N   1 
ATOM   882  C CA  . PHE   A 1 114 ? -28.802 14.044  16.116  1.00 36.72 ? 111 PHE   A CA  1 
ATOM   883  C C   . PHE   A 1 114 ? -28.516 12.825  16.985  1.00 36.94 ? 111 PHE   A C   1 
ATOM   884  O O   . PHE   A 1 114 ? -27.664 12.898  17.878  1.00 35.31 ? 111 PHE   A O   1 
ATOM   885  C CB  . PHE   A 1 114 ? -27.779 14.077  14.980  1.00 37.03 ? 111 PHE   A CB  1 
ATOM   886  C CG  . PHE   A 1 114 ? -27.852 15.300  14.144  1.00 39.42 ? 111 PHE   A CG  1 
ATOM   887  C CD1 . PHE   A 1 114 ? -28.895 15.472  13.237  1.00 48.66 ? 111 PHE   A CD1 1 
ATOM   888  C CD2 . PHE   A 1 114 ? -26.880 16.281  14.242  1.00 42.23 ? 111 PHE   A CD2 1 
ATOM   889  C CE1 . PHE   A 1 114 ? -28.974 16.615  12.438  1.00 49.25 ? 111 PHE   A CE1 1 
ATOM   890  C CE2 . PHE   A 1 114 ? -26.948 17.430  13.455  1.00 49.86 ? 111 PHE   A CE2 1 
ATOM   891  C CZ  . PHE   A 1 114 ? -28.003 17.596  12.551  1.00 51.89 ? 111 PHE   A CZ  1 
ATOM   892  N N   . PRO   A 1 115 ? -29.173 11.681  16.717  1.00 35.70 ? 112 PRO   A N   1 
ATOM   893  C CA  . PRO   A 1 115 ? -28.925 10.477  17.519  1.00 35.81 ? 112 PRO   A CA  1 
ATOM   894  C C   . PRO   A 1 115 ? -27.568 9.853   17.249  1.00 34.04 ? 112 PRO   A C   1 
ATOM   895  O O   . PRO   A 1 115 ? -27.472 8.673   16.901  1.00 33.96 ? 112 PRO   A O   1 
ATOM   896  C CB  . PRO   A 1 115 ? -30.060 9.538   17.089  1.00 35.68 ? 112 PRO   A CB  1 
ATOM   897  C CG  . PRO   A 1 115 ? -30.356 9.948   15.684  1.00 36.87 ? 112 PRO   A CG  1 
ATOM   898  C CD  . PRO   A 1 115 ? -30.189 11.449  15.675  1.00 36.38 ? 112 PRO   A CD  1 
ATOM   899  N N   . MET   A 1 116 ? -26.515 10.636  17.426  1.00 31.56 ? 113 MET   A N   1 
ATOM   900  C CA  . MET   A 1 116 ? -25.157 10.153  17.258  1.00 32.37 ? 113 MET   A CA  1 
ATOM   901  C C   . MET   A 1 116 ? -24.820 9.106   18.322  1.00 30.66 ? 113 MET   A C   1 
ATOM   902  O O   . MET   A 1 116 ? -25.273 9.181   19.466  1.00 30.77 ? 113 MET   A O   1 
ATOM   903  C CB  . MET   A 1 116 ? -24.195 11.339  17.344  1.00 36.33 ? 113 MET   A CB  1 
ATOM   904  C CG  . MET   A 1 116 ? -22.760 10.987  17.563  1.00 37.50 ? 113 MET   A CG  1 
ATOM   905  S SD  . MET   A 1 116 ? -21.712 12.459  17.576  1.00 39.10 ? 113 MET   A SD  1 
ATOM   906  C CE  . MET   A 1 116 ? -22.627 13.602  18.579  1.00 36.25 ? 113 MET   A CE  1 
ATOM   907  N N   . VAL   A 1 117 ? -24.011 8.122   17.930  1.00 28.24 ? 114 VAL   A N   1 
ATOM   908  C CA  . VAL   A 1 117 ? -23.503 7.084   18.834  1.00 32.33 ? 114 VAL   A CA  1 
ATOM   909  C C   . VAL   A 1 117 ? -21.982 7.192   18.881  1.00 33.37 ? 114 VAL   A C   1 
ATOM   910  O O   . VAL   A 1 117 ? -21.300 6.857   17.899  1.00 30.48 ? 114 VAL   A O   1 
ATOM   911  C CB  . VAL   A 1 117 ? -23.915 5.672   18.396  1.00 34.37 ? 114 VAL   A CB  1 
ATOM   912  C CG1 . VAL   A 1 117 ? -23.300 4.626   19.340  1.00 33.92 ? 114 VAL   A CG1 1 
ATOM   913  C CG2 . VAL   A 1 117 ? -25.431 5.547   18.330  1.00 35.14 ? 114 VAL   A CG2 1 
ATOM   914  N N   . PHE   A 1 118 ? -21.447 7.632   20.019  1.00 30.07 ? 115 PHE   A N   1 
ATOM   915  C CA  . PHE   A 1 118 ? -20.004 7.631   20.186  1.00 27.45 ? 115 PHE   A CA  1 
ATOM   916  C C   . PHE   A 1 118 ? -19.456 6.212   20.032  1.00 29.90 ? 115 PHE   A C   1 
ATOM   917  O O   . PHE   A 1 118 ? -20.033 5.256   20.565  1.00 31.17 ? 115 PHE   A O   1 
ATOM   918  C CB  . PHE   A 1 118 ? -19.623 8.211   21.542  1.00 26.67 ? 115 PHE   A CB  1 
ATOM   919  C CG  . PHE   A 1 118 ? -20.109 9.613   21.745  1.00 29.95 ? 115 PHE   A CG  1 
ATOM   920  C CD1 . PHE   A 1 118 ? -19.683 10.638  20.901  1.00 24.83 ? 115 PHE   A CD1 1 
ATOM   921  C CD2 . PHE   A 1 118 ? -20.991 9.914   22.776  1.00 27.54 ? 115 PHE   A CD2 1 
ATOM   922  C CE1 . PHE   A 1 118 ? -20.128 11.934  21.088  1.00 27.54 ? 115 PHE   A CE1 1 
ATOM   923  C CE2 . PHE   A 1 118 ? -21.447 11.214  22.959  1.00 28.09 ? 115 PHE   A CE2 1 
ATOM   924  C CZ  . PHE   A 1 118 ? -21.009 12.223  22.116  1.00 28.47 ? 115 PHE   A CZ  1 
ATOM   925  N N   . PRO   A 1 119 ? -18.364 6.032   19.293  1.00 29.77 ? 116 PRO   A N   1 
ATOM   926  C CA  . PRO   A 1 119 ? -17.876 4.676   19.021  1.00 29.81 ? 116 PRO   A CA  1 
ATOM   927  C C   . PRO   A 1 119 ? -17.253 4.025   20.249  1.00 30.16 ? 116 PRO   A C   1 
ATOM   928  O O   . PRO   A 1 119 ? -16.906 4.679   21.245  1.00 23.32 ? 116 PRO   A O   1 
ATOM   929  C CB  . PRO   A 1 119 ? -16.829 4.889   17.916  1.00 27.58 ? 116 PRO   A CB  1 
ATOM   930  C CG  . PRO   A 1 119 ? -16.329 6.294   18.169  1.00 31.31 ? 116 PRO   A CG  1 
ATOM   931  C CD  . PRO   A 1 119 ? -17.514 7.073   18.681  1.00 27.90 ? 116 PRO   A CD  1 
ATOM   932  N N   . ALA   A 1 120 ? -17.137 2.699   20.162  1.00 30.17 ? 117 ALA   A N   1 
ATOM   933  C CA  . ALA   A 1 120 ? -16.332 1.937   21.108  1.00 27.71 ? 117 ALA   A CA  1 
ATOM   934  C C   . ALA   A 1 120 ? -14.934 2.524   21.206  1.00 26.73 ? 117 ALA   A C   1 
ATOM   935  O O   . ALA   A 1 120 ? -14.351 2.927   20.195  1.00 25.81 ? 117 ALA   A O   1 
ATOM   936  C CB  . ALA   A 1 120 ? -16.236 0.478   20.661  1.00 26.73 ? 117 ALA   A CB  1 
ATOM   937  N N   . TYR   A 1 121 ? -14.394 2.548   22.425  1.00 26.33 ? 118 TYR   A N   1 
ATOM   938  C CA  . TYR   A 1 121 ? -13.002 2.925   22.628  1.00 25.06 ? 118 TYR   A CA  1 
ATOM   939  C C   . TYR   A 1 121 ? -12.109 2.100   21.718  1.00 27.16 ? 118 TYR   A C   1 
ATOM   940  O O   . TYR   A 1 121 ? -12.343 0.907   21.515  1.00 26.08 ? 118 TYR   A O   1 
ATOM   941  C CB  . TYR   A 1 121 ? -12.570 2.705   24.087  1.00 26.71 ? 118 TYR   A CB  1 
ATOM   942  C CG  . TYR   A 1 121 ? -13.186 3.646   25.087  1.00 25.77 ? 118 TYR   A CG  1 
ATOM   943  C CD1 . TYR   A 1 121 ? -14.224 4.494   24.728  1.00 24.04 ? 118 TYR   A CD1 1 
ATOM   944  C CD2 . TYR   A 1 121 ? -12.738 3.675   26.409  1.00 28.27 ? 118 TYR   A CD2 1 
ATOM   945  C CE1 . TYR   A 1 121 ? -14.777 5.359   25.632  1.00 26.75 ? 118 TYR   A CE1 1 
ATOM   946  C CE2 . TYR   A 1 121 ? -13.298 4.534   27.329  1.00 27.60 ? 118 TYR   A CE2 1 
ATOM   947  C CZ  . TYR   A 1 121 ? -14.314 5.367   26.940  1.00 29.29 ? 118 TYR   A CZ  1 
ATOM   948  O OH  . TYR   A 1 121 ? -14.874 6.223   27.849  1.00 32.71 ? 118 TYR   A OH  1 
ATOM   949  N N   . ARG   A 1 122 ? -11.070 2.741   21.190  1.00 22.26 ? 119 ARG   A N   1 
ATOM   950  C CA  . ARG   A 1 122 ? -10.165 2.140   20.219  1.00 26.57 ? 119 ARG   A CA  1 
ATOM   951  C C   . ARG   A 1 122 ? -8.812  1.894   20.875  1.00 23.81 ? 119 ARG   A C   1 
ATOM   952  O O   . ARG   A 1 122 ? -8.198  2.828   21.406  1.00 23.05 ? 119 ARG   A O   1 
ATOM   953  C CB  . ARG   A 1 122 ? -10.003 3.059   18.996  1.00 22.94 ? 119 ARG   A CB  1 
ATOM   954  C CG  . ARG   A 1 122 ? -9.015  2.573   17.981  1.00 26.07 ? 119 ARG   A CG  1 
ATOM   955  C CD  . ARG   A 1 122 ? -9.022  3.450   16.696  1.00 25.30 ? 119 ARG   A CD  1 
ATOM   956  N NE  . ARG   A 1 122 ? -8.632  4.840   16.948  1.00 25.25 ? 119 ARG   A NE  1 
ATOM   957  C CZ  . ARG   A 1 122 ? -7.456  5.367   16.624  1.00 22.80 ? 119 ARG   A CZ  1 
ATOM   958  N NH1 . ARG   A 1 122 ? -6.497  4.640   16.060  1.00 23.32 ? 119 ARG   A NH1 1 
ATOM   959  N NH2 . ARG   A 1 122 ? -7.249  6.665   16.835  1.00 23.44 ? 119 ARG   A NH2 1 
ATOM   960  N N   . LYS   A 1 123 ? -8.332  0.653   20.810  1.00 23.11 ? 120 LYS   A N   1 
ATOM   961  C CA  . LYS   A 1 123 ? -7.044  0.340   21.412  1.00 24.86 ? 120 LYS   A CA  1 
ATOM   962  C C   . LYS   A 1 123 ? -5.937  0.941   20.563  1.00 26.36 ? 120 LYS   A C   1 
ATOM   963  O O   . LYS   A 1 123 ? -5.967  0.851   19.337  1.00 24.66 ? 120 LYS   A O   1 
ATOM   964  C CB  . LYS   A 1 123 ? -6.845  -1.172  21.544  1.00 28.03 ? 120 LYS   A CB  1 
ATOM   965  C CG  . LYS   A 1 123 ? -5.678  -1.552  22.505  1.00 29.51 ? 120 LYS   A CG  1 
ATOM   966  C CD  . LYS   A 1 123 ? -5.369  -3.055  22.466  1.00 40.21 ? 120 LYS   A CD  1 
ATOM   967  C CE  . LYS   A 1 123 ? -4.292  -3.450  23.489  1.00 38.03 ? 120 LYS   A CE  1 
ATOM   968  N NZ  . LYS   A 1 123 ? -3.007  -2.734  23.251  1.00 34.76 ? 120 LYS   A NZ  1 
ATOM   969  N N   . LEU   A 1 124 ? -4.988  1.594   21.208  1.00 23.20 ? 121 LEU   A N   1 
ATOM   970  C CA  . LEU   A 1 124 ? -3.850  2.169   20.505  1.00 22.66 ? 121 LEU   A CA  1 
ATOM   971  C C   . LEU   A 1 124 ? -2.664  1.232   20.668  1.00 26.61 ? 121 LEU   A C   1 
ATOM   972  O O   . LEU   A 1 124 ? -2.469  0.640   21.733  1.00 26.79 ? 121 LEU   A O   1 
ATOM   973  C CB  . LEU   A 1 124 ? -3.522  3.561   21.047  1.00 20.13 ? 121 LEU   A CB  1 
ATOM   974  C CG  . LEU   A 1 124 ? -4.711  4.532   21.025  1.00 25.05 ? 121 LEU   A CG  1 
ATOM   975  C CD1 . LEU   A 1 124 ? -4.366  5.867   21.693  1.00 22.25 ? 121 LEU   A CD1 1 
ATOM   976  C CD2 . LEU   A 1 124 ? -5.231  4.771   19.594  1.00 21.87 ? 121 LEU   A CD2 1 
ATOM   977  N N   . ASP   A 1 125 ? -1.904  1.071   19.596  1.00 21.87 ? 122 ASP   A N   1 
ATOM   978  C CA  . ASP   A 1 125 ? -0.728  0.216   19.573  1.00 27.11 ? 122 ASP   A CA  1 
ATOM   979  C C   . ASP   A 1 125 ? 0.501   1.101   19.428  1.00 26.49 ? 122 ASP   A C   1 
ATOM   980  O O   . ASP   A 1 125 ? 0.641   1.825   18.434  1.00 29.43 ? 122 ASP   A O   1 
ATOM   981  C CB  . ASP   A 1 125 ? -0.799  -0.801  18.436  1.00 32.77 ? 122 ASP   A CB  1 
ATOM   982  C CG  . ASP   A 1 125 ? 0.300   -1.837  18.521  1.00 40.67 ? 122 ASP   A CG  1 
ATOM   983  O OD1 . ASP   A 1 125 ? 1.487   -1.446  18.576  1.00 47.09 ? 122 ASP   A OD1 1 
ATOM   984  O OD2 . ASP   A 1 125 ? -0.007  -3.044  18.563  1.00 52.02 ? 122 ASP   A OD2 1 
ATOM   985  N N   . LEU   A 1 126 ? 1.390   1.046   20.423  1.00 26.60 ? 123 LEU   A N   1 
ATOM   986  C CA  . LEU   A 1 126 ? 2.524   1.966   20.430  1.00 26.65 ? 123 LEU   A CA  1 
ATOM   987  C C   . LEU   A 1 126 ? 3.430   1.773   19.225  1.00 24.14 ? 123 LEU   A C   1 
ATOM   988  O O   . LEU   A 1 126 ? 4.143   2.705   18.837  1.00 24.52 ? 123 LEU   A O   1 
ATOM   989  C CB  . LEU   A 1 126 ? 3.309   1.801   21.740  1.00 22.90 ? 123 LEU   A CB  1 
ATOM   990  C CG  . LEU   A 1 126 ? 2.564   2.357   22.966  1.00 23.37 ? 123 LEU   A CG  1 
ATOM   991  C CD1 . LEU   A 1 126 ? 3.291   2.044   24.275  1.00 24.02 ? 123 LEU   A CD1 1 
ATOM   992  C CD2 . LEU   A 1 126 ? 2.338   3.876   22.823  1.00 21.09 ? 123 LEU   A CD2 1 
ATOM   993  N N   . ARG   A 1 127 ? 3.416   0.593   18.604  1.00 23.90 ? 124 ARG   A N   1 
ATOM   994  C CA  . ARG   A 1 127 ? 4.260   0.412   17.428  1.00 27.91 ? 124 ARG   A CA  1 
ATOM   995  C C   . ARG   A 1 127 ? 3.930   1.407   16.318  1.00 30.43 ? 124 ARG   A C   1 
ATOM   996  O O   . ARG   A 1 127 ? 4.788   1.660   15.470  1.00 30.13 ? 124 ARG   A O   1 
ATOM   997  C CB  . ARG   A 1 127 ? 4.146   -1.020  16.904  1.00 34.45 ? 124 ARG   A CB  1 
ATOM   998  C CG  . ARG   A 1 127 ? 3.018   -1.211  15.918  1.00 40.64 ? 124 ARG   A CG  1 
ATOM   999  C CD  . ARG   A 1 127 ? 2.344   -2.555  16.072  1.00 42.41 ? 124 ARG   A CD  1 
ATOM   1000 N NE  . ARG   A 1 127 ? 1.599   -2.903  14.865  1.00 47.79 ? 124 ARG   A NE  1 
ATOM   1001 C CZ  . ARG   A 1 127 ? 0.615   -3.791  14.821  1.00 58.46 ? 124 ARG   A CZ  1 
ATOM   1002 N NH1 . ARG   A 1 127 ? 0.197   -4.414  15.912  1.00 57.59 ? 124 ARG   A NH1 1 
ATOM   1003 N NH2 . ARG   A 1 127 ? 0.028   -4.054  13.653  1.00 58.06 ? 124 ARG   A NH2 1 
ATOM   1004 N N   . HIS   A 1 128 ? 2.732   2.012   16.322  1.00 27.55 ? 125 HIS   A N   1 
ATOM   1005 C CA  . HIS   A 1 128 ? 2.355   2.964   15.275  1.00 29.96 ? 125 HIS   A CA  1 
ATOM   1006 C C   . HIS   A 1 128 ? 2.926   4.356   15.485  1.00 30.95 ? 125 HIS   A C   1 
ATOM   1007 O O   . HIS   A 1 128 ? 2.860   5.175   14.566  1.00 29.68 ? 125 HIS   A O   1 
ATOM   1008 C CB  . HIS   A 1 128 ? 0.828   3.114   15.177  1.00 28.13 ? 125 HIS   A CB  1 
ATOM   1009 C CG  . HIS   A 1 128 ? 0.121   1.898   14.669  1.00 34.09 ? 125 HIS   A CG  1 
ATOM   1010 N ND1 . HIS   A 1 128 ? -1.068  1.456   15.207  1.00 36.58 ? 125 HIS   A ND1 1 
ATOM   1011 C CD2 . HIS   A 1 128 ? 0.409   1.053   13.650  1.00 34.77 ? 125 HIS   A CD2 1 
ATOM   1012 C CE1 . HIS   A 1 128 ? -1.468  0.374   14.562  1.00 37.74 ? 125 HIS   A CE1 1 
ATOM   1013 N NE2 . HIS   A 1 128 ? -0.589  0.106   13.614  1.00 40.75 ? 125 HIS   A NE2 1 
ATOM   1014 N N   . TYR   A 1 129 ? 3.427   4.672   16.670  1.00 26.16 ? 126 TYR   A N   1 
ATOM   1015 C CA  . TYR   A 1 129 ? 3.810   6.032   16.992  1.00 26.14 ? 126 TYR   A CA  1 
ATOM   1016 C C   . TYR   A 1 129 ? 5.301   6.089   17.252  1.00 31.32 ? 126 TYR   A C   1 
ATOM   1017 O O   . TYR   A 1 129 ? 5.912   5.122   17.721  1.00 31.11 ? 126 TYR   A O   1 
ATOM   1018 C CB  . TYR   A 1 129 ? 3.019   6.569   18.206  1.00 25.53 ? 126 TYR   A CB  1 
ATOM   1019 C CG  . TYR   A 1 129 ? 1.545   6.291   18.035  1.00 28.90 ? 126 TYR   A CG  1 
ATOM   1020 C CD1 . TYR   A 1 129 ? 0.766   7.074   17.178  1.00 24.27 ? 126 TYR   A CD1 1 
ATOM   1021 C CD2 . TYR   A 1 129 ? 0.939   5.214   18.680  1.00 25.91 ? 126 TYR   A CD2 1 
ATOM   1022 C CE1 . TYR   A 1 129 ? -0.576  6.806   16.992  1.00 26.46 ? 126 TYR   A CE1 1 
ATOM   1023 C CE2 . TYR   A 1 129 ? -0.402  4.942   18.506  1.00 28.50 ? 126 TYR   A CE2 1 
ATOM   1024 C CZ  . TYR   A 1 129 ? -1.157  5.736   17.661  1.00 28.17 ? 126 TYR   A CZ  1 
ATOM   1025 O OH  . TYR   A 1 129 ? -2.491  5.443   17.482  1.00 23.99 ? 126 TYR   A OH  1 
ATOM   1026 N N   . ASP   A 1 130 ? 5.877   7.225   16.906  1.00 27.09 ? 127 ASP   A N   1 
ATOM   1027 C CA  . ASP   A 1 130 ? 7.293   7.471   17.076  1.00 31.06 ? 127 ASP   A CA  1 
ATOM   1028 C C   . ASP   A 1 130 ? 7.462   8.978   17.103  1.00 27.84 ? 127 ASP   A C   1 
ATOM   1029 O O   . ASP   A 1 130 ? 6.481   9.726   17.075  1.00 27.77 ? 127 ASP   A O   1 
ATOM   1030 C CB  . ASP   A 1 130 ? 8.116   6.803   15.969  1.00 31.69 ? 127 ASP   A CB  1 
ATOM   1031 C CG  . ASP   A 1 130 ? 7.679   7.225   14.580  1.00 36.79 ? 127 ASP   A CG  1 
ATOM   1032 O OD1 . ASP   A 1 130 ? 7.729   8.440   14.275  1.00 37.61 ? 127 ASP   A OD1 1 
ATOM   1033 O OD2 . ASP   A 1 130 ? 7.261   6.340   13.802  1.00 43.76 ? 127 ASP   A OD2 1 
ATOM   1034 N N   . ASP   A 1 131 ? 8.708   9.433   17.136  1.00 31.82 ? 128 ASP   A N   1 
ATOM   1035 C CA  . ASP   A 1 131 ? 8.944   10.859  17.321  1.00 35.59 ? 128 ASP   A CA  1 
ATOM   1036 C C   . ASP   A 1 131 ? 8.344   11.682  16.177  1.00 31.11 ? 128 ASP   A C   1 
ATOM   1037 O O   . ASP   A 1 131 ? 7.911   12.819  16.390  1.00 30.56 ? 128 ASP   A O   1 
ATOM   1038 C CB  . ASP   A 1 131 ? 10.451  11.098  17.487  1.00 36.28 ? 128 ASP   A CB  1 
ATOM   1039 C CG  . ASP   A 1 131 ? 11.030  10.369  18.717  1.00 40.58 ? 128 ASP   A CG  1 
ATOM   1040 O OD1 . ASP   A 1 131 ? 10.250  9.976   19.627  1.00 42.56 ? 128 ASP   A OD1 1 
ATOM   1041 O OD2 . ASP   A 1 131 ? 12.262  10.193  18.788  1.00 40.00 ? 128 ASP   A OD2 1 
ATOM   1042 N N   . ALA   A 1 132 ? 8.277   11.112  14.974  1.00 28.90 ? 129 ALA   A N   1 
ATOM   1043 C CA  . ALA   A 1 132 ? 7.690   11.817  13.836  1.00 34.32 ? 129 ALA   A CA  1 
ATOM   1044 C C   . ALA   A 1 132 ? 6.163   11.827  13.887  1.00 33.58 ? 129 ALA   A C   1 
ATOM   1045 O O   . ALA   A 1 132 ? 5.529   12.787  13.424  1.00 30.26 ? 129 ALA   A O   1 
ATOM   1046 C CB  . ALA   A 1 132 ? 8.163   11.175  12.536  1.00 37.05 ? 129 ALA   A CB  1 
ATOM   1047 N N   . LEU   A 1 133 ? 5.570   10.792  14.476  1.00 28.25 ? 130 LEU   A N   1 
ATOM   1048 C CA  . LEU   A 1 133 ? 4.117   10.630  14.554  1.00 29.22 ? 130 LEU   A CA  1 
ATOM   1049 C C   . LEU   A 1 133 ? 3.782   10.173  15.969  1.00 25.90 ? 130 LEU   A C   1 
ATOM   1050 O O   . LEU   A 1 133 ? 3.514   8.987   16.207  1.00 27.89 ? 130 LEU   A O   1 
ATOM   1051 C CB  . LEU   A 1 133 ? 3.644   9.597   13.525  1.00 26.46 ? 130 LEU   A CB  1 
ATOM   1052 C CG  . LEU   A 1 133 ? 2.286   9.599   12.833  1.00 37.69 ? 130 LEU   A CG  1 
ATOM   1053 C CD1 . LEU   A 1 133 ? 1.994   10.928  12.156  1.00 27.29 ? 130 LEU   A CD1 1 
ATOM   1054 C CD2 . LEU   A 1 133 ? 2.283   8.491   11.809  1.00 38.63 ? 130 LEU   A CD2 1 
ATOM   1055 N N   . PRO   A 1 134 ? 3.805   11.080  16.944  1.00 22.61 ? 131 PRO   A N   1 
ATOM   1056 C CA  . PRO   A 1 134 ? 3.727   10.654  18.347  1.00 28.11 ? 131 PRO   A CA  1 
ATOM   1057 C C   . PRO   A 1 134 ? 2.327   10.208  18.736  1.00 28.10 ? 131 PRO   A C   1 
ATOM   1058 O O   . PRO   A 1 134 ? 1.346   10.400  18.007  1.00 23.05 ? 131 PRO   A O   1 
ATOM   1059 C CB  . PRO   A 1 134 ? 4.142   11.902  19.131  1.00 27.11 ? 131 PRO   A CB  1 
ATOM   1060 C CG  . PRO   A 1 134 ? 3.813   13.020  18.247  1.00 30.94 ? 131 PRO   A CG  1 
ATOM   1061 C CD  . PRO   A 1 134 ? 4.048   12.529  16.836  1.00 29.09 ? 131 PRO   A CD  1 
ATOM   1062 N N   . LEU   A 1 135 ? 2.267   9.611   19.935  1.00 24.38 ? 132 LEU   A N   1 
ATOM   1063 C CA  . LEU   A 1 135 ? 1.024   9.071   20.472  1.00 25.75 ? 132 LEU   A CA  1 
ATOM   1064 C C   . LEU   A 1 135 ? -0.111  10.086  20.384  1.00 21.99 ? 132 LEU   A C   1 
ATOM   1065 O O   . LEU   A 1 135 ? -1.261  9.733   20.091  1.00 22.49 ? 132 LEU   A O   1 
ATOM   1066 C CB  . LEU   A 1 135 ? 1.249   8.634   21.931  1.00 25.08 ? 132 LEU   A CB  1 
ATOM   1067 C CG  . LEU   A 1 135 ? -0.007  8.251   22.723  1.00 24.12 ? 132 LEU   A CG  1 
ATOM   1068 C CD1 . LEU   A 1 135 ? -0.742  7.131   21.980  1.00 22.60 ? 132 LEU   A CD1 1 
ATOM   1069 C CD2 . LEU   A 1 135 ? 0.323   7.835   24.187  1.00 24.01 ? 132 LEU   A CD2 1 
ATOM   1070 N N   . SER   A 1 136 ? 0.192   11.353  20.644  1.00 22.06 ? 133 SER   A N   1 
ATOM   1071 C CA  . SER   A 1 136 ? -0.828  12.391  20.585  1.00 22.38 ? 133 SER   A CA  1 
ATOM   1072 C C   . SER   A 1 136 ? -1.534  12.469  19.227  1.00 21.79 ? 133 SER   A C   1 
ATOM   1073 O O   . SER   A 1 136 ? -2.659  12.977  19.168  1.00 24.38 ? 133 SER   A O   1 
ATOM   1074 C CB  . SER   A 1 136 ? -0.200  13.735  20.935  1.00 25.71 ? 133 SER   A CB  1 
ATOM   1075 O OG  . SER   A 1 136 ? 0.888   14.020  20.063  1.00 26.83 ? 133 SER   A OG  1 
ATOM   1076 N N   . THR   A 1 137 ? -0.913  12.000  18.134  1.00 20.20 ? 134 THR   A N   1 
ATOM   1077 C CA  . THR   A 1 137 ? -1.591  12.040  16.827  1.00 21.05 ? 134 THR   A CA  1 
ATOM   1078 C C   . THR   A 1 137 ? -2.826  11.147  16.774  1.00 22.84 ? 134 THR   A C   1 
ATOM   1079 O O   . THR   A 1 137 ? -3.623  11.280  15.833  1.00 22.65 ? 134 THR   A O   1 
ATOM   1080 C CB  . THR   A 1 137 ? -0.649  11.644  15.675  1.00 21.39 ? 134 THR   A CB  1 
ATOM   1081 O OG1 . THR   A 1 137 ? -0.239  10.271  15.803  1.00 21.27 ? 134 THR   A OG1 1 
ATOM   1082 C CG2 . THR   A 1 137 ? 0.575   12.530  15.658  1.00 22.78 ? 134 THR   A CG2 1 
ATOM   1083 N N   . ALA   A 1 138 ? -3.011  10.256  17.751  1.00 19.79 ? 135 ALA   A N   1 
ATOM   1084 C CA  . ALA   A 1 138 ? -4.264  9.519   17.826  1.00 23.10 ? 135 ALA   A CA  1 
ATOM   1085 C C   . ALA   A 1 138 ? -5.463  10.440  17.989  1.00 20.55 ? 135 ALA   A C   1 
ATOM   1086 O O   . ALA   A 1 138 ? -6.598  9.979   17.834  1.00 19.65 ? 135 ALA   A O   1 
ATOM   1087 C CB  . ALA   A 1 138 ? -4.220  8.505   18.975  1.00 18.74 ? 135 ALA   A CB  1 
ATOM   1088 N N   . LEU   A 1 139 ? -5.242  11.716  18.319  1.00 20.92 ? 136 LEU   A N   1 
ATOM   1089 C CA  . LEU   A 1 139 ? -6.293  12.719  18.368  1.00 18.33 ? 136 LEU   A CA  1 
ATOM   1090 C C   . LEU   A 1 139 ? -6.274  13.653  17.166  1.00 20.50 ? 136 LEU   A C   1 
ATOM   1091 O O   . LEU   A 1 139 ? -7.100  14.565  17.097  1.00 18.22 ? 136 LEU   A O   1 
ATOM   1092 C CB  . LEU   A 1 139 ? -6.170  13.558  19.657  1.00 17.18 ? 136 LEU   A CB  1 
ATOM   1093 C CG  . LEU   A 1 139 ? -6.416  12.758  20.943  1.00 18.16 ? 136 LEU   A CG  1 
ATOM   1094 C CD1 . LEU   A 1 139 ? -6.142  13.618  22.190  1.00 17.60 ? 136 LEU   A CD1 1 
ATOM   1095 C CD2 . LEU   A 1 139 ? -7.842  12.181  20.969  1.00 20.05 ? 136 LEU   A CD2 1 
ATOM   1096 N N   . GLY   A 1 140 ? -5.335  13.466  16.244  1.00 18.15 ? 137 GLY   A N   1 
ATOM   1097 C CA  . GLY   A 1 140 ? -5.156  14.383  15.132  1.00 22.75 ? 137 GLY   A CA  1 
ATOM   1098 C C   . GLY   A 1 140 ? -5.020  13.654  13.815  1.00 20.20 ? 137 GLY   A C   1 
ATOM   1099 O O   . GLY   A 1 140 ? -5.966  13.007  13.361  1.00 19.72 ? 137 GLY   A O   1 
ATOM   1100 N N   . VAL   A 1 141 ? -3.836  13.724  13.204  1.00 20.61 ? 138 VAL   A N   1 
ATOM   1101 C CA  . VAL   A 1 141 ? -3.667  13.144  11.870  1.00 22.62 ? 138 VAL   A CA  1 
ATOM   1102 C C   . VAL   A 1 141 ? -3.895  11.628  11.878  1.00 22.31 ? 138 VAL   A C   1 
ATOM   1103 O O   . VAL   A 1 141 ? -4.369  11.061  10.884  1.00 22.86 ? 138 VAL   A O   1 
ATOM   1104 C CB  . VAL   A 1 141 ? -2.279  13.508  11.301  1.00 23.95 ? 138 VAL   A CB  1 
ATOM   1105 C CG1 . VAL   A 1 141 ? -1.156  12.833  12.113  1.00 23.04 ? 138 VAL   A CG1 1 
ATOM   1106 C CG2 . VAL   A 1 141 ? -2.196  13.117  9.816   1.00 23.56 ? 138 VAL   A CG2 1 
ATOM   1107 N N   . MET   A 1 142 ? -3.569  10.942  12.975  1.00 22.13 ? 139 MET   A N   1 
ATOM   1108 C CA  . MET   A 1 142 ? -3.909  9.530   13.135  1.00 21.84 ? 139 MET   A CA  1 
ATOM   1109 C C   . MET   A 1 142 ? -5.167  9.335   13.976  1.00 22.79 ? 139 MET   A C   1 
ATOM   1110 O O   . MET   A 1 142 ? -5.320  8.308   14.653  1.00 23.12 ? 139 MET   A O   1 
ATOM   1111 C CB  . MET   A 1 142 ? -2.733  8.760   13.754  1.00 22.64 ? 139 MET   A CB  1 
ATOM   1112 C CG  . MET   A 1 142 ? -1.443  8.790   12.922  1.00 26.25 ? 139 MET   A CG  1 
ATOM   1113 S SD  . MET   A 1 142 ? -1.550  7.735   11.436  1.00 28.77 ? 139 MET   A SD  1 
ATOM   1114 C CE  . MET   A 1 142 ? -1.894  8.900   10.165  1.00 27.63 ? 139 MET   A CE  1 
ATOM   1115 N N   . GLY   A 1 143 ? -6.067  10.313  13.962  1.00 20.46 ? 140 GLY   A N   1 
ATOM   1116 C CA  . GLY   A 1 143 ? -7.319  10.204  14.688  1.00 22.82 ? 140 GLY   A CA  1 
ATOM   1117 C C   . GLY   A 1 143 ? -8.481  10.756  13.875  1.00 22.11 ? 140 GLY   A C   1 
ATOM   1118 O O   . GLY   A 1 143 ? -8.439  10.732  12.642  1.00 19.62 ? 140 GLY   A O   1 
ATOM   1119 N N   . GLY   A 1 144 ? -9.504  11.267  14.554  1.00 18.70 ? 141 GLY   A N   1 
ATOM   1120 C CA  . GLY   A 1 144 ? -10.702 11.754  13.905  1.00 19.91 ? 141 GLY   A CA  1 
ATOM   1121 C C   . GLY   A 1 144 ? -10.431 12.748  12.793  1.00 23.41 ? 141 GLY   A C   1 
ATOM   1122 O O   . GLY   A 1 144 ? -10.948 12.614  11.681  1.00 19.88 ? 141 GLY   A O   1 
ATOM   1123 N N   . PRO   A 1 145 ? -9.627  13.785  13.074  1.00 22.40 ? 142 PRO   A N   1 
ATOM   1124 C CA  . PRO   A 1 145 ? -9.308  14.757  11.999  1.00 21.13 ? 142 PRO   A CA  1 
ATOM   1125 C C   . PRO   A 1 145 ? -8.640  14.124  10.787  1.00 20.90 ? 142 PRO   A C   1 
ATOM   1126 O O   . PRO   A 1 145 ? -9.055  14.381  9.654   1.00 21.20 ? 142 PRO   A O   1 
ATOM   1127 C CB  . PRO   A 1 145 ? -8.383  15.771  12.700  1.00 21.74 ? 142 PRO   A CB  1 
ATOM   1128 C CG  . PRO   A 1 145 ? -8.790  15.685  14.177  1.00 22.41 ? 142 PRO   A CG  1 
ATOM   1129 C CD  . PRO   A 1 145 ? -9.142  14.219  14.400  1.00 21.18 ? 142 PRO   A CD  1 
ATOM   1130 N N   . GLY   A 1 146 ? -7.600  13.309  10.984  1.00 20.86 ? 143 GLY   A N   1 
ATOM   1131 C CA  . GLY   A 1 146 ? -6.996  12.637  9.844   1.00 18.63 ? 143 GLY   A CA  1 
ATOM   1132 C C   . GLY   A 1 146 ? -7.986  11.758  9.101   1.00 21.79 ? 143 GLY   A C   1 
ATOM   1133 O O   . GLY   A 1 146 ? -8.030  11.748  7.863   1.00 21.22 ? 143 GLY   A O   1 
ATOM   1134 N N   . MET   A 1 147 ? -8.813  11.021  9.844   1.00 17.56 ? 144 MET   A N   1 
ATOM   1135 C CA  . MET   A 1 147 ? -9.767  10.120  9.201   1.00 18.33 ? 144 MET   A CA  1 
ATOM   1136 C C   . MET   A 1 147 ? -10.776 10.904  8.361   1.00 18.67 ? 144 MET   A C   1 
ATOM   1137 O O   . MET   A 1 147 ? -11.139 10.478  7.259   1.00 20.81 ? 144 MET   A O   1 
ATOM   1138 C CB  . MET   A 1 147 ? -10.475 9.265   10.257  1.00 18.93 ? 144 MET   A CB  1 
ATOM   1139 C CG  . MET   A 1 147 ? -11.470 8.238   9.681   1.00 20.66 ? 144 MET   A CG  1 
ATOM   1140 S SD  . MET   A 1 147 ? -10.674 6.992   8.644   1.00 22.91 ? 144 MET   A SD  1 
ATOM   1141 C CE  . MET   A 1 147 ? -10.165 5.830   9.841   1.00 23.73 ? 144 MET   A CE  1 
ATOM   1142 N N   . THR   A 1 148 ? -11.224 12.063  8.867   1.00 17.25 ? 145 THR   A N   1 
ATOM   1143 C CA  . THR   A 1 148 ? -12.151 12.930  8.133   1.00 17.05 ? 145 THR   A CA  1 
ATOM   1144 C C   . THR   A 1 148 ? -11.564 13.380  6.795   1.00 18.93 ? 145 THR   A C   1 
ATOM   1145 O O   . THR   A 1 148 ? -12.235 13.337  5.752   1.00 19.41 ? 145 THR   A O   1 
ATOM   1146 C CB  . THR   A 1 148 ? -12.505 14.148  8.991   1.00 19.24 ? 145 THR   A CB  1 
ATOM   1147 O OG1 . THR   A 1 148 ? -13.020 13.702  10.255  1.00 20.12 ? 145 THR   A OG1 1 
ATOM   1148 C CG2 . THR   A 1 148 ? -13.575 15.016  8.290   1.00 19.94 ? 145 THR   A CG2 1 
ATOM   1149 N N   . ALA   A 1 149 ? -10.317 13.851  6.809   1.00 17.73 ? 146 ALA   A N   1 
ATOM   1150 C CA  . ALA   A 1 149 ? -9.693  14.326  5.574   1.00 20.65 ? 146 ALA   A CA  1 
ATOM   1151 C C   . ALA   A 1 149 ? -9.349  13.166  4.641   1.00 20.56 ? 146 ALA   A C   1 
ATOM   1152 O O   . ALA   A 1 149 ? -9.700  13.189  3.453   1.00 20.56 ? 146 ALA   A O   1 
ATOM   1153 C CB  . ALA   A 1 149 ? -8.443  15.146  5.907   1.00 18.55 ? 146 ALA   A CB  1 
ATOM   1154 N N   . TRP   A 1 150 ? -8.639  12.153  5.160   1.00 18.66 ? 147 TRP   A N   1 
ATOM   1155 C CA  . TRP   A 1 150 ? -8.284  10.986  4.350   1.00 23.51 ? 147 TRP   A CA  1 
ATOM   1156 C C   . TRP   A 1 150 ? -9.527  10.263  3.828   1.00 22.99 ? 147 TRP   A C   1 
ATOM   1157 O O   . TRP   A 1 150 ? -9.587  9.877   2.650   1.00 22.56 ? 147 TRP   A O   1 
ATOM   1158 C CB  . TRP   A 1 150 ? -7.409  10.031  5.174   1.00 23.50 ? 147 TRP   A CB  1 
ATOM   1159 C CG  . TRP   A 1 150 ? -7.097  8.743   4.486   1.00 21.43 ? 147 TRP   A CG  1 
ATOM   1160 C CD1 . TRP   A 1 150 ? -6.076  8.498   3.592   1.00 21.80 ? 147 TRP   A CD1 1 
ATOM   1161 C CD2 . TRP   A 1 150 ? -7.817  7.510   4.617   1.00 21.85 ? 147 TRP   A CD2 1 
ATOM   1162 N NE1 . TRP   A 1 150 ? -6.114  7.185   3.184   1.00 23.36 ? 147 TRP   A NE1 1 
ATOM   1163 C CE2 . TRP   A 1 150 ? -7.171  6.559   3.795   1.00 24.27 ? 147 TRP   A CE2 1 
ATOM   1164 C CE3 . TRP   A 1 150 ? -8.944  7.118   5.353   1.00 22.63 ? 147 TRP   A CE3 1 
ATOM   1165 C CZ2 . TRP   A 1 150 ? -7.623  5.243   3.677   1.00 25.51 ? 147 TRP   A CZ2 1 
ATOM   1166 C CZ3 . TRP   A 1 150 ? -9.386  5.796   5.247   1.00 22.77 ? 147 TRP   A CZ3 1 
ATOM   1167 C CH2 . TRP   A 1 150 ? -8.726  4.883   4.406   1.00 24.80 ? 147 TRP   A CH2 1 
ATOM   1168 N N   . GLY   A 1 151 ? -10.527 10.068  4.686   1.00 18.80 ? 148 GLY   A N   1 
ATOM   1169 C CA  . GLY   A 1 151 ? -11.748 9.409   4.231   1.00 20.15 ? 148 GLY   A CA  1 
ATOM   1170 C C   . GLY   A 1 151 ? -12.442 10.169  3.105   1.00 20.54 ? 148 GLY   A C   1 
ATOM   1171 O O   . GLY   A 1 151 ? -12.806 9.590   2.081   1.00 20.19 ? 148 GLY   A O   1 
ATOM   1172 N N   . THR   A 1 152 ? -12.619 11.484  3.273   1.00 20.03 ? 149 THR   A N   1 
ATOM   1173 C CA  . THR   A 1 152 ? -13.294 12.266  2.229   1.00 17.64 ? 149 THR   A CA  1 
ATOM   1174 C C   . THR   A 1 152 ? -12.547 12.164  0.902   1.00 20.02 ? 149 THR   A C   1 
ATOM   1175 O O   . THR   A 1 152 ? -13.161 12.016  -0.162  1.00 19.90 ? 149 THR   A O   1 
ATOM   1176 C CB  . THR   A 1 152 ? -13.424 13.729  2.659   1.00 17.26 ? 149 THR   A CB  1 
ATOM   1177 O OG1 . THR   A 1 152 ? -14.193 13.807  3.876   1.00 17.79 ? 149 THR   A OG1 1 
ATOM   1178 C CG2 . THR   A 1 152 ? -14.121 14.579  1.551   1.00 19.80 ? 149 THR   A CG2 1 
ATOM   1179 N N   . MET   A 1 153 ? -11.212 12.218  0.948   1.00 18.87 ? 150 MET   A N   1 
ATOM   1180 C CA  . MET   A 1 153 ? -10.414 12.320  -0.270  1.00 21.30 ? 150 MET   A CA  1 
ATOM   1181 C C   . MET   A 1 153 ? -10.148 10.973  -0.928  1.00 24.20 ? 150 MET   A C   1 
ATOM   1182 O O   . MET   A 1 153 ? -9.720  10.942  -2.087  1.00 22.34 ? 150 MET   A O   1 
ATOM   1183 C CB  . MET   A 1 153 ? -9.092  13.026  0.035   1.00 19.90 ? 150 MET   A CB  1 
ATOM   1184 C CG  . MET   A 1 153 ? -9.293  14.411  0.670   1.00 23.78 ? 150 MET   A CG  1 
ATOM   1185 S SD  . MET   A 1 153 ? -10.164 15.503  -0.479  1.00 28.75 ? 150 MET   A SD  1 
ATOM   1186 C CE  . MET   A 1 153 ? -8.876  15.733  -1.679  1.00 22.15 ? 150 MET   A CE  1 
ATOM   1187 N N   . THR   A 1 154 ? -10.379 9.867   -0.225  1.00 21.79 ? 151 THR   A N   1 
ATOM   1188 C CA  . THR   A 1 154 ? -10.236 8.555   -0.830  1.00 23.61 ? 151 THR   A CA  1 
ATOM   1189 C C   . THR   A 1 154 ? -11.555 7.857   -1.083  1.00 20.81 ? 151 THR   A C   1 
ATOM   1190 O O   . THR   A 1 154 ? -11.597 6.957   -1.919  1.00 27.48 ? 151 THR   A O   1 
ATOM   1191 C CB  . THR   A 1 154 ? -9.367  7.635   0.043   1.00 23.11 ? 151 THR   A CB  1 
ATOM   1192 O OG1 . THR   A 1 154 ? -9.997  7.425   1.318   1.00 22.08 ? 151 THR   A OG1 1 
ATOM   1193 C CG2 . THR   A 1 154 ? -7.968  8.246   0.240   1.00 27.57 ? 151 THR   A CG2 1 
ATOM   1194 N N   . LYS   A 1 155 ? -12.629 8.231   -0.388  1.00 23.20 ? 152 LYS   A N   1 
ATOM   1195 C CA  . LYS   A 1 155 ? -13.905 7.557   -0.555  1.00 21.94 ? 152 LYS   A CA  1 
ATOM   1196 C C   . LYS   A 1 155 ? -14.963 8.404   -1.250  1.00 28.17 ? 152 LYS   A C   1 
ATOM   1197 O O   . LYS   A 1 155 ? -15.997 7.859   -1.661  1.00 26.54 ? 152 LYS   A O   1 
ATOM   1198 C CB  . LYS   A 1 155 ? -14.440 7.095   0.804   1.00 25.28 ? 152 LYS   A CB  1 
ATOM   1199 C CG  . LYS   A 1 155 ? -13.427 6.267   1.624   1.00 27.71 ? 152 LYS   A CG  1 
ATOM   1200 C CD  . LYS   A 1 155 ? -13.965 5.923   3.016   1.00 24.22 ? 152 LYS   A CD  1 
ATOM   1201 C CE  . LYS   A 1 155 ? -12.876 5.231   3.863   1.00 24.03 ? 152 LYS   A CE  1 
ATOM   1202 N NZ  . LYS   A 1 155 ? -12.554 3.882   3.323   1.00 26.35 ? 152 LYS   A NZ  1 
ATOM   1203 N N   . PHE   A 1 156 ? -14.754 9.712   -1.384  1.00 22.56 ? 153 PHE   A N   1 
ATOM   1204 C CA  . PHE   A 1 156 ? -15.757 10.535  -2.053  1.00 23.42 ? 153 PHE   A CA  1 
ATOM   1205 C C   . PHE   A 1 156 ? -15.135 11.387  -3.150  1.00 23.79 ? 153 PHE   A C   1 
ATOM   1206 O O   . PHE   A 1 156 ? -15.459 11.222  -4.332  1.00 21.60 ? 153 PHE   A O   1 
ATOM   1207 C CB  . PHE   A 1 156 ? -16.500 11.425  -1.055  1.00 21.38 ? 153 PHE   A CB  1 
ATOM   1208 C CG  . PHE   A 1 156 ? -17.372 12.461  -1.714  1.00 19.97 ? 153 PHE   A CG  1 
ATOM   1209 C CD1 . PHE   A 1 156 ? -18.379 12.070  -2.590  1.00 23.62 ? 153 PHE   A CD1 1 
ATOM   1210 C CD2 . PHE   A 1 156 ? -17.186 13.800  -1.472  1.00 21.43 ? 153 PHE   A CD2 1 
ATOM   1211 C CE1 . PHE   A 1 156 ? -19.186 13.015  -3.231  1.00 24.33 ? 153 PHE   A CE1 1 
ATOM   1212 C CE2 . PHE   A 1 156 ? -18.010 14.762  -2.101  1.00 22.30 ? 153 PHE   A CE2 1 
ATOM   1213 C CZ  . PHE   A 1 156 ? -19.000 14.345  -2.996  1.00 20.01 ? 153 PHE   A CZ  1 
ATOM   1214 N N   . MET   A 1 157 ? -14.267 12.319  -2.775  1.00 22.31 ? 154 MET   A N   1 
ATOM   1215 C CA  . MET   A 1 157 ? -13.700 13.228  -3.759  1.00 24.33 ? 154 MET   A CA  1 
ATOM   1216 C C   . MET   A 1 157 ? -12.726 12.482  -4.656  1.00 26.48 ? 154 MET   A C   1 
ATOM   1217 O O   . MET   A 1 157 ? -11.978 11.613  -4.205  1.00 30.37 ? 154 MET   A O   1 
ATOM   1218 C CB  . MET   A 1 157 ? -13.008 14.407  -3.071  1.00 23.28 ? 154 MET   A CB  1 
ATOM   1219 C CG  . MET   A 1 157 ? -13.826 15.700  -3.176  1.00 28.44 ? 154 MET   A CG  1 
ATOM   1220 S SD  . MET   A 1 157 ? -13.057 17.104  -2.366  1.00 37.69 ? 154 MET   A SD  1 
ATOM   1221 C CE  . MET   A 1 157 ? -14.514 18.070  -2.015  1.00 26.31 ? 154 MET   A CE  1 
ATOM   1222 N N   . GLN   A 1 158 ? -12.764 12.796  -5.940  1.00 22.42 ? 155 GLN   A N   1 
ATOM   1223 C CA  . GLN   A 1 158 ? -11.868 12.177  -6.919  1.00 28.89 ? 155 GLN   A CA  1 
ATOM   1224 C C   . GLN   A 1 158 ? -11.109 13.308  -7.596  1.00 24.10 ? 155 GLN   A C   1 
ATOM   1225 O O   . GLN   A 1 158 ? -11.413 13.674  -8.734  1.00 26.37 ? 155 GLN   A O   1 
ATOM   1226 C CB  . GLN   A 1 158 ? -12.642 11.323  -7.936  1.00 28.93 ? 155 GLN   A CB  1 
ATOM   1227 C CG  . GLN   A 1 158 ? -13.558 10.261  -7.323  1.00 36.12 ? 155 GLN   A CG  1 
ATOM   1228 C CD  . GLN   A 1 158 ? -14.511 9.653   -8.352  1.00 49.44 ? 155 GLN   A CD  1 
ATOM   1229 O OE1 . GLN   A 1 158 ? -15.629 10.144  -8.556  1.00 50.62 ? 155 GLN   A OE1 1 
ATOM   1230 N NE2 . GLN   A 1 158 ? -14.066 8.586   -9.011  1.00 56.83 ? 155 GLN   A NE2 1 
ATOM   1231 N N   . VAL   A 1 159 ? -10.140 13.887  -6.888  1.00 23.29 ? 156 VAL   A N   1 
ATOM   1232 C CA  . VAL   A 1 159 ? -9.385  14.998  -7.462  1.00 23.67 ? 156 VAL   A CA  1 
ATOM   1233 C C   . VAL   A 1 159 ? -8.572  14.504  -8.655  1.00 24.05 ? 156 VAL   A C   1 
ATOM   1234 O O   . VAL   A 1 159 ? -7.891  13.474  -8.578  1.00 24.90 ? 156 VAL   A O   1 
ATOM   1235 C CB  . VAL   A 1 159 ? -8.483  15.649  -6.398  1.00 23.81 ? 156 VAL   A CB  1 
ATOM   1236 C CG1 . VAL   A 1 159 ? -7.662  16.762  -7.033  1.00 21.41 ? 156 VAL   A CG1 1 
ATOM   1237 C CG2 . VAL   A 1 159 ? -9.312  16.219  -5.262  1.00 22.44 ? 156 VAL   A CG2 1 
ATOM   1238 N N   . ARG   A 1 160 ? -8.639  15.244  -9.781  1.00 23.51 ? 157 ARG   A N   1 
ATOM   1239 C CA  . ARG   A 1 160 ? -7.883  14.921  -10.986 1.00 23.65 ? 157 ARG   A CA  1 
ATOM   1240 C C   . ARG   A 1 160 ? -6.831  15.997  -11.265 1.00 25.12 ? 157 ARG   A C   1 
ATOM   1241 O O   . ARG   A 1 160 ? -7.001  17.159  -10.870 1.00 23.06 ? 157 ARG   A O   1 
ATOM   1242 C CB  . ARG   A 1 160 ? -8.798  14.811  -12.216 1.00 25.08 ? 157 ARG   A CB  1 
ATOM   1243 C CG  . ARG   A 1 160 ? -9.853  13.712  -12.152 1.00 31.57 ? 157 ARG   A CG  1 
ATOM   1244 C CD  . ARG   A 1 160 ? -9.214  12.353  -11.878 1.00 34.22 ? 157 ARG   A CD  1 
ATOM   1245 N NE  . ARG   A 1 160 ? -8.138  12.067  -12.821 1.00 38.46 ? 157 ARG   A NE  1 
ATOM   1246 C CZ  . ARG   A 1 160 ? -7.177  11.172  -12.620 1.00 41.65 ? 157 ARG   A CZ  1 
ATOM   1247 N NH1 . ARG   A 1 160 ? -7.138  10.433  -11.517 1.00 35.77 ? 157 ARG   A NH1 1 
ATOM   1248 N NH2 . ARG   A 1 160 ? -6.225  11.021  -13.542 1.00 36.04 ? 157 ARG   A NH2 1 
ATOM   1249 N N   . PRO   A 1 161 ? -5.741  15.652  -11.960 1.00 26.53 ? 158 PRO   A N   1 
ATOM   1250 C CA  . PRO   A 1 161 ? -4.736  16.670  -12.288 1.00 24.76 ? 158 PRO   A CA  1 
ATOM   1251 C C   . PRO   A 1 161 ? -5.381  17.813  -13.060 1.00 23.11 ? 158 PRO   A C   1 
ATOM   1252 O O   . PRO   A 1 161 ? -6.179  17.597  -13.971 1.00 25.68 ? 158 PRO   A O   1 
ATOM   1253 C CB  . PRO   A 1 161 ? -3.715  15.907  -13.152 1.00 23.90 ? 158 PRO   A CB  1 
ATOM   1254 C CG  . PRO   A 1 161 ? -3.887  14.462  -12.761 1.00 25.35 ? 158 PRO   A CG  1 
ATOM   1255 C CD  . PRO   A 1 161 ? -5.354  14.304  -12.434 1.00 24.97 ? 158 PRO   A CD  1 
ATOM   1256 N N   . GLY   A 1 162 ? -5.023  19.038  -12.691 1.00 23.56 ? 159 GLY   A N   1 
ATOM   1257 C CA  . GLY   A 1 162 ? -5.600  20.211  -13.305 1.00 25.73 ? 159 GLY   A CA  1 
ATOM   1258 C C   . GLY   A 1 162 ? -6.906  20.684  -12.693 1.00 30.52 ? 159 GLY   A C   1 
ATOM   1259 O O   . GLY   A 1 162 ? -7.388  21.758  -13.069 1.00 27.91 ? 159 GLY   A O   1 
ATOM   1260 N N   . ASP   A 1 163 ? -7.489  19.925  -11.764 1.00 25.23 ? 160 ASP   A N   1 
ATOM   1261 C CA  . ASP   A 1 163 ? -8.650  20.414  -11.027 1.00 24.83 ? 160 ASP   A CA  1 
ATOM   1262 C C   . ASP   A 1 163 ? -8.295  21.657  -10.221 1.00 23.74 ? 160 ASP   A C   1 
ATOM   1263 O O   . ASP   A 1 163 ? -7.155  21.843  -9.784  1.00 24.68 ? 160 ASP   A O   1 
ATOM   1264 C CB  . ASP   A 1 163 ? -9.171  19.348  -10.067 1.00 22.54 ? 160 ASP   A CB  1 
ATOM   1265 C CG  . ASP   A 1 163 ? -10.037 18.318  -10.741 1.00 28.05 ? 160 ASP   A CG  1 
ATOM   1266 O OD1 . ASP   A 1 163 ? -10.390 18.493  -11.926 1.00 24.33 ? 160 ASP   A OD1 1 
ATOM   1267 O OD2 . ASP   A 1 163 ? -10.366 17.322  -10.063 1.00 25.55 ? 160 ASP   A OD2 1 
ATOM   1268 N N   . THR   A 1 164 ? -9.292  22.510  -9.998  1.00 22.95 ? 161 THR   A N   1 
ATOM   1269 C CA  . THR   A 1 164 ? -9.180  23.526  -8.963  1.00 22.84 ? 161 THR   A CA  1 
ATOM   1270 C C   . THR   A 1 164 ? -10.004 23.104  -7.751  1.00 23.26 ? 161 THR   A C   1 
ATOM   1271 O O   . THR   A 1 164 ? -11.209 22.822  -7.872  1.00 21.04 ? 161 THR   A O   1 
ATOM   1272 C CB  . THR   A 1 164 ? -9.615  24.903  -9.476  1.00 22.66 ? 161 THR   A CB  1 
ATOM   1273 O OG1 . THR   A 1 164 ? -8.726  25.303  -10.525 1.00 24.28 ? 161 THR   A OG1 1 
ATOM   1274 C CG2 . THR   A 1 164 ? -9.527  25.949  -8.341  1.00 20.92 ? 161 THR   A CG2 1 
ATOM   1275 N N   . VAL   A 1 165 ? -9.353  23.054  -6.588  1.00 18.32 ? 162 VAL   A N   1 
ATOM   1276 C CA  . VAL   A 1 165 ? -9.982  22.637  -5.337  1.00 20.26 ? 162 VAL   A CA  1 
ATOM   1277 C C   . VAL   A 1 165 ? -10.001 23.820  -4.381  1.00 22.68 ? 162 VAL   A C   1 
ATOM   1278 O O   . VAL   A 1 165 ? -8.963  24.458  -4.159  1.00 23.79 ? 162 VAL   A O   1 
ATOM   1279 C CB  . VAL   A 1 165 ? -9.242  21.451  -4.689  1.00 20.92 ? 162 VAL   A CB  1 
ATOM   1280 C CG1 . VAL   A 1 165 ? -9.927  21.096  -3.369  1.00 19.49 ? 162 VAL   A CG1 1 
ATOM   1281 C CG2 . VAL   A 1 165 ? -9.210  20.236  -5.639  1.00 19.20 ? 162 VAL   A CG2 1 
ATOM   1282 N N   . VAL   A 1 166 ? -11.176 24.119  -3.823  1.00 19.62 ? 163 VAL   A N   1 
ATOM   1283 C CA  . VAL   A 1 166 ? -11.325 25.180  -2.834  1.00 16.69 ? 163 VAL   A CA  1 
ATOM   1284 C C   . VAL   A 1 166 ? -11.559 24.523  -1.480  1.00 21.78 ? 163 VAL   A C   1 
ATOM   1285 O O   . VAL   A 1 166 ? -12.319 23.551  -1.373  1.00 18.85 ? 163 VAL   A O   1 
ATOM   1286 C CB  . VAL   A 1 166 ? -12.492 26.142  -3.180  1.00 19.78 ? 163 VAL   A CB  1 
ATOM   1287 C CG1 . VAL   A 1 166 ? -12.666 27.193  -2.071  1.00 17.07 ? 163 VAL   A CG1 1 
ATOM   1288 C CG2 . VAL   A 1 166 ? -12.259 26.832  -4.528  1.00 20.77 ? 163 VAL   A CG2 1 
ATOM   1289 N N   . VAL   A 1 167 ? -10.894 25.046  -0.451  1.00 19.74 ? 164 VAL   A N   1 
ATOM   1290 C CA  . VAL   A 1 167 ? -11.016 24.567  0.921   1.00 17.72 ? 164 VAL   A CA  1 
ATOM   1291 C C   . VAL   A 1 167 ? -11.317 25.780  1.793   1.00 22.05 ? 164 VAL   A C   1 
ATOM   1292 O O   . VAL   A 1 167 ? -10.455 26.655  1.953   1.00 22.31 ? 164 VAL   A O   1 
ATOM   1293 C CB  . VAL   A 1 167 ? -9.735  23.872  1.403   1.00 21.23 ? 164 VAL   A CB  1 
ATOM   1294 C CG1 . VAL   A 1 167 ? -9.908  23.354  2.833   1.00 19.05 ? 164 VAL   A CG1 1 
ATOM   1295 C CG2 . VAL   A 1 167 ? -9.321  22.725  0.445   1.00 18.13 ? 164 VAL   A CG2 1 
ATOM   1296 N N   . SER   A 1 168 ? -12.519 25.833  2.367   1.00 18.56 ? 165 SER   A N   1 
ATOM   1297 C CA  . SER   A 1 168 ? -12.828 26.857  3.358   1.00 21.47 ? 165 SER   A CA  1 
ATOM   1298 C C   . SER   A 1 168 ? -12.482 26.336  4.751   1.00 26.00 ? 165 SER   A C   1 
ATOM   1299 O O   . SER   A 1 168 ? -12.604 25.139  5.027   1.00 27.07 ? 165 SER   A O   1 
ATOM   1300 C CB  . SER   A 1 168 ? -14.295 27.283  3.277   1.00 20.13 ? 165 SER   A CB  1 
ATOM   1301 O OG  . SER   A 1 168 ? -15.183 26.205  3.519   1.00 24.29 ? 165 SER   A OG  1 
ATOM   1302 N N   . GLY   A 1 169 ? -11.996 27.228  5.607   1.00 22.21 ? 166 GLY   A N   1 
ATOM   1303 C CA  . GLY   A 1 169 ? -11.455 26.798  6.888   1.00 24.49 ? 166 GLY   A CA  1 
ATOM   1304 C C   . GLY   A 1 169 ? -10.140 26.068  6.720   1.00 29.03 ? 166 GLY   A C   1 
ATOM   1305 O O   . GLY   A 1 169 ? -9.907  25.047  7.385   1.00 28.95 ? 166 GLY   A O   1 
ATOM   1306 N N   . ALA   A 1 170 ? -9.263  26.581  5.857   1.00 22.86 ? 167 ALA   A N   1 
ATOM   1307 C CA  . ALA   A 1 170 ? -8.117  25.810  5.390   1.00 26.08 ? 167 ALA   A CA  1 
ATOM   1308 C C   . ALA   A 1 170 ? -6.980  25.741  6.399   1.00 27.32 ? 167 ALA   A C   1 
ATOM   1309 O O   . ALA   A 1 170 ? -6.136  24.849  6.295   1.00 28.70 ? 167 ALA   A O   1 
ATOM   1310 C CB  . ALA   A 1 170 ? -7.594  26.408  4.077   1.00 24.22 ? 167 ALA   A CB  1 
ATOM   1311 N N   . SER   A 1 171 ? -6.933  26.648  7.370   1.00 25.33 ? 168 SER   A N   1 
ATOM   1312 C CA  . SER   A 1 171 ? -5.784  26.731  8.262   1.00 32.17 ? 168 SER   A CA  1 
ATOM   1313 C C   . SER   A 1 171 ? -5.794  25.680  9.367   1.00 29.16 ? 168 SER   A C   1 
ATOM   1314 O O   . SER   A 1 171 ? -4.740  25.420  9.948   1.00 33.34 ? 168 SER   A O   1 
ATOM   1315 C CB  . SER   A 1 171 ? -5.705  28.133  8.873   1.00 30.27 ? 168 SER   A CB  1 
ATOM   1316 O OG  . SER   A 1 171 ? -6.888  28.404  9.591   1.00 38.81 ? 168 SER   A OG  1 
ATOM   1317 N N   . GLY   A 1 172 ? -6.929  25.043  9.646   1.00 25.93 ? 169 GLY   A N   1 
ATOM   1318 C CA  . GLY   A 1 172 ? -6.957  23.929  10.594  1.00 26.60 ? 169 GLY   A CA  1 
ATOM   1319 C C   . GLY   A 1 172 ? -6.307  22.666  10.033  1.00 27.76 ? 169 GLY   A C   1 
ATOM   1320 O O   . GLY   A 1 172 ? -5.885  22.591  8.878   1.00 27.15 ? 169 GLY   A O   1 
ATOM   1321 N N   . MET   A 1 173 ? -6.229  21.641  10.886  1.00 22.39 ? 170 MET   A N   1 
ATOM   1322 C CA  . MET   A 1 173 ? -5.593  20.393  10.467  1.00 24.25 ? 170 MET   A CA  1 
ATOM   1323 C C   . MET   A 1 173 ? -6.353  19.738  9.317   1.00 20.53 ? 170 MET   A C   1 
ATOM   1324 O O   . MET   A 1 173 ? -5.749  19.245  8.360   1.00 20.74 ? 170 MET   A O   1 
ATOM   1325 C CB  . MET   A 1 173 ? -5.486  19.416  11.645  1.00 26.83 ? 170 MET   A CB  1 
ATOM   1326 C CG  . MET   A 1 173 ? -5.264  17.979  11.167  1.00 26.01 ? 170 MET   A CG  1 
ATOM   1327 S SD  . MET   A 1 173 ? -4.565  16.855  12.393  1.00 32.62 ? 170 MET   A SD  1 
ATOM   1328 C CE  . MET   A 1 173 ? -2.953  17.591  12.724  1.00 29.06 ? 170 MET   A CE  1 
ATOM   1329 N N   . ILE   A 1 174 ? -7.678  19.679  9.418   1.00 18.28 ? 171 ILE   A N   1 
ATOM   1330 C CA  . ILE   A 1 174 ? -8.451  18.974  8.403   1.00 20.01 ? 171 ILE   A CA  1 
ATOM   1331 C C   . ILE   A 1 174 ? -8.299  19.675  7.061   1.00 22.43 ? 171 ILE   A C   1 
ATOM   1332 O O   . ILE   A 1 174 ? -7.962  19.051  6.048   1.00 19.94 ? 171 ILE   A O   1 
ATOM   1333 C CB  . ILE   A 1 174 ? -9.923  18.861  8.828   1.00 19.74 ? 171 ILE   A CB  1 
ATOM   1334 C CG1 . ILE   A 1 174 ? -10.024 18.039  10.119  1.00 22.05 ? 171 ILE   A CG1 1 
ATOM   1335 C CG2 . ILE   A 1 174 ? -10.759 18.190  7.737   1.00 21.02 ? 171 ILE   A CG2 1 
ATOM   1336 C CD1 . ILE   A 1 174 ? -11.455 17.752  10.574  1.00 21.29 ? 171 ILE   A CD1 1 
ATOM   1337 N N   . GLY   A 1 175 ? -8.494  20.997  7.053   1.00 19.25 ? 172 GLY   A N   1 
ATOM   1338 C CA  . GLY   A 1 175 ? -8.329  21.758  5.828   1.00 23.13 ? 172 GLY   A CA  1 
ATOM   1339 C C   . GLY   A 1 175 ? -6.939  21.649  5.233   1.00 21.72 ? 172 GLY   A C   1 
ATOM   1340 O O   . GLY   A 1 175 ? -6.788  21.535  4.013   1.00 19.92 ? 172 GLY   A O   1 
ATOM   1341 N N   . THR   A 1 176 ? -5.894  21.708  6.074   1.00 22.08 ? 173 THR   A N   1 
ATOM   1342 C CA  . THR   A 1 176 ? -4.543  21.635  5.517   1.00 22.98 ? 173 THR   A CA  1 
ATOM   1343 C C   . THR   A 1 176 ? -4.239  20.247  4.987   1.00 22.91 ? 173 THR   A C   1 
ATOM   1344 O O   . THR   A 1 176 ? -3.510  20.117  3.997   1.00 22.28 ? 173 THR   A O   1 
ATOM   1345 C CB  . THR   A 1 176 ? -3.459  22.027  6.542   1.00 26.43 ? 173 THR   A CB  1 
ATOM   1346 O OG1 . THR   A 1 176 ? -3.422  21.069  7.605   1.00 33.81 ? 173 THR   A OG1 1 
ATOM   1347 C CG2 . THR   A 1 176 ? -3.696  23.431  7.094   1.00 26.47 ? 173 THR   A CG2 1 
ATOM   1348 N N   . LEU   A 1 177 ? -4.767  19.207  5.640   1.00 18.59 ? 174 LEU   A N   1 
ATOM   1349 C CA  . LEU   A 1 177 ? -4.608  17.852  5.123   1.00 20.64 ? 174 LEU   A CA  1 
ATOM   1350 C C   . LEU   A 1 177 ? -5.320  17.704  3.779   1.00 19.63 ? 174 LEU   A C   1 
ATOM   1351 O O   . LEU   A 1 177 ? -4.746  17.202  2.803   1.00 18.80 ? 174 LEU   A O   1 
ATOM   1352 C CB  . LEU   A 1 177 ? -5.142  16.826  6.132   1.00 18.85 ? 174 LEU   A CB  1 
ATOM   1353 C CG  . LEU   A 1 177 ? -4.370  16.650  7.448   1.00 22.48 ? 174 LEU   A CG  1 
ATOM   1354 C CD1 . LEU   A 1 177 ? -5.074  15.629  8.356   1.00 23.44 ? 174 LEU   A CD1 1 
ATOM   1355 C CD2 . LEU   A 1 177 ? -2.938  16.190  7.163   1.00 21.13 ? 174 LEU   A CD2 1 
ATOM   1356 N N   . VAL   A 1 178 ? -6.577  18.141  3.712   1.00 17.17 ? 175 VAL   A N   1 
ATOM   1357 C CA  . VAL   A 1 178 ? -7.301  18.061  2.445   1.00 19.94 ? 175 VAL   A CA  1 
ATOM   1358 C C   . VAL   A 1 178 ? -6.538  18.807  1.364   1.00 19.62 ? 175 VAL   A C   1 
ATOM   1359 O O   . VAL   A 1 178 ? -6.357  18.306  0.244   1.00 19.26 ? 175 VAL   A O   1 
ATOM   1360 C CB  . VAL   A 1 178 ? -8.732  18.601  2.610   1.00 20.02 ? 175 VAL   A CB  1 
ATOM   1361 C CG1 . VAL   A 1 178 ? -9.408  18.729  1.261   1.00 17.11 ? 175 VAL   A CG1 1 
ATOM   1362 C CG2 . VAL   A 1 178 ? -9.554  17.695  3.553   1.00 16.82 ? 175 VAL   A CG2 1 
ATOM   1363 N N   . GLY   A 1 179 ? -6.031  19.995  1.698   1.00 20.33 ? 176 GLY   A N   1 
ATOM   1364 C CA  . GLY   A 1 179 ? -5.346  20.799  0.694   1.00 18.43 ? 176 GLY   A CA  1 
ATOM   1365 C C   . GLY   A 1 179 ? -4.103  20.123  0.150   1.00 18.69 ? 176 GLY   A C   1 
ATOM   1366 O O   . GLY   A 1 179 ? -3.866  20.112  -1.059  1.00 19.29 ? 176 GLY   A O   1 
ATOM   1367 N N   . GLN   A 1 180 ? -3.282  19.556  1.045   1.00 18.24 ? 177 GLN   A N   1 
ATOM   1368 C CA  . GLN   A 1 180 ? -2.055  18.896  0.607   1.00 22.37 ? 177 GLN   A CA  1 
ATOM   1369 C C   . GLN   A 1 180 ? -2.338  17.612  -0.162  1.00 20.68 ? 177 GLN   A C   1 
ATOM   1370 O O   . GLN   A 1 180 ? -1.586  17.260  -1.077  1.00 19.76 ? 177 GLN   A O   1 
ATOM   1371 C CB  . GLN   A 1 180 ? -1.161  18.582  1.814   1.00 20.04 ? 177 GLN   A CB  1 
ATOM   1372 C CG  . GLN   A 1 180 ? -0.575  19.784  2.528   1.00 22.89 ? 177 GLN   A CG  1 
ATOM   1373 C CD  . GLN   A 1 180 ? 0.123   19.372  3.815   1.00 27.78 ? 177 GLN   A CD  1 
ATOM   1374 O OE1 . GLN   A 1 180 ? 1.324   19.135  3.831   1.00 27.65 ? 177 GLN   A OE1 1 
ATOM   1375 N NE2 . GLN   A 1 180 ? -0.644  19.243  4.893   1.00 24.90 ? 177 GLN   A NE2 1 
ATOM   1376 N N   . MET   A 1 181 ? -3.386  16.880  0.213   1.00 18.85 ? 178 MET   A N   1 
ATOM   1377 C CA  . MET   A 1 181 ? -3.768  15.704  -0.570  1.00 21.20 ? 178 MET   A CA  1 
ATOM   1378 C C   . MET   A 1 181 ? -4.255  16.105  -1.955  1.00 20.26 ? 178 MET   A C   1 
ATOM   1379 O O   . MET   A 1 181 ? -3.971  15.419  -2.940  1.00 21.93 ? 178 MET   A O   1 
ATOM   1380 C CB  . MET   A 1 181 ? -4.845  14.909  0.166   1.00 19.49 ? 178 MET   A CB  1 
ATOM   1381 C CG  . MET   A 1 181 ? -4.290  14.048  1.301   1.00 25.69 ? 178 MET   A CG  1 
ATOM   1382 S SD  . MET   A 1 181 ? -5.600  13.079  2.094   1.00 31.31 ? 178 MET   A SD  1 
ATOM   1383 C CE  . MET   A 1 181 ? -6.406  14.314  2.992   1.00 24.93 ? 178 MET   A CE  1 
ATOM   1384 N N   . ALA   A 1 182 ? -5.031  17.184  -2.036  1.00 18.14 ? 179 ALA   A N   1 
ATOM   1385 C CA  . ALA   A 1 182 ? -5.463  17.683  -3.331  1.00 23.58 ? 179 ALA   A CA  1 
ATOM   1386 C C   . ALA   A 1 182 ? -4.263  18.059  -4.192  1.00 22.88 ? 179 ALA   A C   1 
ATOM   1387 O O   . ALA   A 1 182 ? -4.216  17.727  -5.380  1.00 20.88 ? 179 ALA   A O   1 
ATOM   1388 C CB  . ALA   A 1 182 ? -6.399  18.876  -3.138  1.00 20.94 ? 179 ALA   A CB  1 
ATOM   1389 N N   . LYS   A 1 183 ? -3.270  18.723  -3.596  1.00 21.95 ? 180 LYS   A N   1 
ATOM   1390 C CA  . LYS   A 1 183 ? -2.070  19.093  -4.343  1.00 22.58 ? 180 LYS   A CA  1 
ATOM   1391 C C   . LYS   A 1 183 ? -1.334  17.852  -4.841  1.00 24.12 ? 180 LYS   A C   1 
ATOM   1392 O O   . LYS   A 1 183 ? -0.919  17.798  -6.008  1.00 21.37 ? 180 LYS   A O   1 
ATOM   1393 C CB  . LYS   A 1 183 ? -1.168  19.971  -3.469  1.00 26.24 ? 180 LYS   A CB  1 
ATOM   1394 C CG  . LYS   A 1 183 ? 0.187   20.306  -4.091  1.00 34.52 ? 180 LYS   A CG  1 
ATOM   1395 C CD  . LYS   A 1 183 ? 0.047   21.082  -5.412  1.00 37.82 ? 180 LYS   A CD  1 
ATOM   1396 C CE  . LYS   A 1 183 ? -0.685  22.411  -5.221  1.00 34.49 ? 180 LYS   A CE  1 
ATOM   1397 N NZ  . LYS   A 1 183 ? -0.815  23.179  -6.522  1.00 33.95 ? 180 LYS   A NZ  1 
ATOM   1398 N N   . ARG   A 1 184 ? -1.182  16.833  -3.977  1.00 23.57 ? 181 ARG   A N   1 
ATOM   1399 C CA  . ARG   A 1 184 ? -0.600  15.560  -4.411  1.00 25.47 ? 181 ARG   A CA  1 
ATOM   1400 C C   . ARG   A 1 184 ? -1.354  14.962  -5.585  1.00 25.78 ? 181 ARG   A C   1 
ATOM   1401 O O   . ARG   A 1 184 ? -0.751  14.274  -6.428  1.00 26.05 ? 181 ARG   A O   1 
ATOM   1402 C CB  . ARG   A 1 184 ? -0.580  14.537  -3.264  1.00 28.02 ? 181 ARG   A CB  1 
ATOM   1403 C CG  . ARG   A 1 184 ? 0.555   14.719  -2.269  1.00 34.19 ? 181 ARG   A CG  1 
ATOM   1404 C CD  . ARG   A 1 184 ? 0.555   13.612  -1.196  1.00 34.62 ? 181 ARG   A CD  1 
ATOM   1405 N NE  . ARG   A 1 184 ? 0.474   12.272  -1.772  1.00 32.92 ? 181 ARG   A NE  1 
ATOM   1406 C CZ  . ARG   A 1 184 ? 1.517   11.595  -2.224  1.00 36.13 ? 181 ARG   A CZ  1 
ATOM   1407 N NH1 . ARG   A 1 184 ? 2.744   12.104  -2.184  1.00 41.51 ? 181 ARG   A NH1 1 
ATOM   1408 N NH2 . ARG   A 1 184 ? 1.329   10.381  -2.731  1.00 38.22 ? 181 ARG   A NH2 1 
ATOM   1409 N N   . ALA   A 1 185 ? -2.668  15.184  -5.647  1.00 24.98 ? 182 ALA   A N   1 
ATOM   1410 C CA  . ALA   A 1 185 ? -3.482  14.673  -6.735  1.00 23.64 ? 182 ALA   A CA  1 
ATOM   1411 C C   . ALA   A 1 185 ? -3.399  15.541  -7.985  1.00 22.38 ? 182 ALA   A C   1 
ATOM   1412 O O   . ALA   A 1 185 ? -4.060  15.224  -8.978  1.00 23.06 ? 182 ALA   A O   1 
ATOM   1413 C CB  . ALA   A 1 185 ? -4.948  14.544  -6.282  1.00 22.46 ? 182 ALA   A CB  1 
ATOM   1414 N N   . GLY   A 1 186 ? -2.609  16.612  -7.963  1.00 23.67 ? 183 GLY   A N   1 
ATOM   1415 C CA  . GLY   A 1 186 ? -2.379  17.431  -9.148  1.00 23.64 ? 183 GLY   A CA  1 
ATOM   1416 C C   . GLY   A 1 186 ? -3.228  18.683  -9.256  1.00 23.98 ? 183 GLY   A C   1 
ATOM   1417 O O   . GLY   A 1 186 ? -3.223  19.322  -10.314 1.00 21.76 ? 183 GLY   A O   1 
ATOM   1418 N N   . ALA   A 1 187 ? -3.941  19.047  -8.199  1.00 20.97 ? 184 ALA   A N   1 
ATOM   1419 C CA  . ALA   A 1 187 ? -4.903  20.138  -8.237  1.00 23.78 ? 184 ALA   A CA  1 
ATOM   1420 C C   . ALA   A 1 187 ? -4.243  21.480  -7.983  1.00 23.43 ? 184 ALA   A C   1 
ATOM   1421 O O   . ALA   A 1 187 ? -3.206  21.573  -7.315  1.00 23.93 ? 184 ALA   A O   1 
ATOM   1422 C CB  . ALA   A 1 187 ? -5.995  19.915  -7.182  1.00 19.45 ? 184 ALA   A CB  1 
ATOM   1423 N N   . ARG   A 1 188 ? -4.858  22.528  -8.527  1.00 24.23 ? 185 ARG   A N   1 
ATOM   1424 C CA  . ARG   A 1 188 ? -4.662  23.871  -8.014  1.00 23.73 ? 185 ARG   A CA  1 
ATOM   1425 C C   . ARG   A 1 188 ? -5.503  24.024  -6.754  1.00 23.68 ? 185 ARG   A C   1 
ATOM   1426 O O   . ARG   A 1 188 ? -6.696  23.701  -6.761  1.00 20.00 ? 185 ARG   A O   1 
ATOM   1427 C CB  . ARG   A 1 188 ? -5.075  24.920  -9.055  1.00 23.39 ? 185 ARG   A CB  1 
ATOM   1428 C CG  . ARG   A 1 188 ? -5.035  26.373  -8.522  1.00 21.75 ? 185 ARG   A CG  1 
ATOM   1429 C CD  . ARG   A 1 188 ? -5.482  27.374  -9.597  1.00 24.71 ? 185 ARG   A CD  1 
ATOM   1430 N NE  . ARG   A 1 188 ? -5.524  28.747  -9.105  1.00 28.94 ? 185 ARG   A NE  1 
ATOM   1431 C CZ  . ARG   A 1 188 ? -4.457  29.519  -8.930  1.00 28.46 ? 185 ARG   A CZ  1 
ATOM   1432 N NH1 . ARG   A 1 188 ? -3.238  29.080  -9.187  1.00 32.70 ? 185 ARG   A NH1 1 
ATOM   1433 N NH2 . ARG   A 1 188 ? -4.617  30.763  -8.488  1.00 31.65 ? 185 ARG   A NH2 1 
ATOM   1434 N N   . VAL   A 1 189 ? -4.899  24.518  -5.672  1.00 19.99 ? 186 VAL   A N   1 
ATOM   1435 C CA  . VAL   A 1 189 ? -5.552  24.503  -4.366  1.00 20.43 ? 186 VAL   A CA  1 
ATOM   1436 C C   . VAL   A 1 189 ? -5.704  25.932  -3.854  1.00 23.49 ? 186 VAL   A C   1 
ATOM   1437 O O   . VAL   A 1 189 ? -4.713  26.675  -3.725  1.00 23.46 ? 186 VAL   A O   1 
ATOM   1438 C CB  . VAL   A 1 189 ? -4.787  23.620  -3.361  1.00 22.28 ? 186 VAL   A CB  1 
ATOM   1439 C CG1 . VAL   A 1 189 ? -5.507  23.592  -2.025  1.00 23.05 ? 186 VAL   A CG1 1 
ATOM   1440 C CG2 . VAL   A 1 189 ? -4.621  22.203  -3.923  1.00 20.89 ? 186 VAL   A CG2 1 
ATOM   1441 N N   . VAL   A 1 190 ? -6.944  26.302  -3.537  1.00 21.54 ? 187 VAL   A N   1 
ATOM   1442 C CA  . VAL   A 1 190 ? -7.308  27.629  -3.055  1.00 20.80 ? 187 VAL   A CA  1 
ATOM   1443 C C   . VAL   A 1 190 ? -7.885  27.474  -1.660  1.00 24.42 ? 187 VAL   A C   1 
ATOM   1444 O O   . VAL   A 1 190 ? -8.777  26.648  -1.436  1.00 24.29 ? 187 VAL   A O   1 
ATOM   1445 C CB  . VAL   A 1 190 ? -8.341  28.300  -3.982  1.00 22.26 ? 187 VAL   A CB  1 
ATOM   1446 C CG1 . VAL   A 1 190 ? -8.732  29.669  -3.427  1.00 22.90 ? 187 VAL   A CG1 1 
ATOM   1447 C CG2 . VAL   A 1 190 ? -7.785  28.419  -5.392  1.00 23.78 ? 187 VAL   A CG2 1 
ATOM   1448 N N   . GLY   A 1 191 ? -7.390  28.263  -0.707  1.00 22.31 ? 188 GLY   A N   1 
ATOM   1449 C CA  . GLY   A 1 191 ? -7.855  28.193  0.654   1.00 23.97 ? 188 GLY   A CA  1 
ATOM   1450 C C   . GLY   A 1 191 ? -8.350  29.550  1.130   1.00 29.42 ? 188 GLY   A C   1 
ATOM   1451 O O   . GLY   A 1 191 ? -8.108  30.589  0.497   1.00 27.63 ? 188 GLY   A O   1 
ATOM   1452 N N   . THR   A 1 192 ? -9.074  29.530  2.241   1.00 24.12 ? 189 THR   A N   1 
ATOM   1453 C CA  . THR   A 1 192 ? -9.401  30.745  2.978   1.00 27.94 ? 189 THR   A CA  1 
ATOM   1454 C C   . THR   A 1 192 ? -8.639  30.712  4.294   1.00 30.16 ? 189 THR   A C   1 
ATOM   1455 O O   . THR   A 1 192 ? -8.407  29.633  4.847   1.00 33.29 ? 189 THR   A O   1 
ATOM   1456 C CB  . THR   A 1 192 ? -10.917 30.873  3.215   1.00 29.83 ? 189 THR   A CB  1 
ATOM   1457 O OG1 . THR   A 1 192 ? -11.403 29.735  3.937   1.00 36.17 ? 189 THR   A OG1 1 
ATOM   1458 C CG2 . THR   A 1 192 ? -11.661 30.963  1.897   1.00 28.64 ? 189 THR   A CG2 1 
ATOM   1459 N N   . ALA   A 1 193 ? -8.198  31.879  4.769   1.00 31.36 ? 190 ALA   A N   1 
ATOM   1460 C CA  . ALA   A 1 193 ? -7.498  31.950  6.044   1.00 32.32 ? 190 ALA   A CA  1 
ATOM   1461 C C   . ALA   A 1 193 ? -7.713  33.323  6.676   1.00 34.61 ? 190 ALA   A C   1 
ATOM   1462 O O   . ALA   A 1 193 ? -8.185  34.265  6.034   1.00 34.29 ? 190 ALA   A O   1 
ATOM   1463 C CB  . ALA   A 1 193 ? -5.998  31.644  5.897   1.00 33.10 ? 190 ALA   A CB  1 
ATOM   1464 N N   . GLY   A 1 194 ? -7.339  33.419  7.953   1.00 33.33 ? 191 GLY   A N   1 
ATOM   1465 C CA  . GLY   A 1 194 ? -7.680  34.560  8.777   1.00 38.06 ? 191 GLY   A CA  1 
ATOM   1466 C C   . GLY   A 1 194 ? -6.641  35.662  8.915   1.00 38.18 ? 191 GLY   A C   1 
ATOM   1467 O O   . GLY   A 1 194 ? -6.942  36.695  9.511   1.00 38.96 ? 191 GLY   A O   1 
ATOM   1468 N N   . SER   A 1 195 ? -5.429  35.476  8.393   1.00 34.08 ? 192 SER   A N   1 
ATOM   1469 C CA  . SER   A 1 195 ? -4.417  36.516  8.547   1.00 37.24 ? 192 SER   A CA  1 
ATOM   1470 C C   . SER   A 1 195 ? -3.323  36.304  7.518   1.00 36.27 ? 192 SER   A C   1 
ATOM   1471 O O   . SER   A 1 195 ? -3.147  35.202  6.991   1.00 34.71 ? 192 SER   A O   1 
ATOM   1472 C CB  . SER   A 1 195 ? -3.818  36.530  9.955   1.00 37.41 ? 192 SER   A CB  1 
ATOM   1473 O OG  . SER   A 1 195 ? -2.984  35.401  10.154  1.00 43.02 ? 192 SER   A OG  1 
ATOM   1474 N N   . ALA   A 1 196 ? -2.579  37.379  7.246   1.00 33.14 ? 193 ALA   A N   1 
ATOM   1475 C CA  . ALA   A 1 196 ? -1.500  37.287  6.269   1.00 33.44 ? 193 ALA   A CA  1 
ATOM   1476 C C   . ALA   A 1 196 ? -0.530  36.172  6.631   1.00 31.53 ? 193 ALA   A C   1 
ATOM   1477 O O   . ALA   A 1 196 ? -0.069  35.430  5.752   1.00 31.91 ? 193 ALA   A O   1 
ATOM   1478 C CB  . ALA   A 1 196 ? -0.760  38.620  6.162   1.00 37.25 ? 193 ALA   A CB  1 
ATOM   1479 N N   . GLY   A 1 197 ? -0.221  36.031  7.920   1.00 31.22 ? 194 GLY   A N   1 
ATOM   1480 C CA  . GLY   A 1 197 ? 0.726   35.010  8.337   1.00 35.21 ? 194 GLY   A CA  1 
ATOM   1481 C C   . GLY   A 1 197 ? 0.202   33.605  8.113   1.00 33.22 ? 194 GLY   A C   1 
ATOM   1482 O O   . GLY   A 1 197 ? 0.946   32.721  7.679   1.00 29.39 ? 194 GLY   A O   1 
ATOM   1483 N N   . LYS   A 1 198 ? -1.084  33.381  8.397   1.00 34.29 ? 195 LYS   A N   1 
ATOM   1484 C CA  . LYS   A 1 198 ? -1.668  32.064  8.151   1.00 37.14 ? 195 LYS   A CA  1 
ATOM   1485 C C   . LYS   A 1 198 ? -1.768  31.784  6.657   1.00 32.61 ? 195 LYS   A C   1 
ATOM   1486 O O   . LYS   A 1 198 ? -1.530  30.654  6.216   1.00 33.25 ? 195 LYS   A O   1 
ATOM   1487 C CB  . LYS   A 1 198 ? -3.032  31.951  8.837   1.00 35.88 ? 195 LYS   A CB  1 
ATOM   1488 C CG  . LYS   A 1 198 ? -2.912  31.809  10.362  1.00 44.88 ? 195 LYS   A CG  1 
ATOM   1489 C CD  . LYS   A 1 198 ? -4.175  31.231  10.999  1.00 47.95 ? 195 LYS   A CD  1 
ATOM   1490 C CE  . LYS   A 1 198 ? -3.840  30.278  12.166  1.00 50.38 ? 195 LYS   A CE  1 
ATOM   1491 N NZ  . LYS   A 1 198 ? -5.055  29.684  12.828  1.00 41.28 ? 195 LYS   A NZ  1 
ATOM   1492 N N   . ALA   A 1 199 ? -2.074  32.807  5.854   1.00 33.23 ? 196 ALA   A N   1 
ATOM   1493 C CA  . ALA   A 1 199 ? -2.029  32.641  4.404   1.00 30.24 ? 196 ALA   A CA  1 
ATOM   1494 C C   . ALA   A 1 199 ? -0.647  32.193  3.929   1.00 32.32 ? 196 ALA   A C   1 
ATOM   1495 O O   . ALA   A 1 199 ? -0.535  31.315  3.060   1.00 27.89 ? 196 ALA   A O   1 
ATOM   1496 C CB  . ALA   A 1 199 ? -2.428  33.945  3.708   1.00 29.69 ? 196 ALA   A CB  1 
ATOM   1497 N N   . ARG   A 1 200 ? 0.423   32.809  4.458   1.00 31.63 ? 197 ARG   A N   1 
ATOM   1498 C CA  . ARG   A 1 200 ? 1.769   32.419  4.041   1.00 28.94 ? 197 ARG   A CA  1 
ATOM   1499 C C   . ARG   A 1 200 ? 2.107   31.016  4.522   1.00 25.10 ? 197 ARG   A C   1 
ATOM   1500 O O   . ARG   A 1 200 ? 2.816   30.275  3.837   1.00 30.34 ? 197 ARG   A O   1 
ATOM   1501 C CB  . ARG   A 1 200 ? 2.802   33.427  4.564   1.00 31.14 ? 197 ARG   A CB  1 
ATOM   1502 C CG  . ARG   A 1 200 ? 2.667   34.824  3.955   1.00 32.63 ? 197 ARG   A CG  1 
ATOM   1503 C CD  . ARG   A 1 200 ? 2.889   34.782  2.456   1.00 34.46 ? 197 ARG   A CD  1 
ATOM   1504 N NE  . ARG   A 1 200 ? 4.280   34.486  2.131   1.00 42.49 ? 197 ARG   A NE  1 
ATOM   1505 C CZ  . ARG   A 1 200 ? 4.678   33.750  1.097   1.00 46.49 ? 197 ARG   A CZ  1 
ATOM   1506 N NH1 . ARG   A 1 200 ? 3.807   33.173  0.279   1.00 41.21 ? 197 ARG   A NH1 1 
ATOM   1507 N NH2 . ARG   A 1 200 ? 5.984   33.580  0.884   1.00 43.79 ? 197 ARG   A NH2 1 
ATOM   1508 N N   . TYR   A 1 201 ? 1.614   30.640  5.696   1.00 27.63 ? 198 TYR   A N   1 
ATOM   1509 C CA  . TYR   A 1 201 ? 1.762   29.262  6.155   1.00 30.42 ? 198 TYR   A CA  1 
ATOM   1510 C C   . TYR   A 1 201 ? 1.119   28.282  5.167   1.00 30.21 ? 198 TYR   A C   1 
ATOM   1511 O O   . TYR   A 1 201 ? 1.737   27.285  4.765   1.00 30.40 ? 198 TYR   A O   1 
ATOM   1512 C CB  . TYR   A 1 201 ? 1.157   29.159  7.551   1.00 35.04 ? 198 TYR   A CB  1 
ATOM   1513 C CG  . TYR   A 1 201 ? 0.887   27.768  8.071   1.00 40.16 ? 198 TYR   A CG  1 
ATOM   1514 C CD1 . TYR   A 1 201 ? 1.923   26.937  8.485   1.00 38.12 ? 198 TYR   A CD1 1 
ATOM   1515 C CD2 . TYR   A 1 201 ? -0.420  27.310  8.191   1.00 37.98 ? 198 TYR   A CD2 1 
ATOM   1516 C CE1 . TYR   A 1 201 ? 1.658   25.667  8.990   1.00 44.74 ? 198 TYR   A CE1 1 
ATOM   1517 C CE2 . TYR   A 1 201 ? -0.696  26.059  8.688   1.00 41.14 ? 198 TYR   A CE2 1 
ATOM   1518 C CZ  . TYR   A 1 201 ? 0.340   25.237  9.089   1.00 46.58 ? 198 TYR   A CZ  1 
ATOM   1519 O OH  . TYR   A 1 201 ? 0.040   23.984  9.590   1.00 46.22 ? 198 TYR   A OH  1 
ATOM   1520 N N   . LEU   A 1 202 ? -0.109  28.573  4.726   1.00 31.42 ? 199 LEU   A N   1 
ATOM   1521 C CA  . LEU   A 1 202 ? -0.763  27.697  3.751   1.00 30.04 ? 199 LEU   A CA  1 
ATOM   1522 C C   . LEU   A 1 202 ? 0.006   27.663  2.437   1.00 31.79 ? 199 LEU   A C   1 
ATOM   1523 O O   . LEU   A 1 202 ? 0.080   26.621  1.767   1.00 27.92 ? 199 LEU   A O   1 
ATOM   1524 C CB  . LEU   A 1 202 ? -2.206  28.143  3.527   1.00 30.95 ? 199 LEU   A CB  1 
ATOM   1525 C CG  . LEU   A 1 202 ? -3.062  28.009  4.794   1.00 31.65 ? 199 LEU   A CG  1 
ATOM   1526 C CD1 . LEU   A 1 202 ? -4.517  28.365  4.535   1.00 30.28 ? 199 LEU   A CD1 1 
ATOM   1527 C CD2 . LEU   A 1 202 ? -2.943  26.608  5.359   1.00 33.95 ? 199 LEU   A CD2 1 
ATOM   1528 N N   . SER   A 1 203 ? 0.579   28.798  2.037   1.00 28.26 ? 200 SER   A N   1 
ATOM   1529 C CA  . SER   A 1 203 ? 1.379   28.809  0.817   1.00 31.18 ? 200 SER   A CA  1 
ATOM   1530 C C   . SER   A 1 203 ? 2.610   27.924  0.976   1.00 27.54 ? 200 SER   A C   1 
ATOM   1531 O O   . SER   A 1 203 ? 3.007   27.219  0.043   1.00 29.66 ? 200 SER   A O   1 
ATOM   1532 C CB  . SER   A 1 203 ? 1.755   30.254  0.471   1.00 31.87 ? 200 SER   A CB  1 
ATOM   1533 O OG  . SER   A 1 203 ? 2.309   30.338  -0.819  1.00 42.43 ? 200 SER   A OG  1 
ATOM   1534 N N   . GLN   A 1 204 ? 3.213   27.928  2.165   1.00 31.78 ? 201 GLN   A N   1 
ATOM   1535 C CA  . GLN   A 1 204 ? 4.349   27.046  2.415   1.00 35.77 ? 201 GLN   A CA  1 
ATOM   1536 C C   . GLN   A 1 204 ? 3.960   25.580  2.290   1.00 30.69 ? 201 GLN   A C   1 
ATOM   1537 O O   . GLN   A 1 204 ? 4.782   24.752  1.879   1.00 30.75 ? 201 GLN   A O   1 
ATOM   1538 C CB  . GLN   A 1 204 ? 4.923   27.312  3.809   1.00 33.36 ? 201 GLN   A CB  1 
ATOM   1539 C CG  . GLN   A 1 204 ? 6.314   27.882  3.795   1.00 49.95 ? 201 GLN   A CG  1 
ATOM   1540 C CD  . GLN   A 1 204 ? 6.677   28.533  5.114   1.00 49.57 ? 201 GLN   A CD  1 
ATOM   1541 O OE1 . GLN   A 1 204 ? 6.473   27.954  6.193   1.00 44.79 ? 201 GLN   A OE1 1 
ATOM   1542 N NE2 . GLN   A 1 204 ? 7.204   29.755  5.037   1.00 40.69 ? 201 GLN   A NE2 1 
ATOM   1543 N N   . LEU   A 1 205 ? 2.729   25.232  2.660   1.00 32.57 ? 202 LEU   A N   1 
ATOM   1544 C CA  . LEU   A 1 205 ? 2.263   23.852  2.572   1.00 31.47 ? 202 LEU   A CA  1 
ATOM   1545 C C   . LEU   A 1 205 ? 1.791   23.453  1.176   1.00 33.84 ? 202 LEU   A C   1 
ATOM   1546 O O   . LEU   A 1 205 ? 1.428   22.287  0.976   1.00 34.04 ? 202 LEU   A O   1 
ATOM   1547 C CB  . LEU   A 1 205 ? 1.134   23.618  3.580   1.00 28.40 ? 202 LEU   A CB  1 
ATOM   1548 C CG  . LEU   A 1 205 ? 1.522   23.798  5.053   1.00 31.97 ? 202 LEU   A CG  1 
ATOM   1549 C CD1 . LEU   A 1 205 ? 0.349   23.573  5.974   1.00 33.40 ? 202 LEU   A CD1 1 
ATOM   1550 C CD2 . LEU   A 1 205 ? 2.651   22.868  5.393   1.00 36.38 ? 202 LEU   A CD2 1 
ATOM   1551 N N   . GLY   A 1 206 ? 1.780   24.365  0.209   1.00 31.20 ? 203 GLY   A N   1 
ATOM   1552 C CA  . GLY   A 1 206 ? 1.409   24.029  -1.157  1.00 26.75 ? 203 GLY   A CA  1 
ATOM   1553 C C   . GLY   A 1 206 ? 0.169   24.725  -1.679  1.00 30.94 ? 203 GLY   A C   1 
ATOM   1554 O O   . GLY   A 1 206 ? -0.107  24.627  -2.882  1.00 29.82 ? 203 GLY   A O   1 
ATOM   1555 N N   . PHE   A 1 207 ? -0.602  25.425  -0.848  1.00 26.45 ? 204 PHE   A N   1 
ATOM   1556 C CA  . PHE   A 1 207 ? -1.757  26.149  -1.368  1.00 25.26 ? 204 PHE   A CA  1 
ATOM   1557 C C   . PHE   A 1 207 ? -1.309  27.156  -2.422  1.00 30.26 ? 204 PHE   A C   1 
ATOM   1558 O O   . PHE   A 1 207 ? -0.279  27.819  -2.273  1.00 29.87 ? 204 PHE   A O   1 
ATOM   1559 C CB  . PHE   A 1 207 ? -2.500  26.846  -0.238  1.00 27.00 ? 204 PHE   A CB  1 
ATOM   1560 C CG  . PHE   A 1 207 ? -3.414  25.940  0.534   1.00 24.47 ? 204 PHE   A CG  1 
