data_9JJ4
# 
_entry.id   9JJ4 
# 
_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   9JJ4         pdb_00009jj4 10.2210/pdb9jj4/pdb 
WWPDB D_1300051445 ?            ?                   
# 
_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                        9JJ4 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-12 
_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           Y 
# 
_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 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
3 non-polymer syn 
;(1Z,3E,5S,7S,8R,9S,10S,11R,13R,15R,16S,18Z,25S)-11-ethyl-2,7-dihydroxy-10-methyl-21,26-diazapentacyclo[23.2.1.09,13.08,15.05,16]octacosa-1(2),3,18-triene-20,27,28-trione
;
496.638   2   ? ? ? ? 
4 water       nat water 18.015    141 ? ? ? ? 
# 
_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 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
3 
;(1Z,3E,5S,7S,8R,9S,10S,11R,13R,15R,16S,18Z,25S)-11-ethyl-2,7-dihydroxy-10-methyl-21,26-diazapentacyclo[23.2.1.09,13.08,15.05,16]octacosa-1(2),3,18-triene-20,27,28-trione
;
E8T 
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 
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 
E8T non-polymer         . 
;(1Z,3E,5S,7S,8R,9S,10S,11R,13R,15R,16S,18Z,25S)-11-ethyl-2,7-dihydroxy-10-methyl-21,26-diazapentacyclo[23.2.1.09,13.08,15.05,16]octacosa-1(2),3,18-triene-20,27,28-trione
;
10-epi-deOH-HSAF                             'C29 H40 N2 O5'     496.638 
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_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 E8T ? ? E8T ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAP ? ? NAP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NAP 1  501 501 NAP NAP A . 
D 3 E8T 1  502 502 E8T HSN A . 
E 3 E8T 1  503 502 E8T HSN A . 
F 2 NAP 1  501 501 NAP NAP B . 
G 4 HOH 1  601 139 HOH HOH A . 
G 4 HOH 2  602 120 HOH HOH A . 
G 4 HOH 3  603 74  HOH HOH A . 
G 4 HOH 4  604 42  HOH HOH A . 
G 4 HOH 5  605 80  HOH HOH A . 
G 4 HOH 6  606 23  HOH HOH A . 
G 4 HOH 7  607 13  HOH HOH A . 
G 4 HOH 8  608 11  HOH HOH A . 
G 4 HOH 9  609 28  HOH HOH A . 
G 4 HOH 10 610 81  HOH HOH A . 
G 4 HOH 11 611 8   HOH HOH A . 
G 4 HOH 12 612 22  HOH HOH A . 
G 4 HOH 13 613 106 HOH HOH A . 
G 4 HOH 14 614 118 HOH HOH A . 
G 4 HOH 15 615 92  HOH HOH A . 
G 4 HOH 16 616 47  HOH HOH A . 
G 4 HOH 17 617 88  HOH HOH A . 
G 4 HOH 18 618 7   HOH HOH A . 
G 4 HOH 19 619 1   HOH HOH A . 
G 4 HOH 20 620 15  HOH HOH A . 
G 4 HOH 21 621 51  HOH HOH A . 
G 4 HOH 22 622 36  HOH HOH A . 
G 4 HOH 23 623 76  HOH HOH A . 
G 4 HOH 24 624 38  HOH HOH A . 
G 4 HOH 25 625 26  HOH HOH A . 
G 4 HOH 26 626 40  HOH HOH A . 
G 4 HOH 27 627 95  HOH HOH A . 
G 4 HOH 28 628 66  HOH HOH A . 
G 4 HOH 29 629 14  HOH HOH A . 
G 4 HOH 30 630 56  HOH HOH A . 
G 4 HOH 31 631 44  HOH HOH A . 
G 4 HOH 32 632 33  HOH HOH A . 
G 4 HOH 33 633 69  HOH HOH A . 
G 4 HOH 34 634 87  HOH HOH A . 
G 4 HOH 35 635 25  HOH HOH A . 
G 4 HOH 36 636 84  HOH HOH A . 
G 4 HOH 37 637 41  HOH HOH A . 
G 4 HOH 38 638 34  HOH HOH A . 
G 4 HOH 39 639 100 HOH HOH A . 
G 4 HOH 40 640 77  HOH HOH A . 
G 4 HOH 41 641 98  HOH HOH A . 
G 4 HOH 42 642 107 HOH HOH A . 
G 4 HOH 43 643 101 HOH HOH A . 
G 4 HOH 44 644 72  HOH HOH A . 
G 4 HOH 45 645 37  HOH HOH A . 
G 4 HOH 46 646 16  HOH HOH A . 
G 4 HOH 47 647 9   HOH HOH A . 
G 4 HOH 48 648 89  HOH HOH A . 
G 4 HOH 49 649 79  HOH HOH A . 
G 4 HOH 50 650 85  HOH HOH A . 
G 4 HOH 51 651 130 HOH HOH A . 
G 4 HOH 52 652 60  HOH HOH A . 
G 4 HOH 53 653 68  HOH HOH A . 
G 4 HOH 54 654 141 HOH HOH A . 
G 4 HOH 55 655 132 HOH HOH A . 
G 4 HOH 56 656 58  HOH HOH A . 
G 4 HOH 57 657 75  HOH HOH A . 