ATOM   1561 C CD1 . PHE   A 1 207 ? -2.901  24.971  1.383   1.00 27.09 ? 204 PHE   A CD1 1 
ATOM   1562 C CD2 . PHE   A 1 207 ? -4.785  26.071  0.422   1.00 24.91 ? 204 PHE   A CD2 1 
ATOM   1563 C CE1 . PHE   A 1 207 ? -3.750  24.133  2.105   1.00 25.57 ? 204 PHE   A CE1 1 
ATOM   1564 C CE2 . PHE   A 1 207 ? -5.643  25.246  1.135   1.00 25.22 ? 204 PHE   A CE2 1 
ATOM   1565 C CZ  . PHE   A 1 207 ? -5.134  24.277  1.978   1.00 24.51 ? 204 PHE   A CZ  1 
ATOM   1566 N N   . ASP   A 1 208 ? -2.067  27.240  -3.512  1.00 27.79 ? 205 ASP   A N   1 
ATOM   1567 C CA  . ASP   A 1 208 ? -1.699  28.095  -4.630  1.00 28.05 ? 205 ASP   A CA  1 
ATOM   1568 C C   . ASP   A 1 208 ? -2.227  29.504  -4.476  1.00 32.69 ? 205 ASP   A C   1 
ATOM   1569 O O   . ASP   A 1 208 ? -1.631  30.449  -5.010  1.00 28.71 ? 205 ASP   A O   1 
ATOM   1570 C CB  . ASP   A 1 208 ? -2.203  27.480  -5.941  1.00 30.70 ? 205 ASP   A CB  1 
ATOM   1571 C CG  . ASP   A 1 208 ? -1.526  26.168  -6.246  1.00 33.20 ? 205 ASP   A CG  1 
ATOM   1572 O OD1 . ASP   A 1 208 ? -0.319  26.192  -6.575  1.00 36.27 ? 205 ASP   A OD1 1 
ATOM   1573 O OD2 . ASP   A 1 208 ? -2.175  25.104  -6.109  1.00 31.40 ? 205 ASP   A OD2 1 
ATOM   1574 N N   . ALA   A 1 209 ? -3.318  29.665  -3.735  1.00 27.56 ? 206 ALA   A N   1 
ATOM   1575 C CA  . ALA   A 1 209 ? -3.866  30.972  -3.433  1.00 27.31 ? 206 ALA   A CA  1 
ATOM   1576 C C   . ALA   A 1 209 ? -4.598  30.870  -2.110  1.00 31.23 ? 206 ALA   A C   1 
ATOM   1577 O O   . ALA   A 1 209 ? -5.163  29.829  -1.772  1.00 25.49 ? 206 ALA   A O   1 
ATOM   1578 C CB  . ALA   A 1 209 ? -4.813  31.468  -4.534  1.00 28.83 ? 206 ALA   A CB  1 
ATOM   1579 N N   . VAL   A 1 210 ? -4.565  31.949  -1.346  1.00 28.12 ? 207 VAL   A N   1 
ATOM   1580 C CA  . VAL   A 1 210 ? -5.291  32.012  -0.092  1.00 27.73 ? 207 VAL   A CA  1 
ATOM   1581 C C   . VAL   A 1 210 ? -6.090  33.299  -0.085  1.00 32.83 ? 207 VAL   A C   1 
ATOM   1582 O O   . VAL   A 1 210 ? -5.552  34.365  -0.406  1.00 37.56 ? 207 VAL   A O   1 
ATOM   1583 C CB  . VAL   A 1 210 ? -4.344  31.950  1.118   1.00 32.68 ? 207 VAL   A CB  1 
ATOM   1584 C CG1 . VAL   A 1 210 ? -5.150  31.964  2.403   1.00 30.49 ? 207 VAL   A CG1 1 
ATOM   1585 C CG2 . VAL   A 1 210 ? -3.448  30.716  1.023   1.00 29.81 ? 207 VAL   A CG2 1 
ATOM   1586 N N   . ILE   A 1 211 ? -7.366  33.205  0.275   1.00 29.98 ? 208 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -8.232  34.372  0.379   1.00 31.56 ? 208 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -8.409  34.719  1.847   1.00 34.00 ? 208 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -8.676  33.839  2.676   1.00 31.85 ? 208 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -9.588  34.116  -0.292  1.00 32.74 ? 208 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -9.412  33.975  -1.808  1.00 30.67 ? 208 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -10.568 35.230  0.033   1.00 36.99 ? 208 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.606 33.337  -2.471  1.00 31.35 ? 208 ILE   A CD1 1 
ATOM   1594 N N   . ASP   A 1 212 ? -8.271  35.999  2.170   1.00 36.52 ? 209 ASP   A N   1 
ATOM   1595 C CA  . ASP   A 1 212 ? -8.546  36.505  3.513   1.00 34.56 ? 209 ASP   A CA  1 
ATOM   1596 C C   . ASP   A 1 212 ? -10.053 36.639  3.696   1.00 40.02 ? 209 ASP   A C   1 
ATOM   1597 O O   . ASP   A 1 212 ? -10.669 37.554  3.140   1.00 43.28 ? 209 ASP   A O   1 
ATOM   1598 C CB  . ASP   A 1 212 ? -7.849  37.847  3.717   1.00 42.11 ? 209 ASP   A CB  1 
ATOM   1599 C CG  . ASP   A 1 212 ? -8.016  38.390  5.122   1.00 44.98 ? 209 ASP   A CG  1 
ATOM   1600 O OD1 . ASP   A 1 212 ? -9.133  38.339  5.678   1.00 44.30 ? 209 ASP   A OD1 1 
ATOM   1601 O OD2 . ASP   A 1 212 ? -7.010  38.875  5.674   1.00 54.36 ? 209 ASP   A OD2 1 
ATOM   1602 N N   . TYR   A 1 213 ? -10.650 35.749  4.497   1.00 34.37 ? 210 TYR   A N   1 
ATOM   1603 C CA  . TYR   A 1 213 ? -12.098 35.792  4.684   1.00 41.07 ? 210 TYR   A CA  1 
ATOM   1604 C C   . TYR   A 1 213 ? -12.541 36.946  5.580   1.00 41.97 ? 210 TYR   A C   1 
ATOM   1605 O O   . TYR   A 1 213 ? -13.717 37.320  5.545   1.00 40.89 ? 210 TYR   A O   1 
ATOM   1606 C CB  . TYR   A 1 213 ? -12.617 34.470  5.257   1.00 33.48 ? 210 TYR   A CB  1 
ATOM   1607 C CG  . TYR   A 1 213 ? -12.218 34.161  6.689   1.00 35.73 ? 210 TYR   A CG  1 
ATOM   1608 C CD1 . TYR   A 1 213 ? -12.975 34.629  7.763   1.00 42.62 ? 210 TYR   A CD1 1 
ATOM   1609 C CD2 . TYR   A 1 213 ? -11.114 33.372  6.965   1.00 35.78 ? 210 TYR   A CD2 1 
ATOM   1610 C CE1 . TYR   A 1 213 ? -12.628 34.339  9.071   1.00 37.20 ? 210 TYR   A CE1 1 
ATOM   1611 C CE2 . TYR   A 1 213 ? -10.753 33.073  8.267   1.00 38.92 ? 210 TYR   A CE2 1 
ATOM   1612 C CZ  . TYR   A 1 213 ? -11.514 33.560  9.315   1.00 38.49 ? 210 TYR   A CZ  1 
ATOM   1613 O OH  . TYR   A 1 213 ? -11.160 33.258  10.609  1.00 38.81 ? 210 TYR   A OH  1 
ATOM   1614 N N   . LYS   A 1 214 ? -11.640 37.514  6.382   1.00 39.80 ? 211 LYS   A N   1 
ATOM   1615 C CA  . LYS   A 1 214 ? -12.021 38.683  7.170   1.00 43.76 ? 211 LYS   A CA  1 
ATOM   1616 C C   . LYS   A 1 214 ? -12.192 39.909  6.280   1.00 47.15 ? 211 LYS   A C   1 
ATOM   1617 O O   . LYS   A 1 214 ? -13.053 40.755  6.548   1.00 46.13 ? 211 LYS   A O   1 
ATOM   1618 C CB  . LYS   A 1 214 ? -10.986 38.932  8.268   1.00 36.92 ? 211 LYS   A CB  1 
ATOM   1619 C CG  . LYS   A 1 214 ? -10.739 37.691  9.090   1.00 38.39 ? 211 LYS   A CG  1 
ATOM   1620 C CD  . LYS   A 1 214 ? -10.570 38.008  10.555  1.00 43.49 ? 211 LYS   A CD  1 
ATOM   1621 C CE  . LYS   A 1 214 ? -10.546 36.734  11.383  1.00 44.09 ? 211 LYS   A CE  1 
ATOM   1622 N NZ  . LYS   A 1 214 ? -9.662  36.876  12.584  1.00 51.32 ? 211 LYS   A NZ  1 
ATOM   1623 N N   . LEU   A 1 215 ? -11.444 39.991  5.203   1.00 46.10 ? 212 LEU   A N   1 
ATOM   1624 C CA  . LEU   A 1 215 ? -11.628 41.080  4.280   1.00 47.81 ? 212 LEU   A CA  1 
ATOM   1625 C C   . LEU   A 1 215 ? -12.802 40.805  3.333   1.00 52.71 ? 212 LEU   A C   1 
ATOM   1626 O O   . LEU   A 1 215 ? -13.687 41.630  3.190   1.00 50.94 ? 212 LEU   A O   1 
ATOM   1627 C CB  . LEU   A 1 215 ? -10.339 41.310  3.519   1.00 46.22 ? 212 LEU   A CB  1 
ATOM   1628 C CG  . LEU   A 1 215 ? -9.069  41.315  4.356   1.00 55.57 ? 212 LEU   A CG  1 
ATOM   1629 C CD1 . LEU   A 1 215 ? -7.863  41.646  3.496   1.00 59.40 ? 212 LEU   A CD1 1 
ATOM   1630 C CD2 . LEU   A 1 215 ? -9.166  42.250  5.551   1.00 53.55 ? 212 LEU   A CD2 1 
ATOM   1631 N N   . ALA   A 1 216 ? -12.820 39.641  2.703   1.00 45.94 ? 213 ALA   A N   1 
ATOM   1632 C CA  . ALA   A 1 216 ? -13.911 39.279  1.798   1.00 45.49 ? 213 ALA   A CA  1 
ATOM   1633 C C   . ALA   A 1 216 ? -15.108 38.780  2.616   1.00 48.64 ? 213 ALA   A C   1 
ATOM   1634 O O   . ALA   A 1 216 ? -15.522 37.620  2.546   1.00 39.14 ? 213 ALA   A O   1 
ATOM   1635 C CB  . ALA   A 1 216 ? -13.430 38.244  0.789   1.00 40.76 ? 213 ALA   A CB  1 
ATOM   1636 N N   . ASP   A 1 217 ? -15.691 39.711  3.378   1.00 52.56 ? 214 ASP   A N   1 
ATOM   1637 C CA  . ASP   A 1 217 ? -16.680 39.407  4.408   1.00 51.07 ? 214 ASP   A CA  1 
ATOM   1638 C C   . ASP   A 1 217 ? -18.113 39.287  3.891   1.00 53.31 ? 214 ASP   A C   1 
ATOM   1639 O O   . ASP   A 1 217 ? -19.038 39.154  4.701   1.00 56.23 ? 214 ASP   A O   1 
ATOM   1640 C CB  . ASP   A 1 217 ? -16.631 40.465  5.514   1.00 54.44 ? 214 ASP   A CB  1 
ATOM   1641 C CG  . ASP   A 1 217 ? -16.737 41.876  4.973   1.00 55.52 ? 214 ASP   A CG  1 
ATOM   1642 O OD1 . ASP   A 1 217 ? -17.401 42.070  3.937   1.00 56.85 ? 214 ASP   A OD1 1 
ATOM   1643 O OD2 . ASP   A 1 217 ? -16.138 42.791  5.582   1.00 64.01 ? 214 ASP   A OD2 1 
ATOM   1644 N N   . ASP   A 1 218 ? -18.332 39.334  2.580   1.00 51.52 ? 215 ASP   A N   1 
ATOM   1645 C CA  . ASP   A 1 218 ? -19.651 39.056  2.029   1.00 48.64 ? 215 ASP   A CA  1 
ATOM   1646 C C   . ASP   A 1 218 ? -19.487 38.273  0.737   1.00 46.44 ? 215 ASP   A C   1 
ATOM   1647 O O   . ASP   A 1 218 ? -18.379 38.134  0.207   1.00 43.36 ? 215 ASP   A O   1 
ATOM   1648 C CB  . ASP   A 1 218 ? -20.456 40.342  1.789   1.00 50.80 ? 215 ASP   A CB  1 
ATOM   1649 C CG  . ASP   A 1 218 ? -19.730 41.318  0.896   1.00 53.09 ? 215 ASP   A CG  1 
ATOM   1650 O OD1 . ASP   A 1 218 ? -19.433 40.941  -0.258  1.00 52.87 ? 215 ASP   A OD1 1 
ATOM   1651 O OD2 . ASP   A 1 218 ? -19.453 42.454  1.347   1.00 54.04 ? 215 ASP   A OD2 1 
ATOM   1652 N N   . ALA   A 1 219 ? -20.613 37.759  0.231   1.00 45.34 ? 216 ALA   A N   1 
ATOM   1653 C CA  . ALA   A 1 219 ? -20.572 36.921  -0.966  1.00 47.65 ? 216 ALA   A CA  1 
ATOM   1654 C C   . ALA   A 1 219 ? -20.014 37.686  -2.165  1.00 43.32 ? 216 ALA   A C   1 
ATOM   1655 O O   . ALA   A 1 219 ? -19.284 37.117  -2.985  1.00 44.36 ? 216 ALA   A O   1 
ATOM   1656 C CB  . ALA   A 1 219 ? -21.968 36.366  -1.273  1.00 43.32 ? 216 ALA   A CB  1 
ATOM   1657 N N   . ASP   A 1 220 ? -20.327 38.982  -2.276  1.00 45.98 ? 217 ASP   A N   1 
ATOM   1658 C CA  . ASP   A 1 220 ? -19.847 39.759  -3.418  1.00 47.57 ? 217 ASP   A CA  1 
ATOM   1659 C C   . ASP   A 1 220 ? -18.324 39.820  -3.435  1.00 45.05 ? 217 ASP   A C   1 
ATOM   1660 O O   . ASP   A 1 220 ? -17.686 39.478  -4.438  1.00 40.00 ? 217 ASP   A O   1 
ATOM   1661 C CB  . ASP   A 1 220 ? -20.442 41.170  -3.396  1.00 49.34 ? 217 ASP   A CB  1 
ATOM   1662 C CG  . ASP   A 1 220 ? -21.591 41.337  -4.380  1.00 60.89 ? 217 ASP   A CG  1 
ATOM   1663 O OD1 . ASP   A 1 220 ? -21.992 40.331  -5.011  1.00 65.00 ? 217 ASP   A OD1 1 
ATOM   1664 O OD2 . ASP   A 1 220 ? -22.103 42.473  -4.519  1.00 64.56 ? 217 ASP   A OD2 1 
ATOM   1665 N N   . LYS   A 1 221 ? -17.731 40.207  -2.331  1.00 40.24 ? 218 LYS   A N   1 
ATOM   1666 C CA  . LYS   A 1 221 ? -16.290 40.272  -2.267  1.00 44.92 ? 218 LYS   A CA  1 
ATOM   1667 C C   . LYS   A 1 221 ? -15.658 38.888  -2.357  1.00 39.84 ? 218 LYS   A C   1 
ATOM   1668 O O   . LYS   A 1 221 ? -14.584 38.722  -2.900  1.00 36.58 ? 218 LYS   A O   1 
ATOM   1669 C CB  . LYS   A 1 221 ? -15.850 40.953  -0.981  1.00 45.52 ? 218 LYS   A CB  1 
ATOM   1670 C CG  . LYS   A 1 221 ? -16.564 42.252  -0.665  1.00 47.81 ? 218 LYS   A CG  1 
ATOM   1671 C CD  . LYS   A 1 221 ? -16.369 42.627  0.794   1.00 52.29 ? 218 LYS   A CD  1 
ATOM   1672 C CE  . LYS   A 1 221 ? -16.810 44.055  1.073   1.00 55.23 ? 218 LYS   A CE  1 
ATOM   1673 N NZ  . LYS   A 1 221 ? -16.226 44.571  2.340   1.00 53.33 ? 218 LYS   A NZ  1 
ATOM   1674 N N   . MET   A 1 222 ? -16.342 37.907  -1.800  1.00 38.79 ? 219 MET   A N   1 
ATOM   1675 C CA  . MET   A 1 222 ? -15.834 36.546  -1.888  1.00 35.72 ? 219 MET   A CA  1 
ATOM   1676 C C   . MET   A 1 222 ? -15.921 36.036  -3.321  1.00 32.56 ? 219 MET   A C   1 
ATOM   1677 O O   . MET   A 1 222 ? -14.967 35.440  -3.836  1.00 31.68 ? 219 MET   A O   1 
ATOM   1678 C CB  . MET   A 1 222 ? -16.611 35.652  -0.915  1.00 35.98 ? 219 MET   A CB  1 
ATOM   1679 C CG  . MET   A 1 222 ? -15.995 34.306  -0.645  1.00 33.54 ? 219 MET   A CG  1 
ATOM   1680 S SD  . MET   A 1 222 ? -14.198 34.308  -0.485  1.00 43.80 ? 219 MET   A SD  1 
ATOM   1681 C CE  . MET   A 1 222 ? -13.990 34.332  1.274   1.00 32.89 ? 219 MET   A CE  1 
ATOM   1682 N N   . ARG   A 1 223 ? -17.044 36.297  -3.994  1.00 35.56 ? 220 ARG   A N   1 
ATOM   1683 C CA  . ARG   A 1 223 ? -17.179 35.954  -5.405  1.00 32.89 ? 220 ARG   A CA  1 
ATOM   1684 C C   . ARG   A 1 223 ? -16.033 36.534  -6.223  1.00 35.51 ? 220 ARG   A C   1 
ATOM   1685 O O   . ARG   A 1 223 ? -15.454 35.853  -7.075  1.00 29.41 ? 220 ARG   A O   1 
ATOM   1686 C CB  . ARG   A 1 223 ? -18.524 36.453  -5.942  1.00 37.21 ? 220 ARG   A CB  1 
ATOM   1687 C CG  . ARG   A 1 223 ? -19.461 35.348  -6.397  1.00 44.71 ? 220 ARG   A CG  1 
ATOM   1688 C CD  . ARG   A 1 223 ? -20.783 35.882  -6.973  1.00 44.08 ? 220 ARG   A CD  1 
ATOM   1689 N NE  . ARG   A 1 223 ? -21.432 36.863  -6.107  1.00 50.53 ? 220 ARG   A NE  1 
ATOM   1690 C CZ  . ARG   A 1 223 ? -22.348 36.576  -5.188  1.00 52.38 ? 220 ARG   A CZ  1 
ATOM   1691 N NH1 . ARG   A 1 223 ? -22.725 35.327  -4.946  1.00 48.18 ? 220 ARG   A NH1 1 
ATOM   1692 N NH2 . ARG   A 1 223 ? -22.899 37.566  -4.490  1.00 53.07 ? 220 ARG   A NH2 1 
ATOM   1693 N N   . GLU   A 1 224 ? -15.701 37.806  -5.982  1.00 37.00 ? 221 GLU   A N   1 
ATOM   1694 C CA  . GLU   A 1 224 ? -14.616 38.451  -6.718  1.00 37.50 ? 221 GLU   A CA  1 
ATOM   1695 C C   . GLU   A 1 224 ? -13.258 37.860  -6.358  1.00 31.22 ? 221 GLU   A C   1 
ATOM   1696 O O   . GLU   A 1 224 ? -12.431 37.609  -7.237  1.00 33.15 ? 221 GLU   A O   1 
ATOM   1697 C CB  . GLU   A 1 224 ? -14.631 39.956  -6.449  1.00 38.24 ? 221 GLU   A CB  1 
ATOM   1698 C CG  . GLU   A 1 224 ? -15.774 40.660  -7.161  1.00 47.70 ? 221 GLU   A CG  1 
ATOM   1699 C CD  . GLU   A 1 224 ? -15.862 40.263  -8.626  1.00 55.78 ? 221 GLU   A CD  1 
ATOM   1700 O OE1 . GLU   A 1 224 ? -16.865 39.613  -9.015  1.00 58.19 ? 221 GLU   A OE1 1 
ATOM   1701 O OE2 . GLU   A 1 224 ? -14.915 40.581  -9.384  1.00 54.22 ? 221 GLU   A OE2 1 
ATOM   1702 N N   . ALA   A 1 225 ? -12.999 37.657  -5.064  1.00 31.58 ? 222 ALA   A N   1 
ATOM   1703 C CA  . ALA   A 1 225 ? -11.751 37.014  -4.657  1.00 31.70 ? 222 ALA   A CA  1 
ATOM   1704 C C   . ALA   A 1 225 ? -11.627 35.625  -5.267  1.00 29.17 ? 222 ALA   A C   1 
ATOM   1705 O O   . ALA   A 1 225 ? -10.552 35.241  -5.747  1.00 28.95 ? 222 ALA   A O   1 
ATOM   1706 C CB  . ALA   A 1 225 ? -11.674 36.932  -3.131  1.00 33.06 ? 222 ALA   A CB  1 
ATOM   1707 N N   . LEU   A 1 226 ? -12.726 34.862  -5.269  1.00 28.90 ? 223 LEU   A N   1 
ATOM   1708 C CA  . LEU   A 1 226 ? -12.697 33.515  -5.834  1.00 30.92 ? 223 LEU   A CA  1 
ATOM   1709 C C   . LEU   A 1 226 ? -12.460 33.557  -7.334  1.00 29.31 ? 223 LEU   A C   1 
ATOM   1710 O O   . LEU   A 1 226 ? -11.652 32.789  -7.866  1.00 29.84 ? 223 LEU   A O   1 
ATOM   1711 C CB  . LEU   A 1 226 ? -13.996 32.777  -5.523  1.00 26.60 ? 223 LEU   A CB  1 
ATOM   1712 C CG  . LEU   A 1 226 ? -14.025 32.192  -4.123  1.00 32.53 ? 223 LEU   A CG  1 
ATOM   1713 C CD1 . LEU   A 1 226 ? -15.419 31.695  -3.757  1.00 31.56 ? 223 LEU   A CD1 1 
ATOM   1714 C CD2 . LEU   A 1 226 ? -12.996 31.065  -4.071  1.00 30.38 ? 223 LEU   A CD2 1 
ATOM   1715 N N   . ARG   A 1 227 ? -13.170 34.442  -8.042  1.00 28.49 ? 224 ARG   A N   1 
ATOM   1716 C CA  . ARG   A 1 227 ? -12.952 34.572  -9.480  1.00 30.56 ? 224 ARG   A CA  1 
ATOM   1717 C C   . ARG   A 1 227 ? -11.493 34.847  -9.792  1.00 30.89 ? 224 ARG   A C   1 
ATOM   1718 O O   . ARG   A 1 227 ? -10.953 34.337  -10.780 1.00 31.01 ? 224 ARG   A O   1 
ATOM   1719 C CB  . ARG   A 1 227 ? -13.818 35.688  -10.061 1.00 33.29 ? 224 ARG   A CB  1 
ATOM   1720 C CG  . ARG   A 1 227 ? -15.267 35.316  -10.290 1.00 42.30 ? 224 ARG   A CG  1 
ATOM   1721 C CD  . ARG   A 1 227 ? -15.965 36.436  -11.056 1.00 46.35 ? 224 ARG   A CD  1 
ATOM   1722 N NE  . ARG   A 1 227 ? -17.247 36.776  -10.456 1.00 52.64 ? 224 ARG   A NE  1 
ATOM   1723 C CZ  . ARG   A 1 227 ? -18.317 35.991  -10.495 1.00 54.32 ? 224 ARG   A CZ  1 
ATOM   1724 N NH1 . ARG   A 1 227 ? -18.268 34.781  -11.037 1.00 58.02 ? 224 ARG   A NH1 1 
ATOM   1725 N NH2 . ARG   A 1 227 ? -19.462 36.426  -9.973  1.00 56.27 ? 224 ARG   A NH2 1 
ATOM   1726 N N   . GLU   A 1 228 ? -10.837 35.677  -8.977  1.00 28.37 ? 225 GLU   A N   1 
ATOM   1727 C CA  . GLU   A 1 228 ? -9.428  35.941  -9.250  1.00 29.92 ? 225 GLU   A CA  1 
ATOM   1728 C C   . GLU   A 1 228 ? -8.578  34.706  -8.974  1.00 29.26 ? 225 GLU   A C   1 
ATOM   1729 O O   . GLU   A 1 228 ? -7.715  34.349  -9.786  1.00 29.96 ? 225 GLU   A O   1 
ATOM   1730 C CB  . GLU   A 1 228 ? -8.948  37.128  -8.428  1.00 33.85 ? 225 GLU   A CB  1 
ATOM   1731 C CG  . GLU   A 1 228 ? -7.459  37.346  -8.525  1.00 45.35 ? 225 GLU   A CG  1 
ATOM   1732 C CD  . GLU   A 1 228 ? -6.980  38.457  -7.619  1.00 56.04 ? 225 GLU   A CD  1 
ATOM   1733 O OE1 . GLU   A 1 228 ? -5.747  38.636  -7.500  1.00 65.42 ? 225 GLU   A OE1 1 
ATOM   1734 O OE2 . GLU   A 1 228 ? -7.840  39.149  -7.026  1.00 61.66 ? 225 GLU   A OE2 1 
ATOM   1735 N N   . ALA   A 1 229 ? -8.844  34.009  -7.860  1.00 27.09 ? 226 ALA   A N   1 
ATOM   1736 C CA  . ALA   A 1 229 ? -8.013  32.879  -7.449  1.00 27.98 ? 226 ALA   A CA  1 
ATOM   1737 C C   . ALA   A 1 229 ? -8.330  31.601  -8.215  1.00 29.86 ? 226 ALA   A C   1 
ATOM   1738 O O   . ALA   A 1 229 ? -7.453  30.732  -8.344  1.00 28.75 ? 226 ALA   A O   1 
ATOM   1739 C CB  . ALA   A 1 229 ? -8.167  32.629  -5.948  1.00 28.41 ? 226 ALA   A CB  1 
ATOM   1740 N N   . ALA   A 1 230 ? -9.558  31.475  -8.731  1.00 29.10 ? 227 ALA   A N   1 
ATOM   1741 C CA  . ALA   A 1 230 ? -10.016 30.289  -9.463  1.00 26.06 ? 227 ALA   A CA  1 
ATOM   1742 C C   . ALA   A 1 230 ? -10.621 30.707  -10.800 1.00 29.69 ? 227 ALA   A C   1 
ATOM   1743 O O   . ALA   A 1 230 ? -11.814 30.506  -11.055 1.00 28.16 ? 227 ALA   A O   1 
ATOM   1744 C CB  . ALA   A 1 230 ? -11.030 29.503  -8.634  1.00 27.63 ? 227 ALA   A CB  1 
ATOM   1745 N N   . PRO   A 1 231 ? -9.791  31.279  -11.676 1.00 32.23 ? 228 PRO   A N   1 
ATOM   1746 C CA  . PRO   A 1 231 ? -10.356 31.793  -12.923 1.00 32.79 ? 228 PRO   A CA  1 
ATOM   1747 C C   . PRO   A 1 231 ? -11.073 30.762  -13.811 1.00 34.04 ? 228 PRO   A C   1 
ATOM   1748 O O   . PRO   A 1 231 ? -11.951 31.144  -14.560 1.00 31.87 ? 228 PRO   A O   1 
ATOM   1749 C CB  . PRO   A 1 231 ? -9.123  32.326  -13.640 1.00 34.84 ? 228 PRO   A CB  1 
ATOM   1750 C CG  . PRO   A 1 231 ? -7.986  31.560  -13.091 1.00 34.39 ? 228 PRO   A CG  1 
ATOM   1751 C CD  . PRO   A 1 231 ? -8.325  31.456  -11.651 1.00 33.56 ? 228 PRO   A CD  1 
ATOM   1752 N N   . ASP   A 1 232 ? -10.715 29.503  -13.704 1.00 29.87 ? 229 ASP   A N   1 
ATOM   1753 C CA  . ASP   A 1 232 ? -11.350 28.469  -14.500 1.00 32.56 ? 229 ASP   A CA  1 
ATOM   1754 C C   . ASP   A 1 232 ? -12.487 27.719  -13.774 1.00 30.42 ? 229 ASP   A C   1 
ATOM   1755 O O   . ASP   A 1 232 ? -12.934 26.677  -14.207 1.00 27.85 ? 229 ASP   A O   1 
ATOM   1756 C CB  . ASP   A 1 232 ? -10.286 27.512  -14.986 1.00 35.99 ? 229 ASP   A CB  1 
ATOM   1757 C CG  . ASP   A 1 232 ? -9.130  28.223  -15.671 1.00 42.71 ? 229 ASP   A CG  1 
ATOM   1758 O OD1 . ASP   A 1 232 ? -9.358  28.830  -16.726 1.00 38.12 ? 229 ASP   A OD1 1 
ATOM   1759 O OD2 . ASP   A 1 232 ? -7.994  28.179  -15.156 1.00 44.28 ? 229 ASP   A OD2 1 
ATOM   1760 N N   . GLY   A 1 233 ? -12.971 28.290  -12.693 1.00 27.38 ? 230 GLY   A N   1 
ATOM   1761 C CA  . GLY   A 1 233 ? -14.027 27.650  -11.961 1.00 25.11 ? 230 GLY   A CA  1 
ATOM   1762 C C   . GLY   A 1 233 ? -13.605 26.707  -10.865 1.00 23.46 ? 230 GLY   A C   1 
ATOM   1763 O O   . GLY   A 1 233 ? -12.437 26.440  -10.691 1.00 22.64 ? 230 GLY   A O   1 
ATOM   1764 N N   . VAL   A 1 234 ? -14.575 26.189  -10.157 1.00 20.54 ? 231 VAL   A N   1 
ATOM   1765 C CA  . VAL   A 1 234 ? -14.303 25.329  -9.009  1.00 20.89 ? 231 VAL   A CA  1 
ATOM   1766 C C   . VAL   A 1 234 ? -14.725 23.899  -9.331  1.00 19.01 ? 231 VAL   A C   1 
ATOM   1767 O O   . VAL   A 1 234 ? -15.895 23.644  -9.640  1.00 19.73 ? 231 VAL   A O   1 
ATOM   1768 C CB  . VAL   A 1 234 ? -15.031 25.841  -7.760  1.00 18.69 ? 231 VAL   A CB  1 
ATOM   1769 C CG1 . VAL   A 1 234 ? -14.830 24.857  -6.612  1.00 20.07 ? 231 VAL   A CG1 1 
ATOM   1770 C CG2 . VAL   A 1 234 ? -14.505 27.251  -7.402  1.00 20.73 ? 231 VAL   A CG2 1 
ATOM   1771 N N   . ASP   A 1 235 ? -13.778 22.952  -9.237  1.00 21.51 ? 232 ASP   A N   1 
ATOM   1772 C CA  . ASP   A 1 235 ? -14.119 21.548  -9.470  1.00 19.93 ? 232 ASP   A CA  1 
ATOM   1773 C C   . ASP   A 1 235 ? -14.491 20.812  -8.186  1.00 19.27 ? 232 ASP   A C   1 
ATOM   1774 O O   . ASP   A 1 235 ? -15.424 19.999  -8.193  1.00 18.12 ? 232 ASP   A O   1 
ATOM   1775 C CB  . ASP   A 1 235 ? -12.960 20.833  -10.156 1.00 18.41 ? 232 ASP   A CB  1 
ATOM   1776 C CG  . ASP   A 1 235 ? -12.610 21.474  -11.473 1.00 23.63 ? 232 ASP   A CG  1 
ATOM   1777 O OD1 . ASP   A 1 235 ? -13.477 21.457  -12.389 1.00 22.72 ? 232 ASP   A OD1 1 
ATOM   1778 O OD2 . ASP   A 1 235 ? -11.517 22.069  -11.558 1.00 23.80 ? 232 ASP   A OD2 1 
ATOM   1779 N N   . LYS   A 1 236 ? -13.749 21.029  -7.098  1.00 15.83 ? 233 LYS   A N   1 
ATOM   1780 C CA  . LYS   A 1 236 ? -14.064 20.407  -5.816  1.00 20.05 ? 233 LYS   A CA  1 
ATOM   1781 C C   . LYS   A 1 236 ? -14.073 21.469  -4.735  1.00 19.65 ? 233 LYS   A C   1 
ATOM   1782 O O   . LYS   A 1 236 ? -13.297 22.425  -4.775  1.00 19.43 ? 233 LYS   A O   1 
ATOM   1783 C CB  . LYS   A 1 236 ? -13.063 19.315  -5.393  1.00 17.43 ? 233 LYS   A CB  1 
ATOM   1784 C CG  . LYS   A 1 236 ? -12.452 18.530  -6.534  1.00 26.03 ? 233 LYS   A CG  1 
ATOM   1785 C CD  . LYS   A 1 236 ? -13.374 17.524  -7.112  1.00 21.47 ? 233 LYS   A CD  1 
ATOM   1786 C CE  . LYS   A 1 236 ? -12.667 16.845  -8.260  1.00 27.90 ? 233 LYS   A CE  1 
ATOM   1787 N NZ  . LYS   A 1 236 ? -13.508 15.898  -9.004  1.00 26.60 ? 233 LYS   A NZ  1 
ATOM   1788 N N   . TYR   A 1 237 ? -14.938 21.276  -3.750  1.00 18.81 ? 234 TYR   A N   1 
ATOM   1789 C CA  . TYR   A 1 237 ? -15.030 22.194  -2.631  1.00 17.63 ? 234 TYR   A CA  1 
ATOM   1790 C C   . TYR   A 1 237 ? -15.123 21.373  -1.353  1.00 21.89 ? 234 TYR   A C   1 
ATOM   1791 O O   . TYR   A 1 237 ? -16.054 20.577  -1.199  1.00 20.87 ? 234 TYR   A O   1 
ATOM   1792 C CB  . TYR   A 1 237 ? -16.249 23.109  -2.793  1.00 17.39 ? 234 TYR   A CB  1 
ATOM   1793 C CG  . TYR   A 1 237 ? -16.468 24.137  -1.696  1.00 18.68 ? 234 TYR   A CG  1 
ATOM   1794 C CD1 . TYR   A 1 237 ? -15.401 24.708  -1.013  1.00 17.47 ? 234 TYR   A CD1 1 
ATOM   1795 C CD2 . TYR   A 1 237 ? -17.755 24.545  -1.360  1.00 19.89 ? 234 TYR   A CD2 1 
ATOM   1796 C CE1 . TYR   A 1 237 ? -15.623 25.668  -0.016  1.00 19.61 ? 234 TYR   A CE1 1 
ATOM   1797 C CE2 . TYR   A 1 237 ? -17.986 25.498  -0.363  1.00 21.05 ? 234 TYR   A CE2 1 
ATOM   1798 C CZ  . TYR   A 1 237 ? -16.919 26.059  0.300   1.00 21.42 ? 234 TYR   A CZ  1 
ATOM   1799 O OH  . TYR   A 1 237 ? -17.152 27.002  1.278   1.00 21.98 ? 234 TYR   A OH  1 
ATOM   1800 N N   . PHE   A 1 238 ? -14.150 21.545  -0.452  1.00 19.69 ? 235 PHE   A N   1 
ATOM   1801 C CA  . PHE   A 1 238 ? -14.212 20.966  0.882   1.00 18.10 ? 235 PHE   A CA  1 
ATOM   1802 C C   . PHE   A 1 238 ? -14.630 22.095  1.822   1.00 20.13 ? 235 PHE   A C   1 
ATOM   1803 O O   . PHE   A 1 238 ? -13.866 23.045  2.034   1.00 17.82 ? 235 PHE   A O   1 
ATOM   1804 C CB  . PHE   A 1 238 ? -12.878 20.350  1.306   1.00 16.42 ? 235 PHE   A CB  1 
ATOM   1805 C CG  . PHE   A 1 238 ? -12.975 19.553  2.588   1.00 19.42 ? 235 PHE   A CG  1 
ATOM   1806 C CD1 . PHE   A 1 238 ? -12.830 20.179  3.826   1.00 18.97 ? 235 PHE   A CD1 1 
ATOM   1807 C CD2 . PHE   A 1 238 ? -13.247 18.191  2.553   1.00 17.30 ? 235 PHE   A CD2 1 
ATOM   1808 C CE1 . PHE   A 1 238 ? -12.947 19.445  5.031   1.00 17.13 ? 235 PHE   A CE1 1 
ATOM   1809 C CE2 . PHE   A 1 238 ? -13.354 17.453  3.740   1.00 21.48 ? 235 PHE   A CE2 1 
ATOM   1810 C CZ  . PHE   A 1 238 ? -13.209 18.086  4.981   1.00 17.21 ? 235 PHE   A CZ  1 
ATOM   1811 N N   . ASP   A 1 239 ? -15.849 22.004  2.368   1.00 18.46 ? 236 ASP   A N   1 
ATOM   1812 C CA  . ASP   A 1 239 ? -16.493 23.128  3.053   1.00 19.30 ? 236 ASP   A CA  1 
ATOM   1813 C C   . ASP   A 1 239 ? -16.604 22.844  4.553   1.00 19.29 ? 236 ASP   A C   1 
ATOM   1814 O O   . ASP   A 1 239 ? -17.260 21.880  4.960   1.00 20.10 ? 236 ASP   A O   1 
ATOM   1815 C CB  . ASP   A 1 239 ? -17.875 23.387  2.437   1.00 17.83 ? 236 ASP   A CB  1 
ATOM   1816 C CG  . ASP   A 1 239 ? -18.566 24.636  2.999   1.00 21.65 ? 236 ASP   A CG  1 
ATOM   1817 O OD1 . ASP   A 1 239 ? -17.934 25.421  3.748   1.00 20.90 ? 236 ASP   A OD1 1 
ATOM   1818 O OD2 . ASP   A 1 239 ? -19.779 24.824  2.689   1.00 23.75 ? 236 ASP   A OD2 1 
ATOM   1819 N N   . SER   A 1 240 ? -15.976 23.686  5.366   1.00 20.29 ? 237 SER   A N   1 
ATOM   1820 C CA  . SER   A 1 240 ? -16.193 23.686  6.809   1.00 21.98 ? 237 SER   A CA  1 
ATOM   1821 C C   . SER   A 1 240 ? -16.843 24.974  7.305   1.00 23.80 ? 237 SER   A C   1 
ATOM   1822 O O   . SER   A 1 240 ? -17.018 25.136  8.519   1.00 26.11 ? 237 SER   A O   1 
ATOM   1823 C CB  . SER   A 1 240 ? -14.863 23.468  7.562   1.00 21.45 ? 237 SER   A CB  1 
ATOM   1824 O OG  . SER   A 1 240 ? -14.264 22.198  7.260   1.00 22.77 ? 237 SER   A OG  1 
ATOM   1825 N N   . ILE   A 1 241 ? -17.204 25.899  6.420   1.00 22.47 ? 238 ILE   A N   1 
ATOM   1826 C CA  . ILE   A 1 241 ? -17.630 27.237  6.813   1.00 23.36 ? 238 ILE   A CA  1 
ATOM   1827 C C   . ILE   A 1 241 ? -19.093 27.493  6.463   1.00 23.91 ? 238 ILE   A C   1 
ATOM   1828 O O   . ILE   A 1 241 ? -19.852 28.005  7.287   1.00 24.08 ? 238 ILE   A O   1 
ATOM   1829 C CB  . ILE   A 1 241 ? -16.719 28.312  6.182   1.00 24.68 ? 238 ILE   A CB  1 
ATOM   1830 C CG1 . ILE   A 1 241 ? -15.266 28.069  6.548   1.00 27.99 ? 238 ILE   A CG1 1 
ATOM   1831 C CG2 . ILE   A 1 241 ? -17.184 29.705  6.620   1.00 21.90 ? 238 ILE   A CG2 1 
ATOM   1832 C CD1 . ILE   A 1 241 ? -14.975 28.196  8.053   1.00 31.68 ? 238 ILE   A CD1 1 
ATOM   1833 N N   . GLY   A 1 242 ? -19.495 27.196  5.237   1.00 22.45 ? 239 GLY   A N   1 
ATOM   1834 C CA  . GLY   A 1 242 ? -20.863 27.572  4.895   1.00 22.42 ? 239 GLY   A CA  1 
ATOM   1835 C C   . GLY   A 1 242 ? -20.969 29.083  4.682   1.00 23.12 ? 239 GLY   A C   1 
ATOM   1836 O O   . GLY   A 1 242 ? -19.983 29.779  4.403   1.00 24.58 ? 239 GLY   A O   1 
ATOM   1837 N N   . GLY   A 1 243 ? -22.182 29.606  4.818   1.00 24.96 ? 240 GLY   A N   1 
ATOM   1838 C CA  . GLY   A 1 243 ? -22.278 31.054  4.744   1.00 26.03 ? 240 GLY   A CA  1 
ATOM   1839 C C   . GLY   A 1 243 ? -21.947 31.611  3.365   1.00 27.89 ? 240 GLY   A C   1 
ATOM   1840 O O   . GLY   A 1 243 ? -22.118 30.947  2.326   1.00 25.38 ? 240 GLY   A O   1 
ATOM   1841 N N   . SER   A 1 244 ? -21.455 32.856  3.351   1.00 26.65 ? 241 SER   A N   1 
ATOM   1842 C CA  . SER   A 1 244 ? -21.296 33.576  2.093   1.00 30.56 ? 241 SER   A CA  1 
ATOM   1843 C C   . SER   A 1 244 ? -20.123 33.037  1.276   1.00 27.80 ? 241 SER   A C   1 
ATOM   1844 O O   . SER   A 1 244 ? -20.166 33.089  0.041   1.00 28.47 ? 241 SER   A O   1 
ATOM   1845 C CB  . SER   A 1 244 ? -21.148 35.081  2.346   1.00 33.07 ? 241 SER   A CB  1 
ATOM   1846 O OG  . SER   A 1 244 ? -19.964 35.383  3.055   1.00 38.62 ? 241 SER   A OG  1 
ATOM   1847 N N   . VAL   A 1 245 ? -19.093 32.482  1.925   1.00 25.34 ? 242 VAL   A N   1 
ATOM   1848 C CA  . VAL   A 1 245 ? -18.034 31.831  1.158   1.00 23.29 ? 242 VAL   A CA  1 
ATOM   1849 C C   . VAL   A 1 245 ? -18.612 30.696  0.324   1.00 26.76 ? 242 VAL   A C   1 
ATOM   1850 O O   . VAL   A 1 245 ? -18.288 30.541  -0.862  1.00 25.27 ? 242 VAL   A O   1 
ATOM   1851 C CB  . VAL   A 1 245 ? -16.895 31.343  2.075   1.00 25.83 ? 242 VAL   A CB  1 
ATOM   1852 C CG1 . VAL   A 1 245 ? -17.366 30.242  3.000   1.00 28.73 ? 242 VAL   A CG1 1 
ATOM   1853 C CG2 . VAL   A 1 245 ? -15.731 30.832  1.233   1.00 25.62 ? 242 VAL   A CG2 1 
ATOM   1854 N N   . THR   A 1 246 ? -19.506 29.905  0.918   1.00 23.75 ? 243 THR   A N   1 
ATOM   1855 C CA  . THR   A 1 246 ? -20.084 28.777  0.196   1.00 21.81 ? 243 THR   A CA  1 
ATOM   1856 C C   . THR   A 1 246 ? -21.075 29.256  -0.866  1.00 25.67 ? 243 THR   A C   1 
ATOM   1857 O O   . THR   A 1 246 ? -21.092 28.732  -1.986  1.00 23.57 ? 243 THR   A O   1 
ATOM   1858 C CB  . THR   A 1 246 ? -20.729 27.813  1.200   1.00 23.37 ? 243 THR   A CB  1 
ATOM   1859 O OG1 . THR   A 1 246 ? -19.686 27.197  1.985   1.00 21.62 ? 243 THR   A OG1 1 
ATOM   1860 C CG2 . THR   A 1 246 ? -21.576 26.749  0.504   1.00 21.18 ? 243 THR   A CG2 1 
ATOM   1861 N N   . ASP   A 1 247 ? -21.880 30.278  -0.546  1.00 24.02 ? 244 ASP   A N   1 
ATOM   1862 C CA  . ASP   A 1 247 ? -22.707 30.933  -1.561  1.00 25.51 ? 244 ASP   A CA  1 
ATOM   1863 C C   . ASP   A 1 247 ? -21.881 31.323  -2.785  1.00 22.54 ? 244 ASP   A C   1 
ATOM   1864 O O   . ASP   A 1 247 ? -22.301 31.108  -3.926  1.00 21.64 ? 244 ASP   A O   1 
ATOM   1865 C CB  . ASP   A 1 247 ? -23.387 32.173  -0.972  1.00 25.73 ? 244 ASP   A CB  1 
ATOM   1866 C CG  . ASP   A 1 247 ? -24.393 31.835  0.130   1.00 26.19 ? 244 ASP   A CG  1 
ATOM   1867 O OD1 . ASP   A 1 247 ? -24.891 30.691  0.176   1.00 29.12 ? 244 ASP   A OD1 1 
ATOM   1868 O OD2 . ASP   A 1 247 ? -24.699 32.729  0.949   1.00 28.73 ? 244 ASP   A OD2 1 
ATOM   1869 N N   . ALA   A 1 248 ? -20.706 31.916  -2.558  1.00 21.85 ? 245 ALA   A N   1 
ATOM   1870 C CA  . ALA   A 1 248 ? -19.848 32.343  -3.662  1.00 26.00 ? 245 ALA   A CA  1 
ATOM   1871 C C   . ALA   A 1 248 ? -19.357 31.156  -4.477  1.00 24.57 ? 245 ALA   A C   1 
ATOM   1872 O O   . ALA   A 1 248 ? -19.360 31.200  -5.710  1.00 23.96 ? 245 ALA   A O   1 
ATOM   1873 C CB  . ALA   A 1 248 ? -18.661 33.143  -3.130  1.00 26.30 ? 245 ALA   A CB  1 
ATOM   1874 N N   . VAL   A 1 249 ? -18.913 30.086  -3.813  1.00 24.55 ? 246 VAL   A N   1 
ATOM   1875 C CA  . VAL   A 1 249 ? -18.405 28.937  -4.560  1.00 21.32 ? 246 VAL   A CA  1 
ATOM   1876 C C   . VAL   A 1 249 ? -19.496 28.358  -5.447  1.00 21.98 ? 246 VAL   A C   1 
ATOM   1877 O O   . VAL   A 1 249 ? -19.245 27.977  -6.595  1.00 19.94 ? 246 VAL   A O   1 
ATOM   1878 C CB  . VAL   A 1 249 ? -17.837 27.870  -3.605  1.00 25.14 ? 246 VAL   A CB  1 
ATOM   1879 C CG1 . VAL   A 1 249 ? -17.464 26.615  -4.401  1.00 19.36 ? 246 VAL   A CG1 1 
ATOM   1880 C CG2 . VAL   A 1 249 ? -16.629 28.407  -2.873  1.00 20.42 ? 246 VAL   A CG2 1 
ATOM   1881 N N   . PHE   A 1 250 ? -20.726 28.286  -4.936  1.00 20.95 ? 247 PHE   A N   1 
ATOM   1882 C CA  . PHE   A 1 250 ? -21.792 27.650  -5.687  1.00 22.70 ? 247 PHE   A CA  1 
ATOM   1883 C C   . PHE   A 1 250 ? -22.172 28.422  -6.941  1.00 23.73 ? 247 PHE   A C   1 
ATOM   1884 O O   . PHE   A 1 250 ? -22.842 27.856  -7.811  1.00 24.39 ? 247 PHE   A O   1 
ATOM   1885 C CB  . PHE   A 1 250 ? -23.032 27.453  -4.804  1.00 22.33 ? 247 PHE   A CB  1 
ATOM   1886 C CG  . PHE   A 1 250 ? -23.063 26.120  -4.121  1.00 22.05 ? 247 PHE   A CG  1 
ATOM   1887 C CD1 . PHE   A 1 250 ? -22.066 25.771  -3.222  1.00 22.98 ? 247 PHE   A CD1 1 
ATOM   1888 C CD2 . PHE   A 1 250 ? -24.066 25.201  -4.397  1.00 20.97 ? 247 PHE   A CD2 1 
ATOM   1889 C CE1 . PHE   A 1 250 ? -22.076 24.523  -2.600  1.00 23.96 ? 247 PHE   A CE1 1 
ATOM   1890 C CE2 . PHE   A 1 250 ? -24.080 23.957  -3.781  1.00 24.82 ? 247 PHE   A CE2 1 
ATOM   1891 C CZ  . PHE   A 1 250 ? -23.091 23.620  -2.880  1.00 19.81 ? 247 PHE   A CZ  1 
ATOM   1892 N N   . SER   A 1 251 ? -21.745 29.674  -7.070  1.00 23.45 ? 248 SER   A N   1 
ATOM   1893 C CA  . SER   A 1 251 ? -21.990 30.430  -8.289  1.00 26.95 ? 248 SER   A CA  1 
ATOM   1894 C C   . SER   A 1 251 ? -20.988 30.114  -9.384  1.00 27.41 ? 248 SER   A C   1 
ATOM   1895 O O   . SER   A 1 251 ? -21.099 30.673  -10.483 1.00 27.99 ? 248 SER   A O   1 
ATOM   1896 C CB  . SER   A 1 251 ? -21.957 31.933  -8.003  1.00 24.34 ? 248 SER   A CB  1 
ATOM   1897 O OG  . SER   A 1 251 ? -20.631 32.369  -7.720  1.00 27.17 ? 248 SER   A OG  1 
ATOM   1898 N N   . MET   A 1 252 ? -20.003 29.246  -9.119  1.00 23.80 ? 249 MET   A N   1 
ATOM   1899 C CA  . MET   A 1 252 ? -18.936 29.021  -10.088 1.00 25.94 ? 249 MET   A CA  1 
ATOM   1900 C C   . MET   A 1 252 ? -18.505 27.561  -10.109 1.00 22.90 ? 249 MET   A C   1 
ATOM   1901 O O   . MET   A 1 252 ? -17.324 27.260  -10.342 1.00 21.52 ? 249 MET   A O   1 
ATOM   1902 C CB  . MET   A 1 252 ? -17.741 29.933  -9.792  1.00 23.15 ? 249 MET   A CB  1 
ATOM   1903 C CG  . MET   A 1 252 ? -17.231 29.833  -8.352  1.00 26.71 ? 249 MET   A CG  1 
ATOM   1904 S SD  . MET   A 1 252 ? -15.830 30.947  -8.004  1.00 29.54 ? 249 MET   A SD  1 
ATOM   1905 C CE  . MET   A 1 252 ? -16.666 32.525  -8.039  1.00 28.61 ? 249 MET   A CE  1 
ATOM   1906 N N   . LEU   A 1 253 ? -19.448 26.652  -9.847  1.00 18.61 ? 250 LEU   A N   1 
ATOM   1907 C CA  . LEU   A 1 253 ? -19.168 25.227  -9.890  1.00 19.65 ? 250 LEU   A CA  1 
ATOM   1908 C C   . LEU   A 1 253 ? -19.055 24.761  -11.338 1.00 24.07 ? 250 LEU   A C   1 
ATOM   1909 O O   . LEU   A 1 253 ? -19.882 25.112  -12.184 1.00 18.78 ? 250 LEU   A O   1 
ATOM   1910 C CB  . LEU   A 1 253 ? -20.269 24.449  -9.158  1.00 18.53 ? 250 LEU   A CB  1 
ATOM   1911 C CG  . LEU   A 1 253 ? -20.320 24.585  -7.625  1.00 22.43 ? 250 LEU   A CG  1 
ATOM   1912 C CD1 . LEU   A 1 253 ? -21.656 24.093  -7.101  1.00 25.00 ? 250 LEU   A CD1 1 
ATOM   1913 C CD2 . LEU   A 1 253 ? -19.188 23.806  -6.952  1.00 23.19 ? 250 LEU   A CD2 1 
ATOM   1914 N N   . ASN   A 1 254 ? -18.024 23.971  -11.616 1.00 20.72 ? 251 ASN   A N   1 
ATOM   1915 C CA  . ASN   A 1 254 ? -17.820 23.401  -12.933 1.00 22.01 ? 251 ASN   A CA  1 
ATOM   1916 C C   . ASN   A 1 254 ? -18.640 22.127  -13.099 1.00 22.02 ? 251 ASN   A C   1 
ATOM   1917 O O   . ASN   A 1 254 ? -19.120 21.535  -12.136 1.00 20.14 ? 251 ASN   A O   1 
ATOM   1918 C CB  . ASN   A 1 254 ? -16.325 23.105  -13.159 1.00 20.80 ? 251 ASN   A CB  1 
ATOM   1919 C CG  . ASN   A 1 254 ? -15.517 24.368  -13.409 1.00 25.73 ? 251 ASN   A CG  1 
ATOM   1920 O OD1 . ASN   A 1 254 ? -16.085 25.415  -13.688 1.00 22.96 ? 251 ASN   A OD1 1 
ATOM   1921 N ND2 . ASN   A 1 254 ? -14.195 24.269  -13.331 1.00 24.03 ? 251 ASN   A ND2 1 
ATOM   1922 N N   . VAL   A 1 255 ? -18.776 21.699  -14.355 1.00 22.45 ? 252 VAL   A N   1 
ATOM   1923 C CA  . VAL   A 1 255 ? -19.492 20.469  -14.663 1.00 23.29 ? 252 VAL   A CA  1 
ATOM   1924 C C   . VAL   A 1 255 ? -18.819 19.286  -13.981 1.00 24.36 ? 252 VAL   A C   1 
ATOM   1925 O O   . VAL   A 1 255 ? -17.595 19.131  -14.037 1.00 22.89 ? 252 VAL   A O   1 
ATOM   1926 C CB  . VAL   A 1 255 ? -19.553 20.275  -16.183 1.00 22.26 ? 252 VAL   A CB  1 
ATOM   1927 C CG1 . VAL   A 1 255 ? -20.154 18.917  -16.526 1.00 21.02 ? 252 VAL   A CG1 1 
ATOM   1928 C CG2 . VAL   A 1 255 ? -20.343 21.425  -16.810 1.00 20.16 ? 252 VAL   A CG2 1 
ATOM   1929 N N   . GLY   A 1 256 ? -19.626 18.443  -13.342 1.00 20.04 ? 253 GLY   A N   1 
ATOM   1930 C CA  . GLY   A 1 256 ? -19.115 17.286  -12.644 1.00 24.17 ? 253 GLY   A CA  1 
ATOM   1931 C C   . GLY   A 1 256 ? -18.417 17.598  -11.339 1.00 23.99 ? 253 GLY   A C   1 
ATOM   1932 O O   . GLY   A 1 256 ? -17.653 16.770  -10.849 1.00 21.64 ? 253 GLY   A O   1 
ATOM   1933 N N   . SER   A 1 257 ? -18.684 18.758  -10.740 1.00 20.03 ? 254 SER   A N   1 
ATOM   1934 C CA  . SER   A 1 257 ? -17.971 19.148  -9.529  1.00 20.13 ? 254 SER   A CA  1 
ATOM   1935 C C   . SER   A 1 257 ? -18.460 18.335  -8.329  1.00 23.18 ? 254 SER   A C   1 
ATOM   1936 O O   . SER   A 1 257 ? -19.503 17.672  -8.370  1.00 20.77 ? 254 SER   A O   1 
ATOM   1937 C CB  . SER   A 1 257 ? -18.129 20.648  -9.292  1.00 19.17 ? 254 SER   A CB  1 
ATOM   1938 O OG  . SER   A 1 257 ? -19.487 21.030  -9.481  1.00 22.22 ? 254 SER   A OG  1 
ATOM   1939 N N   . GLN   A 1 258 ? -17.680 18.382  -7.243  1.00 20.02 ? 255 GLN   A N   1 
ATOM   1940 C CA  . GLN   A 1 258 ? -18.037 17.713  -5.993  1.00 24.26 ? 255 GLN   A CA  1 
ATOM   1941 C C   . GLN   A 1 258 ? -17.838 18.642  -4.804  1.00 22.01 ? 255 GLN   A C   1 
ATOM   1942 O O   . GLN   A 1 258 ? -16.812 19.328  -4.708  1.00 21.58 ? 255 GLN   A O   1 
ATOM   1943 C CB  . GLN   A 1 258 ? -17.198 16.455  -5.753  1.00 22.07 ? 255 GLN   A CB  1 
ATOM   1944 C CG  . GLN   A 1 258 ? -17.278 15.396  -6.826  1.00 23.30 ? 255 GLN   A CG  1 
ATOM   1945 C CD  . GLN   A 1 258 ? -16.299 14.261  -6.536  1.00 24.52 ? 255 GLN   A CD  1 
ATOM   1946 O OE1 . GLN   A 1 258 ? -15.091 14.444  -6.621  1.00 21.38 ? 255 GLN   A OE1 1 
ATOM   1947 N NE2 . GLN   A 1 258 ? -16.824 13.104  -6.167  1.00 25.34 ? 255 GLN   A NE2 1 
ATOM   1948 N N   . VAL   A 1 259 ? -18.786 18.598  -3.866  1.00 17.42 ? 256 VAL   A N   1 
ATOM   1949 C CA  . VAL   A 1 259 ? -18.754 19.403  -2.650  1.00 17.98 ? 256 VAL   A CA  1 
ATOM   1950 C C   . VAL   A 1 259 ? -18.873 18.462  -1.457  1.00 21.02 ? 256 VAL   A C   1 
ATOM   1951 O O   . VAL   A 1 259 ? -19.833 17.684  -1.366  1.00 17.76 ? 256 VAL   A O   1 
ATOM   1952 C CB  . VAL   A 1 259 ? -19.880 20.445  -2.623  1.00 18.69 ? 256 VAL   A CB  1 
ATOM   1953 C CG1 . VAL   A 1 259 ? -19.833 21.245  -1.326  1.00 18.25 ? 256 VAL   A CG1 1 
ATOM   1954 C CG2 . VAL   A 1 259 ? -19.826 21.364  -3.863  1.00 20.32 ? 256 VAL   A CG2 1 
ATOM   1955 N N   . ALA   A 1 260 ? -17.899 18.519  -0.554  1.00 18.19 ? 257 ALA   A N   1 
ATOM   1956 C CA  . ALA   A 1 260 ? -17.961 17.785  0.705   1.00 20.08 ? 257 ALA   A CA  1 
ATOM   1957 C C   . ALA   A 1 260 ? -18.282 18.766  1.832   1.00 18.87 ? 257 ALA   A C   1 
ATOM   1958 O O   . ALA   A 1 260 ? -17.593 19.773  1.997   1.00 19.99 ? 257 ALA   A O   1 
ATOM   1959 C CB  . ALA   A 1 260 ? -16.639 17.059  0.978   1.00 20.03 ? 257 ALA   A CB  1 
ATOM   1960 N N   . VAL   A 1 261 ? -19.340 18.490  2.585   1.00 19.28 ? 258 VAL   A N   1 
ATOM   1961 C CA  . VAL   A 1 261 ? -19.777 19.387  3.651   1.00 19.04 ? 258 VAL   A CA  1 
ATOM   1962 C C   . VAL   A 1 261 ? -19.319 18.784  4.969   1.00 22.12 ? 258 VAL   A C   1 
ATOM   1963 O O   . VAL   A 1 261 ? -19.940 17.850  5.486   1.00 19.40 ? 258 VAL   A O   1 
ATOM   1964 C CB  . VAL   A 1 261 ? -21.290 19.618  3.628   1.00 20.28 ? 258 VAL   A CB  1 
ATOM   1965 C CG1 . VAL   A 1 261 ? -21.683 20.561  4.760   1.00 21.06 ? 258 VAL   A CG1 1 
ATOM   1966 C CG2 . VAL   A 1 261 ? -21.710 20.193  2.263   1.00 22.15 ? 258 VAL   A CG2 1 
ATOM   1967 N N   . CYS   A 1 262 ? -18.231 19.341  5.503   1.00 20.08 ? 259 CYS   A N   1 
ATOM   1968 C CA  . CYS   A 1 262 ? -17.601 18.892  6.741   1.00 22.32 ? 259 CYS   A CA  1 
ATOM   1969 C C   . CYS   A 1 262 ? -18.090 19.649  7.967   1.00 25.63 ? 259 CYS   A C   1 
ATOM   1970 O O   . CYS   A 1 262 ? -18.181 19.067  9.058   1.00 22.80 ? 259 CYS   A O   1 
ATOM   1971 C CB  . CYS   A 1 262 ? -16.079 19.043  6.615   1.00 21.97 ? 259 CYS   A CB  1 
ATOM   1972 S SG  . CYS   A 1 262 ? -15.113 18.487  8.034   1.00 25.56 ? 259 CYS   A SG  1 
ATOM   1973 N N   . TRP   A 1 263 ? -18.384 20.936  7.827   1.00 22.04 ? 260 TRP   A N   1 
ATOM   1974 C CA  . TRP   A 1 263 ? -19.010 21.696  8.904   1.00 25.81 ? 260 TRP   A CA  1 
ATOM   1975 C C   . TRP   A 1 263 ? -19.614 22.938  8.273   1.00 24.82 ? 260 TRP   A C   1 
ATOM   1976 O O   . TRP   A 1 263 ? -19.426 23.206  7.082   1.00 23.20 ? 260 TRP   A O   1 
ATOM   1977 C CB  . TRP   A 1 263 ? -18.009 22.072  10.017  1.00 23.24 ? 260 TRP   A CB  1 
ATOM   1978 C CG  . TRP   A 1 263 ? -18.573 21.952  11.436  1.00 27.36 ? 260 TRP   A CG  1 
ATOM   1979 C CD1 . TRP   A 1 263 ? -19.191 20.864  11.983  1.00 27.48 ? 260 TRP   A CD1 1 
ATOM   1980 C CD2 . TRP   A 1 263 ? -18.551 22.960  12.468  1.00 27.19 ? 260 TRP   A CD2 1 
ATOM   1981 N NE1 . TRP   A 1 263 ? -19.558 21.130  13.299  1.00 27.84 ? 260 TRP   A NE1 1 
ATOM   1982 C CE2 . TRP   A 1 263 ? -19.173 22.408  13.614  1.00 28.40 ? 260 TRP   A CE2 1 
ATOM   1983 C CE3 . TRP   A 1 263 ? -18.056 24.272  12.539  1.00 27.49 ? 260 TRP   A CE3 1 
ATOM   1984 C CZ2 . TRP   A 1 263 ? -19.314 23.120  14.809  1.00 27.12 ? 260 TRP   A CZ2 1 
ATOM   1985 C CZ3 . TRP   A 1 263 ? -18.198 24.977  13.738  1.00 25.08 ? 260 TRP   A CZ3 1 
ATOM   1986 C CH2 . TRP   A 1 263 ? -18.829 24.399  14.848  1.00 26.09 ? 260 TRP   A CH2 1 
ATOM   1987 N N   . GLN   A 1 264 ? -20.344 23.698  9.088   1.00 23.80 ? 261 GLN   A N   1 
ATOM   1988 C CA  . GLN   A 1 264 ? -20.972 24.943  8.644   1.00 24.82 ? 261 GLN   A CA  1 
ATOM   1989 C C   . GLN   A 1 264 ? -20.778 25.988  9.749   1.00 24.72 ? 261 GLN   A C   1 
ATOM   1990 O O   . GLN   A 1 264 ? -21.719 26.414  10.414  1.00 25.06 ? 261 GLN   A O   1 
ATOM   1991 C CB  . GLN   A 1 264 ? -22.450 24.728  8.316   1.00 21.72 ? 261 GLN   A CB  1 
ATOM   1992 C CG  . GLN   A 1 264 ? -22.693 23.824  7.118   1.00 22.95 ? 261 GLN   A CG  1 
ATOM   1993 C CD  . GLN   A 1 264 ? -22.394 24.506  5.794   1.00 26.73 ? 261 GLN   A CD  1 
ATOM   1994 O OE1 . GLN   A 1 264 ? -23.251 25.188  5.228   1.00 25.85 ? 261 GLN   A OE1 1 
ATOM   1995 N NE2 . GLN   A 1 264 ? -21.170 24.334  5.298   1.00 21.68 ? 261 GLN   A NE2 1 
ATOM   1996 N N   . TRP   A 1 265 ? -19.523 26.394  9.942   1.00 22.34 ? 262 TRP   A N   1 
ATOM   1997 C CA  . TRP   A 1 265 ? -19.181 27.381  10.967  1.00 26.38 ? 262 TRP   A CA  1 
ATOM   1998 C C   . TRP   A 1 265 ? -20.098 28.599  10.931  1.00 29.12 ? 262 TRP   A C   1 
ATOM   1999 O O   . TRP   A 1 265 ? -20.529 29.096  11.984  1.00 26.46 ? 262 TRP   A O   1 
ATOM   2000 C CB  . TRP   A 1 265 ? -17.735 27.833  10.776  1.00 24.61 ? 262 TRP   A CB  1 
ATOM   2001 C CG  . TRP   A 1 265 ? -17.221 28.768  11.830  1.00 28.97 ? 262 TRP   A CG  1 
ATOM   2002 C CD1 . TRP   A 1 265 ? -17.651 30.046  12.098  1.00 30.29 ? 262 TRP   A CD1 1 
ATOM   2003 C CD2 . TRP   A 1 265 ? -16.151 28.506  12.743  1.00 30.60 ? 262 TRP   A CD2 1 
ATOM   2004 N NE1 . TRP   A 1 265 ? -16.917 30.582  13.142  1.00 30.17 ? 262 TRP   A NE1 1 
ATOM   2005 C CE2 . TRP   A 1 265 ? -15.997 29.654  13.556  1.00 31.99 ? 262 TRP   A CE2 1 
ATOM   2006 C CE3 . TRP   A 1 265 ? -15.326 27.403  12.970  1.00 32.44 ? 262 TRP   A CE3 1 
ATOM   2007 C CZ2 . TRP   A 1 265 ? -15.037 29.731  14.557  1.00 33.86 ? 262 TRP   A CZ2 1 
ATOM   2008 C CZ3 . TRP   A 1 265 ? -14.374 27.480  13.971  1.00 34.88 ? 262 TRP   A CZ3 1 
ATOM   2009 C CH2 . TRP   A 1 265 ? -14.232 28.636  14.747  1.00 35.22 ? 262 TRP   A CH2 1 
ATOM   2010 N N   . ALA   A 1 266 ? -20.359 29.133  9.734   1.00 24.14 ? 263 ALA   A N   1 
ATOM   2011 C CA  . ALA   A 1 266 ? -21.117 30.382  9.637   1.00 27.45 ? 263 ALA   A CA  1 
ATOM   2012 C C   . ALA   A 1 266 ? -22.528 30.225  10.176  1.00 27.31 ? 263 ALA   A C   1 
ATOM   2013 O O   . ALA   A 1 266 ? -23.106 31.190  10.682  1.00 29.45 ? 263 ALA   A O   1 
ATOM   2014 C CB  . ALA   A 1 266 ? -21.163 30.870  8.183   1.00 25.42 ? 263 ALA   A CB  1 
ATOM   2015 N N   . THR   A 1 267 ? -23.106 29.032  10.056  1.00 25.43 ? 264 THR   A N   1 
ATOM   2016 C CA  . THR   A 1 267 ? -24.418 28.773  10.634  1.00 27.86 ? 264 THR   A CA  1 
ATOM   2017 C C   . THR   A 1 267 ? -24.316 28.363  12.105  1.00 32.93 ? 264 THR   A C   1 
ATOM   2018 O O   . THR   A 1 267 ? -24.984 28.950  12.958  1.00 31.89 ? 264 THR   A O   1 
ATOM   2019 C CB  . THR   A 1 267 ? -25.151 27.681  9.845   1.00 27.75 ? 264 THR   A CB  1 
ATOM   2020 O OG1 . THR   A 1 267 ? -25.350 28.116  8.495   1.00 27.77 ? 264 THR   A OG1 1 
ATOM   2021 C CG2 . THR   A 1 267 ? -26.516 27.372  10.488  1.00 27.07 ? 264 THR   A CG2 1 
ATOM   2022 N N   . GLN   A 1 268 ? -23.482 27.362  12.421  1.00 28.64 ? 265 GLN   A N   1 
ATOM   2023 C CA  . GLN   A 1 268 ? -23.458 26.843  13.790  1.00 29.39 ? 265 GLN   A CA  1 
ATOM   2024 C C   . GLN   A 1 268 ? -22.950 27.891  14.776  1.00 26.60 ? 265 GLN   A C   1 
ATOM   2025 O O   . GLN   A 1 268 ? -23.531 28.066  15.849  1.00 28.44 ? 265 GLN   A O   1 
ATOM   2026 C CB  . GLN   A 1 268 ? -22.604 25.577  13.866  1.00 28.82 ? 265 GLN   A CB  1 
ATOM   2027 C CG  . GLN   A 1 268 ? -22.490 24.971  15.273  1.00 29.81 ? 265 GLN   A CG  1 
ATOM   2028 C CD  . GLN   A 1 268 ? -23.841 24.641  15.885  1.00 38.22 ? 265 GLN   A CD  1 
ATOM   2029 O OE1 . GLN   A 1 268 ? -24.776 24.232  15.180  1.00 37.31 ? 265 GLN   A OE1 1 
ATOM   2030 N NE2 . GLN   A 1 268 ? -23.964 24.835  17.205  1.00 33.68 ? 265 GLN   A NE2 1 
ATOM   2031 N N   . VAL   A 1 269 ? -21.879 28.597  14.430  1.00 25.73 ? 266 VAL   A N   1 
ATOM   2032 C CA  . VAL   A 1 269 ? -21.265 29.549  15.344  1.00 28.99 ? 266 VAL   A CA  1 
ATOM   2033 C C   . VAL   A 1 269 ? -21.830 30.950  15.151  1.00 33.13 ? 266 VAL   A C   1 
ATOM   2034 O O   . VAL   A 1 269 ? -22.230 31.607  16.121  1.00 34.92 ? 266 VAL   A O   1 
ATOM   2035 C CB  . VAL   A 1 269 ? -19.732 29.533  15.174  1.00 30.78 ? 266 VAL   A CB  1 
ATOM   2036 C CG1 . VAL   A 1 269 ? -19.091 30.666  15.947  1.00 28.63 ? 266 VAL   A CG1 1 
ATOM   2037 C CG2 . VAL   A 1 269 ? -19.156 28.167  15.623  1.00 29.09 ? 266 VAL   A CG2 1 
ATOM   2038 N N   . GLN   A 1 270 ? -21.913 31.423  13.907  1.00 33.26 ? 267 GLN   A N   1 
ATOM   2039 C CA  . GLN   A 1 270 ? -22.334 32.795  13.633  1.00 33.27 ? 267 GLN   A CA  1 
ATOM   2040 C C   . GLN   A 1 270 ? -23.831 32.933  13.404  1.00 31.29 ? 267 GLN   A C   1 
ATOM   2041 O O   . GLN   A 1 270 ? -24.304 34.050  13.164  1.00 34.58 ? 267 GLN   A O   1 
ATOM   2042 C CB  . GLN   A 1 270 ? -21.561 33.353  12.430  1.00 29.90 ? 267 GLN   A CB  1 
ATOM   2043 C CG  . GLN   A 1 270 ? -20.049 33.375  12.652  1.00 34.65 ? 267 GLN   A CG  1 
ATOM   2044 C CD  . GLN   A 1 270 ? -19.287 33.921  11.457  1.00 46.80 ? 267 GLN   A CD  1 
ATOM   2045 O OE1 . GLN   A 1 270 ? -19.330 33.354  10.357  1.00 39.56 ? 267 GLN   A OE1 1 
ATOM   2046 N NE2 . GLN   A 1 270 ? -18.582 35.032  11.663  1.00 43.41 ? 267 GLN   A NE2 1 
ATOM   2047 N N   . ARG   A 1 271 ? -24.589 31.842  13.486  1.00 29.98 ? 268 ARG   A N   1 
ATOM   2048 C CA  . ARG   A 1 271 ? -26.059 31.897  13.472  1.00 33.89 ? 268 ARG   A CA  1 
ATOM   2049 C C   . ARG   A 1 271 ? -26.600 32.476  12.166  1.00 36.01 ? 268 ARG   A C   1 
ATOM   2050 O O   . ARG   A 1 271 ? -27.641 33.144  12.143  1.00 35.05 ? 268 ARG   A O   1 
ATOM   2051 C CB  . ARG   A 1 271 ? -26.581 32.675  14.687  1.00 37.79 ? 268 ARG   A CB  1 
ATOM   2052 C CG  . ARG   A 1 271 ? -26.348 31.917  15.991  1.00 34.83 ? 268 ARG   A CG  1 
ATOM   2053 C CD  . ARG   A 1 271 ? -26.917 32.641  17.213  1.00 43.52 ? 268 ARG   A CD  1 
ATOM   2054 N NE  . ARG   A 1 271 ? -26.365 33.984  17.347  1.00 40.59 ? 268 ARG   A NE  1 
ATOM   2055 C CZ  . ARG   A 1 271 ? -27.064 35.103  17.205  1.00 39.81 ? 268 ARG   A CZ  1 
ATOM   2056 N NH1 . ARG   A 1 271 ? -28.365 35.083  16.967  1.00 34.27 ? 268 ARG   A NH1 1 
ATOM   2057 N NH2 . ARG   A 1 271 ? -26.441 36.276  17.317  1.00 42.76 ? 268 ARG   A NH2 1 
ATOM   2058 N N   . ASP   A 1 272 ? -25.898 32.206  11.067  1.00 31.90 ? 269 ASP   A N   1 
ATOM   2059 C CA  . ASP   A 1 272 ? -26.314 32.605  9.726   1.00 31.24 ? 269 ASP   A CA  1 
ATOM   2060 C C   . ASP   A 1 272 ? -27.205 31.495  9.178   1.00 32.34 ? 269 ASP   A C   1 
ATOM   2061 O O   . ASP   A 1 272 ? -26.744 30.581  8.500   1.00 33.34 ? 269 ASP   A O   1 
ATOM   2062 C CB  . ASP   A 1 272 ? -25.078 32.847  8.868   1.00 34.29 ? 269 ASP   A CB  1 
ATOM   2063 C CG  . ASP   A 1 272 ? -25.390 33.524  7.553   1.00 41.45 ? 269 ASP   A CG  1 
ATOM   2064 O OD1 . ASP   A 1 272 ? -26.484 33.290  7.003   1.00 40.55 ? 269 ASP   A OD1 1 
ATOM   2065 O OD2 . ASP   A 1 272 ? -24.523 34.283  7.067   1.00 47.72 ? 269 ASP   A OD2 1 
ATOM   2066 N N   . TYR   A 1 273 ? -28.508 31.567  9.468   1.00 30.81 ? 270 TYR   A N   1 
ATOM   2067 C CA  . TYR   A 1 273 ? -29.398 30.451  9.159   1.00 30.95 ? 270 TYR   A CA  1 
ATOM   2068 C C   . TYR   A 1 273 ? -30.081 30.543  7.799   1.00 33.10 ? 270 TYR   A C   1 
ATOM   2069 O O   . TYR   A 1 273 ? -30.580 29.524  7.315   1.00 31.79 ? 270 TYR   A O   1 
ATOM   2070 C CB  . TYR   A 1 273 ? -30.490 30.318  10.227  1.00 32.90 ? 270 TYR   A CB  1 
ATOM   2071 C CG  . TYR   A 1 273 ? -29.936 30.100  11.606  1.00 39.49 ? 270 TYR   A CG  1 
ATOM   2072 C CD1 . TYR   A 1 273 ? -29.401 28.871  11.977  1.00 37.94 ? 270 TYR   A CD1 1 
ATOM   2073 C CD2 . TYR   A 1 273 ? -29.941 31.128  12.542  1.00 42.06 ? 270 TYR   A CD2 1 
ATOM   2074 C CE1 . TYR   A 1 273 ? -28.883 28.670  13.254  1.00 42.60 ? 270 TYR   A CE1 1 
ATOM   2075 C CE2 . TYR   A 1 273 ? -29.427 30.934  13.815  1.00 43.56 ? 270 TYR   A CE2 1 
ATOM   2076 C CZ  . TYR   A 1 273 ? -28.902 29.708  14.166  1.00 42.11 ? 270 TYR   A CZ  1 
ATOM   2077 O OH  . TYR   A 1 273 ? -28.394 29.529  15.438  1.00 47.99 ? 270 TYR   A OH  1 
ATOM   2078 N N   . HIS   A 1 274 ? -30.128 31.718  7.177   1.00 29.07 ? 271 HIS   A N   1 
ATOM   2079 C CA  . HIS   A 1 274 ? -30.868 31.906  5.942   1.00 32.72 ? 271 HIS   A CA  1 
ATOM   2080 C C   . HIS   A 1 274 ? -29.978 32.559  4.898   1.00 32.13 ? 271 HIS   A C   1 
ATOM   2081 O O   . HIS   A 1 274 ? -29.071 33.334  5.219   1.00 35.39 ? 271 HIS   A O   1 
ATOM   2082 C CB  . HIS   A 1 274 ? -32.138 32.753  6.168   1.00 31.71 ? 271 HIS   A CB  1 
ATOM   2083 C CG  . HIS   A 1 274 ? -33.147 32.078  7.042   1.00 40.54 ? 271 HIS   A CG  1 
ATOM   2084 N ND1 . HIS   A 1 274 ? -34.244 31.413  6.535   1.00 45.27 ? 271 HIS   A ND1 1 
ATOM   2085 C CD2 . HIS   A 1 274 ? -33.206 31.930  8.387   1.00 44.47 ? 271 HIS   A CD2 1 
ATOM   2086 C CE1 . HIS   A 1 274 ? -34.942 30.894  7.532   1.00 40.96 ? 271 HIS   A CE1 1 
ATOM   2087 N NE2 . HIS   A 1 274 ? -34.335 31.194  8.667   1.00 48.50 ? 271 HIS   A NE2 1 
ATOM   2088 N N   . GLY   A 1 275 ? -30.250 32.241  3.643   1.00 31.47 ? 272 GLY   A N   1 
ATOM   2089 C CA  . GLY   A 1 275 ? -29.450 32.736  2.551   1.00 31.83 ? 272 GLY   A CA  1 
ATOM   2090 C C   . GLY   A 1 275 ? -30.013 32.314  1.214   1.00 31.47 ? 272 GLY   A C   1 
ATOM   2091 O O   . GLY   A 1 275 ? -31.063 31.658  1.129   1.00 28.07 ? 272 GLY   A O   1 
ATOM   2092 N N   . PRO   A 1 276 ? -29.326 32.685  0.135   1.00 33.81 ? 273 PRO   A N   1 
ATOM   2093 C CA  . PRO   A 1 276 ? -29.799 32.286  -1.195  1.00 25.98 ? 273 PRO   A CA  1 
ATOM   2094 C C   . PRO   A 1 276 ? -29.902 30.771  -1.285  1.00 28.92 ? 273 PRO   A C   1 
ATOM   2095 O O   . PRO   A 1 276 ? -29.066 30.039  -0.755  1.00 26.44 ? 273 PRO   A O   1 
ATOM   2096 C CB  . PRO   A 1 276 ? -28.730 32.847  -2.140  1.00 30.51 ? 273 PRO   A CB  1 
ATOM   2097 C CG  . PRO   A 1 276 ? -27.505 33.051  -1.272  1.00 32.57 ? 273 PRO   A CG  1 
ATOM   2098 C CD  . PRO   A 1 276 ? -28.054 33.429  0.078   1.00 31.20 ? 273 PRO   A CD  1 
ATOM   2099 N N   . ARG   A 1 277 ? -30.953 30.301  -1.946  1.00 24.74 ? 274 ARG   A N   1 
ATOM   2100 C CA  . ARG   A 1 277 ? -31.105 28.869  -2.155  1.00 27.79 ? 274 ARG   A CA  1 
ATOM   2101 C C   . ARG   A 1 277 ? -30.030 28.374  -3.121  1.00 28.87 ? 274 ARG   A C   1 
ATOM   2102 O O   . ARG   A 1 277 ? -29.790 28.985  -4.167  1.00 23.73 ? 274 ARG   A O   1 
ATOM   2103 C CB  . ARG   A 1 277 ? -32.505 28.569  -2.684  1.00 27.24 ? 274 ARG   A CB  1 
ATOM   2104 C CG  . ARG   A 1 277 ? -33.628 29.020  -1.714  1.00 31.44 ? 274 ARG   A CG  1 
ATOM   2105 C CD  . ARG   A 1 277 ? -34.997 28.478  -2.143  1.00 31.31 ? 274 ARG   A CD  1 
ATOM   2106 N NE  . ARG   A 1 277 ? -36.112 29.028  -1.369  1.00 37.12 ? 274 ARG   A NE  1 
ATOM   2107 C CZ  . ARG   A 1 277 ? -36.522 28.556  -0.198  1.00 38.17 ? 274 ARG   A CZ  1 
ATOM   2108 N NH1 . ARG   A 1 277 ? -35.899 27.553  0.399   1.00 35.75 ? 274 ARG   A NH1 1 
ATOM   2109 N NH2 . ARG   A 1 277 ? -37.584 29.104  0.391   1.00 36.98 ? 274 ARG   A NH2 1 
ATOM   2110 N N   . LEU   A 1 278 ? -29.373 27.278  -2.758  1.00 23.21 ? 275 LEU   A N   1 
ATOM   2111 C CA  . LEU   A 1 278 ? -28.200 26.803  -3.480  1.00 24.65 ? 275 LEU   A CA  1 
ATOM   2112 C C   . LEU   A 1 278 ? -28.512 25.727  -4.503  1.00 25.40 ? 275 LEU   A C   1 
ATOM   2113 O O   . LEU   A 1 278 ? -27.854 25.678  -5.543  1.00 24.67 ? 275 LEU   A O   1 
ATOM   2114 C CB  . LEU   A 1 278 ? -27.142 26.274  -2.500  1.00 22.88 ? 275 LEU   A CB  1 
ATOM   2115 C CG  . LEU   A 1 278 ? -26.520 27.347  -1.593  1.00 26.58 ? 275 LEU   A CG  1 
ATOM   2116 C CD1 . LEU   A 1 278 ? -25.343 26.806  -0.789  1.00 26.66 ? 275 LEU   A CD1 1 
ATOM   2117 C CD2 . LEU   A 1 278 ? -26.098 28.550  -2.425  1.00 25.20 ? 275 LEU   A CD2 1 
ATOM   2118 N N   . LEU   A 1 279 ? -29.518 24.889  -4.252  1.00 20.65 ? 276 LEU   A N   1 
ATOM   2119 C CA  . LEU   A 1 279 ? -29.849 23.836  -5.205  1.00 24.04 ? 276 LEU   A CA  1 
ATOM   2120 C C   . LEU   A 1 279 ? -30.167 24.346  -6.614  1.00 26.99 ? 276 LEU   A C   1 
ATOM   2121 O O   . LEU   A 1 279 ? -29.935 23.585  -7.575  1.00 24.41 ? 276 LEU   A O   1 
ATOM   2122 C CB  . LEU   A 1 279 ? -31.019 23.000  -4.658  1.00 20.59 ? 276 LEU   A CB  1 
ATOM   2123 C CG  . LEU   A 1 279 ? -30.736 22.392  -3.275  1.00 23.84 ? 276 LEU   A CG  1 
ATOM   2124 C CD1 . LEU   A 1 279 ? -31.754 21.302  -2.934  1.00 24.24 ? 276 LEU   A CD1 1 
ATOM   2125 C CD2 . LEU   A 1 279 ? -29.324 21.840  -3.216  1.00 24.14 ? 276 LEU   A CD2 1 
ATOM   2126 N N   . PRO   A 1 280 ? -30.690 25.562  -6.820  1.00 24.10 ? 277 PRO   A N   1 
ATOM   2127 C CA  . PRO   A 1 280 ? -30.888 26.044  -8.202  1.00 29.19 ? 277 PRO   A CA  1 
ATOM   2128 C C   . PRO   A 1 280 ? -29.597 26.128  -9.008  1.00 29.14 ? 277 PRO   A C   1 
ATOM   2129 O O   . PRO   A 1 280 ? -29.663 26.250  -10.237 1.00 34.33 ? 277 PRO   A O   1 
ATOM   2130 C CB  . PRO   A 1 280 ? -31.518 27.435  -8.011  1.00 26.93 ? 277 PRO   A CB  1 
ATOM   2131 C CG  . PRO   A 1 280 ? -32.223 27.332  -6.677  1.00 27.08 ? 277 PRO   A CG  1 
ATOM   2132 C CD  . PRO   A 1 280 ? -31.288 26.476  -5.823  1.00 25.06 ? 277 PRO   A CD  1 
ATOM   2133 N N   . TYR   A 1 281 ? -28.433 26.039  -8.365  1.00 23.34 ? 278 TYR   A N   1 
ATOM   2134 C CA  . TYR   A 1 281 ? -27.160 26.229  -9.039  1.00 28.53 ? 278 TYR   A CA  1 
ATOM   2135 C C   . TYR   A 1 281 ? -26.441 24.928  -9.356  1.00 26.64 ? 278 TYR   A C   1 
ATOM   2136 O O   . TYR   A 1 281 ? -25.371 24.976  -9.963  1.00 26.16 ? 278 TYR   A O   1 
ATOM   2137 C CB  . TYR   A 1 281 ? -26.251 27.128  -8.184  1.00 28.46 ? 278 TYR   A CB  1 
ATOM   2138 C CG  . TYR   A 1 281 ? -26.782 28.536  -8.083  1.00 30.96 ? 278 TYR   A CG  1 
ATOM   2139 C CD1 . TYR   A 1 281 ? -27.693 28.890  -7.094  1.00 30.40 ? 278 TYR   A CD1 1 
ATOM   2140 C CD2 . TYR   A 1 281 ? -26.400 29.510  -9.003  1.00 36.50 ? 278 TYR   A CD2 1 
ATOM   2141 C CE1 . TYR   A 1 281 ? -28.202 30.197  -7.017  1.00 31.35 ? 278 TYR   A CE1 1 
ATOM   2142 C CE2 . TYR   A 1 281 ? -26.894 30.812  -8.934  1.00 34.57 ? 278 TYR   A CE2 1 
ATOM   2143 C CZ  . TYR   A 1 281 ? -27.793 31.153  -7.941  1.00 41.02 ? 278 TYR   A CZ  1 
ATOM   2144 O OH  . TYR   A 1 281 ? -28.285 32.449  -7.883  1.00 40.29 ? 278 TYR   A OH  1 
ATOM   2145 N N   . ILE   A 1 282 ? -26.991 23.764  -8.979  1.00 23.12 ? 279 ILE   A N   1 
ATOM   2146 C CA  . ILE   A 1 282 ? -26.238 22.516  -9.131  1.00 23.04 ? 279 ILE   A CA  1 
ATOM   2147 C C   . ILE   A 1 282 ? -26.737 21.655  -10.285 1.00 20.75 ? 279 ILE   A C   1 
ATOM   2148 O O   . ILE   A 1 282 ? -26.186 20.570  -10.515 1.00 23.32 ? 279 ILE   A O   1 
ATOM   2149 C CB  . ILE   A 1 282 ? -26.245 21.680  -7.835  1.00 24.35 ? 279 ILE   A CB  1 
ATOM   2150 C CG1 . ILE   A 1 282 ? -27.639 21.096  -7.566  1.00 20.61 ? 279 ILE   A CG1 1 
ATOM   2151 C CG2 . ILE   A 1 282 ? -25.781 22.532  -6.657  1.00 24.35 ? 279 ILE   A CG2 1 
ATOM   2152 C CD1 . ILE   A 1 282 ? -27.621 19.950  -6.530  1.00 21.52 ? 279 ILE   A CD1 1 
ATOM   2153 N N   . MET   A 1 283 ? -27.731 22.114  -11.044 1.00 20.25 ? 280 MET   A N   1 
ATOM   2154 C CA  . MET   A 1 283 ? -28.332 21.246  -12.052 1.00 21.91 ? 280 MET   A CA  1 
ATOM   2155 C C   . MET   A 1 283 ? -27.488 21.154  -13.324 1.00 22.64 ? 280 MET   A C   1 
ATOM   2156 O O   . MET   A 1 283 ? -27.036 20.065  -13.709 1.00 22.28 ? 280 MET   A O   1 
ATOM   2157 C CB  . MET   A 1 283 ? -29.751 21.718  -12.353 1.00 27.02 ? 280 MET   A CB  1 
ATOM   2158 C CG  . MET   A 1 283 ? -30.758 21.273  -11.299 1.00 27.67 ? 280 MET   A CG  1 
ATOM   2159 S SD  . MET   A 1 283 ? -32.368 22.061  -11.529 1.00 30.56 ? 280 MET   A SD  1 
ATOM   2160 C CE  . MET   A 1 283 ? -32.032 23.737  -11.034 1.00 27.28 ? 280 MET   A CE  1 
ATOM   2161 N N   . PHE   A 1 284 ? -27.247 22.279  -13.995 1.00 23.95 ? 281 PHE   A N   1 
ATOM   2162 C CA  . PHE   A 1 284 ? -26.368 22.210  -15.159 1.00 23.16 ? 281 PHE   A CA  1 
ATOM   2163 C C   . PHE   A 1 284 ? -24.988 21.674  -14.794 1.00 19.65 ? 281 PHE   A C   1 
ATOM   2164 O O   . PHE   A 1 284 ? -24.465 20.819  -15.537 1.00 21.72 ? 281 PHE   A O   1 
ATOM   2165 C CB  . PHE   A 1 284 ? -26.237 23.580  -15.849 1.00 24.96 ? 281 PHE   A CB  1 
ATOM   2166 C CG  . PHE   A 1 284 ? -25.247 23.564  -16.970 1.00 25.44 ? 281 PHE   A CG  1 
ATOM   2167 C CD1 . PHE   A 1 284 ? -25.558 22.925  -18.168 1.00 24.80 ? 281 PHE   A CD1 1 
ATOM   2168 C CD2 . PHE   A 1 284 ? -23.997 24.127  -16.816 1.00 24.56 ? 281 PHE   A CD2 1 
ATOM   2169 C CE1 . PHE   A 1 284 ? -24.630 22.864  -19.208 1.00 25.73 ? 281 PHE   A CE1 1 
ATOM   2170 C CE2 . PHE   A 1 284 ? -23.064 24.080  -17.847 1.00 27.01 ? 281 PHE   A CE2 1 
ATOM   2171 C CZ  . PHE   A 1 284 ? -23.379 23.442  -19.040 1.00 25.74 ? 281 PHE   A CZ  1 
ATOM   2172 N N   . PRO   A 1 285 ? -24.367 22.092  -13.695 1.00 20.38 ? 282 PRO   A N   1 
ATOM   2173 C CA  . PRO   A 1 285 ? -23.050 21.538  -13.349 1.00 20.01 ? 282 PRO   A CA  1 
ATOM   2174 C C   . PRO   A 1 285 ? -23.084 20.059  -13.033 1.00 22.54 ? 282 PRO   A C   1 
ATOM   2175 O O   . PRO   A 1 285 ? -22.013 19.433  -12.964 1.00 24.34 ? 282 PRO   A O   1 
ATOM   2176 C CB  . PRO   A 1 285 ? -22.635 22.353  -12.115 1.00 20.32 ? 282 PRO   A CB  1 
ATOM   2177 C CG  . PRO   A 1 285 ? -23.461 23.608  -12.190 1.00 24.13 ? 282 PRO   A CG  1 
ATOM   2178 C CD  . PRO   A 1 285 ? -24.754 23.220  -12.824 1.00 20.37 ? 282 PRO   A CD  1 
ATOM   2179 N N   . ARG   A 1 286 ? -24.265 19.484  -12.810 1.00 18.47 ? 283 ARG   A N   1 
ATOM   2180 C CA  . ARG   A 1 286 ? -24.366 18.109  -12.333 1.00 21.32 ? 283 ARG   A CA  1 
ATOM   2181 C C   . ARG   A 1 286 ? -23.462 17.892  -11.115 1.00 21.78 ? 283 ARG   A C   1 
ATOM   2182 O O   . ARG   A 1 286 ? -22.724 16.907  -11.023 1.00 19.48 ? 283 ARG   A O   1 
ATOM   2183 C CB  . ARG   A 1 286 ? -24.020 17.133  -13.467 1.00 22.97 ? 283 ARG   A CB  1 
ATOM   2184 C CG  . ARG   A 1 286 ? -25.085 17.047  -14.572 1.00 24.51 ? 283 ARG   A CG  1 
ATOM   2185 C CD  . ARG   A 1 286 ? -24.446 16.945  -15.968 1.00 20.82 ? 283 ARG   A CD  1 
ATOM   2186 N NE  . ARG   A 1 286 ? -24.143 18.279  -16.471 1.00 22.96 ? 283 ARG   A NE  1 
ATOM   2187 C CZ  . ARG   A 1 286 ? -23.565 18.537  -17.638 1.00 25.32 ? 283 ARG   A CZ  1 
ATOM   2188 N NH1 . ARG   A 1 286 ? -23.120 17.568  -18.418 1.00 26.14 ? 283 ARG   A NH1 1 
ATOM   2189 N NH2 . ARG   A 1 286 ? -23.439 19.800  -18.034 1.00 22.65 ? 283 ARG   A NH2 1 
ATOM   2190 N N   . ALA   A 1 287 ? -23.525 18.830  -10.166 1.00 19.44 ? 284 ALA   A N   1 
ATOM   2191 C CA  . ALA   A 1 287 ? -22.675 18.766  -8.982  1.00 19.67 ? 284 ALA   A CA  1 
ATOM   2192 C C   . ALA   A 1 287 ? -23.180 17.720  -8.007  1.00 22.29 ? 284 ALA   A C   1 
ATOM   2193 O O   . ALA   A 1 287 ? -24.384 17.484  -7.896  1.00 21.59 ? 284 ALA   A O   1 
ATOM   2194 C CB  . ALA   A 1 287 ? -22.610 20.122  -8.278  1.00 18.37 ? 284 ALA   A CB  1 
ATOM   2195 N N   . THR   A 1 288 ? -22.246 17.093  -7.291  1.00 19.97 ? 285 THR   A N   1 
ATOM   2196 C CA  . THR   A 1 288 ? -22.569 16.131  -6.238  1.00 20.52 ? 285 THR   A CA  1 
ATOM   2197 C C   . THR   A 1 288 ? -22.144 16.722  -4.907  1.00 22.23 ? 285 THR   A C   1 
ATOM   2198 O O   . THR   A 1 288 ? -20.977 17.089  -4.736  1.00 22.89 ? 285 THR   A O   1 
ATOM   2199 C CB  . THR   A 1 288 ? -21.861 14.788  -6.449  1.00 24.16 ? 285 THR   A CB  1 
ATOM   2200 O OG1 . THR   A 1 288 ? -22.179 14.287  -7.749  1.00 24.83 ? 285 THR   A OG1 1 
ATOM   2201 C CG2 . THR   A 1 288 ? -22.313 13.774  -5.381  1.00 23.89 ? 285 THR   A CG2 1 
ATOM   2202 N N   . ILE   A 1 289 ? -23.086 16.818  -3.982  1.00 18.06 ? 286 ILE   A N   1 
ATOM   2203 C CA  . ILE   A 1 289 ? -22.862 17.342  -2.647  1.00 20.20 ? 286 ILE   A CA  1 
ATOM   2204 C C   . ILE   A 1 289 ? -23.065 16.204  -1.669  1.00 23.41 ? 286 ILE   A C   1 
ATOM   2205 O O   . ILE   A 1 289 ? -24.111 15.547  -1.691  1.00 22.57 ? 286 ILE   A O   1 
ATOM   2206 C CB  . ILE   A 1 289 ? -23.827 18.488  -2.319  1.00 22.04 ? 286 ILE   A CB  1 
ATOM   2207 C CG1 . ILE   A 1 289 ? -23.874 19.499  -3.467  1.00 21.57 ? 286 ILE   A CG1 1 
ATOM   2208 C CG2 . ILE   A 1 289 ? -23.427 19.152  -1.035  1.00 22.55 ? 286 ILE   A CG2 1 
ATOM   2209 C CD1 . ILE   A 1 289 ? -24.958 20.540  -3.249  1.00 27.30 ? 286 ILE   A CD1 1 
ATOM   2210 N N   . ARG   A 1 290 ? -22.100 15.984  -0.806  1.00 19.28 ? 287 ARG   A N   1 
ATOM   2211 C CA  . ARG   A 1 290 ? -22.163 14.915  0.171   1.00 18.05 ? 287 ARG   A CA  1 
ATOM   2212 C C   . ARG   A 1 290 ? -21.862 15.378  1.582   1.00 22.32 ? 287 ARG   A C   1 
ATOM   2213 O O   . ARG   A 1 290 ? -20.839 15.997  1.821   1.00 20.83 ? 287 ARG   A O   1 
ATOM   2214 C CB  . ARG   A 1 290 ? -21.143 13.864  -0.201  1.00 21.08 ? 287 ARG   A CB  1 
ATOM   2215 C CG  . ARG   A 1 290 ? -21.631 12.444  -0.128  1.00 26.03 ? 287 ARG   A CG  1 
ATOM   2216 C CD  . ARG   A 1 290 ? -21.578 11.952  1.289   1.00 27.91 ? 287 ARG   A CD  1 
ATOM   2217 N NE  . ARG   A 1 290 ? -21.261 10.536  1.397   1.00 32.48 ? 287 ARG   A NE  1 
ATOM   2218 C CZ  . ARG   A 1 290 ? -20.660 10.009  2.456   1.00 29.43 ? 287 ARG   A CZ  1 
ATOM   2219 N NH1 . ARG   A 1 290 ? -20.308 10.789  3.462   1.00 21.26 ? 287 ARG   A NH1 1 
ATOM   2220 N NH2 . ARG   A 1 290 ? -20.408 8.714   2.509   1.00 26.14 ? 287 ARG   A NH2 1 
ATOM   2221 N N   . GLY   A 1 291 ? -22.751 15.099  2.522   1.00 21.90 ? 288 GLY   A N   1 
ATOM   2222 C CA  . GLY   A 1 291 ? -22.482 15.423  3.911   1.00 21.01 ? 288 GLY   A CA  1 
ATOM   2223 C C   . GLY   A 1 291 ? -21.473 14.440  4.489   1.00 24.10 ? 288 GLY   A C   1 
ATOM   2224 O O   . GLY   A 1 291 ? -21.513 13.238  4.215   1.00 20.52 ? 288 GLY   A O   1 
ATOM   2225 N N   . ILE   A 1 292 ? -20.552 14.973  5.288   1.00 20.09 ? 289 ILE   A N   1 
ATOM   2226 C CA  . ILE   A 1 292 ? -19.508 14.175  5.922   1.00 23.32 ? 289 ILE   A CA  1 
ATOM   2227 C C   . ILE   A 1 292 ? -19.872 13.952  7.382   1.00 21.63 ? 289 ILE   A C   1 
ATOM   2228 O O   . ILE   A 1 292 ? -20.190 14.900  8.108   1.00 22.48 ? 289 ILE   A O   1 
ATOM   2229 C CB  . ILE   A 1 292 ? -18.132 14.854  5.817   1.00 20.49 ? 289 ILE   A CB  1 
ATOM   2230 C CG1 . ILE   A 1 292 ? -17.804 15.241  4.370   1.00 19.58 ? 289 ILE   A CG1 1 
ATOM   2231 C CG2 . ILE   A 1 292 ? -17.046 13.927  6.402   1.00 21.96 ? 289 ILE   A CG2 1 
ATOM   2232 C CD1 . ILE   A 1 292 ? -17.668 14.076  3.421   1.00 18.86 ? 289 ILE   A CD1 1 
ATOM   2233 N N   . PHE   A 1 293 ? -19.800 12.704  7.823   1.00 21.83 ? 290 PHE   A N   1 
ATOM   2234 C CA  . PHE   A 1 293 ? -19.901 12.383  9.255   1.00 23.44 ? 290 PHE   A CA  1 
ATOM   2235 C C   . PHE   A 1 293 ? -18.900 11.249  9.451   1.00 22.05 ? 290 PHE   A C   1 
ATOM   2236 O O   . PHE   A 1 293 ? -19.238 10.075  9.280   1.00 23.55 ? 290 PHE   A O   1 
ATOM   2237 C CB  . PHE   A 1 293 ? -21.313 11.989  9.663   1.00 23.56 ? 290 PHE   A CB  1 
ATOM   2238 C CG  . PHE   A 1 293 ? -21.523 11.984  11.156  1.00 26.96 ? 290 PHE   A CG  1 
ATOM   2239 C CD1 . PHE   A 1 293 ? -21.577 13.173  11.858  1.00 27.47 ? 290 PHE   A CD1 1 
ATOM   2240 C CD2 . PHE   A 1 293 ? -21.685 10.793  11.844  1.00 26.91 ? 290 PHE   A CD2 1 
ATOM   2241 C CE1 . PHE   A 1 293 ? -21.770 13.176  13.229  1.00 30.32 ? 290 PHE   A CE1 1 
ATOM   2242 C CE2 . PHE   A 1 293 ? -21.881 10.789  13.215  1.00 26.79 ? 290 PHE   A CE2 1 
ATOM   2243 C CZ  . PHE   A 1 293 ? -21.918 11.981  13.906  1.00 28.70 ? 290 PHE   A CZ  1 
ATOM   2244 N N   . SER   A 1 294 ? -17.658 11.609  9.757   1.00 20.35 ? 291 SER   A N   1 
ATOM   2245 C CA  . SER   A 1 294 ? -16.578 10.645  9.561   1.00 25.33 ? 291 SER   A CA  1 
ATOM   2246 C C   . SER   A 1 294 ? -16.635 9.469   10.535  1.00 25.09 ? 291 SER   A C   1 
ATOM   2247 O O   . SER   A 1 294 ? -15.891 8.498   10.333  1.00 23.42 ? 291 SER   A O   1 
ATOM   2248 C CB  . SER   A 1 294 ? -15.237 11.352  9.679   1.00 24.87 ? 291 SER   A CB  1 
ATOM   2249 O OG  . SER   A 1 294 ? -15.299 12.250  10.760  1.00 28.83 ? 291 SER   A OG  1 
ATOM   2250 N N   . LEU   A 1 295 ? -17.518 9.506   11.547  1.00 25.40 ? 292 LEU   A N   1 
ATOM   2251 C CA  . LEU   A 1 295 ? -17.712 8.337   12.414  1.00 26.82 ? 292 LEU   A CA  1 
ATOM   2252 C C   . LEU   A 1 295 ? -18.009 7.071   11.619  1.00 26.29 ? 292 LEU   A C   1 
ATOM   2253 O O   . LEU   A 1 295 ? -17.637 5.968   12.041  1.00 28.25 ? 292 LEU   A O   1 
ATOM   2254 C CB  . LEU   A 1 295 ? -18.861 8.582   13.402  1.00 26.25 ? 292 LEU   A CB  1 
ATOM   2255 C CG  . LEU   A 1 295 ? -18.559 9.556   14.532  1.00 32.88 ? 292 LEU   A CG  1 
ATOM   2256 C CD1 . LEU   A 1 295 ? -19.565 9.415   15.706  1.00 30.26 ? 292 LEU   A CD1 1 
ATOM   2257 C CD2 . LEU   A 1 295 ? -17.128 9.347   15.007  1.00 34.10 ? 292 LEU   A CD2 1 
ATOM   2258 N N   . GLU   A 1 296 ? -18.677 7.198   10.470  1.00 24.03 ? 293 GLU   A N   1 
ATOM   2259 C CA  . GLU   A 1 296 ? -19.023 6.013   9.690   1.00 23.01 ? 293 GLU   A CA  1 
ATOM   2260 C C   . GLU   A 1 296 ? -17.788 5.301   9.168   1.00 23.52 ? 293 GLU   A C   1 
ATOM   2261 O O   . GLU   A 1 296 ? -17.886 4.147   8.749   1.00 24.84 ? 293 GLU   A O   1 
ATOM   2262 C CB  . GLU   A 1 296 ? -19.935 6.374   8.503   1.00 23.74 ? 293 GLU   A CB  1 
ATOM   2263 C CG  . GLU   A 1 296 ? -19.269 7.275   7.459   1.00 24.46 ? 293 GLU   A CG  1 
ATOM   2264 C CD  . GLU   A 1 296 ? -20.026 7.342   6.133   1.00 30.40 ? 293 GLU   A CD  1 
ATOM   2265 O OE1 . GLU   A 1 296 ? -20.710 6.351   5.798   1.00 30.99 ? 293 GLU   A OE1 1 
ATOM   2266 O OE2 . GLU   A 1 296 ? -19.936 8.383   5.426   1.00 28.57 ? 293 GLU   A OE2 1 
ATOM   2267 N N   . TRP   A 1 297 ? -16.629 5.961   9.173   1.00 23.62 ? 294 TRP   A N   1 
ATOM   2268 C CA  . TRP   A 1 297 ? -15.398 5.367   8.678   1.00 22.02 ? 294 TRP   A CA  1 
ATOM   2269 C C   . TRP   A 1 297 ? -14.532 4.790   9.795   1.00 25.80 ? 294 TRP   A C   1 
ATOM   2270 O O   . TRP   A 1 297 ? -13.406 4.374   9.533   1.00 25.48 ? 294 TRP   A O   1 
ATOM   2271 C CB  . TRP   A 1 297 ? -14.618 6.409   7.879   1.00 22.51 ? 294 TRP   A CB  1 
ATOM   2272 C CG  . TRP   A 1 297 ? -15.345 6.886   6.631   1.00 22.93 ? 294 TRP   A CG  1 
ATOM   2273 C CD1 . TRP   A 1 297 ? -16.127 6.140   5.787   1.00 25.31 ? 294 TRP   A CD1 1 
ATOM   2274 C CD2 . TRP   A 1 297 ? -15.346 8.216   6.110   1.00 22.63 ? 294 TRP   A CD2 1 
ATOM   2275 N NE1 . TRP   A 1 297 ? -16.599 6.929   4.756   1.00 22.79 ? 294 TRP   A NE1 1 
ATOM   2276 C CE2 . TRP   A 1 297 ? -16.126 8.206   4.933   1.00 26.21 ? 294 TRP   A CE2 1 
ATOM   2277 C CE3 . TRP   A 1 297 ? -14.736 9.417   6.512   1.00 24.83 ? 294 TRP   A CE3 1 
ATOM   2278 C CZ2 . TRP   A 1 297 ? -16.342 9.357   4.173   1.00 22.31 ? 294 TRP   A CZ2 1 
ATOM   2279 C CZ3 . TRP   A 1 297 ? -14.948 10.566  5.746   1.00 19.56 ? 294 TRP   A CZ3 1 
ATOM   2280 C CH2 . TRP   A 1 297 ? -15.740 10.521  4.589   1.00 21.71 ? 294 TRP   A CH2 1 
ATOM   2281 N N   . PHE   A 1 298 ? -15.027 4.752   11.033  1.00 25.45 ? 295 PHE   A N   1 
ATOM   2282 C CA  . PHE   A 1 298 ? -14.225 4.278   12.160  1.00 24.55 ? 295 PHE   A CA  1 
ATOM   2283 C C   . PHE   A 1 298 ? -14.299 2.756   12.201  1.00 24.64 ? 295 PHE   A C   1 
ATOM   2284 O O   . PHE   A 1 298 ? -15.059 2.157   12.956  1.00 25.13 ? 295 PHE   A O   1 
ATOM   2285 C CB  . PHE   A 1 298 ? -14.697 4.890   13.471  1.00 24.63 ? 295 PHE   A CB  1 
ATOM   2286 C CG  . PHE   A 1 298 ? -14.298 6.329   13.662  1.00 28.88 ? 295 PHE   A CG  1 
ATOM   2287 C CD1 . PHE   A 1 298 ? -14.133 7.173   12.580  1.00 24.09 ? 295 PHE   A CD1 1 
ATOM   2288 C CD2 . PHE   A 1 298 ? -14.068 6.827   14.936  1.00 28.03 ? 295 PHE   A CD2 1 
ATOM   2289 C CE1 . PHE   A 1 298 ? -13.767 8.500   12.769  1.00 27.21 ? 295 PHE   A CE1 1 
ATOM   2290 C CE2 . PHE   A 1 298 ? -13.693 8.139   15.125  1.00 29.11 ? 295 PHE   A CE2 1 
ATOM   2291 C CZ  . PHE   A 1 298 ? -13.555 8.981   14.029  1.00 25.93 ? 295 PHE   A CZ  1 
ATOM   2292 N N   . THR   A 1 299 ? -13.500 2.125   11.353  1.00 24.29 ? 296 THR   A N   1 
ATOM   2293 C CA  . THR   A 1 299 ? -13.411 0.679   11.295  1.00 29.71 ? 296 THR   A CA  1 
ATOM   2294 C C   . THR   A 1 299 ? -11.947 0.279   11.367  1.00 31.86 ? 296 THR   A C   1 
ATOM   2295 O O   . THR   A 1 299 ? -11.042 1.051   11.031  1.00 27.55 ? 296 THR   A O   1 
ATOM   2296 C CB  . THR   A 1 299 ? -14.014 0.107   10.005  1.00 31.88 ? 296 THR   A CB  1 
ATOM   2297 O OG1 . THR   A 1 299 ? -13.147 0.402   8.907   1.00 29.30 ? 296 THR   A OG1 1 
ATOM   2298 C CG2 . THR   A 1 299 ? -15.396 0.692   9.736   1.00 31.45 ? 296 THR   A CG2 1 
ATOM   2299 N N   . GLU   A 1 300 ? -11.721 -0.963  11.787  1.00 31.66 ? 297 GLU   A N   1 
ATOM   2300 C CA  . GLU   A 1 300 ? -10.353 -1.448  11.907  1.00 30.29 ? 297 GLU   A CA  1 
ATOM   2301 C C   . GLU   A 1 300 ? -9.620  -1.358  10.577  1.00 30.71 ? 297 GLU   A C   1 
ATOM   2302 O O   . GLU   A 1 300 ? -8.447  -0.961  10.525  1.00 28.39 ? 297 GLU   A O   1 
ATOM   2303 C CB  . GLU   A 1 300 ? -10.362 -2.887  12.421  1.00 37.61 ? 297 GLU   A CB  1 
ATOM   2304 C CG  . GLU   A 1 300 ? -8.996  -3.500  12.536  1.00 42.07 ? 297 GLU   A CG  1 
ATOM   2305 C CD  . GLU   A 1 300 ? -9.068  -4.962  12.922  1.00 59.12 ? 297 GLU   A CD  1 
ATOM   2306 O OE1 . GLU   A 1 300 ? -9.175  -5.254  14.136  1.00 61.90 ? 297 GLU   A OE1 1 
ATOM   2307 O OE2 . GLU   A 1 300 ? -9.040  -5.813  12.003  1.00 60.94 ? 297 GLU   A OE2 1 
ATOM   2308 N N   . GLN   A 1 301 ? -10.291 -1.701  9.502   1.00 30.04 ? 298 GLN   A N   1 
ATOM   2309 C CA  . GLN   A 1 301 ? -9.659  -1.632  8.210   1.00 32.96 ? 298 GLN   A CA  1 
ATOM   2310 C C   . GLN   A 1 301 ? -9.260  -0.201  7.841   1.00 28.47 ? 298 GLN   A C   1 
ATOM   2311 O O   . GLN   A 1 301 ? -8.197  0.025   7.308   1.00 26.36 ? 298 GLN   A O   1 
ATOM   2312 C CB  . GLN   A 1 301 ? -10.549 -2.227  7.145   1.00 35.41 ? 298 GLN   A CB  1 
ATOM   2313 C CG  . GLN   A 1 301 ? -10.764 -3.719  7.275   1.00 51.65 ? 298 GLN   A CG  1 
ATOM   2314 C CD  . GLN   A 1 301 ? -11.718 -4.255  6.232   1.00 58.18 ? 298 GLN   A CD  1 
ATOM   2315 O OE1 . GLN   A 1 301 ? -12.561 -3.524  5.711   1.00 64.85 ? 298 GLN   A OE1 1 
ATOM   2316 N NE2 . GLN   A 1 301 ? -11.590 -5.532  5.918   1.00 58.74 ? 298 GLN   A NE2 1 
ATOM   2317 N N   . ASN   A 1 302 ? -10.134 0.748   8.133   1.00 30.39 ? 299 ASN   A N   1 
ATOM   2318 C CA  . ASN   A 1 302 ? -9.808  2.121   7.757   1.00 23.72 ? 299 ASN   A CA  1 
ATOM   2319 C C   . ASN   A 1 302 ? -8.671  2.680   8.609   1.00 23.74 ? 299 ASN   A C   1 
ATOM   2320 O O   . ASN   A 1 302 ? -7.811  3.398   8.091   1.00 24.33 ? 299 ASN   A O   1 
ATOM   2321 C CB  . ASN   A 1 302 ? -11.053 3.004   7.849   1.00 24.97 ? 299 ASN   A CB  1 
ATOM   2322 C CG  . ASN   A 1 302 ? -11.977 2.822   6.646   1.00 26.91 ? 299 ASN   A CG  1 
ATOM   2323 O OD1 . ASN   A 1 302 ? -11.523 2.484   5.547   1.00 26.38 ? 299 ASN   A OD1 1 
ATOM   2324 N ND2 . ASN   A 1 302 ? -13.273 3.005   6.861   1.00 26.05 ? 299 ASN   A ND2 1 
ATOM   2325 N N   . TRP   A 1 303 ? -8.648  2.365   9.914   1.00 26.49 ? 300 TRP   A N   1 
ATOM   2326 C CA  . TRP   A 1 303 ? -7.543  2.833   10.757  1.00 25.02 ? 300 TRP   A CA  1 
ATOM   2327 C C   . TRP   A 1 303 ? -6.208  2.276   10.274  1.00 25.18 ? 300 TRP   A C   1 
ATOM   2328 O O   . TRP   A 1 303 ? -5.203  2.988   10.269  1.00 26.54 ? 300 TRP   A O   1 
ATOM   2329 C CB  . TRP   A 1 303 ? -7.784  2.478   12.230  1.00 21.44 ? 300 TRP   A CB  1 
ATOM   2330 C CG  . TRP   A 1 303 ? -8.902  3.306   12.877  1.00 23.94 ? 300 TRP   A CG  1 
ATOM   2331 C CD1 . TRP   A 1 303 ? -10.093 2.837   13.373  1.00 21.37 ? 300 TRP   A CD1 1 
ATOM   2332 C CD2 . TRP   A 1 303 ? -8.930  4.735   13.053  1.00 21.34 ? 300 TRP   A CD2 1 
ATOM   2333 N NE1 . TRP   A 1 303 ? -10.851 3.883   13.850  1.00 23.15 ? 300 TRP   A NE1 1 
ATOM   2334 C CE2 . TRP   A 1 303 ? -10.162 5.057   13.664  1.00 23.30 ? 300 TRP   A CE2 1 
ATOM   2335 C CE3 . TRP   A 1 303 ? -8.021  5.774   12.768  1.00 23.44 ? 300 TRP   A CE3 1 
ATOM   2336 C CZ2 . TRP   A 1 303 ? -10.517 6.373   13.996  1.00 21.62 ? 300 TRP   A CZ2 1 
ATOM   2337 C CZ3 . TRP   A 1 303 ? -8.372  7.084   13.103  1.00 19.96 ? 300 TRP   A CZ3 1 
ATOM   2338 C CH2 . TRP   A 1 303 ? -9.613  7.372   13.706  1.00 22.67 ? 300 TRP   A CH2 1 
ATOM   2339 N N   . SER   A 1 304 ? -6.178  1.006   9.844   1.00 26.16 ? 301 SER   A N   1 
ATOM   2340 C CA  . SER   A 1 304 ? -4.941  0.430   9.320   1.00 31.10 ? 301 SER   A CA  1 
ATOM   2341 C C   . SER   A 1 304 ? -4.524  1.100   8.021   1.00 29.73 ? 301 SER   A C   1 
ATOM   2342 O O   . SER   A 1 304 ? -3.337  1.395   7.819   1.00 27.65 ? 301 SER   A O   1 
ATOM   2343 C CB  . SER   A 1 304 ? -5.096  -1.077  9.085   1.00 34.42 ? 301 SER   A CB  1 
ATOM   2344 O OG  . SER   A 1 304 ? -5.001  -1.793  10.293  1.00 38.94 ? 301 SER   A OG  1 
ATOM   2345 N N   . ALA   A 1 305 ? -5.478  1.318   7.111   1.00 28.60 ? 302 ALA   A N   1 
ATOM   2346 C CA  . ALA   A 1 305 ? -5.148  2.004   5.865   1.00 27.79 ? 302 ALA   A CA  1 
ATOM   2347 C C   . ALA   A 1 305 ? -4.717  3.437   6.134   1.00 24.53 ? 302 ALA   A C   1 
ATOM   2348 O O   . ALA   A 1 305 ? -3.830  3.962   5.451   1.00 28.09 ? 302 ALA   A O   1 
ATOM   2349 C CB  . ALA   A 1 305 ? -6.347  1.968   4.901   1.00 26.41 ? 302 ALA   A CB  1 
ATOM   2350 N N   . LEU   A 1 306 ? -5.343  4.096   7.116   1.00 25.05 ? 303 LEU   A N   1 
ATOM   2351 C CA  . LEU   A 1 306 ? -4.953  5.464   7.452   1.00 25.32 ? 303 LEU   A CA  1 
ATOM   2352 C C   . LEU   A 1 306 ? -3.509  5.513   7.935   1.00 25.52 ? 303 LEU   A C   1 
ATOM   2353 O O   . LEU   A 1 306 ? -2.723  6.355   7.490   1.00 26.50 ? 303 LEU   A O   1 
ATOM   2354 C CB  . LEU   A 1 306 ? -5.890  6.045   8.514   1.00 21.76 ? 303 LEU   A CB  1 
ATOM   2355 C CG  . LEU   A 1 306 ? -5.582  7.473   8.988   1.00 25.43 ? 303 LEU   A CG  1 
ATOM   2356 C CD1 . LEU   A 1 306 ? -6.054  8.471   7.969   1.00 26.95 ? 303 LEU   A CD1 1 
ATOM   2357 C CD2 . LEU   A 1 306 ? -6.222  7.792   10.352  1.00 23.51 ? 303 LEU   A CD2 1 
ATOM   2358 N N   . HIS   A 1 307 ? -3.150  4.619   8.858   1.00 25.39 ? 304 HIS   A N   1 
ATOM   2359 C CA  . HIS   A 1 307 ? -1.775  4.577   9.351   1.00 28.29 ? 304 HIS   A CA  1 
ATOM   2360 C C   . HIS   A 1 307 ? -0.797  4.258   8.227   1.00 29.35 ? 304 HIS   A C   1 
ATOM   2361 O O   . HIS   A 1 307 ? 0.270   4.869   8.133   1.00 29.48 ? 304 HIS   A O   1 
ATOM   2362 C CB  . HIS   A 1 307 ? -1.649  3.553   10.479  1.00 30.02 ? 304 HIS   A CB  1 
ATOM   2363 C CG  . HIS   A 1 307 ? -2.072  4.085   11.815  1.00 34.11 ? 304 HIS   A CG  1 
ATOM   2364 N ND1 . HIS   A 1 307 ? -1.240  4.854   12.601  1.00 32.34 ? 304 HIS   A ND1 1 
ATOM   2365 C CD2 . HIS   A 1 307 ? -3.240  3.978   12.490  1.00 31.84 ? 304 HIS   A CD2 1 
ATOM   2366 C CE1 . HIS   A 1 307 ? -1.880  5.194   13.708  1.00 33.04 ? 304 HIS   A CE1 1 
ATOM   2367 N NE2 . HIS   A 1 307 ? -3.096  4.673   13.665  1.00 33.44 ? 304 HIS   A NE2 1 
ATOM   2368 N N   . GLU   A 1 308 ? -1.144  3.307   7.359   1.00 29.96 ? 305 GLU   A N   1 
ATOM   2369 C CA  . GLU   A 1 308 ? -0.234  2.968   6.267   1.00 31.60 ? 305 GLU   A CA  1 
ATOM   2370 C C   . GLU   A 1 308 ? -0.094  4.130   5.296   1.00 32.05 ? 305 GLU   A C   1 
ATOM   2371 O O   . GLU   A 1 308 ? 1.020   4.562   4.967   1.00 29.47 ? 305 GLU   A O   1 
ATOM   2372 C CB  . GLU   A 1 308 ? -0.727  1.723   5.533   1.00 36.89 ? 305 GLU   A CB  1 
ATOM   2373 C CG  . GLU   A 1 308 ? -0.023  1.510   4.204   1.00 46.27 ? 305 GLU   A CG  1 
ATOM   2374 C CD  . GLU   A 1 308 ? 0.363   0.063   3.982   1.00 56.57 ? 305 GLU   A CD  1 
ATOM   2375 O OE1 . GLU   A 1 308 ? -0.004  -0.778  4.831   1.00 57.81 ? 305 GLU   A OE1 1 
ATOM   2376 O OE2 . GLU   A 1 308 ? 1.032   -0.233  2.965   1.00 66.75 ? 305 GLU   A OE2 1 
ATOM   2377 N N   . GLU   A 1 309 ? -1.222  4.673   4.853   1.00 29.37 ? 306 GLU   A N   1 
ATOM   2378 C CA  . GLU   A 1 309 ? -1.211  5.664   3.790   1.00 31.53 ? 306 GLU   A CA  1 
ATOM   2379 C C   . GLU   A 1 309 ? -0.807  7.044   4.307   1.00 33.32 ? 306 GLU   A C   1 
ATOM   2380 O O   . GLU   A 1 309 ? 0.214   7.603   3.889   1.00 32.48 ? 306 GLU   A O   1 
ATOM   2381 C CB  . GLU   A 1 309 ? -2.584  5.688   3.117   1.00 33.58 ? 306 GLU   A CB  1 
ATOM   2382 C CG  . GLU   A 1 309 ? -2.731  6.765   2.064   1.00 41.95 ? 306 GLU   A CG  1 
ATOM   2383 C CD  . GLU   A 1 309 ? -3.834  6.446   1.069   1.00 40.48 ? 306 GLU   A CD  1 
ATOM   2384 O OE1 . GLU   A 1 309 ? -4.639  5.514   1.325   1.00 40.83 ? 306 GLU   A OE1 1 
ATOM   2385 O OE2 . GLU   A 1 309 ? -3.870  7.126   0.025   1.00 50.97 ? 306 GLU   A OE2 1 
ATOM   2386 N N   . LEU   A 1 310 ? -1.594  7.616   5.222   1.00 29.27 ? 307 LEU   A N   1 
ATOM   2387 C CA  . LEU   A 1 310 ? -1.296  8.969   5.683   1.00 24.62 ? 307 LEU   A CA  1 
ATOM   2388 C C   . LEU   A 1 310 ? -0.072  8.986   6.598   1.00 29.65 ? 307 LEU   A C   1 
ATOM   2389 O O   . LEU   A 1 310 ? 0.764   9.891   6.512   1.00 29.16 ? 307 LEU   A O   1 
ATOM   2390 C CB  . LEU   A 1 310 ? -2.520  9.550   6.398   1.00 30.32 ? 307 LEU   A CB  1 
ATOM   2391 C CG  . LEU   A 1 310 ? -2.629  11.067  6.407   1.00 32.00 ? 307 LEU   A CG  1 
ATOM   2392 C CD1 . LEU   A 1 310 ? -2.524  11.593  4.991   1.00 36.65 ? 307 LEU   A CD1 1 
ATOM   2393 C CD2 . LEU   A 1 310 ? -3.939  11.537  7.046   1.00 31.13 ? 307 LEU   A CD2 1 
ATOM   2394 N N   . GLY   A 1 311 ? 0.044   8.001   7.490   1.00 29.82 ? 308 GLY   A N   1 
ATOM   2395 C CA  . GLY   A 1 311 ? 1.224   7.922   8.341   1.00 31.82 ? 308 GLY   A CA  1 
ATOM   2396 C C   . GLY   A 1 311 ? 2.518   7.857   7.552   1.00 27.73 ? 308 GLY   A C   1 
ATOM   2397 O O   . GLY   A 1 311 ? 3.508   8.495   7.913   1.00 27.68 ? 308 GLY   A O   1 
ATOM   2398 N N   . GLY   A 1 312 ? 2.527   7.099   6.457   1.00 31.30 ? 309 GLY   A N   1 
ATOM   2399 C CA  . GLY   A 1 312 ? 3.710   7.064   5.607   1.00 31.05 ? 309 GLY   A CA  1 
ATOM   2400 C C   . GLY   A 1 312 ? 4.057   8.423   5.023   1.00 30.70 ? 309 GLY   A C   1 
ATOM   2401 O O   . GLY   A 1 312 ? 5.215   8.847   5.042   1.00 27.71 ? 309 GLY   A O   1 
ATOM   2402 N N   . LEU   A 1 313 ? 3.053   9.133   4.498   1.00 31.21 ? 310 LEU   A N   1 
ATOM   2403 C CA  . LEU   A 1 313 ? 3.312   10.456  3.933   1.00 31.24 ? 310 LEU   A CA  1 
ATOM   2404 C C   . LEU   A 1 313 ? 3.881   11.408  4.982   1.00 31.09 ? 310 LEU   A C   1 
ATOM   2405 O O   . LEU   A 1 313 ? 4.798   12.191  4.698   1.00 30.04 ? 310 LEU   A O   1 
ATOM   2406 C CB  . LEU   A 1 313 ? 2.027   11.016  3.323   1.00 33.55 ? 310 LEU   A CB  1 
ATOM   2407 C CG  . LEU   A 1 313 ? 1.596   10.218  2.092   1.00 31.78 ? 310 LEU   A CG  1 
ATOM   2408 C CD1 . LEU   A 1 313 ? 0.173   10.520  1.646   1.00 31.09 ? 310 LEU   A CD1 1 
ATOM   2409 C CD2 . LEU   A 1 313 ? 2.569   10.507  0.962   1.00 36.16 ? 310 LEU   A CD2 1 
ATOM   2410 N N   . VAL   A 1 314 ? 3.362   11.350  6.211   1.00 27.10 ? 311 VAL   A N   1 
ATOM   2411 C CA  . VAL   A 1 314 ? 3.873   12.227  7.260   1.00 28.64 ? 311 VAL   A CA  1 
ATOM   2412 C C   . VAL   A 1 314 ? 5.295   11.833  7.625   1.00 34.22 ? 311 VAL   A C   1 
ATOM   2413 O O   . VAL   A 1 314 ? 6.178   12.688  7.770   1.00 32.49 ? 311 VAL   A O   1 
ATOM   2414 C CB  . VAL   A 1 314 ? 2.957   12.204  8.495   1.00 26.59 ? 311 VAL   A CB  1 
ATOM   2415 C CG1 . VAL   A 1 314 ? 3.647   12.896  9.649   1.00 29.19 ? 311 VAL   A CG1 1 
ATOM   2416 C CG2 . VAL   A 1 314 ? 1.615   12.886  8.185   1.00 27.26 ? 311 VAL   A CG2 1 
ATOM   2417 N N   . ARG   A 1 315 ? 5.537   10.525  7.781   1.00 31.87 ? 312 ARG   A N   1 
ATOM   2418 C CA  . ARG   A 1 315 ? 6.867   10.058  8.160   1.00 35.01 ? 312 ARG   A CA  1 
ATOM   2419 C C   . ARG   A 1 315 ? 7.880   10.383  7.071   1.00 37.62 ? 312 ARG   A C   1 
ATOM   2420 O O   . ARG   A 1 315 ? 8.973   10.881  7.356   1.00 41.23 ? 312 ARG   A O   1 
ATOM   2421 C CB  . ARG   A 1 315 ? 6.841   8.557   8.450   1.00 33.62 ? 312 ARG   A CB  1 
ATOM   2422 C CG  . ARG   A 1 315 ? 6.881   8.207   9.927   1.00 42.23 ? 312 ARG   A CG  1 
ATOM   2423 C CD  . ARG   A 1 315 ? 7.173   6.721   10.139  1.00 40.51 ? 312 ARG   A CD  1 
ATOM   2424 N NE  . ARG   A 1 315 ? 6.129   5.904   9.536   1.00 44.58 ? 312 ARG   A NE  1 
ATOM   2425 C CZ  . ARG   A 1 315 ? 5.034   5.520   10.175  1.00 48.67 ? 312 ARG   A CZ  1 
ATOM   2426 N NH1 . ARG   A 1 315 ? 4.843   5.818   11.456  1.00 41.16 ? 312 ARG   A NH1 1 
ATOM   2427 N NH2 . ARG   A 1 315 ? 4.111   4.814   9.517   1.00 51.40 ? 312 ARG   A NH2 1 
ATOM   2428 N N   . ARG   A 1 316 ? 7.529   10.109  5.808   1.00 39.23 ? 313 ARG   A N   1 
ATOM   2429 C CA  . ARG   A 1 316 ? 8.406   10.465  4.697   1.00 39.08 ? 313 ARG   A CA  1 
ATOM   2430 C C   . ARG   A 1 316 ? 8.487   11.969  4.487   1.00 38.08 ? 313 ARG   A C   1 
ATOM   2431 O O   . ARG   A 1 316 ? 9.227   12.419  3.607   1.00 41.50 ? 313 ARG   A O   1 
ATOM   2432 C CB  . ARG   A 1 316 ? 7.938   9.766   3.414   1.00 37.97 ? 313 ARG   A CB  1 
ATOM   2433 C CG  . ARG   A 1 316 ? 7.752   8.263   3.590   1.00 43.54 ? 313 ARG   A CG  1 
ATOM   2434 C CD  . ARG   A 1 316 ? 7.721   7.525   2.266   1.00 43.07 ? 313 ARG   A CD  1 
ATOM   2435 N NE  . ARG   A 1 316 ? 6.676   8.035   1.390   1.00 42.90 ? 313 ARG   A NE  1 
ATOM   2436 C CZ  . ARG   A 1 316 ? 5.434   7.574   1.368   1.00 44.65 ? 313 ARG   A CZ  1 
ATOM   2437 N NH1 . ARG   A 1 316 ? 5.050   6.585   2.162   1.00 42.91 ? 313 ARG   A NH1 1 
ATOM   2438 N NH2 . ARG   A 1 316 ? 4.557   8.116   0.527   1.00 49.18 ? 313 ARG   A NH2 1 
ATOM   2439 N N   . GLN   A 1 317 ? 7.752   12.754  5.272   1.00 38.27 ? 314 GLN   A N   1 
ATOM   2440 C CA  . GLN   A 1 317 ? 7.788   14.212  5.234   1.00 41.42 ? 314 GLN   A CA  1 
ATOM   2441 C C   . GLN   A 1 317 ? 7.208   14.790  3.948   1.00 39.31 ? 314 GLN   A C   1 
ATOM   2442 O O   . GLN   A 1 317 ? 7.464   15.952  3.621   1.00 45.73 ? 314 GLN   A O   1 
ATOM   2443 C CB  . GLN   A 1 317 ? 9.212   14.732  5.436   1.00 43.32 ? 314 GLN   A CB  1 
ATOM   2444 C CG  . GLN   A 1 317 ? 9.899   14.152  6.652   1.00 49.33 ? 314 GLN   A CG  1 
ATOM   2445 C CD  . GLN   A 1 317 ? 11.097  14.974  7.069   1.00 55.53 ? 314 GLN   A CD  1 
ATOM   2446 O OE1 . GLN   A 1 317 ? 12.199  14.805  6.535   1.00 52.17 ? 314 GLN   A OE1 1 
ATOM   2447 N NE2 . GLN   A 1 317 ? 10.885  15.885  8.018   1.00 52.94 ? 314 GLN   A NE2 1 
ATOM   2448 N N   . GLU   A 1 318 ? 6.442   14.005  3.201   1.00 36.23 ? 315 GLU   A N   1 
ATOM   2449 C CA  . GLU   A 1 318 ? 5.748   14.524  2.031   1.00 42.41 ? 315 GLU   A CA  1 
ATOM   2450 C C   . GLU   A 1 318 ? 4.482   15.273  2.403   1.00 42.49 ? 315 GLU   A C   1 
ATOM   2451 O O   . GLU   A 1 318 ? 3.856   15.893  1.533   1.00 40.08 ? 315 GLU   A O   1 
ATOM   2452 C CB  . GLU   A 1 318 ? 5.396   13.388  1.072   1.00 39.25 ? 315 GLU   A CB  1 
ATOM   2453 C CG  . GLU   A 1 318 ? 6.602   12.606  0.565   1.00 46.74 ? 315 GLU   A CG  1 
ATOM   2454 C CD  . GLU   A 1 318 ? 6.203   11.479  -0.356  1.00 49.91 ? 315 GLU   A CD  1 
ATOM   2455 O OE1 . GLU   A 1 318 ? 5.445   11.754  -1.317  1.00 50.14 ? 315 GLU   A OE1 1 
ATOM   2456 O OE2 . GLU   A 1 318 ? 6.633   10.323  -0.114  1.00 51.58 ? 315 GLU   A OE2 1 
ATOM   2457 N N   . LEU   A 1 319 ? 4.095   15.228  3.670   1.00 36.76 ? 316 LEU   A N   1 
ATOM   2458 C CA  . LEU   A 1 319 ? 2.843   15.806  4.107   1.00 32.82 ? 316 LEU   A CA  1 
ATOM   2459 C C   . LEU   A 1 319 ? 3.023   16.266  5.541   1.00 33.19 ? 316 LEU   A C   1 
ATOM   2460 O O   . LEU   A 1 319 ? 3.595   15.546  6.361   1.00 36.36 ? 316 LEU   A O   1 
ATOM   2461 C CB  . LEU   A 1 319 ? 1.712   14.788  3.981   1.00 34.01 ? 316 LEU   A CB  1 
ATOM   2462 C CG  . LEU   A 1 319 ? 0.306   15.320  4.186   1.00 38.63 ? 316 LEU   A CG  1 
ATOM   2463 C CD1 . LEU   A 1 319 ? -0.562  15.003  2.970   1.00 33.11 ? 316 LEU   A CD1 1 
ATOM   2464 C CD2 . LEU   A 1 319 ? -0.265  14.710  5.439   1.00 40.65 ? 316 LEU   A CD2 1 
ATOM   2465 N N   . VAL   A 1 320 ? 2.530   17.460  5.839   1.00 29.13 ? 317 VAL   A N   1 
ATOM   2466 C CA  . VAL   A 1 320 ? 2.844   18.155  7.081   1.00 31.86 ? 317 VAL   A CA  1 
ATOM   2467 C C   . VAL   A 1 320 ? 1.601   18.172  7.948   1.00 33.32 ? 317 VAL   A C   1 
ATOM   2468 O O   . VAL   A 1 320 ? 0.554   18.681  7.531   1.00 33.26 ? 317 VAL   A O   1 
ATOM   2469 C CB  . VAL   A 1 320 ? 3.343   19.581  6.806   1.00 34.90 ? 317 VAL   A CB  1 
ATOM   2470 C CG1 . VAL   A 1 320 ? 3.241   20.406  8.052   1.00 40.91 ? 317 VAL   A CG1 1 
ATOM   2471 C CG2 . VAL   A 1 320 ? 4.775   19.529  6.302   1.00 35.11 ? 317 VAL   A CG2 1 
ATOM   2472 N N   . ALA   A 1 321 ? 1.723   17.643  9.161   1.00 28.32 ? 318 ALA   A N   1 
ATOM   2473 C CA  . ALA   A 1 321 ? 0.617   17.543  10.104  1.00 34.35 ? 318 ALA   A CA  1 
ATOM   2474 C C   . ALA   A 1 321 ? 1.068   18.167  11.425  1.00 36.93 ? 318 ALA   A C   1 
ATOM   2475 O O   . ALA   A 1 321 ? 1.796   17.550  12.207  1.00 39.04 ? 318 ALA   A O   1 
ATOM   2476 C CB  . ALA   A 1 321 ? 0.192   16.084  10.280  1.00 32.79 ? 318 ALA   A CB  1 
ATOM   2477 N N   . HIS   A 1 322 ? 0.654   19.400  11.667  1.00 33.23 ? 319 HIS   A N   1 
ATOM   2478 C CA  . HIS   A 1 322 ? 1.122   20.133  12.827  1.00 39.38 ? 319 HIS   A CA  1 
ATOM   2479 C C   . HIS   A 1 322 ? 0.156   19.982  14.001  1.00 35.50 ? 319 HIS   A C   1 
ATOM   2480 O O   . HIS   A 1 322 ? -1.057  19.844  13.824  1.00 34.88 ? 319 HIS   A O   1 
ATOM   2481 C CB  . HIS   A 1 322 ? 1.299   21.605  12.468  1.00 38.38 ? 319 HIS   A CB  1 
ATOM   2482 C CG  . HIS   A 1 322 ? 2.474   21.856  11.576  1.00 43.57 ? 319 HIS   A CG  1 
ATOM   2483 N ND1 . HIS   A 1 322 ? 2.457   22.787  10.559  1.00 49.55 ? 319 HIS   A ND1 1 
ATOM   2484 C CD2 . HIS   A 1 322 ? 3.705   21.289  11.548  1.00 44.52 ? 319 HIS   A CD2 1 
ATOM   2485 C CE1 . HIS   A 1 322 ? 3.630   22.791  9.949   1.00 50.47 ? 319 HIS   A CE1 1 
ATOM   2486 N NE2 . HIS   A 1 322 ? 4.404   21.888  10.527  1.00 50.29 ? 319 HIS   A NE2 1 
ATOM   2487 N N   . GLU   A 1 323 ? 0.706   20.017  15.207  1.00 31.76 ? 320 GLU   A N   1 
ATOM   2488 C CA  . GLU   A 1 323 ? -0.127  20.033  16.402  1.00 36.51 ? 320 GLU   A CA  1 
ATOM   2489 C C   . GLU   A 1 323 ? 0.417   21.063  17.381  1.00 33.32 ? 320 GLU   A C   1 
ATOM   2490 O O   . GLU   A 1 323 ? 1.612   21.361  17.403  1.00 31.29 ? 320 GLU   A O   1 
ATOM   2491 C CB  . GLU   A 1 323 ? -0.225  18.636  17.059  1.00 36.80 ? 320 GLU   A CB  1 
ATOM   2492 C CG  . GLU   A 1 323 ? 1.077   18.090  17.592  1.00 38.46 ? 320 GLU   A CG  1 
ATOM   2493 C CD  . GLU   A 1 323 ? 1.011   16.609  17.975  1.00 41.15 ? 320 GLU   A CD  1 
ATOM   2494 O OE1 . GLU   A 1 323 ? -0.094  16.048  18.190  1.00 35.27 ? 320 GLU   A OE1 1 
ATOM   2495 O OE2 . GLU   A 1 323 ? 2.093   15.993  18.051  1.00 43.64 ? 320 GLU   A OE2 1 
ATOM   2496 N N   . THR   A 1 324 ? -0.492  21.627  18.158  1.00 29.98 ? 321 THR   A N   1 
ATOM   2497 C CA  . THR   A 1 324 ? -0.203  22.619  19.185  1.00 33.90 ? 321 THR   A CA  1 
ATOM   2498 C C   . THR   A 1 324 ? -0.637  22.014  20.520  1.00 34.74 ? 321 THR   A C   1 
ATOM   2499 O O   . THR   A 1 324 ? -1.829  22.020  20.845  1.00 32.96 ? 321 THR   A O   1 
ATOM   2500 C CB  . THR   A 1 324 ? -0.955  23.919  18.892  1.00 35.33 ? 321 THR   A CB  1 
ATOM   2501 O OG1 . THR   A 1 324 ? -0.620  24.377  17.576  1.00 36.61 ? 321 THR   A OG1 1 
ATOM   2502 C CG2 . THR   A 1 324 ? -0.616  24.994  19.914  1.00 39.24 ? 321 THR   A CG2 1 
ATOM   2503 N N   . VAL   A 1 325 ? 0.320   21.499  21.291  1.00 30.86 ? 322 VAL   A N   1 
ATOM   2504 C CA  . VAL   A 1 325 ? 0.045   20.726  22.509  1.00 33.00 ? 322 VAL   A CA  1 
ATOM   2505 C C   . VAL   A 1 325 ? 0.252   21.645  23.711  1.00 34.94 ? 322 VAL   A C   1 
ATOM   2506 O O   . VAL   A 1 325 ? 1.387   21.937  24.095  1.00 36.11 ? 322 VAL   A O   1 
ATOM   2507 C CB  . VAL   A 1 325 ? 0.936   19.490  22.611  1.00 36.80 ? 322 VAL   A CB  1 
ATOM   2508 C CG1 . VAL   A 1 325 ? 0.626   18.704  23.886  1.00 34.96 ? 322 VAL   A CG1 1 
ATOM   2509 C CG2 . VAL   A 1 325 ? 0.795   18.613  21.386  1.00 35.56 ? 322 VAL   A CG2 1 
ATOM   2510 N N   . GLN   A 1 326 ? -0.851  22.084  24.312  1.00 32.61 ? 323 GLN   A N   1 
ATOM   2511 C CA  . GLN   A 1 326 ? -0.830  22.818  25.573  1.00 38.43 ? 323 GLN   A CA  1 
ATOM   2512 C C   . GLN   A 1 326 ? -0.759  21.851  26.757  1.00 36.94 ? 323 GLN   A C   1 
ATOM   2513 O O   . GLN   A 1 326 ? -1.367  20.775  26.736  1.00 37.01 ? 323 GLN   A O   1 
ATOM   2514 C CB  . GLN   A 1 326 ? -2.083  23.690  25.677  1.00 33.15 ? 323 GLN   A CB  1 
ATOM   2515 C CG  . GLN   A 1 326 ? -2.263  24.408  27.014  1.00 45.52 ? 323 GLN   A CG  1 
ATOM   2516 C CD  . GLN   A 1 326 ? -1.316  25.598  27.177  1.00 52.71 ? 323 GLN   A CD  1 
ATOM   2517 O OE1 . GLN   A 1 326 ? -0.466  25.616  28.074  1.00 49.88 ? 323 GLN   A OE1 1 
ATOM   2518 N NE2 . GLN   A 1 326 ? -1.462  26.596  26.303  1.00 55.24 ? 323 GLN   A NE2 1 
ATOM   2519 N N   . ASP   A 1 327 ? -0.025  22.236  27.798  1.00 39.43 ? 324 ASP   A N   1 
ATOM   2520 C CA  . ASP   A 1 327 ? 0.137   21.405  28.988  1.00 33.20 ? 324 ASP   A CA  1 
ATOM   2521 C C   . ASP   A 1 327 ? -0.803  21.851  30.104  1.00 36.33 ? 324 ASP   A C   1 
ATOM   2522 O O   . ASP   A 1 327 ? -0.969  23.051  30.356  1.00 35.57 ? 324 ASP   A O   1 
ATOM   2523 C CB  . ASP   A 1 327 ? 1.581   21.443  29.497  1.00 36.26 ? 324 ASP   A CB  1 
ATOM   2524 C CG  . ASP   A 1 327 ? 2.518   20.542  28.700  1.00 43.63 ? 324 ASP   A CG  1 
ATOM   2525 O OD1 . ASP   A 1 327 ? 2.055   19.846  27.778  1.00 42.32 ? 324 ASP   A OD1 1 
ATOM   2526 O OD2 . ASP   A 1 327 ? 3.733   20.515  29.009  1.00 44.79 ? 324 ASP   A OD2 1 
ATOM   2527 N N   . GLY   A 1 328 ? -1.418  20.880  30.776  1.00 36.64 ? 325 GLY   A N   1 
ATOM   2528 C CA  . GLY   A 1 328 ? -2.114  21.168  32.017  1.00 33.44 ? 325 GLY   A CA  1 
ATOM   2529 C C   . GLY   A 1 328 ? -3.624  21.097  31.967  1.00 32.22 ? 325 GLY   A C   1 
ATOM   2530 O O   . GLY   A 1 328 ? -4.268  21.874  31.258  1.00 35.40 ? 325 GLY   A O   1 
ATOM   2531 N N   . PHE   A 1 329 ? -4.198  20.191  32.768  1.00 33.79 ? 326 PHE   A N   1 
ATOM   2532 C CA  . PHE   A 1 329 ? -5.647  20.009  32.788  1.00 33.23 ? 326 PHE   A CA  1 
ATOM   2533 C C   . PHE   A 1 329 ? -6.368  21.317  33.051  1.00 33.87 ? 326 PHE   A C   1 
ATOM   2534 O O   . PHE   A 1 329 ? -7.442  21.572  32.490  1.00 30.93 ? 326 PHE   A O   1 
ATOM   2535 C CB  . PHE   A 1 329 ? -6.031  18.970  33.847  1.00 30.62 ? 326 PHE   A CB  1 
ATOM   2536 C CG  . PHE   A 1 329 ? -7.502  18.640  33.874  1.00 30.41 ? 326 PHE   A CG  1 
ATOM   2537 C CD1 . PHE   A 1 329 ? -8.024  17.656  33.046  1.00 26.03 ? 326 PHE   A CD1 1 
ATOM   2538 C CD2 . PHE   A 1 329 ? -8.361  19.301  34.734  1.00 28.88 ? 326 PHE   A CD2 1 
ATOM   2539 C CE1 . PHE   A 1 329 ? -9.383  17.359  33.064  1.00 25.65 ? 326 PHE   A CE1 1 
ATOM   2540 C CE2 . PHE   A 1 329 ? -9.719  19.006  34.758  1.00 29.25 ? 326 PHE   A CE2 1 
ATOM   2541 C CZ  . PHE   A 1 329 ? -10.225 18.024  33.917  1.00 27.97 ? 326 PHE   A CZ  1 
ATOM   2542 N N   . GLU   A 1 330 ? -5.787  22.170  33.897  1.00 32.68 ? 327 GLU   A N   1 
ATOM   2543 C CA  . GLU   A 1 330 ? -6.444  23.420  34.247  1.00 36.98 ? 327 GLU   A CA  1 
ATOM   2544 C C   . GLU   A 1 330 ? -6.570  24.366  33.057  1.00 34.73 ? 327 GLU   A C   1 
ATOM   2545 O O   . GLU   A 1 330 ? -7.394  25.282  33.103  1.00 35.17 ? 327 GLU   A O   1 
ATOM   2546 C CB  . GLU   A 1 330 ? -5.691  24.105  35.400  1.00 37.84 ? 327 GLU   A CB  1 
ATOM   2547 C CG  . GLU   A 1 330 ? -4.325  24.670  35.032  1.00 33.20 ? 327 GLU   A CG  1 
ATOM   2548 C CD  . GLU   A 1 330 ? -3.190  23.688  35.248  1.00 44.41 ? 327 GLU   A CD  1 
ATOM   2549 O OE1 . GLU   A 1 330 ? -3.432  22.452  35.268  1.00 44.00 ? 327 GLU   A OE1 1 
ATOM   2550 O OE2 . GLU   A 1 330 ? -2.044  24.155  35.404  1.00 43.44 ? 327 GLU   A OE2 1 
ATOM   2551 N N   . HIS   A 1 331 ? -5.797  24.158  31.991  1.00 32.84 ? 328 HIS   A N   1 
ATOM   2552 C CA  . HIS   A 1 331 ? -5.788  25.067  30.849  1.00 29.84 ? 328 HIS   A CA  1 
ATOM   2553 C C   . HIS   A 1 331 ? -6.602  24.570  29.654  1.00 31.58 ? 328 HIS   A C   1 
ATOM   2554 O O   . HIS   A 1 331 ? -6.483  25.136  28.561  1.00 32.67 ? 328 HIS   A O   1 
ATOM   2555 C CB  . HIS   A 1 331 ? -4.342  25.338  30.429  1.00 36.81 ? 328 HIS   A CB  1 
ATOM   2556 C CG  . HIS   A 1 331 ? -3.514  25.943  31.518  1.00 38.45 ? 328 HIS   A CG  1 
ATOM   2557 N ND1 . HIS   A 1 331 ? -3.870  27.109  32.162  1.00 41.47 ? 328 HIS   A ND1 1 
ATOM   2558 C CD2 . HIS   A 1 331 ? -2.362  25.531  32.098  1.00 37.96 ? 328 HIS   A CD2 1 
ATOM   2559 C CE1 . HIS   A 1 331 ? -2.963  27.398  33.079  1.00 38.83 ? 328 HIS   A CE1 1 
ATOM   2560 N NE2 . HIS   A 1 331 ? -2.044  26.450  33.067  1.00 40.09 ? 328 HIS   A NE2 1 
ATOM   2561 N N   . ILE   A 1 332 ? -7.436  23.539  29.830  1.00 30.77 ? 329 ILE   A N   1 
ATOM   2562 C CA  . ILE   A 1 332 ? -8.243  23.040  28.709  1.00 31.69 ? 329 ILE   A CA  1 
ATOM   2563 C C   . ILE   A 1 332 ? -9.190  24.106  28.184  1.00 32.01 ? 329 ILE   A C   1 
ATOM   2564 O O   . ILE   A 1 332 ? -9.226  24.326  26.956  1.00 30.28 ? 329 ILE   A O   1 
ATOM   2565 C CB  . ILE   A 1 332 ? -8.975  21.752  29.119  1.00 28.96 ? 329 ILE   A CB  1 
ATOM   2566 C CG1 . ILE   A 1 332 ? -7.966  20.632  29.365  1.00 24.41 ? 329 ILE   A CG1 1 
ATOM   2567 C CG2 . ILE   A 1 332 ? -10.007 21.342  28.062  1.00 29.90 ? 329 ILE   A CG2 1 
ATOM   2568 C CD1 . ILE   A 1 332 ? -8.617  19.352  29.893  1.00 29.01 ? 329 ILE   A CD1 1 
ATOM   2569 N N   . PRO   A 1 333 ? -9.980  24.793  29.008  1.00 32.67 ? 330 PRO   A N   1 
ATOM   2570 C CA  . PRO   A 1 333 ? -10.859 25.841  28.464  1.00 30.09 ? 330 PRO   A CA  1 
ATOM   2571 C C   . PRO   A 1 333 ? -10.113 26.959  27.742  1.00 31.73 ? 330 PRO   A C   1 
ATOM   2572 O O   . PRO   A 1 333 ? -10.606 27.476  26.736  1.00 32.24 ? 330 PRO   A O   1 
ATOM   2573 C CB  . PRO   A 1 333 ? -11.603 26.338  29.711  1.00 34.98 ? 330 PRO   A CB  1 
ATOM   2574 C CG  . PRO   A 1 333 ? -11.616 25.134  30.632  1.00 29.41 ? 330 PRO   A CG  1 
ATOM   2575 C CD  . PRO   A 1 333 ? -10.271 24.495  30.426  1.00 28.06 ? 330 PRO   A CD  1 
ATOM   2576 N N   . ALA   A 1 334 ? -8.940  27.358  28.232  1.00 31.97 ? 331 ALA   A N   1 
ATOM   2577 C CA  . ALA   A 1 334 ? -8.172  28.392  27.546  1.00 34.93 ? 331 ALA   A CA  1 
ATOM   2578 C C   . ALA   A 1 334 ? -7.703  27.911  26.175  1.00 35.61 ? 331 ALA   A C   1 
ATOM   2579 O O   . ALA   A 1 334 ? -7.761  28.660  25.191  1.00 34.97 ? 331 ALA   A O   1 
ATOM   2580 C CB  . ALA   A 1 334 ? -6.978  28.812  28.404  1.00 35.14 ? 331 ALA   A CB  1 
ATOM   2581 N N   . ALA   A 1 335 ? -7.227  26.670  26.092  1.00 30.12 ? 332 ALA   A N   1 
ATOM   2582 C CA  . ALA   A 1 335 ? -6.821  26.128  24.799  1.00 33.28 ? 332 ALA   A CA  1 
ATOM   2583 C C   . ALA   A 1 335 ? -7.999  26.117  23.835  1.00 31.85 ? 332 ALA   A C   1 
ATOM   2584 O O   . ALA   A 1 335 ? -7.886  26.571  22.689  1.00 34.04 ? 332 ALA   A O   1 
ATOM   2585 C CB  . ALA   A 1 335 ? -6.235  24.728  24.980  1.00 31.08 ? 332 ALA   A CB  1 
ATOM   2586 N N   . TYR   A 1 336 ? -9.153  25.635  24.302  1.00 27.37 ? 333 TYR   A N   1 
ATOM   2587 C CA  . TYR   A 1 336 ? -10.370 25.645  23.499  1.00 31.01 ? 333 TYR   A CA  1 
ATOM   2588 C C   . TYR   A 1 336 ? -10.691 27.044  22.997  1.00 34.64 ? 333 TYR   A C   1 
ATOM   2589 O O   . TYR   A 1 336 ? -11.129 27.223  21.853  1.00 29.58 ? 333 TYR   A O   1 
ATOM   2590 C CB  . TYR   A 1 336 ? -11.515 25.109  24.347  1.00 25.87 ? 333 TYR   A CB  1 
ATOM   2591 C CG  . TYR   A 1 336 ? -12.896 25.118  23.749  1.00 25.88 ? 333 TYR   A CG  1 
ATOM   2592 C CD1 . TYR   A 1 336 ? -13.203 24.375  22.619  1.00 24.69 ? 333 TYR   A CD1 1 
ATOM   2593 C CD2 . TYR   A 1 336 ? -13.933 25.805  24.388  1.00 27.58 ? 333 TYR   A CD2 1 
ATOM   2594 C CE1 . TYR   A 1 336 ? -14.491 24.343  22.115  1.00 25.74 ? 333 TYR   A CE1 1 
ATOM   2595 C CE2 . TYR   A 1 336 ? -15.211 25.786  23.897  1.00 27.28 ? 333 TYR   A CE2 1 
ATOM   2596 C CZ  . TYR   A 1 336 ? -15.496 25.058  22.763  1.00 31.21 ? 333 TYR   A CZ  1 
ATOM   2597 O OH  . TYR   A 1 336 ? -16.789 25.041  22.296  1.00 27.71 ? 333 TYR   A OH  1 
ATOM   2598 N N   . GLN   A 1 337 ? -10.484 28.048  23.855  1.00 34.77 ? 334 GLN   A N   1 
ATOM   2599 C CA  . GLN   A 1 337 ? -10.826 29.418  23.504  1.00 34.72 ? 334 GLN   A CA  1 
ATOM   2600 C C   . GLN   A 1 337 ? -10.007 29.914  22.329  1.00 28.46 ? 334 GLN   A C   1 
ATOM   2601 O O   . GLN   A 1 337 ? -10.501 30.723  21.536  1.00 34.72 ? 334 GLN   A O   1 
ATOM   2602 C CB  . GLN   A 1 337 ? -10.618 30.341  24.705  1.00 34.65 ? 334 GLN   A CB  1 
ATOM   2603 C CG  . GLN   A 1 337 ? -11.122 31.736  24.467  1.00 33.02 ? 334 GLN   A CG  1 
ATOM   2604 C CD  . GLN   A 1 337 ? -12.622 31.792  24.548  1.00 35.21 ? 334 GLN   A CD  1 
ATOM   2605 O OE1 . GLN   A 1 337 ? -13.204 31.461  25.580  1.00 39.06 ? 334 GLN   A OE1 1 
ATOM   2606 N NE2 . GLN   A 1 337 ? -13.266 32.203  23.461  1.00 36.82 ? 334 GLN   A NE2 1 
ATOM   2607 N N   . THR   A 1 338 ? -8.756  29.459  22.204  1.00 30.70 ? 335 THR   A N   1 
ATOM   2608 C CA  . THR   A 1 338 ? -7.923  29.928  21.103  1.00 35.42 ? 335 THR   A CA  1 
ATOM   2609 C C   . THR   A 1 338 ? -8.495  29.551  19.739  1.00 41.18 ? 335 THR   A C   1 
ATOM   2610 O O   . THR   A 1 338 ? -8.130  30.175  18.736  1.00 36.50 ? 335 THR   A O   1 
ATOM   2611 C CB  . THR   A 1 338 ? -6.497  29.381  21.216  1.00 37.74 ? 335 THR   A CB  1 
ATOM   2612 O OG1 . THR   A 1 338 ? -6.498  27.968  20.983  1.00 34.17 ? 335 THR   A OG1 1 
ATOM   2613 C CG2 . THR   A 1 338 ? -5.899  29.676  22.591  1.00 33.71 ? 335 THR   A CG2 1 
ATOM   2614 N N   . LEU   A 1 339 ? -9.364  28.536  19.669  1.00 34.66 ? 336 LEU   A N   1 
ATOM   2615 C CA  . LEU   A 1 339 ? -9.948  28.165  18.382  1.00 33.35 ? 336 LEU   A CA  1 
ATOM   2616 C C   . LEU   A 1 339 ? -10.821 29.280  17.827  1.00 35.24 ? 336 LEU   A C   1 
ATOM   2617 O O   . LEU   A 1 339 ? -10.956 29.408  16.614  1.00 30.01 ? 336 LEU   A O   1 
ATOM   2618 C CB  . LEU   A 1 339 ? -10.783 26.884  18.508  1.00 26.34 ? 336 LEU   A CB  1 
ATOM   2619 C CG  . LEU   A 1 339 ? -10.117 25.600  19.015  1.00 27.70 ? 336 LEU   A CG  1 
ATOM   2620 C CD1 . LEU   A 1 339 ? -11.154 24.469  19.033  1.00 28.34 ? 336 LEU   A CD1 1 
ATOM   2621 C CD2 . LEU   A 1 339 ? -8.933  25.220  18.145  1.00 31.19 ? 336 LEU   A CD2 1 
ATOM   2622 N N   . PHE   A 1 340 ? -11.428 30.087  18.692  1.00 34.97 ? 337 PHE   A N   1 
ATOM   2623 C CA  . PHE   A 1 340 ? -12.433 31.051  18.268  1.00 39.57 ? 337 PHE   A CA  1 
ATOM   2624 C C   . PHE   A 1 340 ? -11.958 32.486  18.264  1.00 44.20 ? 337 PHE   A C   1 
ATOM   2625 O O   . PHE   A 1 340 ? -12.470 33.288  17.484  1.00 46.74 ? 337 PHE   A O   1 
ATOM   2626 C CB  . PHE   A 1 340 ? -13.664 30.978  19.171  1.00 34.83 ? 337 PHE   A CB  1 
ATOM   2627 C CG  . PHE   A 1 340 ? -14.286 29.638  19.217  1.00 37.19 ? 337 PHE   A CG  1 
ATOM   2628 C CD1 . PHE   A 1 340 ? -13.843 28.692  20.128  1.00 30.51 ? 337 PHE   A CD1 1 
ATOM   2629 C CD2 . PHE   A 1 340 ? -15.302 29.313  18.344  1.00 35.12 ? 337 PHE   A CD2 1 
ATOM   2630 C CE1 . PHE   A 1 340 ? -14.413 27.442  20.174  1.00 33.63 ? 337 PHE   A CE1 1 
ATOM   2631 C CE2 . PHE   A 1 340 ? -15.887 28.061  18.385  1.00 35.89 ? 337 PHE   A CE2 1 
ATOM   2632 C CZ  . PHE   A 1 340 ? -15.436 27.123  19.307  1.00 31.67 ? 337 PHE   A CZ  1 
ATOM   2633 N N   . SER   A 1 341 ? -11.009 32.823  19.126  1.00 46.56 ? 338 SER   A N   1 
ATOM   2634 C CA  . SER   A 1 341 ? -10.681 34.208  19.405  1.00 51.93 ? 338 SER   A CA  1 
ATOM   2635 C C   . SER   A 1 341 ? -9.211  34.540  19.238  1.00 52.79 ? 338 SER   A C   1 
ATOM   2636 O O   . SER   A 1 341 ? -8.878  35.727  19.138  1.00 63.50 ? 338 SER   A O   1 
ATOM   2637 C CB  . SER   A 1 341 ? -11.112 34.574  20.836  1.00 51.05 ? 338 SER   A CB  1 
ATOM   2638 O OG  . SER   A 1 341 ? -12.431 34.123  21.105  1.00 45.30 ? 338 SER   A OG  1 
ATOM   2639 N N   . ALA   A 1 342 ? -8.323  33.552  19.213  1.00 50.62 ? 339 ALA   A N   1 
ATOM   2640 C CA  . ALA   A 1 342 ? -6.898  33.813  19.088  1.00 52.61 ? 339 ALA   A CA  1 
ATOM   2641 C C   . ALA   A 1 342 ? -6.197  32.602  18.498  1.00 53.45 ? 339 ALA   A C   1 
ATOM   2642 O O   . ALA   A 1 342 ? -5.453  31.909  19.203  1.00 53.31 ? 339 ALA   A O   1 
ATOM   2643 C CB  . ALA   A 1 342 ? -6.295  34.172  20.450  1.00 60.05 ? 339 ALA   A CB  1 
ATOM   2644 N N   . SER   A 1 343 ? -6.429  32.337  17.209  1.00 56.92 ? 340 SER   A N   1 
ATOM   2645 C CA  . SER   A 1 343 ? -5.860  31.177  16.528  1.00 52.52 ? 340 SER   A CA  1 
ATOM   2646 C C   . SER   A 1 343 ? -4.559  31.488  15.788  1.00 56.58 ? 340 SER   A C   1 
ATOM   2647 O O   . SER   A 1 343 ? -3.996  30.584  15.157  1.00 53.30 ? 340 SER   A O   1 
ATOM   2648 C CB  . SER   A 1 343 ? -6.887  30.580  15.552  1.00 51.94 ? 340 SER   A CB  1 
ATOM   2649 O OG  . SER   A 1 343 ? -7.586  31.588  14.821  1.00 53.53 ? 340 SER   A OG  1 
ATOM   2650 N N   . GLU   A 1 344 ? -4.081  32.724  15.852  1.00 54.30 ? 341 GLU   A N   1 
ATOM   2651 C CA  . GLU   A 1 344 ? -2.889  33.105  15.120  1.00 54.52 ? 341 GLU   A CA  1 
ATOM   2652 C C   . GLU   A 1 344 ? -1.711  32.187  15.369  1.00 57.39 ? 341 GLU   A C   1 
ATOM   2653 O O   . GLU   A 1 344 ? -0.985  31.850  14.448  1.00 54.40 ? 341 GLU   A O   1 
ATOM   2654 C CB  . GLU   A 1 344 ? -2.500  34.529  15.489  1.00 57.17 ? 341 GLU   A CB  1 
ATOM   2655 C CG  . GLU   A 1 344 ? -3.371  35.593  14.848  1.00 60.37 ? 341 GLU   A CG  1 
ATOM   2656 C CD  . GLU   A 1 344 ? -4.804  35.601  15.354  1.00 62.85 ? 341 GLU   A CD  1 
ATOM   2657 O OE1 . GLU   A 1 344 ? -5.069  35.157  16.492  1.00 63.17 ? 341 GLU   A OE1 1 
ATOM   2658 O OE2 . GLU   A 1 344 ? -5.671  36.061  14.596  1.00 65.21 ? 341 GLU   A OE2 1 
ATOM   2659 N N   . SER   A 1 345 ? -1.492  31.825  16.617  1.00 57.08 ? 342 SER   A N   1 
ATOM   2660 C CA  . SER   A 1 345 ? -0.395  30.938  16.971  1.00 55.65 ? 342 SER   A CA  1 
ATOM   2661 C C   . SER   A 1 345 ? -0.761  29.467  16.851  1.00 54.94 ? 342 SER   A C   1 
ATOM   2662 O O   . SER   A 1 345 ? 0.143   28.621  16.859  1.00 55.63 ? 342 SER   A O   1 
ATOM   2663 C CB  . SER   A 1 345 ? 0.089   31.227  18.395  1.00 60.72 ? 342 SER   A CB  1 
ATOM   2664 O OG  . SER   A 1 345 ? 0.681   32.512  18.471  1.00 67.86 ? 342 SER   A OG  1 
ATOM   2665 N N   . ASN   A 1 346 ? -2.049  29.141  16.732  1.00 51.57 ? 343 ASN   A N   1 
ATOM   2666 C CA  . ASN   A 1 346 ? -2.461  27.750  16.576  1.00 49.34 ? 343 ASN   A CA  1 
ATOM   2667 C C   . ASN   A 1 346 ? -2.027  27.226  15.215  1.00 49.83 ? 343 ASN   A C   1 
ATOM   2668 O O   . ASN   A 1 346 ? -2.480  27.716  14.173  1.00 49.57 ? 343 ASN   A O   1 
ATOM   2669 C CB  . ASN   A 1 346 ? -3.973  27.605  16.738  1.00 45.40 ? 343 ASN   A CB  1 
ATOM   2670 C CG  . ASN   A 1 346 ? -4.417  27.737  18.180  1.00 45.81 ? 343 ASN   A CG  1 
ATOM   2671 O OD1 . ASN   A 1 346 ? -3.597  27.703  19.101  1.00 45.82 ? 343 ASN   A OD1 1 
ATOM   2672 N ND2 . ASN   A 1 346 ? -5.721  27.883  18.387  1.00 40.02 ? 343 ASN   A ND2 1 
ATOM   2673 N N   . ARG   A 1 347 ? -1.155  26.229  15.225  1.00 44.89 ? 344 ARG   A N   1 
ATOM   2674 C CA  . ARG   A 1 347 ? -0.806  25.480  14.033  1.00 46.49 ? 344 ARG   A CA  1 
ATOM   2675 C C   . ARG   A 1 347 ? -1.468  24.118  14.127  1.00 46.03 ? 344 ARG   A C   1 
ATOM   2676 O O   . ARG   A 1 347 ? -1.160  23.338  15.041  1.00 42.35 ? 344 ARG   A O   1 
ATOM   2677 C CB  . ARG   A 1 347 ? 0.710   25.339  13.882  1.00 44.54 ? 344 ARG   A CB  1 
ATOM   2678 C CG  . ARG   A 1 347 ? 1.398   26.643  13.565  1.00 49.89 ? 344 ARG   A CG  1 
ATOM   2679 C CD  . ARG   A 1 347 ? 0.785   27.273  12.331  1.00 52.16 ? 344 ARG   A CD  1 
ATOM   2680 N NE  . ARG   A 1 347 ? 1.439   28.522  11.953  1.00 53.89 ? 344 ARG   A NE  1 
ATOM   2681 C CZ  . ARG   A 1 347 ? 0.973   29.729  12.244  1.00 50.36 ? 344 ARG   A CZ  1 
ATOM   2682 N NH1 . ARG   A 1 347 ? -0.138  29.891  12.947  1.00 53.58 ? 344 ARG   A NH1 1 
ATOM   2683 N NH2 . ARG   A 1 347 ? 1.633   30.799  11.813  1.00 53.21 ? 344 ARG   A NH2 1 
ATOM   2684 N N   . GLY   A 1 348 ? -2.388  23.847  13.200  1.00 40.82 ? 345 GLY   A N   1 
ATOM   2685 C CA  . GLY   A 1 348 ? -2.937  22.511  13.096  1.00 36.68 ? 345 GLY   A CA  1 
ATOM   2686 C C   . GLY   A 1 348 ? -3.821  22.169  14.282  1.00 30.22 ? 345 GLY   A C   1 
ATOM   2687 O O   . GLY   A 1 348 ? -4.621  22.988  14.752  1.00 32.70 ? 345 GLY   A O   1 
ATOM   2688 N N   . LYS   A 1 349 ? -3.654  20.945  14.780  1.00 28.70 ? 346 LYS   A N   1 
ATOM   2689 C CA  . LYS   A 1 349 ? -4.528  20.394  15.802  1.00 31.32 ? 346 LYS   A CA  1 
ATOM   2690 C C   . LYS   A 1 349 ? -4.148  20.912  17.187  1.00 32.00 ? 346 LYS   A C   1 
ATOM   2691 O O   . LYS   A 1 349 ? -3.003  20.769  17.625  1.00 30.51 ? 346 LYS   A O   1 
ATOM   2692 C CB  . LYS   A 1 349 ? -4.451  18.867  15.794  1.00 28.59 ? 346 LYS   A CB  1 
ATOM   2693 C CG  . LYS   A 1 349 ? -5.515  18.215  16.670  1.00 27.71 ? 346 LYS   A CG  1 
ATOM   2694 C CD  . LYS   A 1 349 ? -6.883  18.420  16.020  1.00 32.11 ? 346 LYS   A CD  1 
ATOM   2695 C CE  . LYS   A 1 349 ? -8.011  18.071  16.950  1.00 30.80 ? 346 LYS   A CE  1 
ATOM   2696 N NZ  . LYS   A 1 349 ? -8.180  19.096  17.983  1.00 27.53 ? 346 LYS   A NZ  1 
ATOM   2697 N N   . VAL   A 1 350 ? -5.121  21.475  17.891  1.00 26.30 ? 347 VAL   A N   1 
ATOM   2698 C CA  . VAL   A 1 350 ? -4.927  21.934  19.258  1.00 29.84 ? 347 VAL   A CA  1 
ATOM   2699 C C   . VAL   A 1 350 ? -5.371  20.829  20.208  1.00 26.52 ? 347 VAL   A C   1 
ATOM   2700 O O   . VAL   A 1 350 ? -6.469  20.270  20.059  1.00 25.28 ? 347 VAL   A O   1 
ATOM   2701 C CB  . VAL   A 1 350 ? -5.694  23.242  19.505  1.00 26.65 ? 347 VAL   A CB  1 
ATOM   2702 C CG1 . VAL   A 1 350 ? -5.435  23.759  20.905  1.00 28.49 ? 347 VAL   A CG1 1 
ATOM   2703 C CG2 . VAL   A 1 350 ? -5.285  24.289  18.429  1.00 34.75 ? 347 VAL   A CG2 1 
ATOM   2704 N N   . LEU   A 1 351 ? -4.512  20.485  21.163  1.00 24.78 ? 348 LEU   A N   1 
ATOM   2705 C CA  . LEU   A 1 351 ? -4.865  19.492  22.169  1.00 27.13 ? 348 LEU   A CA  1 
ATOM   2706 C C   . LEU   A 1 351 ? -4.130  19.828  23.464  1.00 31.38 ? 348 LEU   A C   1 
ATOM   2707 O O   . LEU   A 1 351 ? -3.237  20.675  23.493  1.00 31.18 ? 348 LEU   A O   1 
ATOM   2708 C CB  . LEU   A 1 351 ? -4.560  18.063  21.682  1.00 28.26 ? 348 LEU   A CB  1 
ATOM   2709 C CG  . LEU   A 1 351 ? -3.124  17.583  21.462  1.00 35.65 ? 348 LEU   A CG  1 
ATOM   2710 C CD1 . LEU   A 1 351 ? -3.097  16.178  20.862  1.00 35.31 ? 348 LEU   A CD1 1 
ATOM   2711 C CD2 . LEU   A 1 351 ? -2.417  18.503  20.529  1.00 39.70 ? 348 LEU   A CD2 1 
ATOM   2712 N N   . VAL   A 1 352 ? -4.503  19.144  24.542  1.00 26.17 ? 349 VAL   A N   1 
ATOM   2713 C CA  . VAL   A 1 352 ? -3.938  19.408  25.861  1.00 27.45 ? 349 VAL   A CA  1 
ATOM   2714 C C   . VAL   A 1 352 ? -3.319  18.124  26.388  1.00 30.04 ? 349 VAL   A C   1 
ATOM   2715 O O   . VAL   A 1 352 ? -3.977  17.076  26.409  1.00 28.40 ? 349 VAL   A O   1 
ATOM   2716 C CB  . VAL   A 1 352 ? -5.005  19.950  26.828  1.00 25.11 ? 349 VAL   A CB  1 
ATOM   2717 C CG1 . VAL   A 1 352 ? -4.429  20.107  28.233  1.00 34.25 ? 349 VAL   A CG1 1 
ATOM   2718 C CG2 . VAL   A 1 352 ? -5.533  21.275  26.319  1.00 27.54 ? 349 VAL   A CG2 1 
ATOM   2719 N N   . ARG   A 1 353 ? -2.048  18.201  26.790  1.00 26.16 ? 350 ARG   A N   1 
ATOM   2720 C CA  . ARG   A 1 353 ? -1.381  17.109  27.476  1.00 26.66 ? 350 ARG   A CA  1 
ATOM   2721 C C   . ARG   A 1 353 ? -1.619  17.268  28.976  1.00 31.61 ? 350 ARG   A C   1 
ATOM   2722 O O   . ARG   A 1 353 ? -1.219  18.277  29.562  1.00 30.83 ? 350 ARG   A O   1 
ATOM   2723 C CB  . ARG   A 1 353 ? 0.115   17.088  27.163  1.00 29.59 ? 350 ARG   A CB  1 
ATOM   2724 C CG  . ARG   A 1 353 ? 0.895   16.064  28.002  1.00 29.85 ? 350 ARG   A CG  1 
ATOM   2725 C CD  . ARG   A 1 353 ? 2.320   15.854  27.496  1.00 34.78 ? 350 ARG   A CD  1 
ATOM   2726 N NE  . ARG   A 1 353 ? 3.155   17.020  27.741  1.00 34.95 ? 350 ARG   A NE  1 
ATOM   2727 C CZ  . ARG   A 1 353 ? 4.469   17.066  27.555  1.00 41.90 ? 350 ARG   A CZ  1 
ATOM   2728 N NH1 . ARG   A 1 353 ? 5.150   16.006  27.138  1.00 35.36 ? 350 ARG   A NH1 1 
ATOM   2729 N NH2 . ARG   A 1 353 ? 5.120   18.206  27.792  1.00 40.64 ? 350 ARG   A NH2 1 
ATOM   2730 N N   . VAL   A 1 354 ? -2.305  16.295  29.576  1.00 29.01 ? 351 VAL   A N   1 
ATOM   2731 C CA  . VAL   A 1 354 ? -2.647  16.335  30.996  1.00 34.33 ? 351 VAL   A CA  1 
ATOM   2732 C C   . VAL   A 1 354 ? -1.489  15.804  31.830  1.00 40.76 ? 351 VAL   A C   1 
ATOM   2733 O O   . VAL   A 1 354 ? -0.978  16.510  32.695  1.00 45.76 ? 351 VAL   A O   1 
ATOM   2734 C CB  . VAL   A 1 354 ? -3.922  15.537  31.305  1.00 31.94 ? 351 VAL   A CB  1 
ATOM   2735 C CG1 . VAL   A 1 354 ? -4.095  15.423  32.817  1.00 40.95 ? 351 VAL   A CG1 1 
ATOM   2736 C CG2 . VAL   A 1 354 ? -5.143  16.193  30.670  1.00 30.57 ? 351 VAL   A CG2 1 
ATOM   2737 N N   . LEU   B 1 1   ? -33.078 27.645  -55.639 1.00 50.67 ? -2  LEU   B N   1 
ATOM   2738 C CA  . LEU   B 1 1   ? -33.913 26.541  -55.953 1.00 48.64 ? -2  LEU   B CA  1 
ATOM   2739 C C   . LEU   B 1 1   ? -35.311 26.905  -55.442 1.00 49.22 ? -2  LEU   B C   1 
ATOM   2740 O O   . LEU   B 1 1   ? -36.294 26.436  -55.999 1.00 48.70 ? -2  LEU   B O   1 
ATOM   2741 C CB  . LEU   B 1 1   ? -33.309 25.272  -55.358 1.00 46.93 ? -2  LEU   B CB  1 
ATOM   2742 C CG  . LEU   B 1 1   ? -32.532 24.435  -56.369 1.00 53.83 ? -2  LEU   B CG  1 
ATOM   2743 C CD1 . LEU   B 1 1   ? -31.332 23.748  -55.736 1.00 48.97 ? -2  LEU   B CD1 1 
ATOM   2744 C CD2 . LEU   B 1 1   ? -33.446 23.425  -57.046 1.00 52.84 ? -2  LEU   B CD2 1 
ATOM   2745 N N   . GLY   B 1 2   ? -35.401 27.763  -54.419 1.00 40.24 ? -1  GLY   B N   1 
ATOM   2746 C CA  . GLY   B 1 2   ? -36.682 28.220  -53.937 1.00 36.81 ? -1  GLY   B CA  1 
ATOM   2747 C C   . GLY   B 1 2   ? -36.907 28.675  -52.499 1.00 41.20 ? -1  GLY   B C   1 
ATOM   2748 O O   . GLY   B 1 2   ? -35.968 28.831  -51.736 1.00 31.23 ? -1  GLY   B O   1 
ATOM   2749 N N   . SER   B 1 3   ? -38.174 28.892  -52.148 1.00 34.48 ? 0   SER   B N   1 
ATOM   2750 C CA  . SER   B 1 3   ? -38.500 29.258  -50.773 1.00 34.23 ? 0   SER   B CA  1 
ATOM   2751 C C   . SER   B 1 3   ? -39.846 28.648  -50.422 1.00 33.26 ? 0   SER   B C   1 
ATOM   2752 O O   . SER   B 1 3   ? -40.595 28.183  -51.291 1.00 33.39 ? 0   SER   B O   1 
ATOM   2753 C CB  . SER   B 1 3   ? -38.536 30.778  -50.573 1.00 31.68 ? 0   SER   B CB  1 
ATOM   2754 O OG  . SER   B 1 3   ? -39.635 31.361  -51.252 1.00 34.58 ? 0   SER   B OG  1 
ATOM   2755 N N   . MET   B 1 4   ? -40.154 28.658  -49.135 1.00 27.99 ? 1   MET   B N   1 
ATOM   2756 C CA  . MET   B 1 4   ? -41.483 28.282  -48.702 1.00 28.12 ? 1   MET   B CA  1 
ATOM   2757 C C   . MET   B 1 4   ? -41.893 29.132  -47.507 1.00 28.52 ? 1   MET   B C   1 
ATOM   2758 O O   . MET   B 1 4   ? -41.068 29.491  -46.657 1.00 25.54 ? 1   MET   B O   1 
ATOM   2759 C CB  . MET   B 1 4   ? -41.571 26.777  -48.382 1.00 30.38 ? 1   MET   B CB  1 
ATOM   2760 C CG  . MET   B 1 4   ? -40.981 26.327  -47.066 1.00 37.83 ? 1   MET   B CG  1 
ATOM   2761 S SD  . MET   B 1 4   ? -41.548 24.650  -46.669 1.00 46.80 ? 1   MET   B SD  1 
ATOM   2762 C CE  . MET   B 1 4   ? -41.529 23.856  -48.284 1.00 32.61 ? 1   MET   B CE  1 
ATOM   2763 N N   . LYS   B 1 5   ? -43.168 29.476  -47.479 1.00 24.51 ? 2   LYS   B N   1 
ATOM   2764 C CA  . LYS   B 1 5   ? -43.733 30.157  -46.332 1.00 24.34 ? 2   LYS   B CA  1 
ATOM   2765 C C   . LYS   B 1 5   ? -43.839 29.192  -45.156 1.00 22.96 ? 2   LYS   B C   1 
ATOM   2766 O O   . LYS   B 1 5   ? -44.177 28.013  -45.323 1.00 24.19 ? 2   LYS   B O   1 
ATOM   2767 C CB  . LYS   B 1 5   ? -45.098 30.737  -46.697 1.00 23.76 ? 2   LYS   B CB  1 
ATOM   2768 C CG  . LYS   B 1 5   ? -45.053 31.712  -47.878 1.00 24.29 ? 2   LYS   B CG  1 
ATOM   2769 C CD  . LYS   B 1 5   ? -44.064 32.849  -47.612 1.00 28.66 ? 2   LYS   B CD  1 
ATOM   2770 C CE  . LYS   B 1 5   ? -44.102 33.906  -48.731 1.00 32.17 ? 2   LYS   B CE  1 
ATOM   2771 N NZ  . LYS   B 1 5   ? -43.872 33.314  -50.090 1.00 34.40 ? 2   LYS   B NZ  1 
ATOM   2772 N N   . THR   B 1 6   ? -43.523 29.701  -43.962 1.00 24.70 ? 3   THR   B N   1 
ATOM   2773 C CA  . THR   B 1 6   ? -43.585 28.944  -42.717 1.00 22.27 ? 3   THR   B CA  1 
ATOM   2774 C C   . THR   B 1 6   ? -44.190 29.840  -41.646 1.00 24.41 ? 3   THR   B C   1 
ATOM   2775 O O   . THR   B 1 6   ? -44.332 31.056  -41.823 1.00 21.21 ? 3   THR   B O   1 
ATOM   2776 C CB  . THR   B 1 6   ? -42.185 28.460  -42.255 1.00 23.83 ? 3   THR   B CB  1 
ATOM   2777 O OG1 . THR   B 1 6   ? -41.430 29.561  -41.728 1.00 22.32 ? 3   THR   B OG1 1 
ATOM   2778 C CG2 . THR   B 1 6   ? -41.406 27.852  -43.433 1.00 23.41 ? 3   THR   B CG2 1 
ATOM   2779 N N   . GLU   B 1 7   ? -44.522 29.237  -40.513 1.00 21.66 ? 4   GLU   B N   1 
ATOM   2780 C CA  . GLU   B 1 7   ? -44.941 30.004  -39.352 1.00 22.68 ? 4   GLU   B CA  1 
ATOM   2781 C C   . GLU   B 1 7   ? -44.036 29.661  -38.180 1.00 22.76 ? 4   GLU   B C   1 
ATOM   2782 O O   . GLU   B 1 7   ? -43.540 28.535  -38.064 1.00 22.65 ? 4   GLU   B O   1 
ATOM   2783 C CB  . GLU   B 1 7   ? -46.406 29.746  -39.001 1.00 21.59 ? 4   GLU   B CB  1 
ATOM   2784 C CG  . GLU   B 1 7   ? -47.364 30.320  -40.044 1.00 28.32 ? 4   GLU   B CG  1 
ATOM   2785 C CD  . GLU   B 1 7   ? -48.827 30.177  -39.631 1.00 36.48 ? 4   GLU   B CD  1 
ATOM   2786 O OE1 . GLU   B 1 7   ? -49.121 29.320  -38.773 1.00 35.98 ? 4   GLU   B OE1 1 
ATOM   2787 O OE2 . GLU   B 1 7   ? -49.673 30.919  -40.172 1.00 40.49 ? 4   GLU   B OE2 1 
ATOM   2788 N N   . ARG   B 1 8   ? -43.813 30.661  -37.334 1.00 20.00 ? 5   ARG   B N   1 
ATOM   2789 C CA  . ARG   B 1 8   ? -42.963 30.548  -36.167 1.00 22.39 ? 5   ARG   B CA  1 
ATOM   2790 C C   . ARG   B 1 8   ? -43.630 31.283  -35.019 1.00 22.02 ? 5   ARG   B C   1 
ATOM   2791 O O   . ARG   B 1 8   ? -44.293 32.302  -35.213 1.00 20.94 ? 5   ARG   B O   1 
ATOM   2792 C CB  . ARG   B 1 8   ? -41.561 31.145  -36.397 1.00 18.93 ? 5   ARG   B CB  1 
ATOM   2793 C CG  . ARG   B 1 8   ? -40.834 30.592  -37.612 1.00 21.13 ? 5   ARG   B CG  1 
ATOM   2794 C CD  . ARG   B 1 8   ? -39.430 31.210  -37.751 1.00 20.33 ? 5   ARG   B CD  1 
ATOM   2795 N NE  . ARG   B 1 8   ? -39.515 32.662  -37.767 1.00 21.00 ? 5   ARG   B NE  1 
ATOM   2796 C CZ  . ARG   B 1 8   ? -38.604 33.477  -37.247 1.00 23.31 ? 5   ARG   B CZ  1 
ATOM   2797 N NH1 . ARG   B 1 8   ? -37.515 33.011  -36.655 1.00 21.95 ? 5   ARG   B NH1 1 
ATOM   2798 N NH2 . ARG   B 1 8   ? -38.801 34.789  -37.305 1.00 22.60 ? 5   ARG   B NH2 1 
ATOM   2799 N N   . TRP   B 1 9   ? -43.434 30.765  -33.818 1.00 20.45 ? 6   TRP   B N   1 
ATOM   2800 C CA  . TRP   B 1 9   ? -43.745 31.499  -32.609 1.00 17.35 ? 6   TRP   B CA  1 
ATOM   2801 C C   . TRP   B 1 9   ? -42.447 32.141  -32.125 1.00 21.43 ? 6   TRP   B C   1 
ATOM   2802 O O   . TRP   B 1 9   ? -41.483 31.439  -31.812 1.00 20.92 ? 6   TRP   B O   1 
ATOM   2803 C CB  . TRP   B 1 9   ? -44.339 30.569  -31.552 1.00 17.87 ? 6   TRP   B CB  1 
ATOM   2804 C CG  . TRP   B 1 9   ? -45.794 30.223  -31.761 1.00 21.54 ? 6   TRP   B CG  1 
ATOM   2805 C CD1 . TRP   B 1 9   ? -46.302 29.046  -32.246 1.00 20.72 ? 6   TRP   B CD1 1 
ATOM   2806 C CD2 . TRP   B 1 9   ? -46.924 31.057  -31.472 1.00 20.49 ? 6   TRP   B CD2 1 
ATOM   2807 N NE1 . TRP   B 1 9   ? -47.679 29.101  -32.278 1.00 20.47 ? 6   TRP   B NE1 1 
ATOM   2808 C CE2 . TRP   B 1 9   ? -48.084 30.324  -31.812 1.00 20.96 ? 6   TRP   B CE2 1 
ATOM   2809 C CE3 . TRP   B 1 9   ? -47.068 32.353  -30.962 1.00 20.78 ? 6   TRP   B CE3 1 
ATOM   2810 C CZ2 . TRP   B 1 9   ? -49.369 30.843  -31.658 1.00 22.35 ? 6   TRP   B CZ2 1 
ATOM   2811 C CZ3 . TRP   B 1 9   ? -48.351 32.868  -30.799 1.00 22.68 ? 6   TRP   B CZ3 1 
ATOM   2812 C CH2 . TRP   B 1 9   ? -49.483 32.118  -31.154 1.00 21.77 ? 6   TRP   B CH2 1 
ATOM   2813 N N   . VAL   B 1 10  ? -42.411 33.464  -32.086 1.00 17.88 ? 7   VAL   B N   1 
ATOM   2814 C CA  . VAL   B 1 10  ? -41.210 34.179  -31.690 1.00 19.96 ? 7   VAL   B CA  1 
ATOM   2815 C C   . VAL   B 1 10  ? -41.450 34.819  -30.339 1.00 20.30 ? 7   VAL   B C   1 
ATOM   2816 O O   . VAL   B 1 10  ? -42.587 35.025  -29.909 1.00 19.54 ? 7   VAL   B O   1 
ATOM   2817 C CB  . VAL   B 1 10  ? -40.791 35.243  -32.724 1.00 16.45 ? 7   VAL   B CB  1 
ATOM   2818 C CG1 . VAL   B 1 10  ? -40.441 34.569  -34.039 1.00 19.19 ? 7   VAL   B CG1 1 
ATOM   2819 C CG2 . VAL   B 1 10  ? -41.912 36.241  -32.927 1.00 21.12 ? 7   VAL   B CG2 1 
ATOM   2820 N N   . VAL   B 1 11  ? -40.357 35.165  -29.676 1.00 18.51 ? 8   VAL   B N   1 
ATOM   2821 C CA  . VAL   B 1 11  ? -40.412 35.772  -28.352 1.00 19.03 ? 8   VAL   B CA  1 
ATOM   2822 C C   . VAL   B 1 11  ? -40.583 37.276  -28.530 1.00 20.86 ? 8   VAL   B C   1 
ATOM   2823 O O   . VAL   B 1 11  ? -39.661 37.979  -28.947 1.00 21.17 ? 8   VAL   B O   1 
ATOM   2824 C CB  . VAL   B 1 11  ? -39.162 35.438  -27.526 1.00 21.25 ? 8   VAL   B CB  1 
ATOM   2825 C CG1 . VAL   B 1 11  ? -39.274 36.051  -26.146 1.00 23.08 ? 8   VAL   B CG1 1 
ATOM   2826 C CG2 . VAL   B 1 11  ? -38.998 33.922  -27.419 1.00 19.64 ? 8   VAL   B CG2 1 
ATOM   2827 N N   . ARG   B 1 12  ? -41.764 37.770  -28.210 1.00 20.04 ? 9   ARG   B N   1 
ATOM   2828 C CA  . ARG   B 1 12  ? -42.087 39.175  -28.392 1.00 23.18 ? 9   ARG   B CA  1 
ATOM   2829 C C   . ARG   B 1 12  ? -41.757 40.003  -27.157 1.00 22.64 ? 9   ARG   B C   1 
ATOM   2830 O O   . ARG   B 1 12  ? -41.390 41.183  -27.286 1.00 23.51 ? 9   ARG   B O   1 
ATOM   2831 C CB  . ARG   B 1 12  ? -43.573 39.298  -28.785 1.00 27.76 ? 9   ARG   B CB  1 
ATOM   2832 C CG  . ARG   B 1 12  ? -44.296 40.504  -28.225 1.00 34.88 ? 9   ARG   B CG  1 
ATOM   2833 C CD  . ARG   B 1 12  ? -45.804 40.545  -28.528 1.00 25.43 ? 9   ARG   B CD  1 
ATOM   2834 N NE  . ARG   B 1 12  ? -46.281 41.874  -28.147 1.00 33.62 ? 9   ARG   B NE  1 
ATOM   2835 C CZ  . ARG   B 1 12  ? -46.364 42.296  -26.888 1.00 39.01 ? 9   ARG   B CZ  1 
ATOM   2836 N NH1 . ARG   B 1 12  ? -46.186 41.475  -25.854 1.00 28.71 ? 9   ARG   B NH1 1 
ATOM   2837 N NH2 . ARG   B 1 12  ? -46.601 43.583  -26.663 1.00 38.86 ? 9   ARG   B NH2 1 
ATOM   2838 N N   . GLU   B 1 13  ? -41.813 39.412  -25.962 1.00 21.30 ? 10  GLU   B N   1 
ATOM   2839 C CA  . GLU   B 1 13  ? -41.538 40.181  -24.750 1.00 24.80 ? 10  GLU   B CA  1 
ATOM   2840 C C   . GLU   B 1 13  ? -41.113 39.237  -23.630 1.00 24.44 ? 10  GLU   B C   1 
ATOM   2841 O O   . GLU   B 1 13  ? -41.656 38.137  -23.506 1.00 23.17 ? 10  GLU   B O   1 
ATOM   2842 C CB  . GLU   B 1 13  ? -42.778 40.992  -24.335 1.00 23.22 ? 10  GLU   B CB  1 
ATOM   2843 C CG  . GLU   B 1 13  ? -42.505 42.019  -23.218 1.00 27.13 ? 10  GLU   B CG  1 
ATOM   2844 C CD  . GLU   B 1 13  ? -43.767 42.768  -22.784 1.00 34.09 ? 10  GLU   B CD  1 
ATOM   2845 O OE1 . GLU   B 1 13  ? -44.858 42.507  -23.343 1.00 30.54 ? 10  GLU   B OE1 1 
ATOM   2846 O OE2 . GLU   B 1 13  ? -43.658 43.618  -21.877 1.00 36.72 ? 10  GLU   B OE2 1 
ATOM   2847 N N   . HIS   B 1 14  ? -40.135 39.664  -22.831 1.00 22.37 ? 11  HIS   B N   1 
ATOM   2848 C CA  . HIS   B 1 14  ? -39.706 38.903  -21.662 1.00 25.07 ? 11  HIS   B CA  1 
ATOM   2849 C C   . HIS   B 1 14  ? -40.574 39.289  -20.467 1.00 26.54 ? 11  HIS   B C   1 
ATOM   2850 O O   . HIS   B 1 14  ? -40.661 40.467  -20.116 1.00 28.29 ? 11  HIS   B O   1 
ATOM   2851 C CB  . HIS   B 1 14  ? -38.233 39.144  -21.357 1.00 22.84 ? 11  HIS   B CB  1 
ATOM   2852 C CG  . HIS   B 1 14  ? -37.312 38.585  -22.399 1.00 23.86 ? 11  HIS   B CG  1 
ATOM   2853 N ND1 . HIS   B 1 14  ? -36.163 39.226  -22.798 1.00 23.48 ? 11  HIS   B ND1 1 
ATOM   2854 C CD2 . HIS   B 1 14  ? -37.386 37.449  -23.136 1.00 23.39 ? 11  HIS   B CD2 1 
ATOM   2855 C CE1 . HIS   B 1 14  ? -35.552 38.499  -23.719 1.00 26.51 ? 11  HIS   B CE1 1 
ATOM   2856 N NE2 . HIS   B 1 14  ? -36.273 37.415  -23.938 1.00 21.31 ? 11  HIS   B NE2 1 
ATOM   2857 N N   . VAL   B 1 15  ? -41.206 38.297  -19.847 1.00 24.77 ? 12  VAL   B N   1 
ATOM   2858 C CA  . VAL   B 1 15  ? -42.068 38.492  -18.683 1.00 26.20 ? 12  VAL   B CA  1 
ATOM   2859 C C   . VAL   B 1 15  ? -41.612 37.507  -17.614 1.00 29.20 ? 12  VAL   B C   1 
ATOM   2860 O O   . VAL   B 1 15  ? -41.692 36.291  -17.825 1.00 30.95 ? 12  VAL   B O   1 
ATOM   2861 C CB  . VAL   B 1 15  ? -43.556 38.274  -19.037 1.00 32.10 ? 12  VAL   B CB  1 
ATOM   2862 C CG1 . VAL   B 1 15  ? -44.439 38.218  -17.772 1.00 36.08 ? 12  VAL   B CG1 1 
ATOM   2863 C CG2 . VAL   B 1 15  ? -44.049 39.362  -20.018 1.00 31.88 ? 12  VAL   B CG2 1 
ATOM   2864 N N   . GLU   B 1 16  ? -41.101 38.025  -16.492 1.00 27.12 ? 13  GLU   B N   1 
ATOM   2865 C CA  . GLU   B 1 16  ? -40.600 37.176  -15.413 1.00 29.58 ? 13  GLU   B CA  1 
ATOM   2866 C C   . GLU   B 1 16  ? -41.747 36.412  -14.743 1.00 30.69 ? 13  GLU   B C   1 
ATOM   2867 O O   . GLU   B 1 16  ? -42.928 36.731  -14.904 1.00 29.27 ? 13  GLU   B O   1 
ATOM   2868 C CB  . GLU   B 1 16  ? -39.872 38.007  -14.364 1.00 31.64 ? 13  GLU   B CB  1 
ATOM   2869 C CG  . GLU   B 1 16  ? -38.600 38.653  -14.850 1.00 38.80 ? 13  GLU   B CG  1 
ATOM   2870 C CD  . GLU   B 1 16  ? -37.400 37.723  -14.787 1.00 46.38 ? 13  GLU   B CD  1 
ATOM   2871 O OE1 . GLU   B 1 16  ? -36.268 38.205  -15.004 1.00 51.90 ? 13  GLU   B OE1 1 
ATOM   2872 O OE2 . GLU   B 1 16  ? -37.581 36.512  -14.508 1.00 51.46 ? 13  GLU   B OE2 1 
ATOM   2873 N N   . GLY   B 1 17  ? -41.381 35.381  -13.971 1.00 31.36 ? 14  GLY   B N   1 
ATOM   2874 C CA  . GLY   B 1 17  ? -42.364 34.660  -13.166 1.00 29.56 ? 14  GLY   B CA  1 
ATOM   2875 C C   . GLY   B 1 17  ? -43.194 33.659  -13.968 1.00 28.06 ? 14  GLY   B C   1 
ATOM   2876 O O   . GLY   B 1 17  ? -42.728 33.031  -14.918 1.00 24.88 ? 14  GLY   B O   1 
ATOM   2877 N N   . VAL   B 1 18  ? -44.449 33.497  -13.544 1.00 25.40 ? 15  VAL   B N   1 
ATOM   2878 C CA  . VAL   B 1 18  ? -45.372 32.615  -14.282 1.00 25.98 ? 15  VAL   B CA  1 
ATOM   2879 C C   . VAL   B 1 18  ? -45.587 33.181  -15.683 1.00 27.39 ? 15  VAL   B C   1 
ATOM   2880 O O   . VAL   B 1 18  ? -45.949 34.364  -15.820 1.00 24.41 ? 15  VAL   B O   1 
ATOM   2881 C CB  . VAL   B 1 18  ? -46.718 32.489  -13.539 1.00 27.67 ? 15  VAL   B CB  1 
ATOM   2882 C CG1 . VAL   B 1 18  ? -47.714 31.694  -14.373 1.00 29.24 ? 15  VAL   B CG1 1 
ATOM   2883 C CG2 . VAL   B 1 18  ? -46.517 31.841  -12.171 1.00 33.65 ? 15  VAL   B CG2 1 
ATOM   2884 N N   . PRO   B 1 19  ? -45.392 32.406  -16.744 1.00 27.27 ? 16  PRO   B N   1 
ATOM   2885 C CA  . PRO   B 1 19  ? -45.531 32.970  -18.093 1.00 25.79 ? 16  PRO   B CA  1 
ATOM   2886 C C   . PRO   B 1 19  ? -46.955 33.446  -18.371 1.00 29.99 ? 16  PRO   B C   1 
ATOM   2887 O O   . PRO   B 1 19  ? -47.935 32.838  -17.935 1.00 29.26 ? 16  PRO   B O   1 
ATOM   2888 C CB  . PRO   B 1 19  ? -45.137 31.799  -19.004 1.00 24.90 ? 16  PRO   B CB  1 
ATOM   2889 C CG  . PRO   B 1 19  ? -44.190 30.958  -18.104 1.00 29.20 ? 16  PRO   B CG  1 
ATOM   2890 C CD  . PRO   B 1 19  ? -44.847 31.033  -16.762 1.00 24.90 ? 16  PRO   B CD  1 
ATOM   2891 N N   . ASP   B 1 20  ? -47.055 34.562  -19.081 1.00 29.90 ? 17  ASP   B N   1 
ATOM   2892 C CA  . ASP   B 1 20  ? -48.292 35.005  -19.728 1.00 26.94 ? 17  ASP   B CA  1 
ATOM   2893 C C   . ASP   B 1 20  ? -48.049 34.775  -21.213 1.00 28.70 ? 17  ASP   B C   1 
ATOM   2894 O O   . ASP   B 1 20  ? -47.536 35.649  -21.920 1.00 23.72 ? 17  ASP   B O   1 
ATOM   2895 C CB  . ASP   B 1 20  ? -48.608 36.468  -19.416 1.00 28.16 ? 17  ASP   B CB  1 
ATOM   2896 C CG  . ASP   B 1 20  ? -49.798 36.990  -20.199 1.00 32.37 ? 17  ASP   B CG  1 
ATOM   2897 O OD1 . ASP   B 1 20  ? -50.387 36.224  -20.988 1.00 30.83 ? 17  ASP   B OD1 1 
ATOM   2898 O OD2 . ASP   B 1 20  ? -50.148 38.174  -20.011 1.00 36.43 ? 17  ASP   B OD2 1 
ATOM   2899 N N   . ALA   B 1 21  ? -48.389 33.570  -21.672 1.00 28.18 ? 18  ALA   B N   1 
ATOM   2900 C CA  . ALA   B 1 21  ? -47.959 33.122  -22.989 1.00 26.47 ? 18  ALA   B CA  1 
ATOM   2901 C C   . ALA   B 1 21  ? -48.573 33.955  -24.109 1.00 28.28 ? 18  ALA   B C   1 
ATOM   2902 O O   . ALA   B 1 21  ? -47.962 34.091  -25.173 1.00 26.82 ? 18  ALA   B O   1 
ATOM   2903 C CB  . ALA   B 1 21  ? -48.305 31.642  -23.178 1.00 26.56 ? 18  ALA   B CB  1 
ATOM   2904 N N   . ALA   B 1 22  ? -49.778 34.502  -23.907 1.00 27.94 ? 19  ALA   B N   1 
ATOM   2905 C CA  . ALA   B 1 22  ? -50.394 35.337  -24.937 1.00 32.78 ? 19  ALA   B CA  1 
ATOM   2906 C C   . ALA   B 1 22  ? -49.638 36.645  -25.122 1.00 29.59 ? 19  ALA   B C   1 
ATOM   2907 O O   . ALA   B 1 22  ? -49.637 37.215  -26.218 1.00 31.29 ? 19  ALA   B O   1 
ATOM   2908 C CB  . ALA   B 1 22  ? -51.860 35.619  -24.585 1.00 36.22 ? 19  ALA   B CB  1 
ATOM   2909 N N   . ARG   B 1 23  ? -48.999 37.139  -24.069 1.00 27.01 ? 20  ARG   B N   1 
ATOM   2910 C CA  . ARG   B 1 23  ? -48.194 38.344  -24.145 1.00 27.60 ? 20  ARG   B CA  1 
ATOM   2911 C C   . ARG   B 1 23  ? -46.758 38.064  -24.591 1.00 30.18 ? 20  ARG   B C   1 
ATOM   2912 O O   . ARG   B 1 23  ? -46.163 38.863  -25.335 1.00 25.06 ? 20  ARG   B O   1 
ATOM   2913 C CB  . ARG   B 1 23  ? -48.216 39.026  -22.776 1.00 31.24 ? 20  ARG   B CB  1 
ATOM   2914 C CG  . ARG   B 1 23  ? -47.393 40.266  -22.653 1.00 34.28 ? 20  ARG   B CG  1 
ATOM   2915 C CD  . ARG   B 1 23  ? -47.406 40.749  -21.197 1.00 34.43 ? 20  ARG   B CD  1 
ATOM   2916 N NE  . ARG   B 1 23  ? -46.762 42.049  -21.104 1.00 45.21 ? 20  ARG   B NE  1 
ATOM   2917 C CZ  . ARG   B 1 23  ? -46.346 42.617  -19.981 1.00 46.37 ? 20  ARG   B CZ  1 
ATOM   2918 N NH1 . ARG   B 1 23  ? -46.504 42.027  -18.806 1.00 41.87 ? 20  ARG   B NH1 1 