G 4 HOH 58 658 46  HOH HOH A . 
G 4 HOH 59 659 45  HOH HOH A . 
G 4 HOH 60 660 103 HOH HOH A . 
G 4 HOH 61 661 114 HOH HOH A . 
G 4 HOH 62 662 43  HOH HOH A . 
G 4 HOH 63 663 131 HOH HOH A . 
G 4 HOH 64 664 3   HOH HOH A . 
G 4 HOH 65 665 125 HOH HOH A . 
G 4 HOH 66 666 111 HOH HOH A . 
G 4 HOH 67 667 63  HOH HOH A . 
G 4 HOH 68 668 90  HOH HOH A . 
G 4 HOH 69 669 121 HOH HOH A . 
G 4 HOH 70 670 133 HOH HOH A . 
G 4 HOH 71 671 119 HOH HOH A . 
G 4 HOH 72 672 104 HOH HOH A . 
G 4 HOH 73 673 116 HOH HOH A . 
G 4 HOH 74 674 65  HOH HOH A . 
G 4 HOH 75 675 115 HOH HOH A . 
G 4 HOH 76 676 109 HOH HOH A . 
G 4 HOH 77 677 127 HOH HOH A . 
G 4 HOH 78 678 128 HOH HOH A . 
G 4 HOH 79 679 129 HOH HOH A . 
G 4 HOH 80 680 71  HOH HOH A . 
G 4 HOH 81 681 20  HOH HOH A . 
H 4 HOH 1  601 122 HOH HOH B . 
H 4 HOH 2  602 140 HOH HOH B . 
H 4 HOH 3  603 12  HOH HOH B . 
H 4 HOH 4  604 32  HOH HOH B . 
H 4 HOH 5  605 54  HOH HOH B . 
H 4 HOH 6  606 29  HOH HOH B . 
H 4 HOH 7  607 48  HOH HOH B . 
H 4 HOH 8  608 82  HOH HOH B . 
H 4 HOH 9  609 97  HOH HOH B . 
H 4 HOH 10 610 6   HOH HOH B . 
H 4 HOH 11 611 61  HOH HOH B . 
H 4 HOH 12 612 112 HOH HOH B . 
H 4 HOH 13 613 55  HOH HOH B . 
H 4 HOH 14 614 2   HOH HOH B . 
H 4 HOH 15 615 10  HOH HOH B . 
H 4 HOH 16 616 39  HOH HOH B . 
H 4 HOH 17 617 30  HOH HOH B . 
H 4 HOH 18 618 50  HOH HOH B . 
H 4 HOH 19 619 35  HOH HOH B . 
H 4 HOH 20 620 99  HOH HOH B . 
H 4 HOH 21 621 24  HOH HOH B . 
H 4 HOH 22 622 53  HOH HOH B . 
H 4 HOH 23 623 5   HOH HOH B . 
H 4 HOH 24 624 4   HOH HOH B . 
H 4 HOH 25 625 94  HOH HOH B . 
H 4 HOH 26 626 19  HOH HOH B . 
H 4 HOH 27 627 57  HOH HOH B . 
H 4 HOH 28 628 52  HOH HOH B . 
H 4 HOH 29 629 113 HOH HOH B . 
H 4 HOH 30 630 18  HOH HOH B . 
H 4 HOH 31 631 124 HOH HOH B . 
H 4 HOH 32 632 27  HOH HOH B . 
H 4 HOH 33 633 49  HOH HOH B . 
H 4 HOH 34 634 67  HOH HOH B . 
H 4 HOH 35 635 62  HOH HOH B . 
H 4 HOH 36 636 17  HOH HOH B . 
H 4 HOH 37 637 59  HOH HOH B . 
H 4 HOH 38 638 21  HOH HOH B . 
H 4 HOH 39 639 135 HOH HOH B . 
H 4 HOH 40 640 64  HOH HOH B . 
H 4 HOH 41 641 123 HOH HOH B . 
H 4 HOH 42 642 102 HOH HOH B . 
H 4 HOH 43 643 110 HOH HOH B . 
H 4 HOH 44 644 91  HOH HOH B . 
H 4 HOH 45 645 108 HOH HOH B . 
H 4 HOH 46 646 96  HOH HOH B . 
H 4 HOH 47 647 138 HOH HOH B . 
H 4 HOH 48 648 134 HOH HOH B . 
H 4 HOH 49 649 31  HOH HOH B . 
H 4 HOH 50 650 83  HOH HOH B . 
H 4 HOH 51 651 78  HOH HOH B . 
H 4 HOH 52 652 137 HOH HOH B . 
H 4 HOH 53 653 126 HOH HOH B . 
H 4 HOH 54 654 70  HOH HOH B . 
H 4 HOH 55 655 136 HOH HOH B . 
H 4 HOH 56 656 117 HOH HOH B . 
H 4 HOH 57 657 73  HOH HOH B . 
H 4 HOH 58 658 105 HOH HOH B . 
H 4 HOH 59 659 93  HOH HOH B . 
H 4 HOH 60 660 86  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 extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .       2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .       3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .       4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JJ4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     87.719 
_cell.length_a_esd                 ? 
_cell.length_b                     87.719 
_cell.length_b_esd                 ? 