ATOM   2919 N NH2 . ARG   B 1 23  ? -45.753 43.807  -20.041 1.00 44.23 ? 20  ARG   B NH2 1 
ATOM   2920 N N   . ILE   B 1 24  ? -46.199 36.924  -24.174 1.00 24.29 ? 21  ILE   B N   1 
ATOM   2921 C CA  . ILE   B 1 24  ? -44.788 36.633  -24.430 1.00 23.21 ? 21  ILE   B CA  1 
ATOM   2922 C C   . ILE   B 1 24  ? -44.538 36.303  -25.905 1.00 21.03 ? 21  ILE   B C   1 
ATOM   2923 O O   . ILE   B 1 24  ? -43.518 36.708  -26.474 1.00 24.30 ? 21  ILE   B O   1 
ATOM   2924 C CB  . ILE   B 1 24  ? -44.320 35.491  -23.504 1.00 21.20 ? 21  ILE   B CB  1 
ATOM   2925 C CG1 . ILE   B 1 24  ? -44.262 36.011  -22.056 1.00 23.96 ? 21  ILE   B CG1 1 
ATOM   2926 C CG2 . ILE   B 1 24  ? -42.954 34.965  -23.967 1.00 19.09 ? 21  ILE   B CG2 1 
ATOM   2927 C CD1 . ILE   B 1 24  ? -44.113 34.930  -20.995 1.00 25.14 ? 21  ILE   B CD1 1 
ATOM   2928 N N   . TYR   B 1 25  ? -45.431 35.538  -26.537 1.00 20.55 ? 22  TYR   B N   1 
ATOM   2929 C CA  . TYR   B 1 25  ? -45.170 34.941  -27.840 1.00 21.13 ? 22  TYR   B CA  1 
ATOM   2930 C C   . TYR   B 1 25  ? -46.056 35.561  -28.917 1.00 23.89 ? 22  TYR   B C   1 
ATOM   2931 O O   . TYR   B 1 25  ? -47.195 35.950  -28.653 1.00 24.62 ? 22  TYR   B O   1 
ATOM   2932 C CB  . TYR   B 1 25  ? -45.415 33.425  -27.808 1.00 21.58 ? 22  TYR   B CB  1 
ATOM   2933 C CG  . TYR   B 1 25  ? -44.526 32.702  -26.824 1.00 24.58 ? 22  TYR   B CG  1 
ATOM   2934 C CD1 . TYR   B 1 25  ? -43.178 32.512  -27.092 1.00 21.52 ? 22  TYR   B CD1 1 
ATOM   2935 C CD2 . TYR   B 1 25  ? -45.041 32.216  -25.621 1.00 25.66 ? 22  TYR   B CD2 1 
ATOM   2936 C CE1 . TYR   B 1 25  ? -42.345 31.846  -26.193 1.00 24.73 ? 22  TYR   B CE1 1 
ATOM   2937 C CE2 . TYR   B 1 25  ? -44.223 31.558  -24.713 1.00 23.76 ? 22  TYR   B CE2 1 
ATOM   2938 C CZ  . TYR   B 1 25  ? -42.886 31.367  -25.004 1.00 23.92 ? 22  TYR   B CZ  1 
ATOM   2939 O OH  . TYR   B 1 25  ? -42.085 30.702  -24.118 1.00 22.46 ? 22  TYR   B OH  1 
ATOM   2940 N N   . GLU   B 1 26  ? -45.522 35.621  -30.137 1.00 23.41 ? 23  GLU   B N   1 
ATOM   2941 C CA  . GLU   B 1 26  ? -46.226 36.136  -31.310 1.00 23.04 ? 23  GLU   B CA  1 
ATOM   2942 C C   . GLU   B 1 26  ? -46.010 35.170  -32.462 1.00 22.16 ? 23  GLU   B C   1 
ATOM   2943 O O   . GLU   B 1 26  ? -44.877 34.725  -32.689 1.00 22.14 ? 23  GLU   B O   1 
ATOM   2944 C CB  . GLU   B 1 26  ? -45.710 37.517  -31.692 1.00 23.94 ? 23  GLU   B CB  1 
ATOM   2945 C CG  . GLU   B 1 26  ? -46.444 38.176  -32.838 1.00 28.27 ? 23  GLU   B CG  1 
ATOM   2946 C CD  . GLU   B 1 26  ? -46.140 39.665  -32.881 1.00 33.64 ? 23  GLU   B CD  1 
ATOM   2947 O OE1 . GLU   B 1 26  ? -46.593 40.400  -31.977 1.00 36.37 ? 23  GLU   B OE1 1 
ATOM   2948 O OE2 . GLU   B 1 26  ? -45.424 40.098  -33.799 1.00 35.39 ? 23  GLU   B OE2 1 
ATOM   2949 N N   . LYS   B 1 27  ? -47.087 34.845  -33.187 1.00 19.20 ? 24  LYS   B N   1 
ATOM   2950 C CA  . LYS   B 1 27  ? -47.007 33.970  -34.344 1.00 21.00 ? 24  LYS   B CA  1 
ATOM   2951 C C   . LYS   B 1 27  ? -46.761 34.818  -35.590 1.00 26.02 ? 24  LYS   B C   1 
ATOM   2952 O O   . LYS   B 1 27  ? -47.530 35.740  -35.877 1.00 23.26 ? 24  LYS   B O   1 
ATOM   2953 C CB  . LYS   B 1 27  ? -48.292 33.159  -34.498 1.00 25.50 ? 24  LYS   B CB  1 
ATOM   2954 C CG  . LYS   B 1 27  ? -48.189 32.051  -35.542 1.00 23.76 ? 24  LYS   B CG  1 
ATOM   2955 C CD  . LYS   B 1 27  ? -49.497 31.279  -35.645 1.00 27.76 ? 24  LYS   B CD  1 
ATOM   2956 C CE  . LYS   B 1 27  ? -50.399 31.942  -36.692 1.00 26.30 ? 24  LYS   B CE  1 
ATOM   2957 N NZ  . LYS   B 1 27  ? -51.817 31.662  -36.459 1.00 43.29 ? 24  LYS   B NZ  1 
ATOM   2958 N N   . VAL   B 1 28  ? -45.706 34.504  -36.334 1.00 22.29 ? 25  VAL   B N   1 
ATOM   2959 C CA  . VAL   B 1 28  ? -45.361 35.249  -37.537 1.00 23.65 ? 25  VAL   B CA  1 
ATOM   2960 C C   . VAL   B 1 28  ? -45.229 34.290  -38.705 1.00 24.74 ? 25  VAL   B C   1 
ATOM   2961 O O   . VAL   B 1 28  ? -44.867 33.122  -38.542 1.00 22.53 ? 25  VAL   B O   1 
ATOM   2962 C CB  . VAL   B 1 28  ? -44.049 36.055  -37.394 1.00 21.89 ? 25  VAL   B CB  1 
ATOM   2963 C CG1 . VAL   B 1 28  ? -44.171 37.105  -36.319 1.00 23.51 ? 25  VAL   B CG1 1 
ATOM   2964 C CG2 . VAL   B 1 28  ? -42.874 35.126  -37.128 1.00 23.18 ? 25  VAL   B CG2 1 
ATOM   2965 N N   . GLU   B 1 29  ? -45.523 34.793  -39.900 1.00 22.57 ? 26  GLU   B N   1 
ATOM   2966 C CA  . GLU   B 1 29  ? -45.231 34.052  -41.116 1.00 26.03 ? 26  GLU   B CA  1 
ATOM   2967 C C   . GLU   B 1 29  ? -43.815 34.395  -41.547 1.00 25.36 ? 26  GLU   B C   1 
ATOM   2968 O O   . GLU   B 1 29  ? -43.423 35.567  -41.545 1.00 26.47 ? 26  GLU   B O   1 
ATOM   2969 C CB  . GLU   B 1 29  ? -46.231 34.376  -42.220 1.00 28.15 ? 26  GLU   B CB  1 
ATOM   2970 C CG  . GLU   B 1 29  ? -45.877 33.749  -43.567 1.00 25.86 ? 26  GLU   B CG  1 
ATOM   2971 C CD  . GLU   B 1 29  ? -46.869 34.138  -44.664 1.00 34.24 ? 26  GLU   B CD  1 
ATOM   2972 O OE1 . GLU   B 1 29  ? -48.080 33.853  -44.524 1.00 34.30 ? 26  GLU   B OE1 1 
ATOM   2973 O OE2 . GLU   B 1 29  ? -46.421 34.727  -45.664 1.00 32.95 ? 26  GLU   B OE2 1 
ATOM   2974 N N   . THR   B 1 30  ? -43.043 33.371  -41.896 1.00 24.66 ? 27  THR   B N   1 
ATOM   2975 C CA  . THR   B 1 30  ? -41.634 33.548  -42.220 1.00 22.72 ? 27  THR   B CA  1 
ATOM   2976 C C   . THR   B 1 30  ? -41.363 32.861  -43.546 1.00 24.76 ? 27  THR   B C   1 
ATOM   2977 O O   . THR   B 1 30  ? -41.622 31.658  -43.693 1.00 24.40 ? 27  THR   B O   1 
ATOM   2978 C CB  . THR   B 1 30  ? -40.737 32.988  -41.108 1.00 26.73 ? 27  THR   B CB  1 
ATOM   2979 O OG1 . THR   B 1 30  ? -40.967 33.717  -39.888 1.00 24.99 ? 27  THR   B OG1 1 
ATOM   2980 C CG2 . THR   B 1 30  ? -39.255 33.085  -41.478 1.00 24.94 ? 27  THR   B CG2 1 
ATOM   2981 N N   . GLU   B 1 31  ? -40.860 33.629  -44.513 1.00 24.07 ? 28  GLU   B N   1 
ATOM   2982 C CA  . GLU   B 1 31  ? -40.412 33.063  -45.776 1.00 26.00 ? 28  GLU   B CA  1 
ATOM   2983 C C   . GLU   B 1 31  ? -39.031 32.461  -45.570 1.00 30.47 ? 28  GLU   B C   1 
ATOM   2984 O O   . GLU   B 1 31  ? -38.098 33.150  -45.140 1.00 28.71 ? 28  GLU   B O   1 
ATOM   2985 C CB  . GLU   B 1 31  ? -40.385 34.121  -46.878 1.00 32.59 ? 28  GLU   B CB  1 
ATOM   2986 C CG  . GLU   B 1 31  ? -39.895 33.536  -48.192 1.00 36.64 ? 28  GLU   B CG  1 
ATOM   2987 C CD  . GLU   B 1 31  ? -40.066 34.454  -49.387 1.00 40.79 ? 28  GLU   B CD  1 
ATOM   2988 O OE1 . GLU   B 1 31  ? -40.981 35.307  -49.390 1.00 43.49 ? 28  GLU   B OE1 1 
ATOM   2989 O OE2 . GLU   B 1 31  ? -39.277 34.302  -50.342 1.00 41.54 ? 28  GLU   B OE2 1 
ATOM   2990 N N   . LEU   B 1 32  ? -38.908 31.177  -45.868 1.00 25.33 ? 29  LEU   B N   1 
ATOM   2991 C CA  . LEU   B 1 32  ? -37.716 30.399  -45.577 1.00 28.72 ? 29  LEU   B CA  1 
ATOM   2992 C C   . LEU   B 1 32  ? -37.053 30.001  -46.889 1.00 35.05 ? 29  LEU   B C   1 
ATOM   2993 O O   . LEU   B 1 32  ? -37.680 29.344  -47.729 1.00 32.85 ? 29  LEU   B O   1 
ATOM   2994 C CB  . LEU   B 1 32  ? -38.092 29.165  -44.756 1.00 27.25 ? 29  LEU   B CB  1 
ATOM   2995 C CG  . LEU   B 1 32  ? -36.999 28.157  -44.443 1.00 32.52 ? 29  LEU   B CG  1 
ATOM   2996 C CD1 . LEU   B 1 32  ? -35.986 28.754  -43.466 1.00 30.85 ? 29  LEU   B CD1 1 
ATOM   2997 C CD2 . LEU   B 1 32  ? -37.628 26.884  -43.890 1.00 25.82 ? 29  LEU   B CD2 1 
ATOM   2998 N N   . ASN   B 1 33  ? -35.794 30.404  -47.068 1.00 35.85 ? 30  ASN   B N   1 
ATOM   2999 C CA  . ASN   B 1 33  ? -35.038 29.989  -48.246 1.00 34.58 ? 30  ASN   B CA  1 
ATOM   3000 C C   . ASN   B 1 33  ? -34.744 28.500  -48.135 1.00 33.22 ? 30  ASN   B C   1 
ATOM   3001 O O   . ASN   B 1 33  ? -34.257 28.034  -47.099 1.00 32.77 ? 30  ASN   B O   1 
ATOM   3002 C CB  . ASN   B 1 33  ? -33.739 30.795  -48.360 1.00 41.34 ? 30  ASN   B CB  1 
ATOM   3003 C CG  . ASN   B 1 33  ? -32.975 30.511  -49.657 1.00 48.45 ? 30  ASN   B CG  1 
ATOM   3004 O OD1 . ASN   B 1 33  ? -32.406 29.434  -49.833 1.00 45.34 ? 30  ASN   B OD1 1 
ATOM   3005 N ND2 . ASN   B 1 33  ? -32.951 31.490  -50.564 1.00 45.66 ? 30  ASN   B ND2 1 
ATOM   3006 N N   . THR   B 1 34  ? -35.070 27.742  -49.184 1.00 32.58 ? 31  THR   B N   1 
ATOM   3007 C CA  . THR   B 1 34  ? -34.931 26.292  -49.157 1.00 33.84 ? 31  THR   B CA  1 
ATOM   3008 C C   . THR   B 1 34  ? -33.749 25.779  -49.977 1.00 39.46 ? 31  THR   B C   1 
ATOM   3009 O O   . THR   B 1 34  ? -33.634 24.563  -50.184 1.00 34.32 ? 31  THR   B O   1 
ATOM   3010 C CB  . THR   B 1 34  ? -36.220 25.619  -49.639 1.00 33.08 ? 31  THR   B CB  1 
ATOM   3011 O OG1 . THR   B 1 34  ? -36.477 25.987  -51.000 1.00 34.44 ? 31  THR   B OG1 1 
ATOM   3012 C CG2 . THR   B 1 34  ? -37.407 26.035  -48.743 1.00 32.87 ? 31  THR   B CG2 1 
ATOM   3013 N N   . ARG   B 1 35  ? -32.877 26.660  -50.459 1.00 34.04 ? 32  ARG   B N   1 
ATOM   3014 C CA  . ARG   B 1 35  ? -31.634 26.201  -51.073 1.00 37.66 ? 32  ARG   B CA  1 
ATOM   3015 C C   . ARG   B 1 35  ? -30.717 25.676  -49.974 1.00 38.45 ? 32  ARG   B C   1 
ATOM   3016 O O   . ARG   B 1 35  ? -30.370 26.407  -49.041 1.00 42.09 ? 32  ARG   B O   1 
ATOM   3017 C CB  . ARG   B 1 35  ? -30.966 27.329  -51.853 1.00 42.48 ? 32  ARG   B CB  1 
ATOM   3018 C CG  . ARG   B 1 35  ? -29.598 26.965  -52.394 1.00 45.95 ? 32  ARG   B CG  1 
ATOM   3019 C CD  . ARG   B 1 35  ? -28.986 28.091  -53.216 1.00 52.02 ? 32  ARG   B CD  1 
ATOM   3020 N NE  . ARG   B 1 35  ? -27.529 28.015  -53.213 1.00 61.23 ? 32  ARG   B NE  1 
ATOM   3021 C CZ  . ARG   B 1 35  ? -26.744 28.460  -54.186 1.00 66.15 ? 32  ARG   B CZ  1 
ATOM   3022 N NH1 . ARG   B 1 35  ? -27.242 28.996  -55.288 1.00 67.59 ? 32  ARG   B NH1 1 
ATOM   3023 N NH2 . ARG   B 1 35  ? -25.423 28.357  -54.052 1.00 66.40 ? 32  ARG   B NH2 1 
ATOM   3024 N N   . LEU   B 1 36  ? -30.343 24.408  -50.058 1.00 30.78 ? 33  LEU   B N   1 
ATOM   3025 C CA  . LEU   B 1 36  ? -29.702 23.746  -48.932 1.00 35.53 ? 33  LEU   B CA  1 
ATOM   3026 C C   . LEU   B 1 36  ? -28.188 23.731  -49.078 1.00 42.48 ? 33  LEU   B C   1 
ATOM   3027 O O   . LEU   B 1 36  ? -27.654 23.470  -50.162 1.00 40.46 ? 33  LEU   B O   1 
ATOM   3028 C CB  . LEU   B 1 36  ? -30.215 22.321  -48.776 1.00 31.01 ? 33  LEU   B CB  1 
ATOM   3029 C CG  . LEU   B 1 36  ? -31.672 22.205  -48.322 1.00 37.05 ? 33  LEU   B CG  1 
ATOM   3030 C CD1 . LEU   B 1 36  ? -32.037 20.739  -48.094 1.00 32.44 ? 33  LEU   B CD1 1 
ATOM   3031 C CD2 . LEU   B 1 36  ? -31.911 23.029  -47.052 1.00 33.03 ? 33  LEU   B CD2 1 
ATOM   3032 N N   . GLY   B 1 37  ? -27.508 24.029  -47.980 1.00 41.67 ? 34  GLY   B N   1 
ATOM   3033 C CA  . GLY   B 1 37  ? -26.092 23.750  -47.883 1.00 41.68 ? 34  GLY   B CA  1 
ATOM   3034 C C   . GLY   B 1 37  ? -25.831 22.257  -47.946 1.00 42.32 ? 34  GLY   B C   1 
ATOM   3035 O O   . GLY   B 1 37  ? -26.724 21.420  -47.853 1.00 38.20 ? 34  GLY   B O   1 
ATOM   3036 N N   . GLU   B 1 38  ? -24.585 21.898  -48.186 1.00 44.61 ? 35  GLU   B N   1 
ATOM   3037 C CA  . GLU   B 1 38  ? -24.225 20.494  -48.365 1.00 45.78 ? 35  GLU   B CA  1 
ATOM   3038 C C   . GLU   B 1 38  ? -24.621 19.562  -47.242 1.00 43.78 ? 35  GLU   B C   1 
ATOM   3039 O O   . GLU   B 1 38  ? -25.006 18.431  -47.489 1.00 41.11 ? 35  GLU   B O   1 
ATOM   3040 C CB  . GLU   B 1 38  ? -22.717 20.399  -48.586 1.00 49.48 ? 35  GLU   B CB  1 
ATOM   3041 C CG  . GLU   B 1 38  ? -22.277 20.666  -50.009 1.00 52.67 ? 35  GLU   B CG  1 
ATOM   3042 C CD  . GLU   B 1 38  ? -21.332 19.600  -50.521 1.00 64.50 ? 35  GLU   B CD  1 
ATOM   3043 O OE1 . GLU   B 1 38  ? -20.322 19.321  -49.837 1.00 64.42 ? 35  GLU   B OE1 1 
ATOM   3044 O OE2 . GLU   B 1 38  ? -21.601 19.036  -51.602 1.00 58.24 ? 35  GLU   B OE2 1 
ATOM   3045 N N   . GLU   B 1 39  ? -24.518 20.039  -46.017 1.00 38.57 ? 36  GLU   B N   1 
ATOM   3046 C CA  . GLU   B 1 39  ? -24.902 19.216  -44.876 1.00 39.44 ? 36  GLU   B CA  1 
ATOM   3047 C C   . GLU   B 1 39  ? -26.262 19.606  -44.310 1.00 37.16 ? 36  GLU   B C   1 
ATOM   3048 O O   . GLU   B 1 39  ? -26.663 19.091  -43.261 1.00 35.40 ? 36  GLU   B O   1 
ATOM   3049 C CB  . GLU   B 1 39  ? -23.837 19.306  -43.784 1.00 35.88 ? 36  GLU   B CB  1 
ATOM   3050 C CG  . GLU   B 1 39  ? -22.447 18.933  -44.272 1.00 48.84 ? 36  GLU   B CG  1 
ATOM   3051 C CD  . GLU   B 1 39  ? -21.357 19.397  -43.322 1.00 59.04 ? 36  GLU   B CD  1 
ATOM   3052 O OE1 . GLU   B 1 39  ? -20.612 20.343  -43.676 1.00 60.57 ? 36  GLU   B OE1 1 
ATOM   3053 O OE2 . GLU   B 1 39  ? -21.254 18.822  -42.219 1.00 56.73 ? 36  GLU   B OE2 1 
ATOM   3054 N N   . GLN   B 1 40  ? -26.983 20.490  -44.980 1.00 32.26 ? 37  GLN   B N   1 
ATOM   3055 C CA  . GLN   B 1 40  ? -28.232 21.010  -44.450 1.00 35.57 ? 37  GLN   B CA  1 
ATOM   3056 C C   . GLN   B 1 40  ? -29.431 20.178  -44.892 1.00 37.89 ? 37  GLN   B C   1 
ATOM   3057 O O   . GLN   B 1 40  ? -29.443 19.567  -45.968 1.00 34.67 ? 37  GLN   B O   1 
ATOM   3058 C CB  . GLN   B 1 40  ? -28.414 22.466  -44.872 1.00 35.91 ? 37  GLN   B CB  1 
ATOM   3059 C CG  . GLN   B 1 40  ? -27.469 23.404  -44.137 1.00 35.60 ? 37  GLN   B CG  1 
ATOM   3060 C CD  . GLN   B 1 40  ? -27.741 24.852  -44.463 1.00 39.89 ? 37  GLN   B CD  1 
ATOM   3061 O OE1 . GLN   B 1 40  ? -28.038 25.196  -45.608 1.00 36.64 ? 37  GLN   B OE1 1 
ATOM   3062 N NE2 . GLN   B 1 40  ? -27.661 25.712  -43.453 1.00 39.42 ? 37  GLN   B NE2 1 
ATOM   3063 N N   . MET   B 1 41  ? -30.442 20.159  -44.030 1.00 32.42 ? 38  MET   B N   1 
ATOM   3064 C CA  . MET   B 1 41  ? -31.720 19.527  -44.292 1.00 29.34 ? 38  MET   B CA  1 
ATOM   3065 C C   . MET   B 1 41  ? -32.833 20.560  -44.145 1.00 34.16 ? 38  MET   B C   1 
ATOM   3066 O O   . MET   B 1 41  ? -32.727 21.497  -43.342 1.00 29.59 ? 38  MET   B O   1 
ATOM   3067 C CB  . MET   B 1 41  ? -31.959 18.357  -43.326 1.00 30.32 ? 38  MET   B CB  1 
ATOM   3068 C CG  . MET   B 1 41  ? -30.778 17.387  -43.188 1.00 31.94 ? 38  MET   B CG  1 
ATOM   3069 S SD  . MET   B 1 41  ? -30.903 16.409  -41.690 1.00 36.38 ? 38  MET   B SD  1 
ATOM   3070 C CE  . MET   B 1 41  ? -30.434 17.661  -40.444 1.00 33.43 ? 38  MET   B CE  1 
ATOM   3071 N N   . LEU   B 1 42  ? -33.886 20.398  -44.952 1.00 27.73 ? 39  LEU   B N   1 
ATOM   3072 C CA  . LEU   B 1 42  ? -35.159 21.068  -44.719 1.00 31.22 ? 39  LEU   B CA  1 
ATOM   3073 C C   . LEU   B 1 42  ? -36.030 20.112  -43.922 1.00 28.85 ? 39  LEU   B C   1 
ATOM   3074 O O   . LEU   B 1 42  ? -36.128 18.932  -44.267 1.00 31.13 ? 39  LEU   B O   1 
ATOM   3075 C CB  . LEU   B 1 42  ? -35.852 21.445  -46.035 1.00 27.96 ? 39  LEU   B CB  1 
ATOM   3076 C CG  . LEU   B 1 42  ? -37.269 22.026  -45.941 1.00 28.43 ? 39  LEU   B CG  1 
ATOM   3077 C CD1 . LEU   B 1 42  ? -37.249 23.416  -45.303 1.00 25.89 ? 39  LEU   B CD1 1 
ATOM   3078 C CD2 . LEU   B 1 42  ? -37.947 22.067  -47.328 1.00 29.13 ? 39  LEU   B CD2 1 
ATOM   3079 N N   . LEU   B 1 43  ? -36.636 20.606  -42.849 1.00 25.81 ? 40  LEU   B N   1 
ATOM   3080 C CA  . LEU   B 1 43  ? -37.397 19.744  -41.965 1.00 26.92 ? 40  LEU   B CA  1 
ATOM   3081 C C   . LEU   B 1 43  ? -38.787 20.316  -41.720 1.00 27.13 ? 40  LEU   B C   1 
ATOM   3082 O O   . LEU   B 1 43  ? -38.962 21.535  -41.595 1.00 24.92 ? 40  LEU   B O   1 
ATOM   3083 C CB  . LEU   B 1 43  ? -36.659 19.536  -40.638 1.00 29.63 ? 40  LEU   B CB  1 
ATOM   3084 C CG  . LEU   B 1 43  ? -35.257 18.913  -40.740 1.00 24.69 ? 40  LEU   B CG  1 
ATOM   3085 C CD1 . LEU   B 1 43  ? -34.189 19.950  -40.451 1.00 28.44 ? 40  LEU   B CD1 1 
ATOM   3086 C CD2 . LEU   B 1 43  ? -35.136 17.756  -39.770 1.00 29.16 ? 40  LEU   B CD2 1 
ATOM   3087 N N   . LYS   B 1 44  ? -39.768 19.414  -41.673 1.00 24.97 ? 41  LYS   B N   1 
ATOM   3088 C CA  . LYS   B 1 44  ? -41.142 19.721  -41.305 1.00 31.65 ? 41  LYS   B CA  1 
ATOM   3089 C C   . LYS   B 1 44  ? -41.416 19.215  -39.888 1.00 27.07 ? 41  LYS   B C   1 
ATOM   3090 O O   . LYS   B 1 44  ? -41.158 18.049  -39.576 1.00 27.21 ? 41  LYS   B O   1 
ATOM   3091 C CB  . LYS   B 1 44  ? -42.113 19.070  -42.295 1.00 27.20 ? 41  LYS   B CB  1 
ATOM   3092 C CG  . LYS   B 1 44  ? -43.562 19.170  -41.872 1.00 28.69 ? 41  LYS   B CG  1 
ATOM   3093 C CD  . LYS   B 1 44  ? -44.515 18.792  -43.018 1.00 35.82 ? 41  LYS   B CD  1 
ATOM   3094 C CE  . LYS   B 1 44  ? -45.220 17.474  -42.736 1.00 38.45 ? 41  LYS   B CE  1 
ATOM   3095 N NZ  . LYS   B 1 44  ? -46.125 17.044  -43.859 1.00 40.23 ? 41  LYS   B NZ  1 
ATOM   3096 N N   . THR   B 1 45  ? -41.947 20.085  -39.040 1.00 23.54 ? 42  THR   B N   1 
ATOM   3097 C CA  . THR   B 1 45  ? -42.235 19.719  -37.660 1.00 26.82 ? 42  THR   B CA  1 
ATOM   3098 C C   . THR   B 1 45  ? -43.529 18.913  -37.571 1.00 26.90 ? 42  THR   B C   1 
ATOM   3099 O O   . THR   B 1 45  ? -44.560 19.307  -38.123 1.00 25.18 ? 42  THR   B O   1 
ATOM   3100 C CB  . THR   B 1 45  ? -42.345 20.977  -36.796 1.00 25.74 ? 42  THR   B CB  1 
ATOM   3101 O OG1 . THR   B 1 45  ? -41.116 21.701  -36.862 1.00 24.95 ? 42  THR   B OG1 1 
ATOM   3102 C CG2 . THR   B 1 45  ? -42.638 20.609  -35.352 1.00 20.19 ? 42  THR   B CG2 1 
ATOM   3103 N N   . LEU   B 1 46  ? -43.480 17.794  -36.857 1.00 25.88 ? 43  LEU   B N   1 
ATOM   3104 C CA  . LEU   B 1 46  ? -44.653 16.953  -36.655 1.00 27.63 ? 43  LEU   B CA  1 
ATOM   3105 C C   . LEU   B 1 46  ? -45.251 17.109  -35.268 1.00 28.70 ? 43  LEU   B C   1 
ATOM   3106 O O   . LEU   B 1 46  ? -46.478 17.194  -35.130 1.00 27.78 ? 43  LEU   B O   1 
ATOM   3107 C CB  . LEU   B 1 46  ? -44.301 15.481  -36.894 1.00 25.93 ? 43  LEU   B CB  1 
ATOM   3108 C CG  . LEU   B 1 46  ? -43.664 15.102  -38.229 1.00 29.87 ? 43  LEU   B CG  1 
ATOM   3109 C CD1 . LEU   B 1 46  ? -43.487 13.578  -38.315 1.00 30.82 ? 43  LEU   B CD1 1 
ATOM   3110 C CD2 . LEU   B 1 46  ? -44.480 15.623  -39.413 1.00 30.63 ? 43  LEU   B CD2 1 
ATOM   3111 N N   . TYR   B 1 47  ? -44.404 17.132  -34.239 1.00 27.57 ? 44  TYR   B N   1 
ATOM   3112 C CA  . TYR   B 1 47  ? -44.814 17.352  -32.858 1.00 25.55 ? 44  TYR   B CA  1 
ATOM   3113 C C   . TYR   B 1 47  ? -43.808 18.282  -32.191 1.00 27.47 ? 44  TYR   B C   1 
ATOM   3114 O O   . TYR   B 1 47  ? -42.615 18.264  -32.518 1.00 25.17 ? 44  TYR   B O   1 
ATOM   3115 C CB  . TYR   B 1 47  ? -44.859 16.071  -32.028 1.00 27.74 ? 44  TYR   B CB  1 
ATOM   3116 C CG  . TYR   B 1 47  ? -45.867 15.005  -32.414 1.00 25.87 ? 44  TYR   B CG  1 
ATOM   3117 C CD1 . TYR   B 1 47  ? -45.587 14.102  -33.429 1.00 27.16 ? 44  TYR   B CD1 1 
ATOM   3118 C CD2 . TYR   B 1 47  ? -47.051 14.859  -31.713 1.00 26.66 ? 44  TYR   B CD2 1 
ATOM   3119 C CE1 . TYR   B 1 47  ? -46.490 13.099  -33.768 1.00 33.01 ? 44  TYR   B CE1 1 
ATOM   3120 C CE2 . TYR   B 1 47  ? -47.962 13.857  -32.036 1.00 29.70 ? 44  TYR   B CE2 1 
ATOM   3121 C CZ  . TYR   B 1 47  ? -47.672 12.984  -33.064 1.00 30.45 ? 44  TYR   B CZ  1 
ATOM   3122 O OH  . TYR   B 1 47  ? -48.554 11.993  -33.394 1.00 36.76 ? 44  TYR   B OH  1 
ATOM   3123 N N   . VAL   B 1 48  ? -44.295 19.087  -31.252 1.00 24.73 ? 45  VAL   B N   1 
ATOM   3124 C CA  . VAL   B 1 48  ? -43.441 19.861  -30.359 1.00 24.29 ? 45  VAL   B CA  1 
ATOM   3125 C C   . VAL   B 1 48  ? -43.830 19.524  -28.929 1.00 24.11 ? 45  VAL   B C   1 
ATOM   3126 O O   . VAL   B 1 48  ? -44.985 19.189  -28.637 1.00 24.10 ? 45  VAL   B O   1 
ATOM   3127 C CB  . VAL   B 1 48  ? -43.521 21.396  -30.561 1.00 22.18 ? 45  VAL   B CB  1 
ATOM   3128 C CG1 . VAL   B 1 48  ? -43.182 21.784  -31.996 1.00 20.49 ? 45  VAL   B CG1 1 
ATOM   3129 C CG2 . VAL   B 1 48  ? -44.888 21.946  -30.121 1.00 22.43 ? 45  VAL   B CG2 1 
ATOM   3130 N N   . SER   B 1 49  ? -42.848 19.636  -28.035 1.00 19.35 ? 46  SER   B N   1 
ATOM   3131 C CA  . SER   B 1 49  ? -43.076 19.574  -26.606 1.00 24.60 ? 46  SER   B CA  1 
ATOM   3132 C C   . SER   B 1 49  ? -43.255 20.977  -26.033 1.00 22.19 ? 46  SER   B C   1 
ATOM   3133 O O   . SER   B 1 49  ? -42.723 21.962  -26.554 1.00 23.67 ? 46  SER   B O   1 
ATOM   3134 C CB  . SER   B 1 49  ? -41.897 18.860  -25.920 1.00 23.38 ? 46  SER   B CB  1 
ATOM   3135 O OG  . SER   B 1 49  ? -42.070 18.764  -24.525 1.00 27.93 ? 46  SER   B OG  1 
ATOM   3136 N N   . VAL   B 1 50  ? -44.024 21.064  -24.960 1.00 19.76 ? 47  VAL   B N   1 
ATOM   3137 C CA  . VAL   B 1 50  ? -44.015 22.230  -24.084 1.00 23.47 ? 47  VAL   B CA  1 
ATOM   3138 C C   . VAL   B 1 50  ? -43.639 21.739  -22.695 1.00 23.60 ? 47  VAL   B C   1 
ATOM   3139 O O   . VAL   B 1 50  ? -44.045 20.645  -22.288 1.00 26.01 ? 47  VAL   B O   1 
ATOM   3140 C CB  . VAL   B 1 50  ? -45.372 22.968  -24.069 1.00 24.59 ? 47  VAL   B CB  1 
ATOM   3141 C CG1 . VAL   B 1 50  ? -45.777 23.330  -25.501 1.00 26.05 ? 47  VAL   B CG1 1 
ATOM   3142 C CG2 . VAL   B 1 50  ? -46.460 22.102  -23.416 1.00 22.59 ? 47  VAL   B CG2 1 
ATOM   3143 N N   . ASP   B 1 51  ? -42.818 22.519  -21.992 1.00 25.19 ? 48  ASP   B N   1 
ATOM   3144 C CA  . ASP   B 1 51  ? -42.231 22.068  -20.734 1.00 23.61 ? 48  ASP   B CA  1 
ATOM   3145 C C   . ASP   B 1 51  ? -41.950 23.273  -19.867 1.00 22.55 ? 48  ASP   B C   1 
ATOM   3146 O O   . ASP   B 1 51  ? -41.647 24.359  -20.389 1.00 23.44 ? 48  ASP   B O   1 
ATOM   3147 C CB  . ASP   B 1 51  ? -40.905 21.304  -20.922 1.00 22.09 ? 48  ASP   B CB  1 
ATOM   3148 C CG  . ASP   B 1 51  ? -40.984 20.225  -21.943 1.00 23.61 ? 48  ASP   B CG  1 
ATOM   3149 O OD1 . ASP   B 1 51  ? -40.903 20.548  -23.146 1.00 25.69 ? 48  ASP   B OD1 1 
ATOM   3150 O OD2 . ASP   B 1 51  ? -41.074 19.041  -21.551 1.00 26.71 ? 48  ASP   B OD2 1 
ATOM   3151 N N   . PRO   B 1 52  ? -41.979 23.108  -18.548 1.00 21.39 ? 49  PRO   B N   1 
ATOM   3152 C CA  . PRO   B 1 52  ? -41.646 24.237  -17.672 1.00 22.69 ? 49  PRO   B CA  1 
ATOM   3153 C C   . PRO   B 1 52  ? -40.239 24.785  -17.902 1.00 20.56 ? 49  PRO   B C   1 
ATOM   3154 O O   . PRO   B 1 52  ? -40.044 25.996  -17.762 1.00 23.12 ? 49  PRO   B O   1 
ATOM   3155 C CB  . PRO   B 1 52  ? -41.818 23.652  -16.259 1.00 25.24 ? 49  PRO   B CB  1 
ATOM   3156 C CG  . PRO   B 1 52  ? -42.750 22.460  -16.436 1.00 24.27 ? 49  PRO   B CG  1 
ATOM   3157 C CD  . PRO   B 1 52  ? -42.381 21.901  -17.798 1.00 23.37 ? 49  PRO   B CD  1 
ATOM   3158 N N   . TYR   B 1 53  ? -39.255 23.951  -18.263 1.00 21.16 ? 50  TYR   B N   1 
ATOM   3159 C CA  . TYR   B 1 53  ? -37.911 24.494  -18.434 1.00 22.71 ? 50  TYR   B CA  1 
ATOM   3160 C C   . TYR   B 1 53  ? -37.818 25.480  -19.597 1.00 23.20 ? 50  TYR   B C   1 
ATOM   3161 O O   . TYR   B 1 53  ? -36.808 26.184  -19.710 1.00 22.04 ? 50  TYR   B O   1 
ATOM   3162 C CB  . TYR   B 1 53  ? -36.879 23.377  -18.617 1.00 22.45 ? 50  TYR   B CB  1 
ATOM   3163 C CG  . TYR   B 1 53  ? -37.084 22.491  -19.820 1.00 23.04 ? 50  TYR   B CG  1 
ATOM   3164 C CD1 . TYR   B 1 53  ? -36.927 22.979  -21.105 1.00 21.90 ? 50  TYR   B CD1 1 
ATOM   3165 C CD2 . TYR   B 1 53  ? -37.404 21.154  -19.663 1.00 24.73 ? 50  TYR   B CD2 1 
ATOM   3166 C CE1 . TYR   B 1 53  ? -37.108 22.172  -22.208 1.00 24.49 ? 50  TYR   B CE1 1 
ATOM   3167 C CE2 . TYR   B 1 53  ? -37.584 20.330  -20.763 1.00 23.52 ? 50  TYR   B CE2 1 
ATOM   3168 C CZ  . TYR   B 1 53  ? -37.431 20.847  -22.027 1.00 26.89 ? 50  TYR   B CZ  1 
ATOM   3169 O OH  . TYR   B 1 53  ? -37.597 20.034  -23.121 1.00 26.45 ? 50  TYR   B OH  1 
ATOM   3170 N N   . LEU   B 1 54  ? -38.837 25.560  -20.459 1.00 20.58 ? 51  LEU   B N   1 
ATOM   3171 C CA  . LEU   B 1 54  ? -38.824 26.588  -21.498 1.00 22.68 ? 51  LEU   B CA  1 
ATOM   3172 C C   . LEU   B 1 54  ? -38.961 27.988  -20.922 1.00 22.95 ? 51  LEU   B C   1 
ATOM   3173 O O   . LEU   B 1 54  ? -38.580 28.957  -21.592 1.00 21.92 ? 51  LEU   B O   1 
ATOM   3174 C CB  . LEU   B 1 54  ? -39.950 26.370  -22.508 1.00 18.05 ? 51  LEU   B CB  1 
ATOM   3175 C CG  . LEU   B 1 54  ? -39.924 25.058  -23.300 1.00 25.24 ? 51  LEU   B CG  1 
ATOM   3176 C CD1 . LEU   B 1 54  ? -41.142 24.951  -24.241 1.00 21.43 ? 51  LEU   B CD1 1 
ATOM   3177 C CD2 . LEU   B 1 54  ? -38.625 24.905  -24.070 1.00 21.70 ? 51  LEU   B CD2 1 
ATOM   3178 N N   . GLN   B 1 55  ? -39.511 28.118  -19.715 1.00 19.55 ? 52  GLN   B N   1 
ATOM   3179 C CA  . GLN   B 1 55  ? -39.735 29.438  -19.123 1.00 20.80 ? 52  GLN   B CA  1 
ATOM   3180 C C   . GLN   B 1 55  ? -38.427 30.224  -19.018 1.00 21.25 ? 52  GLN   B C   1 
ATOM   3181 O O   . GLN   B 1 55  ? -38.378 31.410  -19.362 1.00 22.18 ? 52  GLN   B O   1 
ATOM   3182 C CB  . GLN   B 1 55  ? -40.399 29.275  -17.753 1.00 22.23 ? 52  GLN   B CB  1 
ATOM   3183 C CG  . GLN   B 1 55  ? -40.787 30.579  -17.054 1.00 21.57 ? 52  GLN   B CG  1 
ATOM   3184 C CD  . GLN   B 1 55  ? -39.687 31.076  -16.144 1.00 25.45 ? 52  GLN   B CD  1 
ATOM   3185 O OE1 . GLN   B 1 55  ? -38.579 30.516  -16.119 1.00 26.44 ? 52  GLN   B OE1 1 
ATOM   3186 N NE2 . GLN   B 1 55  ? -39.974 32.128  -15.391 1.00 27.18 ? 52  GLN   B NE2 1 
ATOM   3187 N N   . GLY   B 1 56  ? -37.346 29.565  -18.550 1.00 20.37 ? 53  GLY   B N   1 
ATOM   3188 C CA  . GLY   B 1 56  ? -36.040 30.219  -18.477 1.00 21.15 ? 53  GLY   B CA  1 
ATOM   3189 C C   . GLY   B 1 56  ? -35.301 30.294  -19.802 1.00 21.85 ? 53  GLY   B C   1 
ATOM   3190 O O   . GLY   B 1 56  ? -34.572 31.263  -20.055 1.00 20.70 ? 53  GLY   B O   1 
ATOM   3191 N N   . ILE   B 1 57  ? -35.464 29.299  -20.668 1.00 22.41 ? 54  ILE   B N   1 
ATOM   3192 C CA  . ILE   B 1 57  ? -34.898 29.421  -22.008 1.00 21.98 ? 54  ILE   B CA  1 
ATOM   3193 C C   . ILE   B 1 57  ? -35.481 30.648  -22.694 1.00 21.59 ? 54  ILE   B C   1 
ATOM   3194 O O   . ILE   B 1 57  ? -34.763 31.452  -23.298 1.00 21.97 ? 54  ILE   B O   1 
ATOM   3195 C CB  . ILE   B 1 57  ? -35.154 28.130  -22.808 1.00 22.25 ? 54  ILE   B CB  1 
ATOM   3196 C CG1 . ILE   B 1 57  ? -34.412 26.960  -22.142 1.00 27.91 ? 54  ILE   B CG1 1 
ATOM   3197 C CG2 . ILE   B 1 57  ? -34.691 28.295  -24.268 1.00 22.78 ? 54  ILE   B CG2 1 
ATOM   3198 C CD1 . ILE   B 1 57  ? -34.511 25.647  -22.910 1.00 24.21 ? 54  ILE   B CD1 1 
ATOM   3199 N N   . CYS   B 1 58  ? -36.793 30.832  -22.569 1.00 20.12 ? 55  CYS   B N   1 
ATOM   3200 C CA  . CYS   B 1 58  ? -37.456 31.989  -23.148 1.00 20.86 ? 55  CYS   B CA  1 
ATOM   3201 C C   . CYS   B 1 58  ? -36.811 33.293  -22.677 1.00 22.72 ? 55  CYS   B C   1 
ATOM   3202 O O   . CYS   B 1 58  ? -36.502 34.183  -23.483 1.00 21.42 ? 55  CYS   B O   1 
ATOM   3203 C CB  . CYS   B 1 58  ? -38.940 31.949  -22.775 1.00 21.23 ? 55  CYS   B CB  1 
ATOM   3204 S SG  . CYS   B 1 58  ? -39.875 33.294  -23.491 1.00 23.88 ? 55  CYS   B SG  1 
ATOM   3205 N N   . LEU   B 1 59  ? -36.621 33.429  -21.359 1.00 22.94 ? 56  LEU   B N   1 
ATOM   3206 C CA  . LEU   B 1 59  ? -36.030 34.642  -20.811 1.00 20.97 ? 56  LEU   B CA  1 
ATOM   3207 C C   . LEU   B 1 59  ? -34.613 34.877  -21.334 1.00 23.65 ? 56  LEU   B C   1 
ATOM   3208 O O   . LEU   B 1 59  ? -34.157 36.026  -21.377 1.00 20.46 ? 56  LEU   B O   1 
ATOM   3209 C CB  . LEU   B 1 59  ? -36.045 34.591  -19.278 1.00 20.82 ? 56  LEU   B CB  1 
ATOM   3210 C CG  . LEU   B 1 59  ? -37.468 34.647  -18.690 1.00 23.37 ? 56  LEU   B CG  1 
ATOM   3211 C CD1 . LEU   B 1 59  ? -37.478 34.128  -17.250 1.00 29.57 ? 56  LEU   B CD1 1 
ATOM   3212 C CD2 . LEU   B 1 59  ? -37.995 36.062  -18.750 1.00 20.39 ? 56  LEU   B CD2 1 
ATOM   3213 N N   . ASP   B 1 60  ? -33.900 33.814  -21.735 1.00 22.46 ? 57  ASP   B N   1 
ATOM   3214 C CA  . ASP   B 1 60  ? -32.577 33.960  -22.337 1.00 22.64 ? 57  ASP   B CA  1 
ATOM   3215 C C   . ASP   B 1 60  ? -32.618 34.045  -23.860 1.00 24.11 ? 57  ASP   B C   1 
ATOM   3216 O O   . ASP   B 1 60  ? -31.552 34.079  -24.487 1.00 22.31 ? 57  ASP   B O   1 
ATOM   3217 C CB  . ASP   B 1 60  ? -31.657 32.796  -21.937 1.00 22.16 ? 57  ASP   B CB  1 
ATOM   3218 C CG  . ASP   B 1 60  ? -31.281 32.812  -20.456 1.00 26.87 ? 57  ASP   B CG  1 
ATOM   3219 O OD1 . ASP   B 1 60  ? -31.247 33.890  -19.835 1.00 25.85 ? 57  ASP   B OD1 1 
ATOM   3220 O OD2 . ASP   B 1 60  ? -31.016 31.719  -19.913 1.00 26.92 ? 57  ASP   B OD2 1 
ATOM   3221 N N   . THR   B 1 61  ? -33.796 34.063  -24.466 1.00 21.77 ? 58  THR   B N   1 
ATOM   3222 C CA  . THR   B 1 61  ? -33.933 34.131  -25.922 1.00 21.36 ? 58  THR   B CA  1 
ATOM   3223 C C   . THR   B 1 61  ? -34.029 35.584  -26.376 1.00 21.35 ? 58  THR   B C   1 
ATOM   3224 O O   . THR   B 1 61  ? -34.884 36.330  -25.878 1.00 20.92 ? 58  THR   B O   1 
ATOM   3225 C CB  . THR   B 1 61  ? -35.188 33.380  -26.382 1.00 22.75 ? 58  THR   B CB  1 
ATOM   3226 O OG1 . THR   B 1 61  ? -35.117 32.008  -25.958 1.00 20.51 ? 58  THR   B OG1 1 
ATOM   3227 C CG2 . THR   B 1 61  ? -35.314 33.441  -27.923 1.00 19.29 ? 58  THR   B CG2 1 
ATOM   3228 N N   . PRO   B 1 62  ? -33.182 36.031  -27.302 1.00 22.65 ? 59  PRO   B N   1 
ATOM   3229 C CA  . PRO   B 1 62  ? -33.272 37.426  -27.764 1.00 22.96 ? 59  PRO   B CA  1 
ATOM   3230 C C   . PRO   B 1 62  ? -34.644 37.731  -28.357 1.00 21.77 ? 59  PRO   B C   1 
ATOM   3231 O O   . PRO   B 1 62  ? -35.216 36.921  -29.075 1.00 21.35 ? 59  PRO   B O   1 
ATOM   3232 C CB  . PRO   B 1 62  ? -32.166 37.522  -28.823 1.00 24.04 ? 59  PRO   B CB  1 
ATOM   3233 C CG  . PRO   B 1 62  ? -31.174 36.460  -28.445 1.00 20.55 ? 59  PRO   B CG  1 
ATOM   3234 C CD  . PRO   B 1 62  ? -32.005 35.333  -27.840 1.00 22.80 ? 59  PRO   B CD  1 
ATOM   3235 N N   . ILE   B 1 63  ? -35.179 38.917  -28.040 1.00 20.74 ? 60  ILE   B N   1 
ATOM   3236 C CA  . ILE   B 1 63  ? -36.455 39.355  -28.617 1.00 20.52 ? 60  ILE   B CA  1 
ATOM   3237 C C   . ILE   B 1 63  ? -36.425 39.174  -30.131 1.00 20.50 ? 60  ILE   B C   1 
ATOM   3238 O O   . ILE   B 1 63  ? -35.457 39.560  -30.792 1.00 22.03 ? 60  ILE   B O   1 
ATOM   3239 C CB  . ILE   B 1 63  ? -36.728 40.826  -28.227 1.00 22.79 ? 60  ILE   B CB  1 
ATOM   3240 C CG1 . ILE   B 1 63  ? -36.789 40.991  -26.699 1.00 22.98 ? 60  ILE   B CG1 1 
ATOM   3241 C CG2 . ILE   B 1 63  ? -38.002 41.358  -28.887 1.00 20.60 ? 60  ILE   B CG2 1 
ATOM   3242 C CD1 . ILE   B 1 63  ? -37.777 40.054  -26.048 1.00 21.82 ? 60  ILE   B CD1 1 
ATOM   3243 N N   . GLY   B 1 64  ? -37.488 38.591  -30.691 1.00 20.23 ? 61  GLY   B N   1 
ATOM   3244 C CA  . GLY   B 1 64  ? -37.580 38.355  -32.115 1.00 20.18 ? 61  GLY   B CA  1 
ATOM   3245 C C   . GLY   B 1 64  ? -37.139 36.977  -32.582 1.00 23.62 ? 61  GLY   B C   1 
ATOM   3246 O O   . GLY   B 1 64  ? -37.474 36.583  -33.713 1.00 19.57 ? 61  GLY   B O   1 
ATOM   3247 N N   . ASP   B 1 65  ? -36.385 36.244  -31.765 1.00 18.09 ? 62  ASP   B N   1 
ATOM   3248 C CA  . ASP   B 1 65  ? -35.992 34.882  -32.102 1.00 21.54 ? 62  ASP   B CA  1 
ATOM   3249 C C   . ASP   B 1 65  ? -37.130 33.907  -31.824 1.00 21.63 ? 62  ASP   B C   1 
ATOM   3250 O O   . ASP   B 1 65  ? -37.969 34.150  -30.959 1.00 20.44 ? 62  ASP   B O   1 
ATOM   3251 C CB  . ASP   B 1 65  ? -34.746 34.472  -31.295 1.00 19.58 ? 62  ASP   B CB  1 
ATOM   3252 C CG  . ASP   B 1 65  ? -33.462 35.056  -31.875 1.00 25.71 ? 62  ASP   B CG  1 
ATOM   3253 O OD1 . ASP   B 1 65  ? -33.557 35.904  -32.798 1.00 26.61 ? 62  ASP   B OD1 1 
ATOM   3254 O OD2 . ASP   B 1 65  ? -32.365 34.649  -31.422 1.00 26.67 ? 62  ASP   B OD2 1 
ATOM   3255 N N   . HIS   B 1 66  ? -37.149 32.796  -32.565 1.00 21.34 ? 63  HIS   B N   1 
ATOM   3256 C CA  . HIS   B 1 66  ? -38.155 31.757  -32.350 1.00 21.82 ? 63  HIS   B CA  1 
ATOM   3257 C C   . HIS   B 1 66  ? -37.938 31.060  -31.009 1.00 20.83 ? 63  HIS   B C   1 
ATOM   3258 O O   . HIS   B 1 66  ? -36.831 31.039  -30.466 1.00 19.32 ? 63  HIS   B O   1 
ATOM   3259 C CB  . HIS   B 1 66  ? -38.120 30.716  -33.482 1.00 20.91 ? 63  HIS   B CB  1 
ATOM   3260 C CG  . HIS   B 1 66  ? -37.037 29.679  -33.347 1.00 22.77 ? 63  HIS   B CG  1 
ATOM   3261 N ND1 . HIS   B 1 66  ? -35.759 29.871  -33.830 1.00 22.90 ? 63  HIS   B ND1 1 
ATOM   3262 C CD2 . HIS   B 1 66  ? -37.059 28.421  -32.830 1.00 21.42 ? 63  HIS   B CD2 1 
ATOM   3263 C CE1 . HIS   B 1 66  ? -35.035 28.785  -33.600 1.00 23.00 ? 63  HIS   B CE1 1 
ATOM   3264 N NE2 . HIS   B 1 66  ? -35.799 27.889  -32.995 1.00 22.78 ? 63  HIS   B NE2 1 
ATOM   3265 N N   . MET   B 1 67  ? -39.017 30.500  -30.463 1.00 20.55 ? 64  MET   B N   1 
ATOM   3266 C CA  . MET   B 1 67  ? -38.941 29.790  -29.191 1.00 18.80 ? 64  MET   B CA  1 
ATOM   3267 C C   . MET   B 1 67  ? -38.402 28.387  -29.426 1.00 21.38 ? 64  MET   B C   1 
ATOM   3268 O O   . MET   B 1 67  ? -39.021 27.593  -30.148 1.00 21.32 ? 64  MET   B O   1 
ATOM   3269 C CB  . MET   B 1 67  ? -40.319 29.728  -28.523 1.00 20.04 ? 64  MET   B CB  1 
ATOM   3270 C CG  . MET   B 1 67  ? -40.352 29.041  -27.140 1.00 17.71 ? 64  MET   B CG  1 
ATOM   3271 S SD  . MET   B 1 67  ? -39.524 29.992  -25.836 1.00 23.94 ? 64  MET   B SD  1 
ATOM   3272 C CE  . MET   B 1 67  ? -38.025 29.169  -25.577 1.00 28.65 ? 64  MET   B CE  1 
ATOM   3273 N N   . GLY   B 1 68  ? -37.256 28.084  -28.814 1.00 20.58 ? 65  GLY   B N   1 
ATOM   3274 C CA  . GLY   B 1 68  ? -36.739 26.729  -28.863 1.00 21.26 ? 65  GLY   B CA  1 
ATOM   3275 C C   . GLY   B 1 68  ? -37.636 25.742  -28.136 1.00 21.07 ? 65  GLY   B C   1 
ATOM   3276 O O   . GLY   B 1 68  ? -38.391 26.094  -27.225 1.00 20.02 ? 65  GLY   B O   1 
ATOM   3277 N N   . ALA   B 1 69  ? -37.550 24.481  -28.553 1.00 22.74 ? 66  ALA   B N   1 
ATOM   3278 C CA  . ALA   B 1 69  ? -38.332 23.422  -27.926 1.00 21.58 ? 66  ALA   B CA  1 
ATOM   3279 C C   . ALA   B 1 69  ? -37.916 22.082  -28.522 1.00 19.61 ? 66  ALA   B C   1 
ATOM   3280 O O   . ALA   B 1 69  ? -37.467 22.022  -29.668 1.00 21.06 ? 66  ALA   B O   1 
ATOM   3281 C CB  . ALA   B 1 69  ? -39.843 23.653  -28.123 1.00 19.56 ? 66  ALA   B CB  1 
ATOM   3282 N N   . ASP   B 1 70  ? -38.061 21.018  -27.731 1.00 20.86 ? 67  ASP   B N   1 
ATOM   3283 C CA  . ASP   B 1 70  ? -37.871 19.669  -28.247 1.00 24.05 ? 67  ASP   B CA  1 
ATOM   3284 C C   . ASP   B 1 70  ? -38.969 19.350  -29.259 1.00 24.16 ? 67  ASP   B C   1 
ATOM   3285 O O   . ASP   B 1 70  ? -40.136 19.702  -29.057 1.00 22.26 ? 67  ASP   B O   1 
ATOM   3286 C CB  . ASP   B 1 70  ? -37.904 18.651  -27.101 1.00 24.53 ? 67  ASP   B CB  1 
ATOM   3287 C CG  . ASP   B 1 70  ? -37.234 17.317  -27.468 1.00 29.67 ? 67  ASP   B CG  1 
ATOM   3288 O OD1 . ASP   B 1 70  ? -36.699 17.191  -28.585 1.00 28.74 ? 67  ASP   B OD1 1 
ATOM   3289 O OD2 . ASP   B 1 70  ? -37.229 16.388  -26.611 1.00 29.67 ? 67  ASP   B OD2 1 
ATOM   3290 N N   . SER   B 1 71  ? -38.603 18.681  -30.355 1.00 23.74 ? 68  SER   B N   1 
ATOM   3291 C CA  . SER   B 1 71  ? -39.588 18.421  -31.402 1.00 23.35 ? 68  SER   B CA  1 
ATOM   3292 C C   . SER   B 1 71  ? -39.264 17.134  -32.152 1.00 28.59 ? 68  SER   B C   1 
ATOM   3293 O O   . SER   B 1 71  ? -38.137 16.627  -32.118 1.00 26.90 ? 68  SER   B O   1 
ATOM   3294 C CB  . SER   B 1 71  ? -39.672 19.586  -32.407 1.00 24.71 ? 68  SER   B CB  1 
ATOM   3295 O OG  . SER   B 1 71  ? -38.500 19.682  -33.214 1.00 23.12 ? 68  SER   B OG  1 
ATOM   3296 N N   . ILE   B 1 72  ? -40.282 16.615  -32.838 1.00 25.46 ? 69  ILE   B N   1 
ATOM   3297 C CA  . ILE   B 1 72  ? -40.146 15.533  -33.810 1.00 24.70 ? 69  ILE   B CA  1 
ATOM   3298 C C   . ILE   B 1 72  ? -40.335 16.122  -35.197 1.00 25.37 ? 69  ILE   B C   1 
ATOM   3299 O O   . ILE   B 1 72  ? -41.332 16.804  -35.455 1.00 25.47 ? 69  ILE   B O   1 
ATOM   3300 C CB  . ILE   B 1 72  ? -41.168 14.410  -33.562 1.00 27.32 ? 69  ILE   B CB  1 
ATOM   3301 C CG1 . ILE   B 1 72  ? -40.918 13.748  -32.213 1.00 25.68 ? 69  ILE   B CG1 1 
ATOM   3302 C CG2 . ILE   B 1 72  ? -41.111 13.370  -34.695 1.00 25.63 ? 69  ILE   B CG2 1 
ATOM   3303 C CD1 . ILE   B 1 72  ? -42.139 12.992  -31.718 1.00 31.35 ? 69  ILE   B CD1 1 
ATOM   3304 N N   . MET   B 1 73  ? -39.402 15.821  -36.099 1.00 26.28 ? 70  MET   B N   1 
ATOM   3305 C CA  . MET   B 1 73  ? -39.346 16.451  -37.404 1.00 28.67 ? 70  MET   B CA  1 
ATOM   3306 C C   . MET   B 1 73  ? -39.171 15.411  -38.500 1.00 28.55 ? 70  MET   B C   1 
ATOM   3307 O O   . MET   B 1 73  ? -38.617 14.328  -38.276 1.00 27.87 ? 70  MET   B O   1 
ATOM   3308 C CB  . MET   B 1 73  ? -38.198 17.455  -37.473 1.00 22.80 ? 70  MET   B CB  1 
ATOM   3309 C CG  . MET   B 1 73  ? -38.356 18.635  -36.544 1.00 21.79 ? 70  MET   B CG  1 
ATOM   3310 S SD  . MET   B 1 73  ? -36.739 19.451  -36.387 1.00 27.32 ? 70  MET   B SD  1 
ATOM   3311 C CE  . MET   B 1 73  ? -36.014 18.468  -35.073 1.00 27.64 ? 70  MET   B CE  1 
ATOM   3312 N N   . GLN   B 1 74  ? -39.621 15.764  -39.698 1.00 28.99 ? 71  GLN   B N   1 
ATOM   3313 C CA  . GLN   B 1 74  ? -39.474 14.910  -40.870 1.00 27.88 ? 71  GLN   B CA  1 
ATOM   3314 C C   . GLN   B 1 74  ? -38.602 15.610  -41.900 1.00 29.22 ? 71  GLN   B C   1 
ATOM   3315 O O   . GLN   B 1 74  ? -38.838 16.779  -42.235 1.00 28.39 ? 71  GLN   B O   1 
ATOM   3316 C CB  . GLN   B 1 74  ? -40.846 14.564  -41.463 1.00 30.12 ? 71  GLN   B CB  1 
ATOM   3317 C CG  . GLN   B 1 74  ? -40.789 13.798  -42.772 1.00 30.61 ? 71  GLN   B CG  1 
ATOM   3318 C CD  . GLN   B 1 74  ? -42.175 13.479  -43.293 1.00 42.42 ? 71  GLN   B CD  1 
ATOM   3319 O OE1 . GLN   B 1 74  ? -42.918 14.373  -43.697 1.00 45.46 ? 71  GLN   B OE1 1 
ATOM   3320 N NE2 . GLN   B 1 74  ? -42.536 12.206  -43.273 1.00 47.53 ? 71  GLN   B NE2 1 
ATOM   3321 N N   . VAL   B 1 75  ? -37.589 14.900  -42.398 1.00 29.60 ? 72  VAL   B N   1 
ATOM   3322 C CA  . VAL   B 1 75  ? -36.699 15.476  -43.399 1.00 29.26 ? 72  VAL   B CA  1 
ATOM   3323 C C   . VAL   B 1 75  ? -37.447 15.594  -44.719 1.00 35.54 ? 72  VAL   B C   1 
ATOM   3324 O O   . VAL   B 1 75  ? -37.866 14.587  -45.306 1.00 30.80 ? 72  VAL   B O   1 
ATOM   3325 C CB  . VAL   B 1 75  ? -35.437 14.620  -43.571 1.00 29.81 ? 72  VAL   B CB  1 
ATOM   3326 C CG1 . VAL   B 1 75  ? -34.440 15.335  -44.464 1.00 31.08 ? 72  VAL   B CG1 1 
ATOM   3327 C CG2 . VAL   B 1 75  ? -34.832 14.281  -42.220 1.00 33.49 ? 72  VAL   B CG2 1 
ATOM   3328 N N   . LEU   B 1 76  ? -37.627 16.826  -45.195 1.00 30.35 ? 73  LEU   B N   1 
ATOM   3329 C CA  . LEU   B 1 76  ? -38.271 17.033  -46.488 1.00 33.88 ? 73  LEU   B CA  1 
ATOM   3330 C C   . LEU   B 1 76  ? -37.270 16.972  -47.624 1.00 36.38 ? 73  LEU   B C   1 
ATOM   3331 O O   . LEU   B 1 76  ? -37.567 16.424  -48.686 1.00 36.07 ? 73  LEU   B O   1 
ATOM   3332 C CB  . LEU   B 1 76  ? -38.995 18.382  -46.529 1.00 29.41 ? 73  LEU   B CB  1 
ATOM   3333 C CG  . LEU   B 1 76  ? -40.250 18.523  -45.658 1.00 31.63 ? 73  LEU   B CG  1 
ATOM   3334 C CD1 . LEU   B 1 76  ? -40.863 19.888  -45.884 1.00 28.04 ? 73  LEU   B CD1 1 
ATOM   3335 C CD2 . LEU   B 1 76  ? -41.242 17.425  -45.987 1.00 37.13 ? 73  LEU   B CD2 1 
ATOM   3336 N N   . ASP   B 1 77  ? -36.094 17.549  -47.415 1.00 33.36 ? 74  ASP   B N   1 
ATOM   3337 C CA  . ASP   B 1 77  ? -35.047 17.595  -48.422 1.00 33.35 ? 74  ASP   B CA  1 
ATOM   3338 C C   . ASP   B 1 77  ? -33.727 17.621  -47.678 1.00 36.20 ? 74  ASP   B C   1 
ATOM   3339 O O   . ASP   B 1 77  ? -33.671 17.972  -46.497 1.00 36.04 ? 74  ASP   B O   1 
ATOM   3340 C CB  . ASP   B 1 77  ? -35.197 18.819  -49.333 1.00 31.64 ? 74  ASP   B CB  1 
ATOM   3341 C CG  . ASP   B 1 77  ? -34.294 18.762  -50.563 1.00 44.18 ? 74  ASP   B CG  1 
ATOM   3342 O OD1 . ASP   B 1 77  ? -33.788 17.663  -50.908 1.00 42.22 ? 74  ASP   B OD1 1 
ATOM   3343 O OD2 . ASP   B 1 77  ? -34.100 19.830  -51.190 1.00 39.99 ? 74  ASP   B OD2 1 
ATOM   3344 N N   . ALA   B 1 78  ? -32.660 17.242  -48.370 1.00 34.54 ? 75  ALA   B N   1 
ATOM   3345 C CA  . ALA   B 1 78  ? -31.373 17.134  -47.702 1.00 38.11 ? 75  ALA   B CA  1 
ATOM   3346 C C   . ALA   B 1 78  ? -30.260 17.320  -48.714 1.00 40.65 ? 75  ALA   B C   1 
ATOM   3347 O O   . ALA   B 1 78  ? -30.342 16.803  -49.834 1.00 38.84 ? 75  ALA   B O   1 
ATOM   3348 C CB  . ALA   B 1 78  ? -31.228 15.784  -46.996 1.00 36.04 ? 75  ALA   B CB  1 
ATOM   3349 N N   . GLY   B 1 79  ? -29.230 18.065  -48.318 1.00 35.49 ? 76  GLY   B N   1 
ATOM   3350 C CA  . GLY   B 1 79  ? -28.043 18.204  -49.128 1.00 40.10 ? 76  GLY   B CA  1 
ATOM   3351 C C   . GLY   B 1 79  ? -27.302 16.885  -49.207 1.00 41.24 ? 76  GLY   B C   1 
ATOM   3352 O O   . GLY   B 1 79  ? -27.552 15.962  -48.424 1.00 39.95 ? 76  GLY   B O   1 
ATOM   3353 N N   . PRO   B 1 80  ? -26.372 16.766  -50.156 1.00 45.36 ? 77  PRO   B N   1 
ATOM   3354 C CA  . PRO   B 1 80  ? -25.737 15.456  -50.385 1.00 48.84 ? 77  PRO   B CA  1 
ATOM   3355 C C   . PRO   B 1 80  ? -24.991 14.915  -49.174 1.00 44.79 ? 77  PRO   B C   1 
ATOM   3356 O O   . PRO   B 1 80  ? -24.963 13.693  -48.974 1.00 45.19 ? 77  PRO   B O   1 
ATOM   3357 C CB  . PRO   B 1 80  ? -24.799 15.724  -51.572 1.00 49.16 ? 77  PRO   B CB  1 
ATOM   3358 C CG  . PRO   B 1 80  ? -24.560 17.194  -51.547 1.00 51.79 ? 77  PRO   B CG  1 
ATOM   3359 C CD  . PRO   B 1 80  ? -25.828 17.813  -51.032 1.00 45.88 ? 77  PRO   B CD  1 
ATOM   3360 N N   . ASN   B 1 81  ? -24.400 15.777  -48.343 1.00 45.64 ? 78  ASN   B N   1 
ATOM   3361 C CA  . ASN   B 1 81  ? -23.678 15.331  -47.156 1.00 44.42 ? 78  ASN   B CA  1 
ATOM   3362 C C   . ASN   B 1 81  ? -24.488 15.497  -45.874 1.00 42.87 ? 78  ASN   B C   1 
ATOM   3363 O O   . ASN   B 1 81  ? -23.906 15.668  -44.801 1.00 41.77 ? 78  ASN   B O   1 
ATOM   3364 C CB  . ASN   B 1 81  ? -22.347 16.074  -47.028 1.00 47.09 ? 78  ASN   B CB  1 
ATOM   3365 C CG  . ASN   B 1 81  ? -21.346 15.645  -48.067 1.00 56.53 ? 78  ASN   B CG  1 
ATOM   3366 O OD1 . ASN   B 1 81  ? -21.506 14.598  -48.698 1.00 57.84 ? 78  ASN   B OD1 1 
ATOM   3367 N ND2 . ASN   B 1 81  ? -20.300 16.445  -48.255 1.00 56.88 ? 78  ASN   B ND2 1 
ATOM   3368 N N   . ALA   B 1 82  ? -25.825 15.437  -45.959 1.00 44.81 ? 79  ALA   B N   1 
ATOM   3369 C CA  . ALA   B 1 82  ? -26.640 15.630  -44.768 1.00 39.17 ? 79  ALA   B CA  1 
ATOM   3370 C C   . ALA   B 1 82  ? -26.628 14.380  -43.891 1.00 40.37 ? 79  ALA   B C   1 
ATOM   3371 O O   . ALA   B 1 82  ? -26.541 13.258  -44.398 1.00 40.59 ? 79  ALA   B O   1 
ATOM   3372 C CB  . ALA   B 1 82  ? -28.078 15.971  -45.150 1.00 35.94 ? 79  ALA   B CB  1 
ATOM   3373 N N   . PRO   B 1 83  ? -26.720 14.546  -42.569 1.00 37.65 ? 80  PRO   B N   1 
ATOM   3374 C CA  . PRO   B 1 83  ? -26.747 13.371  -41.688 1.00 35.84 ? 80  PRO   B CA  1 
ATOM   3375 C C   . PRO   B 1 83  ? -27.955 12.485  -41.900 1.00 39.32 ? 80  PRO   B C   1 
ATOM   3376 O O   . PRO   B 1 83  ? -27.946 11.339  -41.444 1.00 41.40 ? 80  PRO   B O   1 
ATOM   3377 C CB  . PRO   B 1 83  ? -26.768 13.991  -40.284 1.00 41.77 ? 80  PRO   B CB  1 
ATOM   3378 C CG  . PRO   B 1 83  ? -27.458 15.313  -40.494 1.00 35.88 ? 80  PRO   B CG  1 
ATOM   3379 C CD  . PRO   B 1 83  ? -26.911 15.799  -41.813 1.00 33.82 ? 80  PRO   B CD  1 
ATOM   3380 N N   . PHE   B 1 84  ? -29.007 12.979  -42.551 1.00 39.04 ? 81  PHE   B N   1 
ATOM   3381 C CA  . PHE   B 1 84  ? -30.233 12.214  -42.693 1.00 40.21 ? 81  PHE   B CA  1 
ATOM   3382 C C   . PHE   B 1 84  ? -30.807 12.432  -44.085 1.00 39.36 ? 81  PHE   B C   1 
ATOM   3383 O O   . PHE   B 1 84  ? -30.476 13.399  -44.773 1.00 39.41 ? 81  PHE   B O   1 
ATOM   3384 C CB  . PHE   B 1 84  ? -31.246 12.585  -41.604 1.00 36.82 ? 81  PHE   B CB  1 
ATOM   3385 C CG  . PHE   B 1 84  ? -30.709 12.415  -40.215 1.00 38.21 ? 81  PHE   B CG  1 
ATOM   3386 C CD1 . PHE   B 1 84  ? -30.464 11.151  -39.701 1.00 40.43 ? 81  PHE   B CD1 1 
ATOM   3387 C CD2 . PHE   B 1 84  ? -30.431 13.524  -39.425 1.00 38.29 ? 81  PHE   B CD2 1 
ATOM   3388 C CE1 . PHE   B 1 84  ? -29.964 10.992  -38.412 1.00 39.85 ? 81  PHE   B CE1 1 
ATOM   3389 C CE2 . PHE   B 1 84  ? -29.927 13.374  -38.146 1.00 39.10 ? 81  PHE   B CE2 1 
ATOM   3390 C CZ  . PHE   B 1 84  ? -29.695 12.108  -37.635 1.00 36.32 ? 81  PHE   B CZ  1 
ATOM   3391 N N   . ARG   B 1 85  ? -31.664 11.511  -44.502 1.00 40.13 ? 82  ARG   B N   1 
ATOM   3392 C CA  . ARG   B 1 85  ? -32.187 11.534  -45.856 1.00 39.01 ? 82  ARG   B CA  1 
ATOM   3393 C C   . ARG   B 1 85  ? -33.668 11.886  -45.869 1.00 35.80 ? 82  ARG   B C   1 
ATOM   3394 O O   . ARG   B 1 85  ? -34.372 11.738  -44.862 1.00 35.29 ? 82  ARG   B O   1 
ATOM   3395 C CB  . ARG   B 1 85  ? -31.989 10.177  -46.550 1.00 41.45 ? 82  ARG   B CB  1 
ATOM   3396 C CG  . ARG   B 1 85  ? -30.568 9.625   -46.516 1.00 45.41 ? 82  ARG   B CG  1 
ATOM   3397 C CD  . ARG   B 1 85  ? -29.549 10.639  -46.998 1.00 46.99 ? 82  ARG   B CD  1 
ATOM   3398 N NE  . ARG   B 1 85  ? -29.997 11.375  -48.174 1.00 48.08 ? 82  ARG   B NE  1 
ATOM   3399 C CZ  . ARG   B 1 85  ? -29.425 12.489  -48.618 1.00 50.35 ? 82  ARG   B CZ  1 
ATOM   3400 N NH1 . ARG   B 1 85  ? -28.380 13.024  -48.000 1.00 43.16 ? 82  ARG   B NH1 1 
ATOM   3401 N NH2 . ARG   B 1 85  ? -29.916 13.085  -49.703 1.00 46.38 ? 82  ARG   B NH2 1 
ATOM   3402 N N   . PRO   B 1 86  ? -34.171 12.357  -47.007 1.00 34.87 ? 83  PRO   B N   1 
ATOM   3403 C CA  . PRO   B 1 86  ? -35.601 12.652  -47.125 1.00 37.80 ? 83  PRO   B CA  1 
ATOM   3404 C C   . PRO   B 1 86  ? -36.461 11.488  -46.657 1.00 37.41 ? 83  PRO   B C   1 
ATOM   3405 O O   . PRO   B 1 86  ? -36.173 10.319  -46.926 1.00 38.15 ? 83  PRO   B O   1 
ATOM   3406 C CB  . PRO   B 1 86  ? -35.772 12.924  -48.622 1.00 35.54 ? 83  PRO   B CB  1 
ATOM   3407 C CG  . PRO   B 1 86  ? -34.458 13.522  -49.019 1.00 38.75 ? 83  PRO   B CG  1 
ATOM   3408 C CD  . PRO   B 1 86  ? -33.412 12.814  -48.183 1.00 37.57 ? 83  PRO   B CD  1 
ATOM   3409 N N   . GLY   B 1 87  ? -37.524 11.823  -45.936 1.00 33.89 ? 84  GLY   B N   1 
ATOM   3410 C CA  . GLY   B 1 87  ? -38.389 10.848  -45.333 1.00 33.92 ? 84  GLY   B CA  1 
ATOM   3411 C C   . GLY   B 1 87  ? -37.977 10.396  -43.946 1.00 33.33 ? 84  GLY   B C   1 
ATOM   3412 O O   . GLY   B 1 87  ? -38.800 9.802   -43.238 1.00 31.80 ? 84  GLY   B O   1 
ATOM   3413 N N   . ASP   B 1 88  ? -36.733 10.644  -43.536 1.00 34.40 ? 85  ASP   B N   1 
ATOM   3414 C CA  . ASP   B 1 88  ? -36.311 10.255  -42.199 1.00 34.28 ? 85  ASP   B CA  1 
ATOM   3415 C C   . ASP   B 1 88  ? -37.049 11.076  -41.146 1.00 33.27 ? 85  ASP   B C   1 
ATOM   3416 O O   . ASP   B 1 88  ? -37.360 12.250  -41.347 1.00 33.35 ? 85  ASP   B O   1 
ATOM   3417 C CB  . ASP   B 1 88  ? -34.801 10.441  -42.031 1.00 35.85 ? 85  ASP   B CB  1 
ATOM   3418 C CG  . ASP   B 1 88  ? -33.989 9.375   -42.761 1.00 41.20 ? 85  ASP   B CG  1 
ATOM   3419 O OD1 . ASP   B 1 88  ? -34.547 8.299   -43.078 1.00 35.21 ? 85  ASP   B OD1 1 
ATOM   3420 O OD2 . ASP   B 1 88  ? -32.792 9.612   -43.004 1.00 40.34 ? 85  ASP   B OD2 1 
ATOM   3421 N N   . LEU   B 1 89  ? -37.341 10.435  -40.013 1.00 35.59 ? 86  LEU   B N   1 
ATOM   3422 C CA  . LEU   B 1 89  ? -37.908 11.102  -38.846 1.00 33.85 ? 86  LEU   B CA  1 
ATOM   3423 C C   . LEU   B 1 89  ? -36.813 11.279  -37.802 1.00 36.61 ? 86  LEU   B C   1 
ATOM   3424 O O   . LEU   B 1 89  ? -36.007 10.365  -37.581 1.00 33.01 ? 86  LEU   B O   1 
ATOM   3425 C CB  . LEU   B 1 89  ? -39.070 10.298  -38.258 1.00 30.07 ? 86  LEU   B CB  1 
ATOM   3426 C CG  . LEU   B 1 89  ? -40.208 9.991   -39.230 1.00 35.65 ? 86  LEU   B CG  1 
ATOM   3427 C CD1 . LEU   B 1 89  ? -41.277 9.136   -38.560 1.00 36.56 ? 86  LEU   B CD1 1 
ATOM   3428 C CD2 . LEU   B 1 89  ? -40.811 11.274  -39.768 1.00 30.11 ? 86  LEU   B CD2 1 
ATOM   3429 N N   . VAL   B 1 90  ? -36.769 12.463  -37.176 1.00 33.30 ? 87  VAL   B N   1 
ATOM   3430 C CA  . VAL   B 1 90  ? -35.708 12.785  -36.227 1.00 29.67 ? 87  VAL   B CA  1 
ATOM   3431 C C   . VAL   B 1 90  ? -36.271 13.570  -35.048 1.00 29.26 ? 87  VAL   B C   1 
ATOM   3432 O O   . VAL   B 1 90  ? -37.266 14.292  -35.163 1.00 27.89 ? 87  VAL   B O   1 
ATOM   3433 C CB  . VAL   B 1 90  ? -34.545 13.577  -36.880 1.00 30.58 ? 87  VAL   B CB  1 
ATOM   3434 C CG1 . VAL   B 1 90  ? -33.906 12.772  -37.987 1.00 34.51 ? 87  VAL   B CG1 1 
ATOM   3435 C CG2 . VAL   B 1 90  ? -35.034 14.922  -37.411 1.00 30.48 ? 87  VAL   B CG2 1 
ATOM   3436 N N   . GLN   B 1 91  ? -35.608 13.432  -33.905 1.00 28.69 ? 88  GLN   B N   1 
ATOM   3437 C CA  . GLN   B 1 91  ? -35.908 14.217  -32.720 1.00 27.11 ? 88  GLN   B CA  1 
ATOM   3438 C C   . GLN   B 1 91  ? -34.754 15.177  -32.465 1.00 31.85 ? 88  GLN   B C   1 
ATOM   3439 O O   . GLN   B 1 91  ? -33.583 14.830  -32.668 1.00 32.12 ? 88  GLN   B O   1 
ATOM   3440 C CB  . GLN   B 1 91  ? -36.144 13.318  -31.504 1.00 26.11 ? 88  GLN   B CB  1 
ATOM   3441 C CG  . GLN   B 1 91  ? -36.286 14.082  -30.167 1.00 29.49 ? 88  GLN   B CG  1 
ATOM   3442 C CD  . GLN   B 1 91  ? -34.976 14.230  -29.430 1.00 30.62 ? 88  GLN   B CD  1 
ATOM   3443 O OE1 . GLN   B 1 91  ? -34.145 13.314  -29.407 1.00 38.16 ? 88  GLN   B OE1 1 
ATOM   3444 N NE2 . GLN   B 1 91  ? -34.773 15.381  -28.803 1.00 31.22 ? 88  GLN   B NE2 1 
ATOM   3445 N N   . GLY   B 1 92  ? -35.090 16.385  -32.038 1.00 25.91 ? 89  GLY   B N   1 
ATOM   3446 C CA  . GLY   B 1 92  ? -34.081 17.407  -31.805 1.00 26.33 ? 89  GLY   B CA  1 
ATOM   3447 C C   . GLY   B 1 92  ? -34.772 18.686  -31.398 1.00 25.70 ? 89  GLY   B C   1 
ATOM   3448 O O   . GLY   B 1 92  ? -36.004 18.771  -31.381 1.00 23.29 ? 89  GLY   B O   1 
ATOM   3449 N N   . PHE   B 1 93  ? -33.959 19.690  -31.070 1.00 25.14 ? 90  PHE   B N   1 
ATOM   3450 C CA  . PHE   B 1 93  ? -34.465 20.953  -30.526 1.00 26.94 ? 90  PHE   B CA  1 
ATOM   3451 C C   . PHE   B 1 93  ? -34.864 21.900  -31.657 1.00 23.69 ? 90  PHE   B C   1 
ATOM   3452 O O   . PHE   B 1 93  ? -34.279 22.968  -31.866 1.00 25.76 ? 90  PHE   B O   1 
ATOM   3453 C CB  . PHE   B 1 93  ? -33.425 21.592  -29.614 1.00 22.85 ? 90  PHE   B CB  1 
ATOM   3454 C CG  . PHE   B 1 93  ? -34.015 22.486  -28.550 1.00 24.33 ? 90  PHE   B CG  1 
ATOM   3455 C CD1 . PHE   B 1 93  ? -34.837 21.958  -27.576 1.00 20.42 ? 90  PHE   B CD1 1 
ATOM   3456 C CD2 . PHE   B 1 93  ? -33.730 23.850  -28.517 1.00 24.42 ? 90  PHE   B CD2 1 
ATOM   3457 C CE1 . PHE   B 1 93  ? -35.372 22.768  -26.573 1.00 23.97 ? 90  PHE   B CE1 1 
ATOM   3458 C CE2 . PHE   B 1 93  ? -34.255 24.655  -27.513 1.00 22.93 ? 90  PHE   B CE2 1 
ATOM   3459 C CZ  . PHE   B 1 93  ? -35.066 24.105  -26.542 1.00 21.43 ? 90  PHE   B CZ  1 
ATOM   3460 N N   . GLY   B 1 94  ? -35.883 21.475  -32.410 1.00 23.70 ? 91  GLY   B N   1 
ATOM   3461 C CA  . GLY   B 1 94  ? -36.308 22.242  -33.573 1.00 22.76 ? 91  GLY   B CA  1 
ATOM   3462 C C   . GLY   B 1 94  ? -37.111 23.483  -33.258 1.00 23.65 ? 91  GLY   B C   1 
ATOM   3463 O O   . GLY   B 1 94  ? -37.170 24.395  -34.089 1.00 23.62 ? 91  GLY   B O   1 
ATOM   3464 N N   . GLY   B 1 95  ? -37.754 23.531  -32.094 1.00 21.27 ? 92  GLY   B N   1 
ATOM   3465 C CA  . GLY   B 1 95  ? -38.504 24.714  -31.692 1.00 23.78 ? 92  GLY   B CA  1 
ATOM   3466 C C   . GLY   B 1 95  ? -39.914 24.805  -32.275 1.00 21.16 ? 92  GLY   B C   1 
ATOM   3467 O O   . GLY   B 1 95  ? -40.381 23.959  -33.047 1.00 20.34 ? 92  GLY   B O   1 
ATOM   3468 N N   . TRP   B 1 96  ? -40.595 25.885  -31.876 1.00 20.11 ? 93  TRP   B N   1 
ATOM   3469 C CA  . TRP   B 1 96  ? -41.972 26.180  -32.271 1.00 20.96 ? 93  TRP   B CA  1 
ATOM   3470 C C   . TRP   B 1 96  ? -41.974 26.869  -33.640 1.00 19.71 ? 93  TRP   B C   1 
ATOM   3471 O O   . TRP   B 1 96  ? -42.161 28.082  -33.771 1.00 20.58 ? 93  TRP   B O   1 
ATOM   3472 C CB  . TRP   B 1 96  ? -42.648 27.053  -31.219 1.00 15.83 ? 93  TRP   B CB  1 
ATOM   3473 C CG  . TRP   B 1 96  ? -42.824 26.428  -29.847 1.00 19.21 ? 93  TRP   B CG  1 
ATOM   3474 C CD1 . TRP   B 1 96  ? -42.588 25.119  -29.478 1.00 20.86 ? 93  TRP   B CD1 1 
ATOM   3475 C CD2 . TRP   B 1 96  ? -43.271 27.098  -28.664 1.00 17.07 ? 93  TRP   B CD2 1 
ATOM   3476 N NE1 . TRP   B 1 96  ? -42.870 24.950  -28.140 1.00 19.23 ? 93  TRP   B NE1 1 
ATOM   3477 C CE2 . TRP   B 1 96  ? -43.294 26.147  -27.620 1.00 18.65 ? 93  TRP   B CE2 1 
ATOM   3478 C CE3 . TRP   B 1 96  ? -43.667 28.415  -28.389 1.00 20.18 ? 93  TRP   B CE3 1 
ATOM   3479 C CZ2 . TRP   B 1 96  ? -43.668 26.480  -26.312 1.00 20.65 ? 93  TRP   B CZ2 1 
ATOM   3480 C CZ3 . TRP   B 1 96  ? -44.054 28.736  -27.106 1.00 22.71 ? 93  TRP   B CZ3 1 
ATOM   3481 C CH2 . TRP   B 1 96  ? -44.061 27.769  -26.079 1.00 20.39 ? 93  TRP   B CH2 1 
ATOM   3482 N N   . ARG   B 1 97  ? -41.709 26.065  -34.671 1.00 18.45 ? 94  ARG   B N   1 
ATOM   3483 C CA  . ARG   B 1 97  ? -41.734 26.500  -36.060 1.00 20.53 ? 94  ARG   B CA  1 
ATOM   3484 C C   . ARG   B 1 97  ? -42.373 25.392  -36.883 1.00 22.80 ? 94  ARG   B C   1 
ATOM   3485 O O   . ARG   B 1 97  ? -42.209 24.210  -36.564 1.00 22.74 ? 94  ARG   B O   1 
ATOM   3486 C CB  . ARG   B 1 97  ? -40.314 26.791  -36.589 1.00 23.08 ? 94  ARG   B CB  1 
ATOM   3487 C CG  . ARG   B 1 97  ? -39.495 27.776  -35.721 1.00 22.75 ? 94  ARG   B CG  1 
ATOM   3488 C CD  . ARG   B 1 97  ? -38.055 27.951  -36.256 1.00 22.67 ? 94  ARG   B CD  1 
ATOM   3489 N NE  . ARG   B 1 97  ? -37.160 26.865  -35.832 1.00 20.76 ? 94  ARG   B NE  1 
ATOM   3490 C CZ  . ARG   B 1 97  ? -35.876 26.769  -36.163 1.00 25.07 ? 94  ARG   B CZ  1 
ATOM   3491 N NH1 . ARG   B 1 97  ? -35.286 27.675  -36.933 1.00 23.61 ? 94  ARG   B NH1 1 
ATOM   3492 N NH2 . ARG   B 1 97  ? -35.159 25.744  -35.700 1.00 20.18 ? 94  ARG   B NH2 1 
ATOM   3493 N N   . THR   B 1 98  ? -43.103 25.762  -37.948 1.00 24.39 ? 95  THR   B N   1 
ATOM   3494 C CA  . THR   B 1 98  ? -43.684 24.720  -38.800 1.00 21.04 ? 95  THR   B CA  1 
ATOM   3495 C C   . THR   B 1 98  ? -42.603 24.016  -39.609 1.00 24.07 ? 95  THR   B C   1 
ATOM   3496 O O   . THR   B 1 98  ? -42.698 22.809  -39.869 1.00 22.43 ? 95  THR   B O   1 
ATOM   3497 C CB  . THR   B 1 98  ? -44.747 25.297  -39.746 1.00 22.79 ? 95  THR   B CB  1 
ATOM   3498 O OG1 . THR   B 1 98  ? -44.137 26.217  -40.651 1.00 20.47 ? 95  THR   B OG1 1 
ATOM   3499 C CG2 . THR   B 1 98  ? -45.874 26.005  -38.987 1.00 20.22 ? 95  THR   B CG2 1 
ATOM   3500 N N   . HIS   B 1 99  ? -41.586 24.762  -40.039 1.00 23.46 ? 96  HIS   B N   1 
ATOM   3501 C CA  . HIS   B 1 99  ? -40.511 24.234  -40.867 1.00 25.37 ? 96  HIS   B CA  1 
ATOM   3502 C C   . HIS   B 1 99  ? -39.237 24.975  -40.508 1.00 24.43 ? 96  HIS   B C   1 
ATOM   3503 O O   . HIS   B 1 99  ? -39.276 26.097  -40.007 1.00 24.26 ? 96  HIS   B O   1 
ATOM   3504 C CB  . HIS   B 1 99  ? -40.767 24.409  -42.380 1.00 22.73 ? 96  HIS   B CB  1 
ATOM   3505 C CG  . HIS   B 1 99  ? -42.097 23.905  -42.851 1.00 27.14 ? 96  HIS   B CG  1 
ATOM   3506 N ND1 . HIS   B 1 99  ? -43.284 24.526  -42.531 1.00 25.21 ? 96  HIS   B ND1 1 
ATOM   3507 C CD2 . HIS   B 1 99  ? -42.424 22.856  -43.648 1.00 28.68 ? 96  HIS   B CD2 1 
ATOM   3508 C CE1 . HIS   B 1 99  ? -44.288 23.870  -43.091 1.00 26.51 ? 96  HIS   B CE1 1 
ATOM   3509 N NE2 . HIS   B 1 99  ? -43.795 22.851  -43.774 1.00 25.37 ? 96  HIS   B NE2 1 
ATOM   3510 N N   . LEU   B 1 100 ? -38.098 24.346  -40.815 1.00 22.26 ? 97  LEU   B N   1 
ATOM   3511 C CA  . LEU   B 1 100 ? -36.798 24.920  -40.489 1.00 22.58 ? 97  LEU   B CA  1 
ATOM   3512 C C   . LEU   B 1 100 ? -35.729 24.266  -41.353 1.00 22.97 ? 97  LEU   B C   1 
ATOM   3513 O O   . LEU   B 1 100 ? -35.905 23.155  -41.857 1.00 24.64 ? 97  LEU   B O   1 
ATOM   3514 C CB  . LEU   B 1 100 ? -36.458 24.714  -39.008 1.00 21.37 ? 97  LEU   B CB  1 
ATOM   3515 C CG  . LEU   B 1 100 ? -36.459 23.248  -38.603 1.00 20.96 ? 97  LEU   B CG  1 
ATOM   3516 C CD1 . LEU   B 1 100 ? -35.114 22.796  -37.981 1.00 25.43 ? 97  LEU   B CD1 1 
ATOM   3517 C CD2 . LEU   B 1 100 ? -37.610 22.981  -37.630 1.00 22.67 ? 97  LEU   B CD2 1 
ATOM   3518 N N   . VAL   B 1 101 ? -34.604 24.957  -41.487 1.00 26.58 ? 98  VAL   B N   1 
ATOM   3519 C CA  . VAL   B 1 101 ? -33.414 24.429  -42.149 1.00 26.47 ? 98  VAL   B CA  1 
ATOM   3520 C C   . VAL   B 1 101 ? -32.321 24.255  -41.103 1.00 27.95 ? 98  VAL   B C   1 
ATOM   3521 O O   . VAL   B 1 101 ? -32.038 25.181  -40.332 1.00 25.84 ? 98  VAL   B O   1 
ATOM   3522 C CB  . VAL   B 1 101 ? -32.936 25.361  -43.275 1.00 27.43 ? 98  VAL   B CB  1 
ATOM   3523 C CG1 . VAL   B 1 101 ? -31.502 25.000  -43.691 1.00 28.65 ? 98  VAL   B CG1 1 
ATOM   3524 C CG2 . VAL   B 1 101 ? -33.876 25.294  -44.460 1.00 25.34 ? 98  VAL   B CG2 1 
ATOM   3525 N N   . SER   B 1 102 ? -31.683 23.088  -41.094 1.00 26.14 ? 99  SER   B N   1 
ATOM   3526 C CA  . SER   B 1 102 ? -30.629 22.845  -40.116 1.00 29.11 ? 99  SER   B CA  1 
ATOM   3527 C C   . SER   B 1 102 ? -29.716 21.742  -40.630 1.00 34.10 ? 99  SER   B C   1 
ATOM   3528 O O   . SER   B 1 102 ? -30.130 20.905  -41.438 1.00 31.49 ? 99  SER   B O   1 
ATOM   3529 C CB  . SER   B 1 102 ? -31.212 22.467  -38.747 1.00 26.88 ? 99  SER   B CB  1 
ATOM   3530 O OG  . SER   B 1 102 ? -30.227 21.937  -37.882 1.00 29.67 ? 99  SER   B OG  1 
ATOM   3531 N N   . ASP   B 1 103 ? -28.470 21.752  -40.153 1.00 32.80 ? 100 ASP   B N   1 
ATOM   3532 C CA  . ASP   B 1 103 ? -27.562 20.637  -40.388 1.00 33.37 ? 100 ASP   B CA  1 
ATOM   3533 C C   . ASP   B 1 103 ? -27.646 19.591  -39.291 1.00 30.89 ? 100 ASP   B C   1 
ATOM   3534 O O   . ASP   B 1 103 ? -26.961 18.572  -39.371 1.00 31.90 ? 100 ASP   B O   1 
ATOM   3535 C CB  . ASP   B 1 103 ? -26.119 21.143  -40.550 1.00 34.38 ? 100 ASP   B CB  1 
ATOM   3536 C CG  . ASP   B 1 103 ? -25.573 21.821  -39.298 1.00 34.83 ? 100 ASP   B CG  1 
ATOM   3537 O OD1 . ASP   B 1 103 ? -26.121 21.618  -38.186 1.00 32.93 ? 100 ASP   B OD1 1 
ATOM   3538 O OD2 . ASP   B 1 103 ? -24.575 22.562  -39.426 1.00 36.21 ? 100 ASP   B OD2 1 
ATOM   3539 N N   . GLY   B 1 104 ? -28.474 19.817  -38.276 1.00 30.41 ? 101 GLY   B N   1 
ATOM   3540 C CA  . GLY   B 1 104 ? -28.652 18.853  -37.208 1.00 31.09 ? 101 GLY   B CA  1 
ATOM   3541 C C   . GLY   B 1 104 ? -27.437 18.574  -36.331 1.00 28.51 ? 101 GLY   B C   1 
ATOM   3542 O O   . GLY   B 1 104 ? -27.447 17.600  -35.580 1.00 30.36 ? 101 GLY   B O   1 
ATOM   3543 N N   . LYS   B 1 105 ? -26.401 19.410  -36.406 1.00 29.49 ? 102 LYS   B N   1 
ATOM   3544 C CA  . LYS   B 1 105 ? -25.227 19.240  -35.552 1.00 32.88 ? 102 LYS   B CA  1 
ATOM   3545 C C   . LYS   B 1 105 ? -25.490 19.814  -34.159 1.00 31.20 ? 102 LYS   B C   1 
ATOM   3546 O O   . LYS   B 1 105 ? -26.409 20.606  -33.975 1.00 30.72 ? 102 LYS   B O   1 
ATOM   3547 C CB  . LYS   B 1 105 ? -24.015 19.933  -36.173 1.00 31.33 ? 102 LYS   B CB  1 
ATOM   3548 C CG  . LYS   B 1 105 ? -23.533 19.327  -37.491 1.00 34.04 ? 102 LYS   B CG  1 
ATOM   3549 C CD  . LYS   B 1 105 ? -22.390 20.133  -38.047 1.00 37.37 ? 102 LYS   B CD  1 
ATOM   3550 C CE  . LYS   B 1 105 ? -21.946 19.638  -39.413 1.00 48.89 ? 102 LYS   B CE  1 
ATOM   3551 N NZ  . LYS   B 1 105 ? -20.928 20.570  -39.986 1.00 48.65 ? 102 LYS   B NZ  1 
ATOM   3552 N N   . PRO   B 1 106 ? -24.689 19.431  -33.159 1.00 31.67 ? 103 PRO   B N   1 
ATOM   3553 C CA  . PRO   B 1 106 ? -24.807 20.067  -31.838 1.00 31.51 ? 103 PRO   B CA  1 
ATOM   3554 C C   . PRO   B 1 106 ? -24.640 21.574  -31.970 1.00 27.86 ? 103 PRO   B C   1 
ATOM   3555 O O   . PRO   B 1 106 ? -23.882 22.050  -32.813 1.00 29.10 ? 103 PRO   B O   1 
ATOM   3556 C CB  . PRO   B 1 106 ? -23.657 19.438  -31.033 1.00 29.49 ? 103 PRO   B CB  1 
ATOM   3557 C CG  . PRO   B 1 106 ? -23.330 18.180  -31.752 1.00 31.73 ? 103 PRO   B CG  1 
ATOM   3558 C CD  . PRO   B 1 106 ? -23.568 18.478  -33.211 1.00 28.32 ? 103 PRO   B CD  1 
ATOM   3559 N N   . LYS   B 1 107 ? -25.375 22.329  -31.151 1.00 28.86 ? 104 LYS   B N   1 
ATOM   3560 C CA  . LYS   B 1 107 ? -25.369 23.790  -31.253 1.00 29.50 ? 104 LYS   B CA  1 
ATOM   3561 C C   . LYS   B 1 107 ? -25.272 24.386  -29.862 1.00 28.17 ? 104 LYS   B C   1 
ATOM   3562 O O   . LYS   B 1 107 ? -26.129 24.121  -29.009 1.00 24.74 ? 104 LYS   B O   1 
ATOM   3563 C CB  . LYS   B 1 107 ? -26.625 24.333  -31.962 1.00 30.13 ? 104 LYS   B CB  1 
ATOM   3564 C CG  . LYS   B 1 107 ? -26.698 24.052  -33.462 1.00 37.78 ? 104 LYS   B CG  1 
ATOM   3565 C CD  . LYS   B 1 107 ? -25.323 24.199  -34.137 1.00 45.28 ? 104 LYS   B CD  1 
ATOM   3566 C CE  . LYS   B 1 107 ? -25.431 24.150  -35.668 1.00 44.73 ? 104 LYS   B CE  1 
ATOM   3567 N NZ  . LYS   B 1 107 ? -26.542 23.234  -36.100 1.00 39.65 ? 104 LYS   B NZ  1 
ATOM   3568 N N   . LEU   B 1 108 ? -24.239 25.202  -29.648 1.00 25.98 ? 105 LEU   B N   1 
ATOM   3569 C CA  . LEU   B 1 108 ? -24.114 25.943  -28.398 1.00 27.07 ? 105 LEU   B CA  1 
ATOM   3570 C C   . LEU   B 1 108 ? -25.273 26.925  -28.229 1.00 26.50 ? 105 LEU   B C   1 
ATOM   3571 O O   . LEU   B 1 108 ? -25.631 27.647  -29.161 1.00 25.18 ? 105 LEU   B O   1 
ATOM   3572 C CB  . LEU   B 1 108 ? -22.783 26.702  -28.377 1.00 27.84 ? 105 LEU   B CB  1 
ATOM   3573 C CG  . LEU   B 1 108 ? -22.590 27.652  -27.196 1.00 27.11 ? 105 LEU   B CG  1 
ATOM   3574 C CD1 . LEU   B 1 108 ? -22.435 26.893  -25.871 1.00 29.75 ? 105 LEU   B CD1 1 
ATOM   3575 C CD2 . LEU   B 1 108 ? -21.381 28.541  -27.470 1.00 35.08 ? 105 LEU   B CD2 1 
ATOM   3576 N N   . TRP   B 1 109 ? -25.850 26.964  -27.028 1.00 22.79 ? 106 TRP   B N   1 
ATOM   3577 C CA  . TRP   B 1 109 ? -26.911 27.920  -26.696 1.00 26.38 ? 106 TRP   B CA  1 
ATOM   3578 C C   . TRP   B 1 109 ? -26.217 29.205  -26.262 1.00 28.46 ? 106 TRP   B C   1 
ATOM   3579 O O   . TRP   B 1 109 ? -25.828 29.384  -25.102 1.00 24.69 ? 106 TRP   B O   1 
ATOM   3580 C CB  . TRP   B 1 109 ? -27.827 27.351  -25.617 1.00 23.47 ? 106 TRP   B CB  1 
ATOM   3581 C CG  . TRP   B 1 109 ? -28.985 28.248  -25.164 1.00 22.09 ? 106 TRP   B CG  1 
ATOM   3582 C CD1 . TRP   B 1 109 ? -29.399 28.438  -23.881 1.00 21.60 ? 106 TRP   B CD1 1 
ATOM   3583 C CD2 . TRP   B 1 109 ? -29.868 29.033  -25.993 1.00 23.71 ? 106 TRP   B CD2 1 
ATOM   3584 N NE1 . TRP   B 1 109 ? -30.482 29.293  -23.847 1.00 23.41 ? 106 TRP   B NE1 1 
ATOM   3585 C CE2 . TRP   B 1 109 ? -30.781 29.683  -25.127 1.00 19.74 ? 106 TRP   B CE2 1 
ATOM   3586 C CE3 . TRP   B 1 109 ? -29.967 29.258  -27.374 1.00 24.11 ? 106 TRP   B CE3 1 
ATOM   3587 C CZ2 . TRP   B 1 109 ? -31.796 30.524  -25.593 1.00 21.70 ? 106 TRP   B CZ2 1 
ATOM   3588 C CZ3 . TRP   B 1 109 ? -30.976 30.113  -27.845 1.00 25.34 ? 106 TRP   B CZ3 1 
ATOM   3589 C CH2 . TRP   B 1 109 ? -31.881 30.730  -26.951 1.00 22.65 ? 106 TRP   B CH2 1 
ATOM   3590 N N   . GLN   B 1 110 ? -26.034 30.109  -27.227 1.00 28.94 ? 107 GLN   B N   1 
ATOM   3591 C CA  . GLN   B 1 110 ? -25.090 31.202  -27.048 1.00 28.52 ? 107 GLN   B CA  1 
ATOM   3592 C C   . GLN   B 1 110 ? -25.559 32.243  -26.051 1.00 26.54 ? 107 GLN   B C   1 
ATOM   3593 O O   . GLN   B 1 110 ? -24.722 32.937  -25.474 1.00 26.71 ? 107 GLN   B O   1 
ATOM   3594 C CB  . GLN   B 1 110 ? -24.807 31.882  -28.391 1.00 31.66 ? 107 GLN   B CB  1 
ATOM   3595 C CG  . GLN   B 1 110 ? -24.227 30.958  -29.430 1.00 31.91 ? 107 GLN   B CG  1 
ATOM   3596 C CD  . GLN   B 1 110 ? -24.174 31.624  -30.790 1.00 48.64 ? 107 GLN   B CD  1 
ATOM   3597 O OE1 . GLN   B 1 110 ? -23.213 32.323  -31.117 1.00 50.56 ? 107 GLN   B OE1 1 
ATOM   3598 N NE2 . GLN   B 1 110 ? -25.226 31.429  -31.583 1.00 50.57 ? 107 GLN   B NE2 1 
ATOM   3599 N N   . THR   B 1 111 ? -26.859 32.379  -25.832 1.00 23.61 ? 108 THR   B N   1 
ATOM   3600 C CA  . THR   B 1 111 ? -27.364 33.377  -24.895 1.00 22.72 ? 108 THR   B CA  1 
ATOM   3601 C C   . THR   B 1 111 ? -27.798 32.775  -23.560 1.00 27.85 ? 108 THR   B C   1 
ATOM   3602 O O   . THR   B 1 111 ? -28.451 33.464  -22.772 1.00 22.28 ? 108 THR   B O   1 
ATOM   3603 C CB  . THR   B 1 111 ? -28.532 34.136  -25.516 1.00 22.41 ? 108 THR   B CB  1 
ATOM   3604 O OG1 . THR   B 1 111 ? -29.515 33.190  -25.978 1.00 23.31 ? 108 THR   B OG1 1 
ATOM   3605 C CG2 . THR   B 1 111 ? -28.039 35.053  -26.702 1.00 25.29 ? 108 THR   B CG2 1 
ATOM   3606 N N   . GLY   B 1 112 ? -27.431 31.520  -23.280 1.00 25.28 ? 109 GLY   B N   1 
ATOM   3607 C CA  . GLY   B 1 112 ? -27.951 30.838  -22.108 1.00 26.94 ? 109 GLY   B CA  1 
ATOM   3608 C C   . GLY   B 1 112 ? -27.307 31.279  -20.806 1.00 28.98 ? 109 GLY   B C   1 
ATOM   3609 O O   . GLY   B 1 112 ? -26.155 31.692  -20.759 1.00 29.95 ? 109 GLY   B O   1 
ATOM   3610 N N   . THR   B 1 113 ? -28.086 31.183  -19.726 1.00 24.95 ? 110 THR   B N   1 
ATOM   3611 C CA  . THR   B 1 113 ? -27.524 31.334  -18.389 1.00 24.72 ? 110 THR   B CA  1 
ATOM   3612 C C   . THR   B 1 113 ? -26.345 30.396  -18.197 1.00 30.97 ? 110 THR   B C   1 
ATOM   3613 O O   . THR   B 1 113 ? -25.318 30.770  -17.618 1.00 28.23 ? 110 THR   B O   1 
ATOM   3614 C CB  . THR   B 1 113 ? -28.599 31.049  -17.338 1.00 29.56 ? 110 THR   B CB  1 
ATOM   3615 O OG1 . THR   B 1 113 ? -29.643 32.011  -17.463 1.00 29.70 ? 110 THR   B OG1 1 
ATOM   3616 C CG2 . THR   B 1 113 ? -28.009 31.121  -15.904 1.00 28.46 ? 110 THR   B CG2 1 
ATOM   3617 N N   . PHE   B 1 114 ? -26.482 29.166  -18.680 1.00 27.29 ? 111 PHE   B N   1 
ATOM   3618 C CA  . PHE   B 1 114 ? -25.482 28.126  -18.678 1.00 29.10 ? 111 PHE   B CA  1 
ATOM   3619 C C   . PHE   B 1 114 ? -25.123 27.805  -20.122 1.00 29.80 ? 111 PHE   B C   1 
ATOM   3620 O O   . PHE   B 1 114 ? -26.003 27.839  -20.995 1.00 25.32 ? 111 PHE   B O   1 
ATOM   3621 C CB  . PHE   B 1 114 ? -26.012 26.855  -17.973 1.00 27.81 ? 111 PHE   B CB  1 
ATOM   3622 C CG  . PHE   B 1 114 ? -26.238 27.028  -16.481 1.00 35.80 ? 111 PHE   B CG  1 
ATOM   3623 C CD1 . PHE   B 1 114 ? -25.155 27.064  -15.597 1.00 34.85 ? 111 PHE   B CD1 1 
ATOM   3624 C CD2 . PHE   B 1 114 ? -27.525 27.144  -15.959 1.00 30.00 ? 111 PHE   B CD2 1 
ATOM   3625 C CE1 . PHE   B 1 114 ? -25.343 27.212  -14.215 1.00 34.82 ? 111 PHE   B CE1 1 
ATOM   3626 C CE2 . PHE   B 1 114 ? -27.726 27.298  -14.573 1.00 37.71 ? 111 PHE   B CE2 1 
ATOM   3627 C CZ  . PHE   B 1 114 ? -26.629 27.332  -13.698 1.00 36.50 ? 111 PHE   B CZ  1 
ATOM   3628 N N   . PRO   B 1 115 ? -23.846 27.506  -20.411 1.00 29.51 ? 112 PRO   B N   1 
ATOM   3629 C CA  . PRO   B 1 115 ? -23.413 27.216  -21.799 1.00 29.23 ? 112 PRO   B CA  1 
ATOM   3630 C C   . PRO   B 1 115 ? -23.801 25.816  -22.251 1.00 29.33 ? 112 PRO   B C   1 
ATOM   3631 O O   . PRO   B 1 115 ? -22.964 25.006  -22.655 1.00 27.87 ? 112 PRO   B O   1 
ATOM   3632 C CB  . PRO   B 1 115 ? -21.890 27.376  -21.696 1.00 27.21 ? 112 PRO   B CB  1 
ATOM   3633 C CG  . PRO   B 1 115 ? -21.584 26.901  -20.305 1.00 31.69 ? 112 PRO   B CG  1 
ATOM   3634 C CD  . PRO   B 1 115 ? -22.714 27.490  -19.467 1.00 29.78 ? 112 PRO   B CD  1 
ATOM   3635 N N   . MET   B 1 116 ? -25.089 25.504  -22.214 1.00 26.27 ? 113 MET   B N   1 
ATOM   3636 C CA  . MET   B 1 116 ? -25.471 24.172  -22.643 1.00 24.24 ? 113 MET   B CA  1 
ATOM   3637 C C   . MET   B 1 116 ? -25.367 24.059  -24.160 1.00 27.31 ? 113 MET   B C   1 
ATOM   3638 O O   . MET   B 1 116 ? -25.502 25.047  -24.894 1.00 26.39 ? 113 MET   B O   1 
ATOM   3639 C CB  . MET   B 1 116 ? -26.881 23.837  -22.158 1.00 30.83 ? 113 MET   B CB  1 
ATOM   3640 C CG  . MET   B 1 116 ? -28.002 24.424  -22.988 1.00 30.80 ? 113 MET   B CG  1 
ATOM   3641 S SD  . MET   B 1 116 ? -29.614 23.732  -22.536 1.00 31.56 ? 113 MET   B SD  1 
ATOM   3642 C CE  . MET   B 1 116 ? -30.604 25.213  -22.600 1.00 29.26 ? 113 MET   B CE  1 
ATOM   3643 N N   . VAL   B 1 117 ? -25.069 22.847  -24.628 1.00 28.16 ? 114 VAL   B N   1 
ATOM   3644 C CA  . VAL   B 1 117 ? -25.017 22.542  -26.055 1.00 26.13 ? 114 VAL   B CA  1 
ATOM   3645 C C   . VAL   B 1 117 ? -26.207 21.648  -26.390 1.00 28.05 ? 114 VAL   B C   1 
ATOM   3646 O O   . VAL   B 1 117 ? -26.366 20.569  -25.807 1.00 27.10 ? 114 VAL   B O   1 
ATOM   3647 C CB  . VAL   B 1 117 ? -23.690 21.874  -26.450 1.00 30.10 ? 114 VAL   B CB  1 
ATOM   3648 C CG1 . VAL   B 1 117 ? -23.685 21.537  -27.937 1.00 29.96 ? 114 VAL   B CG1 1 
ATOM   3649 C CG2 . VAL   B 1 117 ? -22.512 22.795  -26.130 1.00 26.74 ? 114 VAL   B CG2 1 
ATOM   3650 N N   . PHE   B 1 118 ? -27.053 22.096  -27.321 1.00 25.25 ? 115 PHE   B N   1 
ATOM   3651 C CA  . PHE   B 1 118 ? -28.141 21.240  -27.766 1.00 28.44 ? 115 PHE   B CA  1 
ATOM   3652 C C   . PHE   B 1 118 ? -27.568 20.075  -28.575 1.00 29.52 ? 115 PHE   B C   1 
ATOM   3653 O O   . PHE   B 1 118 ? -26.641 20.266  -29.369 1.00 30.42 ? 115 PHE   B O   1 
ATOM   3654 C CB  . PHE   B 1 118 ? -29.160 22.028  -28.591 1.00 26.33 ? 115 PHE   B CB  1 
ATOM   3655 C CG  . PHE   B 1 118 ? -29.830 23.149  -27.818 1.00 24.64 ? 115 PHE   B CG  1 
ATOM   3656 C CD1 . PHE   B 1 118 ? -30.602 22.873  -26.695 1.00 25.13 ? 115 PHE   B CD1 1 
ATOM   3657 C CD2 . PHE   B 1 118 ? -29.692 24.468  -28.229 1.00 24.26 ? 115 PHE   B CD2 1 
ATOM   3658 C CE1 . PHE   B 1 118 ? -31.219 23.890  -25.990 1.00 24.81 ? 115 PHE   B CE1 1 
ATOM   3659 C CE2 . PHE   B 1 118 ? -30.315 25.497  -27.529 1.00 22.04 ? 115 PHE   B CE2 1 
ATOM   3660 C CZ  . PHE   B 1 118 ? -31.073 25.218  -26.418 1.00 21.50 ? 115 PHE   B CZ  1 
ATOM   3661 N N   . PRO   B 1 119 ? -28.077 18.861  -28.383 1.00 29.96 ? 116 PRO   B N   1 
ATOM   3662 C CA  . PRO   B 1 119 ? -27.449 17.681  -29.000 1.00 30.74 ? 116 PRO   B CA  1 
ATOM   3663 C C   . PRO   B 1 119 ? -27.702 17.616  -30.498 1.00 31.31 ? 116 PRO   B C   1 
ATOM   3664 O O   . PRO   B 1 119 ? -28.552 18.313  -31.068 1.00 28.13 ? 116 PRO   B O   1 
ATOM   3665 C CB  . PRO   B 1 119 ? -28.109 16.505  -28.280 1.00 29.47 ? 116 PRO   B CB  1 
ATOM   3666 C CG  . PRO   B 1 119 ? -29.431 17.038  -27.847 1.00 30.45 ? 116 PRO   B CG  1 
ATOM   3667 C CD  . PRO   B 1 119 ? -29.178 18.490  -27.481 1.00 26.43 ? 116 PRO   B CD  1 
ATOM   3668 N N   . ALA   B 1 120 ? -26.930 16.750  -31.149 1.00 29.24 ? 117 ALA   B N   1 
ATOM   3669 C CA  . ALA   B 1 120 ? -27.202 16.452  -32.542 1.00 31.65 ? 117 ALA   B CA  1 
ATOM   3670 C C   . ALA   B 1 120 ? -28.581 15.817  -32.659 1.00 27.28 ? 117 ALA   B C   1 
ATOM   3671 O O   . ALA   B 1 120 ? -29.071 15.171  -31.725 1.00 28.20 ? 117 ALA   B O   1 
ATOM   3672 C CB  . ALA   B 1 120 ? -26.126 15.519  -33.119 1.00 29.60 ? 117 ALA   B CB  1 
ATOM   3673 N N   . TYR   B 1 121 ? -29.222 16.033  -33.806 1.00 29.22 ? 118 TYR   B N   1 
ATOM   3674 C CA  . TYR   B 1 121 ? -30.510 15.396  -34.066 1.00 28.20 ? 118 TYR   B CA  1 
ATOM   3675 C C   . TYR   B 1 121 ? -30.369 13.884  -33.987 1.00 32.49 ? 118 TYR   B C   1 
ATOM   3676 O O   . TYR   B 1 121 ? -29.338 13.312  -34.356 1.00 29.63 ? 118 TYR   B O   1 
ATOM   3677 C CB  . TYR   B 1 121 ? -31.050 15.787  -35.444 1.00 30.27 ? 118 TYR   B CB  1 
ATOM   3678 C CG  . TYR   B 1 121 ? -31.522 17.220  -35.551 1.00 31.01 ? 118 TYR   B CG  1 
ATOM   3679 C CD1 . TYR   B 1 121 ? -31.405 18.098  -34.476 1.00 30.04 ? 118 TYR   B CD1 1 
ATOM   3680 C CD2 . TYR   B 1 121 ? -32.080 17.700  -36.731 1.00 30.88 ? 118 TYR   B CD2 1 
ATOM   3681 C CE1 . TYR   B 1 121 ? -31.832 19.414  -34.571 1.00 29.08 ? 118 TYR   B CE1 1 
ATOM   3682 C CE2 . TYR   B 1 121 ? -32.513 19.011  -36.832 1.00 32.19 ? 118 TYR   B CE2 1 
ATOM   3683 C CZ  . TYR   B 1 121 ? -32.383 19.863  -35.748 1.00 35.27 ? 118 TYR   B CZ  1 
ATOM   3684 O OH  . TYR   B 1 121 ? -32.810 21.174  -35.844 1.00 40.09 ? 118 TYR   B OH  1 
ATOM   3685 N N   . ARG   B 1 122 ? -31.434 13.234  -33.520 1.00 28.04 ? 119 ARG   B N   1 
ATOM   3686 C CA  . ARG   B 1 122 ? -31.463 11.796  -33.279 1.00 31.45 ? 119 ARG   B CA  1 
ATOM   3687 C C   . ARG   B 1 122 ? -32.403 11.130  -34.280 1.00 32.88 ? 119 ARG   B C   1 
ATOM   3688 O O   . ARG   B 1 122 ? -33.588 11.477  -34.350 1.00 29.15 ? 119 ARG   B O   1 
ATOM   3689 C CB  . ARG   B 1 122 ? -31.922 11.510  -31.851 1.00 33.05 ? 119 ARG   B CB  1 
ATOM   3690 C CG  . ARG   B 1 122 ? -31.980 10.052  -31.490 1.00 35.47 ? 119 ARG   B CG  1 
ATOM   3691 C CD  . ARG   B 1 122 ? -32.136 9.911   -29.990 1.00 36.37 ? 119 ARG   B CD  1 
ATOM   3692 N NE  . ARG   B 1 122 ? -33.407 10.454  -29.523 1.00 33.39 ? 119 ARG   B NE  1 
ATOM   3693 C CZ  . ARG   B 1 122 ? -34.489 9.721   -29.302 1.00 30.20 ? 119 ARG   B CZ  1 
ATOM   3694 N NH1 . ARG   B 1 122 ? -34.495 8.414   -29.522 1.00 34.76 ? 119 ARG   B NH1 1 
ATOM   3695 N NH2 . ARG   B 1 122 ? -35.588 10.309  -28.837 1.00 30.24 ? 119 ARG   B NH2 1 
ATOM   3696 N N   . LYS   B 1 123 ? -31.889 10.171  -35.042 1.00 31.76 ? 120 LYS   B N   1 
ATOM   3697 C CA  . LYS   B 1 123 ? -32.756 9.478   -35.989 1.00 34.06 ? 120 LYS   B CA  1 
ATOM   3698 C C   . LYS   B 1 123 ? -33.686 8.532   -35.249 1.00 32.67 ? 120 LYS   B C   1 
ATOM   3699 O O   . LYS   B 1 123 ? -33.275 7.818   -34.332 1.00 33.80 ? 120 LYS   B O   1 
ATOM   3700 C CB  . LYS   B 1 123 ? -31.943 8.697   -37.025 1.00 36.60 ? 120 LYS   B CB  1 
ATOM   3701 C CG  . LYS   B 1 123 ? -32.809 8.080   -38.139 1.00 35.98 ? 120 LYS   B CG  1 
ATOM   3702 C CD  . LYS   B 1 123 ? -31.937 7.527   -39.251 1.00 43.12 ? 120 LYS   B CD  1 
ATOM   3703 C CE  . LYS   B 1 123 ? -32.744 7.075   -40.451 1.00 45.67 ? 120 LYS   B CE  1 
ATOM   3704 N NZ  . LYS   B 1 123 ? -33.655 5.956   -40.101 1.00 49.79 ? 120 LYS   B NZ  1 
ATOM   3705 N N   . LEU   B 1 124 ? -34.957 8.556   -35.634 1.00 32.56 ? 121 LEU   B N   1 
ATOM   3706 C CA  . LEU   B 1 124 ? -35.962 7.652   -35.107 1.00 33.61 ? 121 LEU   B CA  1 
ATOM   3707 C C   . LEU   B 1 124 ? -36.242 6.570   -36.143 1.00 39.04 ? 121 LEU   B C   1 
ATOM   3708 O O   . LEU   B 1 124 ? -36.141 6.799   -37.348 1.00 40.97 ? 121 LEU   B O   1 
ATOM   3709 C CB  . LEU   B 1 124 ? -37.255 8.402   -34.771 1.00 29.87 ? 121 LEU   B CB  1 
ATOM   3710 C CG  . LEU   B 1 124 ? -37.149 9.680   -33.925 1.00 30.51 ? 121 LEU   B CG  1 
ATOM   3711 C CD1 . LEU   B 1 124 ? -38.489 10.388  -33.870 1.00 30.05 ? 121 LEU   B CD1 1 
ATOM   3712 C CD2 . LEU   B 1 124 ? -36.644 9.381   -32.520 1.00 28.57 ? 121 LEU   B CD2 1 
ATOM   3713 N N   . ASP   B 1 125 ? -36.578 5.379   -35.672 1.00 46.41 ? 122 ASP   B N   1 
ATOM   3714 C CA  . ASP   B 1 125 ? -36.925 4.283   -36.566 1.00 49.40 ? 122 ASP   B CA  1 
ATOM   3715 C C   . ASP   B 1 125 ? -38.354 3.866   -36.271 1.00 46.31 ? 122 ASP   B C   1 
ATOM   3716 O O   . ASP   B 1 125 ? -38.668 3.471   -35.142 1.00 47.38 ? 122 ASP   B O   1 
ATOM   3717 C CB  . ASP   B 1 125 ? -35.967 3.106   -36.412 1.00 58.48 ? 122 ASP   B CB  1 
ATOM   3718 C CG  . ASP   B 1 125 ? -36.383 1.908   -37.248 1.00 64.60 ? 122 ASP   B CG  1 
ATOM   3719 O OD1 . ASP   B 1 125 ? -36.237 1.959   -38.493 1.00 68.41 ? 122 ASP   B OD1 1 
ATOM   3720 O OD2 . ASP   B 1 125 ? -36.867 0.922   -36.651 1.00 64.12 ? 122 ASP   B OD2 1 
ATOM   3721 N N   . LEU   B 1 126 ? -39.220 3.980   -37.281 1.00 48.94 ? 123 LEU   B N   1 
ATOM   3722 C CA  . LEU   B 1 126 ? -40.635 3.699   -37.070 1.00 54.00 ? 123 LEU   B CA  1 
ATOM   3723 C C   . LEU   B 1 126 ? -40.848 2.310   -36.492 1.00 53.96 ? 123 LEU   B C   1 
ATOM   3724 O O   . LEU   B 1 126 ? -41.831 2.077   -35.780 1.00 55.03 ? 123 LEU   B O   1 
ATOM   3725 C CB  . LEU   B 1 126 ? -41.410 3.859   -38.374 1.00 49.26 ? 123 LEU   B CB  1 
ATOM   3726 C CG  . LEU   B 1 126 ? -41.957 5.253   -38.662 1.00 45.68 ? 123 LEU   B CG  1 
ATOM   3727 C CD1 . LEU   B 1 126 ? -42.528 5.306   -40.070 1.00 53.31 ? 123 LEU   B CD1 1 
ATOM   3728 C CD2 . LEU   B 1 126 ? -43.020 5.630   -37.642 1.00 43.90 ? 123 LEU   B CD2 1 
ATOM   3729 N N   . ARG   B 1 127 ? -39.926 1.386   -36.756 1.00 54.40 ? 124 ARG   B N   1 
ATOM   3730 C CA  . ARG   B 1 127 ? -40.129 0.004   -36.352 1.00 57.17 ? 124 ARG   B CA  1 
ATOM   3731 C C   . ARG   B 1 127 ? -40.124 -0.193  -34.841 1.00 59.37 ? 124 ARG   B C   1 
ATOM   3732 O O   . ARG   B 1 127 ? -40.446 -1.296  -34.388 1.00 62.93 ? 124 ARG   B O   1 
ATOM   3733 C CB  . ARG   B 1 127 ? -39.071 -0.884  -36.998 1.00 61.19 ? 124 ARG   B CB  1 
ATOM   3734 C CG  . ARG   B 1 127 ? -38.944 -0.690  -38.502 1.00 64.42 ? 124 ARG   B CG  1 
ATOM   3735 C CD  . ARG   B 1 127 ? -37.658 -1.332  -38.994 1.00 70.26 ? 124 ARG   B CD  1 
ATOM   3736 N NE  . ARG   B 1 127 ? -36.675 -1.412  -37.917 1.00 68.79 ? 124 ARG   B NE  1 
ATOM   3737 C CZ  . ARG   B 1 127 ? -35.397 -1.725  -38.083 1.00 74.11 ? 124 ARG   B CZ  1 
ATOM   3738 N NH1 . ARG   B 1 127 ? -34.902 -1.996  -39.282 1.00 71.48 ? 124 ARG   B NH1 1 
ATOM   3739 N NH2 . ARG   B 1 127 ? -34.594 -1.761  -37.021 1.00 73.18 ? 124 ARG   B NH2 1 
ATOM   3740 N N   . HIS   B 1 128 ? -39.773 0.822   -34.051 1.00 54.70 ? 125 HIS   B N   1 
ATOM   3741 C CA  . HIS   B 1 128 ? -39.856 0.706   -32.601 1.00 50.04 ? 125 HIS   B CA  1 
ATOM   3742 C C   . HIS   B 1 128 ? -41.183 1.200   -32.051 1.00 50.81 ? 125 HIS   B C   1 
ATOM   3743 O O   . HIS   B 1 128 ? -41.399 1.132   -30.835 1.00 53.06 ? 125 HIS   B O   1 
ATOM   3744 C CB  . HIS   B 1 128 ? -38.710 1.472   -31.923 1.00 52.40 ? 125 HIS   B CB  1 
ATOM   3745 C CG  . HIS   B 1 128 ? -37.421 1.430   -32.683 1.00 56.13 ? 125 HIS   B CG  1 
ATOM   3746 N ND1 . HIS   B 1 128 ? -36.723 0.262   -32.907 1.00 62.91 ? 125 HIS   B ND1 1 
ATOM   3747 C CD2 . HIS   B 1 128 ? -36.708 2.413   -33.280 1.00 56.27 ? 125 HIS   B CD2 1 
ATOM   3748 C CE1 . HIS   B 1 128 ? -35.637 0.527   -33.612 1.00 61.06 ? 125 HIS   B CE1 1 
ATOM   3749 N NE2 . HIS   B 1 128 ? -35.603 1.825   -33.849 1.00 62.49 ? 125 HIS   B NE2 1 
ATOM   3750 N N   . TYR   B 1 129 ? -42.079 1.684   -32.908 1.00 46.06 ? 126 TYR   B N   1 
ATOM   3751 C CA  . TYR   B 1 129 ? -43.288 2.362   -32.465 1.00 49.12 ? 126 TYR   B CA  1 
ATOM   3752 C C   . TYR   B 1 129 ? -44.527 1.629   -32.955 1.00 50.07 ? 126 TYR   B C   1 
ATOM   3753 O O   . TYR   B 1 129 ? -44.595 1.200   -34.111 1.00 53.49 ? 126 TYR   B O   1 
ATOM   3754 C CB  . TYR   B 1 129 ? -43.297 3.819   -32.950 1.00 42.62 ? 126 TYR   B CB  1 
ATOM   3755 C CG  . TYR   B 1 129 ? -42.053 4.545   -32.511 1.00 43.29 ? 126 TYR   B CG  1 
ATOM   3756 C CD1 . TYR   B 1 129 ? -41.912 4.979   -31.194 1.00 40.52 ? 126 TYR   B CD1 1 
ATOM   3757 C CD2 . TYR   B 1 129 ? -40.998 4.749   -33.390 1.00 43.19 ? 126 TYR   B CD2 1 
ATOM   3758 C CE1 . TYR   B 1 129 ? -40.760 5.624   -30.776 1.00 41.39 ? 126 TYR   B CE1 1 
ATOM   3759 C CE2 . TYR   B 1 129 ? -39.844 5.396   -32.984 1.00 42.03 ? 126 TYR   B CE2 1 
ATOM   3760 C CZ  . TYR   B 1 129 ? -39.733 5.833   -31.678 1.00 41.45 ? 126 TYR   B CZ  1 
ATOM   3761 O OH  . TYR   B 1 129 ? -38.592 6.469   -31.265 1.00 38.23 ? 126 TYR   B OH  1 
ATOM   3762 N N   . ASP   B 1 130 ? -45.492 1.492   -32.051 1.00 47.78 ? 127 ASP   B N   1 
ATOM   3763 C CA  . ASP   B 1 130 ? -46.804 0.915   -32.322 1.00 55.00 ? 127 ASP   B CA  1 
ATOM   3764 C C   . ASP   B 1 130 ? -47.835 1.769   -31.596 1.00 53.23 ? 127 ASP   B C   1 
ATOM   3765 O O   . ASP   B 1 130 ? -47.508 2.793   -30.994 1.00 45.18 ? 127 ASP   B O   1 
ATOM   3766 C CB  . ASP   B 1 130 ? -46.873 -0.560  -31.883 1.00 51.69 ? 127 ASP   B CB  1 
ATOM   3767 C CG  . ASP   B 1 130 ? -46.050 -0.838  -30.631 1.00 58.93 ? 127 ASP   B CG  1 
ATOM   3768 O OD1 . ASP   B 1 130 ? -46.172 -0.073  -29.647 1.00 60.88 ? 127 ASP   B OD1 1 
ATOM   3769 O OD2 . ASP   B 1 130 ? -45.258 -1.807  -30.632 1.00 65.29 ? 127 ASP   B OD2 1 
ATOM   3770 N N   . ASP   B 1 131 ? -49.094 1.336   -31.634 1.00 55.62 ? 128 ASP   B N   1 
ATOM   3771 C CA  . ASP   B 1 131 ? -50.142 2.080   -30.938 1.00 52.93 ? 128 ASP   B CA  1 
ATOM   3772 C C   . ASP   B 1 131 ? -49.912 2.111   -29.430 1.00 51.68 ? 128 ASP   B C   1 
ATOM   3773 O O   . ASP   B 1 131 ? -50.392 3.021   -28.748 1.00 47.84 ? 128 ASP   B O   1 
ATOM   3774 C CB  . ASP   B 1 131 ? -51.509 1.477   -31.252 1.00 60.42 ? 128 ASP   B CB  1 
ATOM   3775 C CG  . ASP   B 1 131 ? -51.807 1.455   -32.740 1.00 67.28 ? 128 ASP   B CG  1 
ATOM   3776 O OD1 . ASP   B 1 131 ? -51.544 2.476   -33.415 1.00 67.93 ? 128 ASP   B OD1 1 
ATOM   3777 O OD2 . ASP   B 1 131 ? -52.295 0.416   -33.238 1.00 70.54 ? 128 ASP   B OD2 1 
ATOM   3778 N N   . ALA   B 1 132 ? -49.199 1.118   -28.887 1.00 53.81 ? 129 ALA   B N   1 
ATOM   3779 C CA  . ALA   B 1 132 ? -48.893 1.110   -27.460 1.00 48.91 ? 129 ALA   B CA  1 
ATOM   3780 C C   . ALA   B 1 132 ? -47.760 2.065   -27.125 1.00 50.66 ? 129 ALA   B C   1 
ATOM   3781 O O   . ALA   B 1 132 ? -47.726 2.634   -26.027 1.00 51.45 ? 129 ALA   B O   1 
ATOM   3782 C CB  . ALA   B 1 132 ? -48.520 -0.304  -27.007 1.00 52.76 ? 129 ALA   B CB  1 
ATOM   3783 N N   . LEU   B 1 133 ? -46.831 2.245   -28.052 1.00 42.99 ? 130 LEU   B N   1 
ATOM   3784 C CA  . LEU   B 1 133 ? -45.675 3.114   -27.868 1.00 42.85 ? 130 LEU   B CA  1 
ATOM   3785 C C   . LEU   B 1 133 ? -45.563 3.960   -29.127 1.00 33.60 ? 130 LEU   B C   1 
ATOM   3786 O O   . LEU   B 1 133 ? -44.712 3.703   -29.983 1.00 35.98 ? 130 LEU   B O   1 
ATOM   3787 C CB  . LEU   B 1 133 ? -44.413 2.294   -27.615 1.00 40.59 ? 130 LEU   B CB  1 
ATOM   3788 C CG  . LEU   B 1 133 ? -43.381 2.981   -26.733 1.00 41.87 ? 130 LEU   B CG  1 
ATOM   3789 C CD1 . LEU   B 1 133 ? -44.034 3.368   -25.419 1.00 36.48 ? 130 LEU   B CD1 1 
ATOM   3790 C CD2 . LEU   B 1 133 ? -42.200 2.060   -26.497 1.00 48.09 ? 130 LEU   B CD2 1 
ATOM   3791 N N   . PRO   B 1 134 ? -46.429 4.956   -29.286 1.00 32.12 ? 131 PRO   B N   1 
ATOM   3792 C CA  . PRO   B 1 134 ? -46.496 5.685   -30.560 1.00 35.89 ? 131 PRO   B CA  1 
ATOM   3793 C C   . PRO   B 1 134 ? -45.279 6.576   -30.763 1.00 37.51 ? 131 PRO   B C   1 
ATOM   3794 O O   . PRO   B 1 134 ? -44.498 6.845   -29.846 1.00 32.79 ? 131 PRO   B O   1 
ATOM   3795 C CB  . PRO   B 1 134 ? -47.786 6.500   -30.442 1.00 37.04 ? 131 PRO   B CB  1 
ATOM   3796 C CG  . PRO   B 1 134 ? -48.029 6.632   -28.973 1.00 38.28 ? 131 PRO   B CG  1 
ATOM   3797 C CD  . PRO   B 1 134 ? -47.461 5.389   -28.332 1.00 32.50 ? 131 PRO   B CD  1 
ATOM   3798 N N   . LEU   B 1 135 ? -45.128 7.029   -32.013 1.00 35.42 ? 132 LEU   B N   1 
ATOM   3799 C CA  . LEU   B 1 135 ? -44.002 7.882   -32.382 1.00 34.33 ? 132 LEU   B CA  1 
ATOM   3800 C C   . LEU   B 1 135 ? -43.845 9.060   -31.424 1.00 32.31 ? 132 LEU   B C   1 
ATOM   3801 O O   . LEU   B 1 135 ? -42.721 9.453   -31.084 1.00 29.38 ? 132 LEU   B O   1 
ATOM   3802 C CB  . LEU   B 1 135 ? -44.183 8.382   -33.816 1.00 35.68 ? 132 LEU   B CB  1 
ATOM   3803 C CG  . LEU   B 1 135 ? -43.230 9.450   -34.354 1.00 28.75 ? 132 LEU   B CG  1 
ATOM   3804 C CD1 . LEU   B 1 135 ? -41.813 8.912   -34.489 1.00 29.74 ? 132 LEU   B CD1 1 
ATOM   3805 C CD2 . LEU   B 1 135 ? -43.739 9.951   -35.706 1.00 29.51 ? 132 LEU   B CD2 1 
ATOM   3806 N N   . SER   B 1 136 ? -44.963 9.634   -30.975 1.00 27.89 ? 133 SER   B N   1 
ATOM   3807 C CA  . SER   B 1 136 ? -44.919 10.775  -30.073 1.00 27.20 ? 133 SER   B CA  1 
ATOM   3808 C C   . SER   B 1 136 ? -44.129 10.495  -28.798 1.00 33.91 ? 133 SER   B C   1 
ATOM   3809 O O   . SER   B 1 136 ? -43.705 11.449  -28.129 1.00 31.19 ? 133 SER   B O   1 
ATOM   3810 C CB  . SER   B 1 136 ? -46.340 11.202  -29.716 1.00 27.39 ? 133 SER   B CB  1 
ATOM   3811 O OG  . SER   B 1 136 ? -47.063 10.138  -29.140 1.00 30.97 ? 133 SER   B OG  1 
ATOM   3812 N N   . THR   B 1 137 ? -43.950 9.221   -28.427 1.00 32.06 ? 134 THR   B N   1 
ATOM   3813 C CA  . THR   B 1 137 ? -43.176 8.895   -27.236 1.00 30.59 ? 134 THR   B CA  1 
ATOM   3814 C C   . THR   B 1 137 ? -41.711 9.290   -27.376 1.00 28.41 ? 134 THR   B C   1 
ATOM   3815 O O   . THR   B 1 137 ? -40.996 9.310   -26.362 1.00 27.48 ? 134 THR   B O   1 
ATOM   3816 C CB  . THR   B 1 137 ? -43.258 7.387   -26.903 1.00 28.25 ? 134 THR   B CB  1 
ATOM   3817 O OG1 . THR   B 1 137 ? -42.658 6.622   -27.953 1.00 31.71 ? 134 THR   B OG1 1 
ATOM   3818 C CG2 . THR   B 1 137 ? -44.695 6.929   -26.693 1.00 28.17 ? 134 THR   B CG2 1 
ATOM   3819 N N   . ALA   B 1 138 ? -41.245 9.605   -28.593 1.00 25.34 ? 135 ALA   B N   1 
ATOM   3820 C CA  . ALA   B 1 138 ? -39.890 10.128  -28.748 1.00 28.09 ? 135 ALA   B CA  1 
ATOM   3821 C C   . ALA   B 1 138 ? -39.708 11.503  -28.098 1.00 26.92 ? 135 ALA   B C   1 
ATOM   3822 O O   . ALA   B 1 138 ? -38.566 11.972  -27.996 1.00 26.71 ? 135 ALA   B O   1 
ATOM   3823 C CB  . ALA   B 1 138 ? -39.498 10.182  -30.227 1.00 26.44 ? 135 ALA   B CB  1 
ATOM   3824 N N   . LEU   B 1 139 ? -40.788 12.142  -27.638 1.00 24.15 ? 136 LEU   B N   1 
ATOM   3825 C CA  . LEU   B 1 139 ? -40.727 13.371  -26.851 1.00 24.87 ? 136 LEU   B CA  1 
ATOM   3826 C C   . LEU   B 1 139 ? -41.131 13.153  -25.404 1.00 26.26 ? 136 LEU   B C   1 
ATOM   3827 O O   . LEU   B 1 139 ? -41.125 14.109  -24.616 1.00 27.27 ? 136 LEU   B O   1 
ATOM   3828 C CB  . LEU   B 1 139 ? -41.625 14.459  -27.466 1.00 24.91 ? 136 LEU   B CB  1 
ATOM   3829 C CG  . LEU   B 1 139 ? -41.174 15.001  -28.824 1.00 27.27 ? 136 LEU   B CG  1 
ATOM   3830 C CD1 . LEU   B 1 139 ? -42.195 16.016  -29.381 1.00 25.40 ? 136 LEU   B CD1 1 
ATOM   3831 C CD2 . LEU   B 1 139 ? -39.788 15.623  -28.721 1.00 25.58 ? 136 LEU   B CD2 1 
ATOM   3832 N N   . GLY   B 1 140 ? -41.481 11.925  -25.032 1.00 29.03 ? 137 GLY   B N   1 
ATOM   3833 C CA  . GLY   B 1 140 ? -41.851 11.614  -23.667 1.00 27.21 ? 137 GLY   B CA  1 
ATOM   3834 C C   . GLY   B 1 140 ? -41.095 10.414  -23.118 1.00 31.02 ? 137 GLY   B C   1 
ATOM   3835 O O   . GLY   B 1 140 ? -39.874 10.482  -22.949 1.00 25.76 ? 137 GLY   B O   1 
ATOM   3836 N N   . VAL   B 1 141 ? -41.797 9.296   -22.870 1.00 28.93 ? 138 VAL   B N   1 
ATOM   3837 C CA  . VAL   B 1 141 ? -41.168 8.186   -22.158 1.00 29.07 ? 138 VAL   B CA  1 
ATOM   3838 C C   . VAL   B 1 141 ? -40.004 7.605   -22.951 1.00 30.71 ? 138 VAL   B C   1 
ATOM   3839 O O   . VAL   B 1 141 ? -39.040 7.092   -22.364 1.00 30.44 ? 138 VAL   B O   1 
ATOM   3840 C CB  . VAL   B 1 141 ? -42.209 7.107   -21.794 1.00 32.28 ? 138 VAL   B CB  1 
ATOM   3841 C CG1 . VAL   B 1 141 ? -42.789 6.467   -23.043 1.00 27.82 ? 138 VAL   B CG1 1 
ATOM   3842 C CG2 . VAL   B 1 141 ? -41.571 6.052   -20.901 1.00 32.20 ? 138 VAL   B CG2 1 
ATOM   3843 N N   . MET   B 1 142 ? -40.048 7.683   -24.284 1.00 25.38 ? 139 MET   B N   1 
ATOM   3844 C CA  . MET   B 1 142 ? -38.917 7.295   -25.119 1.00 25.63 ? 139 MET   B CA  1 
ATOM   3845 C C   . MET   B 1 142 ? -38.112 8.508   -25.575 1.00 27.14 ? 139 MET   B C   1 
ATOM   3846 O O   . MET   B 1 142 ? -37.470 8.462   -26.623 1.00 27.37 ? 139 MET   B O   1 
ATOM   3847 C CB  . MET   B 1 142 ? -39.377 6.497   -26.340 1.00 28.88 ? 139 MET   B CB  1 
ATOM   3848 C CG  . MET   B 1 142 ? -40.164 5.229   -26.028 1.00 35.34 ? 139 MET   B CG  1 
ATOM   3849 S SD  . MET   B 1 142 ? -39.114 3.878   -25.403 1.00 38.73 ? 139 MET   B SD  1 
ATOM   3850 C CE  . MET   B 1 142 ? -39.638 3.864   -23.697 1.00 35.60 ? 139 MET   B CE  1 
ATOM   3851 N N   . GLY   B 1 143 ? -38.173 9.605   -24.829 1.00 29.36 ? 140 GLY   B N   1 
ATOM   3852 C CA  . GLY   B 1 143 ? -37.416 10.787  -25.182 1.00 26.95 ? 140 GLY   B CA  1 
ATOM   3853 C C   . GLY   B 1 143 ? -36.786 11.408  -23.952 1.00 29.02 ? 140 GLY   B C   1 
ATOM   3854 O O   . GLY   B 1 143 ? -36.515 10.717  -22.956 1.00 28.01 ? 140 GLY   B O   1 
ATOM   3855 N N   . GLY   B 1 144 ? -36.566 12.715  -24.000 1.00 25.59 ? 141 GLY   B N   1 
ATOM   3856 C CA  . GLY   B 1 144 ? -35.950 13.425  -22.906 1.00 24.16 ? 141 GLY   B CA  1 
ATOM   3857 C C   . GLY   B 1 144 ? -36.530 13.090  -21.553 1.00 27.75 ? 141 GLY   B C   1 
ATOM   3858 O O   . GLY   B 1 144 ? -35.803 12.744  -20.618 1.00 27.75 ? 141 GLY   B O   1 
ATOM   3859 N N   . PRO   B 1 145 ? -37.850 13.226  -21.398 1.00 26.70 ? 142 PRO   B N   1 
ATOM   3860 C CA  . PRO   B 1 145 ? -38.423 13.001  -20.062 1.00 25.21 ? 142 PRO   B CA  1 
ATOM   3861 C C   . PRO   B 1 145 ? -38.213 11.576  -19.574 1.00 28.61 ? 142 PRO   B C   1 
ATOM   3862 O O   . PRO   B 1 145 ? -37.881 11.380  -18.399 1.00 26.90 ? 142 PRO   B O   1 
ATOM   3863 C CB  . PRO   B 1 145 ? -39.903 13.361  -20.249 1.00 27.87 ? 142 PRO   B CB  1 
ATOM   3864 C CG  . PRO   B 1 145 ? -39.884 14.372  -21.427 1.00 25.98 ? 142 PRO   B CG  1 
ATOM   3865 C CD  . PRO   B 1 145 ? -38.841 13.779  -22.340 1.00 27.37 ? 142 PRO   B CD  1 
ATOM   3866 N N   . GLY   B 1 146 ? -38.346 10.580  -20.454 1.00 27.40 ? 143 GLY   B N   1 
ATOM   3867 C CA  . GLY   B 1 146 ? -38.032 9.215   -20.057 1.00 29.11 ? 143 GLY   B CA  1 
ATOM   3868 C C   . GLY   B 1 146 ? -36.572 9.032   -19.680 1.00 28.59 ? 143 GLY   B C   1 
ATOM   3869 O O   . GLY   B 1 146 ? -36.255 8.394   -18.669 1.00 26.96 ? 143 GLY   B O   1 
ATOM   3870 N N   . MET   B 1 147 ? -35.661 9.584   -20.489 1.00 25.90 ? 144 MET   B N   1 
ATOM   3871 C CA  . MET   B 1 147 ? -34.231 9.505   -20.178 1.00 25.26 ? 144 MET   B CA  1 
ATOM   3872 C C   . MET   B 1 147 ? -33.913 10.161  -18.831 1.00 27.64 ? 144 MET   B C   1 
ATOM   3873 O O   . MET   B 1 147 ? -33.042 9.688   -18.088 1.00 25.71 ? 144 MET   B O   1 
ATOM   3874 C CB  . MET   B 1 147 ? -33.422 10.153  -21.303 1.00 26.67 ? 144 MET   B CB  1 
ATOM   3875 C CG  . MET   B 1 147 ? -31.905 10.016  -21.139 1.00 28.09 ? 144 MET   B CG  1 
ATOM   3876 S SD  . MET   B 1 147 ? -31.385 8.283   -21.125 1.00 30.66 ? 144 MET   B SD  1 
ATOM   3877 C CE  . MET   B 1 147 ? -31.374 7.831   -22.836 1.00 28.40 ? 144 MET   B CE  1 
ATOM   3878 N N   . THR   B 1 148 ? -34.618 11.248  -18.492 1.00 25.99 ? 145 THR   B N   1 
ATOM   3879 C CA  . THR   B 1 148 ? -34.383 11.919  -17.216 1.00 25.85 ? 145 THR   B CA  1 
ATOM   3880 C C   . THR   B 1 148 ? -34.751 11.006  -16.044 1.00 28.94 ? 145 THR   B C   1 
ATOM   3881 O O   . THR   B 1 148 ? -33.967 10.836  -15.101 1.00 24.11 ? 145 THR   B O   1 
ATOM   3882 C CB  . THR   B 1 148 ? -35.180 13.228  -17.155 1.00 24.03 ? 145 THR   B CB  1 
ATOM   3883 O OG1 . THR   B 1 148 ? -34.856 14.042  -18.292 1.00 25.25 ? 145 THR   B OG1 1 
ATOM   3884 C CG2 . THR   B 1 148 ? -34.858 14.004  -15.881 1.00 23.66 ? 145 THR   B CG2 1 
ATOM   3885 N N   . ALA   B 1 149 ? -35.949 10.419  -16.085 1.00 23.84 ? 146 ALA   B N   1 
ATOM   3886 C CA  . ALA   B 1 149 ? -36.396 9.542   -15.003 1.00 26.39 ? 146 ALA   B CA  1 
ATOM   3887 C C   . ALA   B 1 149 ? -35.547 8.279   -14.932 1.00 25.35 ? 146 ALA   B C   1 
ATOM   3888 O O   . ALA   B 1 149 ? -35.055 7.911   -13.861 1.00 29.26 ? 146 ALA   B O   1 
ATOM   3889 C CB  . ALA   B 1 149 ? -37.875 9.183   -15.192 1.00 28.62 ? 146 ALA   B CB  1 
ATOM   3890 N N   . TRP   B 1 150 ? -35.346 7.619   -16.072 1.00 26.81 ? 147 TRP   B N   1 
ATOM   3891 C CA  . TRP   B 1 150 ? -34.657 6.333   -16.095 1.00 29.58 ? 147 TRP   B CA  1 
ATOM   3892 C C   . TRP   B 1 150 ? -33.171 6.488   -15.789 1.00 30.32 ? 147 TRP   B C   1 
ATOM   3893 O O   . TRP   B 1 150 ? -32.599 5.692   -15.031 1.00 28.88 ? 147 TRP   B O   1 
ATOM   3894 C CB  . TRP   B 1 150 ? -34.866 5.674   -17.461 1.00 30.75 ? 147 TRP   B CB  1 
ATOM   3895 C CG  . TRP   B 1 150 ? -34.012 4.478   -17.711 1.00 30.75 ? 147 TRP   B CG  1 
ATOM   3896 C CD1 . TRP   B 1 150 ? -34.292 3.186   -17.357 1.00 33.85 ? 147 TRP   B CD1 1 
ATOM   3897 C CD2 . TRP   B 1 150 ? -32.741 4.443   -18.384 1.00 31.93 ? 147 TRP   B CD2 1 
ATOM   3898 N NE1 . TRP   B 1 150 ? -33.275 2.356   -17.763 1.00 33.64 ? 147 TRP   B NE1 1 
ATOM   3899 C CE2 . TRP   B 1 150 ? -32.309 3.098   -18.390 1.00 31.58 ? 147 TRP   B CE2 1 
ATOM   3900 C CE3 . TRP   B 1 150 ? -31.925 5.417   -18.978 1.00 29.24 ? 147 TRP   B CE3 1 
ATOM   3901 C CZ2 . TRP   B 1 150 ? -31.095 2.701   -18.965 1.00 34.36 ? 147 TRP   B CZ2 1 
ATOM   3902 C CZ3 . TRP   B 1 150 ? -30.720 5.023   -19.543 1.00 31.38 ? 147 TRP   B CZ3 1 
ATOM   3903 C CH2 . TRP   B 1 150 ? -30.316 3.674   -19.534 1.00 35.28 ? 147 TRP   B CH2 1 
ATOM   3904 N N   . GLY   B 1 151 ? -32.526 7.495   -16.379 1.00 26.40 ? 148 GLY   B N   1 
ATOM   3905 C CA  . GLY   B 1 151 ? -31.134 7.761   -16.043 1.00 25.25 ? 148 GLY   B CA  1 
ATOM   3906 C C   . GLY   B 1 151 ? -30.935 8.016   -14.559 1.00 28.81 ? 148 GLY   B C   1 
ATOM   3907 O O   . GLY   B 1 151 ? -30.015 7.473   -13.940 1.00 28.90 ? 148 GLY   B O   1 
ATOM   3908 N N   . THR   B 1 152 ? -31.805 8.841   -13.960 1.00 23.71 ? 149 THR   B N   1 
ATOM   3909 C CA  . THR   B 1 152 ? -31.679 9.116   -12.531 1.00 24.89 ? 149 THR   B CA  1 
ATOM   3910 C C   . THR   B 1 152 ? -31.825 7.840   -11.711 1.00 29.26 ? 149 THR   B C   1 
ATOM   3911 O O   . THR   B 1 152 ? -31.077 7.625   -10.748 1.00 26.38 ? 149 THR   B O   1 
ATOM   3912 C CB  . THR   B 1 152 ? -32.717 10.152  -12.084 1.00 22.69 ? 149 THR   B CB  1 
ATOM   3913 O OG1 . THR   B 1 152 ? -32.547 11.365  -12.831 1.00 27.89 ? 149 THR   B OG1 1 
ATOM   3914 C CG2 . THR   B 1 152 ? -32.572 10.477  -10.596 1.00 21.92 ? 149 THR   B CG2 1 
ATOM   3915 N N   . MET   B 1 153 ? -32.791 6.984   -12.074 1.00 26.33 ? 150 MET   B N   1 
ATOM   3916 C CA  . MET   B 1 153 ? -33.123 5.820   -11.256 1.00 26.09 ? 150 MET   B CA  1 
ATOM   3917 C C   . MET   B 1 153 ? -32.177 4.649   -11.483 1.00 27.28 ? 150 MET   B C   1 
ATOM   3918 O O   . MET   B 1 153 ? -32.124 3.748   -10.643 1.00 31.86 ? 150 MET   B O   1 
ATOM   3919 C CB  . MET   B 1 153 ? -34.561 5.355   -11.528 1.00 27.91 ? 150 MET   B CB  1 
ATOM   3920 C CG  . MET   B 1 153 ? -35.633 6.358   -11.144 1.00 28.68 ? 150 MET   B CG  1 
ATOM   3921 S SD  . MET   B 1 153 ? -35.320 7.164   -9.556  1.00 33.54 ? 150 MET   B SD  1 
ATOM   3922 C CE  . MET   B 1 153 ? -35.815 5.897   -8.420  1.00 31.24 ? 150 MET   B CE  1 
ATOM   3923 N N   . THR   B 1 154 ? -31.423 4.636   -12.578 1.00 23.71 ? 151 THR   B N   1 
ATOM   3924 C CA  . THR   B 1 154 ? -30.463 3.569   -12.824 1.00 30.38 ? 151 THR   B CA  1 
ATOM   3925 C C   . THR   B 1 154 ? -29.010 4.018   -12.766 1.00 31.47 ? 151 THR   B C   1 
ATOM   3926 O O   . THR   B 1 154 ? -28.122 3.157   -12.744 1.00 33.86 ? 151 THR   B O   1 
ATOM   3927 C CB  . THR   B 1 154 ? -30.700 2.913   -14.189 1.00 29.53 ? 151 THR   B CB  1 
ATOM   3928 O OG1 . THR   B 1 154 ? -30.391 3.844   -15.237 1.00 31.83 ? 151 THR   B OG1 1 
ATOM   3929 C CG2 . THR   B 1 154 ? -32.138 2.437   -14.324 1.00 32.50 ? 151 THR   B CG2 1 
ATOM   3930 N N   . LYS   B 1 155 ? -28.731 5.326   -12.764 1.00 31.20 ? 152 LYS   B N   1 
ATOM   3931 C CA  . LYS   B 1 155 ? -27.349 5.805   -12.745 1.00 28.65 ? 152 LYS   B CA  1 
ATOM   3932 C C   . LYS   B 1 155 ? -26.981 6.559   -11.475 1.00 31.65 ? 152 LYS   B C   1 
ATOM   3933 O O   . LYS   B 1 155 ? -25.792 6.836   -11.258 1.00 30.99 ? 152 LYS   B O   1 
ATOM   3934 C CB  . LYS   B 1 155 ? -27.079 6.705   -13.962 1.00 30.24 ? 152 LYS   B CB  1 
ATOM   3935 C CG  . LYS   B 1 155 ? -27.365 6.046   -15.298 1.00 31.07 ? 152 LYS   B CG  1 
ATOM   3936 C CD  . LYS   B 1 155 ? -26.991 6.966   -16.460 1.00 32.97 ? 152 LYS   B CD  1 
ATOM   3937 C CE  . LYS   B 1 155 ? -27.475 6.389   -17.791 1.00 29.99 ? 152 LYS   B CE  1 
ATOM   3938 N NZ  . LYS   B 1 155 ? -26.855 5.071   -18.133 1.00 33.54 ? 152 LYS   B NZ  1 
ATOM   3939 N N   . PHE   B 1 156 ? -27.956 6.916   -10.645 1.00 27.30 ? 153 PHE   B N   1 
ATOM   3940 C CA  . PHE   B 1 156 ? -27.675 7.646   -9.412  1.00 30.17 ? 153 PHE   B CA  1 
ATOM   3941 C C   . PHE   B 1 156 ? -28.402 7.037   -8.221  1.00 26.13 ? 153 PHE   B C   1 
ATOM   3942 O O   . PHE   B 1 156 ? -27.778 6.528   -7.284  1.00 28.64 ? 153 PHE   B O   1 
ATOM   3943 C CB  . PHE   B 1 156 ? -28.082 9.117   -9.532  1.00 29.15 ? 153 PHE   B CB  1 
ATOM   3944 C CG  . PHE   B 1 156 ? -28.024 9.866   -8.220  1.00 25.25 ? 153 PHE   B CG  1 
ATOM   3945 C CD1 . PHE   B 1 156 ? -26.835 9.929   -7.500  1.00 24.84 ? 153 PHE   B CD1 1 
ATOM   3946 C CD2 . PHE   B 1 156 ? -29.147 10.490  -7.706  1.00 25.35 ? 153 PHE   B CD2 1 
ATOM   3947 C CE1 . PHE   B 1 156 ? -26.761 10.595  -6.285  1.00 23.75 ? 153 PHE   B CE1 1 
ATOM   3948 C CE2 . PHE   B 1 156 ? -29.085 11.175  -6.491  1.00 24.67 ? 153 PHE   B CE2 1 
ATOM   3949 C CZ  . PHE   B 1 156 ? -27.876 11.223  -5.777  1.00 25.54 ? 153 PHE   B CZ  1 
ATOM   3950 N N   . MET   B 1 157 ? -29.725 7.117   -8.232  1.00 29.02 ? 154 MET   B N   1 
ATOM   3951 C CA  . MET   B 1 157 ? -30.503 6.639   -7.102  1.00 27.46 ? 154 MET   B CA  1 
ATOM   3952 C C   . MET   B 1 157 ? -30.486 5.122   -7.053  1.00 32.10 ? 154 MET   B C   1 
ATOM   3953 O O   . MET   B 1 157 ? -30.656 4.456   -8.078  1.00 32.20 ? 154 MET   B O   1 
ATOM   3954 C CB  . MET   B 1 157 ? -31.937 7.146   -7.201  1.00 29.20 ? 154 MET   B CB  1 
ATOM   3955 C CG  . MET   B 1 157 ? -32.225 8.217   -6.177  1.00 32.92 ? 154 MET   B CG  1 
ATOM   3956 S SD  . MET   B 1 157 ? -33.838 8.951   -6.417  1.00 38.22 ? 154 MET   B SD  1 
ATOM   3957 C CE  . MET   B 1 157 ? -33.528 10.488  -5.545  1.00 28.49 ? 154 MET   B CE  1 
ATOM   3958 N N   . GLN   B 1 158 ? -30.282 4.576   -5.854  1.00 32.84 ? 155 GLN   B N   1 
ATOM   3959 C CA  . GLN   B 1 158 ? -30.290 3.128   -5.614  1.00 34.50 ? 155 GLN   B CA  1 
ATOM   3960 C C   . GLN   B 1 158 ? -31.434 2.822   -4.659  1.00 34.50 ? 155 GLN   B C   1 
ATOM   3961 O O   . GLN   B 1 158 ? -31.214 2.670   -3.459  1.00 33.81 ? 155 GLN   B O   1 
ATOM   3962 C CB  . GLN   B 1 158 ? -28.967 2.659   -5.049  1.00 36.23 ? 155 GLN   B CB  1 
ATOM   3963 C CG  . GLN   B 1 158 ? -27.738 3.194   -5.748  1.00 40.45 ? 155 GLN   B CG  1 
ATOM   3964 C CD  . GLN   B 1 158 ? -26.485 3.012   -4.905  1.00 47.81 ? 155 GLN   B CD  1 
ATOM   3965 O OE1 . GLN   B 1 158 ? -26.399 3.513   -3.774  1.00 49.50 ? 155 GLN   B OE1 1 
ATOM   3966 N NE2 . GLN   B 1 158 ? -25.515 2.279   -5.440  1.00 43.54 ? 155 GLN   B NE2 1 
ATOM   3967 N N   . VAL   B 1 159 ? -32.655 2.728   -5.195  1.00 32.09 ? 156 VAL   B N   1 
ATOM   3968 C CA  . VAL   B 1 159 ? -33.811 2.480   -4.339  1.00 34.66 ? 156 VAL   B CA  1 
ATOM   3969 C C   . VAL   B 1 159 ? -33.769 1.034   -3.857  1.00 33.99 ? 156 VAL   B C   1 
ATOM   3970 O O   . VAL   B 1 159 ? -33.523 0.107   -4.644  1.00 29.65 ? 156 VAL   B O   1 
ATOM   3971 C CB  . VAL   B 1 159 ? -35.119 2.784   -5.093  1.00 37.17 ? 156 VAL   B CB  1 
ATOM   3972 C CG1 . VAL   B 1 159 ? -36.310 2.544   -4.185  1.00 32.40 ? 156 VAL   B CG1 1 
ATOM   3973 C CG2 . VAL   B 1 159 ? -35.140 4.228   -5.600  1.00 32.47 ? 156 VAL   B CG2 1 
ATOM   3974 N N   . ARG   B 1 160 ? -34.006 0.837   -2.582  1.00 31.86 ? 157 ARG   B N   1 
ATOM   3975 C CA  . ARG   B 1 160 ? -33.997 -0.492  -2.013  1.00 35.50 ? 157 ARG   B CA  1 
ATOM   3976 C C   . ARG   B 1 160 ? -35.323 -0.796  -1.328  1.00 32.29 ? 157 ARG   B C   1 
ATOM   3977 O O   . ARG   B 1 160 ? -35.999 0.101   -0.873  1.00 30.41 ? 157 ARG   B O   1 
ATOM   3978 C CB  . ARG   B 1 160 ? -32.874 -0.606  -1.006  1.00 33.23 ? 157 ARG   B CB  1 
ATOM   3979 C CG  . ARG   B 1 160 ? -31.485 -0.496  -1.587  1.00 40.43 ? 157 ARG   B CG  1 
ATOM   3980 C CD  . ARG   B 1 160 ? -30.501 -0.104  -0.503  1.00 47.02 ? 157 ARG   B CD  1 
ATOM   3981 N NE  . ARG   B 1 160 ? -29.906 1.196   -0.774  1.00 52.10 ? 157 ARG   B NE  1 
ATOM   3982 C CZ  . ARG   B 1 160 ? -28.734 1.363   -1.369  1.00 48.03 ? 157 ARG   B CZ  1 
ATOM   3983 N NH1 . ARG   B 1 160 ? -28.020 0.315   -1.748  1.00 51.53 ? 157 ARG   B NH1 1 
ATOM   3984 N NH2 . ARG   B 1 160 ? -28.274 2.578   -1.583  1.00 47.03 ? 157 ARG   B NH2 1 
ATOM   3985 N N   . PRO   B 1 161 ? -35.677 -2.088  -1.245  1.00 34.70 ? 158 PRO   B N   1 
ATOM   3986 C CA  . PRO   B 1 161 ? -36.973 -2.423  -0.647  1.00 33.06 ? 158 PRO   B CA  1 
ATOM   3987 C C   . PRO   B 1 161 ? -37.080 -1.822  0.742   1.00 30.56 ? 158 PRO   B C   1 
ATOM   3988 O O   . PRO   B 1 161 ? -36.155 -1.913  1.549   1.00 36.61 ? 158 PRO   B O   1 
ATOM   3989 C CB  . PRO   B 1 161 ? -36.972 -3.959  -0.621  1.00 35.38 ? 158 PRO   B CB  1 
ATOM   3990 C CG  . PRO   B 1 161 ? -36.072 -4.350  -1.739  1.00 38.17 ? 158 PRO   B CG  1 
ATOM   3991 C CD  . PRO   B 1 161 ? -34.984 -3.281  -1.771  1.00 35.38 ? 158 PRO   B CD  1 
ATOM   3992 N N   . GLY   B 1 162 ? -38.205 -1.167  1.004   1.00 31.49 ? 159 GLY   B N   1 
ATOM   3993 C CA  . GLY   B 1 162 ? -38.440 -0.528  2.276   1.00 29.33 ? 159 GLY   B CA  1 
ATOM   3994 C C   . GLY   B 1 162 ? -37.999 0.918   2.367   1.00 31.18 ? 159 GLY   B C   1 
ATOM   3995 O O   . GLY   B 1 162 ? -38.269 1.564   3.391   1.00 35.25 ? 159 GLY   B O   1 
ATOM   3996 N N   . ASP   B 1 163 ? -37.304 1.440   1.352   1.00 33.19 ? 160 ASP   B N   1 
ATOM   3997 C CA  . ASP   B 1 163 ? -37.048 2.877   1.288   1.00 33.07 ? 160 ASP   B CA  1 
ATOM   3998 C C   . ASP   B 1 163 ? -38.361 3.645   1.300   1.00 32.32 ? 160 ASP   B C   1 
ATOM   3999 O O   . ASP   B 1 163 ? -39.400 3.148   0.859   1.00 35.56 ? 160 ASP   B O   1 
ATOM   4000 C CB  . ASP   B 1 163 ? -36.275 3.243   0.016   1.00 28.22 ? 160 ASP   B CB  1 
ATOM   4001 C CG  . ASP   B 1 163 ? -34.808 2.856   0.083   1.00 31.65 ? 160 ASP   B CG  1 
ATOM   4002 O OD1 . ASP   B 1 163 ? -34.298 2.623   1.205   1.00 31.89 ? 160 ASP   B OD1 1 
ATOM   4003 O OD2 . ASP   B 1 163 ? -34.162 2.803   -0.989  1.00 31.89 ? 160 ASP   B OD2 1 
ATOM   4004 N N   . THR   B 1 164 ? -38.313 4.868   1.812   1.00 29.89 ? 161 THR   B N   1 
ATOM   4005 C CA  . THR   B 1 164 ? -39.355 5.847   1.539   1.00 33.30 ? 161 THR   B CA  1 
ATOM   4006 C C   . THR   B 1 164 ? -38.810 6.853   0.525   1.00 34.98 ? 161 THR   B C   1 
ATOM   4007 O O   . THR   B 1 164 ? -37.766 7.481   0.761   1.00 30.99 ? 161 THR   B O   1 
ATOM   4008 C CB  . THR   B 1 164 ? -39.820 6.537   2.814   1.00 32.71 ? 161 THR   B CB  1 
ATOM   4009 O OG1 . THR   B 1 164 ? -40.564 5.603   3.604   1.00 35.18 ? 161 THR   B OG1 1 
ATOM   4010 C CG2 . THR   B 1 164 ? -40.709 7.719   2.483   1.00 36.34 ? 161 THR   B CG2 1 
ATOM   4011 N N   . VAL   B 1 165 ? -39.500 6.971   -0.608  1.00 27.44 ? 162 VAL   B N   1 
ATOM   4012 C CA  . VAL   B 1 165 ? -39.118 7.842   -1.717  1.00 29.15 ? 162 VAL   B CA  1 
ATOM   4013 C C   . VAL   B 1 165 ? -40.146 8.961   -1.810  1.00 30.55 ? 162 VAL   B C   1 
ATOM   4014 O O   . VAL   B 1 165 ? -41.355 8.693   -1.855  1.00 28.37 ? 162 VAL   B O   1 
ATOM   4015 C CB  . VAL   B 1 165 ? -39.043 7.058   -3.040  1.00 28.44 ? 162 VAL   B CB  1 
ATOM   4016 C CG1 . VAL   B 1 165 ? -38.743 7.997   -4.242  1.00 26.18 ? 162 VAL   B CG1 1 
ATOM   4017 C CG2 . VAL   B 1 165 ? -38.016 5.939   -2.961  1.00 26.37 ? 162 VAL   B CG2 1 
ATOM   4018 N N   . VAL   B 1 166 ? -39.671 10.210  -1.832  1.00 25.34 ? 163 VAL   B N   1 
ATOM   4019 C CA  . VAL   B 1 166 ? -40.516 11.391  -1.972  1.00 23.68 ? 163 VAL   B CA  1 
ATOM   4020 C C   . VAL   B 1 166 ? -40.251 12.015  -3.337  1.00 28.65 ? 163 VAL   B C   1 
ATOM   4021 O O   . VAL   B 1 166 ? -39.096 12.126  -3.767  1.00 23.20 ? 163 VAL   B O   1 
ATOM   4022 C CB  . VAL   B 1 166 ? -40.264 12.408  -0.840  1.00 27.19 ? 163 VAL   B CB  1 
ATOM   4023 C CG1 . VAL   B 1 166 ? -41.065 13.691  -1.066  1.00 25.06 ? 163 VAL   B CG1 1 
ATOM   4024 C CG2 . VAL   B 1 166 ? -40.640 11.805  0.509   1.00 28.54 ? 163 VAL   B CG2 1 
ATOM   4025 N N   . VAL   B 1 167 ? -41.323 12.410  -4.028  1.00 27.44 ? 164 VAL   B N   1 
ATOM   4026 C CA  . VAL   B 1 167 ? -41.246 13.018  -5.359  1.00 25.59 ? 164 VAL   B CA  1 
ATOM   4027 C C   . VAL   B 1 167 ? -42.024 14.333  -5.306  1.00 30.58 ? 164 VAL   B C   1 
ATOM   4028 O O   . VAL   B 1 167 ? -43.254 14.318  -5.193  1.00 29.18 ? 164 VAL   B O   1 
ATOM   4029 C CB  . VAL   B 1 167 ? -41.811 12.090  -6.450  1.00 24.63 ? 164 VAL   B CB  1 
ATOM   4030 C CG1 . VAL   B 1 167 ? -41.707 12.717  -7.852  1.00 25.29 ? 164 VAL   B CG1 1 
ATOM   4031 C CG2 . VAL   B 1 167 ? -41.093 10.731  -6.431  1.00 26.73 ? 164 VAL   B CG2 1 
ATOM   4032 N N   . SER   B 1 168 ? -41.323 15.469  -5.371  1.00 25.56 ? 165 SER   B N   1 
ATOM   4033 C CA  . SER   B 1 168 ? -42.007 16.754  -5.477  1.00 24.06 ? 165 SER   B CA  1 
ATOM   4034 C C   . SER   B 1 168 ? -42.268 17.065  -6.951  1.00 26.64 ? 165 SER   B C   1 
ATOM   4035 O O   . SER   B 1 168 ? -41.430 16.795  -7.814  1.00 30.19 ? 165 SER   B O   1 
ATOM   4036 C CB  . SER   B 1 168 ? -41.212 17.881  -4.812  1.00 26.60 ? 165 SER   B CB  1 
ATOM   4037 O OG  . SER   B 1 168 ? -39.957 18.078  -5.446  1.00 25.33 ? 165 SER   B OG  1 
ATOM   4038 N N   . GLY   B 1 169 ? -43.448 17.615  -7.237  1.00 31.47 ? 166 GLY   B N   1 
ATOM   4039 C CA  . GLY   B 1 169 ? -43.904 17.756  -8.615  1.00 24.30 ? 166 GLY   B CA  1 
ATOM   4040 C C   . GLY   B 1 169 ? -44.098 16.410  -9.282  1.00 30.74 ? 166 GLY   B C   1 
ATOM   4041 O O   . GLY   B 1 169 ? -43.533 16.145  -10.352 1.00 28.47 ? 166 GLY   B O   1 
ATOM   4042 N N   . ALA   B 1 170 ? -44.861 15.530  -8.664  1.00 27.17 ? 167 ALA   B N   1 
ATOM   4043 C CA  . ALA   B 1 170 ? -44.992 14.155  -9.149  1.00 29.48 ? 167 ALA   B CA  1 
ATOM   4044 C C   . ALA   B 1 170 ? -46.068 13.844  -10.174 1.00 30.43 ? 167 ALA   B C   1 
ATOM   4045 O O   . ALA   B 1 170 ? -46.067 12.762  -10.717 1.00 28.01 ? 167 ALA   B O   1 
ATOM   4046 C CB  . ALA   B 1 170 ? -45.205 13.266  -7.940  1.00 29.33 ? 167 ALA   B CB  1 
ATOM   4047 N N   . SER   B 1 171 ? -46.963 14.780  -10.430 1.00 29.39 ? 168 SER   B N   1 
ATOM   4048 C CA  . SER   B 1 171 ? -48.087 14.574  -11.354 1.00 33.24 ? 168 SER   B CA  1 
ATOM   4049 C C   . SER   B 1 171 ? -47.725 14.445  -12.816 1.00 32.17 ? 168 SER   B C   1 
ATOM   4050 O O   . SER   B 1 171 ? -48.485 13.908  -13.556 1.00 33.19 ? 168 SER   B O   1 
ATOM   4051 C CB  . SER   B 1 171 ? -49.114 15.712  -11.201 1.00 36.16 ? 168 SER   B CB  1 
ATOM   4052 O OG  . SER   B 1 171 ? -48.561 16.975  -11.412 1.00 32.95 ? 168 SER   B OG  1 
ATOM   4053 N N   . GLY   B 1 172 ? -46.586 14.980  -13.213 1.00 29.80 ? 169 GLY   B N   1 
ATOM   4054 C CA  . GLY   B 1 172 ? -46.159 14.910  -14.581 1.00 27.85 ? 169 GLY   B CA  1 
ATOM   4055 C C   . GLY   B 1 172 ? -45.552 13.595  -14.973 1.00 31.31 ? 169 GLY   B C   1 
ATOM   4056 O O   . GLY   B 1 172 ? -45.477 12.688  -14.167 1.00 31.20 ? 169 GLY   B O   1 
ATOM   4057 N N   . MET   B 1 173 ? -45.093 13.503  -16.206 1.00 28.27 ? 170 MET   B N   1 
ATOM   4058 C CA  . MET   B 1 173 ? -44.518 12.267  -16.680 1.00 25.78 ? 170 MET   B CA  1 
ATOM   4059 C C   . MET   B 1 173 ? -43.257 11.895  -15.923 1.00 30.22 ? 170 MET   B C   1 
ATOM   4060 O O   . MET   B 1 173 ? -43.062 10.746  -15.592 1.00 26.76 ? 170 MET   B O   1 
ATOM   4061 C CB  . MET   B 1 173 ? -44.190 12.299  -18.166 1.00 30.57 ? 170 MET   B CB  1 
ATOM   4062 C CG  . MET   B 1 173 ? -43.321 11.138  -18.607 1.00 33.38 ? 170 MET   B CG  1 
ATOM   4063 S SD  . MET   B 1 173 ? -43.059 10.959  -20.376 1.00 35.36 ? 170 MET   B SD  1 
ATOM   4064 C CE  . MET   B 1 173 ? -44.636 10.267  -20.852 1.00 38.86 ? 170 MET   B CE  1 
ATOM   4065 N N   . ILE   B 1 174 ? -42.416 12.878  -15.631 1.00 27.50 ? 171 ILE   B N   1 
ATOM   4066 C CA  . ILE   B 1 174 ? -41.143 12.495  -15.027 1.00 26.56 ? 171 ILE   B CA  1 
ATOM   4067 C C   . ILE   B 1 174 ? -41.370 11.972  -13.613 1.00 26.73 ? 171 ILE   B C   1 
ATOM   4068 O O   . ILE   B 1 174 ? -40.861 10.905  -13.242 1.00 27.12 ? 171 ILE   B O   1 
ATOM   4069 C CB  . ILE   B 1 174 ? -40.152 13.673  -15.065 1.00 26.47 ? 171 ILE   B CB  1 
ATOM   4070 C CG1 . ILE   B 1 174 ? -39.877 14.057  -16.527 1.00 27.14 ? 171 ILE   B CG1 1 
ATOM   4071 C CG2 . ILE   B 1 174 ? -38.872 13.311  -14.327 1.00 24.39 ? 171 ILE   B CG2 1 
ATOM   4072 C CD1 . ILE   B 1 174 ? -38.749 15.075  -16.751 1.00 24.00 ? 171 ILE   B CD1 1 
ATOM   4073 N N   . GLY   B 1 175 ? -42.177 12.686  -12.826 1.00 23.37 ? 172 GLY   B N   1 
ATOM   4074 C CA  . GLY   B 1 175 ? -42.416 12.282  -11.451 1.00 28.56 ? 172 GLY   B CA  1 
ATOM   4075 C C   . GLY   B 1 175 ? -43.164 10.963  -11.340 1.00 32.69 ? 172 GLY   B C   1 
ATOM   4076 O O   . GLY   B 1 175 ? -42.864 10.139  -10.466 1.00 25.78 ? 172 GLY   B O   1 
ATOM   4077 N N   . THR   B 1 176 ? -44.155 10.742  -12.215 1.00 28.50 ? 173 THR   B N   1 
ATOM   4078 C CA  . THR   B 1 176 ? -44.862 9.468   -12.180 1.00 30.91 ? 173 THR   B CA  1 
ATOM   4079 C C   . THR   B 1 176 ? -43.971 8.323   -12.644 1.00 29.76 ? 173 THR   B C   1 
ATOM   4080 O O   . THR   B 1 176 ? -44.097 7.210   -12.131 1.00 31.72 ? 173 THR   B O   1 
ATOM   4081 C CB  . THR   B 1 176 ? -46.146 9.514   -13.027 1.00 30.96 ? 173 THR   B CB  1 
ATOM   4082 O OG1 . THR   B 1 176 ? -45.819 9.737   -14.399 1.00 30.50 ? 173 THR   B OG1 1 
ATOM   4083 C CG2 . THR   B 1 176 ? -47.087 10.596  -12.533 1.00 30.40 ? 173 THR   B CG2 1 
ATOM   4084 N N   . LEU   B 1 177 ? -43.065 8.559   -13.597 1.00 26.55 ? 174 LEU   B N   1 
ATOM   4085 C CA  . LEU   B 1 177 ? -42.124 7.503   -13.971 1.00 27.76 ? 174 LEU   B CA  1 
ATOM   4086 C C   . LEU   B 1 177 ? -41.204 7.170   -12.807 1.00 28.88 ? 174 LEU   B C   1 
ATOM   4087 O O   . LEU   B 1 177 ? -41.010 5.997   -12.470 1.00 28.17 ? 174 LEU   B O   1 
ATOM   4088 C CB  . LEU   B 1 177 ? -41.295 7.905   -15.191 1.00 31.60 ? 174 LEU   B CB  1 
ATOM   4089 C CG  . LEU   B 1 177 ? -41.965 8.047   -16.553 1.00 35.43 ? 174 LEU   B CG  1 
ATOM   4090 C CD1 . LEU   B 1 177 ? -40.958 8.576   -17.580 1.00 32.46 ? 174 LEU   B CD1 1 
ATOM   4091 C CD2 . LEU   B 1 177 ? -42.543 6.714   -17.011 1.00 36.21 ? 174 LEU   B CD2 1 
ATOM   4092 N N   . VAL   B 1 178 ? -40.622 8.203   -12.189 1.00 27.67 ? 175 VAL   B N   1 
ATOM   4093 C CA  . VAL   B 1 178 ? -39.798 8.015   -10.996 1.00 25.71 ? 175 VAL   B CA  1 
ATOM   4094 C C   . VAL   B 1 178 ? -40.575 7.224   -9.950  1.00 30.57 ? 175 VAL   B C   1 
ATOM   4095 O O   . VAL   B 1 178 ? -40.096 6.209   -9.429  1.00 31.44 ? 175 VAL   B O   1 
ATOM   4096 C CB  . VAL   B 1 178 ? -39.338 9.380   -10.442 1.00 26.51 ? 175 VAL   B CB  1 
ATOM   4097 C CG1 . VAL   B 1 178 ? -38.667 9.229   -9.062  1.00 22.02 ? 175 VAL   B CG1 1 
ATOM   4098 C CG2 . VAL   B 1 178 ? -38.384 10.074  -11.415 1.00 25.46 ? 175 VAL   B CG2 1 
ATOM   4099 N N   . GLY   B 1 179 ? -41.796 7.675   -9.643  1.00 26.55 ? 176 GLY   B N   1 
ATOM   4100 C CA  . GLY   B 1 179 ? -42.593 7.025   -8.609  1.00 29.82 ? 176 GLY   B CA  1 
ATOM   4101 C C   . GLY   B 1 179 ? -42.845 5.552   -8.882  1.00 28.03 ? 176 GLY   B C   1 
ATOM   4102 O O   . GLY   B 1 179 ? -42.746 4.716   -7.978  1.00 30.46 ? 176 GLY   B O   1 
ATOM   4103 N N   . GLN   B 1 180 ? -43.167 5.214   -10.127 1.00 31.28 ? 177 GLN   B N   1 
ATOM   4104 C CA  . GLN   B 1 180 ? -43.457 3.827   -10.476 1.00 30.82 ? 177 GLN   B CA  1 
ATOM   4105 C C   . GLN   B 1 180 ? -42.201 2.974   -10.460 1.00 35.15 ? 177 GLN   B C   1 
ATOM   4106 O O   . GLN   B 1 180 ? -42.237 1.812   -10.030 1.00 31.54 ? 177 GLN   B O   1 
ATOM   4107 C CB  . GLN   B 1 180 ? -44.132 3.760   -11.846 1.00 28.63 ? 177 GLN   B CB  1 
ATOM   4108 C CG  . GLN   B 1 180 ? -45.568 4.259   -11.838 1.00 32.10 ? 177 GLN   B CG  1 
ATOM   4109 C CD  . GLN   B 1 180 ? -46.179 4.285   -13.226 1.00 35.78 ? 177 GLN   B CD  1 
ATOM   4110 O OE1 . GLN   B 1 180 ? -46.837 3.340   -13.647 1.00 47.19 ? 177 GLN   B OE1 1 
ATOM   4111 N NE2 . GLN   B 1 180 ? -45.962 5.374   -13.942 1.00 38.07 ? 177 GLN   B NE2 1 
ATOM   4112 N N   . MET   B 1 181 ? -41.084 3.519   -10.945 1.00 30.67 ? 178 MET   B N   1 
ATOM   4113 C CA  . MET   B 1 181 ? -39.829 2.787   -10.874 1.00 29.75 ? 178 MET   B CA  1 
ATOM   4114 C C   . MET   B 1 181 ? -39.419 2.552   -9.422  1.00 34.34 ? 178 MET   B C   1 
ATOM   4115 O O   . MET   B 1 181 ? -38.858 1.501   -9.088  1.00 35.55 ? 178 MET   B O   1 
ATOM   4116 C CB  . MET   B 1 181 ? -38.744 3.539   -11.651 1.00 32.73 ? 178 MET   B CB  1 
ATOM   4117 C CG  . MET   B 1 181 ? -38.666 3.183   -13.133 1.00 34.49 ? 178 MET   B CG  1 
ATOM   4118 S SD  . MET   B 1 181 ? -37.612 4.339   -14.042 1.00 34.12 ? 178 MET   B SD  1 
ATOM   4119 C CE  . MET   B 1 181 ? -38.166 5.869   -13.258 1.00 34.24 ? 178 MET   B CE  1 
ATOM   4120 N N   . ALA   B 1 182 ? -39.703 3.519   -8.535  1.00 29.94 ? 179 ALA   B N   1 
ATOM   4121 C CA  . ALA   B 1 182 ? -39.392 3.338   -7.120  1.00 32.69 ? 179 ALA   B CA  1 
ATOM   4122 C C   . ALA   B 1 182 ? -40.281 2.269   -6.496  1.00 35.01 ? 179 ALA   B C   1 
ATOM   4123 O O   . ALA   B 1 182 ? -39.817 1.450   -5.696  1.00 29.73 ? 179 ALA   B O   1 
ATOM   4124 C CB  . ALA   B 1 182 ? -39.547 4.661   -6.369  1.00 27.67 ? 179 ALA   B CB  1 
ATOM   4125 N N   . LYS   B 1 183 ? -41.565 2.261   -6.848  1.00 33.41 ? 180 LYS   B N   1 
ATOM   4126 C CA  . LYS   B 1 183 ? -42.461 1.248   -6.300  1.00 32.26 ? 180 LYS   B CA  1 
ATOM   4127 C C   . LYS   B 1 183 ? -42.050 -0.152  -6.758  1.00 33.66 ? 180 LYS   B C   1 
ATOM   4128 O O   . LYS   B 1 183 ? -42.090 -1.107  -5.972  1.00 34.03 ? 180 LYS   B O   1 
ATOM   4129 C CB  . LYS   B 1 183 ? -43.904 1.566   -6.685  1.00 34.88 ? 180 LYS   B CB  1 
ATOM   4130 C CG  . LYS   B 1 183 ? -44.907 0.502   -6.258  1.00 41.34 ? 180 LYS   B CG  1 
ATOM   4131 C CD  . LYS   B 1 183 ? -44.843 0.247   -4.757  1.00 42.09 ? 180 LYS   B CD  1 
ATOM   4132 C CE  . LYS   B 1 183 ? -45.355 1.421   -3.982  1.00 32.22 ? 180 LYS   B CE  1 
ATOM   4133 N NZ  . LYS   B 1 183 ? -45.414 1.106   -2.538  1.00 37.85 ? 180 LYS   B NZ  1 
ATOM   4134 N N   . ARG   B 1 184 ? -41.619 -0.287  -8.016  1.00 31.16 ? 181 ARG   B N   1 
ATOM   4135 C CA  . ARG   B 1 184 ? -41.176 -1.585  -8.522  1.00 36.64 ? 181 ARG   B CA  1 
ATOM   4136 C C   . ARG   B 1 184 ? -39.941 -2.083  -7.787  1.00 38.72 ? 181 ARG   B C   1 
ATOM   4137 O O   . ARG   B 1 184 ? -39.692 -3.296  -7.741  1.00 31.96 ? 181 ARG   B O   1 
ATOM   4138 C CB  . ARG   B 1 184 ? -40.878 -1.513  -10.021 1.00 33.06 ? 181 ARG   B CB  1 
ATOM   4139 C CG  . ARG   B 1 184 ? -42.105 -1.361  -10.912 1.00 38.16 ? 181 ARG   B CG  1 
ATOM   4140 C CD  . ARG   B 1 184 ? -41.709 -1.265  -12.380 1.00 37.00 ? 181 ARG   B CD  1 
ATOM   4141 N NE  . ARG   B 1 184 ? -40.901 -2.396  -12.828 1.00 44.08 ? 181 ARG   B NE  1 
ATOM   4142 C CZ  . ARG   B 1 184 ? -41.406 -3.534  -13.284 1.00 46.76 ? 181 ARG   B CZ  1 
ATOM   4143 N NH1 . ARG   B 1 184 ? -42.716 -3.728  -13.354 1.00 51.21 ? 181 ARG   B NH1 1 
ATOM   4144 N NH2 . ARG   B 1 184 ? -40.581 -4.498  -13.679 1.00 46.72 ? 181 ARG   B NH2 1 
ATOM   4145 N N   . ALA   B 1 185 ? -39.140 -1.167  -7.247  1.00 34.97 ? 182 ALA   B N   1 
ATOM   4146 C CA  . ALA   B 1 185 ? -37.948 -1.521  -6.487  1.00 36.57 ? 182 ALA   B CA  1 
ATOM   4147 C C   . ALA   B 1 185 ? -38.259 -1.813  -5.027  1.00 35.59 ? 182 ALA   B C   1 
ATOM   4148 O O   . ALA   B 1 185 ? -37.335 -2.110  -4.260  1.00 35.92 ? 182 ALA   B O   1 
ATOM   4149 C CB  . ALA   B 1 185 ? -36.908 -0.396  -6.596  1.00 33.60 ? 182 ALA   B CB  1 
ATOM   4150 N N   . GLY   B 1 186 ? -39.526 -1.728  -4.631  1.00 33.26 ? 183 GLY   B N   1 
ATOM   4151 C CA  . GLY   B 1 186 ? -39.943 -2.051  -3.284  1.00 31.26 ? 183 GLY   B CA  1 
ATOM   4152 C C   . GLY   B 1 186 ? -40.075 -0.881  -2.340  1.00 33.86 ? 183 GLY   B C   1 
ATOM   4153 O O   . GLY   B 1 186 ? -40.097 -1.093  -1.123  1.00 34.49 ? 183 GLY   B O   1 
ATOM   4154 N N   . ALA   B 1 187 ? -40.160 0.342   -2.843  1.00 30.41 ? 184 ALA   B N   1 
ATOM   4155 C CA  . ALA   B 1 187 ? -40.211 1.485   -1.947  1.00 30.65 ? 184 ALA   B CA  1 
ATOM   4156 C C   . ALA   B 1 187 ? -41.646 1.869   -1.586  1.00 27.58 ? 184 ALA   B C   1 
ATOM   4157 O O   . ALA   B 1 187 ? -42.602 1.557   -2.298  1.00 37.06 ? 184 ALA   B O   1 
ATOM   4158 C CB  . ALA   B 1 187 ? -39.511 2.689   -2.587  1.00 32.67 ? 184 ALA   B CB  1 
ATOM   4159 N N   . ARG   B 1 188 ? -41.774 2.582   -0.475  1.00 27.79 ? 185 ARG   B N   1 
ATOM   4160 C CA  . ARG   B 1 188 ? -42.924 3.445   -0.244  1.00 32.40 ? 185 ARG   B CA  1 
ATOM   4161 C C   . ARG   B 1 188 ? -42.694 4.745   -1.012  1.00 35.22 ? 185 ARG   B C   1 
ATOM   4162 O O   . ARG   B 1 188 ? -41.590 5.295   -0.975  1.00 31.73 ? 185 ARG   B O   1 
ATOM   4163 C CB  . ARG   B 1 188 ? -43.085 3.716   1.246   1.00 31.63 ? 185 ARG   B CB  1 
ATOM   4164 C CG  . ARG   B 1 188 ? -44.174 4.706   1.624   1.00 29.94 ? 185 ARG   B CG  1 
ATOM   4165 C CD  . ARG   B 1 188 ? -44.243 4.862   3.135   1.00 34.42 ? 185 ARG   B CD  1 
ATOM   4166 N NE  . ARG   B 1 188 ? -45.276 5.812   3.535   1.00 32.47 ? 185 ARG   B NE  1 
ATOM   4167 C CZ  . ARG   B 1 188 ? -46.579 5.549   3.512   1.00 34.28 ? 185 ARG   B CZ  1 
ATOM   4168 N NH1 . ARG   B 1 188 ? -47.036 4.361   3.151   1.00 32.95 ? 185 ARG   B NH1 1 
ATOM   4169 N NH2 . ARG   B 1 188 ? -47.443 6.508   3.842   1.00 28.87 ? 185 ARG   B NH2 1 
ATOM   4170 N N   . VAL   B 1 189 ? -43.719 5.229   -1.719  1.00 33.83 ? 186 VAL   B N   1 
ATOM   4171 C CA  . VAL   B 1 189 ? -43.584 6.364   -2.635  1.00 29.95 ? 186 VAL   B CA  1 
ATOM   4172 C C   . VAL   B 1 189 ? -44.601 7.435   -2.250  1.00 33.08 ? 186 VAL   B C   1 
ATOM   4173 O O   . VAL   B 1 189 ? -45.812 7.176   -2.229  1.00 34.45 ? 186 VAL   B O   1 
ATOM   4174 C CB  . VAL   B 1 189 ? -43.759 5.931   -4.103  1.00 31.38 ? 186 VAL   B CB  1 
ATOM   4175 C CG1 . VAL   B 1 189 ? -43.599 7.115   -5.044  1.00 26.33 ? 186 VAL   B CG1 1 
ATOM   4176 C CG2 . VAL   B 1 189 ? -42.777 4.835   -4.450  1.00 28.99 ? 186 VAL   B CG2 1 
ATOM   4177 N N   . VAL   B 1 190 ? -44.104 8.622   -1.912  1.00 27.01 ? 187 VAL   B N   1 
ATOM   4178 C CA  . VAL   B 1 190 ? -44.915 9.794   -1.615  1.00 23.75 ? 187 VAL   B CA  1 
ATOM   4179 C C   . VAL   B 1 190 ? -44.685 10.823  -2.721  1.00 32.13 ? 187 VAL   B C   1 
ATOM   4180 O O   . VAL   B 1 190 ? -43.545 11.050  -3.144  1.00 29.31 ? 187 VAL   B O   1 
ATOM   4181 C CB  . VAL   B 1 190 ? -44.555 10.375  -0.237  1.00 23.09 ? 187 VAL   B CB  1 
ATOM   4182 C CG1 . VAL   B 1 190 ? -45.286 11.668  0.032   1.00 26.48 ? 187 VAL   B CG1 1 
ATOM   4183 C CG2 . VAL   B 1 190 ? -44.823 9.335   0.878   1.00 28.64 ? 187 VAL   B CG2 1 
ATOM   4184 N N   . GLY   B 1 191 ? -45.773 11.436  -3.198  1.00 33.03 ? 188 GLY   B N   1 
ATOM   4185 C CA  . GLY   B 1 191 ? -45.687 12.514  -4.163  1.00 30.03 ? 188 GLY   B CA  1 
ATOM   4186 C C   . GLY   B 1 191 ? -46.458 13.742  -3.697  1.00 34.27 ? 188 GLY   B C   1 
ATOM   4187 O O   . GLY   B 1 191 ? -47.171 13.719  -2.688  1.00 32.68 ? 188 GLY   B O   1 
ATOM   4188 N N   . THR   B 1 192 ? -46.293 14.826  -4.445  1.00 33.46 ? 189 THR   B N   1 
ATOM   4189 C CA  . THR   B 1 192 ? -47.129 16.016  -4.302  1.00 36.35 ? 189 THR   B CA  1 
ATOM   4190 C C   . THR   B 1 192 ? -47.883 16.234  -5.610  1.00 36.56 ? 189 THR   B C   1 
ATOM   4191 O O   . THR   B 1 192 ? -47.393 15.875  -6.687  1.00 37.46 ? 189 THR   B O   1 
ATOM   4192 C CB  . THR   B 1 192 ? -46.301 17.265  -3.961  1.00 37.86 ? 189 THR   B CB  1 
ATOM   4193 O OG1 . THR   B 1 192 ? -45.514 17.636  -5.097  1.00 44.70 ? 189 THR   B OG1 1 
ATOM   4194 C CG2 . THR   B 1 192 ? -45.379 16.987  -2.800  1.00 34.18 ? 189 THR   B CG2 1 
ATOM   4195 N N   . ALA   B 1 193 ? -49.087 16.804  -5.513  1.00 36.25 ? 190 ALA   B N   1 
ATOM   4196 C CA  . ALA   B 1 193 ? -49.914 17.047  -6.689  1.00 34.50 ? 190 ALA   B CA  1 
ATOM   4197 C C   . ALA   B 1 193 ? -50.884 18.173  -6.382  1.00 36.49 ? 190 ALA   B C   1 
ATOM   4198 O O   . ALA   B 1 193 ? -51.120 18.508  -5.221  1.00 37.26 ? 190 ALA   B O   1 
ATOM   4199 C CB  . ALA   B 1 193 ? -50.670 15.790  -7.133  1.00 41.50 ? 190 ALA   B CB  1 
ATOM   4200 N N   . GLY   B 1 194 ? -51.454 18.747  -7.445  1.00 36.37 ? 191 GLY   B N   1 
ATOM   4201 C CA  . GLY   B 1 194 ? -52.151 20.015  -7.323  1.00 37.11 ? 191 GLY   B CA  1 
ATOM   4202 C C   . GLY   B 1 194 ? -53.662 19.985  -7.188  1.00 39.01 ? 191 GLY   B C   1 
ATOM   4203 O O   . GLY   B 1 194 ? -54.273 21.020  -6.894  1.00 37.32 ? 191 GLY   B O   1 
ATOM   4204 N N   . SER   B 1 195 ? -54.284 18.828  -7.399  1.00 38.49 ? 192 SER   B N   1 
ATOM   4205 C CA  . SER   B 1 195 ? -55.736 18.737  -7.294  1.00 43.59 ? 192 SER   B CA  1 
ATOM   4206 C C   . SER   B 1 195 ? -56.126 17.357  -6.779  1.00 45.25 ? 192 SER   B C   1 
ATOM   4207 O O   . SER   B 1 195 ? -55.336 16.405  -6.827  1.00 43.34 ? 192 SER   B O   1 
ATOM   4208 C CB  . SER   B 1 195 ? -56.414 19.024  -8.642  1.00 41.33 ? 192 SER   B CB  1 
ATOM   4209 O OG  . SER   B 1 195 ? -55.929 18.163  -9.654  1.00 39.49 ? 192 SER   B OG  1 
ATOM   4210 N N   . ALA   B 1 196 ? -57.357 17.262  -6.267  1.00 42.43 ? 193 ALA   B N   1 
ATOM   4211 C CA  . ALA   B 1 196 ? -57.863 15.964  -5.832  1.00 39.68 ? 193 ALA   B CA  1 
ATOM   4212 C C   . ALA   B 1 196 ? -57.864 14.969  -6.983  1.00 38.04 ? 193 ALA   B C   1 
ATOM   4213 O O   . ALA   B 1 196 ? -57.539 13.792  -6.797  1.00 40.14 ? 193 ALA   B O   1 
ATOM   4214 C CB  . ALA   B 1 196 ? -59.269 16.108  -5.243  1.00 42.80 ? 193 ALA   B CB  1 
ATOM   4215 N N   . GLY   B 1 197 ? -58.206 15.430  -8.189  1.00 39.50 ? 194 GLY   B N   1 
ATOM   4216 C CA  . GLY   B 1 197 ? -58.229 14.534  -9.332  1.00 37.40 ? 194 GLY   B CA  1 
ATOM   4217 C C   . GLY   B 1 197 ? -56.868 13.940  -9.645  1.00 43.72 ? 194 GLY   B C   1 
ATOM   4218 O O   . GLY   B 1 197 ? -56.750 12.744  -9.918  1.00 39.73 ? 194 GLY   B O   1 
ATOM   4219 N N   . LYS   B 1 198 ? -55.819 14.768  -9.619  1.00 41.30 ? 195 LYS   B N   1 
ATOM   4220 C CA  . LYS   B 1 198 ? -54.476 14.249  -9.865  1.00 41.88 ? 195 LYS   B CA  1 
ATOM   4221 C C   . LYS   B 1 198 ? -54.035 13.317  -8.745  1.00 36.91 ? 195 LYS   B C   1 
ATOM   4222 O O   . LYS   B 1 198 ? -53.372 12.306  -8.998  1.00 41.68 ? 195 LYS   B O   1 
ATOM   4223 C CB  . LYS   B 1 198 ? -53.475 15.398  -10.011 1.00 41.47 ? 195 LYS   B CB  1 
ATOM   4224 C CG  . LYS   B 1 198 ? -53.727 16.312  -11.183 1.00 42.32 ? 195 LYS   B CG  1 
ATOM   4225 C CD  . LYS   B 1 198 ? -52.844 15.980  -12.360 1.00 39.09 ? 195 LYS   B CD  1 
ATOM   4226 C CE  . LYS   B 1 198 ? -52.930 17.095  -13.380 1.00 38.74 ? 195 LYS   B CE  1 
ATOM   4227 N NZ  . LYS   B 1 198 ? -51.577 17.592  -13.777 1.00 39.02 ? 195 LYS   B NZ  1 
ATOM   4228 N N   . ALA   B 1 199 ? -54.383 13.653  -7.498  1.00 38.07 ? 196 ALA   B N   1 
ATOM   4229 C CA  . ALA   B 1 199 ? -54.016 12.809  -6.366  1.00 39.99 ? 196 ALA   B CA  1 
ATOM   4230 C C   . ALA   B 1 199 ? -54.539 11.385  -6.528  1.00 37.96 ? 196 ALA   B C   1 
ATOM   4231 O O   . ALA   B 1 199 ? -53.820 10.422  -6.240  1.00 35.68 ? 196 ALA   B O   1 
ATOM   4232 C CB  . ALA   B 1 199 ? -54.535 13.430  -5.069  1.00 37.27 ? 196 ALA   B CB  1 
ATOM   4233 N N   . ARG   B 1 200 ? -55.793 11.224  -6.982  1.00 41.16 ? 197 ARG   B N   1 
ATOM   4234 C CA  . ARG   B 1 200 ? -56.321 9.874   -7.207  1.00 38.99 ? 197 ARG   B CA  1 
ATOM   4235 C C   . ARG   B 1 200 ? -55.680 9.224   -8.422  1.00 39.53 ? 197 ARG   B C   1 
ATOM   4236 O O   . ARG   B 1 200 ? -55.531 7.995   -8.470  1.00 36.55 ? 197 ARG   B O   1 
ATOM   4237 C CB  . ARG   B 1 200 ? -57.841 9.903   -7.373  1.00 42.22 ? 197 ARG   B CB  1 
ATOM   4238 C CG  . ARG   B 1 200 ? -58.599 10.417  -6.155  1.00 45.31 ? 197 ARG   B CG  1 
ATOM   4239 C CD  . ARG   B 1 200 ? -60.115 10.313  -6.361  1.00 51.42 ? 197 ARG   B CD  1 
ATOM   4240 N NE  . ARG   B 1 200 ? -60.569 11.115  -7.490  1.00 48.67 ? 197 ARG   B NE  1 
ATOM   4241 C CZ  . ARG   B 1 200 ? -60.992 12.370  -7.397  1.00 46.16 ? 197 ARG   B CZ  1 
ATOM   4242 N NH1 . ARG   B 1 200 ? -61.084 12.986  -6.227  1.00 51.68 ? 197 ARG   B NH1 1 
ATOM   4243 N NH2 . ARG   B 1 200 ? -61.332 13.024  -8.504  1.00 47.99 ? 197 ARG   B NH2 1 
ATOM   4244 N N   . TYR   B 1 201 ? -55.301 10.025  -9.418  1.00 34.41 ? 198 TYR   B N   1 
ATOM   4245 C CA  . TYR   B 1 201 ? -54.566 9.474   -10.547 1.00 36.49 ? 198 TYR   B CA  1 
ATOM   4246 C C   . TYR   B 1 201 ? -53.221 8.900   -10.090 1.00 34.94 ? 198 TYR   B C   1 
ATOM   4247 O O   . TYR   B 1 201 ? -52.860 7.771   -10.443 1.00 35.42 ? 198 TYR   B O   1 
ATOM   4248 C CB  . TYR   B 1 201 ? -54.396 10.560  -11.618 1.00 37.32 ? 198 TYR   B CB  1 
ATOM   4249 C CG  . TYR   B 1 201 ? -53.474 10.193  -12.754 1.00 37.72 ? 198 TYR   B CG  1 
ATOM   4250 C CD1 . TYR   B 1 201 ? -53.846 9.243   -13.694 1.00 43.84 ? 198 TYR   B CD1 1 
ATOM   4251 C CD2 . TYR   B 1 201 ? -52.233 10.810  -12.898 1.00 39.48 ? 198 TYR   B CD2 1 
ATOM   4252 C CE1 . TYR   B 1 201 ? -53.012 8.908   -14.737 1.00 43.40 ? 198 TYR   B CE1 1 
ATOM   4253 C CE2 . TYR   B 1 201 ? -51.389 10.483  -13.947 1.00 37.82 ? 198 TYR   B CE2 1 
ATOM   4254 C CZ  . TYR   B 1 201 ? -51.782 9.531   -14.860 1.00 43.20 ? 198 TYR   B CZ  1 
ATOM   4255 O OH  . TYR   B 1 201 ? -50.952 9.184   -15.905 1.00 44.60 ? 198 TYR   B OH  1 
ATOM   4256 N N   . LEU   B 1 202 ? -52.468 9.662   -9.288  1.00 34.40 ? 199 LEU   B N   1 
ATOM   4257 C CA  . LEU   B 1 202 ? -51.175 9.162   -8.809  1.00 33.79 ? 199 LEU   B CA  1 
ATOM   4258 C C   . LEU   B 1 202 ? -51.348 7.923   -7.937  1.00 33.29 ? 199 LEU   B C   1 
ATOM   4259 O O   . LEU   B 1 202 ? -50.589 6.952   -8.059  1.00 36.60 ? 199 LEU   B O   1 
ATOM   4260 C CB  . LEU   B 1 202 ? -50.445 10.257  -8.031  1.00 36.06 ? 199 LEU   B CB  1 
ATOM   4261 C CG  . LEU   B 1 202 ? -49.788 11.406  -8.810  1.00 35.06 ? 199 LEU   B CG  1 
ATOM   4262 C CD1 . LEU   B 1 202 ? -49.125 12.372  -7.839  1.00 31.83 ? 199 LEU   B CD1 1 
ATOM   4263 C CD2 . LEU   B 1 202 ? -48.774 10.865  -9.789  1.00 36.27 ? 199 LEU   B CD2 1 
ATOM   4264 N N   . SER   B 1 203 ? -52.340 7.941   -7.047  1.00 34.46 ? 200 SER   B N   1 
ATOM   4265 C CA  . SER   B 1 203 ? -52.608 6.776   -6.206  1.00 38.15 ? 200 SER   B CA  1 
ATOM   4266 C C   . SER   B 1 203 ? -52.816 5.525   -7.051  1.00 35.68 ? 200 SER   B C   1 
ATOM   4267 O O   . SER   B 1 203 ? -52.130 4.508   -6.862  1.00 32.53 ? 200 SER   B O   1 
ATOM   4268 C CB  . SER   B 1 203 ? -53.824 7.038   -5.325  1.00 32.77 ? 200 SER   B CB  1 
ATOM   4269 O OG  . SER   B 1 203 ? -53.579 8.131   -4.468  1.00 32.86 ? 200 SER   B OG  1 
ATOM   4270 N N   . GLN   B 1 204 ? -53.732 5.596   -8.024  1.00 33.24 ? 201 GLN   B N   1 
ATOM   4271 C CA  . GLN   B 1 204 ? -53.979 4.461   -8.905  1.00 34.15 ? 201 GLN   B CA  1 
ATOM   4272 C C   . GLN   B 1 204 ? -52.794 4.142   -9.797  1.00 38.25 ? 201 GLN   B C   1 
ATOM   4273 O O   . GLN   B 1 204 ? -52.858 3.174   -10.573 1.00 38.50 ? 201 GLN   B O   1 
ATOM   4274 C CB  . GLN   B 1 204 ? -55.231 4.715   -9.748  1.00 35.97 ? 201 GLN   B CB  1 
ATOM   4275 C CG  . GLN   B 1 204 ? -56.487 4.899   -8.888  1.00 43.14 ? 201 GLN   B CG  1 
ATOM   4276 C CD  . GLN   B 1 204 ? -57.790 4.796   -9.668  1.00 48.15 ? 201 GLN   B CD  1 
ATOM   4277 O OE1 . GLN   B 1 204 ? -57.924 3.985   -10.601 1.00 46.37 ? 201 GLN   B OE1 1 