_cell.length_c                     226.086 
_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                         9JJ4 
_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                   9JJ4 
_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             2.79 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.94 
_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   8.5-9.0 
_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         2021-07-17 
_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                                       9JJ4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.597 
_reflns.d_resolution_low                               81.78 
_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                                     28235 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_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                                   0.998 
_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                                    2.60 
_reflns_shell.d_res_low                                     2.74 
_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                             4021 
_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                                  0.789 
_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                                 9JJ4 
_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                            2.60 
_refine.ls_d_res_low                             43.86 
_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                     28137 
_refine.ls_number_reflns_R_free                  1407 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2021 
_refine.ls_R_factor_R_free                       0.2635 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1989 
_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                 28.27 
_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                            0.41 
_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                       2.60 
_refine_hist.d_res_low                        43.86 
_refine_hist.number_atoms_solvent             141 
_refine_hist.number_atoms_total               5781 
_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        5640 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.008  ? 5784 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.015  ? 7874 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.778 ? 2234 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 862  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 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' 2.60 2.69  . . 138 2616 100.00 . . . . 0.2857 . . . . . . . . . . . 0.3997 
'X-RAY DIFFRACTION' 2.69 2.80  . . 138 2610 100.00 . . . . 0.2660 . . . . . . . . . . . 0.3626 
'X-RAY DIFFRACTION' 2.80 2.92  . . 138 2629 100.00 . . . . 0.2509 . . . . . . . . . . . 0.3346 
'X-RAY DIFFRACTION' 2.93 3.08  . . 137 2607 100.00 . . . . 0.2756 . . . . . . . . . . . 0.3718 
'X-RAY DIFFRACTION' 3.08 3.27  . . 140 2657 100.00 . . . . 0.2423 . . . . . . . . . . . 0.3558 
'X-RAY DIFFRACTION' 3.27 3.52  . . 138 2638 100.00 . . . . 0.2210 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 3.52 3.88  . . 141 2665 100.00 . . . . 0.2084 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 3.88 4.44  . . 142 2697 100.00 . . . . 0.1642 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 4.44 5.59  . . 143 2716 100.00 . . . . 0.1543 . . . . . . . . . . . 0.1847 
'X-RAY DIFFRACTION' 5.59 43.86 . . 152 2895 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1925 
# 
_struct.entry_id                     9JJ4 
_struct.title                        'NADP-dependent oxidoreductase complexed with NADP and substrate 1a' 