ATOM   4278 N NE2 . GLN   B 1 204 ? -58.767 5.620   -9.287  1.00 44.16 ? 201 GLN   B NE2 1 
ATOM   4279 N N   . LEU   B 1 205 ? -51.717 4.926   -9.725  1.00 33.97 ? 202 LEU   B N   1 
ATOM   4280 C CA  . LEU   B 1 205 ? -50.476 4.558   -10.390 1.00 36.87 ? 202 LEU   B CA  1 
ATOM   4281 C C   . LEU   B 1 205 ? -49.500 3.864   -9.449  1.00 36.59 ? 202 LEU   B C   1 
ATOM   4282 O O   . LEU   B 1 205 ? -48.477 3.347   -9.914  1.00 39.52 ? 202 LEU   B O   1 
ATOM   4283 C CB  . LEU   B 1 205 ? -49.818 5.801   -11.013 1.00 36.02 ? 202 LEU   B CB  1 
ATOM   4284 C CG  . LEU   B 1 205 ? -50.573 6.347   -12.229 1.00 40.68 ? 202 LEU   B CG  1 
ATOM   4285 C CD1 . LEU   B 1 205 ? -49.944 7.637   -12.740 1.00 42.28 ? 202 LEU   B CD1 1 
ATOM   4286 C CD2 . LEU   B 1 205 ? -50.619 5.299   -13.332 1.00 41.81 ? 202 LEU   B CD2 1 
ATOM   4287 N N   . GLY   B 1 206 ? -49.795 3.833   -8.151  1.00 34.13 ? 203 GLY   B N   1 
ATOM   4288 C CA  . GLY   B 1 206 ? -48.969 3.118   -7.200  1.00 32.14 ? 203 GLY   B CA  1 
ATOM   4289 C C   . GLY   B 1 206 ? -48.504 3.958   -6.031  1.00 34.41 ? 203 GLY   B C   1 
ATOM   4290 O O   . GLY   B 1 206 ? -47.965 3.414   -5.060  1.00 35.66 ? 203 GLY   B O   1 
ATOM   4291 N N   . PHE   B 1 207 ? -48.700 5.283   -6.106  1.00 32.12 ? 204 PHE   B N   1 
ATOM   4292 C CA  . PHE   B 1 207 ? -48.271 6.162   -5.019  1.00 32.24 ? 204 PHE   B CA  1 
ATOM   4293 C C   . PHE   B 1 207 ? -49.008 5.811   -3.737  1.00 36.03 ? 204 PHE   B C   1 
ATOM   4294 O O   . PHE   B 1 207 ? -50.226 5.622   -3.744  1.00 34.18 ? 204 PHE   B O   1 
ATOM   4295 C CB  . PHE   B 1 207 ? -48.512 7.626   -5.389  1.00 32.14 ? 204 PHE   B CB  1 
ATOM   4296 C CG  . PHE   B 1 207 ? -47.431 8.211   -6.277  1.00 33.76 ? 204 PHE   B CG  1 
ATOM   4297 C CD1 . PHE   B 1 207 ? -47.239 7.730   -7.562  1.00 31.14 ? 204 PHE   B CD1 1 
ATOM   4298 C CD2 . PHE   B 1 207 ? -46.610 9.232   -5.814  1.00 34.11 ? 204 PHE   B CD2 1 
ATOM   4299 C CE1 . PHE   B 1 207 ? -46.244 8.252   -8.375  1.00 34.05 ? 204 PHE   B CE1 1 
ATOM   4300 C CE2 . PHE   B 1 207 ? -45.613 9.764   -6.627  1.00 32.47 ? 204 PHE   B CE2 1 
ATOM   4301 C CZ  . PHE   B 1 207 ? -45.437 9.265   -7.912  1.00 28.91 ? 204 PHE   B CZ  1 
ATOM   4302 N N   . ASP   B 1 208 ? -48.253 5.729   -2.634  1.00 29.97 ? 205 ASP   B N   1 
ATOM   4303 C CA  . ASP   B 1 208 ? -48.793 5.411   -1.318  1.00 35.31 ? 205 ASP   B CA  1 
ATOM   4304 C C   . ASP   B 1 208 ? -49.395 6.624   -0.629  1.00 36.69 ? 205 ASP   B C   1 
ATOM   4305 O O   . ASP   B 1 208 ? -50.290 6.478   0.206   1.00 33.96 ? 205 ASP   B O   1 
ATOM   4306 C CB  . ASP   B 1 208 ? -47.686 4.806   -0.448  1.00 33.66 ? 205 ASP   B CB  1 
ATOM   4307 C CG  . ASP   B 1 208 ? -47.153 3.521   -1.032  1.00 36.41 ? 205 ASP   B CG  1 
ATOM   4308 O OD1 . ASP   B 1 208 ? -47.879 2.504   -0.960  1.00 38.43 ? 205 ASP   B OD1 1 
ATOM   4309 O OD2 . ASP   B 1 208 ? -46.035 3.523   -1.595  1.00 34.06 ? 205 ASP   B OD2 1 
ATOM   4310 N N   . ALA   B 1 209 ? -48.928 7.823   -0.956  1.00 30.78 ? 206 ALA   B N   1 
ATOM   4311 C CA  . ALA   B 1 209 ? -49.495 9.036   -0.397  1.00 30.19 ? 206 ALA   B CA  1 
ATOM   4312 C C   . ALA   B 1 209 ? -49.247 10.167  -1.381  1.00 34.40 ? 206 ALA   B C   1 
ATOM   4313 O O   . ALA   B 1 209 ? -48.257 10.159  -2.116  1.00 30.98 ? 206 ALA   B O   1 
ATOM   4314 C CB  . ALA   B 1 209 ? -48.904 9.361   0.980   1.00 30.52 ? 206 ALA   B CB  1 
ATOM   4315 N N   . VAL   B 1 210 ? -50.178 11.120  -1.413  1.00 35.36 ? 207 VAL   B N   1 
ATOM   4316 C CA  . VAL   B 1 210 ? -50.074 12.297  -2.270  1.00 37.01 ? 207 VAL   B CA  1 
ATOM   4317 C C   . VAL   B 1 210 ? -50.471 13.505  -1.442  1.00 39.28 ? 207 VAL   B C   1 
ATOM   4318 O O   . VAL   B 1 210 ? -51.589 13.554  -0.911  1.00 34.10 ? 207 VAL   B O   1 
ATOM   4319 C CB  . VAL   B 1 210 ? -50.960 12.212  -3.526  1.00 35.38 ? 207 VAL   B CB  1 
ATOM   4320 C CG1 . VAL   B 1 210 ? -50.755 13.458  -4.380  1.00 37.36 ? 207 VAL   B CG1 1 
ATOM   4321 C CG2 . VAL   B 1 210 ? -50.657 10.961  -4.324  1.00 30.30 ? 207 VAL   B CG2 1 
ATOM   4322 N N   . ILE   B 1 211 ? -49.555 14.471  -1.326  1.00 29.02 ? 208 ILE   B N   1 
ATOM   4323 C CA  . ILE   B 1 211 ? -49.763 15.695  -0.568  1.00 32.58 ? 208 ILE   B CA  1 
ATOM   4324 C C   . ILE   B 1 211 ? -50.257 16.790  -1.501  1.00 38.05 ? 208 ILE   B C   1 
ATOM   4325 O O   . ILE   B 1 211 ? -49.737 16.963  -2.612  1.00 37.36 ? 208 ILE   B O   1 
ATOM   4326 C CB  . ILE   B 1 211 ? -48.462 16.115  0.137   1.00 33.12 ? 208 ILE   B CB  1 
ATOM   4327 C CG1 . ILE   B 1 211 ? -47.974 14.985  1.054   1.00 37.68 ? 208 ILE   B CG1 1 
ATOM   4328 C CG2 . ILE   B 1 211 ? -48.666 17.412  0.899   1.00 32.89 ? 208 ILE   B CG2 1 
ATOM   4329 C CD1 . ILE   B 1 211 ? -46.779 15.344  1.894   1.00 35.17 ? 208 ILE   B CD1 1 
ATOM   4330 N N   . ASP   B 1 212 ? -51.272 17.534  -1.057  1.00 40.36 ? 209 ASP   B N   1 
ATOM   4331 C CA  . ASP   B 1 212 ? -51.786 18.672  -1.817  1.00 38.48 ? 209 ASP   B CA  1 
ATOM   4332 C C   . ASP   B 1 212 ? -50.892 19.864  -1.511  1.00 37.00 ? 209 ASP   B C   1 
ATOM   4333 O O   . ASP   B 1 212 ? -50.989 20.472  -0.443  1.00 33.69 ? 209 ASP   B O   1 
ATOM   4334 C CB  . ASP   B 1 212 ? -53.244 18.957  -1.462  1.00 43.93 ? 209 ASP   B CB  1 
ATOM   4335 C CG  . ASP   B 1 212 ? -53.879 20.027  -2.361  1.00 46.19 ? 209 ASP   B CG  1 
ATOM   4336 O OD1 . ASP   B 1 212 ? -53.245 21.079  -2.590  1.00 47.24 ? 209 ASP   B OD1 1 
ATOM   4337 O OD2 . ASP   B 1 212 ? -55.016 19.808  -2.847  1.00 54.32 ? 209 ASP   B OD2 1 
ATOM   4338 N N   . TYR   B 1 213 ? -50.011 20.198  -2.457  1.00 39.23 ? 210 TYR   B N   1 
ATOM   4339 C CA  . TYR   B 1 213 ? -49.031 21.255  -2.225  1.00 36.88 ? 210 TYR   B CA  1 
ATOM   4340 C C   . TYR   B 1 213 ? -49.665 22.635  -2.165  1.00 37.26 ? 210 TYR   B C   1 
ATOM   4341 O O   . TYR   B 1 213 ? -49.059 23.553  -1.605  1.00 38.45 ? 210 TYR   B O   1 
ATOM   4342 C CB  . TYR   B 1 213 ? -47.949 21.230  -3.314  1.00 36.75 ? 210 TYR   B CB  1 
ATOM   4343 C CG  . TYR   B 1 213 ? -48.398 21.665  -4.703  1.00 34.30 ? 210 TYR   B CG  1 
ATOM   4344 C CD1 . TYR   B 1 213 ? -48.476 23.012  -5.044  1.00 33.80 ? 210 TYR   B CD1 1 
ATOM   4345 C CD2 . TYR   B 1 213 ? -48.694 20.724  -5.683  1.00 31.58 ? 210 TYR   B CD2 1 
ATOM   4346 C CE1 . TYR   B 1 213 ? -48.864 23.410  -6.320  1.00 34.53 ? 210 TYR   B CE1 1 
ATOM   4347 C CE2 . TYR   B 1 213 ? -49.081 21.106  -6.958  1.00 32.88 ? 210 TYR   B CE2 1 
ATOM   4348 C CZ  . TYR   B 1 213 ? -49.165 22.451  -7.275  1.00 36.26 ? 210 TYR   B CZ  1 
ATOM   4349 O OH  . TYR   B 1 213 ? -49.556 22.836  -8.541  1.00 32.33 ? 210 TYR   B OH  1 
ATOM   4350 N N   . LYS   B 1 214 ? -50.857 22.807  -2.741  1.00 37.66 ? 211 LYS   B N   1 
ATOM   4351 C CA  . LYS   B 1 214 ? -51.547 24.090  -2.648  1.00 38.30 ? 211 LYS   B CA  1 
ATOM   4352 C C   . LYS   B 1 214 ? -52.097 24.315  -1.246  1.00 41.63 ? 211 LYS   B C   1 
ATOM   4353 O O   . LYS   B 1 214 ? -52.063 25.440  -0.729  1.00 41.09 ? 211 LYS   B O   1 
ATOM   4354 C CB  . LYS   B 1 214 ? -52.662 24.153  -3.693  1.00 40.06 ? 211 LYS   B CB  1 
ATOM   4355 C CG  . LYS   B 1 214 ? -52.144 24.021  -5.115  1.00 39.91 ? 211 LYS   B CG  1 
ATOM   4356 C CD  . LYS   B 1 214 ? -53.264 23.930  -6.134  1.00 44.47 ? 211 LYS   B CD  1 
ATOM   4357 C CE  . LYS   B 1 214 ? -52.703 24.031  -7.546  1.00 42.51 ? 211 LYS   B CE  1 
ATOM   4358 N NZ  . LYS   B 1 214 ? -53.738 23.709  -8.575  1.00 47.46 ? 211 LYS   B NZ  1 
ATOM   4359 N N   . LEU   B 1 215 ? -52.601 23.257  -0.609  1.00 39.64 ? 212 LEU   B N   1 
ATOM   4360 C CA  . LEU   B 1 215 ? -53.032 23.385  0.783   1.00 43.25 ? 212 LEU   B CA  1 
ATOM   4361 C C   . LEU   B 1 215 ? -51.835 23.535  1.717   1.00 44.93 ? 212 LEU   B C   1 
ATOM   4362 O O   . LEU   B 1 215 ? -51.813 24.426  2.576   1.00 44.29 ? 212 LEU   B O   1 
ATOM   4363 C CB  . LEU   B 1 215 ? -53.887 22.182  1.184   1.00 42.27 ? 212 LEU   B CB  1 
ATOM   4364 C CG  . LEU   B 1 215 ? -55.390 22.452  1.097   1.00 55.72 ? 212 LEU   B CG  1 
ATOM   4365 C CD1 . LEU   B 1 215 ? -56.180 21.220  1.507   1.00 53.39 ? 212 LEU   B CD1 1 
ATOM   4366 C CD2 . LEU   B 1 215 ? -55.770 23.669  1.958   1.00 49.26 ? 212 LEU   B CD2 1 
ATOM   4367 N N   . ALA   B 1 216 ? -50.829 22.671  1.562   1.00 44.50 ? 213 ALA   B N   1 
ATOM   4368 C CA  . ALA   B 1 216 ? -49.631 22.707  2.404   1.00 39.52 ? 213 ALA   B CA  1 
ATOM   4369 C C   . ALA   B 1 216 ? -48.608 23.661  1.785   1.00 47.13 ? 213 ALA   B C   1 
ATOM   4370 O O   . ALA   B 1 216 ? -47.582 23.265  1.226   1.00 43.37 ? 213 ALA   B O   1 
ATOM   4371 C CB  . ALA   B 1 216 ? -49.064 21.305  2.578   1.00 38.93 ? 213 ALA   B CB  1 
ATOM   4372 N N   . ASP   B 1 217 ? -48.915 24.953  1.890   1.00 47.05 ? 214 ASP   B N   1 
ATOM   4373 C CA  . ASP   B 1 217 ? -48.156 25.983  1.193   1.00 48.20 ? 214 ASP   B CA  1 
ATOM   4374 C C   . ASP   B 1 217 ? -47.002 26.551  2.020   1.00 48.92 ? 214 ASP   B C   1 
ATOM   4375 O O   . ASP   B 1 217 ? -46.349 27.499  1.569   1.00 48.80 ? 214 ASP   B O   1 
ATOM   4376 C CB  . ASP   B 1 217 ? -49.096 27.109  0.755   1.00 49.07 ? 214 ASP   B CB  1 
ATOM   4377 C CG  . ASP   B 1 217 ? -49.902 27.684  1.907   1.00 51.45 ? 214 ASP   B CG  1 
ATOM   4378 O OD1 . ASP   B 1 217 ? -49.758 27.196  3.048   1.00 53.49 ? 214 ASP   B OD1 1 
ATOM   4379 O OD2 . ASP   B 1 217 ? -50.676 28.635  1.670   1.00 53.53 ? 214 ASP   B OD2 1 
ATOM   4380 N N   . ASP   B 1 218 ? -46.743 25.986  3.204   1.00 48.69 ? 215 ASP   B N   1 
ATOM   4381 C CA  . ASP   B 1 218 ? -45.669 26.375  4.109   1.00 45.25 ? 215 ASP   B CA  1 
ATOM   4382 C C   . ASP   B 1 218 ? -44.700 25.217  4.290   1.00 40.68 ? 215 ASP   B C   1 
ATOM   4383 O O   . ASP   B 1 218 ? -45.025 24.058  4.007   1.00 39.63 ? 215 ASP   B O   1 
ATOM   4384 C CB  . ASP   B 1 218 ? -46.201 26.752  5.509   1.00 47.07 ? 215 ASP   B CB  1 
ATOM   4385 C CG  . ASP   B 1 218 ? -46.986 28.032  5.507   1.00 55.96 ? 215 ASP   B CG  1 
ATOM   4386 O OD1 . ASP   B 1 218 ? -47.225 28.591  4.412   1.00 64.91 ? 215 ASP   B OD1 1 
ATOM   4387 O OD2 . ASP   B 1 218 ? -47.361 28.487  6.608   1.00 58.75 ? 215 ASP   B OD2 1 
ATOM   4388 N N   . ALA   B 1 219 ? -43.510 25.535  4.801   1.00 37.44 ? 216 ALA   B N   1 
ATOM   4389 C CA  . ALA   B 1 219 ? -42.631 24.469  5.276   1.00 44.36 ? 216 ALA   B CA  1 
ATOM   4390 C C   . ALA   B 1 219 ? -43.189 23.816  6.541   1.00 39.61 ? 216 ALA   B C   1 
ATOM   4391 O O   . ALA   B 1 219 ? -43.028 22.606  6.730   1.00 40.25 ? 216 ALA   B O   1 
ATOM   4392 C CB  . ALA   B 1 219 ? -41.214 25.002  5.513   1.00 40.86 ? 216 ALA   B CB  1 
ATOM   4393 N N   . ASP   B 1 220 ? -43.871 24.586  7.397   1.00 40.64 ? 217 ASP   B N   1 
ATOM   4394 C CA  . ASP   B 1 220 ? -44.511 23.988  8.566   1.00 41.55 ? 217 ASP   B CA  1 
ATOM   4395 C C   . ASP   B 1 220 ? -45.583 22.990  8.151   1.00 38.83 ? 217 ASP   B C   1 
ATOM   4396 O O   . ASP   B 1 220 ? -45.577 21.833  8.593   1.00 38.46 ? 217 ASP   B O   1 
ATOM   4397 C CB  . ASP   B 1 220 ? -45.110 25.065  9.462   1.00 45.33 ? 217 ASP   B CB  1 
ATOM   4398 C CG  . ASP   B 1 220 ? -44.075 25.741  10.324  1.00 53.86 ? 217 ASP   B CG  1 
ATOM   4399 O OD1 . ASP   B 1 220 ? -43.004 25.135  10.544  1.00 58.11 ? 217 ASP   B OD1 1 
ATOM   4400 O OD2 . ASP   B 1 220 ? -44.324 26.880  10.771  1.00 62.14 ? 217 ASP   B OD2 1 
ATOM   4401 N N   . LYS   B 1 221 ? -46.518 23.422  7.299   1.00 39.26 ? 218 LYS   B N   1 
ATOM   4402 C CA  . LYS   B 1 221 ? -47.568 22.521  6.831   1.00 36.55 ? 218 LYS   B CA  1 
ATOM   4403 C C   . LYS   B 1 221 ? -46.986 21.357  6.041   1.00 38.82 ? 218 LYS   B C   1 
ATOM   4404 O O   . LYS   B 1 221 ? -47.509 20.236  6.094   1.00 34.25 ? 218 LYS   B O   1 
ATOM   4405 C CB  . LYS   B 1 221 ? -48.582 23.284  5.979   1.00 40.88 ? 218 LYS   B CB  1 
ATOM   4406 C CG  . LYS   B 1 221 ? -49.257 24.449  6.691   1.00 46.94 ? 218 LYS   B CG  1 
ATOM   4407 C CD  . LYS   B 1 221 ? -50.128 25.236  5.717   1.00 47.44 ? 218 LYS   B CD  1 
ATOM   4408 C CE  . LYS   B 1 221 ? -50.738 26.459  6.384   1.00 50.87 ? 218 LYS   B CE  1 
ATOM   4409 N NZ  . LYS   B 1 221 ? -51.607 27.211  5.435   1.00 57.34 ? 218 LYS   B NZ  1 
ATOM   4410 N N   . MET   B 1 222 ? -45.916 21.604  5.273   1.00 36.48 ? 219 MET   B N   1 
ATOM   4411 C CA  . MET   B 1 222 ? -45.317 20.519  4.502   1.00 35.88 ? 219 MET   B CA  1 
ATOM   4412 C C   . MET   B 1 222 ? -44.624 19.519  5.418   1.00 35.95 ? 219 MET   B C   1 
ATOM   4413 O O   . MET   B 1 222 ? -44.729 18.304  5.213   1.00 38.68 ? 219 MET   B O   1 
ATOM   4414 C CB  . MET   B 1 222 ? -44.338 21.073  3.456   1.00 35.17 ? 219 MET   B CB  1 
ATOM   4415 C CG  . MET   B 1 222 ? -44.905 21.095  2.039   1.00 33.19 ? 219 MET   B CG  1 
ATOM   4416 S SD  . MET   B 1 222 ? -45.444 19.468  1.476   1.00 45.25 ? 219 MET   B SD  1 
ATOM   4417 C CE  . MET   B 1 222 ? -45.957 19.851  -0.196  1.00 40.08 ? 219 MET   B CE  1 
ATOM   4418 N N   . ARG   B 1 223 ? -43.905 20.010  6.427   1.00 32.92 ? 220 ARG   B N   1 
ATOM   4419 C CA  . ARG   B 1 223 ? -43.336 19.115  7.430   1.00 40.11 ? 220 ARG   B CA  1 
ATOM   4420 C C   . ARG   B 1 223 ? -44.420 18.244  8.051   1.00 39.40 ? 220 ARG   B C   1 
ATOM   4421 O O   . ARG   B 1 223 ? -44.302 17.015  8.087   1.00 38.19 ? 220 ARG   B O   1 
ATOM   4422 C CB  . ARG   B 1 223 ? -42.607 19.924  8.509   1.00 41.49 ? 220 ARG   B CB  1 
ATOM   4423 C CG  . ARG   B 1 223 ? -41.127 20.164  8.218   1.00 43.71 ? 220 ARG   B CG  1 
ATOM   4424 C CD  . ARG   B 1 223 ? -40.399 20.856  9.383   1.00 42.94 ? 220 ARG   B CD  1 
ATOM   4425 N NE  . ARG   B 1 223 ? -40.757 22.266  9.501   1.00 44.22 ? 220 ARG   B NE  1 
ATOM   4426 C CZ  . ARG   B 1 223 ? -40.179 23.247  8.817   1.00 47.60 ? 220 ARG   B CZ  1 
ATOM   4427 N NH1 . ARG   B 1 223 ? -39.198 23.011  7.957   1.00 47.01 ? 220 ARG   B NH1 1 
ATOM   4428 N NH2 . ARG   B 1 223 ? -40.601 24.497  8.992   1.00 47.71 ? 220 ARG   B NH2 1 
ATOM   4429 N N   . GLU   B 1 224 ? -45.496 18.873  8.535   1.00 42.37 ? 221 GLU   B N   1 
ATOM   4430 C CA  . GLU   B 1 224 ? -46.627 18.123  9.074   1.00 40.15 ? 221 GLU   B CA  1 
ATOM   4431 C C   . GLU   B 1 224 ? -47.085 17.044  8.104   1.00 37.93 ? 221 GLU   B C   1 
ATOM   4432 O O   . GLU   B 1 224 ? -47.200 15.871  8.471   1.00 42.30 ? 221 GLU   B O   1 
ATOM   4433 C CB  . GLU   B 1 224 ? -47.781 19.067  9.402   1.00 40.17 ? 221 GLU   B CB  1 
ATOM   4434 C CG  . GLU   B 1 224 ? -47.923 19.351  10.883  1.00 52.45 ? 221 GLU   B CG  1 
ATOM   4435 C CD  . GLU   B 1 224 ? -47.574 18.142  11.749  1.00 62.63 ? 221 GLU   B CD  1 
ATOM   4436 O OE1 . GLU   B 1 224 ? -48.240 17.085  11.605  1.00 63.05 ? 221 GLU   B OE1 1 
ATOM   4437 O OE2 . GLU   B 1 224 ? -46.628 18.247  12.565  1.00 58.98 ? 221 GLU   B OE2 1 
ATOM   4438 N N   . ALA   B 1 225 ? -47.351 17.426  6.853   1.00 41.51 ? 222 ALA   B N   1 
ATOM   4439 C CA  . ALA   B 1 225 ? -47.853 16.468  5.872   1.00 38.70 ? 222 ALA   B CA  1 
ATOM   4440 C C   . ALA   B 1 225 ? -46.834 15.365  5.590   1.00 37.56 ? 222 ALA   B C   1 
ATOM   4441 O O   . ALA   B 1 225 ? -47.203 14.207  5.355   1.00 37.23 ? 222 ALA   B O   1 
ATOM   4442 C CB  . ALA   B 1 225 ? -48.221 17.193  4.582   1.00 37.67 ? 222 ALA   B CB  1 
ATOM   4443 N N   . LEU   B 1 226 ? -45.541 15.708  5.583   1.00 35.66 ? 223 LEU   B N   1 
ATOM   4444 C CA  . LEU   B 1 226 ? -44.525 14.701  5.293   1.00 40.09 ? 223 LEU   B CA  1 
ATOM   4445 C C   . LEU   B 1 226 ? -44.350 13.744  6.461   1.00 37.55 ? 223 LEU   B C   1 
ATOM   4446 O O   . LEU   B 1 226 ? -44.101 12.548  6.262   1.00 40.52 ? 223 LEU   B O   1 
ATOM   4447 C CB  . LEU   B 1 226 ? -43.198 15.371  4.953   1.00 37.12 ? 223 LEU   B CB  1 
ATOM   4448 C CG  . LEU   B 1 226 ? -43.194 15.927  3.533   1.00 38.01 ? 223 LEU   B CG  1 
ATOM   4449 C CD1 . LEU   B 1 226 ? -42.047 16.908  3.380   1.00 33.14 ? 223 LEU   B CD1 1 
ATOM   4450 C CD2 . LEU   B 1 226 ? -43.069 14.760  2.550   1.00 30.40 ? 223 LEU   B CD2 1 
ATOM   4451 N N   . ARG   B 1 227 ? -44.465 14.249  7.693   1.00 40.63 ? 224 ARG   B N   1 
ATOM   4452 C CA  . ARG   B 1 227 ? -44.385 13.353  8.840   1.00 43.21 ? 224 ARG   B CA  1 
ATOM   4453 C C   . ARG   B 1 227 ? -45.528 12.341  8.843   1.00 41.42 ? 224 ARG   B C   1 
ATOM   4454 O O   . ARG   B 1 227 ? -45.327 11.189  9.243   1.00 43.12 ? 224 ARG   B O   1 
ATOM   4455 C CB  . ARG   B 1 227 ? -44.339 14.163  10.133  1.00 43.99 ? 224 ARG   B CB  1 
ATOM   4456 C CG  . ARG   B 1 227 ? -42.925 14.640  10.446  1.00 49.62 ? 224 ARG   B CG  1 
ATOM   4457 C CD  . ARG   B 1 227 ? -42.800 15.165  11.861  1.00 55.91 ? 224 ARG   B CD  1 
ATOM   4458 N NE  . ARG   B 1 227 ? -43.678 16.309  12.057  1.00 58.72 ? 224 ARG   B NE  1 
ATOM   4459 C CZ  . ARG   B 1 227 ? -43.324 17.567  11.832  1.00 54.39 ? 224 ARG   B CZ  1 
ATOM   4460 N NH1 . ARG   B 1 227 ? -42.091 17.881  11.465  1.00 52.05 ? 224 ARG   B NH1 1 
ATOM   4461 N NH2 . ARG   B 1 227 ? -44.231 18.532  11.971  1.00 51.65 ? 224 ARG   B NH2 1 
ATOM   4462 N N   . GLU   B 1 228 ? -46.721 12.721  8.366   1.00 38.57 ? 225 GLU   B N   1 
ATOM   4463 C CA  . GLU   B 1 228 ? -47.768 11.715  8.215   1.00 36.21 ? 225 GLU   B CA  1 
ATOM   4464 C C   . GLU   B 1 228 ? -47.439 10.745  7.092   1.00 41.18 ? 225 GLU   B C   1 
ATOM   4465 O O   . GLU   B 1 228 ? -47.545 9.523   7.260   1.00 42.67 ? 225 GLU   B O   1 
ATOM   4466 C CB  . GLU   B 1 228 ? -49.130 12.352  7.947   1.00 43.64 ? 225 GLU   B CB  1 
ATOM   4467 C CG  . GLU   B 1 228 ? -50.141 11.270  7.549   1.00 46.38 ? 225 GLU   B CG  1 
ATOM   4468 C CD  . GLU   B 1 228 ? -51.472 11.794  7.052   1.00 54.37 ? 225 GLU   B CD  1 
ATOM   4469 O OE1 . GLU   B 1 228 ? -51.675 13.030  7.030   1.00 55.33 ? 225 GLU   B OE1 1 
ATOM   4470 O OE2 . GLU   B 1 228 ? -52.323 10.950  6.685   1.00 49.09 ? 225 GLU   B OE2 1 
ATOM   4471 N N   . ALA   B 1 229 ? -47.054 11.272  5.926   1.00 36.34 ? 226 ALA   B N   1 
ATOM   4472 C CA  . ALA   B 1 229 ? -46.891 10.428  4.743   1.00 31.58 ? 226 ALA   B CA  1 
ATOM   4473 C C   . ALA   B 1 229 ? -45.606 9.611   4.772   1.00 34.23 ? 226 ALA   B C   1 
ATOM   4474 O O   . ALA   B 1 229 ? -45.528 8.563   4.118   1.00 30.46 ? 226 ALA   B O   1 
ATOM   4475 C CB  . ALA   B 1 229 ? -46.921 11.298  3.486   1.00 35.44 ? 226 ALA   B CB  1 
ATOM   4476 N N   . ALA   B 1 230 ? -44.585 10.070  5.497   1.00 33.98 ? 227 ALA   B N   1 
ATOM   4477 C CA  . ALA   B 1 230 ? -43.290 9.395   5.561   1.00 39.34 ? 227 ALA   B CA  1 
ATOM   4478 C C   . ALA   B 1 230 ? -42.871 9.276   7.020   1.00 37.85 ? 227 ALA   B C   1 
ATOM   4479 O O   . ALA   B 1 230 ? -41.917 9.928   7.466   1.00 36.43 ? 227 ALA   B O   1 
ATOM   4480 C CB  . ALA   B 1 230 ? -42.233 10.138  4.743   1.00 37.41 ? 227 ALA   B CB  1 
ATOM   4481 N N   . PRO   B 1 231 ? -43.559 8.434   7.793   1.00 39.48 ? 228 PRO   B N   1 
ATOM   4482 C CA  . PRO   B 1 231 ? -43.290 8.390   9.241   1.00 40.23 ? 228 PRO   B CA  1 
ATOM   4483 C C   . PRO   B 1 231 ? -41.895 7.881   9.591   1.00 37.86 ? 228 PRO   B C   1 
ATOM   4484 O O   . PRO   B 1 231 ? -41.378 8.227   10.659  1.00 38.15 ? 228 PRO   B O   1 
ATOM   4485 C CB  . PRO   B 1 231 ? -44.383 7.450   9.763   1.00 38.04 ? 228 PRO   B CB  1 
ATOM   4486 C CG  . PRO   B 1 231 ? -44.595 6.497   8.619   1.00 40.37 ? 228 PRO   B CG  1 
ATOM   4487 C CD  . PRO   B 1 231 ? -44.451 7.344   7.360   1.00 38.14 ? 228 PRO   B CD  1 
ATOM   4488 N N   . ASP   B 1 232 ? -41.260 7.089   8.727   1.00 37.92 ? 229 ASP   B N   1 
ATOM   4489 C CA  . ASP   B 1 232 ? -39.931 6.557   8.996   1.00 39.87 ? 229 ASP   B CA  1 
ATOM   4490 C C   . ASP   B 1 232 ? -38.804 7.415   8.406   1.00 36.38 ? 229 ASP   B C   1 
ATOM   4491 O O   . ASP   B 1 232 ? -37.670 6.933   8.302   1.00 35.87 ? 229 ASP   B O   1 
ATOM   4492 C CB  . ASP   B 1 232 ? -39.840 5.119   8.468   1.00 38.12 ? 229 ASP   B CB  1 
ATOM   4493 C CG  . ASP   B 1 232 ? -40.846 4.190   9.146   1.00 46.24 ? 229 ASP   B CG  1 
ATOM   4494 O OD1 . ASP   B 1 232 ? -40.964 4.258   10.390  1.00 42.54 ? 229 ASP   B OD1 1 
ATOM   4495 O OD2 . ASP   B 1 232 ? -41.525 3.412   8.439   1.00 44.82 ? 229 ASP   B OD2 1 
ATOM   4496 N N   . GLY   B 1 233 ? -39.085 8.671   8.043   1.00 37.83 ? 230 GLY   B N   1 
ATOM   4497 C CA  . GLY   B 1 233 ? -38.102 9.521   7.386   1.00 32.14 ? 230 GLY   B CA  1 
ATOM   4498 C C   . GLY   B 1 233 ? -38.079 9.348   5.878   1.00 31.19 ? 230 GLY   B C   1 
ATOM   4499 O O   . GLY   B 1 233 ? -38.856 8.592   5.281   1.00 33.77 ? 230 GLY   B O   1 
ATOM   4500 N N   . VAL   B 1 234 ? -37.139 10.051  5.241   1.00 29.63 ? 231 VAL   B N   1 
ATOM   4501 C CA  . VAL   B 1 234 ? -37.028 10.083  3.786   1.00 28.07 ? 231 VAL   B CA  1 
ATOM   4502 C C   . VAL   B 1 234 ? -35.666 9.536   3.385   1.00 26.16 ? 231 VAL   B C   1 
ATOM   4503 O O   . VAL   B 1 234 ? -34.630 10.101  3.756   1.00 23.57 ? 231 VAL   B O   1 
ATOM   4504 C CB  . VAL   B 1 234 ? -37.224 11.504  3.239   1.00 27.57 ? 231 VAL   B CB  1 
ATOM   4505 C CG1 . VAL   B 1 234 ? -37.033 11.526  1.708   1.00 25.76 ? 231 VAL   B CG1 1 
ATOM   4506 C CG2 . VAL   B 1 234 ? -38.593 12.039  3.662   1.00 23.34 ? 231 VAL   B CG2 1 
ATOM   4507 N N   . ASP   B 1 235 ? -35.675 8.451   2.614   1.00 25.59 ? 232 ASP   B N   1 
ATOM   4508 C CA  . ASP   B 1 235 ? -34.457 7.862   2.075   1.00 27.45 ? 232 ASP   B CA  1 
ATOM   4509 C C   . ASP   B 1 235 ? -34.074 8.442   0.713   1.00 28.94 ? 232 ASP   B C   1 
ATOM   4510 O O   . ASP   B 1 235 ? -32.887 8.660   0.452   1.00 26.03 ? 232 ASP   B O   1 
ATOM   4511 C CB  . ASP   B 1 235 ? -34.623 6.352   1.951   1.00 26.04 ? 232 ASP   B CB  1 
ATOM   4512 C CG  . ASP   B 1 235 ? -34.919 5.709   3.276   1.00 32.09 ? 232 ASP   B CG  1 
ATOM   4513 O OD1 . ASP   B 1 235 ? -34.033 5.772   4.163   1.00 25.97 ? 232 ASP   B OD1 1 
ATOM   4514 O OD2 . ASP   B 1 235 ? -36.052 5.193   3.434   1.00 30.81 ? 232 ASP   B OD2 1 
ATOM   4515 N N   . LYS   B 1 236 ? -35.043 8.672   -0.177  1.00 23.52 ? 233 LYS   B N   1 
ATOM   4516 C CA  . LYS   B 1 236 ? -34.749 9.242   -1.486  1.00 26.69 ? 233 LYS   B CA  1 
ATOM   4517 C C   . LYS   B 1 236 ? -35.688 10.412  -1.747  1.00 26.84 ? 233 LYS   B C   1 
ATOM   4518 O O   . LYS   B 1 236 ? -36.867 10.361  -1.387  1.00 27.59 ? 233 LYS   B O   1 
ATOM   4519 C CB  . LYS   B 1 236 ? -34.883 8.200   -2.623  1.00 28.18 ? 233 LYS   B CB  1 
ATOM   4520 C CG  . LYS   B 1 236 ? -34.327 6.773   -2.324  1.00 35.10 ? 233 LYS   B CG  1 
ATOM   4521 C CD  . LYS   B 1 236 ? -32.819 6.738   -2.219  1.00 34.34 ? 233 LYS   B CD  1 
ATOM   4522 C CE  . LYS   B 1 236 ? -32.232 5.349   -2.521  1.00 34.27 ? 233 LYS   B CE  1 
ATOM   4523 N NZ  . LYS   B 1 236 ? -31.917 4.579   -1.300  1.00 33.88 ? 233 LYS   B NZ  1 
ATOM   4524 N N   . TYR   B 1 237 ? -35.173 11.452  -2.410  1.00 24.57 ? 234 TYR   B N   1 
ATOM   4525 C CA  . TYR   B 1 237 ? -35.984 12.608  -2.783  1.00 24.79 ? 234 TYR   B CA  1 
ATOM   4526 C C   . TYR   B 1 237 ? -35.653 12.985  -4.217  1.00 26.98 ? 234 TYR   B C   1 
ATOM   4527 O O   . TYR   B 1 237 ? -34.498 13.283  -4.532  1.00 22.88 ? 234 TYR   B O   1 
ATOM   4528 C CB  . TYR   B 1 237 ? -35.737 13.776  -1.826  1.00 25.48 ? 234 TYR   B CB  1 
ATOM   4529 C CG  . TYR   B 1 237 ? -36.563 15.033  -2.045  1.00 23.46 ? 234 TYR   B CG  1 
ATOM   4530 C CD1 . TYR   B 1 237 ? -37.833 14.983  -2.616  1.00 28.90 ? 234 TYR   B CD1 1 
ATOM   4531 C CD2 . TYR   B 1 237 ? -36.056 16.281  -1.668  1.00 22.41 ? 234 TYR   B CD2 1 
ATOM   4532 C CE1 . TYR   B 1 237 ? -38.576 16.146  -2.811  1.00 27.27 ? 234 TYR   B CE1 1 
ATOM   4533 C CE2 . TYR   B 1 237 ? -36.778 17.439  -1.865  1.00 25.64 ? 234 TYR   B CE2 1 
ATOM   4534 C CZ  . TYR   B 1 237 ? -38.039 17.371  -2.433  1.00 27.24 ? 234 TYR   B CZ  1 
ATOM   4535 O OH  . TYR   B 1 237 ? -38.749 18.532  -2.612  1.00 26.19 ? 234 TYR   B OH  1 
ATOM   4536 N N   . PHE   B 1 238 ? -36.657 12.921  -5.092  1.00 26.56 ? 235 PHE   B N   1 
ATOM   4537 C CA  . PHE   B 1 238 ? -36.543 13.406  -6.463  1.00 26.48 ? 235 PHE   B CA  1 
ATOM   4538 C C   . PHE   B 1 238 ? -37.255 14.752  -6.523  1.00 27.16 ? 235 PHE   B C   1 
ATOM   4539 O O   . PHE   B 1 238 ? -38.485 14.820  -6.427  1.00 25.55 ? 235 PHE   B O   1 
ATOM   4540 C CB  . PHE   B 1 238 ? -37.136 12.413  -7.457  1.00 23.13 ? 235 PHE   B CB  1 
ATOM   4541 C CG  . PHE   B 1 238 ? -36.894 12.775  -8.887  1.00 23.40 ? 235 PHE   B CG  1 
ATOM   4542 C CD1 . PHE   B 1 238 ? -37.736 13.663  -9.551  1.00 25.41 ? 235 PHE   B CD1 1 
ATOM   4543 C CD2 . PHE   B 1 238 ? -35.836 12.214  -9.586  1.00 25.12 ? 235 PHE   B CD2 1 
ATOM   4544 C CE1 . PHE   B 1 238 ? -37.504 14.003  -10.876 1.00 23.27 ? 235 PHE   B CE1 1 
ATOM   4545 C CE2 . PHE   B 1 238 ? -35.609 12.541  -10.908 1.00 22.05 ? 235 PHE   B CE2 1 
ATOM   4546 C CZ  . PHE   B 1 238 ? -36.446 13.452  -11.550 1.00 21.87 ? 235 PHE   B CZ  1 
ATOM   4547 N N   . ASP   B 1 239 ? -36.480 15.824  -6.669  1.00 26.09 ? 236 ASP   B N   1 
ATOM   4548 C CA  . ASP   B 1 239 ? -36.957 17.176  -6.401  1.00 24.62 ? 236 ASP   B CA  1 
ATOM   4549 C C   . ASP   B 1 239 ? -37.095 17.939  -7.714  1.00 25.48 ? 236 ASP   B C   1 
ATOM   4550 O O   . ASP   B 1 239 ? -36.102 18.140  -8.424  1.00 22.87 ? 236 ASP   B O   1 
ATOM   4551 C CB  . ASP   B 1 239 ? -36.005 17.905  -5.455  1.00 23.40 ? 236 ASP   B CB  1 
ATOM   4552 C CG  . ASP   B 1 239 ? -36.501 19.279  -5.074  1.00 23.56 ? 236 ASP   B CG  1 
ATOM   4553 O OD1 . ASP   B 1 239 ? -37.641 19.627  -5.426  1.00 26.64 ? 236 ASP   B OD1 1 
ATOM   4554 O OD2 . ASP   B 1 239 ? -35.742 20.028  -4.422  1.00 27.25 ? 236 ASP   B OD2 1 
ATOM   4555 N N   . SER   B 1 240 ? -38.319 18.379  -8.021  1.00 24.00 ? 237 SER   B N   1 
ATOM   4556 C CA  . SER   B 1 240 ? -38.549 19.249  -9.161  1.00 24.85 ? 237 SER   B CA  1 
ATOM   4557 C C   . SER   B 1 240 ? -39.056 20.618  -8.764  1.00 23.59 ? 237 SER   B C   1 
ATOM   4558 O O   . SER   B 1 240 ? -39.311 21.446  -9.656  1.00 23.02 ? 237 SER   B O   1 
ATOM   4559 C CB  . SER   B 1 240 ? -39.536 18.610  -10.154 1.00 21.88 ? 237 SER   B CB  1 
ATOM   4560 O OG  . SER   B 1 240 ? -38.924 17.547  -10.885 1.00 24.00 ? 237 SER   B OG  1 
ATOM   4561 N N   . ILE   B 1 241 ? -39.204 20.894  -7.466  1.00 20.11 ? 238 ILE   B N   1 
ATOM   4562 C CA  . ILE   B 1 241 ? -39.922 22.070  -6.994  1.00 19.31 ? 238 ILE   B CA  1 
ATOM   4563 C C   . ILE   B 1 241 ? -39.039 23.007  -6.185  1.00 22.12 ? 238 ILE   B C   1 
ATOM   4564 O O   . ILE   B 1 241 ? -39.110 24.234  -6.350  1.00 24.55 ? 238 ILE   B O   1 
ATOM   4565 C CB  . ILE   B 1 241 ? -41.164 21.650  -6.165  1.00 24.27 ? 238 ILE   B CB  1 
ATOM   4566 C CG1 . ILE   B 1 241 ? -42.083 20.747  -7.005  1.00 28.43 ? 238 ILE   B CG1 1 
ATOM   4567 C CG2 . ILE   B 1 241 ? -41.876 22.867  -5.650  1.00 24.96 ? 238 ILE   B CG2 1 
ATOM   4568 C CD1 . ILE   B 1 241 ? -42.632 21.407  -8.275  1.00 24.55 ? 238 ILE   B CD1 1 
ATOM   4569 N N   . GLY   B 1 242 ? -38.202 22.465  -5.295  1.00 24.15 ? 239 GLY   B N   1 
ATOM   4570 C CA  . GLY   B 1 242 ? -37.442 23.353  -4.429  1.00 21.19 ? 239 GLY   B CA  1 
ATOM   4571 C C   . GLY   B 1 242 ? -38.347 24.040  -3.410  1.00 27.73 ? 239 GLY   B C   1 
ATOM   4572 O O   . GLY   B 1 242 ? -39.426 23.570  -3.077  1.00 26.10 ? 239 GLY   B O   1 
ATOM   4573 N N   . GLY   B 1 243 ? -37.865 25.171  -2.897  1.00 26.41 ? 240 GLY   B N   1 
ATOM   4574 C CA  . GLY   B 1 243 ? -38.695 25.971  -2.016  1.00 25.82 ? 240 GLY   B CA  1 
ATOM   4575 C C   . GLY   B 1 243 ? -39.058 25.254  -0.725  1.00 32.33 ? 240 GLY   B C   1 
ATOM   4576 O O   . GLY   B 1 243 ? -38.264 24.500  -0.149  1.00 27.07 ? 240 GLY   B O   1 
ATOM   4577 N N   . SER   B 1 244 ? -40.288 25.503  -0.254  1.00 29.87 ? 241 SER   B N   1 
ATOM   4578 C CA  . SER   B 1 244 ? -40.681 25.060  1.081   1.00 33.34 ? 241 SER   B CA  1 
ATOM   4579 C C   . SER   B 1 244 ? -40.837 23.542  1.168   1.00 31.47 ? 241 SER   B C   1 
ATOM   4580 O O   . SER   B 1 244 ? -40.595 22.969  2.237   1.00 31.61 ? 241 SER   B O   1 
ATOM   4581 C CB  . SER   B 1 244 ? -41.978 25.763  1.505   1.00 33.74 ? 241 SER   B CB  1 
ATOM   4582 O OG  . SER   B 1 244 ? -42.998 25.512  0.561   1.00 37.96 ? 241 SER   B OG  1 
ATOM   4583 N N   . VAL   B 1 245 ? -41.226 22.861  0.083   1.00 30.44 ? 242 VAL   B N   1 
ATOM   4584 C CA  . VAL   B 1 245 ? -41.312 21.399  0.168   1.00 27.38 ? 242 VAL   B CA  1 
ATOM   4585 C C   . VAL   B 1 245 ? -39.925 20.800  0.385   1.00 31.04 ? 242 VAL   B C   1 
ATOM   4586 O O   . VAL   B 1 245 ? -39.733 19.944  1.256   1.00 28.85 ? 242 VAL   B O   1 
ATOM   4587 C CB  . VAL   B 1 245 ? -42.012 20.796  -1.066  1.00 33.73 ? 242 VAL   B CB  1 
ATOM   4588 C CG1 . VAL   B 1 245 ? -41.251 21.078  -2.395  1.00 29.60 ? 242 VAL   B CG1 1 
ATOM   4589 C CG2 . VAL   B 1 245 ? -42.179 19.298  -0.883  1.00 31.69 ? 242 VAL   B CG2 1 
ATOM   4590 N N   . THR   B 1 246 ? -38.928 21.289  -0.361  1.00 25.55 ? 243 THR   B N   1 
ATOM   4591 C CA  . THR   B 1 246 ? -37.552 20.827  -0.200  1.00 26.22 ? 243 THR   B CA  1 
ATOM   4592 C C   . THR   B 1 246 ? -36.990 21.174  1.180   1.00 28.20 ? 243 THR   B C   1 
ATOM   4593 O O   . THR   B 1 246 ? -36.301 20.353  1.802   1.00 27.72 ? 243 THR   B O   1 
ATOM   4594 C CB  . THR   B 1 246 ? -36.700 21.418  -1.333  1.00 23.07 ? 243 THR   B CB  1 
ATOM   4595 O OG1 . THR   B 1 246 ? -37.118 20.830  -2.570  1.00 24.78 ? 243 THR   B OG1 1 
ATOM   4596 C CG2 . THR   B 1 246 ? -35.202 21.174  -1.126  1.00 23.64 ? 243 THR   B CG2 1 
ATOM   4597 N N   . ASP   B 1 247 ? -37.268 22.383  1.683   1.00 26.18 ? 244 ASP   B N   1 
ATOM   4598 C CA  . ASP   B 1 247 ? -36.856 22.716  3.045   1.00 28.17 ? 244 ASP   B CA  1 
ATOM   4599 C C   . ASP   B 1 247 ? -37.365 21.683  4.051   1.00 31.83 ? 244 ASP   B C   1 
ATOM   4600 O O   . ASP   B 1 247 ? -36.640 21.283  4.973   1.00 28.96 ? 244 ASP   B O   1 
ATOM   4601 C CB  . ASP   B 1 247 ? -37.361 24.113  3.427   1.00 31.88 ? 244 ASP   B CB  1 
ATOM   4602 C CG  . ASP   B 1 247 ? -36.722 25.224  2.588   1.00 35.76 ? 244 ASP   B CG  1 
ATOM   4603 O OD1 . ASP   B 1 247 ? -35.631 24.999  2.018   1.00 30.19 ? 244 ASP   B OD1 1 
ATOM   4604 O OD2 . ASP   B 1 247 ? -37.309 26.328  2.516   1.00 32.98 ? 244 ASP   B OD2 1 
ATOM   4605 N N   . ALA   B 1 248 ? -38.610 21.236  3.884   1.00 27.99 ? 245 ALA   B N   1 
ATOM   4606 C CA  . ALA   B 1 248 ? -39.206 20.294  4.829   1.00 29.45 ? 245 ALA   B CA  1 
ATOM   4607 C C   . ALA   B 1 248 ? -38.610 18.899  4.677   1.00 30.42 ? 245 ALA   B C   1 
ATOM   4608 O O   . ALA   B 1 248 ? -38.337 18.226  5.675   1.00 29.16 ? 245 ALA   B O   1 
ATOM   4609 C CB  . ALA   B 1 248 ? -40.719 20.259  4.639   1.00 29.86 ? 245 ALA   B CB  1 
ATOM   4610 N N   . VAL   B 1 249 ? -38.413 18.442  3.442   1.00 28.34 ? 246 VAL   B N   1 
ATOM   4611 C CA  . VAL   B 1 249 ? -37.808 17.132  3.228   1.00 24.31 ? 246 VAL   B CA  1 
ATOM   4612 C C   . VAL   B 1 249 ? -36.433 17.069  3.885   1.00 28.46 ? 246 VAL   B C   1 
ATOM   4613 O O   . VAL   B 1 249 ? -36.078 16.069  4.527   1.00 27.89 ? 246 VAL   B O   1 
ATOM   4614 C CB  . VAL   B 1 249 ? -37.734 16.805  1.722   1.00 31.26 ? 246 VAL   B CB  1 
ATOM   4615 C CG1 . VAL   B 1 249 ? -36.794 15.647  1.492   1.00 26.97 ? 246 VAL   B CG1 1 
ATOM   4616 C CG2 . VAL   B 1 249 ? -39.128 16.479  1.162   1.00 28.35 ? 246 VAL   B CG2 1 
ATOM   4617 N N   . PHE   B 1 250 ? -35.653 18.143  3.769   1.00 26.30 ? 247 PHE   B N   1 
ATOM   4618 C CA  . PHE   B 1 250 ? -34.318 18.161  4.351   1.00 27.77 ? 247 PHE   B CA  1 
ATOM   4619 C C   . PHE   B 1 250 ? -34.346 18.123  5.877   1.00 32.68 ? 247 PHE   B C   1 
ATOM   4620 O O   . PHE   B 1 250 ? -33.326 17.805  6.495   1.00 31.39 ? 247 PHE   B O   1 
ATOM   4621 C CB  . PHE   B 1 250 ? -33.546 19.390  3.857   1.00 27.74 ? 247 PHE   B CB  1 
ATOM   4622 C CG  . PHE   B 1 250 ? -32.814 19.166  2.542   1.00 29.26 ? 247 PHE   B CG  1 
ATOM   4623 C CD1 . PHE   B 1 250 ? -33.504 18.820  1.393   1.00 25.28 ? 247 PHE   B CD1 1 
ATOM   4624 C CD2 . PHE   B 1 250 ? -31.433 19.285  2.475   1.00 28.83 ? 247 PHE   B CD2 1 
ATOM   4625 C CE1 . PHE   B 1 250 ? -32.830 18.604  0.188   1.00 27.56 ? 247 PHE   B CE1 1 
ATOM   4626 C CE2 . PHE   B 1 250 ? -30.751 19.084  1.270   1.00 26.21 ? 247 PHE   B CE2 1 
ATOM   4627 C CZ  . PHE   B 1 250 ? -31.453 18.744  0.128   1.00 25.48 ? 247 PHE   B CZ  1 
ATOM   4628 N N   . SER   B 1 251 ? -35.479 18.434  6.508   1.00 29.94 ? 248 SER   B N   1 
ATOM   4629 C CA  . SER   B 1 251 ? -35.552 18.292  7.962   1.00 31.83 ? 248 SER   B CA  1 
ATOM   4630 C C   . SER   B 1 251 ? -35.692 16.839  8.401   1.00 30.11 ? 248 SER   B C   1 
ATOM   4631 O O   . SER   B 1 251 ? -35.641 16.564  9.602   1.00 33.73 ? 248 SER   B O   1 
ATOM   4632 C CB  . SER   B 1 251 ? -36.730 19.101  8.523   1.00 29.17 ? 248 SER   B CB  1 
ATOM   4633 O OG  . SER   B 1 251 ? -37.964 18.460  8.207   1.00 30.51 ? 248 SER   B OG  1 
ATOM   4634 N N   . MET   B 1 252 ? -35.874 15.902  7.466   1.00 26.73 ? 249 MET   B N   1 
ATOM   4635 C CA  . MET   B 1 252 ? -36.187 14.532  7.842   1.00 29.63 ? 249 MET   B CA  1 
ATOM   4636 C C   . MET   B 1 252 ? -35.459 13.531  6.963   1.00 30.67 ? 249 MET   B C   1 
ATOM   4637 O O   . MET   B 1 252 ? -35.961 12.424  6.723   1.00 28.29 ? 249 MET   B O   1 
ATOM   4638 C CB  . MET   B 1 252 ? -37.702 14.285  7.784   1.00 35.08 ? 249 MET   B CB  1 
ATOM   4639 C CG  . MET   B 1 252 ? -38.312 14.601  6.428   1.00 32.90 ? 249 MET   B CG  1 
ATOM   4640 S SD  . MET   B 1 252 ? -40.118 14.501  6.382   1.00 40.55 ? 249 MET   B SD  1 
ATOM   4641 C CE  . MET   B 1 252 ? -40.578 15.773  7.539   1.00 29.65 ? 249 MET   B CE  1 
ATOM   4642 N N   . LEU   B 1 253 ? -34.273 13.897  6.480   1.00 32.45 ? 250 LEU   B N   1 
ATOM   4643 C CA  . LEU   B 1 253 ? -33.464 12.979  5.688   1.00 26.52 ? 250 LEU   B CA  1 
ATOM   4644 C C   . LEU   B 1 253 ? -32.873 11.889  6.572   1.00 28.72 ? 250 LEU   B C   1 
ATOM   4645 O O   . LEU   B 1 253 ? -32.321 12.177  7.639   1.00 28.00 ? 250 LEU   B O   1 
ATOM   4646 C CB  . LEU   B 1 253 ? -32.345 13.738  4.978   1.00 27.15 ? 250 LEU   B CB  1 
ATOM   4647 C CG  . LEU   B 1 253 ? -32.826 14.709  3.910   1.00 27.90 ? 250 LEU   B CG  1 
ATOM   4648 C CD1 . LEU   B 1 253 ? -31.663 15.523  3.415   1.00 28.17 ? 250 LEU   B CD1 1 
ATOM   4649 C CD2 . LEU   B 1 253 ? -33.437 13.903  2.773   1.00 28.80 ? 250 LEU   B CD2 1 
ATOM   4650 N N   . ASN   B 1 254 ? -32.980 10.647  6.115   1.00 28.39 ? 251 ASN   B N   1 
ATOM   4651 C CA  . ASN   B 1 254 ? -32.405 9.505   6.803   1.00 28.24 ? 251 ASN   B CA  1 
ATOM   4652 C C   . ASN   B 1 254 ? -30.925 9.368   6.456   1.00 30.56 ? 251 ASN   B C   1 
ATOM   4653 O O   . ASN   B 1 254 ? -30.418 9.976   5.507   1.00 24.18 ? 251 ASN   B O   1 
ATOM   4654 C CB  . ASN   B 1 254 ? -33.157 8.219   6.438   1.00 26.29 ? 251 ASN   B CB  1 
ATOM   4655 C CG  . ASN   B 1 254 ? -34.555 8.155   7.067   1.00 31.53 ? 251 ASN   B CG  1 
ATOM   4656 O OD1 . ASN   B 1 254 ? -34.883 8.942   7.947   1.00 31.37 ? 251 ASN   B OD1 1 
ATOM   4657 N ND2 . ASN   B 1 254 ? -35.375 7.215   6.605   1.00 29.36 ? 251 ASN   B ND2 1 
ATOM   4658 N N   . VAL   B 1 255 ? -30.228 8.554   7.258   1.00 27.64 ? 252 VAL   B N   1 
ATOM   4659 C CA  . VAL   B 1 255 ? -28.818 8.269   7.013   1.00 25.22 ? 252 VAL   B CA  1 
ATOM   4660 C C   . VAL   B 1 255 ? -28.662 7.626   5.651   1.00 25.19 ? 252 VAL   B C   1 
ATOM   4661 O O   . VAL   B 1 255 ? -29.414 6.714   5.293   1.00 28.10 ? 252 VAL   B O   1 
ATOM   4662 C CB  . VAL   B 1 255 ? -28.257 7.364   8.128   1.00 26.33 ? 252 VAL   B CB  1 
ATOM   4663 C CG1 . VAL   B 1 255 ? -26.858 6.832   7.752   1.00 27.18 ? 252 VAL   B CG1 1 
ATOM   4664 C CG2 . VAL   B 1 255 ? -28.214 8.122   9.458   1.00 26.55 ? 252 VAL   B CG2 1 
ATOM   4665 N N   . GLY   B 1 256 ? -27.681 8.096   4.878   1.00 23.42 ? 253 GLY   B N   1 
ATOM   4666 C CA  . GLY   B 1 256 ? -27.415 7.529   3.564   1.00 24.26 ? 253 GLY   B CA  1 
ATOM   4667 C C   . GLY   B 1 256 ? -28.393 7.934   2.475   1.00 25.02 ? 253 GLY   B C   1 
ATOM   4668 O O   . GLY   B 1 256 ? -28.369 7.351   1.380   1.00 22.10 ? 253 GLY   B O   1 
ATOM   4669 N N   . SER   B 1 257 ? -29.245 8.917   2.736   1.00 24.49 ? 254 SER   B N   1 
ATOM   4670 C CA  . SER   B 1 257 ? -30.267 9.310   1.779   1.00 24.86 ? 254 SER   B CA  1 
ATOM   4671 C C   . SER   B 1 257 ? -29.638 9.884   0.506   1.00 27.47 ? 254 SER   B C   1 
ATOM   4672 O O   . SER   B 1 257 ? -28.482 10.312  0.487   1.00 24.37 ? 254 SER   B O   1 
ATOM   4673 C CB  . SER   B 1 257 ? -31.213 10.316  2.430   1.00 23.35 ? 254 SER   B CB  1 
ATOM   4674 O OG  . SER   B 1 257 ? -30.492 11.314  3.119   1.00 23.53 ? 254 SER   B OG  1 
ATOM   4675 N N   . GLN   B 1 258 ? -30.424 9.882   -0.581  1.00 24.20 ? 255 GLN   B N   1 
ATOM   4676 C CA  . GLN   B 1 258 ? -30.027 10.507  -1.838  1.00 24.52 ? 255 GLN   B CA  1 
ATOM   4677 C C   . GLN   B 1 258 ? -31.097 11.480  -2.323  1.00 28.75 ? 255 GLN   B C   1 
ATOM   4678 O O   . GLN   B 1 258 ? -32.288 11.159  -2.305  1.00 25.72 ? 255 GLN   B O   1 
ATOM   4679 C CB  . GLN   B 1 258 ? -29.780 9.470   -2.930  1.00 25.75 ? 255 GLN   B CB  1 
ATOM   4680 C CG  . GLN   B 1 258 ? -28.707 8.452   -2.620  1.00 24.63 ? 255 GLN   B CG  1 
ATOM   4681 C CD  . GLN   B 1 258 ? -28.677 7.344   -3.643  1.00 30.91 ? 255 GLN   B CD  1 
ATOM   4682 O OE1 . GLN   B 1 258 ? -29.601 6.532   -3.720  1.00 29.57 ? 255 GLN   B OE1 1 
ATOM   4683 N NE2 . GLN   B 1 258 ? -27.621 7.315   -4.450  1.00 31.04 ? 255 GLN   B NE2 1 
ATOM   4684 N N   . VAL   B 1 259 ? -30.648 12.638  -2.824  1.00 22.91 ? 256 VAL   B N   1 
ATOM   4685 C CA  . VAL   B 1 259 ? -31.509 13.699  -3.345  1.00 21.80 ? 256 VAL   B CA  1 
ATOM   4686 C C   . VAL   B 1 259 ? -31.082 13.996  -4.787  1.00 25.49 ? 256 VAL   B C   1 
ATOM   4687 O O   . VAL   B 1 259 ? -29.919 14.339  -5.043  1.00 22.46 ? 256 VAL   B O   1 
ATOM   4688 C CB  . VAL   B 1 259 ? -31.427 14.959  -2.465  1.00 23.65 ? 256 VAL   B CB  1 
ATOM   4689 C CG1 . VAL   B 1 259 ? -32.323 16.083  -3.009  1.00 23.13 ? 256 VAL   B CG1 1 
ATOM   4690 C CG2 . VAL   B 1 259 ? -31.808 14.624  -1.021  1.00 24.18 ? 256 VAL   B CG2 1 
ATOM   4691 N N   . ALA   B 1 260 ? -32.008 13.850  -5.731  1.00 23.70 ? 257 ALA   B N   1 
ATOM   4692 C CA  . ALA   B 1 260 ? -31.769 14.253  -7.111  1.00 22.76 ? 257 ALA   B CA  1 
ATOM   4693 C C   . ALA   B 1 260 ? -32.503 15.563  -7.374  1.00 24.57 ? 257 ALA   B C   1 
ATOM   4694 O O   . ALA   B 1 260 ? -33.707 15.671  -7.113  1.00 23.39 ? 257 ALA   B O   1 
ATOM   4695 C CB  . ALA   B 1 260 ? -32.218 13.175  -8.094  1.00 21.31 ? 257 ALA   B CB  1 
ATOM   4696 N N   . VAL   B 1 261 ? -31.773 16.559  -7.866  1.00 21.83 ? 258 VAL   B N   1 
ATOM   4697 C CA  . VAL   B 1 261 ? -32.328 17.883  -8.115  1.00 25.59 ? 258 VAL   B CA  1 
ATOM   4698 C C   . VAL   B 1 261 ? -32.578 17.976  -9.615  1.00 25.24 ? 258 VAL   B C   1 
ATOM   4699 O O   . VAL   B 1 261 ? -31.657 18.205  -10.411 1.00 22.69 ? 258 VAL   B O   1 
ATOM   4700 C CB  . VAL   B 1 261 ? -31.410 18.998  -7.598  1.00 24.58 ? 258 VAL   B CB  1 
ATOM   4701 C CG1 . VAL   B 1 261 ? -31.992 20.382  -7.918  1.00 22.99 ? 258 VAL   B CG1 1 
ATOM   4702 C CG2 . VAL   B 1 261 ? -31.205 18.841  -6.099  1.00 21.18 ? 258 VAL   B CG2 1 
ATOM   4703 N N   . CYS   B 1 262 ? -33.842 17.788  -9.993  1.00 24.25 ? 259 CYS   B N   1 
ATOM   4704 C CA  . CYS   B 1 262 ? -34.281 17.812  -11.382 1.00 23.05 ? 259 CYS   B CA  1 
ATOM   4705 C C   . CYS   B 1 262 ? -34.725 19.202  -11.836 1.00 22.93 ? 259 CYS   B C   1 
ATOM   4706 O O   . CYS   B 1 262 ? -34.536 19.559  -13.007 1.00 22.86 ? 259 CYS   B O   1 
ATOM   4707 C CB  . CYS   B 1 262 ? -35.420 16.795  -11.567 1.00 24.34 ? 259 CYS   B CB  1 
ATOM   4708 S SG  . CYS   B 1 262 ? -36.035 16.638  -13.249 1.00 27.23 ? 259 CYS   B SG  1 
ATOM   4709 N N   . TRP   B 1 263 ? -35.301 19.999  -10.942 1.00 22.14 ? 260 TRP   B N   1 
ATOM   4710 C CA  . TRP   B 1 263 ? -35.714 21.367  -11.252 1.00 25.22 ? 260 TRP   B CA  1 
ATOM   4711 C C   . TRP   B 1 263 ? -35.996 22.061  -9.931  1.00 22.01 ? 260 TRP   B C   1 
ATOM   4712 O O   . TRP   B 1 263 ? -36.039 21.423  -8.878  1.00 24.15 ? 260 TRP   B O   1 
ATOM   4713 C CB  . TRP   B 1 263 ? -36.948 21.417  -12.176 1.00 23.59 ? 260 TRP   B CB  1 
ATOM   4714 C CG  . TRP   B 1 263 ? -36.846 22.545  -13.213 1.00 23.20 ? 260 TRP   B CG  1 
ATOM   4715 C CD1 . TRP   B 1 263 ? -35.824 22.750  -14.110 1.00 24.81 ? 260 TRP   B CD1 1 
ATOM   4716 C CD2 . TRP   B 1 263 ? -37.793 23.598  -13.444 1.00 22.98 ? 260 TRP   B CD2 1 
ATOM   4717 N NE1 . TRP   B 1 263 ? -36.080 23.861  -14.873 1.00 21.85 ? 260 TRP   B NE1 1 
ATOM   4718 C CE2 . TRP   B 1 263 ? -37.280 24.399  -14.496 1.00 24.76 ? 260 TRP   B CE2 1 
ATOM   4719 C CE3 . TRP   B 1 263 ? -39.033 23.939  -12.876 1.00 25.57 ? 260 TRP   B CE3 1 
ATOM   4720 C CZ2 . TRP   B 1 263 ? -37.952 25.525  -14.979 1.00 21.72 ? 260 TRP   B CZ2 1 
ATOM   4721 C CZ3 . TRP   B 1 263 ? -39.700 25.058  -13.359 1.00 26.92 ? 260 TRP   B CZ3 1 
ATOM   4722 C CH2 . TRP   B 1 263 ? -39.162 25.834  -14.406 1.00 24.20 ? 260 TRP   B CH2 1 
ATOM   4723 N N   . GLN   B 1 264 ? -36.184 23.388  -9.992  1.00 19.84 ? 261 GLN   B N   1 
ATOM   4724 C CA  . GLN   B 1 264 ? -36.491 24.190  -8.811  1.00 23.26 ? 261 GLN   B CA  1 
ATOM   4725 C C   . GLN   B 1 264 ? -37.594 25.209  -9.144  1.00 25.61 ? 261 GLN   B C   1 
ATOM   4726 O O   . GLN   B 1 264 ? -37.385 26.422  -9.165  1.00 22.37 ? 261 GLN   B O   1 
ATOM   4727 C CB  . GLN   B 1 264 ? -35.240 24.884  -8.288  1.00 23.44 ? 261 GLN   B CB  1 
ATOM   4728 C CG  . GLN   B 1 264 ? -34.183 23.890  -7.807  1.00 23.59 ? 261 GLN   B CG  1 
ATOM   4729 C CD  . GLN   B 1 264 ? -34.509 23.357  -6.428  1.00 22.53 ? 261 GLN   B CD  1 
ATOM   4730 O OE1 . GLN   B 1 264 ? -34.246 24.023  -5.430  1.00 24.87 ? 261 GLN   B OE1 1 
ATOM   4731 N NE2 . GLN   B 1 264 ? -35.108 22.172  -6.369  1.00 19.83 ? 261 GLN   B NE2 1 
ATOM   4732 N N   . TRP   B 1 265 ? -38.807 24.695  -9.358  1.00 24.01 ? 262 TRP   B N   1 
ATOM   4733 C CA  . TRP   B 1 265 ? -39.936 25.533  -9.759  1.00 25.49 ? 262 TRP   B CA  1 
ATOM   4734 C C   . TRP   B 1 265 ? -40.121 26.725  -8.825  1.00 26.70 ? 262 TRP   B C   1 
ATOM   4735 O O   . TRP   B 1 265 ? -40.331 27.856  -9.279  1.00 24.49 ? 262 TRP   B O   1 
ATOM   4736 C CB  . TRP   B 1 265 ? -41.196 24.668  -9.805  1.00 22.60 ? 262 TRP   B CB  1 
ATOM   4737 C CG  . TRP   B 1 265 ? -42.449 25.365  -10.233 1.00 26.74 ? 262 TRP   B CG  1 
ATOM   4738 C CD1 . TRP   B 1 265 ? -43.098 26.372  -9.579  1.00 26.38 ? 262 TRP   B CD1 1 
ATOM   4739 C CD2 . TRP   B 1 265 ? -43.233 25.065  -11.390 1.00 24.16 ? 262 TRP   B CD2 1 
ATOM   4740 N NE1 . TRP   B 1 265 ? -44.227 26.734  -10.275 1.00 25.52 ? 262 TRP   B NE1 1 
ATOM   4741 C CE2 . TRP   B 1 265 ? -44.341 25.933  -11.380 1.00 24.49 ? 262 TRP   B CE2 1 
ATOM   4742 C CE3 . TRP   B 1 265 ? -43.113 24.134  -12.429 1.00 23.99 ? 262 TRP   B CE3 1 
ATOM   4743 C CZ2 . TRP   B 1 265 ? -45.316 25.915  -12.380 1.00 24.22 ? 262 TRP   B CZ2 1 
ATOM   4744 C CZ3 . TRP   B 1 265 ? -44.089 24.114  -13.418 1.00 27.39 ? 262 TRP   B CZ3 1 
ATOM   4745 C CH2 . TRP   B 1 265 ? -45.164 25.006  -13.392 1.00 27.50 ? 262 TRP   B CH2 1 
ATOM   4746 N N   . ALA   B 1 266 ? -40.057 26.484  -7.508  1.00 23.57 ? 263 ALA   B N   1 
ATOM   4747 C CA  . ALA   B 1 266 ? -40.223 27.552  -6.528  1.00 23.73 ? 263 ALA   B CA  1 
ATOM   4748 C C   . ALA   B 1 266 ? -39.271 28.718  -6.776  1.00 24.53 ? 263 ALA   B C   1 
ATOM   4749 O O   . ALA   B 1 266 ? -39.627 29.880  -6.573  1.00 25.84 ? 263 ALA   B O   1 
ATOM   4750 C CB  . ALA   B 1 266 ? -40.005 26.990  -5.118  1.00 27.05 ? 263 ALA   B CB  1 
ATOM   4751 N N   . THR   B 1 267 ? -38.041 28.429  -7.192  1.00 22.04 ? 264 THR   B N   1 
ATOM   4752 C CA  . THR   B 1 267 ? -37.109 29.519  -7.465  1.00 25.35 ? 264 THR   B CA  1 
ATOM   4753 C C   . THR   B 1 267 ? -37.277 30.069  -8.880  1.00 26.03 ? 264 THR   B C   1 
ATOM   4754 O O   . THR   B 1 267 ? -37.433 31.279  -9.061  1.00 25.39 ? 264 THR   B O   1 
ATOM   4755 C CB  . THR   B 1 267 ? -35.664 29.050  -7.253  1.00 24.87 ? 264 THR   B CB  1 
ATOM   4756 O OG1 . THR   B 1 267 ? -35.489 28.677  -5.871  1.00 27.71 ? 264 THR   B OG1 1 
ATOM   4757 C CG2 . THR   B 1 267 ? -34.673 30.185  -7.625  1.00 23.97 ? 264 THR   B CG2 1 
ATOM   4758 N N   . GLN   B 1 268 ? -37.216 29.237  -9.896  1.00 24.70 ? 265 GLN   B N   1 
ATOM   4759 C CA  . GLN   B 1 268 ? -37.280 29.716  -11.266 1.00 26.88 ? 265 GLN   B CA  1 
ATOM   4760 C C   . GLN   B 1 268 ? -38.602 30.394  -11.624 1.00 28.54 ? 265 GLN   B C   1 
ATOM   4761 O O   . GLN   B 1 268 ? -38.602 31.452  -12.221 1.00 27.18 ? 265 GLN   B O   1 
ATOM   4762 C CB  . GLN   B 1 268 ? -36.989 28.591  -12.261 1.00 25.35 ? 265 GLN   B CB  1 
ATOM   4763 C CG  . GLN   B 1 268 ? -36.988 29.038  -13.710 1.00 29.39 ? 265 GLN   B CG  1 
ATOM   4764 C CD  . GLN   B 1 268 ? -35.869 30.018  -14.007 1.00 35.21 ? 265 GLN   B CD  1 
ATOM   4765 O OE1 . GLN   B 1 268 ? -34.845 30.015  -13.339 1.00 31.33 ? 265 GLN   B OE1 1 
ATOM   4766 N NE2 . GLN   B 1 268 ? -36.060 30.855  -15.010 1.00 29.19 ? 265 GLN   B NE2 1 
ATOM   4767 N N   . VAL   B 1 269 ? -39.706 29.773  -11.262 1.00 24.07 ? 266 VAL   B N   1 
ATOM   4768 C CA  . VAL   B 1 269 ? -41.013 30.332  -11.625 1.00 24.52 ? 266 VAL   B CA  1 
ATOM   4769 C C   . VAL   B 1 269 ? -41.544 31.271  -10.545 1.00 28.84 ? 266 VAL   B C   1 
ATOM   4770 O O   . VAL   B 1 269 ? -41.962 32.396  -10.839 1.00 28.51 ? 266 VAL   B O   1 
ATOM   4771 C CB  . VAL   B 1 269 ? -42.020 29.198  -11.929 1.00 26.28 ? 266 VAL   B CB  1 
ATOM   4772 C CG1 . VAL   B 1 269 ? -43.444 29.768  -12.166 1.00 28.47 ? 266 VAL   B CG1 1 
ATOM   4773 C CG2 . VAL   B 1 269 ? -41.563 28.391  -13.128 1.00 27.43 ? 266 VAL   B CG2 1 
ATOM   4774 N N   . GLN   B 1 270 ? -41.544 30.845  -9.279  1.00 27.32 ? 267 GLN   B N   1 
ATOM   4775 C CA  . GLN   B 1 270 ? -42.150 31.659  -8.230  1.00 26.14 ? 267 GLN   B CA  1 
ATOM   4776 C C   . GLN   B 1 270 ? -41.178 32.658  -7.625  1.00 28.84 ? 267 GLN   B C   1 
ATOM   4777 O O   . GLN   B 1 270 ? -41.575 33.430  -6.746  1.00 26.61 ? 267 GLN   B O   1 
ATOM   4778 C CB  . GLN   B 1 270 ? -42.738 30.761  -7.133  1.00 27.79 ? 267 GLN   B CB  1 
ATOM   4779 C CG  . GLN   B 1 270 ? -43.808 29.808  -7.638  1.00 28.59 ? 267 GLN   B CG  1 
ATOM   4780 C CD  . GLN   B 1 270 ? -44.342 28.900  -6.539  1.00 37.40 ? 267 GLN   B CD  1 
ATOM   4781 O OE1 . GLN   B 1 270 ? -43.670 27.958  -6.100  1.00 33.75 ? 267 GLN   B OE1 1 
ATOM   4782 N NE2 . GLN   B 1 270 ? -45.553 29.184  -6.081  1.00 35.86 ? 267 GLN   B NE2 1 
ATOM   4783 N N   . ARG   B 1 271 ? -39.915 32.652  -8.067  1.00 25.21 ? 268 ARG   B N   1 
ATOM   4784 C CA  . ARG   B 1 271 ? -38.928 33.662  -7.683  1.00 28.30 ? 268 ARG   B CA  1 
ATOM   4785 C C   . ARG   B 1 271 ? -38.671 33.657  -6.179  1.00 30.36 ? 268 ARG   B C   1 
ATOM   4786 O O   . ARG   B 1 271 ? -38.344 34.686  -5.576  1.00 28.15 ? 268 ARG   B O   1 
ATOM   4787 C CB  . ARG   B 1 271 ? -39.358 35.044  -8.180  1.00 30.77 ? 268 ARG   B CB  1 
ATOM   4788 C CG  . ARG   B 1 271 ? -39.743 34.990  -9.684  1.00 38.06 ? 268 ARG   B CG  1 
ATOM   4789 C CD  . ARG   B 1 271 ? -40.026 36.360  -10.269 1.00 35.53 ? 268 ARG   B CD  1 
ATOM   4790 N NE  . ARG   B 1 271 ? -38.803 37.147  -10.294 1.00 41.09 ? 268 ARG   B NE  1 
ATOM   4791 C CZ  . ARG   B 1 271 ? -38.739 38.410  -10.690 1.00 50.04 ? 268 ARG   B CZ  1 
ATOM   4792 N NH1 . ARG   B 1 271 ? -39.823 39.069  -11.070 1.00 40.00 ? 268 ARG   B NH1 1 
ATOM   4793 N NH2 . ARG   B 1 271 ? -37.558 39.027  -10.702 1.00 48.97 ? 268 ARG   B NH2 1 
ATOM   4794 N N   . ASP   B 1 272 ? -38.788 32.480  -5.579  1.00 26.51 ? 269 ASP   B N   1 
ATOM   4795 C CA  . ASP   B 1 272 ? -38.429 32.253  -4.179  1.00 32.07 ? 269 ASP   B CA  1 
ATOM   4796 C C   . ASP   B 1 272 ? -36.921 32.013  -4.124  1.00 28.94 ? 269 ASP   B C   1 
ATOM   4797 O O   . ASP   B 1 272 ? -36.444 30.879  -4.219  1.00 31.07 ? 269 ASP   B O   1 
ATOM   4798 C CB  . ASP   B 1 272 ? -39.214 31.064  -3.631  1.00 32.28 ? 269 ASP   B CB  1 
ATOM   4799 C CG  . ASP   B 1 272 ? -39.157 30.967  -2.118  1.00 41.86 ? 269 ASP   B CG  1 
ATOM   4800 O OD1 . ASP   B 1 272 ? -38.181 31.466  -1.523  1.00 40.05 ? 269 ASP   B OD1 1 
ATOM   4801 O OD2 . ASP   B 1 272 ? -40.108 30.390  -1.528  1.00 43.01 ? 269 ASP   B OD2 1 
ATOM   4802 N N   . TYR   B 1 273 ? -36.154 33.093  -3.980  1.00 25.99 ? 270 TYR   B N   1 
ATOM   4803 C CA  . TYR   B 1 273 ? -34.705 33.010  -4.125  1.00 32.64 ? 270 TYR   B CA  1 
ATOM   4804 C C   . TYR   B 1 273 ? -33.971 32.776  -2.814  1.00 34.68 ? 270 TYR   B C   1 
ATOM   4805 O O   . TYR   B 1 273 ? -32.796 32.393  -2.846  1.00 32.06 ? 270 TYR   B O   1 
ATOM   4806 C CB  . TYR   B 1 273 ? -34.144 34.294  -4.757  1.00 32.32 ? 270 TYR   B CB  1 
ATOM   4807 C CG  . TYR   B 1 273 ? -34.682 34.605  -6.137  1.00 35.39 ? 270 TYR   B CG  1 
ATOM   4808 C CD1 . TYR   B 1 273 ? -34.408 33.779  -7.214  1.00 34.55 ? 270 TYR   B CD1 1 
ATOM   4809 C CD2 . TYR   B 1 273 ? -35.447 35.746  -6.364  1.00 37.54 ? 270 TYR   B CD2 1 
ATOM   4810 C CE1 . TYR   B 1 273 ? -34.893 34.065  -8.484  1.00 38.10 ? 270 TYR   B CE1 1 
ATOM   4811 C CE2 . TYR   B 1 273 ? -35.937 36.043  -7.627  1.00 35.61 ? 270 TYR   B CE2 1 
ATOM   4812 C CZ  . TYR   B 1 273 ? -35.657 35.200  -8.682  1.00 42.19 ? 270 TYR   B CZ  1 
ATOM   4813 O OH  . TYR   B 1 273 ? -36.144 35.493  -9.939  1.00 45.30 ? 270 TYR   B OH  1 
ATOM   4814 N N   . HIS   B 1 274 ? -34.622 33.009  -1.674  1.00 30.34 ? 271 HIS   B N   1 
ATOM   4815 C CA  . HIS   B 1 274 ? -33.971 32.964  -0.373  1.00 33.81 ? 271 HIS   B CA  1 
ATOM   4816 C C   . HIS   B 1 274 ? -34.744 32.055  0.566   1.00 32.56 ? 271 HIS   B C   1 
ATOM   4817 O O   . HIS   B 1 274 ? -35.959 31.891  0.434   1.00 34.46 ? 271 HIS   B O   1 
ATOM   4818 C CB  . HIS   B 1 274 ? -33.848 34.362  0.240   1.00 40.16 ? 271 HIS   B CB  1 
ATOM   4819 C CG  . HIS   B 1 274 ? -32.657 35.117  -0.251  1.00 40.83 ? 271 HIS   B CG  1 
ATOM   4820 N ND1 . HIS   B 1 274 ? -31.516 35.275  0.508   1.00 46.26 ? 271 HIS   B ND1 1 
ATOM   4821 C CD2 . HIS   B 1 274 ? -32.407 35.719  -1.439  1.00 42.06 ? 271 HIS   B CD2 1 
ATOM   4822 C CE1 . HIS   B 1 274 ? -30.620 35.957  -0.185  1.00 42.01 ? 271 HIS   B CE1 1 
ATOM   4823 N NE2 . HIS   B 1 274 ? -31.134 36.236  -1.371  1.00 48.35 ? 271 HIS   B NE2 1 
ATOM   4824 N N   . GLY   B 1 275 ? -34.019 31.453  1.507   1.00 29.52 ? 272 GLY   B N   1 
ATOM   4825 C CA  . GLY   B 1 275 ? -34.602 30.518  2.435   1.00 31.47 ? 272 GLY   B CA  1 
ATOM   4826 C C   . GLY   B 1 275 ? -33.578 29.942  3.394   1.00 30.99 ? 272 GLY   B C   1 
ATOM   4827 O O   . GLY   B 1 275 ? -32.406 30.340  3.419   1.00 30.47 ? 272 GLY   B O   1 
ATOM   4828 N N   . PRO   B 1 276 ? -34.012 28.999  4.220   1.00 34.85 ? 273 PRO   B N   1 
ATOM   4829 C CA  . PRO   B 1 276 ? -33.087 28.392  5.187   1.00 32.71 ? 273 PRO   B CA  1 
ATOM   4830 C C   . PRO   B 1 276 ? -31.938 27.707  4.464   1.00 30.73 ? 273 PRO   B C   1 
ATOM   4831 O O   . PRO   B 1 276 ? -32.131 27.065  3.431   1.00 31.06 ? 273 PRO   B O   1 
ATOM   4832 C CB  . PRO   B 1 276 ? -33.965 27.385  5.938   1.00 31.32 ? 273 PRO   B CB  1 
ATOM   4833 C CG  . PRO   B 1 276 ? -35.106 27.102  5.019   1.00 34.25 ? 273 PRO   B CG  1 
ATOM   4834 C CD  . PRO   B 1 276 ? -35.327 28.338  4.195   1.00 30.29 ? 273 PRO   B CD  1 
ATOM   4835 N N   . ARG   B 1 277 ? -30.728 27.874  4.996   1.00 28.34 ? 274 ARG   B N   1 
ATOM   4836 C CA  . ARG   B 1 277 ? -29.586 27.147  4.456   1.00 29.81 ? 274 ARG   B CA  1 
ATOM   4837 C C   . ARG   B 1 277 ? -29.755 25.663  4.750   1.00 32.44 ? 274 ARG   B C   1 
ATOM   4838 O O   . ARG   B 1 277 ? -30.019 25.270  5.893   1.00 28.35 ? 274 ARG   B O   1 
ATOM   4839 C CB  . ARG   B 1 277 ? -28.280 27.672  5.053   1.00 31.11 ? 274 ARG   B CB  1 
ATOM   4840 C CG  . ARG   B 1 277 ? -28.156 29.205  5.017   1.00 34.79 ? 274 ARG   B CG  1 
ATOM   4841 C CD  . ARG   B 1 277 ? -26.753 29.616  5.389   1.00 36.12 ? 274 ARG   B CD  1 
ATOM   4842 N NE  . ARG   B 1 277 ? -26.478 31.038  5.214   1.00 39.81 ? 274 ARG   B NE  1 
ATOM   4843 C CZ  . ARG   B 1 277 ? -26.087 31.594  4.074   1.00 34.56 ? 274 ARG   B CZ  1 
ATOM   4844 N NH1 . ARG   B 1 277 ? -26.095 30.919  2.942   1.00 34.68 ? 274 ARG   B NH1 1 
ATOM   4845 N NH2 . ARG   B 1 277 ? -25.668 32.857  4.076   1.00 33.61 ? 274 ARG   B NH2 1 
ATOM   4846 N N   . LEU   B 1 278 ? -29.611 24.844  3.707   1.00 25.86 ? 275 LEU   B N   1 
ATOM   4847 C CA  . LEU   B 1 278 ? -29.886 23.416  3.778   1.00 26.77 ? 275 LEU   B CA  1 
ATOM   4848 C C   . LEU   B 1 278 ? -28.652 22.566  4.095   1.00 30.04 ? 275 LEU   B C   1 
ATOM   4849 O O   . LEU   B 1 278 ? -28.804 21.497  4.704   1.00 28.05 ? 275 LEU   B O   1 
ATOM   4850 C CB  . LEU   B 1 278 ? -30.493 22.935  2.455   1.00 26.55 ? 275 LEU   B CB  1 
ATOM   4851 C CG  . LEU   B 1 278 ? -31.842 23.596  2.158   1.00 33.65 ? 275 LEU   B CG  1 
ATOM   4852 C CD1 . LEU   B 1 278 ? -32.522 22.946  0.961   1.00 28.22 ? 275 LEU   B CD1 1 
ATOM   4853 C CD2 . LEU   B 1 278 ? -32.741 23.537  3.399   1.00 30.25 ? 275 LEU   B CD2 1 
ATOM   4854 N N   . LEU   B 1 279 ? -27.459 22.990  3.670   1.00 24.64 ? 276 LEU   B N   1 
ATOM   4855 C CA  . LEU   B 1 279 ? -26.273 22.159  3.870   1.00 26.02 ? 276 LEU   B CA  1 
ATOM   4856 C C   . LEU   B 1 279 ? -26.032 21.809  5.330   1.00 27.75 ? 276 LEU   B C   1 
ATOM   4857 O O   . LEU   B 1 279 ? -25.524 20.696  5.578   1.00 26.07 ? 276 LEU   B O   1 
ATOM   4858 C CB  . LEU   B 1 279 ? -25.037 22.862  3.273   1.00 24.73 ? 276 LEU   B CB  1 
ATOM   4859 C CG  . LEU   B 1 279 ? -25.175 23.167  1.784   1.00 23.60 ? 276 LEU   B CG  1 
ATOM   4860 C CD1 . LEU   B 1 279 ? -23.835 23.607  1.197   1.00 28.35 ? 276 LEU   B CD1 1 
ATOM   4861 C CD2 . LEU   B 1 279 ? -25.701 21.952  1.073   1.00 24.70 ? 276 LEU   B CD2 1 
ATOM   4862 N N   . PRO   B 1 280 ? -26.360 22.653  6.310   1.00 27.05 ? 277 PRO   B N   1 
ATOM   4863 C CA  . PRO   B 1 280 ? -26.263 22.242  7.717   1.00 30.68 ? 277 PRO   B CA  1 
ATOM   4864 C C   . PRO   B 1 280 ? -27.053 20.983  8.061   1.00 33.15 ? 277 PRO   B C   1 
ATOM   4865 O O   . PRO   B 1 280 ? -26.834 20.414  9.135   1.00 39.85 ? 277 PRO   B O   1 
ATOM   4866 C CB  . PRO   B 1 280 ? -26.818 23.461  8.468   1.00 32.18 ? 277 PRO   B CB  1 
ATOM   4867 C CG  . PRO   B 1 280 ? -26.596 24.621  7.536   1.00 28.48 ? 277 PRO   B CG  1 
ATOM   4868 C CD  . PRO   B 1 280 ? -26.754 24.077  6.157   1.00 27.45 ? 277 PRO   B CD  1 
ATOM   4869 N N   . TYR   B 1 281 ? -27.955 20.522  7.201   1.00 27.85 ? 278 TYR   B N   1 
ATOM   4870 C CA  . TYR   B 1 281 ? -28.821 19.402  7.545   1.00 29.87 ? 278 TYR   B CA  1 
ATOM   4871 C C   . TYR   B 1 281 ? -28.371 18.090  6.929   1.00 31.76 ? 278 TYR   B C   1 
ATOM   4872 O O   . TYR   B 1 281 ? -29.030 17.071  7.148   1.00 31.60 ? 278 TYR   B O   1 
ATOM   4873 C CB  . TYR   B 1 281 ? -30.267 19.706  7.123   1.00 32.89 ? 278 TYR   B CB  1 
ATOM   4874 C CG  . TYR   B 1 281 ? -30.879 20.842  7.916   1.00 35.18 ? 278 TYR   B CG  1 
ATOM   4875 C CD1 . TYR   B 1 281 ? -30.476 22.151  7.699   1.00 33.31 ? 278 TYR   B CD1 1 
ATOM   4876 C CD2 . TYR   B 1 281 ? -31.837 20.603  8.903   1.00 41.28 ? 278 TYR   B CD2 1 
ATOM   4877 C CE1 . TYR   B 1 281 ? -31.007 23.199  8.421   1.00 35.34 ? 278 TYR   B CE1 1 
ATOM   4878 C CE2 . TYR   B 1 281 ? -32.387 21.653  9.639   1.00 41.14 ? 278 TYR   B CE2 1 
ATOM   4879 C CZ  . TYR   B 1 281 ? -31.966 22.947  9.392   1.00 49.14 ? 278 TYR   B CZ  1 
ATOM   4880 O OH  . TYR   B 1 281 ? -32.493 23.994  10.122  1.00 49.30 ? 278 TYR   B OH  1 
ATOM   4881 N N   . ILE   B 1 282 ? -27.275 18.078  6.164   1.00 25.46 ? 279 ILE   B N   1 
ATOM   4882 C CA  . ILE   B 1 282 ? -26.894 16.885  5.421   1.00 24.10 ? 279 ILE   B CA  1 
ATOM   4883 C C   . ILE   B 1 282 ? -25.676 16.194  6.006   1.00 20.28 ? 279 ILE   B C   1 
ATOM   4884 O O   . ILE   B 1 282 ? -25.262 15.153  5.477   1.00 22.77 ? 279 ILE   B O   1 
ATOM   4885 C CB  . ILE   B 1 282 ? -26.668 17.193  3.927   1.00 24.23 ? 279 ILE   B CB  1 
ATOM   4886 C CG1 . ILE   B 1 282 ? -25.323 17.880  3.689   1.00 21.88 ? 279 ILE   B CG1 1 
ATOM   4887 C CG2 . ILE   B 1 282 ? -27.803 18.072  3.379   1.00 25.87 ? 279 ILE   B CG2 1 
ATOM   4888 C CD1 . ILE   B 1 282 ? -24.993 18.005  2.182   1.00 20.94 ? 279 ILE   B CD1 1 
ATOM   4889 N N   . MET   B 1 283 ? -25.092 16.720  7.075   1.00 23.58 ? 280 MET   B N   1 
ATOM   4890 C CA  . MET   B 1 283 ? -23.848 16.140  7.597   1.00 23.61 ? 280 MET   B CA  1 
ATOM   4891 C C   . MET   B 1 283 ? -24.116 14.834  8.338   1.00 22.90 ? 280 MET   B C   1 
ATOM   4892 O O   . MET   B 1 283 ? -23.684 13.762  7.903   1.00 23.73 ? 280 MET   B O   1 
ATOM   4893 C CB  . MET   B 1 283 ? -23.132 17.148  8.499   1.00 26.32 ? 280 MET   B CB  1 
ATOM   4894 C CG  . MET   B 1 283 ? -22.272 18.099  7.702   1.00 26.93 ? 280 MET   B CG  1 
ATOM   4895 S SD  . MET   B 1 283 ? -21.782 19.594  8.556   1.00 30.59 ? 280 MET   B SD  1 
ATOM   4896 C CE  . MET   B 1 283 ? -23.360 20.298  8.987   1.00 26.93 ? 280 MET   B CE  1 
ATOM   4897 N N   . PHE   B 1 284 ? -24.836 14.900  9.452   1.00 24.77 ? 281 PHE   B N   1 
ATOM   4898 C CA  . PHE   B 1 284 ? -25.143 13.655  10.152  1.00 24.57 ? 281 PHE   B CA  1 
ATOM   4899 C C   . PHE   B 1 284 ? -25.807 12.637  9.240   1.00 23.31 ? 281 PHE   B C   1 
ATOM   4900 O O   . PHE   B 1 284 ? -25.403 11.467  9.274   1.00 23.61 ? 281 PHE   B O   1 
ATOM   4901 C CB  . PHE   B 1 284 ? -26.013 13.885  11.401  1.00 28.15 ? 281 PHE   B CB  1 
ATOM   4902 C CG  . PHE   B 1 284 ? -26.403 12.591  12.072  1.00 28.91 ? 281 PHE   B CG  1 
ATOM   4903 C CD1 . PHE   B 1 284 ? -25.468 11.875  12.814  1.00 30.93 ? 281 PHE   B CD1 1 
ATOM   4904 C CD2 . PHE   B 1 284 ? -27.656 12.027  11.860  1.00 33.62 ? 281 PHE   B CD2 1 
ATOM   4905 C CE1 . PHE   B 1 284 ? -25.801 10.649  13.395  1.00 30.59 ? 281 PHE   B CE1 1 
ATOM   4906 C CE2 . PHE   B 1 284 ? -27.995 10.804  12.437  1.00 34.09 ? 281 PHE   B CE2 1 
ATOM   4907 C CZ  . PHE   B 1 284 ? -27.063 10.116  13.206  1.00 29.10 ? 281 PHE   B CZ  1 
ATOM   4908 N N   . PRO   B 1 285 ? -26.787 12.996  8.402   1.00 22.31 ? 282 PRO   B N   1 
ATOM   4909 C CA  . PRO   B 1 285 ? -27.383 12.007  7.482   1.00 25.13 ? 282 PRO   B CA  1 
ATOM   4910 C C   . PRO   B 1 285 ? -26.430 11.493  6.412   1.00 24.74 ? 282 PRO   B C   1 
ATOM   4911 O O   . PRO   B 1 285 ? -26.770 10.520  5.732   1.00 24.14 ? 282 PRO   B O   1 
ATOM   4912 C CB  . PRO   B 1 285 ? -28.546 12.783  6.839   1.00 27.55 ? 282 PRO   B CB  1 
ATOM   4913 C CG  . PRO   B 1 285 ? -28.880 13.850  7.857   1.00 28.75 ? 282 PRO   B CG  1 
ATOM   4914 C CD  . PRO   B 1 285 ? -27.564 14.247  8.458   1.00 28.65 ? 282 PRO   B CD  1 
ATOM   4915 N N   . ARG   B 1 286 ? -25.260 12.106  6.231   1.00 22.78 ? 283 ARG   B N   1 
ATOM   4916 C CA  . ARG   B 1 286 ? -24.381 11.735  5.128   1.00 23.85 ? 283 ARG   B CA  1 
ATOM   4917 C C   . ARG   B 1 286 ? -25.162 11.678  3.815   1.00 22.38 ? 283 ARG   B C   1 
ATOM   4918 O O   . ARG   B 1 286 ? -24.992 10.764  3.002   1.00 22.26 ? 283 ARG   B O   1 
ATOM   4919 C CB  . ARG   B 1 286 ? -23.683 10.405  5.397   1.00 22.77 ? 283 ARG   B CB  1 
ATOM   4920 C CG  . ARG   B 1 286 ? -22.683 10.463  6.570   1.00 24.61 ? 283 ARG   B CG  1 
ATOM   4921 C CD  . ARG   B 1 286 ? -23.411 10.245  7.901   1.00 33.38 ? 283 ARG   B CD  1 
ATOM   4922 N NE  . ARG   B 1 286 ? -23.464 8.835   8.216   1.00 28.48 ? 283 ARG   B NE  1 
ATOM   4923 C CZ  . ARG   B 1 286 ? -23.923 8.295   9.342   1.00 30.77 ? 283 ARG   B CZ  1 
ATOM   4924 N NH1 . ARG   B 1 286 ? -24.546 9.010   10.271  1.00 26.87 ? 283 ARG   B NH1 1 
ATOM   4925 N NH2 . ARG   B 1 286 ? -23.737 6.998   9.546   1.00 31.17 ? 283 ARG   B NH2 1 
ATOM   4926 N N   . ALA   B 1 287 ? -26.046 12.656  3.619   1.00 22.58 ? 284 ALA   B N   1 
ATOM   4927 C CA  . ALA   B 1 287 ? -26.869 12.689  2.420   1.00 23.78 ? 284 ALA   B CA  1 
ATOM   4928 C C   . ALA   B 1 287 ? -26.033 13.043  1.197   1.00 25.37 ? 284 ALA   B C   1 
ATOM   4929 O O   . ALA   B 1 287 ? -25.101 13.852  1.281   1.00 24.40 ? 284 ALA   B O   1 
ATOM   4930 C CB  . ALA   B 1 287 ? -28.005 13.702  2.598   1.00 23.52 ? 284 ALA   B CB  1 
ATOM   4931 N N   . THR   B 1 288 ? -26.372 12.440  0.051   1.00 20.67 ? 285 THR   B N   1 
ATOM   4932 C CA  . THR   B 1 288 ? -25.766 12.780  -1.233  1.00 22.54 ? 285 THR   B CA  1 
ATOM   4933 C C   . THR   B 1 288 ? -26.805 13.481  -2.113  1.00 27.97 ? 285 THR   B C   1 
ATOM   4934 O O   . THR   B 1 288 ? -27.885 12.928  -2.361  1.00 24.25 ? 285 THR   B O   1 
ATOM   4935 C CB  . THR   B 1 288 ? -25.225 11.533  -1.943  1.00 24.74 ? 285 THR   B CB  1 
ATOM   4936 O OG1 . THR   B 1 288 ? -24.298 10.853  -1.082  1.00 23.89 ? 285 THR   B OG1 1 
ATOM   4937 C CG2 . THR   B 1 288 ? -24.490 11.935  -3.228  1.00 24.07 ? 285 THR   B CG2 1 
ATOM   4938 N N   . ILE   B 1 289 ? -26.470 14.688  -2.581  1.00 21.89 ? 286 ILE   B N   1 
ATOM   4939 C CA  . ILE   B 1 289 ? -27.314 15.507  -3.451  1.00 21.22 ? 286 ILE   B CA  1 
ATOM   4940 C C   . ILE   B 1 289 ? -26.628 15.614  -4.806  1.00 25.89 ? 286 ILE   B C   1 
ATOM   4941 O O   . ILE   B 1 289 ? -25.434 15.941  -4.878  1.00 25.21 ? 286 ILE   B O   1 
ATOM   4942 C CB  . ILE   B 1 289 ? -27.552 16.908  -2.860  1.00 20.80 ? 286 ILE   B CB  1 
ATOM   4943 C CG1 . ILE   B 1 289 ? -27.973 16.823  -1.396  1.00 25.53 ? 286 ILE   B CG1 1 
ATOM   4944 C CG2 . ILE   B 1 289 ? -28.611 17.686  -3.661  1.00 25.54 ? 286 ILE   B CG2 1 
ATOM   4945 C CD1 . ILE   B 1 289 ? -27.749 18.109  -0.625  1.00 26.46 ? 286 ILE   B CD1 1 
ATOM   4946 N N   . ARG   B 1 290 ? -27.380 15.354  -5.883  1.00 19.14 ? 287 ARG   B N   1 
ATOM   4947 C CA  . ARG   B 1 290 ? -26.851 15.403  -7.246  1.00 22.91 ? 287 ARG   B CA  1 
ATOM   4948 C C   . ARG   B 1 290 ? -27.770 16.236  -8.140  1.00 22.93 ? 287 ARG   B C   1 
ATOM   4949 O O   . ARG   B 1 290 ? -28.974 15.970  -8.225  1.00 20.48 ? 287 ARG   B O   1 
ATOM   4950 C CB  . ARG   B 1 290 ? -26.700 13.978  -7.783  1.00 22.94 ? 287 ARG   B CB  1 
ATOM   4951 C CG  . ARG   B 1 290 ? -26.497 13.821  -9.280  1.00 27.13 ? 287 ARG   B CG  1 
ATOM   4952 C CD  . ARG   B 1 290 ? -25.046 13.806  -9.665  1.00 28.99 ? 287 ARG   B CD  1 
ATOM   4953 N NE  . ARG   B 1 290 ? -24.721 12.973  -10.830 1.00 26.10 ? 287 ARG   B NE  1 
ATOM   4954 C CZ  . ARG   B 1 290 ? -25.041 13.243  -12.094 1.00 29.74 ? 287 ARG   B CZ  1 
ATOM   4955 N NH1 . ARG   B 1 290 ? -25.903 14.198  -12.404 1.00 27.67 ? 287 ARG   B NH1 1 
ATOM   4956 N NH2 . ARG   B 1 290 ? -24.496 12.521  -13.070 1.00 27.32 ? 287 ARG   B NH2 1 