_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        9JJ4 
_struct_keywords.text            'alcohol dehydrogenase, 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 3 ? 
F N N 2 ? 
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 9JJ4 A 4 ? 354 ? C3PTT2 1 ? 351 ? 1 351 
2 1 9JJ4 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 9JJ4 LEU A 1 ? UNP C3PTT2 ? ? 'expression tag' -2 1 
1 9JJ4 GLY A 2 ? UNP C3PTT2 ? ? 'expression tag' -1 2 
1 9JJ4 SER A 3 ? UNP C3PTT2 ? ? 'expression tag' 0  3 
2 9JJ4 LEU B 1 ? UNP C3PTT2 ? ? 'expression tag' -2 4 
2 9JJ4 GLY B 2 ? UNP C3PTT2 ? ? 'expression tag' -1 5 
2 9JJ4 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)' 6910  ? 
1 MORE         -36   ? 
1 'SSA (A^2)'  27320 ? 
# 
_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  ? LEU A 59  ? TYR A 50  LEU A 56  1 ? 7  
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 ? GLY A 206 ? SER A 192 GLY A 203 1 ? 12 
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 ? MET A 252 ? GLY A 239 MET A 249 1 ? 11 
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 ? THR A 338 ? HIS A 328 THR A 335 1 ? 8  
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 ALA B 196 ? LEU B 205 ? ALA B 193 LEU B 202 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 ? PHE B 250 ? GLY B 239 PHE B 247 1 ? 9  
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 
HELX_P HELX_P29 AD2 SER B 343 ? ASN B 346 ? SER B 340 ASN B 343 5 ? 4  
# 
_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 ? TRP A 109 ? LYS A 104 TRP A 106 
AA4 2  MET A 116 ? PHE A 118 ? MET A 113 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 46  ? N LEU A 43  O ILE A 72  ? O ILE A 69  
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 TRP A 109 ? N TRP A 106 O MET A 116 ? O MET A 113 
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 LYS A 236 ? O LYS A 233 
AA5 4  5  N VAL A 234 ? N VAL A 231 O ASN A 254 ? O ASN A 251 
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 ASN B 254 ? O ASN B 251 N VAL B 234 ? N VAL B 231 
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 VAL B 190 ? O VAL B 187 
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 42  ? N LEU B 39  O ASP B 77  ? O ASP B 74  
AA8 3  4  N MET B 73  ? N MET B 70  O VAL B 90  ? O VAL B 87  
AA8 4  5  N LEU B 89  ? N LEU B 86  O LEU B 124 ? O LEU B 121 
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 LYS B 349 ? O LYS B 346 N THR B 324 ? N THR B 321 
AB1 1  2  N LYS B 107 ? N LYS B 104 O PHE B 118 ? O PHE B 115 
# 
_pdbx_entry_details.entry_id                   9JJ4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 MET A 139 ? ? -98.58  33.20   
2  1 PHE A 153 ? ? -144.27 -65.87  
3  1 ARG A 313 ? ? -68.37  1.18    
4  1 LEU A 316 ? ? -173.75 124.60  
5  1 SER A 338 ? ? 74.41   -38.20  
6  1 SER A 342 ? ? 92.47   -4.68   
7  1 PHE B 153 ? ? -127.76 -67.20  
8  1 SER B 192 ? ? -121.48 -168.10 
9  1 PRO B 277 ? ? -64.74  0.26    
10 1 PHE B 290 ? ? -152.08 80.89   
11 1 PHE B 295 ? ? -69.83  78.25   
12 1 ALA B 318 ? ? -116.06 68.62   
13 1 ALA B 339 ? ? -151.32 46.00   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
E8T C1   C N S 88  
E8T C2   C N S 89  
E8T C3   C N N 90  
E8T C4   C N N 91  
E8T C6   C N N 92  
E8T O5   O N N 93  
E8T C7   C N N 94  
E8T C8   C N N 95  
E8T C9   C N N 96  
E8T C10  C N N 97  
E8T N11  N N N 98  
E8T C12  C N N 99  
E8T C13  C N N 100 
E8T C14  C N N 101 
E8T C15  C N N 102 
E8T C16  C N N 103 
E8T N17  N N N 104 
E8T C18  C N S 105 
E8T C19  C N N 106 
E8T O20  O N N 107 
E8T O21  O N N 108 
E8T C22  C N R 109 
E8T C23  C N R 110 
E8T C24  C N S 111 
E8T C25  C N N 112 
E8T C26  C N N 113 
E8T C27  C N R 114 
E8T C28  C N S 115 
E8T C29  C N N 116 
E8T C30  C N R 117 
E8T C31  C N S 118 
E8T O32  O N N 119 
E8T C33  C N N 120 
E8T C34  C N N 121 
E8T O35  O N N 122 
E8T C36  C N N 123 
E8T HC1  H N N 124 
E8T HC2  H N N 125 
E8T HC3  H N N 126 
E8T HC4A H N N 127 
E8T HC4B H N N 128 
E8T HC7  H N N 129 
E8T HC8  H N N 130 
E8T HC9A H N N 131 
E8T HC9B H N N 132 
E8T H10A H N N 133 
E8T H10B H N N 134 
E8T HN11 H N N 135 
E8T H12B H N N 136 
E8T H12A H N N 137 
E8T HC14 H N N 138 
E8T HN17 H N N 139 
E8T HC18 H N N 140 
E8T HC22 H N N 141 
E8T HC23 H N N 142 
E8T HC24 H N N 143 
E8T H25B H N N 144 
E8T H25A H N N 145 
E8T H26B H N N 146 
E8T H26A H N N 147 
E8T HC27 H N N 148 
E8T HC28 H N N 149 
E8T H29B H N N 150 
E8T H29A H N N 151 
E8T HC30 H N N 152 
E8T HC31 H N N 153 
E8T HO32 H N N 154 
E8T H33C H N N 155 
E8T H33B H N N 156 
E8T H33A H N N 157 
E8T H34B H N N 158 
E8T H34A H N N 159 
E8T HO35 H N N 160 
E8T H36C H N N 161 
E8T H36A H N N 162 
E8T H36B H N N 163 
GLN N    N N N 164 
GLN CA   C N S 165 
GLN C    C N N 166 
GLN O    O N N 167 
GLN CB   C N N 168 
GLN CG   C N N 169 
GLN CD   C N N 170 
GLN OE1  O N N 171 
GLN NE2  N N N 172 
GLN OXT  O N N 173 
GLN H    H N N 174 
GLN H2   H N N 175 
GLN HA   H N N 176 
GLN HB2  H N N 177 
GLN HB3  H N N 178 
GLN HG2  H N N 179 
GLN HG3  H N N 180 
GLN HE21 H N N 181 
GLN HE22 H N N 182 
GLN HXT  H N N 183 
GLU N    N N N 184 
GLU CA   C N S 185 
GLU C    C N N 186 
GLU O    O N N 187 
GLU CB   C N N 188 
GLU CG   C N N 189 
GLU CD   C N N 190 
GLU OE1  O N N 191 
GLU OE2  O N N 192 
GLU OXT  O N N 193 
GLU H    H N N 194 
GLU H2   H N N 195 
GLU HA   H N N 196 
GLU HB2  H N N 197 
GLU HB3  H N N 198 
GLU HG2  H N N 199 
GLU HG3  H N N 200 
GLU HE2  H N N 201 
GLU HXT  H N N 202 
GLY N    N N N 203 
GLY CA   C N N 204 
GLY C    C N N 205 
GLY O    O N N 206 
GLY OXT  O N N 207 
GLY H    H N N 208 
GLY H2   H N N 209 
GLY HA2  H N N 210 
GLY HA3  H N N 211 
GLY HXT  H N N 212 
HIS N    N N N 213 
HIS CA   C N S 214 
HIS C    C N N 215 
HIS O    O N N 216 
HIS CB   C N N 217 
HIS CG   C Y N 218 
HIS ND1  N Y N 219 
HIS CD2  C Y N 220 
HIS CE1  C Y N 221 
HIS NE2  N Y N 222 
HIS OXT  O N N 223 
HIS H    H N N 224 
HIS H2   H N N 225 
HIS HA   H N N 226 
HIS HB2  H N N 227 
HIS HB3  H N N 228 
HIS HD1  H N N 229 
HIS HD2  H N N 230 
HIS HE1  H N N 231 
HIS HE2  H N N 232 
HIS HXT  H N N 233 
HOH O    O N N 234 
HOH H1   H N N 235 
HOH H2   H N N 236 
ILE N    N N N 237 
ILE CA   C N S 238 
ILE C    C N N 239 
ILE O    O N N 240 
ILE CB   C N S 241 
ILE CG1  C N N 242 
ILE CG2  C N N 243 
ILE CD1  C N N 244 
ILE OXT  O N N 245 
ILE H    H N N 246 
ILE H2   H N N 247 
ILE HA   H N N 248 
ILE HB   H N N 249 
ILE HG12 H N N 250 
ILE HG13 H N N 251 
ILE HG21 H N N 252 
ILE HG22 H N N 253 
ILE HG23 H N N 254 
ILE HD11 H N N 255 
ILE HD12 H N N 256 
ILE HD13 H N N 257 
ILE HXT  H N N 258 
LEU N    N N N 259 
LEU CA   C N S 260 
LEU C    C N N 261 
LEU O    O N N 262 
LEU CB   C N N 263 
LEU CG   C N N 264 
LEU CD1  C N N 265 
LEU CD2  C N N 266 
LEU OXT  O N N 267 
LEU H    H N N 268 
LEU H2   H N N 269 
LEU HA   H N N 270 
LEU HB2  H N N 271 
LEU HB3  H N N 272 
LEU HG   H N N 273 
LEU HD11 H N N 274 
LEU HD12 H N N 275 
LEU HD13 H N N 276 
LEU HD21 H N N 277 
LEU HD22 H N N 278 
LEU HD23 H N N 279 
LEU HXT  H N N 280 
LYS N    N N N 281 
LYS CA   C N S 282 
LYS C    C N N 283 
LYS O    O N N 284 
LYS CB   C N N 285 
LYS CG   C N N 286 
LYS CD   C N N 287 
LYS CE   C N N 288 
LYS NZ   N N N 289 
LYS OXT  O N N 290 
LYS H    H N N 291 
LYS H2   H N N 292 
LYS HA   H N N 293 
LYS HB2  H N N 294 
LYS HB3  H N N 295 
LYS HG2  H N N 296 
LYS HG3  H N N 297 
LYS HD2  H N N 298 
LYS HD3  H N N 299 
LYS HE2  H N N 300 
LYS HE3  H N N 301 
LYS HZ1  H N N 302 
LYS HZ2  H N N 303 