ATOM   4957 N N   . GLY   B 1 291 ? -27.210 17.241  -8.808  1.00 23.20 ? 288 GLY   B N   1 
ATOM   4958 C CA  . GLY   B 1 291 ? -27.960 17.926  -9.845  1.00 20.58 ? 288 GLY   B CA  1 
ATOM   4959 C C   . GLY   B 1 291 ? -28.104 17.061  -11.088 1.00 21.09 ? 288 GLY   B C   1 
ATOM   4960 O O   . GLY   B 1 291 ? -27.159 16.408  -11.536 1.00 21.31 ? 288 GLY   B O   1 
ATOM   4961 N N   . ILE   B 1 292 ? -29.303 17.077  -11.659 1.00 21.30 ? 289 ILE   B N   1 
ATOM   4962 C CA  . ILE   B 1 292 ? -29.632 16.313  -12.863 1.00 21.22 ? 289 ILE   B CA  1 
ATOM   4963 C C   . ILE   B 1 292 ? -29.553 17.239  -14.072 1.00 20.51 ? 289 ILE   B C   1 
ATOM   4964 O O   . ILE   B 1 292 ? -30.082 18.352  -14.042 1.00 21.52 ? 289 ILE   B O   1 
ATOM   4965 C CB  . ILE   B 1 292 ? -31.040 15.694  -12.747 1.00 20.72 ? 289 ILE   B CB  1 
ATOM   4966 C CG1 . ILE   B 1 292 ? -31.145 14.834  -11.470 1.00 20.46 ? 289 ILE   B CG1 1 
ATOM   4967 C CG2 . ILE   B 1 292 ? -31.427 14.942  -14.029 1.00 25.84 ? 289 ILE   B CG2 1 
ATOM   4968 C CD1 . ILE   B 1 292 ? -30.039 13.810  -11.342 1.00 22.59 ? 289 ILE   B CD1 1 
ATOM   4969 N N   . PHE   B 1 293 ? -28.889 16.783  -15.135 1.00 20.31 ? 290 PHE   B N   1 
ATOM   4970 C CA  . PHE   B 1 293 ? -28.905 17.499  -16.415 1.00 22.04 ? 290 PHE   B CA  1 
ATOM   4971 C C   . PHE   B 1 293 ? -28.856 16.417  -17.494 1.00 21.23 ? 290 PHE   B C   1 
ATOM   4972 O O   . PHE   B 1 293 ? -27.782 16.031  -17.951 1.00 24.03 ? 290 PHE   B O   1 
ATOM   4973 C CB  . PHE   B 1 293 ? -27.752 18.487  -16.539 1.00 21.18 ? 290 PHE   B CB  1 
ATOM   4974 C CG  . PHE   B 1 293 ? -27.926 19.484  -17.678 1.00 25.04 ? 290 PHE   B CG  1 
ATOM   4975 C CD1 . PHE   B 1 293 ? -28.830 20.536  -17.563 1.00 25.64 ? 290 PHE   B CD1 1 
ATOM   4976 C CD2 . PHE   B 1 293 ? -27.218 19.335  -18.854 1.00 19.80 ? 290 PHE   B CD2 1 
ATOM   4977 C CE1 . PHE   B 1 293 ? -29.010 21.435  -18.616 1.00 28.87 ? 290 PHE   B CE1 1 
ATOM   4978 C CE2 . PHE   B 1 293 ? -27.380 20.233  -19.906 1.00 23.99 ? 290 PHE   B CE2 1 
ATOM   4979 C CZ  . PHE   B 1 293 ? -28.282 21.281  -19.789 1.00 23.80 ? 290 PHE   B CZ  1 
ATOM   4980 N N   . SER   B 1 294 ? -30.037 15.903  -17.857 1.00 23.73 ? 291 SER   B N   1 
ATOM   4981 C CA  . SER   B 1 294 ? -30.080 14.603  -18.529 1.00 26.50 ? 291 SER   B CA  1 
ATOM   4982 C C   . SER   B 1 294 ? -29.479 14.619  -19.932 1.00 25.05 ? 291 SER   B C   1 
ATOM   4983 O O   . SER   B 1 294 ? -29.240 13.539  -20.489 1.00 24.80 ? 291 SER   B O   1 
ATOM   4984 C CB  . SER   B 1 294 ? -31.519 14.086  -18.562 1.00 32.32 ? 291 SER   B CB  1 
ATOM   4985 O OG  . SER   B 1 294 ? -32.425 15.110  -18.937 1.00 34.24 ? 291 SER   B OG  1 
ATOM   4986 N N   . LEU   B 1 295 ? -29.217 15.796  -20.513 1.00 22.48 ? 292 LEU   B N   1 
ATOM   4987 C CA  . LEU   B 1 295 ? -28.474 15.854  -21.764 1.00 24.93 ? 292 LEU   B CA  1 
ATOM   4988 C C   . LEU   B 1 295 ? -27.213 15.007  -21.720 1.00 26.51 ? 292 LEU   B C   1 
ATOM   4989 O O   . LEU   B 1 295 ? -26.802 14.456  -22.749 1.00 25.96 ? 292 LEU   B O   1 
ATOM   4990 C CB  . LEU   B 1 295 ? -28.087 17.297  -22.109 1.00 30.74 ? 292 LEU   B CB  1 
ATOM   4991 C CG  . LEU   B 1 295 ? -29.177 18.189  -22.695 1.00 34.95 ? 292 LEU   B CG  1 
ATOM   4992 C CD1 . LEU   B 1 295 ? -28.568 19.487  -23.238 1.00 32.25 ? 292 LEU   B CD1 1 
ATOM   4993 C CD2 . LEU   B 1 295 ? -29.903 17.445  -23.796 1.00 35.86 ? 292 LEU   B CD2 1 
ATOM   4994 N N   . GLU   B 1 296 ? -26.581 14.888  -20.549 1.00 23.42 ? 293 GLU   B N   1 
ATOM   4995 C CA  . GLU   B 1 296 ? -25.344 14.112  -20.475 1.00 26.77 ? 293 GLU   B CA  1 
ATOM   4996 C C   . GLU   B 1 296 ? -25.573 12.642  -20.792 1.00 26.24 ? 293 GLU   B C   1 
ATOM   4997 O O   . GLU   B 1 296 ? -24.619 11.948  -21.153 1.00 28.80 ? 293 GLU   B O   1 
ATOM   4998 C CB  . GLU   B 1 296 ? -24.678 14.248  -19.092 1.00 25.01 ? 293 GLU   B CB  1 
ATOM   4999 C CG  . GLU   B 1 296 ? -25.483 13.682  -17.922 1.00 23.24 ? 293 GLU   B CG  1 
ATOM   5000 C CD  . GLU   B 1 296 ? -24.656 13.505  -16.649 1.00 28.48 ? 293 GLU   B CD  1 
ATOM   5001 O OE1 . GLU   B 1 296 ? -23.434 13.283  -16.752 1.00 31.11 ? 293 GLU   B OE1 1 
ATOM   5002 O OE2 . GLU   B 1 296 ? -25.228 13.589  -15.542 1.00 26.32 ? 293 GLU   B OE2 1 
ATOM   5003 N N   . TRP   B 1 297 ? -26.810 12.158  -20.679 1.00 25.91 ? 294 TRP   B N   1 
ATOM   5004 C CA  . TRP   B 1 297 ? -27.131 10.756  -20.932 1.00 26.49 ? 294 TRP   B CA  1 
ATOM   5005 C C   . TRP   B 1 297 ? -27.589 10.481  -22.362 1.00 30.92 ? 294 TRP   B C   1 
ATOM   5006 O O   . TRP   B 1 297 ? -27.912 9.325   -22.680 1.00 28.46 ? 294 TRP   B O   1 
ATOM   5007 C CB  . TRP   B 1 297 ? -28.206 10.289  -19.939 1.00 23.36 ? 294 TRP   B CB  1 
ATOM   5008 C CG  . TRP   B 1 297 ? -27.717 10.328  -18.514 1.00 24.94 ? 294 TRP   B CG  1 
ATOM   5009 C CD1 . TRP   B 1 297 ? -26.450 10.066  -18.075 1.00 25.51 ? 294 TRP   B CD1 1 
ATOM   5010 C CD2 . TRP   B 1 297 ? -28.478 10.684  -17.355 1.00 25.07 ? 294 TRP   B CD2 1 
ATOM   5011 N NE1 . TRP   B 1 297 ? -26.381 10.224  -16.710 1.00 25.27 ? 294 TRP   B NE1 1 
ATOM   5012 C CE2 . TRP   B 1 297 ? -27.615 10.593  -16.242 1.00 26.59 ? 294 TRP   B CE2 1 
ATOM   5013 C CE3 . TRP   B 1 297 ? -29.809 11.059  -17.146 1.00 25.78 ? 294 TRP   B CE3 1 
ATOM   5014 C CZ2 . TRP   B 1 297 ? -28.038 10.864  -14.943 1.00 25.98 ? 294 TRP   B CZ2 1 
ATOM   5015 C CZ3 . TRP   B 1 297 ? -30.228 11.327  -15.843 1.00 26.60 ? 294 TRP   B CZ3 1 
ATOM   5016 C CH2 . TRP   B 1 297 ? -29.344 11.227  -14.762 1.00 25.91 ? 294 TRP   B CH2 1 
ATOM   5017 N N   . PHE   B 1 298 ? -27.595 11.491  -23.239 1.00 27.92 ? 295 PHE   B N   1 
ATOM   5018 C CA  . PHE   B 1 298 ? -28.070 11.324  -24.617 1.00 30.01 ? 295 PHE   B CA  1 
ATOM   5019 C C   . PHE   B 1 298 ? -26.974 10.636  -25.434 1.00 31.73 ? 295 PHE   B C   1 
ATOM   5020 O O   . PHE   B 1 298 ? -26.223 11.256  -26.187 1.00 31.38 ? 295 PHE   B O   1 
ATOM   5021 C CB  . PHE   B 1 298 ? -28.484 12.665  -25.226 1.00 26.95 ? 295 PHE   B CB  1 
ATOM   5022 C CG  . PHE   B 1 298 ? -29.824 13.185  -24.724 1.00 28.64 ? 295 PHE   B CG  1 
ATOM   5023 C CD1 . PHE   B 1 298 ? -30.253 12.918  -23.432 1.00 28.71 ? 295 PHE   B CD1 1 
ATOM   5024 C CD2 . PHE   B 1 298 ? -30.659 13.927  -25.559 1.00 32.26 ? 295 PHE   B CD2 1 
ATOM   5025 C CE1 . PHE   B 1 298 ? -31.495 13.389  -22.964 1.00 28.06 ? 295 PHE   B CE1 1 
ATOM   5026 C CE2 . PHE   B 1 298 ? -31.900 14.405  -25.106 1.00 30.34 ? 295 PHE   B CE2 1 
ATOM   5027 C CZ  . PHE   B 1 298 ? -32.320 14.132  -23.815 1.00 31.14 ? 295 PHE   B CZ  1 
ATOM   5028 N N   . THR   B 1 299 ? -26.880 9.318   -25.268 1.00 32.92 ? 296 THR   B N   1 
ATOM   5029 C CA  . THR   B 1 299 ? -25.949 8.494   -26.027 1.00 31.83 ? 296 THR   B CA  1 
ATOM   5030 C C   . THR   B 1 299 ? -26.702 7.342   -26.676 1.00 32.64 ? 296 THR   B C   1 
ATOM   5031 O O   . THR   B 1 299 ? -27.752 6.913   -26.181 1.00 31.42 ? 296 THR   B O   1 
ATOM   5032 C CB  . THR   B 1 299 ? -24.819 7.919   -25.147 1.00 37.49 ? 296 THR   B CB  1 
ATOM   5033 O OG1 . THR   B 1 299 ? -25.354 6.917   -24.268 1.00 33.52 ? 296 THR   B OG1 1 
ATOM   5034 C CG2 . THR   B 1 299 ? -24.171 9.022   -24.317 1.00 39.11 ? 296 THR   B CG2 1 
ATOM   5035 N N   . GLU   B 1 300 ? -26.150 6.841   -27.788 1.00 37.12 ? 297 GLU   B N   1 
ATOM   5036 C CA  . GLU   B 1 300 ? -26.784 5.733   -28.496 1.00 37.67 ? 297 GLU   B CA  1 
ATOM   5037 C C   . GLU   B 1 300 ? -26.983 4.534   -27.584 1.00 36.05 ? 297 GLU   B C   1 
ATOM   5038 O O   . GLU   B 1 300 ? -28.052 3.915   -27.587 1.00 36.22 ? 297 GLU   B O   1 
ATOM   5039 C CB  . GLU   B 1 300 ? -25.954 5.331   -29.709 1.00 42.99 ? 297 GLU   B CB  1 
ATOM   5040 C CG  . GLU   B 1 300 ? -26.017 6.291   -30.861 1.00 47.47 ? 297 GLU   B CG  1 
ATOM   5041 C CD  . GLU   B 1 300 ? -25.613 5.629   -32.164 1.00 63.30 ? 297 GLU   B CD  1 
ATOM   5042 O OE1 . GLU   B 1 300 ? -25.792 6.268   -33.229 1.00 62.95 ? 297 GLU   B OE1 1 
ATOM   5043 O OE2 . GLU   B 1 300 ? -25.129 4.472   -32.125 1.00 65.22 ? 297 GLU   B OE2 1 
ATOM   5044 N N   . GLN   B 1 301 ? -25.966 4.187   -26.794 1.00 35.20 ? 298 GLN   B N   1 
ATOM   5045 C CA  . GLN   B 1 301 ? -26.112 3.052   -25.889 1.00 39.23 ? 298 GLN   B CA  1 
ATOM   5046 C C   . GLN   B 1 301 ? -27.237 3.293   -24.896 1.00 35.18 ? 298 GLN   B C   1 
ATOM   5047 O O   . GLN   B 1 301 ? -28.006 2.376   -24.584 1.00 33.40 ? 298 GLN   B O   1 
ATOM   5048 C CB  . GLN   B 1 301 ? -24.795 2.774   -25.155 1.00 41.25 ? 298 GLN   B CB  1 
ATOM   5049 C CG  . GLN   B 1 301 ? -23.567 2.874   -26.048 1.00 46.38 ? 298 GLN   B CG  1 
ATOM   5050 C CD  . GLN   B 1 301 ? -23.030 4.304   -26.138 1.00 51.96 ? 298 GLN   B CD  1 
ATOM   5051 O OE1 . GLN   B 1 301 ? -23.057 4.939   -27.202 1.00 46.79 ? 298 GLN   B OE1 1 
ATOM   5052 N NE2 . GLN   B 1 301 ? -22.538 4.822   -25.007 1.00 56.35 ? 298 GLN   B NE2 1 
ATOM   5053 N N   . ASN   B 1 302 ? -27.366 4.526   -24.397 1.00 34.17 ? 299 ASN   B N   1 
ATOM   5054 C CA  . ASN   B 1 302 ? -28.408 4.800   -23.409 1.00 34.14 ? 299 ASN   B CA  1 
ATOM   5055 C C   . ASN   B 1 302 ? -29.800 4.760   -24.036 1.00 31.36 ? 299 ASN   B C   1 
ATOM   5056 O O   . ASN   B 1 302 ? -30.763 4.339   -23.384 1.00 33.77 ? 299 ASN   B O   1 
ATOM   5057 C CB  . ASN   B 1 302 ? -28.173 6.152   -22.737 1.00 32.71 ? 299 ASN   B CB  1 
ATOM   5058 C CG  . ASN   B 1 302 ? -27.053 6.116   -21.703 1.00 35.34 ? 299 ASN   B CG  1 
ATOM   5059 O OD1 . ASN   B 1 302 ? -26.829 5.106   -21.038 1.00 32.71 ? 299 ASN   B OD1 1 
ATOM   5060 N ND2 . ASN   B 1 302 ? -26.351 7.236   -21.559 1.00 33.50 ? 299 ASN   B ND2 1 
ATOM   5061 N N   . TRP   B 1 303 ? -29.939 5.219   -25.283 1.00 33.43 ? 300 TRP   B N   1 
ATOM   5062 C CA  . TRP   B 1 303 ? -31.252 5.165   -25.931 1.00 33.30 ? 300 TRP   B CA  1 
ATOM   5063 C C   . TRP   B 1 303 ? -31.676 3.720   -26.173 1.00 32.16 ? 300 TRP   B C   1 
ATOM   5064 O O   . TRP   B 1 303 ? -32.813 3.335   -25.876 1.00 35.39 ? 300 TRP   B O   1 
ATOM   5065 C CB  . TRP   B 1 303 ? -31.243 5.962   -27.239 1.00 32.86 ? 300 TRP   B CB  1 
ATOM   5066 C CG  . TRP   B 1 303 ? -31.220 7.455   -27.006 1.00 33.65 ? 300 TRP   B CG  1 
ATOM   5067 C CD1 . TRP   B 1 303 ? -30.231 8.323   -27.352 1.00 30.21 ? 300 TRP   B CD1 1 
ATOM   5068 C CD2 . TRP   B 1 303 ? -32.230 8.239   -26.350 1.00 28.91 ? 300 TRP   B CD2 1 
ATOM   5069 N NE1 . TRP   B 1 303 ? -30.568 9.604   -26.966 1.00 29.98 ? 300 TRP   B NE1 1 
ATOM   5070 C CE2 . TRP   B 1 303 ? -31.786 9.575   -26.344 1.00 30.89 ? 300 TRP   B CE2 1 
ATOM   5071 C CE3 . TRP   B 1 303 ? -33.467 7.938   -25.770 1.00 31.94 ? 300 TRP   B CE3 1 
ATOM   5072 C CZ2 . TRP   B 1 303 ? -32.532 10.610  -25.772 1.00 27.02 ? 300 TRP   B CZ2 1 
ATOM   5073 C CZ3 . TRP   B 1 303 ? -34.209 8.961   -25.210 1.00 28.38 ? 300 TRP   B CZ3 1 
ATOM   5074 C CH2 . TRP   B 1 303 ? -33.734 10.285  -25.217 1.00 30.92 ? 300 TRP   B CH2 1 
ATOM   5075 N N   . SER   B 1 304 ? -30.760 2.902   -26.691 1.00 33.78 ? 301 SER   B N   1 
ATOM   5076 C CA  . SER   B 1 304 ? -31.039 1.475   -26.843 1.00 35.81 ? 301 SER   B CA  1 
ATOM   5077 C C   . SER   B 1 304 ? -31.402 0.846   -25.509 1.00 34.94 ? 301 SER   B C   1 
ATOM   5078 O O   . SER   B 1 304 ? -32.377 0.092   -25.416 1.00 38.50 ? 301 SER   B O   1 
ATOM   5079 C CB  . SER   B 1 304 ? -29.831 0.769   -27.456 1.00 40.01 ? 301 SER   B CB  1 
ATOM   5080 O OG  . SER   B 1 304 ? -29.473 1.376   -28.685 1.00 40.53 ? 301 SER   B OG  1 
ATOM   5081 N N   . ALA   B 1 305 ? -30.649 1.169   -24.453 1.00 33.81 ? 302 ALA   B N   1 
ATOM   5082 C CA  . ALA   B 1 305 ? -30.969 0.629   -23.132 1.00 35.48 ? 302 ALA   B CA  1 
ATOM   5083 C C   . ALA   B 1 305 ? -32.330 1.118   -22.640 1.00 35.47 ? 302 ALA   B C   1 
ATOM   5084 O O   . ALA   B 1 305 ? -33.100 0.344   -22.059 1.00 36.90 ? 302 ALA   B O   1 
ATOM   5085 C CB  . ALA   B 1 305 ? -29.866 0.988   -22.131 1.00 34.41 ? 302 ALA   B CB  1 
ATOM   5086 N N   . LEU   B 1 306 ? -32.644 2.401   -22.856 1.00 34.26 ? 303 LEU   B N   1 
ATOM   5087 C CA  . LEU   B 1 306 ? -33.950 2.919   -22.449 1.00 33.41 ? 303 LEU   B CA  1 
ATOM   5088 C C   . LEU   B 1 306 ? -35.073 2.212   -23.200 1.00 33.98 ? 303 LEU   B C   1 
ATOM   5089 O O   . LEU   B 1 306 ? -36.083 1.813   -22.608 1.00 37.02 ? 303 LEU   B O   1 
ATOM   5090 C CB  . LEU   B 1 306 ? -34.024 4.433   -22.691 1.00 30.95 ? 303 LEU   B CB  1 
ATOM   5091 C CG  . LEU   B 1 306 ? -35.386 5.107   -22.458 1.00 32.56 ? 303 LEU   B CG  1 
ATOM   5092 C CD1 . LEU   B 1 306 ? -35.630 5.330   -20.976 1.00 33.95 ? 303 LEU   B CD1 1 
ATOM   5093 C CD2 . LEU   B 1 306 ? -35.482 6.448   -23.200 1.00 32.75 ? 303 LEU   B CD2 1 
ATOM   5094 N N   . HIS   B 1 307 ? -34.925 2.078   -24.520 1.00 38.49 ? 304 HIS   B N   1 
ATOM   5095 C CA  . HIS   B 1 307 ? -35.932 1.372   -25.305 1.00 39.52 ? 304 HIS   B CA  1 
ATOM   5096 C C   . HIS   B 1 307 ? -36.115 -0.054  -24.796 1.00 43.30 ? 304 HIS   B C   1 
ATOM   5097 O O   . HIS   B 1 307 ? -37.240 -0.490  -24.518 1.00 44.76 ? 304 HIS   B O   1 
ATOM   5098 C CB  . HIS   B 1 307 ? -35.545 1.381   -26.778 1.00 38.88 ? 304 HIS   B CB  1 
ATOM   5099 C CG  . HIS   B 1 307 ? -36.146 2.515   -27.552 1.00 51.40 ? 304 HIS   B CG  1 
ATOM   5100 N ND1 . HIS   B 1 307 ? -37.428 2.465   -28.069 1.00 55.81 ? 304 HIS   B ND1 1 
ATOM   5101 C CD2 . HIS   B 1 307 ? -35.649 3.727   -27.898 1.00 44.13 ? 304 HIS   B CD2 1 
ATOM   5102 C CE1 . HIS   B 1 307 ? -37.691 3.598   -28.697 1.00 49.78 ? 304 HIS   B CE1 1 
ATOM   5103 N NE2 . HIS   B 1 307 ? -36.629 4.381   -28.608 1.00 44.83 ? 304 HIS   B NE2 1 
ATOM   5104 N N   . GLU   B 1 308 ? -35.013 -0.790  -24.644 1.00 41.62 ? 305 GLU   B N   1 
ATOM   5105 C CA  . GLU   B 1 308 ? -35.053 -2.143  -24.102 1.00 42.03 ? 305 GLU   B CA  1 
ATOM   5106 C C   . GLU   B 1 308 ? -35.793 -2.205  -22.773 1.00 43.96 ? 305 GLU   B C   1 
ATOM   5107 O O   . GLU   B 1 308 ? -36.850 -2.838  -22.676 1.00 49.40 ? 305 GLU   B O   1 
ATOM   5108 C CB  . GLU   B 1 308 ? -33.631 -2.684  -23.916 1.00 47.57 ? 305 GLU   B CB  1 
ATOM   5109 C CG  . GLU   B 1 308 ? -33.075 -3.457  -25.097 1.00 53.06 ? 305 GLU   B CG  1 
ATOM   5110 C CD  . GLU   B 1 308 ? -33.226 -4.963  -24.931 1.00 68.21 ? 305 GLU   B CD  1 
ATOM   5111 O OE1 . GLU   B 1 308 ? -34.352 -5.484  -25.115 1.00 65.87 ? 305 GLU   B OE1 1 
ATOM   5112 O OE2 . GLU   B 1 308 ? -32.215 -5.624  -24.607 1.00 72.36 ? 305 GLU   B OE2 1 
ATOM   5113 N N   . GLU   B 1 309 ? -35.242 -1.557  -21.740 1.00 40.03 ? 306 GLU   B N   1 
ATOM   5114 C CA  . GLU   B 1 309 ? -35.777 -1.721  -20.393 1.00 42.81 ? 306 GLU   B CA  1 
ATOM   5115 C C   . GLU   B 1 309 ? -37.163 -1.108  -20.253 1.00 42.46 ? 306 GLU   B C   1 
ATOM   5116 O O   . GLU   B 1 309 ? -38.043 -1.699  -19.619 1.00 45.36 ? 306 GLU   B O   1 
ATOM   5117 C CB  . GLU   B 1 309 ? -34.832 -1.103  -19.360 1.00 40.41 ? 306 GLU   B CB  1 
ATOM   5118 C CG  . GLU   B 1 309 ? -33.427 -1.669  -19.379 1.00 41.29 ? 306 GLU   B CG  1 
ATOM   5119 C CD  . GLU   B 1 309 ? -32.524 -1.048  -18.312 1.00 44.37 ? 306 GLU   B CD  1 
ATOM   5120 O OE1 . GLU   B 1 309 ? -33.044 -0.533  -17.290 1.00 39.95 ? 306 GLU   B OE1 1 
ATOM   5121 O OE2 . GLU   B 1 309 ? -31.285 -1.081  -18.503 1.00 45.79 ? 306 GLU   B OE2 1 
ATOM   5122 N N   . LEU   B 1 310 ? -37.370 0.091   -20.793 1.00 46.19 ? 307 LEU   B N   1 
ATOM   5123 C CA  . LEU   B 1 310 ? -38.633 0.779   -20.556 1.00 41.26 ? 307 LEU   B CA  1 
ATOM   5124 C C   . LEU   B 1 310 ? -39.699 0.433   -21.585 1.00 42.10 ? 307 LEU   B C   1 
ATOM   5125 O O   . LEU   B 1 310 ? -40.885 0.366   -21.233 1.00 39.26 ? 307 LEU   B O   1 
ATOM   5126 C CB  . LEU   B 1 310 ? -38.426 2.294   -20.533 1.00 45.59 ? 307 LEU   B CB  1 
ATOM   5127 C CG  . LEU   B 1 310 ? -37.939 2.916   -19.222 1.00 40.24 ? 307 LEU   B CG  1 
ATOM   5128 C CD1 . LEU   B 1 310 ? -38.272 4.398   -19.218 1.00 44.75 ? 307 LEU   B CD1 1 
ATOM   5129 C CD2 . LEU   B 1 310 ? -38.537 2.219   -18.012 1.00 47.99 ? 307 LEU   B CD2 1 
ATOM   5130 N N   . GLY   B 1 311 ? -39.297 0.204   -22.837 1.00 41.34 ? 308 GLY   B N   1 
ATOM   5131 C CA  . GLY   B 1 311 ? -40.269 -0.057  -23.888 1.00 45.41 ? 308 GLY   B CA  1 
ATOM   5132 C C   . GLY   B 1 311 ? -41.190 -1.217  -23.562 1.00 48.52 ? 308 GLY   B C   1 
ATOM   5133 O O   . GLY   B 1 311 ? -42.413 -1.115  -23.706 1.00 47.50 ? 308 GLY   B O   1 
ATOM   5134 N N   . GLY   B 1 312 ? -40.618 -2.335  -23.123 1.00 50.20 ? 309 GLY   B N   1 
ATOM   5135 C CA  . GLY   B 1 312 ? -41.422 -3.486  -22.765 1.00 55.94 ? 309 GLY   B CA  1 
ATOM   5136 C C   . GLY   B 1 312 ? -42.451 -3.165  -21.701 1.00 55.52 ? 309 GLY   B C   1 
ATOM   5137 O O   . GLY   B 1 312 ? -43.662 -3.292  -21.931 1.00 55.98 ? 309 GLY   B O   1 
ATOM   5138 N N   . LEU   B 1 313 ? -41.968 -2.724  -20.536 1.00 54.70 ? 310 LEU   B N   1 
ATOM   5139 C CA  . LEU   B 1 313 ? -42.853 -2.388  -19.425 1.00 52.37 ? 310 LEU   B CA  1 
ATOM   5140 C C   . LEU   B 1 313 ? -44.003 -1.499  -19.868 1.00 50.47 ? 310 LEU   B C   1 
ATOM   5141 O O   . LEU   B 1 313 ? -45.150 -1.703  -19.458 1.00 54.69 ? 310 LEU   B O   1 
ATOM   5142 C CB  . LEU   B 1 313 ? -42.048 -1.707  -18.317 1.00 55.32 ? 310 LEU   B CB  1 
ATOM   5143 C CG  . LEU   B 1 313 ? -40.764 -2.449  -17.935 1.00 57.68 ? 310 LEU   B CG  1 
ATOM   5144 C CD1 . LEU   B 1 313 ? -39.853 -1.584  -17.083 1.00 53.24 ? 310 LEU   B CD1 1 
ATOM   5145 C CD2 . LEU   B 1 313 ? -41.111 -3.744  -17.204 1.00 57.35 ? 310 LEU   B CD2 1 
ATOM   5146 N N   . VAL   B 1 314 ? -43.721 -0.515  -20.721 1.00 48.42 ? 311 VAL   B N   1 
ATOM   5147 C CA  . VAL   B 1 314 ? -44.736 0.472   -21.085 1.00 52.64 ? 311 VAL   B CA  1 
ATOM   5148 C C   . VAL   B 1 314 ? -45.852 -0.170  -21.904 1.00 57.36 ? 311 VAL   B C   1 
ATOM   5149 O O   . VAL   B 1 314 ? -47.036 -0.053  -21.564 1.00 61.65 ? 311 VAL   B O   1 
ATOM   5150 C CB  . VAL   B 1 314 ? -44.107 1.655   -21.842 1.00 46.68 ? 311 VAL   B CB  1 
ATOM   5151 C CG1 . VAL   B 1 314 ? -45.200 2.462   -22.536 1.00 43.04 ? 311 VAL   B CG1 1 
ATOM   5152 C CG2 . VAL   B 1 314 ? -43.300 2.531   -20.892 1.00 40.91 ? 311 VAL   B CG2 1 
ATOM   5153 N N   . ARG   B 1 315 ? -45.497 -0.829  -23.016 1.00 60.96 ? 312 ARG   B N   1 
ATOM   5154 C CA  . ARG   B 1 315 ? -46.527 -1.265  -23.960 1.00 59.62 ? 312 ARG   B CA  1 
ATOM   5155 C C   . ARG   B 1 315 ? -47.543 -2.195  -23.304 1.00 62.25 ? 312 ARG   B C   1 
ATOM   5156 O O   . ARG   B 1 315 ? -48.713 -2.214  -23.709 1.00 63.75 ? 312 ARG   B O   1 
ATOM   5157 C CB  . ARG   B 1 315 ? -45.899 -1.927  -25.195 1.00 59.76 ? 312 ARG   B CB  1 
ATOM   5158 C CG  . ARG   B 1 315 ? -44.628 -2.734  -24.964 1.00 55.81 ? 312 ARG   B CG  1 
ATOM   5159 C CD  . ARG   B 1 315 ? -44.115 -3.333  -26.283 1.00 60.38 ? 312 ARG   B CD  1 
ATOM   5160 N NE  . ARG   B 1 315 ? -44.108 -2.370  -27.384 1.00 59.87 ? 312 ARG   B NE  1 
ATOM   5161 C CZ  . ARG   B 1 315 ? -43.026 -1.756  -27.849 1.00 59.00 ? 312 ARG   B CZ  1 
ATOM   5162 N NH1 . ARG   B 1 315 ? -41.827 -1.975  -27.330 1.00 60.99 ? 312 ARG   B NH1 1 
ATOM   5163 N NH2 . ARG   B 1 315 ? -43.149 -0.901  -28.863 1.00 55.31 ? 312 ARG   B NH2 1 
ATOM   5164 N N   . ARG   B 1 316 ? -47.129 -2.953  -22.285 1.00 62.76 ? 313 ARG   B N   1 
ATOM   5165 C CA  . ARG   B 1 316 ? -48.045 -3.792  -21.520 1.00 63.30 ? 313 ARG   B CA  1 
ATOM   5166 C C   . ARG   B 1 316 ? -48.837 -3.016  -20.469 1.00 63.30 ? 313 ARG   B C   1 
ATOM   5167 O O   . ARG   B 1 316 ? -49.596 -3.631  -19.714 1.00 59.62 ? 313 ARG   B O   1 
ATOM   5168 C CB  . ARG   B 1 316 ? -47.274 -4.928  -20.845 1.00 62.04 ? 313 ARG   B CB  1 
ATOM   5169 C CG  . ARG   B 1 316 ? -46.798 -5.994  -21.810 1.00 64.19 ? 313 ARG   B CG  1 
ATOM   5170 C CD  . ARG   B 1 316 ? -45.294 -6.089  -21.818 1.00 62.47 ? 313 ARG   B CD  1 
ATOM   5171 N NE  . ARG   B 1 316 ? -44.752 -6.245  -20.476 1.00 58.49 ? 313 ARG   B NE  1 
ATOM   5172 C CZ  . ARG   B 1 316 ? -43.485 -6.537  -20.217 1.00 62.63 ? 313 ARG   B CZ  1 
ATOM   5173 N NH1 . ARG   B 1 316 ? -42.611 -6.734  -21.190 1.00 59.15 ? 313 ARG   B NH1 1 
ATOM   5174 N NH2 . ARG   B 1 316 ? -43.084 -6.636  -18.950 1.00 62.82 ? 313 ARG   B NH2 1 
ATOM   5175 N N   . GLN   B 1 317 ? -48.675 -1.690  -20.411 1.00 63.59 ? 314 GLN   B N   1 
ATOM   5176 C CA  . GLN   B 1 317 ? -49.353 -0.807  -19.455 1.00 62.43 ? 314 GLN   B CA  1 
ATOM   5177 C C   . GLN   B 1 317 ? -49.050 -1.161  -18.000 1.00 63.62 ? 314 GLN   B C   1 
ATOM   5178 O O   . GLN   B 1 317 ? -49.765 -0.716  -17.092 1.00 56.16 ? 314 GLN   B O   1 
ATOM   5179 C CB  . GLN   B 1 317 ? -50.867 -0.788  -19.688 1.00 63.88 ? 314 GLN   B CB  1 
ATOM   5180 C CG  . GLN   B 1 317 ? -51.252 -0.495  -21.129 1.00 66.26 ? 314 GLN   B CG  1 
ATOM   5181 C CD  . GLN   B 1 317 ? -52.652 0.074   -21.258 1.00 74.00 ? 314 GLN   B CD  1 
ATOM   5182 O OE1 . GLN   B 1 317 ? -53.120 0.811   -20.386 1.00 73.47 ? 314 GLN   B OE1 1 
ATOM   5183 N NE2 . GLN   B 1 317 ? -53.331 -0.265  -22.349 1.00 71.25 ? 314 GLN   B NE2 1 
ATOM   5184 N N   . GLU   B 1 318 ? -48.000 -1.958  -17.768 1.00 56.85 ? 315 GLU   B N   1 
ATOM   5185 C CA  . GLU   B 1 318 ? -47.497 -2.171  -16.412 1.00 56.76 ? 315 GLU   B CA  1 
ATOM   5186 C C   . GLU   B 1 318 ? -46.870 -0.895  -15.863 1.00 59.54 ? 315 GLU   B C   1 
ATOM   5187 O O   . GLU   B 1 318 ? -47.256 -0.402  -14.796 1.00 56.44 ? 315 GLU   B O   1 
ATOM   5188 C CB  . GLU   B 1 318 ? -46.485 -3.311  -16.423 1.00 54.44 ? 315 GLU   B CB  1 
ATOM   5189 C CG  . GLU   B 1 318 ? -46.780 -4.306  -17.520 1.00 64.22 ? 315 GLU   B CG  1 
ATOM   5190 C CD  . GLU   B 1 318 ? -45.960 -5.568  -17.410 1.00 70.55 ? 315 GLU   B CD  1 
ATOM   5191 O OE1 . GLU   B 1 318 ? -45.973 -6.355  -18.382 1.00 70.52 ? 315 GLU   B OE1 1 
ATOM   5192 O OE2 . GLU   B 1 318 ? -45.306 -5.769  -16.358 1.00 73.21 ? 315 GLU   B OE2 1 
ATOM   5193 N N   . LEU   B 1 319 ? -45.888 -0.353  -16.584 1.00 57.24 ? 316 LEU   B N   1 
ATOM   5194 C CA  . LEU   B 1 319 ? -45.385 0.993   -16.343 1.00 49.83 ? 316 LEU   B CA  1 
ATOM   5195 C C   . LEU   B 1 319 ? -46.165 1.953   -17.238 1.00 45.62 ? 316 LEU   B C   1 
ATOM   5196 O O   . LEU   B 1 319 ? -46.174 1.799   -18.465 1.00 46.71 ? 316 LEU   B O   1 
ATOM   5197 C CB  . LEU   B 1 319 ? -43.885 1.054   -16.624 1.00 50.31 ? 316 LEU   B CB  1 
ATOM   5198 C CG  . LEU   B 1 319 ? -43.031 1.943   -15.728 1.00 50.68 ? 316 LEU   B CG  1 
ATOM   5199 C CD1 . LEU   B 1 319 ? -41.556 1.614   -15.931 1.00 55.72 ? 316 LEU   B CD1 1 
ATOM   5200 C CD2 . LEU   B 1 319 ? -43.313 3.391   -16.054 1.00 47.57 ? 316 LEU   B CD2 1 
ATOM   5201 N N   . VAL   B 1 320 ? -46.837 2.917   -16.624 1.00 42.79 ? 317 VAL   B N   1 
ATOM   5202 C CA  . VAL   B 1 320 ? -47.835 3.740   -17.299 1.00 47.55 ? 317 VAL   B CA  1 
ATOM   5203 C C   . VAL   B 1 320 ? -47.188 5.028   -17.795 1.00 49.77 ? 317 VAL   B C   1 
ATOM   5204 O O   . VAL   B 1 320 ? -46.676 5.820   -16.995 1.00 48.74 ? 317 VAL   B O   1 
ATOM   5205 C CB  . VAL   B 1 320 ? -49.010 4.051   -16.361 1.00 48.38 ? 317 VAL   B CB  1 
ATOM   5206 C CG1 . VAL   B 1 320 ? -49.728 5.312   -16.803 1.00 48.34 ? 317 VAL   B CG1 1 
ATOM   5207 C CG2 . VAL   B 1 320 ? -49.974 2.873   -16.312 1.00 52.13 ? 317 VAL   B CG2 1 
ATOM   5208 N N   . ALA   B 1 321 ? -47.238 5.242   -19.111 1.00 41.77 ? 318 ALA   B N   1 
ATOM   5209 C CA  . ALA   B 1 321 ? -46.762 6.458   -19.770 1.00 44.71 ? 318 ALA   B CA  1 
ATOM   5210 C C   . ALA   B 1 321 ? -47.920 7.072   -20.559 1.00 43.12 ? 318 ALA   B C   1 
ATOM   5211 O O   . ALA   B 1 321 ? -48.243 6.619   -21.661 1.00 45.29 ? 318 ALA   B O   1 
ATOM   5212 C CB  . ALA   B 1 321 ? -45.578 6.157   -20.686 1.00 37.71 ? 318 ALA   B CB  1 
ATOM   5213 N N   . HIS   B 1 322 ? -48.551 8.090   -19.988 1.00 40.60 ? 319 HIS   B N   1 
ATOM   5214 C CA  . HIS   B 1 322 ? -49.659 8.782   -20.623 1.00 42.12 ? 319 HIS   B CA  1 
ATOM   5215 C C   . HIS   B 1 322 ? -49.163 10.007  -21.386 1.00 39.74 ? 319 HIS   B C   1 
ATOM   5216 O O   . HIS   B 1 322 ? -48.027 10.459  -21.225 1.00 39.04 ? 319 HIS   B O   1 
ATOM   5217 C CB  . HIS   B 1 322 ? -50.691 9.188   -19.574 1.00 41.35 ? 319 HIS   B CB  1 
ATOM   5218 C CG  . HIS   B 1 322 ? -51.433 8.030   -18.981 1.00 44.27 ? 319 HIS   B CG  1 
ATOM   5219 N ND1 . HIS   B 1 322 ? -51.819 7.990   -17.658 1.00 43.49 ? 319 HIS   B ND1 1 
ATOM   5220 C CD2 . HIS   B 1 322 ? -51.862 6.872   -19.535 1.00 44.06 ? 319 HIS   B CD2 1 
ATOM   5221 C CE1 . HIS   B 1 322 ? -52.460 6.859   -17.424 1.00 49.39 ? 319 HIS   B CE1 1 
ATOM   5222 N NE2 . HIS   B 1 322 ? -52.495 6.160   -18.544 1.00 45.71 ? 319 HIS   B NE2 1 
ATOM   5223 N N   . GLU   B 1 323 ? -50.038 10.556  -22.222 1.00 38.11 ? 320 GLU   B N   1 
ATOM   5224 C CA  . GLU   B 1 323 ? -49.723 11.802  -22.905 1.00 36.79 ? 320 GLU   B CA  1 
ATOM   5225 C C   . GLU   B 1 323 ? -51.012 12.565  -23.153 1.00 38.40 ? 320 GLU   B C   1 
ATOM   5226 O O   . GLU   B 1 323 ? -52.097 11.978  -23.228 1.00 34.83 ? 320 GLU   B O   1 
ATOM   5227 C CB  . GLU   B 1 323 ? -48.959 11.561  -24.219 1.00 30.52 ? 320 GLU   B CB  1 
ATOM   5228 C CG  . GLU   B 1 323 ? -49.797 11.069  -25.373 1.00 37.93 ? 320 GLU   B CG  1 
ATOM   5229 C CD  . GLU   B 1 323 ? -48.971 10.343  -26.445 1.00 46.70 ? 320 GLU   B CD  1 
ATOM   5230 O OE1 . GLU   B 1 323 ? -47.750 10.639  -26.604 1.00 39.16 ? 320 GLU   B OE1 1 
ATOM   5231 O OE2 . GLU   B 1 323 ? -49.549 9.466   -27.134 1.00 54.02 ? 320 GLU   B OE2 1 
ATOM   5232 N N   . THR   B 1 324 ? -50.878 13.884  -23.239 1.00 35.78 ? 321 THR   B N   1 
ATOM   5233 C CA  . THR   B 1 324 ? -51.963 14.806  -23.566 1.00 34.66 ? 321 THR   B CA  1 
ATOM   5234 C C   . THR   B 1 324 ? -51.501 15.563  -24.807 1.00 33.49 ? 321 THR   B C   1 
ATOM   5235 O O   . THR   B 1 324 ? -50.662 16.464  -24.706 1.00 28.76 ? 321 THR   B O   1 
ATOM   5236 C CB  . THR   B 1 324 ? -52.251 15.757  -22.406 1.00 32.39 ? 321 THR   B CB  1 
ATOM   5237 O OG1 . THR   B 1 324 ? -52.498 15.009  -21.211 1.00 30.22 ? 321 THR   B OG1 1 
ATOM   5238 C CG2 . THR   B 1 324 ? -53.460 16.640  -22.707 1.00 34.48 ? 321 THR   B CG2 1 
ATOM   5239 N N   . VAL   B 1 325 ? -52.024 15.190  -25.972 1.00 29.77 ? 322 VAL   B N   1 
ATOM   5240 C CA  . VAL   B 1 325 ? -51.588 15.746  -27.249 1.00 30.06 ? 322 VAL   B CA  1 
ATOM   5241 C C   . VAL   B 1 325 ? -52.631 16.750  -27.719 1.00 32.27 ? 322 VAL   B C   1 
ATOM   5242 O O   . VAL   B 1 325 ? -53.748 16.371  -28.083 1.00 33.64 ? 322 VAL   B O   1 
ATOM   5243 C CB  . VAL   B 1 325 ? -51.378 14.653  -28.302 1.00 33.56 ? 322 VAL   B CB  1 
ATOM   5244 C CG1 . VAL   B 1 325 ? -50.897 15.280  -29.608 1.00 32.58 ? 322 VAL   B CG1 1 
ATOM   5245 C CG2 . VAL   B 1 325 ? -50.409 13.592  -27.791 1.00 33.77 ? 322 VAL   B CG2 1 
ATOM   5246 N N   . GLN   B 1 326 ? -52.277 18.030  -27.717 1.00 32.78 ? 323 GLN   B N   1 
ATOM   5247 C CA  . GLN   B 1 326 ? -53.129 19.042  -28.321 1.00 33.99 ? 323 GLN   B CA  1 
ATOM   5248 C C   . GLN   B 1 326 ? -52.865 19.125  -29.822 1.00 34.20 ? 323 GLN   B C   1 
ATOM   5249 O O   . GLN   B 1 326 ? -51.751 18.889  -30.286 1.00 33.16 ? 323 GLN   B O   1 
ATOM   5250 C CB  . GLN   B 1 326 ? -52.890 20.399  -27.656 1.00 32.83 ? 323 GLN   B CB  1 
ATOM   5251 C CG  . GLN   B 1 326 ? -53.750 21.522  -28.215 1.00 41.43 ? 323 GLN   B CG  1 
ATOM   5252 C CD  . GLN   B 1 326 ? -55.233 21.281  -27.984 1.00 53.31 ? 323 GLN   B CD  1 
ATOM   5253 O OE1 . GLN   B 1 326 ? -56.046 21.402  -28.909 1.00 54.35 ? 323 GLN   B OE1 1 
ATOM   5254 N NE2 . GLN   B 1 326 ? -55.592 20.922  -26.748 1.00 51.31 ? 323 GLN   B NE2 1 
ATOM   5255 N N   . ASP   B 1 327 ? -53.900 19.460  -30.587 1.00 35.40 ? 324 ASP   B N   1 
ATOM   5256 C CA  . ASP   B 1 327 ? -53.765 19.596  -32.033 1.00 35.49 ? 324 ASP   B CA  1 
ATOM   5257 C C   . ASP   B 1 327 ? -53.624 21.061  -32.416 1.00 33.28 ? 324 ASP   B C   1 
ATOM   5258 O O   . ASP   B 1 327 ? -54.326 21.928  -31.882 1.00 29.70 ? 324 ASP   B O   1 
ATOM   5259 C CB  . ASP   B 1 327 ? -54.965 19.006  -32.782 1.00 39.64 ? 324 ASP   B CB  1 
ATOM   5260 C CG  . ASP   B 1 327 ? -54.939 17.494  -32.855 1.00 49.54 ? 324 ASP   B CG  1 
ATOM   5261 O OD1 . ASP   B 1 327 ? -53.871 16.876  -32.634 1.00 45.56 ? 324 ASP   B OD1 1 
ATOM   5262 O OD2 . ASP   B 1 327 ? -56.006 16.914  -33.157 1.00 58.96 ? 324 ASP   B OD2 1 
ATOM   5263 N N   . GLY   B 1 328 ? -52.714 21.335  -33.347 1.00 32.38 ? 325 GLY   B N   1 
ATOM   5264 C CA  . GLY   B 1 328 ? -52.710 22.641  -33.977 1.00 27.31 ? 325 GLY   B CA  1 
ATOM   5265 C C   . GLY   B 1 328 ? -51.568 23.548  -33.577 1.00 27.60 ? 325 GLY   B C   1 
ATOM   5266 O O   . GLY   B 1 328 ? -51.448 23.940  -32.412 1.00 25.38 ? 325 GLY   B O   1 
ATOM   5267 N N   . PHE   B 1 329 ? -50.748 23.917  -34.569 1.00 25.23 ? 326 PHE   B N   1 
ATOM   5268 C CA  . PHE   B 1 329 ? -49.621 24.814  -34.333 1.00 25.11 ? 326 PHE   B CA  1 
ATOM   5269 C C   . PHE   B 1 329 ? -50.066 26.102  -33.653 1.00 22.75 ? 326 PHE   B C   1 
ATOM   5270 O O   . PHE   B 1 329 ? -49.372 26.626  -32.767 1.00 21.31 ? 326 PHE   B O   1 
ATOM   5271 C CB  . PHE   B 1 329 ? -48.924 25.106  -35.669 1.00 24.12 ? 326 PHE   B CB  1 
ATOM   5272 C CG  . PHE   B 1 329 ? -47.684 25.949  -35.546 1.00 23.89 ? 326 PHE   B CG  1 
ATOM   5273 C CD1 . PHE   B 1 329 ? -46.455 25.355  -35.301 1.00 22.64 ? 326 PHE   B CD1 1 
ATOM   5274 C CD2 . PHE   B 1 329 ? -47.744 27.329  -35.701 1.00 20.79 ? 326 PHE   B CD2 1 
ATOM   5275 C CE1 . PHE   B 1 329 ? -45.289 26.121  -35.187 1.00 21.22 ? 326 PHE   B CE1 1 
ATOM   5276 C CE2 . PHE   B 1 329 ? -46.587 28.107  -35.589 1.00 22.25 ? 326 PHE   B CE2 1 
ATOM   5277 C CZ  . PHE   B 1 329 ? -45.351 27.485  -35.330 1.00 20.90 ? 326 PHE   B CZ  1 
ATOM   5278 N N   . GLU   B 1 330 ? -51.230 26.635  -34.041 1.00 26.14 ? 327 GLU   B N   1 
ATOM   5279 C CA  . GLU   B 1 330 ? -51.682 27.890  -33.442 1.00 26.38 ? 327 GLU   B CA  1 
ATOM   5280 C C   . GLU   B 1 330 ? -51.983 27.760  -31.948 1.00 21.25 ? 327 GLU   B C   1 
ATOM   5281 O O   . GLU   B 1 330 ? -52.164 28.781  -31.269 1.00 23.68 ? 327 GLU   B O   1 
ATOM   5282 C CB  . GLU   B 1 330 ? -52.922 28.413  -34.195 1.00 27.21 ? 327 GLU   B CB  1 
ATOM   5283 C CG  . GLU   B 1 330 ? -54.162 27.506  -34.095 1.00 30.63 ? 327 GLU   B CG  1 
ATOM   5284 C CD  . GLU   B 1 330 ? -54.193 26.376  -35.132 1.00 39.31 ? 327 GLU   B CD  1 
ATOM   5285 O OE1 . GLU   B 1 330 ? -53.136 25.786  -35.466 1.00 39.51 ? 327 GLU   B OE1 1 
ATOM   5286 O OE2 . GLU   B 1 330 ? -55.302 26.071  -35.618 1.00 48.70 ? 327 GLU   B OE2 1 
ATOM   5287 N N   . HIS   B 1 331 ? -52.041 26.544  -31.410 1.00 24.39 ? 328 HIS   B N   1 
ATOM   5288 C CA  . HIS   B 1 331 ? -52.377 26.362  -30.004 1.00 27.16 ? 328 HIS   B CA  1 
ATOM   5289 C C   . HIS   B 1 331 ? -51.163 26.083  -29.118 1.00 26.88 ? 328 HIS   B C   1 
ATOM   5290 O O   . HIS   B 1 331 ? -51.338 25.814  -27.926 1.00 25.61 ? 328 HIS   B O   1 
ATOM   5291 C CB  . HIS   B 1 331 ? -53.394 25.229  -29.865 1.00 25.92 ? 328 HIS   B CB  1 
ATOM   5292 C CG  . HIS   B 1 331 ? -54.687 25.509  -30.558 1.00 30.20 ? 328 HIS   B CG  1 
ATOM   5293 N ND1 . HIS   B 1 331 ? -55.383 26.686  -30.377 1.00 31.52 ? 328 HIS   B ND1 1 
ATOM   5294 C CD2 . HIS   B 1 331 ? -55.407 24.775  -31.439 1.00 34.49 ? 328 HIS   B CD2 1 
ATOM   5295 C CE1 . HIS   B 1 331 ? -56.473 26.668  -31.126 1.00 34.86 ? 328 HIS   B CE1 1 
ATOM   5296 N NE2 . HIS   B 1 331 ? -56.510 25.521  -31.781 1.00 35.40 ? 328 HIS   B NE2 1 
ATOM   5297 N N   . ILE   B 1 332 ? -49.936 26.145  -29.661 1.00 25.09 ? 329 ILE   B N   1 
ATOM   5298 C CA  . ILE   B 1 332 ? -48.757 25.806  -28.850 1.00 24.99 ? 329 ILE   B CA  1 
ATOM   5299 C C   . ILE   B 1 332 ? -48.652 26.677  -27.603 1.00 23.64 ? 329 ILE   B C   1 
ATOM   5300 O O   . ILE   B 1 332 ? -48.481 26.123  -26.501 1.00 23.46 ? 329 ILE   B O   1 
ATOM   5301 C CB  . ILE   B 1 332 ? -47.487 25.830  -29.716 1.00 25.02 ? 329 ILE   B CB  1 
ATOM   5302 C CG1 . ILE   B 1 332 ? -47.546 24.705  -30.740 1.00 21.58 ? 329 ILE   B CG1 1 
ATOM   5303 C CG2 . ILE   B 1 332 ? -46.238 25.654  -28.826 1.00 21.21 ? 329 ILE   B CG2 1 
ATOM   5304 C CD1 . ILE   B 1 332 ? -46.502 24.787  -31.807 1.00 22.50 ? 329 ILE   B CD1 1 
ATOM   5305 N N   . PRO   B 1 333 ? -48.761 28.008  -27.675 1.00 23.84 ? 330 PRO   B N   1 
ATOM   5306 C CA  . PRO   B 1 333 ? -48.631 28.806  -26.437 1.00 22.36 ? 330 PRO   B CA  1 
ATOM   5307 C C   . PRO   B 1 333 ? -49.731 28.530  -25.421 1.00 26.41 ? 330 PRO   B C   1 
ATOM   5308 O O   . PRO   B 1 333 ? -49.482 28.612  -24.206 1.00 24.11 ? 330 PRO   B O   1 
ATOM   5309 C CB  . PRO   B 1 333 ? -48.667 30.264  -26.936 1.00 21.12 ? 330 PRO   B CB  1 
ATOM   5310 C CG  . PRO   B 1 333 ? -48.284 30.172  -28.408 1.00 24.82 ? 330 PRO   B CG  1 
ATOM   5311 C CD  . PRO   B 1 333 ? -48.829 28.849  -28.889 1.00 22.10 ? 330 PRO   B CD  1 
ATOM   5312 N N   . ALA   B 1 334 ? -50.944 28.211  -25.883 1.00 26.87 ? 331 ALA   B N   1 
ATOM   5313 C CA  . ALA   B 1 334 ? -52.033 27.908  -24.962 1.00 28.36 ? 331 ALA   B CA  1 
ATOM   5314 C C   . ALA   B 1 334 ? -51.801 26.575  -24.260 1.00 24.12 ? 331 ALA   B C   1 
ATOM   5315 O O   . ALA   B 1 334 ? -52.054 26.448  -23.058 1.00 27.32 ? 331 ALA   B O   1 
ATOM   5316 C CB  . ALA   B 1 334 ? -53.369 27.903  -25.710 1.00 30.20 ? 331 ALA   B CB  1 
ATOM   5317 N N   . ALA   B 1 335 ? -51.314 25.570  -24.992 1.00 24.02 ? 332 ALA   B N   1 
ATOM   5318 C CA  . ALA   B 1 335 ? -50.931 24.316  -24.353 1.00 27.18 ? 332 ALA   B CA  1 
ATOM   5319 C C   . ALA   B 1 335 ? -49.843 24.552  -23.313 1.00 28.41 ? 332 ALA   B C   1 
ATOM   5320 O O   . ALA   B 1 335 ? -49.946 24.094  -22.166 1.00 26.88 ? 332 ALA   B O   1 
ATOM   5321 C CB  . ALA   B 1 335 ? -50.469 23.312  -25.402 1.00 26.26 ? 332 ALA   B CB  1 
ATOM   5322 N N   . TYR   B 1 336 ? -48.793 25.278  -23.696 1.00 24.08 ? 333 TYR   B N   1 
ATOM   5323 C CA  . TYR   B 1 336 ? -47.748 25.659  -22.752 1.00 23.53 ? 333 TYR   B CA  1 
ATOM   5324 C C   . TYR   B 1 336 ? -48.349 26.317  -21.512 1.00 26.77 ? 333 TYR   B C   1 
ATOM   5325 O O   . TYR   B 1 336 ? -48.005 25.974  -20.379 1.00 24.08 ? 333 TYR   B O   1 
ATOM   5326 C CB  . TYR   B 1 336 ? -46.760 26.588  -23.467 1.00 21.83 ? 333 TYR   B CB  1 
ATOM   5327 C CG  . TYR   B 1 336 ? -45.652 27.183  -22.645 1.00 22.65 ? 333 TYR   B CG  1 
ATOM   5328 C CD1 . TYR   B 1 336 ? -44.637 26.387  -22.103 1.00 23.18 ? 333 TYR   B CD1 1 
ATOM   5329 C CD2 . TYR   B 1 336 ? -45.595 28.559  -22.434 1.00 23.01 ? 333 TYR   B CD2 1 
ATOM   5330 C CE1 . TYR   B 1 336 ? -43.598 26.971  -21.356 1.00 24.50 ? 333 TYR   B CE1 1 
ATOM   5331 C CE2 . TYR   B 1 336 ? -44.579 29.142  -21.701 1.00 22.08 ? 333 TYR   B CE2 1 
ATOM   5332 C CZ  . TYR   B 1 336 ? -43.586 28.341  -21.159 1.00 21.96 ? 333 TYR   B CZ  1 
ATOM   5333 O OH  . TYR   B 1 336 ? -42.588 28.941  -20.432 1.00 24.35 ? 333 TYR   B OH  1 
ATOM   5334 N N   . GLN   B 1 337 ? -49.298 27.233  -21.711 1.00 26.46 ? 334 GLN   B N   1 
ATOM   5335 C CA  . GLN   B 1 337 ? -49.879 27.954  -20.579 1.00 26.15 ? 334 GLN   B CA  1 
ATOM   5336 C C   . GLN   B 1 337 ? -50.521 27.000  -19.566 1.00 25.97 ? 334 GLN   B C   1 
ATOM   5337 O O   . GLN   B 1 337 ? -50.449 27.245  -18.354 1.00 27.45 ? 334 GLN   B O   1 
ATOM   5338 C CB  . GLN   B 1 337 ? -50.909 28.971  -21.071 1.00 29.18 ? 334 GLN   B CB  1 
ATOM   5339 C CG  . GLN   B 1 337 ? -51.455 29.870  -19.980 1.00 26.61 ? 334 GLN   B CG  1 
ATOM   5340 C CD  . GLN   B 1 337 ? -50.435 30.865  -19.505 1.00 34.23 ? 334 GLN   B CD  1 
ATOM   5341 O OE1 . GLN   B 1 337 ? -50.003 31.747  -20.261 1.00 30.01 ? 334 GLN   B OE1 1 
ATOM   5342 N NE2 . GLN   B 1 337 ? -50.038 30.742  -18.242 1.00 31.23 ? 334 GLN   B NE2 1 
ATOM   5343 N N   . THR   B 1 338 ? -51.131 25.895  -20.037 1.00 25.93 ? 335 THR   B N   1 
ATOM   5344 C CA  . THR   B 1 338 ? -51.838 25.006  -19.110 1.00 27.25 ? 335 THR   B CA  1 
ATOM   5345 C C   . THR   B 1 338 ? -50.893 24.406  -18.077 1.00 32.98 ? 335 THR   B C   1 
ATOM   5346 O O   . THR   B 1 338 ? -51.329 24.026  -16.978 1.00 25.08 ? 335 THR   B O   1 
ATOM   5347 C CB  . THR   B 1 338 ? -52.571 23.870  -19.831 1.00 30.30 ? 335 THR   B CB  1 
ATOM   5348 O OG1 . THR   B 1 338 ? -51.633 22.932  -20.389 1.00 23.89 ? 335 THR   B OG1 1 
ATOM   5349 C CG2 . THR   B 1 338 ? -53.532 24.397  -20.931 1.00 28.74 ? 335 THR   B CG2 1 
ATOM   5350 N N   . LEU   B 1 339 ? -49.603 24.294  -18.415 1.00 26.37 ? 336 LEU   B N   1 
ATOM   5351 C CA  . LEU   B 1 339 ? -48.631 23.762  -17.466 1.00 27.05 ? 336 LEU   B CA  1 
ATOM   5352 C C   . LEU   B 1 339 ? -48.631 24.564  -16.180 1.00 26.24 ? 336 LEU   B C   1 
ATOM   5353 O O   . LEU   B 1 339 ? -48.469 24.006  -15.091 1.00 27.31 ? 336 LEU   B O   1 
ATOM   5354 C CB  . LEU   B 1 339 ? -47.228 23.773  -18.083 1.00 25.57 ? 336 LEU   B CB  1 
ATOM   5355 C CG  . LEU   B 1 339 ? -46.936 22.843  -19.249 1.00 25.00 ? 336 LEU   B CG  1 
ATOM   5356 C CD1 . LEU   B 1 339 ? -45.482 23.049  -19.693 1.00 25.38 ? 336 LEU   B CD1 1 
ATOM   5357 C CD2 . LEU   B 1 339 ? -47.183 21.394  -18.861 1.00 29.39 ? 336 LEU   B CD2 1 
ATOM   5358 N N   . PHE   B 1 340 ? -48.802 25.876  -16.283 1.00 28.11 ? 337 PHE   B N   1 
ATOM   5359 C CA  . PHE   B 1 340 ? -48.705 26.760  -15.131 1.00 27.24 ? 337 PHE   B CA  1 
ATOM   5360 C C   . PHE   B 1 340 ? -50.052 27.141  -14.547 1.00 30.94 ? 337 PHE   B C   1 
ATOM   5361 O O   . PHE   B 1 340 ? -50.139 27.406  -13.351 1.00 31.11 ? 337 PHE   B O   1 
ATOM   5362 C CB  . PHE   B 1 340 ? -47.971 28.047  -15.520 1.00 22.66 ? 337 PHE   B CB  1 
ATOM   5363 C CG  . PHE   B 1 340 ? -46.656 27.798  -16.208 1.00 29.76 ? 337 PHE   B CG  1 
ATOM   5364 C CD1 . PHE   B 1 340 ? -46.598 27.617  -17.582 1.00 26.53 ? 337 PHE   B CD1 1 
ATOM   5365 C CD2 . PHE   B 1 340 ? -45.482 27.720  -15.480 1.00 26.98 ? 337 PHE   B CD2 1 
ATOM   5366 C CE1 . PHE   B 1 340 ? -45.387 27.381  -18.218 1.00 30.05 ? 337 PHE   B CE1 1 
ATOM   5367 C CE2 . PHE   B 1 340 ? -44.267 27.475  -16.112 1.00 28.12 ? 337 PHE   B CE2 1 
ATOM   5368 C CZ  . PHE   B 1 340 ? -44.229 27.320  -17.488 1.00 25.66 ? 337 PHE   B CZ  1 
ATOM   5369 N N   . SER   B 1 341 ? -51.098 27.182  -15.364 1.00 29.09 ? 338 SER   B N   1 
ATOM   5370 C CA  . SER   B 1 341 ? -52.334 27.858  -15.007 1.00 34.85 ? 338 SER   B CA  1 
ATOM   5371 C C   . SER   B 1 341 ? -53.559 26.960  -14.967 1.00 32.16 ? 338 SER   B C   1 
ATOM   5372 O O   . SER   B 1 341 ? -54.533 27.312  -14.300 1.00 38.30 ? 338 SER   B O   1 
ATOM   5373 C CB  . SER   B 1 341 ? -52.605 29.005  -15.998 1.00 32.56 ? 338 SER   B CB  1 
ATOM   5374 O OG  . SER   B 1 341 ? -51.532 29.928  -15.971 1.00 28.28 ? 338 SER   B OG  1 
ATOM   5375 N N   . ALA   B 1 342 ? -53.538 25.825  -15.646 1.00 33.78 ? 339 ALA   B N   1 
ATOM   5376 C CA  . ALA   B 1 342 ? -54.725 25.001  -15.815 1.00 37.93 ? 339 ALA   B CA  1 
ATOM   5377 C C   . ALA   B 1 342 ? -54.293 23.575  -16.106 1.00 34.45 ? 339 ALA   B C   1 
ATOM   5378 O O   . ALA   B 1 342 ? -54.675 22.999  -17.135 1.00 36.52 ? 339 ALA   B O   1 
ATOM   5379 C CB  . ALA   B 1 342 ? -55.607 25.563  -16.950 1.00 36.53 ? 339 ALA   B CB  1 
ATOM   5380 N N   . SER   B 1 343 ? -53.497 22.998  -15.215 1.00 30.85 ? 340 SER   B N   1 
ATOM   5381 C CA  . SER   B 1 343 ? -52.966 21.658  -15.439 1.00 31.03 ? 340 SER   B CA  1 
ATOM   5382 C C   . SER   B 1 343 ? -53.891 20.544  -14.953 1.00 36.21 ? 340 SER   B C   1 
ATOM   5383 O O   . SER   B 1 343 ? -53.564 19.366  -15.157 1.00 29.12 ? 340 SER   B O   1 
ATOM   5384 C CB  . SER   B 1 343 ? -51.601 21.512  -14.750 1.00 34.14 ? 340 SER   B CB  1 
ATOM   5385 O OG  . SER   B 1 343 ? -51.679 21.724  -13.346 1.00 34.46 ? 340 SER   B OG  1 
ATOM   5386 N N   . GLU   B 1 344 ? -55.031 20.881  -14.328 1.00 35.34 ? 341 GLU   B N   1 
ATOM   5387 C CA  . GLU   B 1 344 ? -55.853 19.868  -13.661 1.00 38.16 ? 341 GLU   B CA  1 
ATOM   5388 C C   . GLU   B 1 344 ? -56.233 18.733  -14.600 1.00 40.12 ? 341 GLU   B C   1 
ATOM   5389 O O   . GLU   B 1 344 ? -56.305 17.573  -14.182 1.00 42.50 ? 341 GLU   B O   1 
ATOM   5390 C CB  . GLU   B 1 344 ? -57.116 20.500  -13.065 1.00 40.28 ? 341 GLU   B CB  1 
ATOM   5391 C CG  . GLU   B 1 344 ? -56.844 21.613  -12.062 1.00 42.69 ? 341 GLU   B CG  1 
ATOM   5392 C CD  . GLU   B 1 344 ? -56.592 22.966  -12.733 1.00 49.72 ? 341 GLU   B CD  1 
ATOM   5393 O OE1 . GLU   B 1 344 ? -56.957 23.133  -13.925 1.00 48.20 ? 341 GLU   B OE1 1 
ATOM   5394 O OE2 . GLU   B 1 344 ? -56.032 23.870  -12.064 1.00 54.29 ? 341 GLU   B OE2 1 
ATOM   5395 N N   . SER   B 1 345 ? -56.469 19.046  -15.882 1.00 34.03 ? 342 SER   B N   1 
ATOM   5396 C CA  . SER   B 1 345 ? -56.904 18.069  -16.878 1.00 36.77 ? 342 SER   B CA  1 
ATOM   5397 C C   . SER   B 1 345 ? -55.756 17.368  -17.596 1.00 41.12 ? 342 SER   B C   1 
ATOM   5398 O O   . SER   B 1 345 ? -56.002 16.381  -18.300 1.00 40.07 ? 342 SER   B O   1 
ATOM   5399 C CB  . SER   B 1 345 ? -57.795 18.747  -17.934 1.00 40.12 ? 342 SER   B CB  1 
ATOM   5400 O OG  . SER   B 1 345 ? -58.937 19.339  -17.332 1.00 54.10 ? 342 SER   B OG  1 
ATOM   5401 N N   . ASN   B 1 346 ? -54.524 17.857  -17.448 1.00 35.43 ? 343 ASN   B N   1 
ATOM   5402 C CA  . ASN   B 1 346 ? -53.381 17.274  -18.134 1.00 31.02 ? 343 ASN   B CA  1 
ATOM   5403 C C   . ASN   B 1 346 ? -52.982 15.948  -17.492 1.00 33.02 ? 343 ASN   B C   1 
ATOM   5404 O O   . ASN   B 1 346 ? -53.080 15.766  -16.275 1.00 36.09 ? 343 ASN   B O   1 
ATOM   5405 C CB  . ASN   B 1 346 ? -52.201 18.242  -18.087 1.00 33.23 ? 343 ASN   B CB  1 
ATOM   5406 C CG  . ASN   B 1 346 ? -52.383 19.435  -19.012 1.00 34.14 ? 343 ASN   B CG  1 
ATOM   5407 O OD1 . ASN   B 1 346 ? -53.159 19.387  -19.967 1.00 34.10 ? 343 ASN   B OD1 1 
ATOM   5408 N ND2 . ASN   B 1 346 ? -51.636 20.503  -18.748 1.00 28.75 ? 343 ASN   B ND2 1 
ATOM   5409 N N   . ARG   B 1 347 ? -52.521 15.017  -18.329 1.00 34.24 ? 344 ARG   B N   1 
ATOM   5410 C CA  . ARG   B 1 347 ? -52.061 13.703  -17.888 1.00 36.38 ? 344 ARG   B CA  1 
ATOM   5411 C C   . ARG   B 1 347 ? -50.808 13.331  -18.665 1.00 33.38 ? 344 ARG   B C   1 
ATOM   5412 O O   . ARG   B 1 347 ? -50.813 13.333  -19.901 1.00 28.92 ? 344 ARG   B O   1 
ATOM   5413 C CB  . ARG   B 1 347 ? -53.128 12.607  -18.099 1.00 39.73 ? 344 ARG   B CB  1 
ATOM   5414 C CG  . ARG   B 1 347 ? -54.418 12.766  -17.299 1.00 41.64 ? 344 ARG   B CG  1 
ATOM   5415 C CD  . ARG   B 1 347 ? -54.190 12.653  -15.799 1.00 43.59 ? 344 ARG   B CD  1 
ATOM   5416 N NE  . ARG   B 1 347 ? -55.432 12.722  -15.029 1.00 41.26 ? 344 ARG   B NE  1 
ATOM   5417 C CZ  . ARG   B 1 347 ? -55.948 13.833  -14.515 1.00 43.43 ? 344 ARG   B CZ  1 
ATOM   5418 N NH1 . ARG   B 1 347 ? -55.389 15.016  -14.714 1.00 42.97 ? 344 ARG   B NH1 1 
ATOM   5419 N NH2 . ARG   B 1 347 ? -57.051 13.757  -13.774 1.00 40.82 ? 344 ARG   B NH2 1 
ATOM   5420 N N   . GLY   B 1 348 ? -49.748 12.977  -17.948 1.00 34.01 ? 345 GLY   B N   1 
ATOM   5421 C CA  . GLY   B 1 348 ? -48.550 12.571  -18.656 1.00 34.50 ? 345 GLY   B CA  1 
ATOM   5422 C C   . GLY   B 1 348 ? -47.893 13.737  -19.388 1.00 28.49 ? 345 GLY   B C   1 
ATOM   5423 O O   . GLY   B 1 348 ? -47.981 14.900  -18.980 1.00 29.82 ? 345 GLY   B O   1 
ATOM   5424 N N   . LYS   B 1 349 ? -47.225 13.411  -20.486 1.00 32.11 ? 346 LYS   B N   1 
ATOM   5425 C CA  . LYS   B 1 349 ? -46.477 14.401  -21.250 1.00 33.15 ? 346 LYS   B CA  1 
ATOM   5426 C C   . LYS   B 1 349 ? -47.436 15.224  -22.110 1.00 32.18 ? 346 LYS   B C   1 
ATOM   5427 O O   . LYS   B 1 349 ? -48.184 14.663  -22.917 1.00 27.43 ? 346 LYS   B O   1 
ATOM   5428 C CB  . LYS   B 1 349 ? -45.432 13.711  -22.126 1.00 31.72 ? 346 LYS   B CB  1 
ATOM   5429 C CG  . LYS   B 1 349 ? -44.516 14.681  -22.866 1.00 25.43 ? 346 LYS   B CG  1 
ATOM   5430 C CD  . LYS   B 1 349 ? -43.583 15.392  -21.855 1.00 32.45 ? 346 LYS   B CD  1 
ATOM   5431 C CE  . LYS   B 1 349 ? -42.862 16.585  -22.483 1.00 30.57 ? 346 LYS   B CE  1 
ATOM   5432 N NZ  . LYS   B 1 349 ? -43.794 17.736  -22.699 1.00 27.69 ? 346 LYS   B NZ  1 
ATOM   5433 N N   . VAL   B 1 350 ? -47.410 16.543  -21.942 1.00 28.49 ? 347 VAL   B N   1 
ATOM   5434 C CA  . VAL   B 1 350 ? -48.192 17.458  -22.772 1.00 32.11 ? 347 VAL   B CA  1 
ATOM   5435 C C   . VAL   B 1 350 ? -47.391 17.791  -24.026 1.00 29.57 ? 347 VAL   B C   1 
ATOM   5436 O O   . VAL   B 1 350 ? -46.264 18.299  -23.934 1.00 28.01 ? 347 VAL   B O   1 
ATOM   5437 C CB  . VAL   B 1 350 ? -48.549 18.736  -22.000 1.00 28.28 ? 347 VAL   B CB  1 
ATOM   5438 C CG1 . VAL   B 1 350 ? -49.331 19.701  -22.892 1.00 28.90 ? 347 VAL   B CG1 1 
ATOM   5439 C CG2 . VAL   B 1 350 ? -49.328 18.392  -20.737 1.00 29.50 ? 347 VAL   B CG2 1 
ATOM   5440 N N   . LEU   B 1 351 ? -47.974 17.517  -25.194 1.00 22.60 ? 348 LEU   B N   1 
ATOM   5441 C CA  . LEU   B 1 351 ? -47.366 17.770  -26.491 1.00 23.50 ? 348 LEU   B CA  1 
ATOM   5442 C C   . LEU   B 1 351 ? -48.383 18.464  -27.385 1.00 28.90 ? 348 LEU   B C   1 
ATOM   5443 O O   . LEU   B 1 351 ? -49.571 18.552  -27.059 1.00 31.35 ? 348 LEU   B O   1 
ATOM   5444 C CB  . LEU   B 1 351 ? -46.896 16.478  -27.171 1.00 28.09 ? 348 LEU   B CB  1 
ATOM   5445 C CG  . LEU   B 1 351 ? -45.944 15.540  -26.427 1.00 33.42 ? 348 LEU   B CG  1 
ATOM   5446 C CD1 . LEU   B 1 351 ? -45.791 14.241  -27.207 1.00 28.24 ? 348 LEU   B CD1 1 
ATOM   5447 C CD2 . LEU   B 1 351 ? -44.577 16.201  -26.208 1.00 29.08 ? 348 LEU   B CD2 1 
ATOM   5448 N N   . VAL   B 1 352 ? -47.910 18.966  -28.524 1.00 26.37 ? 349 VAL   B N   1 
ATOM   5449 C CA  . VAL   B 1 352 ? -48.789 19.512  -29.552 1.00 27.05 ? 349 VAL   B CA  1 
ATOM   5450 C C   . VAL   B 1 352 ? -48.464 18.817  -30.857 1.00 27.46 ? 349 VAL   B C   1 
ATOM   5451 O O   . VAL   B 1 352 ? -47.300 18.780  -31.268 1.00 28.12 ? 349 VAL   B O   1 
ATOM   5452 C CB  . VAL   B 1 352 ? -48.651 21.045  -29.699 1.00 25.59 ? 349 VAL   B CB  1 
ATOM   5453 C CG1 . VAL   B 1 352 ? -49.563 21.565  -30.819 1.00 28.19 ? 349 VAL   B CG1 1 
ATOM   5454 C CG2 . VAL   B 1 352 ? -48.967 21.741  -28.385 1.00 23.46 ? 349 VAL   B CG2 1 
ATOM   5455 N N   . ARG   B 1 353 ? -49.486 18.252  -31.502 1.00 29.18 ? 350 ARG   B N   1 
ATOM   5456 C CA  . ARG   B 1 353 ? -49.326 17.688  -32.836 1.00 30.28 ? 350 ARG   B CA  1 
ATOM   5457 C C   . ARG   B 1 353 ? -49.565 18.778  -33.876 1.00 28.94 ? 350 ARG   B C   1 
ATOM   5458 O O   . ARG   B 1 353 ? -50.605 19.443  -33.863 1.00 30.97 ? 350 ARG   B O   1 
ATOM   5459 C CB  . ARG   B 1 353 ? -50.282 16.508  -33.075 1.00 29.76 ? 350 ARG   B CB  1 
ATOM   5460 C CG  . ARG   B 1 353 ? -49.948 15.744  -34.378 1.00 32.12 ? 350 ARG   B CG  1 
ATOM   5461 C CD  . ARG   B 1 353 ? -50.751 14.446  -34.524 1.00 35.17 ? 350 ARG   B CD  1 
ATOM   5462 N NE  . ARG   B 1 353 ? -52.178 14.709  -34.651 1.00 39.31 ? 350 ARG   B NE  1 
ATOM   5463 C CZ  . ARG   B 1 353 ? -52.803 14.901  -35.808 1.00 50.51 ? 350 ARG   B CZ  1 
ATOM   5464 N NH1 . ARG   B 1 353 ? -52.151 14.864  -36.963 1.00 43.49 ? 350 ARG   B NH1 1 
ATOM   5465 N NH2 . ARG   B 1 353 ? -54.115 15.132  -35.807 1.00 45.36 ? 350 ARG   B NH2 1 
ATOM   5466 N N   . VAL   B 1 354 ? -48.598 18.952  -34.769 1.00 27.99 ? 351 VAL   B N   1 
ATOM   5467 C CA  . VAL   B 1 354 ? -48.605 20.057  -35.729 1.00 32.45 ? 351 VAL   B CA  1 
ATOM   5468 C C   . VAL   B 1 354 ? -49.035 19.558  -37.103 1.00 34.27 ? 351 VAL   B C   1 
ATOM   5469 O O   . VAL   B 1 354 ? -50.159 19.834  -37.524 1.00 44.79 ? 351 VAL   B O   1 
ATOM   5470 C CB  . VAL   B 1 354 ? -47.214 20.742  -35.795 1.00 28.95 ? 351 VAL   B CB  1 
ATOM   5471 C CG1 . VAL   B 1 354 ? -47.170 21.743  -36.928 1.00 35.29 ? 351 VAL   B CG1 1 
ATOM   5472 C CG2 . VAL   B 1 354 ? -46.921 21.437  -34.480 1.00 30.46 ? 351 VAL   B CG2 1 
HETATM 5473 C C8  . A1EDK C 2 .   ? -17.953 14.449  16.641  1.00 34.94 ? 401 A1EDK A C8  1 
HETATM 5474 C C5  . A1EDK C 2 .   ? -13.605 12.159  16.345  1.00 33.94 ? 401 A1EDK A C5  1 
HETATM 5475 C C6  . A1EDK C 2 .   ? -15.866 13.307  16.906  1.00 33.34 ? 401 A1EDK A C6  1 
HETATM 5476 N N1  . A1EDK C 2 .   ? -23.481 19.001  17.308  1.00 40.40 ? 401 A1EDK A N1  1 
HETATM 5477 C C2  . A1EDK C 2 .   ? -14.827 9.832   18.269  1.00 36.03 ? 401 A1EDK A C2  1 
HETATM 5478 C C4  . A1EDK C 2 .   ? -15.036 12.001  16.872  1.00 36.62 ? 401 A1EDK A C4  1 
HETATM 5479 C C21 . A1EDK C 2 .   ? -21.610 17.599  12.809  1.00 37.80 ? 401 A1EDK A C21 1 
HETATM 5480 C C23 . A1EDK C 2 .   ? -19.584 16.195  13.189  1.00 32.83 ? 401 A1EDK A C23 1 
HETATM 5481 C C24 . A1EDK C 2 .   ? -18.382 15.809  13.870  1.00 38.67 ? 401 A1EDK A C24 1 
HETATM 5482 C C25 . A1EDK C 2 .   ? -17.765 14.648  13.741  1.00 39.43 ? 401 A1EDK A C25 1 
HETATM 5483 C C27 . A1EDK C 2 .   ? -17.980 13.780  18.061  1.00 31.15 ? 401 A1EDK A C27 1 
HETATM 5484 C C29 . A1EDK C 2 .   ? -16.544 11.725  18.699  1.00 31.35 ? 401 A1EDK A C29 1 
HETATM 5485 C C1  . A1EDK C 2 .   ? -14.629 9.268   19.665  1.00 32.71 ? 401 A1EDK A C1  1 
HETATM 5486 C C10 . A1EDK C 2 .   ? -19.898 15.968  16.512  1.00 39.38 ? 401 A1EDK A C10 1 
HETATM 5487 C C11 . A1EDK C 2 .   ? -21.300 16.294  16.578  1.00 39.91 ? 401 A1EDK A C11 1 
HETATM 5488 C C12 . A1EDK C 2 .   ? -21.800 17.481  16.894  1.00 36.54 ? 401 A1EDK A C12 1 
HETATM 5489 C C13 . A1EDK C 2 .   ? -23.150 17.728  17.070  1.00 38.68 ? 401 A1EDK A C13 1 
HETATM 5490 C C14 . A1EDK C 2 .   ? -24.865 19.460  17.184  1.00 40.51 ? 401 A1EDK A C14 1 
HETATM 5491 C C15 . A1EDK C 2 .   ? -25.191 19.671  15.705  1.00 44.43 ? 401 A1EDK A C15 1 
HETATM 5492 C C16 . A1EDK C 2 .   ? -24.478 20.872  15.096  1.00 44.77 ? 401 A1EDK A C16 1 
HETATM 5493 C C17 . A1EDK C 2 .   ? -23.685 20.604  13.814  1.00 38.88 ? 401 A1EDK A C17 1 
HETATM 5494 C C18 . A1EDK C 2 .   ? -22.403 19.787  14.002  1.00 38.80 ? 401 A1EDK A C18 1 
HETATM 5495 C C19 . A1EDK C 2 .   ? -22.471 18.659  13.101  1.00 39.79 ? 401 A1EDK A C19 1 
HETATM 5496 C C20 . A1EDK C 2 .   ? -23.773 18.728  12.432  1.00 35.81 ? 401 A1EDK A C20 1 
HETATM 5497 C C22 . A1EDK C 2 .   ? -20.353 17.325  13.377  1.00 37.47 ? 401 A1EDK A C22 1 
HETATM 5498 C C26 . A1EDK C 2 .   ? -16.604 14.165  14.571  1.00 36.44 ? 401 A1EDK A C26 1 
HETATM 5499 C C28 . A1EDK C 2 .   ? -16.579 13.207  18.291  1.00 32.95 ? 401 A1EDK A C28 1 
HETATM 5500 C C3  . A1EDK C 2 .   ? -15.122 11.314  18.267  1.00 29.54 ? 401 A1EDK A C3  1 
HETATM 5501 C C7  . A1EDK C 2 .   ? -17.007 13.518  15.877  1.00 32.54 ? 401 A1EDK A C7  1 
HETATM 5502 C C9  . A1EDK C 2 .   ? -19.375 14.756  16.341  1.00 38.56 ? 401 A1EDK A C9  1 
HETATM 5503 N N2  . A1EDK C 2 .   ? -24.435 19.817  12.844  1.00 36.46 ? 401 A1EDK A N2  1 
HETATM 5504 O O1  . A1EDK C 2 .   ? -24.169 17.875  11.607  1.00 39.23 ? 401 A1EDK A O1  1 
HETATM 5505 O O2  . A1EDK C 2 .   ? -22.068 16.688  11.960  1.00 39.88 ? 401 A1EDK A O2  1 
HETATM 5506 O O3  . A1EDK C 2 .   ? -15.917 13.277  13.692  1.00 45.87 ? 401 A1EDK A O3  1 
HETATM 5507 O O4  . A1EDK C 2 .   ? -21.516 20.111  14.786  1.00 41.85 ? 401 A1EDK A O4  1 
HETATM 5508 O O5  . A1EDK C 2 .   ? -23.978 16.818  17.069  1.00 40.48 ? 401 A1EDK A O5  1 
HETATM 5509 H H1  . A1EDK C 2 .   ? -17.473 15.287  16.456  1.00 41.96 ? 401 A1EDK A H1  1 
HETATM 5510 H H3  . A1EDK C 2 .   ? -13.623 12.639  15.499  1.00 40.76 ? 401 A1EDK A H3  1 
HETATM 5511 H H4  . A1EDK C 2 .   ? -13.211 11.279  16.211  1.00 40.76 ? 401 A1EDK A H4  1 
HETATM 5512 H H2  . A1EDK C 2 .   ? -13.076 12.657  16.991  1.00 40.76 ? 401 A1EDK A H2  1 
HETATM 5513 H H5  . A1EDK C 2 .   ? -15.262 14.086  16.828  1.00 40.03 ? 401 A1EDK A H5  1 
HETATM 5514 H H6  . A1EDK C 2 .   ? -22.863 19.569  17.541  1.00 48.51 ? 401 A1EDK A H6  1 
HETATM 5515 H H7  . A1EDK C 2 .   ? -14.014 9.671   17.738  1.00 43.26 ? 401 A1EDK A H7  1 
HETATM 5516 H H8  . A1EDK C 2 .   ? -15.572 9.360   17.833  1.00 43.26 ? 401 A1EDK A H8  1 
HETATM 5517 H H9  . A1EDK C 2 .   ? -15.565 11.414  16.276  1.00 43.98 ? 401 A1EDK A H9  1 
HETATM 5518 H H10 . A1EDK C 2 .   ? -19.892 15.600  12.525  1.00 39.43 ? 401 A1EDK A H10 1 
HETATM 5519 H H12 . A1EDK C 2 .   ? -18.007 16.451  14.461  1.00 46.44 ? 401 A1EDK A H12 1 
HETATM 5520 H H13 . A1EDK C 2 .   ? -18.068 14.067  13.080  1.00 47.35 ? 401 A1EDK A H13 1 
HETATM 5521 H H15 . A1EDK C 2 .   ? -18.652 13.068  18.089  1.00 37.42 ? 401 A1EDK A H15 1 
HETATM 5522 H H14 . A1EDK C 2 .   ? -18.196 14.446  18.747  1.00 37.42 ? 401 A1EDK A H14 1 
HETATM 5523 H H16 . A1EDK C 2 .   ? -16.670 11.615  19.654  1.00 37.65 ? 401 A1EDK A H16 1 
HETATM 5524 H H17 . A1EDK C 2 .   ? -17.220 11.210  18.232  1.00 37.65 ? 401 A1EDK A H17 1 
HETATM 5525 H H20 . A1EDK C 2 .   ? -13.925 9.761   20.126  1.00 39.28 ? 401 A1EDK A H20 1 
HETATM 5526 H H18 . A1EDK C 2 .   ? -14.376 8.327   19.611  1.00 39.28 ? 401 A1EDK A H18 1 
HETATM 5527 H H19 . A1EDK C 2 .   ? -15.458 9.345   20.175  1.00 39.28 ? 401 A1EDK A H19 1 
HETATM 5528 H H21 . A1EDK C 2 .   ? -19.293 16.695  16.600  1.00 47.29 ? 401 A1EDK A H21 1 
HETATM 5529 H H22 . A1EDK C 2 .   ? -21.907 15.599  16.379  1.00 47.92 ? 401 A1EDK A H22 1 
HETATM 5530 H H23 . A1EDK C 2 .   ? -21.205 18.195  17.005  1.00 43.88 ? 401 A1EDK A H23 1 
HETATM 5531 H H25 . A1EDK C 2 .   ? -25.466 18.794  17.576  1.00 48.64 ? 401 A1EDK A H25 1 
HETATM 5532 H H24 . A1EDK C 2 .   ? -24.976 20.296  17.682  1.00 48.64 ? 401 A1EDK A H24 1 
HETATM 5533 H H27 . A1EDK C 2 .   ? -24.943 18.861  15.207  1.00 53.34 ? 401 A1EDK A H27 1 
HETATM 5534 H H26 . A1EDK C 2 .   ? -26.161 19.786  15.606  1.00 53.34 ? 401 A1EDK A H26 1 
HETATM 5535 H H29 . A1EDK C 2 .   ? -25.150 21.560  14.902  1.00 53.76 ? 401 A1EDK A H29 1 
HETATM 5536 H H28 . A1EDK C 2 .   ? -23.862 21.234  15.767  1.00 53.76 ? 401 A1EDK A H28 1 
HETATM 5537 H H30 . A1EDK C 2 .   ? -23.413 21.478  13.423  1.00 46.69 ? 401 A1EDK A H30 1 
HETATM 5538 H H32 . A1EDK C 2 .   ? -19.988 17.982  13.952  1.00 45.00 ? 401 A1EDK A H32 1 
HETATM 5539 H H33 . A1EDK C 2 .   ? -15.998 14.898  14.839  1.00 43.76 ? 401 A1EDK A H33 1 
HETATM 5540 H H34 . A1EDK C 2 .   ? -16.079 13.748  18.959  1.00 39.57 ? 401 A1EDK A H34 1 
HETATM 5541 H H35 . A1EDK C 2 .   ? -14.475 11.700  18.918  1.00 35.48 ? 401 A1EDK A H35 1 
HETATM 5542 H H36 . A1EDK C 2 .   ? -17.398 12.630  15.678  1.00 39.08 ? 401 A1EDK A H36 1 
HETATM 5543 H H37 . A1EDK C 2 .   ? -19.912 14.066  16.022  1.00 46.30 ? 401 A1EDK A H37 1 
HETATM 5544 H H38 . A1EDK C 2 .   ? -25.226 20.021  12.557  1.00 43.78 ? 401 A1EDK A H38 1 
HETATM 5545 H H39 . A1EDK C 2 .   ? -21.519 16.032  11.920  1.00 47.89 ? 401 A1EDK A H39 1 
HETATM 5546 H H40 . A1EDK C 2 .   ? -15.975 12.485  14.003  1.00 55.07 ? 401 A1EDK A H40 1 
HETATM 5547 P PA  . NAP   D 3 .   ? -10.335 24.422  12.456  1.00 34.16 ? 402 NAP   A PA  1 
HETATM 5548 O O1A . NAP   D 3 .   ? -8.993  24.593  13.085  1.00 40.96 ? 402 NAP   A O1A 1 
HETATM 5549 O O2A . NAP   D 3 .   ? -10.551 24.656  10.994  1.00 39.99 ? 402 NAP   A O2A 1 
HETATM 5550 O O5B . NAP   D 3 .   ? -11.380 25.322  13.342  1.00 42.55 ? 402 NAP   A O5B 1 
HETATM 5551 C C5B . NAP   D 3 .   ? -11.048 26.642  13.757  1.00 41.54 ? 402 NAP   A C5B 1 
HETATM 5552 C C4B . NAP   D 3 .   ? -10.491 27.479  12.604  1.00 45.11 ? 402 NAP   A C4B 1 
HETATM 5553 O O4B . NAP   D 3 .   ? -11.542 27.962  11.772  1.00 45.30 ? 402 NAP   A O4B 1 
HETATM 5554 C C3B . NAP   D 3 .   ? -9.755  28.752  13.069  1.00 47.57 ? 402 NAP   A C3B 1 
HETATM 5555 O O3B . NAP   D 3 .   ? -8.399  28.534  13.358  1.00 46.22 ? 402 NAP   A O3B 1 
HETATM 5556 C C2B . NAP   D 3 .   ? -10.001 29.759  11.911  1.00 39.66 ? 402 NAP   A C2B 1 
HETATM 5557 O O2B . NAP   D 3 .   ? -8.890  29.749  11.069  1.00 49.30 ? 402 NAP   A O2B 1 
HETATM 5558 C C1B . NAP   D 3 .   ? -11.168 29.152  11.117  1.00 43.37 ? 402 NAP   A C1B 1 
HETATM 5559 N N9A . NAP   D 3 .   ? -12.318 30.023  10.868  1.00 38.50 ? 402 NAP   A N9A 1 
HETATM 5560 C C8A . NAP   D 3 .   ? -13.203 30.610  11.736  1.00 38.18 ? 402 NAP   A C8A 1 
HETATM 5561 N N7A . NAP   D 3 .   ? -14.123 31.321  11.138  1.00 38.01 ? 402 NAP   A N7A 1 
HETATM 5562 C C5A . NAP   D 3 .   ? -13.841 31.197  9.806   1.00 36.02 ? 402 NAP   A C5A 1 
HETATM 5563 C C6A . NAP   D 3 .   ? -14.447 31.710  8.645   1.00 40.29 ? 402 NAP   A C6A 1 
HETATM 5564 N N6A . NAP   D 3 .   ? -15.525 32.501  8.670   1.00 39.89 ? 402 NAP   A N6A 1 
HETATM 5565 N N1A . NAP   D 3 .   ? -13.908 31.391  7.473   1.00 33.02 ? 402 NAP   A N1A 1 
HETATM 5566 C C2A . NAP   D 3 .   ? -12.835 30.603  7.437   1.00 34.27 ? 402 NAP   A C2A 1 
HETATM 5567 N N3A . NAP   D 3 .   ? -12.183 30.059  8.447   1.00 43.19 ? 402 NAP   A N3A 1 
HETATM 5568 C C4A . NAP   D 3 .   ? -12.728 30.393  9.617   1.00 37.26 ? 402 NAP   A C4A 1 
HETATM 5569 O O3  . NAP   D 3 .   ? -10.913 22.936  12.723  1.00 39.15 ? 402 NAP   A O3  1 
HETATM 5570 P PN  . NAP   D 3 .   ? -10.353 21.493  12.184  1.00 33.77 ? 402 NAP   A PN  1 
HETATM 5571 O O1N . NAP   D 3 .   ? -9.906  20.633  13.321  1.00 38.20 ? 402 NAP   A O1N 1 
HETATM 5572 O O2N . NAP   D 3 .   ? -9.532  21.708  10.952  1.00 28.55 ? 402 NAP   A O2N 1 
HETATM 5573 O O5D . NAP   D 3 .   ? -11.831 20.927  11.714  1.00 29.42 ? 402 NAP   A O5D 1 
HETATM 5574 C C5D . NAP   D 3 .   ? -12.543 21.549  10.677  1.00 31.01 ? 402 NAP   A C5D 1 
HETATM 5575 C C4D . NAP   D 3 .   ? -14.042 21.630  10.970  1.00 30.00 ? 402 NAP   A C4D 1 
HETATM 5576 O O4D . NAP   D 3 .   ? -14.618 20.309  10.808  1.00 27.41 ? 402 NAP   A O4D 1 
HETATM 5577 C C3D . NAP   D 3 .   ? -14.351 22.041  12.404  1.00 31.97 ? 402 NAP   A C3D 1 
HETATM 5578 O O3D . NAP   D 3 .   ? -15.451 22.922  12.355  1.00 29.27 ? 402 NAP   A O3D 1 
HETATM 5579 C C2D . NAP   D 3 .   ? -14.772 20.723  13.065  1.00 28.01 ? 402 NAP   A C2D 1 
HETATM 5580 O O2D . NAP   D 3 .   ? -15.685 20.945  14.083  1.00 25.44 ? 402 NAP   A O2D 1 
HETATM 5581 C C1D . NAP   D 3 .   ? -15.437 20.001  11.878  1.00 29.10 ? 402 NAP   A C1D 1 
HETATM 5582 N N1N . NAP   D 3 .   ? -15.428 18.504  11.864  1.00 29.65 ? 402 NAP   A N1N 1 
HETATM 5583 C C2N . NAP   D 3 .   ? -16.384 17.834  11.204  1.00 30.65 ? 402 NAP   A C2N 1 
HETATM 5584 C C3N . NAP   D 3 .   ? -16.367 16.458  11.130  1.00 31.28 ? 402 NAP   A C3N 1 
HETATM 5585 C C7N . NAP   D 3 .   ? -17.430 15.649  10.420  1.00 28.27 ? 402 NAP   A C7N 1 
HETATM 5586 O O7N . NAP   D 3 .   ? -17.384 14.429  10.518  1.00 28.56 ? 402 NAP   A O7N 1 
HETATM 5587 N N7N . NAP   D 3 .   ? -18.364 16.306  9.708   1.00 26.19 ? 402 NAP   A N7N 1 
HETATM 5588 C C4N . NAP   D 3 .   ? -15.309 15.791  11.743  1.00 28.90 ? 402 NAP   A C4N 1 
HETATM 5589 C C5N . NAP   D 3 .   ? -14.323 16.507  12.404  1.00 30.22 ? 402 NAP   A C5N 1 
HETATM 5590 C C6N . NAP   D 3 .   ? -14.393 17.875  12.444  1.00 28.91 ? 402 NAP   A C6N 1 
HETATM 5591 P P2B . NAP   D 3 .   ? -7.952  31.204  10.887  1.00 43.54 ? 402 NAP   A P2B 1 
HETATM 5592 O O1X . NAP   D 3 .   ? -8.964  32.343  10.922  1.00 41.08 ? 402 NAP   A O1X 1 
HETATM 5593 O O2X . NAP   D 3 .   ? -7.067  31.075  12.109  1.00 37.73 ? 402 NAP   A O2X 1 
HETATM 5594 O O3X . NAP   D 3 .   ? -7.230  31.051  9.550   1.00 33.42 ? 402 NAP   A O3X 1 
HETATM 5595 C C8  . A1EDK E 2 .   ? -33.448 21.380  -21.711 1.00 32.11 ? 401 A1EDK B C8  1 
HETATM 5596 C C5  . A1EDK E 2 .   ? -34.868 17.130  -23.678 1.00 31.92 ? 401 A1EDK B C5  1 
HETATM 5597 C C6  . A1EDK E 2 .   ? -34.163 19.530  -22.936 1.00 33.85 ? 401 A1EDK B C6  1 
HETATM 5598 N N1  . A1EDK E 2 .   ? -32.567 27.641  -18.258 1.00 30.16 ? 401 A1EDK B N1  1 
HETATM 5599 C C2  . A1EDK E 2 .   ? -32.874 17.782  -26.124 1.00 36.30 ? 401 A1EDK B C2  1 
HETATM 5600 C C4  . A1EDK E 2 .   ? -33.871 18.279  -23.809 1.00 38.57 ? 401 A1EDK B C4  1 
HETATM 5601 C C21 . A1EDK E 2 .   ? -31.974 23.171  -15.814 1.00 34.51 ? 401 A1EDK B C21 1 
HETATM 5602 C C23 . A1EDK E 2 .   ? -32.594 21.605  -17.535 1.00 29.99 ? 401 A1EDK B C23 1 
HETATM 5603 C C24 . A1EDK E 2 .   ? -33.420 20.888  -18.425 1.00 35.78 ? 401 A1EDK B C24 1 
HETATM 5604 C C25 . A1EDK E 2 .   ? -32.879 20.025  -19.259 1.00 34.95 ? 401 A1EDK B C25 1 
HETATM 5605 C C27 . A1EDK E 2 .   ? -33.260 21.819  -23.191 1.00 28.75 ? 401 A1EDK B C27 1 
HETATM 5606 C C29 . A1EDK E 2 .   ? -33.067 20.141  -25.092 1.00 28.65 ? 401 A1EDK B C29 1 
HETATM 5607 C C1  . A1EDK E 2 .   ? -33.136 17.957  -27.593 1.00 29.12 ? 401 A1EDK B C1  1 
HETATM 5608 C C10 . A1EDK E 2 .   ? -33.119 23.414  -20.339 1.00 33.42 ? 401 A1EDK B C10 1 
HETATM 5609 C C11 . A1EDK E 2 .   ? -32.351 24.478  -19.785 1.00 32.27 ? 401 A1EDK B C11 1 
HETATM 5610 C C12 . A1EDK E 2 .   ? -32.804 25.602  -19.252 1.00 30.47 ? 401 A1EDK B C12 1 
HETATM 5611 C C13 . A1EDK E 2 .   ? -31.973 26.609  -18.855 1.00 32.50 ? 401 A1EDK B C13 1 
HETATM 5612 C C14 . A1EDK E 2 .   ? -31.797 28.685  -17.578 1.00 36.82 ? 401 A1EDK B C14 1 
HETATM 5613 C C15 . A1EDK E 2 .   ? -31.414 28.206  -16.175 1.00 37.57 ? 401 A1EDK B C15 1 
HETATM 5614 C C16 . A1EDK E 2 .   ? -32.600 27.988  -15.250 1.00 34.51 ? 401 A1EDK B C16 1 
HETATM 5615 C C17 . A1EDK E 2 .   ? -32.718 26.607  -14.615 1.00 33.24 ? 401 A1EDK B C17 1 
HETATM 5616 C C18 . A1EDK E 2 .   ? -33.035 25.403  -15.495 1.00 32.49 ? 401 A1EDK B C18 1 
HETATM 5617 C C19 . A1EDK E 2 .   ? -32.024 24.420  -15.279 1.00 33.28 ? 401 A1EDK B C19 1 
HETATM 5618 C C20 . A1EDK E 2 .   ? -31.000 25.013  -14.426 1.00 32.13 ? 401 A1EDK B C20 1 
HETATM 5619 C C22 . A1EDK E 2 .   ? -32.864 22.666  -16.752 1.00 35.35 ? 401 A1EDK B C22 1 
HETATM 5620 C C26 . A1EDK E 2 .   ? -33.507 19.280  -20.412 1.00 35.59 ? 401 A1EDK B C26 1 
HETATM 5621 C C28 . A1EDK E 2 .   ? -33.953 20.690  -23.961 1.00 29.87 ? 401 A1EDK B C28 1 
HETATM 5622 C C3  . A1EDK E 2 .   ? -33.667 18.748  -25.282 1.00 33.78 ? 401 A1EDK B C3  1 
HETATM 5623 C C7  . A1EDK E 2 .   ? -33.217 19.861  -21.750 1.00 33.18 ? 401 A1EDK B C7  1 
HETATM 5624 C C9  . A1EDK E 2 .   ? -32.639 22.329  -20.903 1.00 32.06 ? 401 A1EDK B C9  1 
HETATM 5625 N N2  . A1EDK E 2 .   ? -31.456 26.200  -13.991 1.00 30.13 ? 401 A1EDK B N2  1 
HETATM 5626 O O1  . A1EDK E 2 .   ? -29.958 24.420  -14.069 1.00 35.74 ? 401 A1EDK B O1  1 
HETATM 5627 O O2  . A1EDK E 2 .   ? -30.994 22.377  -15.439 1.00 38.45 ? 401 A1EDK B O2  1 
HETATM 5628 O O3  . A1EDK E 2 .   ? -32.887 18.007  -20.104 1.00 38.73 ? 401 A1EDK B O3  1 
HETATM 5629 O O4  . A1EDK E 2 .   ? -34.055 25.301  -16.163 1.00 37.45 ? 401 A1EDK B O4  1 
HETATM 5630 O O5  . A1EDK E 2 .   ? -30.763 26.559  -19.095 1.00 36.90 ? 401 A1EDK B O5  1 
HETATM 5631 H H1  . A1EDK E 2 .   ? -34.353 21.380  -21.326 1.00 38.56 ? 401 A1EDK B H1  1 
HETATM 5632 H H3  . A1EDK E 2 .   ? -34.921 16.853  -22.747 1.00 38.34 ? 401 A1EDK B H3  1 
HETATM 5633 H H4  . A1EDK E 2 .   ? -34.572 16.381  -24.224 1.00 38.34 ? 401 A1EDK B H4  1 
HETATM 5634 H H2  . A1EDK E 2 .   ? -35.744 17.426  -23.980 1.00 38.34 ? 401 A1EDK B H2  1 
HETATM 5635 H H5  . A1EDK E 2 .   ? -35.081 19.484  -22.573 1.00 40.66 ? 401 A1EDK B H5  1 