LYS HZ3  H N N 304 
LYS HXT  H N N 305 
MET N    N N N 306 
MET CA   C N S 307 
MET C    C N N 308 
MET O    O N N 309 
MET CB   C N N 310 
MET CG   C N N 311 
MET SD   S N N 312 
MET CE   C N N 313 
MET OXT  O N N 314 
MET H    H N N 315 
MET H2   H N N 316 
MET HA   H N N 317 
MET HB2  H N N 318 
MET HB3  H N N 319 
MET HG2  H N N 320 
MET HG3  H N N 321 
MET HE1  H N N 322 
MET HE2  H N N 323 
MET HE3  H N N 324 
MET HXT  H N N 325 
NAP PA   P N R 326 
NAP O1A  O N N 327 
NAP O2A  O N N 328 
NAP O5B  O N N 329 
NAP C5B  C N N 330 
NAP C4B  C N R 331 
NAP O4B  O N N 332 
NAP C3B  C N R 333 
NAP O3B  O N N 334 
NAP C2B  C N R 335 
NAP O2B  O N N 336 
NAP C1B  C N R 337 
NAP N9A  N Y N 338 
NAP C8A  C Y N 339 
NAP N7A  N Y N 340 
NAP C5A  C Y N 341 
NAP C6A  C Y N 342 
NAP N6A  N N N 343 
NAP N1A  N Y N 344 
NAP C2A  C Y N 345 
NAP N3A  N Y N 346 
NAP C4A  C Y N 347 
NAP O3   O N N 348 
NAP PN   P N N 349 
NAP O1N  O N N 350 
NAP O2N  O N N 351 
NAP O5D  O N N 352 
NAP C5D  C N N 353 
NAP C4D  C N R 354 
NAP O4D  O N N 355 
NAP C3D  C N S 356 
NAP O3D  O N N 357 
NAP C2D  C N R 358 
NAP O2D  O N N 359 
NAP C1D  C N R 360 
NAP N1N  N Y N 361 
NAP C2N  C Y N 362 
NAP C3N  C Y N 363 
NAP C7N  C N N 364 
NAP O7N  O N N 365 
NAP N7N  N N N 366 
NAP C4N  C Y N 367 
NAP C5N  C Y N 368 
NAP C6N  C Y N 369 
NAP P2B  P N N 370 
NAP O1X  O N N 371 
NAP O2X  O N N 372 
NAP O3X  O N N 373 
NAP HOA2 H N N 374 
NAP H51A H N N 375 
NAP H52A H N N 376 
NAP H4B  H N N 377 
NAP H3B  H N N 378 
NAP HO3A H N N 379 
NAP H2B  H N N 380 
NAP H1B  H N N 381 
NAP H8A  H N N 382 
NAP H61A H N N 383 
NAP H62A H N N 384 
NAP H2A  H N N 385 
NAP H51N H N N 386 
NAP H52N H N N 387 
NAP H4D  H N N 388 
NAP H3D  H N N 389 
NAP HO3N H N N 390 
NAP H2D  H N N 391 
NAP HO2N H N N 392 
NAP H1D  H N N 393 
NAP H2N  H N N 394 
NAP H71N H N N 395 
NAP H72N H N N 396 
NAP H4N  H N N 397 
NAP H5N  H N N 398 
NAP H6N  H N N 399 
NAP HOP2 H N N 400 
NAP HOP3 H N N 401 
PHE N    N N N 402 
PHE CA   C N S 403 
PHE C    C N N 404 
PHE O    O N N 405 
PHE CB   C N N 406 
PHE CG   C Y N 407 
PHE CD1  C Y N 408 
PHE CD2  C Y N 409 
PHE CE1  C Y N 410 
PHE CE2  C Y N 411 
PHE CZ   C Y N 412 
PHE OXT  O N N 413 
PHE H    H N N 414 
PHE H2   H N N 415 
PHE HA   H N N 416 
PHE HB2  H N N 417 
PHE HB3  H N N 418 
PHE HD1  H N N 419 
PHE HD2  H N N 420 
PHE HE1  H N N 421 
PHE HE2  H N N 422 
PHE HZ   H N N 423 
PHE HXT  H N N 424 
PRO N    N N N 425 
PRO CA   C N S 426 
PRO C    C N N 427 
PRO O    O N N 428 
PRO CB   C N N 429 
PRO CG   C N N 430 
PRO CD   C N N 431 
PRO OXT  O N N 432 
PRO H    H N N 433 
PRO HA   H N N 434 
PRO HB2  H N N 435 
PRO HB3  H N N 436 
PRO HG2  H N N 437 
PRO HG3  H N N 438 
PRO HD2  H N N 439 
PRO HD3  H N N 440 
PRO HXT  H N N 441 
SER N    N N N 442 
SER CA   C N S 443 
SER C    C N N 444 
SER O    O N N 445 
SER CB   C N N 446 
SER OG   O N N 447 
SER OXT  O N N 448 
SER H    H N N 449 
SER H2   H N N 450 
SER HA   H N N 451 
SER HB2  H N N 452 
SER HB3  H N N 453 
SER HG   H N N 454 
SER HXT  H N N 455 
THR N    N N N 456 
THR CA   C N S 457 
THR C    C N N 458 
THR O    O N N 459 
THR CB   C N R 460 
THR OG1  O N N 461 
THR CG2  C N N 462 
THR OXT  O N N 463 
THR H    H N N 464 
THR H2   H N N 465 
THR HA   H N N 466 
THR HB   H N N 467 
THR HG1  H N N 468 
THR HG21 H N N 469 
THR HG22 H N N 470 
THR HG23 H N N 471 
THR HXT  H N N 472 
TRP N    N N N 473 
TRP CA   C N S 474 
TRP C    C N N 475 
TRP O    O N N 476 
TRP CB   C N N 477 
TRP CG   C Y N 478 
TRP CD1  C Y N 479 
TRP CD2  C Y N 480 
TRP NE1  N Y N 481 
TRP CE2  C Y N 482 
TRP CE3  C Y N 483 
TRP CZ2  C Y N 484 
TRP CZ3  C Y N 485 
TRP CH2  C Y N 486 
TRP OXT  O N N 487 
TRP H    H N N 488 
TRP H2   H N N 489 
TRP HA   H N N 490 
TRP HB2  H N N 491 
TRP HB3  H N N 492 
TRP HD1  H N N 493 
TRP HE1  H N N 494 
TRP HE3  H N N 495 
TRP HZ2  H N N 496 
TRP HZ3  H N N 497 
TRP HH2  H N N 498 
TRP HXT  H N N 499 
TYR N    N N N 500 
TYR CA   C N S 501 
TYR C    C N N 502 
TYR O    O N N 503 
TYR CB   C N N 504 
TYR CG   C Y N 505 
TYR CD1  C Y N 506 
TYR CD2  C Y N 507 
TYR CE1  C Y N 508 
TYR CE2  C Y N 509 
TYR CZ   C Y N 510 
TYR OH   O N N 511 
TYR OXT  O N N 512 
TYR H    H N N 513 
TYR H2   H N N 514 
TYR HA   H N N 515 
TYR HB2  H N N 516 
TYR HB3  H N N 517 
TYR HD1  H N N 518 
TYR HD2  H N N 519 
TYR HE1  H N N 520 
TYR HE2  H N N 521 
TYR HH   H N N 522 
TYR HXT  H N N 523 
VAL N    N N N 524 
VAL CA   C N S 525 
VAL C    C N N 526 
VAL O    O N N 527 
VAL CB   C N N 528 
VAL CG1  C N N 529 
VAL CG2  C N N 530 
VAL OXT  O N N 531 
VAL H    H N N 532 
VAL H2   H N N 533 
VAL HA   H N N 534 
VAL HB   H N N 535 
VAL HG11 H N N 536 
VAL HG12 H N N 537 
VAL HG13 H N N 538 
VAL HG21 H N N 539 
VAL HG22 H N N 540 
VAL HG23 H N N 541 
VAL HXT  H N N 542 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
E8T N17 C18  sing N N 83  
E8T N17 C15  sing N N 84  
E8T C18 C12  sing N N 85  
E8T C18 C19  sing N N 86  
E8T C12 C9   sing N N 87  
E8T O20 C15  doub N N 88  
E8T C15 C16  sing N N 89  
E8T C19 O21  doub N N 90  
E8T C19 C16  sing N N 91  
E8T C9  C10  sing N N 92  
E8T C16 C13  doub N Z 93  
E8T C10 N11  sing N N 94  
E8T C13 O35  sing N N 95  
E8T C13 C14  sing N N 96  
E8T N11 C6   sing N N 97  
E8T C14 C3   doub N E 98  
E8T C6  O5   doub N N 99  
E8T C6  C7   sing N N 100 
E8T C7  C8   doub N Z 101 
E8T C3  C1   sing N N 102 
E8T C8  C4   sing N N 103 
E8T C1  C25  sing N N 104 
E8T C1  C2   sing N N 105 
E8T C25 C24  sing N N 106 
E8T C4  C2   sing N N 107 
E8T C2  C22  sing N N 108 
E8T C24 O32  sing N N 109 
E8T C24 C23  sing N N 110 
E8T C22 C23  sing N N 111 
E8T C22 C26  sing N N 112 
E8T C23 C28  sing N N 113 
E8T C26 C27  sing N N 114 
E8T C28 C27  sing N N 115 
E8T C28 C31  sing N N 116 
E8T C27 C29  sing N N 117 
E8T C33 C31  sing N N 118 
E8T C31 C30  sing N N 119 
E8T C29 C30  sing N N 120 
E8T C30 C34  sing N N 121 
E8T C34 C36  sing N N 122 
E8T C1  HC1  sing N N 123 
E8T C2  HC2  sing N N 124 
E8T C3  HC3  sing N N 125 
E8T C4  HC4A sing N N 126 
E8T C4  HC4B sing N N 127 
E8T C7  HC7  sing N N 128 
E8T C8  HC8  sing N N 129 
E8T C9  HC9A sing N N 130 
E8T C9  HC9B sing N N 131 
E8T C10 H10A sing N N 132 
E8T C10 H10B sing N N 133 
E8T N11 HN11 sing N N 134 
E8T C12 H12B sing N N 135 
E8T C12 H12A sing N N 136 
E8T C14 HC14 sing N N 137 
E8T N17 HN17 sing N N 138 
E8T C18 HC18 sing N N 139 
E8T C22 HC22 sing N N 140 
E8T C23 HC23 sing N N 141 
E8T C24 HC24 sing N N 142 
E8T C25 H25B sing N N 143 
E8T C25 H25A sing N N 144 
E8T C26 H26B sing N N 145 
E8T C26 H26A sing N N 146 
E8T C27 HC27 sing N N 147 
E8T C28 HC28 sing N N 148 
E8T C29 H29B sing N N 149 
E8T C29 H29A sing N N 150 
E8T C30 HC30 sing N N 151 
E8T C31 HC31 sing N N 152 
E8T O32 HO32 sing N N 153 
E8T C33 H33C sing N N 154 
E8T C33 H33B sing N N 155 
E8T C33 H33A sing N N 156 
E8T C34 H34B sing N N 157 
E8T C34 H34A sing N N 158 
E8T O35 HO35 sing N N 159 
E8T C36 H36C sing N N 160 
E8T C36 H36A sing N N 161 
E8T C36 H36B sing N N 162 
GLN N   CA   sing N N 163 
GLN N   H    sing N N 164 
GLN N   H2   sing N N 165 
GLN CA  C    sing N N 166 
GLN CA  CB   sing N N 167 
GLN CA  HA   sing N N 168 
GLN C   O    doub N N 169 
GLN C   OXT  sing N N 170 
GLN CB  CG   sing N N 171 
GLN CB  HB2  sing N N 172 
GLN CB  HB3  sing N N 173 
GLN CG  CD   sing N N 174 
GLN CG  HG2  sing N N 175 
GLN CG  HG3  sing N N 176 
GLN CD  OE1  doub N N 177 
GLN CD  NE2  sing N N 178 
GLN NE2 HE21 sing N N 179 
GLN NE2 HE22 sing N N 180 
GLN OXT HXT  sing N N 181 