HETATM 5636 H H6  . A1EDK E 2 .   ? -33.436 27.698  -18.271 1.00 36.23 ? 401 A1EDK B H6  1 
HETATM 5637 H H7  . A1EDK E 2 .   ? -33.105 16.863  -25.859 1.00 43.59 ? 401 A1EDK B H7  1 
HETATM 5638 H H8  . A1EDK E 2 .   ? -31.916 17.917  -25.947 1.00 43.59 ? 401 A1EDK B H8  1 
HETATM 5639 H H9  . A1EDK E 2 .   ? -32.977 17.998  -23.490 1.00 46.31 ? 401 A1EDK B H9  1 
HETATM 5640 H H10 . A1EDK E 2 .   ? -31.705 21.293  -17.477 1.00 36.02 ? 401 A1EDK B H10 1 
HETATM 5641 H H12 . A1EDK E 2 .   ? -34.359 21.036  -18.412 1.00 42.96 ? 401 A1EDK B H12 1 
HETATM 5642 H H13 . A1EDK E 2 .   ? -31.976 19.840  -19.128 1.00 41.97 ? 401 A1EDK B H13 1 
HETATM 5643 H H15 . A1EDK E 2 .   ? -32.310 21.882  -23.426 1.00 34.53 ? 401 A1EDK B H15 1 
HETATM 5644 H H14 . A1EDK E 2 .   ? -33.686 22.684  -23.363 1.00 34.53 ? 401 A1EDK B H14 1 
HETATM 5645 H H16 . A1EDK E 2 .   ? -33.139 20.674  -25.899 1.00 34.42 ? 401 A1EDK B H16 1 
HETATM 5646 H H17 . A1EDK E 2 .   ? -32.134 20.095  -24.830 1.00 34.42 ? 401 A1EDK B H17 1 
HETATM 5647 H H20 . A1EDK E 2 .   ? -32.503 17.423  -28.109 1.00 34.98 ? 401 A1EDK B H20 1 
HETATM 5648 H H18 . A1EDK E 2 .   ? -33.035 18.896  -27.839 1.00 34.98 ? 401 A1EDK B H18 1 
HETATM 5649 H H19 . A1EDK E 2 .   ? -34.043 17.668  -27.805 1.00 34.98 ? 401 A1EDK B H19 1 
HETATM 5650 H H21 . A1EDK E 2 .   ? -34.064 23.505  -20.292 1.00 40.13 ? 401 A1EDK B H21 1 
HETATM 5651 H H22 . A1EDK E 2 .   ? -31.414 24.360  -19.804 1.00 38.76 ? 401 A1EDK B H22 1 
HETATM 5652 H H23 . A1EDK E 2 .   ? -33.727 25.711  -19.143 1.00 36.60 ? 401 A1EDK B H23 1 
HETATM 5653 H H25 . A1EDK E 2 .   ? -32.336 29.501  -17.524 1.00 44.22 ? 401 A1EDK B H25 1 
HETATM 5654 H H24 . A1EDK E 2 .   ? -30.995 28.888  -18.101 1.00 44.22 ? 401 A1EDK B H24 1 
HETATM 5655 H H27 . A1EDK E 2 .   ? -30.911 27.366  -16.256 1.00 45.11 ? 401 A1EDK B H27 1 
HETATM 5656 H H26 . A1EDK E 2 .   ? -30.809 28.867  -15.772 1.00 45.11 ? 401 A1EDK B H26 1 
HETATM 5657 H H29 . A1EDK E 2 .   ? -32.550 28.652  -14.530 1.00 41.44 ? 401 A1EDK B H29 1 
HETATM 5658 H H28 . A1EDK E 2 .   ? -33.420 28.159  -15.761 1.00 41.44 ? 401 A1EDK B H28 1 
HETATM 5659 H H30 . A1EDK E 2 .   ? -33.489 26.651  -13.987 1.00 39.93 ? 401 A1EDK B H30 1 
HETATM 5660 H H32 . A1EDK E 2 .   ? -33.708 23.084  -16.852 1.00 42.45 ? 401 A1EDK B H32 1 
HETATM 5661 H H33 . A1EDK E 2 .   ? -34.492 19.226  -20.461 1.00 42.74 ? 401 A1EDK B H33 1 
HETATM 5662 H H34 . A1EDK E 2 .   ? -34.851 20.955  -24.296 1.00 35.88 ? 401 A1EDK B H34 1 
HETATM 5663 H H35 . A1EDK E 2 .   ? -34.531 18.874  -25.761 1.00 40.57 ? 401 A1EDK B H35 1 
HETATM 5664 H H36 . A1EDK E 2 .   ? -32.310 19.542  -21.986 1.00 39.85 ? 401 A1EDK B H36 1 
HETATM 5665 H H37 . A1EDK E 2 .   ? -31.735 22.132  -20.796 1.00 38.51 ? 401 A1EDK B H37 1 
HETATM 5666 H H38 . A1EDK E 2 .   ? -31.036 26.671  -13.398 1.00 36.18 ? 401 A1EDK B H38 1 
HETATM 5667 H H39 . A1EDK E 2 .   ? -31.103 21.602  -15.788 1.00 46.18 ? 401 A1EDK B H39 1 
HETATM 5668 H H40 . A1EDK E 2 .   ? -33.015 17.476  -20.759 1.00 46.51 ? 401 A1EDK B H40 1 
HETATM 5669 P PA  . NAP   F 3 .   ? -44.565 18.582  -14.790 1.00 31.35 ? 402 NAP   B PA  1 
HETATM 5670 O O1A . NAP   F 3 .   ? -45.786 17.979  -15.411 1.00 30.20 ? 402 NAP   B O1A 1 
HETATM 5671 O O2A . NAP   F 3 .   ? -44.139 18.222  -13.393 1.00 34.74 ? 402 NAP   B O2A 1 
HETATM 5672 O O5B . NAP   F 3 .   ? -44.671 20.213  -14.914 1.00 29.71 ? 402 NAP   B O5B 1 
HETATM 5673 C C5B . NAP   F 3 .   ? -45.855 20.958  -14.684 1.00 26.20 ? 402 NAP   B C5B 1 
HETATM 5674 C C4B . NAP   F 3 .   ? -46.539 20.568  -13.372 1.00 31.79 ? 402 NAP   B C4B 1 
HETATM 5675 O O4B . NAP   F 3 .   ? -45.893 21.106  -12.228 1.00 32.10 ? 402 NAP   B O4B 1 
HETATM 5676 C C3B . NAP   F 3 .   ? -47.971 21.122  -13.241 1.00 30.61 ? 402 NAP   B C3B 1 
HETATM 5677 O O3B . NAP   F 3 .   ? -48.887 20.360  -13.968 1.00 31.55 ? 402 NAP   B O3B 1 
HETATM 5678 C C2B . NAP   F 3 .   ? -48.207 21.031  -11.723 1.00 30.07 ? 402 NAP   B C2B 1 
HETATM 5679 O O2B . NAP   F 3 .   ? -48.769 19.776  -11.512 1.00 29.79 ? 402 NAP   B O2B 1 
HETATM 5680 C C1B . NAP   F 3 .   ? -46.784 21.033  -11.140 1.00 32.25 ? 402 NAP   B C1B 1 
HETATM 5681 N N9A . NAP   F 3 .   ? -46.519 22.090  -10.182 1.00 29.39 ? 402 NAP   B N9A 1 
HETATM 5682 C C8A . NAP   F 3 .   ? -46.578 23.446  -10.358 1.00 30.00 ? 402 NAP   B C8A 1 
HETATM 5683 N N7A . NAP   F 3 .   ? -46.275 24.106  -9.280  1.00 33.52 ? 402 NAP   B N7A 1 
HETATM 5684 C C5A . NAP   F 3 .   ? -46.005 23.146  -8.337  1.00 31.26 ? 402 NAP   B C5A 1 
HETATM 5685 C C6A . NAP   F 3 .   ? -45.619 23.202  -6.978  1.00 30.92 ? 402 NAP   B C6A 1 
HETATM 5686 N N6A . NAP   F 3 .   ? -45.441 24.340  -6.321  1.00 35.11 ? 402 NAP   B N6A 1 
HETATM 5687 N N1A . NAP   F 3 .   ? -45.437 22.055  -6.321  1.00 33.29 ? 402 NAP   B N1A 1 
HETATM 5688 C C2A . NAP   F 3 .   ? -45.610 20.901  -6.973  1.00 32.73 ? 402 NAP   B C2A 1 
HETATM 5689 N N3A . NAP   F 3 .   ? -45.971 20.716  -8.234  1.00 33.17 ? 402 NAP   B N3A 1 
HETATM 5690 C C4A . NAP   F 3 .   ? -46.154 21.880  -8.877  1.00 31.95 ? 402 NAP   B C4A 1 
HETATM 5691 O O3  . NAP   F 3 .   ? -43.287 18.359  -15.790 1.00 28.10 ? 402 NAP   B O3  1 
HETATM 5692 P PN  . NAP   F 3 .   ? -42.478 17.032  -16.309 1.00 31.67 ? 402 NAP   B PN  1 
HETATM 5693 O O1N . NAP   F 3 .   ? -42.376 17.014  -17.801 1.00 29.09 ? 402 NAP   B O1N 1 
HETATM 5694 O O2N . NAP   F 3 .   ? -42.946 15.842  -15.531 1.00 29.10 ? 402 NAP   B O2N 1 
HETATM 5695 O O5D . NAP   F 3 .   ? -40.969 17.433  -15.746 1.00 29.22 ? 402 NAP   B O5D 1 
HETATM 5696 C C5D . NAP   F 3 .   ? -40.806 17.767  -14.394 1.00 26.24 ? 402 NAP   B C5D 1 
HETATM 5697 C C4D . NAP   F 3 .   ? -39.805 18.895  -14.173 1.00 26.61 ? 402 NAP   B C4D 1 
HETATM 5698 O O4D . NAP   F 3 .   ? -38.498 18.462  -14.632 1.00 25.91 ? 402 NAP   B O4D 1 
HETATM 5699 C C3D . NAP   F 3 .   ? -40.101 20.173  -14.943 1.00 23.55 ? 402 NAP   B C3D 1 
HETATM 5700 O O3D . NAP   F 3 .   ? -39.755 21.233  -14.104 1.00 23.00 ? 402 NAP   B O3D 1 
HETATM 5701 C C2D . NAP   F 3 .   ? -39.097 20.151  -16.100 1.00 27.06 ? 402 NAP   B C2D 1 
HETATM 5702 O O2D . NAP   F 3 .   ? -38.746 21.450  -16.481 1.00 26.79 ? 402 NAP   B O2D 1 
HETATM 5703 C C1D . NAP   F 3 .   ? -37.919 19.439  -15.410 1.00 24.93 ? 402 NAP   B C1D 1 
HETATM 5704 N N1N . NAP   F 3 .   ? -36.892 18.748  -16.256 1.00 29.55 ? 402 NAP   B N1N 1 
HETATM 5705 C C2N . NAP   F 3 .   ? -35.602 18.769  -15.872 1.00 25.40 ? 402 NAP   B C2N 1 
HETATM 5706 C C3N . NAP   F 3 .   ? -34.625 18.109  -16.595 1.00 26.19 ? 402 NAP   B C3N 1 
HETATM 5707 C C7N . NAP   F 3 .   ? -33.169 18.129  -16.177 1.00 25.89 ? 402 NAP   B C7N 1 
HETATM 5708 O O7N . NAP   F 3 .   ? -32.335 17.615  -16.893 1.00 26.59 ? 402 NAP   B O7N 1 
HETATM 5709 N N7N . NAP   F 3 .   ? -32.876 18.726  -15.015 1.00 23.57 ? 402 NAP   B N7N 1 
HETATM 5710 C C4N . NAP   F 3 .   ? -35.017 17.411  -17.732 1.00 26.88 ? 402 NAP   B C4N 1 
HETATM 5711 C C5N . NAP   F 3 .   ? -36.361 17.395  -18.115 1.00 26.35 ? 402 NAP   B C5N 1 
HETATM 5712 C C6N . NAP   F 3 .   ? -37.287 18.068  -17.343 1.00 27.32 ? 402 NAP   B C6N 1 
HETATM 5713 P P2B . NAP   F 3 .   ? -50.323 19.690  -10.737 1.00 33.11 ? 402 NAP   B P2B 1 
HETATM 5714 O O1X . NAP   F 3 .   ? -50.451 20.940  -9.902  1.00 29.43 ? 402 NAP   B O1X 1 
HETATM 5715 O O2X . NAP   F 3 .   ? -51.247 19.610  -11.952 1.00 30.41 ? 402 NAP   B O2X 1 
HETATM 5716 O O3X . NAP   F 3 .   ? -50.198 18.389  -9.935  1.00 33.72 ? 402 NAP   B O3X 1 
HETATM 5717 O O   . HOH   G 4 .   ? -30.057 33.669  16.534  1.00 40.23 ? 501 HOH   A O   1 
HETATM 5718 O O   . HOH   G 4 .   ? -19.929 33.562  -10.032 1.00 42.96 ? 502 HOH   A O   1 
HETATM 5719 O O   . HOH   G 4 .   ? -22.378 -0.326  28.400  1.00 42.89 ? 503 HOH   A O   1 
HETATM 5720 O O   . HOH   G 4 .   ? 3.615   16.653  19.698  1.00 42.50 ? 504 HOH   A O   1 
HETATM 5721 O O   . HOH   G 4 .   ? -21.360 -9.020  39.773  1.00 36.88 ? 505 HOH   A O   1 
HETATM 5722 O O   . HOH   G 4 .   ? 3.082   -2.659  19.921  1.00 36.06 ? 506 HOH   A O   1 
HETATM 5723 O O   . HOH   G 4 .   ? -9.752  22.691  8.723   1.00 29.79 ? 507 HOH   A O   1 
HETATM 5724 O O   . HOH   G 4 .   ? -11.519 28.948  -17.873 1.00 42.34 ? 508 HOH   A O   1 
HETATM 5725 O O   . HOH   G 4 .   ? -20.579 24.229  38.315  1.00 52.05 ? 509 HOH   A O   1 
HETATM 5726 O O   . HOH   G 4 .   ? -18.095 7.303   41.059  1.00 42.36 ? 510 HOH   A O   1 
HETATM 5727 O O   . HOH   G 4 .   ? -22.877 5.733   6.854   1.00 29.84 ? 511 HOH   A O   1 
HETATM 5728 O O   . HOH   G 4 .   ? -33.671 26.751  1.222   1.00 32.91 ? 512 HOH   A O   1 
HETATM 5729 O O   . HOH   G 4 .   ? -12.927 40.599  -3.202  1.00 44.18 ? 513 HOH   A O   1 
HETATM 5730 O O   . HOH   G 4 .   ? -6.946  26.757  12.303  1.00 38.07 ? 514 HOH   A O   1 
HETATM 5731 O O   . HOH   G 4 .   ? -17.866 32.655  -12.346 1.00 45.36 ? 515 HOH   A O   1 
HETATM 5732 O O   . HOH   G 4 .   ? -9.310  10.568  17.370  1.00 21.61 ? 516 HOH   A O   1 
HETATM 5733 O O   . HOH   G 4 .   ? -10.519 -6.642  23.773  1.00 42.60 ? 517 HOH   A O   1 
HETATM 5734 O O   . HOH   G 4 .   ? -24.627 35.261  0.653   1.00 39.57 ? 518 HOH   A O   1 
HETATM 5735 O O   . HOH   G 4 .   ? -16.881 7.735   27.397  1.00 38.71 ? 519 HOH   A O   1 
HETATM 5736 O O   . HOH   G 4 .   ? -6.952  24.081  -12.100 1.00 35.26 ? 520 HOH   A O   1 
HETATM 5737 O O   . HOH   G 4 .   ? -2.465  15.514  17.401  1.00 29.21 ? 521 HOH   A O   1 
HETATM 5738 O O   . HOH   G 4 .   ? 3.096   20.517  25.540  1.00 39.90 ? 522 HOH   A O   1 
HETATM 5739 O O   . HOH   G 4 .   ? -7.701  37.063  15.805  1.00 56.02 ? 523 HOH   A O   1 
HETATM 5740 O O   . HOH   G 4 .   ? -21.225 21.217  17.442  1.00 31.66 ? 524 HOH   A O   1 
HETATM 5741 O O   . HOH   G 4 .   ? -18.667 10.538  6.030   1.00 20.51 ? 525 HOH   A O   1 
HETATM 5742 O O   . HOH   G 4 .   ? -4.127  6.082   15.599  1.00 25.63 ? 526 HOH   A O   1 
HETATM 5743 O O   . HOH   G 4 .   ? -15.960 6.864   22.254  1.00 30.20 ? 527 HOH   A O   1 
HETATM 5744 O O   . HOH   G 4 .   ? 10.085  11.547  9.594   1.00 38.45 ? 528 HOH   A O   1 
HETATM 5745 O O   . HOH   G 4 .   ? -23.523 27.096  -10.188 1.00 32.23 ? 529 HOH   A O   1 
HETATM 5746 O O   . HOH   G 4 .   ? -20.707 15.484  -9.519  1.00 23.77 ? 530 HOH   A O   1 
HETATM 5747 O O   . HOH   G 4 .   ? -19.437 35.957  28.049  1.00 44.13 ? 531 HOH   A O   1 
HETATM 5748 O O   . HOH   G 4 .   ? 0.831   15.839  13.907  1.00 36.10 ? 532 HOH   A O   1 
HETATM 5749 O O   . HOH   G 4 .   ? -25.747 24.511  12.783  1.00 43.97 ? 533 HOH   A O   1 
HETATM 5750 O O   . HOH   G 4 .   ? -24.153 27.688  6.220   1.00 30.75 ? 534 HOH   A O   1 
HETATM 5751 O O   . HOH   G 4 .   ? -10.390 0.376   40.338  1.00 31.92 ? 535 HOH   A O   1 
HETATM 5752 O O   . HOH   G 4 .   ? -12.740 26.109  10.376  1.00 37.14 ? 536 HOH   A O   1 
HETATM 5753 O O   . HOH   G 4 .   ? -3.855  12.812  -3.140  1.00 25.44 ? 537 HOH   A O   1 
HETATM 5754 O O   . HOH   G 4 .   ? -10.864 11.709  28.799  1.00 23.02 ? 538 HOH   A O   1 
HETATM 5755 O O   . HOH   G 4 .   ? -26.708 27.523  15.656  1.00 42.52 ? 539 HOH   A O   1 
HETATM 5756 O O   . HOH   G 4 .   ? -13.963 -0.511  6.580   1.00 41.07 ? 540 HOH   A O   1 
HETATM 5757 O O   . HOH   G 4 .   ? -11.427 15.932  16.976  1.00 26.90 ? 541 HOH   A O   1 
HETATM 5758 O O   . HOH   G 4 .   ? -6.761  35.414  -12.001 1.00 40.03 ? 542 HOH   A O   1 
HETATM 5759 O O   . HOH   G 4 .   ? -14.814 17.435  -10.702 1.00 25.99 ? 543 HOH   A O   1 
HETATM 5760 O O   . HOH   G 4 .   ? -1.330  34.739  12.102  1.00 46.23 ? 544 HOH   A O   1 
HETATM 5761 O O   . HOH   G 4 .   ? -12.331 5.802   17.517  1.00 32.10 ? 545 HOH   A O   1 
HETATM 5762 O O   . HOH   G 4 .   ? -7.314  24.811  15.112  1.00 41.64 ? 546 HOH   A O   1 
HETATM 5763 O O   . HOH   G 4 .   ? -9.629  6.374   -3.587  1.00 44.14 ? 547 HOH   A O   1 
HETATM 5764 O O   . HOH   G 4 .   ? -24.807 17.657  20.478  1.00 33.39 ? 548 HOH   A O   1 
HETATM 5765 O O   . HOH   G 4 .   ? -3.588  34.270  18.507  1.00 60.33 ? 549 HOH   A O   1 
HETATM 5766 O O   . HOH   G 4 .   ? -18.689 6.103   31.558  1.00 43.82 ? 550 HOH   A O   1 
HETATM 5767 O O   . HOH   G 4 .   ? -15.092 24.950  10.676  1.00 30.82 ? 551 HOH   A O   1 
HETATM 5768 O O   . HOH   G 4 .   ? -18.482 25.691  24.245  1.00 30.72 ? 552 HOH   A O   1 
HETATM 5769 O O   . HOH   G 4 .   ? -2.501  -0.116  24.288  1.00 21.98 ? 553 HOH   A O   1 
HETATM 5770 O O   . HOH   G 4 .   ? -26.117 15.580  18.067  1.00 31.04 ? 554 HOH   A O   1 
HETATM 5771 O O   . HOH   G 4 .   ? -14.394 31.153  -10.789 1.00 39.89 ? 555 HOH   A O   1 
HETATM 5772 O O   . HOH   G 4 .   ? -24.095 29.034  2.129   1.00 29.66 ? 556 HOH   A O   1 
HETATM 5773 O O   . HOH   G 4 .   ? -20.435 4.889   16.286  1.00 36.64 ? 557 HOH   A O   1 
HETATM 5774 O O   . HOH   G 4 .   ? -20.571 5.348   3.306   1.00 39.41 ? 558 HOH   A O   1 
HETATM 5775 O O   . HOH   G 4 .   ? -11.803 22.618  6.258   1.00 25.79 ? 559 HOH   A O   1 
HETATM 5776 O O   . HOH   G 4 .   ? -6.890  -1.148  12.713  1.00 36.56 ? 560 HOH   A O   1 
HETATM 5777 O O   . HOH   G 4 .   ? -23.937 9.671   26.097  1.00 41.18 ? 561 HOH   A O   1 
HETATM 5778 O O   . HOH   G 4 .   ? -14.836 32.644  16.360  1.00 47.13 ? 562 HOH   A O   1 
HETATM 5779 O O   . HOH   G 4 .   ? -20.934 28.870  22.659  1.00 29.90 ? 563 HOH   A O   1 
HETATM 5780 O O   . HOH   G 4 .   ? -5.954  28.789  31.824  1.00 36.32 ? 564 HOH   A O   1 
HETATM 5781 O O   . HOH   G 4 .   ? -20.944 -2.613  31.300  1.00 46.77 ? 565 HOH   A O   1 
HETATM 5782 O O   . HOH   G 4 .   ? -5.246  12.826  -9.344  1.00 27.39 ? 566 HOH   A O   1 
HETATM 5783 O O   . HOH   G 4 .   ? -21.377 15.052  28.829  1.00 29.52 ? 567 HOH   A O   1 
HETATM 5784 O O   . HOH   G 4 .   ? -27.329 13.770  32.428  1.00 47.69 ? 568 HOH   A O   1 
HETATM 5785 O O   . HOH   G 4 .   ? -15.680 33.479  11.622  1.00 47.09 ? 569 HOH   A O   1 
HETATM 5786 O O   . HOH   G 4 .   ? -24.314 26.598  3.177   1.00 28.42 ? 570 HOH   A O   1 
HETATM 5787 O O   . HOH   G 4 .   ? -10.995 -3.778  40.569  1.00 40.48 ? 571 HOH   A O   1 
HETATM 5788 O O   . HOH   G 4 .   ? -0.579  -2.979  22.063  1.00 39.17 ? 572 HOH   A O   1 
HETATM 5789 O O   . HOH   G 4 .   ? 7.725   17.958  27.069  1.00 44.33 ? 573 HOH   A O   1 
HETATM 5790 O O   . HOH   G 4 .   ? -30.182 11.148  20.830  1.00 41.21 ? 574 HOH   A O   1 
HETATM 5791 O O   . HOH   G 4 .   ? -12.159 32.016  28.027  1.00 40.29 ? 575 HOH   A O   1 
HETATM 5792 O O   . HOH   G 4 .   ? -12.092 16.506  -12.678 1.00 36.24 ? 576 HOH   A O   1 
HETATM 5793 O O   . HOH   G 4 .   ? -26.801 34.320  -9.192  1.00 44.07 ? 577 HOH   A O   1 
HETATM 5794 O O   . HOH   G 4 .   ? 1.268   4.701   33.349  1.00 24.03 ? 578 HOH   A O   1 
HETATM 5795 O O   . HOH   G 4 .   ? -17.405 9.532   -5.221  1.00 34.56 ? 579 HOH   A O   1 
HETATM 5796 O O   . HOH   G 4 .   ? -17.690 14.173  44.682  1.00 46.91 ? 580 HOH   A O   1 
HETATM 5797 O O   . HOH   G 4 .   ? -19.354 -4.157  33.480  1.00 33.88 ? 581 HOH   A O   1 
HETATM 5798 O O   . HOH   G 4 .   ? -24.823 26.328  36.617  1.00 42.27 ? 582 HOH   A O   1 
HETATM 5799 O O   . HOH   G 4 .   ? -1.275  -0.029  8.939   1.00 35.74 ? 583 HOH   A O   1 
HETATM 5800 O O   . HOH   G 4 .   ? -21.183 31.094  34.202  1.00 42.22 ? 584 HOH   A O   1 
HETATM 5801 O O   . HOH   G 4 .   ? -18.281 12.223  34.988  1.00 29.11 ? 585 HOH   A O   1 
HETATM 5802 O O   . HOH   G 4 .   ? -31.261 31.045  -5.237  1.00 28.02 ? 586 HOH   A O   1 
HETATM 5803 O O   . HOH   G 4 .   ? -13.194 16.413  20.922  1.00 22.52 ? 587 HOH   A O   1 
HETATM 5804 O O   . HOH   G 4 .   ? -29.531 37.568  17.109  1.00 42.18 ? 588 HOH   A O   1 
HETATM 5805 O O   . HOH   G 4 .   ? -14.469 11.741  37.052  1.00 34.11 ? 589 HOH   A O   1 
HETATM 5806 O O   . HOH   G 4 .   ? -14.390 2.721   1.631   1.00 39.34 ? 590 HOH   A O   1 
HETATM 5807 O O   . HOH   G 4 .   ? 3.028   15.099  21.431  1.00 34.21 ? 591 HOH   A O   1 
HETATM 5808 O O   . HOH   G 4 .   ? -26.507 17.565  35.512  1.00 40.31 ? 592 HOH   A O   1 
HETATM 5809 O O   . HOH   G 4 .   ? -20.728 16.709  26.759  1.00 29.43 ? 593 HOH   A O   1 
HETATM 5810 O O   . HOH   G 4 .   ? -7.325  31.358  25.616  1.00 33.63 ? 594 HOH   A O   1 
HETATM 5811 O O   . HOH   G 4 .   ? -4.450  26.646  12.553  1.00 37.02 ? 595 HOH   A O   1 
HETATM 5812 O O   . HOH   G 4 .   ? -17.444 12.332  27.395  1.00 28.65 ? 596 HOH   A O   1 
HETATM 5813 O O   . HOH   G 4 .   ? -2.838  2.705   17.242  1.00 28.74 ? 597 HOH   A O   1 
HETATM 5814 O O   . HOH   G 4 .   ? 6.766   3.707   13.084  1.00 38.36 ? 598 HOH   A O   1 
HETATM 5815 O O   . HOH   G 4 .   ? -13.225 26.650  37.321  1.00 37.19 ? 599 HOH   A O   1 
HETATM 5816 O O   . HOH   G 4 .   ? -14.047 1.890   17.635  1.00 34.84 ? 600 HOH   A O   1 
HETATM 5817 O O   . HOH   G 4 .   ? 1.087   17.963  -1.382  1.00 36.95 ? 601 HOH   A O   1 
HETATM 5818 O O   . HOH   G 4 .   ? -11.054 9.016   -4.591  1.00 41.46 ? 602 HOH   A O   1 
HETATM 5819 O O   . HOH   G 4 .   ? -2.612  23.238  10.004  1.00 39.46 ? 603 HOH   A O   1 
HETATM 5820 O O   . HOH   G 4 .   ? -21.701 27.224  -12.208 1.00 30.27 ? 604 HOH   A O   1 
HETATM 5821 O O   . HOH   G 4 .   ? -15.511 19.571  -12.090 1.00 27.21 ? 605 HOH   A O   1 
HETATM 5822 O O   . HOH   G 4 .   ? -10.449 4.671   1.409   1.00 23.00 ? 606 HOH   A O   1 
HETATM 5823 O O   . HOH   G 4 .   ? -12.081 18.787  14.605  1.00 35.09 ? 607 HOH   A O   1 
HETATM 5824 O O   . HOH   G 4 .   ? -7.834  10.030  45.743  1.00 42.66 ? 608 HOH   A O   1 
HETATM 5825 O O   . HOH   G 4 .   ? -22.858 -8.211  37.320  1.00 43.34 ? 609 HOH   A O   1 
HETATM 5826 O O   . HOH   G 4 .   ? -0.171  13.183  29.739  1.00 33.14 ? 610 HOH   A O   1 
HETATM 5827 O O   . HOH   G 4 .   ? -8.191  34.914  16.544  1.00 55.10 ? 611 HOH   A O   1 
HETATM 5828 O O   . HOH   G 4 .   ? 2.108   6.530   2.119   1.00 35.15 ? 612 HOH   A O   1 
HETATM 5829 O O   . HOH   G 4 .   ? -18.484 5.175   23.602  1.00 32.19 ? 613 HOH   A O   1 
HETATM 5830 O O   . HOH   G 4 .   ? -18.111 5.894   2.631   1.00 31.85 ? 614 HOH   A O   1 
HETATM 5831 O O   . HOH   G 4 .   ? 5.799   15.728  8.091   1.00 43.95 ? 615 HOH   A O   1 
HETATM 5832 O O   . HOH   G 4 .   ? -8.391  23.005  -15.378 1.00 43.35 ? 616 HOH   A O   1 
HETATM 5833 O O   . HOH   G 4 .   ? -26.382 6.479   26.195  1.00 40.96 ? 617 HOH   A O   1 
HETATM 5834 O O   . HOH   G 4 .   ? -21.129 26.160  23.546  1.00 35.84 ? 618 HOH   A O   1 
HETATM 5835 O O   . HOH   G 4 .   ? -7.939  27.282  31.196  1.00 33.36 ? 619 HOH   A O   1 
HETATM 5836 O O   . HOH   G 4 .   ? -17.572 4.401   39.028  1.00 44.04 ? 620 HOH   A O   1 
HETATM 5837 O O   . HOH   G 4 .   ? -5.544  12.763  34.085  1.00 29.62 ? 621 HOH   A O   1 
HETATM 5838 O O   . HOH   G 4 .   ? -9.709  14.407  18.154  1.00 22.08 ? 622 HOH   A O   1 
HETATM 5839 O O   . HOH   G 4 .   ? 5.414   30.937  2.958   1.00 40.76 ? 623 HOH   A O   1 
HETATM 5840 O O   . HOH   G 4 .   ? 4.267   13.708  25.382  1.00 32.42 ? 624 HOH   A O   1 
HETATM 5841 O O   . HOH   G 4 .   ? -10.026 21.075  16.111  1.00 35.61 ? 625 HOH   A O   1 
HETATM 5842 O O   . HOH   G 4 .   ? -9.210  28.149  -11.729 1.00 35.23 ? 626 HOH   A O   1 
HETATM 5843 O O   . HOH   G 4 .   ? -1.806  15.114  14.602  1.00 24.25 ? 627 HOH   A O   1 
HETATM 5844 O O   . HOH   G 4 .   ? -8.240  36.478  -4.673  1.00 39.74 ? 628 HOH   A O   1 
HETATM 5845 O O   . HOH   G 4 .   ? 3.043   21.490  20.499  1.00 39.60 ? 629 HOH   A O   1 
HETATM 5846 O O   . HOH   G 4 .   ? 1.511   4.650   11.943  1.00 36.73 ? 630 HOH   A O   1 
HETATM 5847 O O   . HOH   G 4 .   ? -18.114 8.189   0.198   1.00 38.46 ? 631 HOH   A O   1 
HETATM 5848 O O   . HOH   G 4 .   ? -13.263 5.558   19.999  1.00 28.36 ? 632 HOH   A O   1 
HETATM 5849 O O   . HOH   G 4 .   ? -23.155 11.681  -8.327  1.00 32.49 ? 633 HOH   A O   1 
HETATM 5850 O O   . HOH   G 4 .   ? 3.250   14.474  13.220  1.00 41.82 ? 634 HOH   A O   1 
HETATM 5851 O O   . HOH   G 4 .   ? 4.302   16.957  10.143  1.00 43.48 ? 635 HOH   A O   1 
HETATM 5852 O O   . HOH   G 4 .   ? -18.132 8.172   29.892  1.00 37.64 ? 636 HOH   A O   1 
HETATM 5853 O O   . HOH   G 4 .   ? -15.865 -6.088  27.394  1.00 39.73 ? 637 HOH   A O   1 
HETATM 5854 O O   . HOH   G 4 .   ? 6.514   14.750  11.611  1.00 39.16 ? 638 HOH   A O   1 
HETATM 5855 O O   . HOH   G 4 .   ? 4.624   8.495   21.080  1.00 29.56 ? 639 HOH   A O   1 
HETATM 5856 O O   . HOH   G 4 .   ? -13.894 -2.715  12.360  1.00 39.19 ? 640 HOH   A O   1 
HETATM 5857 O O   . HOH   G 4 .   ? -20.317 36.785  5.635   1.00 49.38 ? 641 HOH   A O   1 
HETATM 5858 O O   . HOH   G 4 .   ? -21.261 14.233  33.516  1.00 34.75 ? 642 HOH   A O   1 
HETATM 5859 O O   . HOH   G 4 .   ? -23.982 14.452  29.365  1.00 38.31 ? 643 HOH   A O   1 
HETATM 5860 O O   . HOH   G 4 .   ? -1.520  20.342  35.606  1.00 41.94 ? 644 HOH   A O   1 
HETATM 5861 O O   . HOH   G 4 .   ? -26.365 17.585  9.784   1.00 33.47 ? 645 HOH   A O   1 
HETATM 5862 O O   . HOH   G 4 .   ? -5.660  1.894   16.094  1.00 44.04 ? 646 HOH   A O   1 
HETATM 5863 O O   . HOH   G 4 .   ? -2.652  -1.224  11.843  1.00 44.62 ? 647 HOH   A O   1 
HETATM 5864 O O   . HOH   G 4 .   ? -2.362  -2.777  20.186  1.00 37.19 ? 648 HOH   A O   1 
HETATM 5865 O O   . HOH   G 4 .   ? -9.323  12.712  -4.396  1.00 27.85 ? 649 HOH   A O   1 
HETATM 5866 O O   . HOH   G 4 .   ? -12.624 -3.367  9.727   1.00 39.05 ? 650 HOH   A O   1 
HETATM 5867 O O   . HOH   G 4 .   ? -13.954 -0.913  23.613  1.00 38.68 ? 651 HOH   A O   1 
HETATM 5868 O O   . HOH   G 4 .   ? -7.432  27.488  15.870  1.00 40.64 ? 652 HOH   A O   1 
HETATM 5869 O O   . HOH   G 4 .   ? -28.944 6.187   17.062  1.00 50.92 ? 653 HOH   A O   1 
HETATM 5870 O O   . HOH   G 4 .   ? -19.411 11.907  -6.665  1.00 29.36 ? 654 HOH   A O   1 
HETATM 5871 O O   . HOH   G 4 .   ? -9.678  -1.539  19.480  1.00 28.54 ? 655 HOH   A O   1 
HETATM 5872 O O   . HOH   G 4 .   ? -5.817  17.050  -16.792 1.00 37.05 ? 656 HOH   A O   1 
HETATM 5873 O O   . HOH   G 4 .   ? -9.125  29.127  7.898   1.00 34.59 ? 657 HOH   A O   1 
HETATM 5874 O O   . HOH   G 4 .   ? -15.692 -6.703  43.112  1.00 51.29 ? 658 HOH   A O   1 
HETATM 5875 O O   . HOH   G 4 .   ? -2.255  11.932  -0.856  1.00 34.92 ? 659 HOH   A O   1 
HETATM 5876 O O   . HOH   G 4 .   ? -21.951 15.590  36.606  1.00 40.61 ? 660 HOH   A O   1 
HETATM 5877 O O   . HOH   G 4 .   ? -7.369  -0.952  17.546  1.00 39.75 ? 661 HOH   A O   1 
HETATM 5878 O O   . HOH   G 4 .   ? -31.141 25.724  -1.059  1.00 41.27 ? 662 HOH   A O   1 
HETATM 5879 O O   . HOH   G 4 .   ? -24.685 29.031  18.332  1.00 35.38 ? 663 HOH   A O   1 
HETATM 5880 O O   . HOH   G 4 .   ? 2.578   11.995  22.393  1.00 35.53 ? 664 HOH   A O   1 
HETATM 5881 O O   . HOH   G 4 .   ? -6.783  -1.831  5.569   1.00 34.57 ? 665 HOH   A O   1 
HETATM 5882 O O   . HOH   G 4 .   ? -29.598 31.365  17.350  1.00 45.81 ? 666 HOH   A O   1 
HETATM 5883 O O   . HOH   G 4 .   ? -18.699 8.250   33.484  1.00 33.88 ? 667 HOH   A O   1 
HETATM 5884 O O   . HOH   G 4 .   ? -29.312 24.664  24.731  1.00 54.21 ? 668 HOH   A O   1 
HETATM 5885 O O   . HOH   G 4 .   ? -16.481 -3.875  26.945  1.00 38.77 ? 669 HOH   A O   1 
HETATM 5886 O O   . HOH   G 4 .   ? -7.805  22.002  16.871  1.00 34.53 ? 670 HOH   A O   1 
HETATM 5887 O O   . HOH   G 4 .   ? -23.404 7.779   15.095  1.00 32.27 ? 671 HOH   A O   1 
HETATM 5888 O O   . HOH   G 4 .   ? 12.972  7.378   19.107  1.00 23.75 ? 672 HOH   A O   1 
HETATM 5889 O O   . HOH   G 4 .   ? -8.524  34.244  13.146  1.00 49.85 ? 673 HOH   A O   1 
HETATM 5890 O O   . HOH   G 4 .   ? -26.744 28.134  18.393  1.00 45.30 ? 674 HOH   A O   1 
HETATM 5891 O O   . HOH   G 4 .   ? -15.657 20.077  -16.016 1.00 34.58 ? 675 HOH   A O   1 
HETATM 5892 O O   . HOH   G 4 .   ? -20.607 2.974   36.635  1.00 48.91 ? 676 HOH   A O   1 
HETATM 5893 O O   . HOH   G 4 .   ? -13.183 27.909  32.079  1.00 43.75 ? 677 HOH   A O   1 
HETATM 5894 O O   . HOH   G 4 .   ? -7.281  21.907  13.638  1.00 33.86 ? 678 HOH   A O   1 
HETATM 5895 O O   . HOH   G 4 .   ? -21.742 22.934  11.554  1.00 25.81 ? 679 HOH   A O   1 
HETATM 5896 O O   . HOH   G 4 .   ? -27.696 27.929  30.771  1.00 42.94 ? 680 HOH   A O   1 
HETATM 5897 O O   . HOH   G 4 .   ? -22.577 27.054  25.976  1.00 33.25 ? 681 HOH   A O   1 
HETATM 5898 O O   . HOH   G 4 .   ? -26.134 3.782   24.707  1.00 36.91 ? 682 HOH   A O   1 
HETATM 5899 O O   . HOH   G 4 .   ? -20.850 24.885  -14.960 1.00 33.63 ? 683 HOH   A O   1 
HETATM 5900 O O   . HOH   G 4 .   ? -15.138 2.559   4.621   1.00 33.13 ? 684 HOH   A O   1 
HETATM 5901 O O   . HOH   G 4 .   ? -2.614  18.365  34.466  1.00 32.40 ? 685 HOH   A O   1 
HETATM 5902 O O   . HOH   G 4 .   ? -26.421 13.518  27.782  1.00 36.28 ? 686 HOH   A O   1 
HETATM 5903 O O   . HOH   G 4 .   ? -0.383  36.542  3.022   1.00 40.29 ? 687 HOH   A O   1 
HETATM 5904 O O   . HOH   G 4 .   ? -16.707 33.229  14.462  1.00 33.83 ? 688 HOH   A O   1 
HETATM 5905 O O   . HOH   G 4 .   ? -29.022 34.514  7.939   1.00 41.02 ? 689 HOH   A O   1 
HETATM 5906 O O   . HOH   G 4 .   ? -0.425  37.698  10.369  1.00 38.56 ? 690 HOH   A O   1 
HETATM 5907 O O   . HOH   G 4 .   ? -12.525 24.471  -16.155 1.00 43.28 ? 691 HOH   A O   1 
HETATM 5908 O O   . HOH   G 4 .   ? -13.436 -11.371 29.046  1.00 43.70 ? 692 HOH   A O   1 
HETATM 5909 O O   . HOH   G 4 .   ? -6.401  28.216  -12.645 1.00 39.14 ? 693 HOH   A O   1 
HETATM 5910 O O   . HOH   G 4 .   ? -21.417 14.697  -12.526 1.00 37.73 ? 694 HOH   A O   1 
HETATM 5911 O O   . HOH   G 4 .   ? -9.216  10.213  -9.393  1.00 44.47 ? 695 HOH   A O   1 
HETATM 5912 O O   . HOH   G 4 .   ? -13.240 14.229  -11.461 1.00 39.53 ? 696 HOH   A O   1 
HETATM 5913 O O   . HOH   G 4 .   ? -12.847 3.362   16.004  1.00 28.46 ? 697 HOH   A O   1 
HETATM 5914 O O   . HOH   G 4 .   ? -19.729 2.065   31.375  1.00 36.15 ? 698 HOH   A O   1 
HETATM 5915 O O   . HOH   G 4 .   ? -18.849 32.488  4.931   1.00 31.82 ? 699 HOH   A O   1 
HETATM 5916 O O   . HOH   G 4 .   ? -5.518  33.637  12.152  1.00 49.29 ? 700 HOH   A O   1 
HETATM 5917 O O   . HOH   G 4 .   ? -21.748 20.321  -20.456 1.00 38.55 ? 701 HOH   A O   1 
HETATM 5918 O O   . HOH   G 4 .   ? -13.103 -3.349  41.348  1.00 41.92 ? 702 HOH   A O   1 
HETATM 5919 O O   . HOH   G 4 .   ? -3.784  8.707   38.724  1.00 36.92 ? 703 HOH   A O   1 
HETATM 5920 O O   . HOH   G 4 .   ? -29.625 21.658  31.292  1.00 38.38 ? 704 HOH   A O   1 
HETATM 5921 O O   . HOH   G 4 .   ? -7.820  38.123  0.083   1.00 43.35 ? 705 HOH   A O   1 
HETATM 5922 O O   . HOH   G 4 .   ? -17.843 1.358   17.545  1.00 27.74 ? 706 HOH   A O   1 
HETATM 5923 O O   . HOH   G 4 .   ? -10.518 0.862   3.192   1.00 44.72 ? 707 HOH   A O   1 
HETATM 5924 O O   . HOH   G 4 .   ? -5.942  21.271  37.525  1.00 45.88 ? 708 HOH   A O   1 
HETATM 5925 O O   . HOH   G 4 .   ? -19.011 16.967  41.187  1.00 39.31 ? 709 HOH   A O   1 
HETATM 5926 O O   . HOH   G 4 .   ? -15.379 21.174  43.699  1.00 46.24 ? 710 HOH   A O   1 
HETATM 5927 O O   . HOH   G 4 .   ? -25.932 10.798  26.846  1.00 33.77 ? 711 HOH   A O   1 
HETATM 5928 O O   . HOH   G 4 .   ? -16.899 8.091   35.446  1.00 27.93 ? 712 HOH   A O   1 
HETATM 5929 O O   . HOH   G 4 .   ? -1.439  7.128   33.438  1.00 36.67 ? 713 HOH   A O   1 
HETATM 5930 O O   . HOH   G 4 .   ? -29.450 26.249  29.911  1.00 43.94 ? 714 HOH   A O   1 
HETATM 5931 O O   . HOH   G 4 .   ? -16.408 4.799   -1.849  1.00 45.04 ? 715 HOH   A O   1 
HETATM 5932 O O   . HOH   G 4 .   ? -19.676 31.474  -13.114 1.00 41.24 ? 716 HOH   A O   1 
HETATM 5933 O O   . HOH   G 4 .   ? 11.240  7.966   16.116  1.00 35.14 ? 717 HOH   A O   1 
HETATM 5934 O O   . HOH   G 4 .   ? -17.192 23.202  -16.562 1.00 24.13 ? 718 HOH   A O   1 
HETATM 5935 O O   . HOH   G 4 .   ? -2.024  20.556  10.593  1.00 38.63 ? 719 HOH   A O   1 
HETATM 5936 O O   . HOH   G 4 .   ? 3.827   20.072  15.306  1.00 42.75 ? 720 HOH   A O   1 
HETATM 5937 O O   . HOH   G 4 .   ? -14.346 35.781  17.622  1.00 47.43 ? 721 HOH   A O   1 
HETATM 5938 O O   . HOH   G 4 .   ? -21.247 34.340  6.116   1.00 38.80 ? 722 HOH   A O   1 
HETATM 5939 O O   . HOH   G 4 .   ? -15.311 34.763  24.490  1.00 48.99 ? 723 HOH   A O   1 
HETATM 5940 O O   . HOH   G 4 .   ? 7.212   9.506   20.423  1.00 36.32 ? 724 HOH   A O   1 
HETATM 5941 O O   . HOH   G 4 .   ? -1.267  23.880  -9.595  1.00 37.10 ? 725 HOH   A O   1 
HETATM 5942 O O   . HOH   G 4 .   ? 1.531   18.319  31.923  1.00 49.62 ? 726 HOH   A O   1 
HETATM 5943 O O   . HOH   G 4 .   ? -29.946 34.382  9.996   1.00 40.33 ? 727 HOH   A O   1 
HETATM 5944 O O   . HOH   G 4 .   ? 4.919   2.513   12.377  1.00 42.10 ? 728 HOH   A O   1 
HETATM 5945 O O   . HOH   G 4 .   ? -29.633 28.861  -12.115 1.00 37.05 ? 729 HOH   A O   1 
HETATM 5946 O O   . HOH   G 4 .   ? -12.641 -9.496  27.564  1.00 47.45 ? 730 HOH   A O   1 
HETATM 5947 O O   . HOH   G 4 .   ? -12.375 14.844  14.452  1.00 35.86 ? 731 HOH   A O   1 
HETATM 5948 O O   . HOH   G 4 .   ? -18.004 28.097  -13.544 1.00 35.15 ? 732 HOH   A O   1 
HETATM 5949 O O   . HOH   G 4 .   ? -10.467 23.613  -14.307 1.00 41.72 ? 733 HOH   A O   1 
HETATM 5950 O O   . HOH   G 4 .   ? -27.651 20.599  12.457  1.00 50.00 ? 734 HOH   A O   1 
HETATM 5951 O O   . HOH   G 4 .   ? 8.915   13.989  10.028  1.00 43.78 ? 735 HOH   A O   1 
HETATM 5952 O O   . HOH   G 4 .   ? -19.994 3.078   5.152   1.00 48.72 ? 736 HOH   A O   1 
HETATM 5953 O O   . HOH   G 4 .   ? 2.200   2.579   11.280  1.00 41.61 ? 737 HOH   A O   1 
HETATM 5954 O O   . HOH   G 4 .   ? -11.970 41.153  -0.285  1.00 51.18 ? 738 HOH   A O   1 
HETATM 5955 O O   . HOH   G 4 .   ? -24.234 31.776  -11.453 1.00 45.13 ? 739 HOH   A O   1 
HETATM 5956 O O   . HOH   G 4 .   ? -23.871 29.791  -12.365 1.00 40.89 ? 740 HOH   A O   1 
HETATM 5957 O O   . HOH   G 4 .   ? -8.555  27.880  35.103  1.00 48.35 ? 741 HOH   A O   1 
HETATM 5958 O O   . HOH   G 4 .   ? -2.093  7.444   38.118  1.00 41.72 ? 742 HOH   A O   1 
HETATM 5959 O O   . HOH   G 4 .   ? -16.915 2.316   5.907   1.00 43.75 ? 743 HOH   A O   1 
HETATM 5960 O O   . HOH   G 4 .   ? -18.542 2.105   12.441  1.00 40.38 ? 744 HOH   A O   1 
HETATM 5961 O O   . HOH   G 4 .   ? -23.076 12.379  31.432  1.00 45.09 ? 745 HOH   A O   1 
HETATM 5962 O O   . HOH   G 4 .   ? -4.289  0.420   12.989  1.00 42.20 ? 746 HOH   A O   1 
HETATM 5963 O O   . HOH   G 4 .   ? -29.486 19.892  27.182  1.00 46.14 ? 747 HOH   A O   1 
HETATM 5964 O O   . HOH   G 4 .   ? -14.886 23.531  -16.752 1.00 41.97 ? 748 HOH   A O   1 
HETATM 5965 O O   . HOH   G 4 .   ? -12.346 -0.401  18.183  1.00 46.07 ? 749 HOH   A O   1 
HETATM 5966 O O   . HOH   G 4 .   ? -6.709  12.618  -3.083  1.00 40.62 ? 750 HOH   A O   1 
HETATM 5967 O O   . HOH   G 4 .   ? -10.263 30.579  29.160  1.00 43.85 ? 751 HOH   A O   1 
HETATM 5968 O O   . HOH   G 4 .   ? -25.430 35.826  -2.551  1.00 35.74 ? 752 HOH   A O   1 
HETATM 5969 O O   . HOH   G 4 .   ? -4.855  10.637  0.296   1.00 50.88 ? 753 HOH   A O   1 
HETATM 5970 O O   . HOH   G 4 .   ? -4.775  23.393  -15.041 1.00 39.29 ? 754 HOH   A O   1 
HETATM 5971 O O   . HOH   G 4 .   ? -3.553  -1.474  5.554   1.00 46.84 ? 755 HOH   A O   1 
HETATM 5972 O O   . HOH   G 4 .   ? -19.622 8.567   -1.480  1.00 41.78 ? 756 HOH   A O   1 
HETATM 5973 O O   . HOH   G 4 .   ? -18.261 35.478  15.341  1.00 45.86 ? 757 HOH   A O   1 
HETATM 5974 O O   . HOH   G 4 .   ? -16.229 29.026  -14.584 1.00 44.91 ? 758 HOH   A O   1 
HETATM 5975 O O   . HOH   G 4 .   ? 1.220   0.932   9.032   1.00 42.47 ? 759 HOH   A O   1 
HETATM 5976 O O   . HOH   G 4 .   ? -22.580 5.708   14.568  1.00 45.59 ? 760 HOH   A O   1 
HETATM 5977 O O   . HOH   G 4 .   ? -0.581  4.242   35.009  1.00 37.52 ? 761 HOH   A O   1 
HETATM 5978 O O   . HOH   G 4 .   ? -0.744  12.043  32.756  1.00 48.14 ? 762 HOH   A O   1 
HETATM 5979 O O   . HOH   G 4 .   ? -19.945 15.153  -15.192 1.00 40.07 ? 763 HOH   A O   1 
HETATM 5980 O O   . HOH   G 4 .   ? -16.645 10.901  36.587  1.00 34.97 ? 764 HOH   A O   1 
HETATM 5981 O O   . HOH   G 4 .   ? 4.368   18.227  24.063  1.00 38.74 ? 765 HOH   A O   1 
HETATM 5982 O O   . HOH   G 4 .   ? -17.555 15.709  -15.753 1.00 45.20 ? 766 HOH   A O   1 
HETATM 5983 O O   . HOH   G 4 .   ? 3.116   15.842  23.858  1.00 30.57 ? 767 HOH   A O   1 
HETATM 5984 O O   . HOH   G 4 .   ? -25.603 1.751   21.359  1.00 38.67 ? 768 HOH   A O   1 
HETATM 5985 O O   . HOH   G 4 .   ? -24.546 23.250  11.047  1.00 35.94 ? 769 HOH   A O   1 
HETATM 5986 O O   . HOH   G 4 .   ? -12.994 3.400   -1.260  1.00 51.85 ? 770 HOH   A O   1 
HETATM 5987 O O   . HOH   G 4 .   ? -5.939  19.526  -17.328 1.00 30.84 ? 771 HOH   A O   1 
HETATM 5988 O O   . HOH   G 4 .   ? 8.863   15.312  26.012  1.00 36.20 ? 772 HOH   A O   1 
HETATM 5989 O O   . HOH   G 4 .   ? -4.098  20.668  -16.171 1.00 35.27 ? 773 HOH   A O   1 
HETATM 5990 O O   . HOH   G 4 .   ? -15.549 15.819  -14.738 1.00 43.14 ? 774 HOH   A O   1 
HETATM 5991 O O   . HOH   G 4 .   ? -20.061 12.738  26.601  1.00 33.34 ? 775 HOH   A O   1 
HETATM 5992 O O   . HOH   G 4 .   ? -10.197 29.230  31.539  1.00 47.20 ? 776 HOH   A O   1 
HETATM 5993 O O   . HOH   G 4 .   ? -11.159 0.156   15.618  1.00 39.92 ? 777 HOH   A O   1 
HETATM 5994 O O   . HOH   G 4 .   ? -33.792 34.716  4.227   1.00 44.76 ? 778 HOH   A O   1 
HETATM 5995 O O   . HOH   G 4 .   ? -5.788  14.767  39.315  1.00 46.33 ? 779 HOH   A O   1 
HETATM 5996 O O   . HOH   G 4 .   ? -15.779 31.281  -12.950 1.00 44.86 ? 780 HOH   A O   1 
HETATM 5997 O O   . HOH   G 4 .   ? -13.181 11.876  -12.015 1.00 45.39 ? 781 HOH   A O   1 
HETATM 5998 O O   . HOH   G 4 .   ? -4.838  10.957  -7.208  1.00 29.16 ? 782 HOH   A O   1 
HETATM 5999 O O   . HOH   G 4 .   ? -13.518 35.947  25.372  1.00 52.26 ? 783 HOH   A O   1 
HETATM 6000 O O   . HOH   G 4 .   ? -8.328  1.762   41.722  1.00 39.84 ? 784 HOH   A O   1 
HETATM 6001 O O   . HOH   G 4 .   ? -17.621 -2.596  22.241  1.00 39.32 ? 785 HOH   A O   1 
HETATM 6002 O O   . HOH   G 4 .   ? -20.968 14.557  24.932  1.00 30.34 ? 786 HOH   A O   1 
HETATM 6003 O O   . HOH   G 4 .   ? -20.562 2.699   17.182  1.00 40.94 ? 787 HOH   A O   1 
HETATM 6004 O O   . HOH   G 4 .   ? -28.087 12.740  29.789  1.00 45.45 ? 788 HOH   A O   1 
HETATM 6005 O O   . HOH   G 4 .   ? -20.569 9.312   28.933  1.00 44.18 ? 789 HOH   A O   1 
HETATM 6006 O O   . HOH   G 4 .   ? -16.709 4.206   0.793   1.00 34.23 ? 790 HOH   A O   1 
HETATM 6007 O O   . HOH   G 4 .   ? -18.525 6.513   37.216  1.00 43.62 ? 791 HOH   A O   1 
HETATM 6008 O O   . HOH   G 4 .   ? 4.178   19.160  21.135  1.00 47.93 ? 792 HOH   A O   1 
HETATM 6009 O O   . HOH   G 4 .   ? -8.331  2.778   1.316   1.00 41.96 ? 793 HOH   A O   1 
HETATM 6010 O O   . HOH   G 4 .   ? -8.447  -0.203  15.081  1.00 32.42 ? 794 HOH   A O   1 
HETATM 6011 O O   . HOH   G 4 .   ? -28.895 2.930   23.768  1.00 47.17 ? 795 HOH   A O   1 
HETATM 6012 O O   . HOH   G 4 .   ? -18.212 -1.084  17.663  1.00 39.63 ? 796 HOH   A O   1 
HETATM 6013 O O   . HOH   G 4 .   ? -20.614 10.083  26.812  1.00 42.41 ? 797 HOH   A O   1 
HETATM 6014 O O   . HOH   G 4 .   ? -28.698 26.959  35.233  1.00 42.43 ? 798 HOH   A O   1 
HETATM 6015 O O   . HOH   G 4 .   ? -23.167 9.923   -6.168  1.00 43.74 ? 799 HOH   A O   1 
HETATM 6016 O O   . HOH   G 4 .   ? -22.363 22.695  38.719  1.00 48.84 ? 800 HOH   A O   1 
HETATM 6017 O O   . HOH   G 4 .   ? -8.502  32.397  28.047  1.00 49.57 ? 801 HOH   A O   1 
HETATM 6018 O O   . HOH   G 4 .   ? -4.176  16.860  36.281  1.00 40.22 ? 802 HOH   A O   1 
HETATM 6019 O O   . HOH   G 4 .   ? -4.254  14.047  36.114  1.00 33.22 ? 803 HOH   A O   1 
HETATM 6020 O O   . HOH   G 4 .   ? -21.001 10.397  -4.900  1.00 39.92 ? 804 HOH   A O   1 
HETATM 6021 O O   . HOH   G 4 .   ? -31.519 6.323   18.840  1.00 46.64 ? 805 HOH   A O   1 
HETATM 6022 O O   . HOH   G 4 .   ? -9.754  -4.196  20.229  1.00 42.23 ? 806 HOH   A O   1 
HETATM 6023 O O   . HOH   G 4 .   ? -19.573 9.070   37.746  1.00 45.91 ? 807 HOH   A O   1 
HETATM 6024 O O   . HOH   G 4 .   ? -16.994 -2.918  19.623  1.00 44.52 ? 808 HOH   A O   1 
HETATM 6025 O O   . HOH   H 4 .   ? -48.516 12.502  -15.268 1.00 37.95 ? 501 HOH   B O   1 
HETATM 6026 O O   . HOH   H 4 .   ? -31.443 28.853  -56.623 1.00 49.45 ? 502 HOH   B O   1 
HETATM 6027 O O   . HOH   H 4 .   ? -34.812 -0.934  -15.927 1.00 50.55 ? 503 HOH   B O   1 
HETATM 6028 O O   . HOH   H 4 .   ? -27.298 29.706  1.397   1.00 39.46 ? 504 HOH   B O   1 
HETATM 6029 O O   . HOH   H 4 .   ? -31.947 32.712  -30.201 1.00 29.24 ? 505 HOH   B O   1 
HETATM 6030 O O   . HOH   H 4 .   ? -50.186 16.036  -14.974 1.00 36.58 ? 506 HOH   B O   1 
HETATM 6031 O O   . HOH   H 4 .   ? -36.669 5.377   -32.215 1.00 43.16 ? 507 HOH   B O   1 
HETATM 6032 O O   . HOH   H 4 .   ? -28.167 24.728  -12.482 1.00 30.19 ? 508 HOH   B O   1 
HETATM 6033 O O   . HOH   H 4 .   ? -37.502 -0.012  -10.392 1.00 36.87 ? 509 HOH   B O   1 
HETATM 6034 O O   . HOH   H 4 .   ? -45.423 17.147  -46.172 1.00 34.89 ? 510 HOH   B O   1 
HETATM 6035 O O   . HOH   H 4 .   ? -52.915 22.448  -10.488 1.00 38.31 ? 511 HOH   B O   1 
HETATM 6036 O O   . HOH   H 4 .   ? -31.772 13.430  -28.797 1.00 39.12 ? 512 HOH   B O   1 
HETATM 6037 O O   . HOH   H 4 .   ? -28.062 4.997   -1.168  1.00 39.60 ? 513 HOH   B O   1 
HETATM 6038 O O   . HOH   H 4 .   ? -49.296 16.402  -17.529 1.00 33.28 ? 514 HOH   B O   1 
HETATM 6039 O O   . HOH   H 4 .   ? -36.626 7.700   -39.609 1.00 39.30 ? 515 HOH   B O   1 
HETATM 6040 O O   . HOH   H 4 .   ? -40.301 -6.331  -20.345 1.00 46.32 ? 516 HOH   B O   1 
HETATM 6041 O O   . HOH   H 4 .   ? -38.689 34.422  -13.691 1.00 37.41 ? 517 HOH   B O   1 
HETATM 6042 O O   . HOH   H 4 .   ? -35.661 27.211  -17.730 1.00 26.91 ? 518 HOH   B O   1 
HETATM 6043 O O   . HOH   H 4 .   ? -44.472 2.504   -36.253 1.00 51.73 ? 519 HOH   B O   1 
HETATM 6044 O O   . HOH   H 4 .   ? -32.006 35.027  2.964   1.00 46.37 ? 520 HOH   B O   1 
HETATM 6045 O O   . HOH   H 4 .   ? -32.518 14.177  9.158   1.00 32.43 ? 521 HOH   B O   1 
HETATM 6046 O O   . HOH   H 4 .   ? -48.692 37.981  -28.614 1.00 36.72 ? 522 HOH   B O   1 
HETATM 6047 O O   . HOH   H 4 .   ? -35.072 -2.883  -5.092  1.00 43.91 ? 523 HOH   B O   1 
HETATM 6048 O O   . HOH   H 4 .   ? -46.063 17.425  -11.466 1.00 33.93 ? 524 HOH   B O   1 
HETATM 6049 O O   . HOH   H 4 .   ? -31.389 29.532  -21.151 1.00 22.67 ? 525 HOH   B O   1 
HETATM 6050 O O   . HOH   H 4 .   ? -57.761 21.966  -16.034 1.00 50.94 ? 526 HOH   B O   1 
HETATM 6051 O O   . HOH   H 4 .   ? -45.237 8.357   -16.454 1.00 42.31 ? 527 HOH   B O   1 
HETATM 6052 O O   . HOH   H 4 .   ? -39.232 3.562   4.641   1.00 36.69 ? 528 HOH   B O   1 
HETATM 6053 O O   . HOH   H 4 .   ? -48.838 1.760   -3.205  1.00 33.87 ? 529 HOH   B O   1 
HETATM 6054 O O   . HOH   H 4 .   ? -27.698 14.103  -15.119 1.00 22.79 ? 530 HOH   B O   1 
HETATM 6055 O O   . HOH   H 4 .   ? -31.738 16.511  8.030   1.00 36.77 ? 531 HOH   B O   1 
HETATM 6056 O O   . HOH   H 4 .   ? -48.270 17.558  -13.893 1.00 30.58 ? 532 HOH   B O   1 
HETATM 6057 O O   . HOH   H 4 .   ? -22.253 11.649  -15.154 1.00 43.28 ? 533 HOH   B O   1 
HETATM 6058 O O   . HOH   H 4 .   ? -46.682 26.389  -8.159  1.00 33.87 ? 534 HOH   B O   1 
HETATM 6059 O O   . HOH   H 4 .   ? -21.762 15.165  -17.297 1.00 28.28 ? 535 HOH   B O   1 
HETATM 6060 O O   . HOH   H 4 .   ? -44.409 42.466  -33.922 1.00 28.16 ? 536 HOH   B O   1 
HETATM 6061 O O   . HOH   H 4 .   ? -28.841 27.973  -20.094 1.00 25.07 ? 537 HOH   B O   1 
HETATM 6062 O O   . HOH   H 4 .   ? -43.384 19.986  -11.645 1.00 24.91 ? 538 HOH   B O   1 
HETATM 6063 O O   . HOH   H 4 .   ? -42.179 42.531  -19.674 1.00 41.70 ? 539 HOH   B O   1 
HETATM 6064 O O   . HOH   H 4 .   ? -37.143 13.797  -26.391 1.00 29.25 ? 540 HOH   B O   1 
HETATM 6065 O O   . HOH   H 4 .   ? -43.299 37.326  -43.467 1.00 38.09 ? 541 HOH   B O   1 
HETATM 6066 O O   . HOH   H 4 .   ? -49.950 36.208  -35.014 1.00 40.83 ? 542 HOH   B O   1 
HETATM 6067 O O   . HOH   H 4 .   ? -47.418 18.260  -17.435 1.00 32.26 ? 543 HOH   B O   1 
HETATM 6068 O O   . HOH   H 4 .   ? -30.463 26.582  8.112   1.00 36.57 ? 544 HOH   B O   1 
HETATM 6069 O O   . HOH   H 4 .   ? -27.275 -0.130  -24.773 1.00 47.39 ? 545 HOH   B O   1 
HETATM 6070 O O   . HOH   H 4 .   ? -58.549 19.502  -5.624  1.00 46.32 ? 546 HOH   B O   1 
HETATM 6071 O O   . HOH   H 4 .   ? -39.252 27.175  4.057   1.00 42.04 ? 547 HOH   B O   1 
HETATM 6072 O O   . HOH   H 4 .   ? -32.208 23.132  -34.202 1.00 37.78 ? 548 HOH   B O   1 
HETATM 6073 O O   . HOH   H 4 .   ? -28.788 28.037  -42.952 1.00 43.48 ? 549 HOH   B O   1 
HETATM 6074 O O   . HOH   H 4 .   ? -31.433 15.548  -30.616 1.00 33.32 ? 550 HOH   B O   1 
HETATM 6075 O O   . HOH   H 4 .   ? -42.256 33.719  -17.679 1.00 22.91 ? 551 HOH   B O   1 
HETATM 6076 O O   . HOH   H 4 .   ? -53.531 24.402  -12.718 1.00 40.89 ? 552 HOH   B O   1 
HETATM 6077 O O   . HOH   H 4 .   ? -35.046 22.066  -50.154 1.00 43.38 ? 553 HOH   B O   1 
HETATM 6078 O O   . HOH   H 4 .   ? -40.504 30.081  1.071   1.00 47.10 ? 554 HOH   B O   1 
HETATM 6079 O O   . HOH   H 4 .   ? -31.728 2.660   1.869   1.00 47.49 ? 555 HOH   B O   1 
HETATM 6080 O O   . HOH   H 4 .   ? -51.771 31.265  -13.688 1.00 40.49 ? 556 HOH   B O   1 
HETATM 6081 O O   . HOH   H 4 .   ? -47.888 34.638  -47.882 1.00 37.31 ? 557 HOH   B O   1 
HETATM 6082 O O   . HOH   H 4 .   ? -37.162 7.257   -28.980 1.00 35.78 ? 558 HOH   B O   1 
HETATM 6083 O O   . HOH   H 4 .   ? -43.230 18.798  -19.589 1.00 27.01 ? 559 HOH   B O   1 
HETATM 6084 O O   . HOH   H 4 .   ? -50.113 19.855  6.532   1.00 38.57 ? 560 HOH   B O   1 
HETATM 6085 O O   . HOH   H 4 .   ? -36.410 35.535  -35.926 1.00 27.99 ? 561 HOH   B O   1 
HETATM 6086 O O   . HOH   H 4 .   ? -42.342 38.255  -10.705 1.00 49.23 ? 562 HOH   B O   1 
HETATM 6087 O O   . HOH   H 4 .   ? -35.631 33.839  -44.377 1.00 38.45 ? 563 HOH   B O   1 
HETATM 6088 O O   . HOH   H 4 .   ? -40.589 36.355  -40.112 1.00 31.16 ? 564 HOH   B O   1 
HETATM 6089 O O   . HOH   H 4 .   ? -33.196 0.159   -7.300  1.00 45.10 ? 565 HOH   B O   1 
HETATM 6090 O O   . HOH   H 4 .   ? -43.401 15.111  -12.818 1.00 28.78 ? 566 HOH   B O   1 
HETATM 6091 O O   . HOH   H 4 .   ? -39.214 28.759  -40.301 1.00 25.12 ? 567 HOH   B O   1 
HETATM 6092 O O   . HOH   H 4 .   ? -25.128 6.136   -7.252  1.00 40.95 ? 568 HOH   B O   1 
HETATM 6093 O O   . HOH   H 4 .   ? -40.783 12.143  8.463   1.00 44.63 ? 569 HOH   B O   1 
HETATM 6094 O O   . HOH   H 4 .   ? -28.934 14.811  -51.504 1.00 45.89 ? 570 HOH   B O   1 
HETATM 6095 O O   . HOH   H 4 .   ? -41.844 42.792  -29.384 1.00 24.13 ? 571 HOH   B O   1 
HETATM 6096 O O   . HOH   H 4 .   ? -22.089 12.692  -21.649 1.00 48.12 ? 572 HOH   B O   1 
HETATM 6097 O O   . HOH   H 4 .   ? -33.689 29.468  -10.979 1.00 37.71 ? 573 HOH   B O   1 
HETATM 6098 O O   . HOH   H 4 .   ? -42.309 31.466  -21.301 1.00 23.45 ? 574 HOH   B O   1 
HETATM 6099 O O   . HOH   H 4 .   ? -41.599 6.809   5.779   1.00 39.34 ? 575 HOH   B O   1 
HETATM 6100 O O   . HOH   H 4 .   ? -25.120 18.188  -26.012 1.00 35.93 ? 576 HOH   B O   1 
HETATM 6101 O O   . HOH   H 4 .   ? -25.851 9.301   0.491   1.00 25.56 ? 577 HOH   B O   1 
HETATM 6102 O O   . HOH   H 4 .   ? -40.521 32.999  -19.787 1.00 21.13 ? 578 HOH   B O   1 
HETATM 6103 O O   . HOH   H 4 .   ? -33.074 3.251   -8.124  1.00 35.70 ? 579 HOH   B O   1 
HETATM 6104 O O   . HOH   H 4 .   ? -46.433 24.172  -1.449  1.00 44.70 ? 580 HOH   B O   1 
HETATM 6105 O O   . HOH   H 4 .   ? -48.683 39.684  -30.404 1.00 36.75 ? 581 HOH   B O   1 
HETATM 6106 O O   . HOH   H 4 .   ? -31.080 19.292  -30.968 1.00 35.90 ? 582 HOH   B O   1 
HETATM 6107 O O   . HOH   H 4 .   ? -42.141 31.087  -50.249 1.00 31.96 ? 583 HOH   B O   1 
HETATM 6108 O O   . HOH   H 4 .   ? -48.681 39.660  -18.275 1.00 42.16 ? 584 HOH   B O   1 
HETATM 6109 O O   . HOH   H 4 .   ? -56.769 18.864  -29.557 1.00 48.83 ? 585 HOH   B O   1 
HETATM 6110 O O   . HOH   H 4 .   ? -46.066 1.916   2.460   1.00 42.83 ? 586 HOH   B O   1 
HETATM 6111 O O   . HOH   H 4 .   ? -52.991 8.338   7.051   1.00 39.25 ? 587 HOH   B O   1 
HETATM 6112 O O   . HOH   H 4 .   ? -47.010 37.065  -40.076 1.00 28.78 ? 588 HOH   B O   1 
HETATM 6113 O O   . HOH   H 4 .   ? -28.577 20.888  -31.951 1.00 35.68 ? 589 HOH   B O   1 
HETATM 6114 O O   . HOH   H 4 .   ? -37.479 34.008  -0.363  1.00 44.38 ? 590 HOH   B O   1 
HETATM 6115 O O   . HOH   H 4 .   ? -39.355 21.844  -34.636 1.00 23.10 ? 591 HOH   B O   1 
HETATM 6116 O O   . HOH   H 4 .   ? -41.143 21.359  -11.760 1.00 25.89 ? 592 HOH   B O   1 
HETATM 6117 O O   . HOH   H 4 .   ? -38.051 38.575  -35.488 1.00 34.21 ? 593 HOH   B O   1 
HETATM 6118 O O   . HOH   H 4 .   ? -44.340 9.197   -23.861 1.00 29.09 ? 594 HOH   B O   1 
HETATM 6119 O O   . HOH   H 4 .   ? -45.082 21.467  -39.770 1.00 25.96 ? 595 HOH   B O   1 
HETATM 6120 O O   . HOH   H 4 .   ? -53.711 19.667  -10.754 1.00 40.27 ? 596 HOH   B O   1 
HETATM 6121 O O   . HOH   H 4 .   ? -38.951 17.682  -22.702 1.00 24.07 ? 597 HOH   B O   1 
HETATM 6122 O O   . HOH   H 4 .   ? -46.139 43.173  -30.563 1.00 40.80 ? 598 HOH   B O   1 
HETATM 6123 O O   . HOH   H 4 .   ? -41.499 45.291  -22.197 1.00 34.97 ? 599 HOH   B O   1 
HETATM 6124 O O   . HOH   H 4 .   ? -33.862 38.636  -32.877 1.00 26.74 ? 600 HOH   B O   1 
HETATM 6125 O O   . HOH   H 4 .   ? -47.002 9.309   -18.067 1.00 41.38 ? 601 HOH   B O   1 
HETATM 6126 O O   . HOH   H 4 .   ? -29.429 4.055   -29.969 1.00 40.59 ? 602 HOH   B O   1 
HETATM 6127 O O   . HOH   H 4 .   ? -35.315 24.570  -53.058 1.00 42.31 ? 603 HOH   B O   1 
HETATM 6128 O O   . HOH   H 4 .   ? -49.621 9.863   -30.128 1.00 37.37 ? 604 HOH   B O   1 
HETATM 6129 O O   . HOH   H 4 .   ? -24.323 28.116  -31.541 1.00 36.77 ? 605 HOH   B O   1 
HETATM 6130 O O   . HOH   H 4 .   ? -30.403 36.507  -31.966 1.00 39.78 ? 606 HOH   B O   1 
HETATM 6131 O O   . HOH   H 4 .   ? -43.671 26.493  -3.764  1.00 39.43 ? 607 HOH   B O   1 
HETATM 6132 O O   . HOH   H 4 .   ? -34.676 32.372  -34.255 1.00 25.13 ? 608 HOH   B O   1 
HETATM 6133 O O   . HOH   H 4 .   ? -40.630 15.429  -10.419 1.00 29.29 ? 609 HOH   B O   1 
HETATM 6134 O O   . HOH   H 4 .   ? -35.708 26.218  -4.612  1.00 27.16 ? 610 HOH   B O   1 
HETATM 6135 O O   . HOH   H 4 .   ? -35.523 24.884  -0.740  1.00 32.47 ? 611 HOH   B O   1 
HETATM 6136 O O   . HOH   H 4 .   ? -23.822 5.522   -12.691 1.00 43.11 ? 612 HOH   B O   1 
HETATM 6137 O O   . HOH   H 4 .   ? -38.333 32.185  1.828   1.00 49.65 ? 613 HOH   B O   1 
HETATM 6138 O O   . HOH   H 4 .   ? -31.456 6.469   3.416   1.00 29.91 ? 614 HOH   B O   1 
HETATM 6139 O O   . HOH   H 4 .   ? -54.239 27.816  -22.027 1.00 28.93 ? 615 HOH   B O   1 
HETATM 6140 O O   . HOH   H 4 .   ? -33.491 41.314  -29.911 1.00 23.38 ? 616 HOH   B O   1 
HETATM 6141 O O   . HOH   H 4 .   ? -39.026 21.350  -25.144 1.00 22.41 ? 617 HOH   B O   1 
HETATM 6142 O O   . HOH   H 4 .   ? -44.555 0.311   -10.365 1.00 34.16 ? 618 HOH   B O   1 
HETATM 6143 O O   . HOH   H 4 .   ? -44.713 21.395  11.205  1.00 43.57 ? 619 HOH   B O   1 
HETATM 6144 O O   . HOH   H 4 .   ? -34.852 25.680  -31.559 1.00 23.18 ? 620 HOH   B O   1 
HETATM 6145 O O   . HOH   H 4 .   ? -36.176 41.996  -22.451 1.00 40.33 ? 621 HOH   B O   1 
HETATM 6146 O O   . HOH   H 4 .   ? -51.232 27.626  -2.260  1.00 45.22 ? 622 HOH   B O   1 
HETATM 6147 O O   . HOH   H 4 .   ? -34.161 31.794  -45.275 1.00 35.91 ? 623 HOH   B O   1 
HETATM 6148 O O   . HOH   H 4 .   ? -36.464 33.249  -11.577 1.00 38.48 ? 624 HOH   B O   1 
HETATM 6149 O O   . HOH   H 4 .   ? -28.257 2.981   -16.830 1.00 33.11 ? 625 HOH   B O   1 
HETATM 6150 O O   . HOH   H 4 .   ? -34.074 30.575  -30.292 1.00 29.63 ? 626 HOH   B O   1 
HETATM 6151 O O   . HOH   H 4 .   ? -38.428 -0.075  -28.703 1.00 55.19 ? 627 HOH   B O   1 
HETATM 6152 O O   . HOH   H 4 .   ? -49.359 33.778  -27.583 1.00 31.71 ? 628 HOH   B O   1 
HETATM 6153 O O   . HOH   H 4 .   ? -43.997 36.146  -45.705 1.00 41.21 ? 629 HOH   B O   1 
HETATM 6154 O O   . HOH   H 4 .   ? -35.317 29.821  -27.714 1.00 22.83 ? 630 HOH   B O   1 
HETATM 6155 O O   . HOH   H 4 .   ? -49.935 23.940  -12.690 1.00 33.36 ? 631 HOH   B O   1 
HETATM 6156 O O   . HOH   H 4 .   ? -50.931 22.867  -37.174 1.00 24.40 ? 632 HOH   B O   1 
HETATM 6157 O O   . HOH   H 4 .   ? -53.269 31.266  -31.995 1.00 38.89 ? 633 HOH   B O   1 
HETATM 6158 O O   . HOH   H 4 .   ? -30.727 5.832   1.029   1.00 36.41 ? 634 HOH   B O   1 
HETATM 6159 O O   . HOH   H 4 .   ? -40.062 18.141  -18.979 1.00 27.53 ? 635 HOH   B O   1 
HETATM 6160 O O   . HOH   H 4 .   ? -39.558 16.452  -24.915 1.00 26.81 ? 636 HOH   B O   1 
HETATM 6161 O O   . HOH   H 4 .   ? -41.025 25.769  -52.718 1.00 41.20 ? 637 HOH   B O   1 
HETATM 6162 O O   . HOH   H 4 .   ? -29.573 32.812  -28.798 1.00 23.85 ? 638 HOH   B O   1 
HETATM 6163 O O   . HOH   H 4 .   ? -52.053 29.357  -28.480 1.00 26.69 ? 639 HOH   B O   1 
HETATM 6164 O O   . HOH   H 4 .   ? -24.574 20.767  -22.741 1.00 29.39 ? 640 HOH   B O   1 
HETATM 6165 O O   . HOH   H 4 .   ? -49.532 20.239  -16.840 1.00 31.98 ? 641 HOH   B O   1 
HETATM 6166 O O   . HOH   H 4 .   ? -52.899 19.384  -36.870 1.00 43.30 ? 642 HOH   B O   1 
HETATM 6167 O O   . HOH   H 4 .   ? -30.956 22.751  -52.300 1.00 44.72 ? 643 HOH   B O   1 
HETATM 6168 O O   . HOH   H 4 .   ? -27.297 25.858  2.371   1.00 37.96 ? 644 HOH   B O   1 
HETATM 6169 O O   . HOH   H 4 .   ? -33.706 24.573  -2.676  1.00 29.97 ? 645 HOH   B O   1 
HETATM 6170 O O   . HOH   H 4 .   ? -48.158 15.683  -36.894 1.00 35.71 ? 646 HOH   B O   1 
HETATM 6171 O O   . HOH   H 4 .   ? -46.724 5.690   -33.983 1.00 45.32 ? 647 HOH   B O   1 
HETATM 6172 O O   . HOH   H 4 .   ? -53.775 10.432  -24.967 1.00 48.87 ? 648 HOH   B O   1 
HETATM 6173 O O   . HOH   H 4 .   ? -31.756 7.296   9.337   1.00 29.83 ? 649 HOH   B O   1 
HETATM 6174 O O   . HOH   H 4 .   ? -42.109 28.008  4.397   1.00 39.06 ? 650 HOH   B O   1 
HETATM 6175 O O   . HOH   H 4 .   ? -43.367 34.736  -9.942  1.00 35.37 ? 651 HOH   B O   1 
HETATM 6176 O O   . HOH   H 4 .   ? -52.181 8.754   -22.889 1.00 38.12 ? 652 HOH   B O   1 
HETATM 6177 O O   . HOH   H 4 .   ? -23.586 30.455  -21.162 1.00 40.22 ? 653 HOH   B O   1 
HETATM 6178 O O   . HOH   H 4 .   ? -21.694 10.007  -1.979  1.00 37.56 ? 654 HOH   B O   1 
HETATM 6179 O O   . HOH   H 4 .   ? -52.311 38.551  -21.878 1.00 46.14 ? 655 HOH   B O   1 
HETATM 6180 O O   . HOH   H 4 .   ? -54.872 28.993  -28.725 1.00 36.00 ? 656 HOH   B O   1 
HETATM 6181 O O   . HOH   H 4 .   ? -45.169 11.358  -25.537 1.00 32.96 ? 657 HOH   B O   1 
HETATM 6182 O O   . HOH   H 4 .   ? -42.122 24.337  -2.393  1.00 33.21 ? 658 HOH   B O   1 
HETATM 6183 O O   . HOH   H 4 .   ? -24.157 9.481   -15.021 1.00 32.94 ? 659 HOH   B O   1 
HETATM 6184 O O   . HOH   H 4 .   ? -51.674 32.880  -22.331 1.00 31.68 ? 660 HOH   B O   1 
HETATM 6185 O O   . HOH   H 4 .   ? -56.349 24.787  -7.928  1.00 52.98 ? 661 HOH   B O   1 
HETATM 6186 O O   . HOH   H 4 .   ? -32.840 28.290  -38.369 1.00 40.19 ? 662 HOH   B O   1 
HETATM 6187 O O   . HOH   H 4 .   ? -49.672 25.070  -10.391 1.00 41.48 ? 663 HOH   B O   1 
HETATM 6188 O O   . HOH   H 4 .   ? -46.983 18.514  -39.519 1.00 30.61 ? 664 HOH   B O   1 
HETATM 6189 O O   . HOH   H 4 .   ? -52.150 25.981  -11.810 1.00 47.61 ? 665 HOH   B O   1 
HETATM 6190 O O   . HOH   H 4 .   ? -47.393 9.396   -32.554 1.00 29.80 ? 666 HOH   B O   1 
HETATM 6191 O O   . HOH   H 4 .   ? -48.084 10.274  -16.152 1.00 40.23 ? 667 HOH   B O   1 
HETATM 6192 O O   . HOH   H 4 .   ? -33.615 -3.223  2.122   1.00 43.57 ? 668 HOH   B O   1 
HETATM 6193 O O   . HOH   H 4 .   ? -22.513 25.960  -31.874 1.00 27.68 ? 669 HOH   B O   1 
HETATM 6194 O O   . HOH   H 4 .   ? -53.840 25.440  4.420   1.00 46.37 ? 670 HOH   B O   1 
HETATM 6195 O O   . HOH   H 4 .   ? -52.449 17.027  1.573   1.00 44.79 ? 671 HOH   B O   1 
HETATM 6196 O O   . HOH   H 4 .   ? -50.776 11.941  -31.481 1.00 36.98 ? 672 HOH   B O   1 
HETATM 6197 O O   . HOH   H 4 .   ? -44.896 15.594  -18.301 1.00 31.12 ? 673 HOH   B O   1 
HETATM 6198 O O   . HOH   H 4 .   ? -45.665 21.387  -45.502 1.00 33.54 ? 674 HOH   B O   1 
HETATM 6199 O O   . HOH   H 4 .   ? -24.872 15.307  -29.618 1.00 30.27 ? 675 HOH   B O   1 
HETATM 6200 O O   . HOH   H 4 .   ? -23.859 22.769  -45.132 1.00 43.41 ? 676 HOH   B O   1 
HETATM 6201 O O   . HOH   H 4 .   ? -50.472 -1.889  -33.430 1.00 60.22 ? 677 HOH   B O   1 
HETATM 6202 O O   . HOH   H 4 .   ? -29.170 9.061   -34.822 1.00 36.85 ? 678 HOH   B O   1 
HETATM 6203 O O   . HOH   H 4 .   ? -37.366 24.625  -58.061 1.00 55.06 ? 679 HOH   B O   1 
HETATM 6204 O O   . HOH   H 4 .   ? -41.082 40.915  -15.896 1.00 39.63 ? 680 HOH   B O   1 
HETATM 6205 O O   . HOH   H 4 .   ? -23.489 30.393  -23.602 1.00 36.43 ? 681 HOH   B O   1 
HETATM 6206 O O   . HOH   H 4 .   ? -23.678 8.114   -28.803 1.00 40.48 ? 682 HOH   B O   1 
HETATM 6207 O O   . HOH   H 4 .   ? -50.177 2.646   0.907   1.00 43.30 ? 683 HOH   B O   1 
HETATM 6208 O O   . HOH   H 4 .   ? -32.242 25.376  -35.317 1.00 35.55 ? 684 HOH   B O   1 
HETATM 6209 O O   . HOH   H 4 .   ? -40.614 35.641  -21.026 1.00 23.01 ? 685 HOH   B O   1 
HETATM 6210 O O   . HOH   H 4 .   ? -35.210 25.356  -11.996 1.00 22.63 ? 686 HOH   B O   1 
HETATM 6211 O O   . HOH   H 4 .   ? -30.513 7.027   -33.534 1.00 41.63 ? 687 HOH   B O   1 
HETATM 6212 O O   . HOH   H 4 .   ? -52.355 10.462  -27.391 1.00 45.88 ? 688 HOH   B O   1 
HETATM 6213 O O   . HOH   H 4 .   ? -34.543 27.782  -40.513 1.00 23.39 ? 689 HOH   B O   1 
HETATM 6214 O O   . HOH   H 4 .   ? -39.224 24.844  -51.297 1.00 43.84 ? 690 HOH   B O   1 
HETATM 6215 O O   . HOH   H 4 .   ? -26.134 13.599  -28.049 1.00 43.44 ? 691 HOH   B O   1 
HETATM 6216 O O   . HOH   H 4 .   ? -33.000 32.342  -17.744 1.00 36.86 ? 692 HOH   B O   1 
HETATM 6217 O O   . HOH   H 4 .   ? -24.872 8.372   -3.876  1.00 37.33 ? 693 HOH   B O   1 
HETATM 6218 O O   . HOH   H 4 .   ? -44.883 0.459   0.351   1.00 44.03 ? 694 HOH   B O   1 
HETATM 6219 O O   . HOH   H 4 .   ? -45.899 17.754  -19.632 1.00 28.76 ? 695 HOH   B O   1 
HETATM 6220 O O   . HOH   H 4 .   ? -41.763 27.665  -1.752  1.00 40.49 ? 696 HOH   B O   1 
HETATM 6221 O O   . HOH   H 4 .   ? -44.693 20.308  -3.960  1.00 39.01 ? 697 HOH   B O   1 
HETATM 6222 O O   . HOH   H 4 .   ? -36.908 35.650  -2.561  1.00 44.86 ? 698 HOH   B O   1 
HETATM 6223 O O   . HOH   H 4 .   ? -46.685 0.978   -9.368  1.00 42.41 ? 699 HOH   B O   1 
HETATM 6224 O O   . HOH   H 4 .   ? -24.134 7.314   -19.500 1.00 32.25 ? 700 HOH   B O   1 
HETATM 6225 O O   . HOH   H 4 .   ? -45.472 35.547  -11.563 1.00 36.63 ? 701 HOH   B O   1 
HETATM 6226 O O   . HOH   H 4 .   ? -46.494 28.662  -9.706  1.00 28.82 ? 702 HOH   B O   1 
HETATM 6227 O O   . HOH   H 4 .   ? -29.049 0.303   -12.304 1.00 48.28 ? 703 HOH   B O   1 
HETATM 6228 O O   . HOH   H 4 .   ? -49.854 35.881  -32.469 1.00 26.90 ? 704 HOH   B O   1 
HETATM 6229 O O   . HOH   H 4 .   ? -34.974 34.988  -14.106 1.00 49.38 ? 705 HOH   B O   1 
HETATM 6230 O O   . HOH   H 4 .   ? -52.985 21.172  -22.476 1.00 43.90 ? 706 HOH   B O   1 
HETATM 6231 O O   . HOH   H 4 .   ? -39.201 16.925  10.533  1.00 46.51 ? 707 HOH   B O   1 
HETATM 6232 O O   . HOH   H 4 .   ? -34.677 38.515  -19.653 1.00 36.64 ? 708 HOH   B O   1 
HETATM 6233 O O   . HOH   H 4 .   ? -29.260 11.855  -28.610 1.00 31.13 ? 709 HOH   B O   1 
HETATM 6234 O O   . HOH   H 4 .   ? -33.388 29.758  -53.176 1.00 41.32 ? 710 HOH   B O   1 
HETATM 6235 O O   . HOH   H 4 .   ? -53.878 12.708  -26.128 1.00 38.64 ? 711 HOH   B O   1 
HETATM 6236 O O   . HOH   H 4 .   ? -43.305 15.020  -46.709 1.00 42.43 ? 712 HOH   B O   1 
HETATM 6237 O O   . HOH   H 4 .   ? -60.824 4.596   -11.538 1.00 45.77 ? 713 HOH   B O   1 
HETATM 6238 O O   . HOH   H 4 .   ? -53.592 16.858  -4.292  1.00 43.44 ? 714 HOH   B O   1 
HETATM 6239 O O   . HOH   H 4 .   ? -46.557 32.054  -51.109 1.00 24.74 ? 715 HOH   B O   1 
HETATM 6240 O O   . HOH   H 4 .   ? -28.536 27.814  -30.362 1.00 36.38 ? 716 HOH   B O   1 
HETATM 6241 O O   . HOH   H 4 .   ? -31.853 37.843  -22.551 1.00 43.00 ? 717 HOH   B O   1 
HETATM 6242 O O   . HOH   H 4 .   ? -35.863 11.291  9.857   1.00 42.74 ? 718 HOH   B O   1 
HETATM 6243 O O   . HOH   H 4 .   ? -25.540 6.656   12.204  1.00 36.84 ? 719 HOH   B O   1 
HETATM 6244 O O   . HOH   H 4 .   ? -47.596 38.553  -37.413 1.00 39.40 ? 720 HOH   B O   1 
HETATM 6245 O O   . HOH   H 4 .   ? -27.641 24.793  -39.535 1.00 36.70 ? 721 HOH   B O   1 
HETATM 6246 O O   . HOH   H 4 .   ? -26.819 14.638  -36.658 1.00 41.24 ? 722 HOH   B O   1 
HETATM 6247 O O   . HOH   H 4 .   ? -53.093 9.963   -0.710  1.00 41.10 ? 723 HOH   B O   1 
HETATM 6248 O O   . HOH   H 4 .   ? -33.216 40.948  -26.461 1.00 39.06 ? 724 HOH   B O   1 
HETATM 6249 O O   . HOH   H 4 .   ? -51.999 30.236  4.152   1.00 55.81 ? 725 HOH   B O   1 
HETATM 6250 O O   . HOH   H 4 .   ? -29.477 26.201  0.753   1.00 37.61 ? 726 HOH   B O   1 
HETATM 6251 O O   . HOH   H 4 .   ? -27.816 30.238  -30.004 1.00 32.21 ? 727 HOH   B O   1 
HETATM 6252 O O   . HOH   H 4 .   ? -30.233 27.818  -41.045 1.00 44.74 ? 728 HOH   B O   1 
HETATM 6253 O O   . HOH   H 4 .   ? -50.351 35.402  -29.438 1.00 37.25 ? 729 HOH   B O   1 
HETATM 6254 O O   . HOH   H 4 .   ? -40.647 13.530  -46.733 1.00 42.26 ? 730 HOH   B O   1 
HETATM 6255 O O   . HOH   H 4 .   ? -33.950 33.329  -15.607 1.00 41.01 ? 731 HOH   B O   1 
HETATM 6256 O O   . HOH   H 4 .   ? -35.609 32.208  -52.430 1.00 43.63 ? 732 HOH   B O   1 
HETATM 6257 O O   . HOH   H 4 .   ? -47.828 19.917  -44.152 1.00 39.62 ? 733 HOH   B O   1 
HETATM 6258 O O   . HOH   H 4 .   ? -46.578 3.701   -35.161 1.00 52.81 ? 734 HOH   B O   1 
HETATM 6259 O O   . HOH   H 4 .   ? -30.947 37.397  -24.673 1.00 38.83 ? 735 HOH   B O   1 
HETATM 6260 O O   . HOH   H 4 .   ? -54.661 23.421  -24.647 1.00 48.41 ? 736 HOH   B O   1 
HETATM 6261 O O   . HOH   H 4 .   ? -25.679 2.220   -14.918 1.00 45.54 ? 737 HOH   B O   1 
HETATM 6262 O O   . HOH   H 4 .   ? -26.619 11.364  -50.888 1.00 51.05 ? 738 HOH   B O   1 
HETATM 6263 O O   . HOH   H 4 .   ? -44.604 22.960  -3.094  1.00 37.13 ? 739 HOH   B O   1 
HETATM 6264 O O   . HOH   H 4 .   ? -24.499 2.596   -21.567 1.00 54.58 ? 740 HOH   B O   1 
HETATM 6265 O O   . HOH   H 4 .   ? -40.847 32.975  0.705   1.00 51.50 ? 741 HOH   B O   1 
HETATM 6266 O O   . HOH   H 4 .   ? -35.394 2.009   -9.262  1.00 44.32 ? 742 HOH   B O   1 
HETATM 6267 O O   . HOH   H 4 .   ? -38.140 26.410  7.202   1.00 38.39 ? 743 HOH   B O   1 
HETATM 6268 O O   . HOH   H 4 .   ? -23.598 13.295  -24.796 1.00 45.29 ? 744 HOH   B O   1 
HETATM 6269 O O   . HOH   H 4 .   ? -33.227 27.058  -10.949 1.00 32.15 ? 745 HOH   B O   1 
HETATM 6270 O O   . HOH   H 4 .   ? -26.234 1.744   -19.813 1.00 54.11 ? 746 HOH   B O   1 
HETATM 6271 O O   . HOH   H 4 .   ? -47.201 30.995  -8.760  1.00 34.35 ? 747 HOH   B O   1 
HETATM 6272 O O   . HOH   H 4 .   ? -34.000 32.074  -54.002 1.00 45.27 ? 748 HOH   B O   1 
HETATM 6273 O O   . HOH   H 4 .   ? -49.448 34.566  -39.623 1.00 44.27 ? 749 HOH   B O   1 
HETATM 6274 O O   . HOH   H 4 .   ? -51.899 34.033  -33.587 1.00 43.04 ? 750 HOH   B O   1 
HETATM 6275 O O   . HOH   H 4 .   ? -36.539 29.539  -39.963 1.00 29.35 ? 751 HOH   B O   1 
HETATM 6276 O O   . HOH   H 4 .   ? -54.183 31.947  -14.196 1.00 51.08 ? 752 HOH   B O   1 
HETATM 6277 O O   . HOH   H 4 .   ? -52.086 31.390  -24.160 1.00 32.29 ? 753 HOH   B O   1 
HETATM 6278 O O   . HOH   H 4 .   ? -36.312 -2.839  -9.463  1.00 41.70 ? 754 HOH   B O   1 
HETATM 6279 O O   . HOH   H 4 .   ? -48.386 7.368   -34.022 1.00 42.12 ? 755 HOH   B O   1 
HETATM 6280 O O   . HOH   H 4 .   ? -51.687 34.244  -17.749 1.00 45.30 ? 756 HOH   B O   1 
HETATM 6281 O O   . HOH   H 4 .   ? -20.799 22.967  -30.549 1.00 43.01 ? 757 HOH   B O   1 
HETATM 6282 O O   . HOH   H 4 .   ? -32.298 29.010  -31.558 1.00 34.55 ? 758 HOH   B O   1 
HETATM 6283 O O   . HOH   H 4 .   ? -54.339 28.111  -19.393 1.00 34.94 ? 759 HOH   B O   1 
HETATM 6284 O O   . HOH   H 4 .   ? -32.855 18.238  11.904  1.00 49.73 ? 760 HOH   B O   1 
HETATM 6285 O O   . HOH   H 4 .   ? -23.569 18.619  -23.716 1.00 42.30 ? 761 HOH   B O   1 
HETATM 6286 O O   . HOH   H 4 .   ? -37.584 22.129  -51.090 1.00 40.99 ? 762 HOH   B O   1 
HETATM 6287 O O   . HOH   H 4 .   ? -33.120 27.152  -30.049 1.00 29.82 ? 763 HOH   B O   1 
HETATM 6288 O O   . HOH   H 4 .   ? -54.650 30.267  -18.583 1.00 40.17 ? 764 HOH   B O   1 
HETATM 6289 O O   . HOH   H 4 .   ? -33.636 42.030  -24.379 1.00 42.02 ? 765 HOH   B O   1 
HETATM 6290 O O   . HOH   H 4 .   ? -44.771 10.255  -40.369 1.00 43.91 ? 766 HOH   B O   1 
HETATM 6291 O O   . HOH   H 4 .   ? -51.808 32.009  -27.334 1.00 37.86 ? 767 HOH   B O   1 
HETATM 6292 O O   . HOH   H 4 .   ? -54.471 5.030   -15.037 1.00 51.65 ? 768 HOH   B O   1 
HETATM 6293 O O   . HOH   H 4 .   ? -33.299 27.993  -27.416 1.00 23.18 ? 769 HOH   B O   1 
HETATM 6294 O O   . HOH   H 4 .   ? -43.658 43.353  -31.434 1.00 29.49 ? 770 HOH   B O   1 
HETATM 6295 O O   . HOH   H 4 .   ? -35.571 1.551   -11.849 1.00 48.56 ? 771 HOH   B O   1 
HETATM 6296 O O   . HOH   H 4 .   ? -23.525 6.647   -14.866 1.00 41.25 ? 772 HOH   B O   1 
HETATM 6297 O O   . HOH   H 4 .   ? -52.956 12.346  -31.153 1.00 44.87 ? 773 HOH   B O   1 
HETATM 6298 O O   . HOH   H 4 .   ? -56.317 25.943  -23.076 1.00 39.97 ? 774 HOH   B O   1 
HETATM 6299 O O   . HOH   H 4 .   ? -32.904 28.909  -42.366 1.00 37.18 ? 775 HOH   B O   1 
HETATM 6300 O O   . HOH   H 4 .   ? -34.399 -2.727  -7.902  1.00 39.18 ? 776 HOH   B O   1 
HETATM 6301 O O   . HOH   H 4 .   ? -52.803 33.097  -30.310 1.00 42.05 ? 777 HOH   B O   1 
HETATM 6302 O O   . HOH   H 4 .   ? -30.730 25.661  -31.373 1.00 42.30 ? 778 HOH   B O   1 
HETATM 6303 O O   . HOH   H 4 .   ? -25.612 31.165  -13.146 1.00 47.84 ? 779 HOH   B O   1 
HETATM 6304 O O   . HOH   H 4 .   ? -35.750 -0.059  -13.709 1.00 53.71 ? 780 HOH   B O   1 
HETATM 6305 O O   . HOH   H 4 .   ? -54.588 30.185  -23.205 1.00 34.54 ? 781 HOH   B O   1 
HETATM 6306 O O   . HOH   H 4 .   ? -23.674 17.137  -27.948 1.00 36.90 ? 782 HOH   B O   1 
HETATM 6307 O O   . HOH   H 4 .   ? -31.058 27.233  -34.035 1.00 40.60 ? 783 HOH   B O   1 
HETATM 6308 O O   . HOH   H 4 .   ? -29.926 6.707   -30.961 1.00 41.48 ? 784 HOH   B O   1 
HETATM 6309 O O   . HOH   H 4 .   ? -57.325 25.317  -20.325 1.00 42.88 ? 785 HOH   B O   1 
HETATM 6310 O O   . HOH   H 4 .   ? -28.941 22.383  13.082  1.00 50.53 ? 786 HOH   B O   1 
HETATM 6311 O O   . HOH   H 4 .   ? -56.945 28.880  -26.242 1.00 54.24 ? 787 HOH   B O   1 
HETATM 6312 O O   . HOH   H 4 .   ? -57.269 27.240  -19.189 1.00 45.44 ? 788 HOH   B O   1 
HETATM 6313 O O   . HOH   H 4 .   ? -21.445 18.230  -28.478 1.00 42.93 ? 789 HOH   B O   1 
HETATM 6314 O O   . HOH   H 4 .   ? -56.674 30.418  -24.650 1.00 48.10 ? 790 HOH   B O   1 
# 