GLU N   CA   sing N N 182 
GLU N   H    sing N N 183 
GLU N   H2   sing N N 184 
GLU CA  C    sing N N 185 
GLU CA  CB   sing N N 186 
GLU CA  HA   sing N N 187 
GLU C   O    doub N N 188 
GLU C   OXT  sing N N 189 
GLU CB  CG   sing N N 190 
GLU CB  HB2  sing N N 191 
GLU CB  HB3  sing N N 192 
GLU CG  CD   sing N N 193 
GLU CG  HG2  sing N N 194 
GLU CG  HG3  sing N N 195 
GLU CD  OE1  doub N N 196 
GLU CD  OE2  sing N N 197 
GLU OE2 HE2  sing N N 198 
GLU OXT HXT  sing N N 199 
GLY N   CA   sing N N 200 
GLY N   H    sing N N 201 
GLY N   H2   sing N N 202 
GLY CA  C    sing N N 203 
GLY CA  HA2  sing N N 204 
GLY CA  HA3  sing N N 205 
GLY C   O    doub N N 206 
GLY C   OXT  sing N N 207 
GLY OXT HXT  sing N N 208 
HIS N   CA   sing N N 209 
HIS N   H    sing N N 210 
HIS N   H2   sing N N 211 
HIS CA  C    sing N N 212 
HIS CA  CB   sing N N 213 
HIS CA  HA   sing N N 214 
HIS C   O    doub N N 215 
HIS C   OXT  sing N N 216 
HIS CB  CG   sing N N 217 
HIS CB  HB2  sing N N 218 
HIS CB  HB3  sing N N 219 
HIS CG  ND1  sing Y N 220 
HIS CG  CD2  doub Y N 221 
HIS ND1 CE1  doub Y N 222 
HIS ND1 HD1  sing N N 223 
HIS CD2 NE2  sing Y N 224 
HIS CD2 HD2  sing N N 225 
HIS CE1 NE2  sing Y N 226 
HIS CE1 HE1  sing N N 227 
HIS NE2 HE2  sing N N 228 
HIS OXT HXT  sing N N 229 
HOH O   H1   sing N N 230 
HOH O   H2   sing N N 231 
ILE N   CA   sing N N 232 
ILE N   H    sing N N 233 
ILE N   H2   sing N N 234 
ILE CA  C    sing N N 235 
ILE CA  CB   sing N N 236 
ILE CA  HA   sing N N 237 
ILE C   O    doub N N 238 
ILE C   OXT  sing N N 239 
ILE CB  CG1  sing N N 240 
ILE CB  CG2  sing N N 241 
ILE CB  HB   sing N N 242 
ILE CG1 CD1  sing N N 243 
ILE CG1 HG12 sing N N 244 
ILE CG1 HG13 sing N N 245 
ILE CG2 HG21 sing N N 246 
ILE CG2 HG22 sing N N 247 
ILE CG2 HG23 sing N N 248 
ILE CD1 HD11 sing N N 249 
ILE CD1 HD12 sing N N 250 
ILE CD1 HD13 sing N N 251 
ILE OXT HXT  sing N N 252 
LEU N   CA   sing N N 253 
LEU N   H    sing N N 254 
LEU N   H2   sing N N 255 
LEU CA  C    sing N N 256 
LEU CA  CB   sing N N 257 
LEU CA  HA   sing N N 258 
LEU C   O    doub N N 259 
LEU C   OXT  sing N N 260 
LEU CB  CG   sing N N 261 
LEU CB  HB2  sing N N 262 
LEU CB  HB3  sing N N 263 
LEU CG  CD1  sing N N 264 
LEU CG  CD2  sing N N 265 
LEU CG  HG   sing N N 266 
LEU CD1 HD11 sing N N 267 
LEU CD1 HD12 sing N N 268 
LEU CD1 HD13 sing N N 269 
LEU CD2 HD21 sing N N 270 
LEU CD2 HD22 sing N N 271 
LEU CD2 HD23 sing N N 272 
LEU OXT HXT  sing N N 273 
LYS N   CA   sing N N 274 
LYS N   H    sing N N 275 
LYS N   H2   sing N N 276 
LYS CA  C    sing N N 277 
LYS CA  CB   sing N N 278 
LYS CA  HA   sing N N 279 
LYS C   O    doub N N 280 
LYS C   OXT  sing N N 281 
LYS CB  CG   sing N N 282 
LYS CB  HB2  sing N N 283 
LYS CB  HB3  sing N N 284 
LYS CG  CD   sing N N 285 
LYS CG  HG2  sing N N 286 
LYS CG  HG3  sing N N 287 
LYS CD  CE   sing N N 288 
LYS CD  HD2  sing N N 289 
LYS CD  HD3  sing N N 290 
LYS CE  NZ   sing N N 291 
LYS CE  HE2  sing N N 292 
LYS CE  HE3  sing N N 293 
LYS NZ  HZ1  sing N N 294 
LYS NZ  HZ2  sing N N 295 
LYS NZ  HZ3  sing N N 296 
LYS OXT HXT  sing N N 297 
MET N   CA   sing N N 298 
MET N   H    sing N N 299 
MET N   H2   sing N N 300 
MET CA  C    sing N N 301 
MET CA  CB   sing N N 302 
MET CA  HA   sing N N 303 
MET C   O    doub N N 304 
MET C   OXT  sing N N 305 
MET CB  CG   sing N N 306 
MET CB  HB2  sing N N 307 
MET CB  HB3  sing N N 308 
MET CG  SD   sing N N 309 
MET CG  HG2  sing N N 310 
MET CG  HG3  sing N N 311 
MET SD  CE   sing N N 312 
MET CE  HE1  sing N N 313 
MET CE  HE2  sing N N 314 
MET CE  HE3  sing N N 315 
MET OXT HXT  sing N N 316 
NAP PA  O1A  doub N N 317 
NAP PA  O2A  sing N N 318 
NAP PA  O5B  sing N N 319 
NAP PA  O3   sing N N 320 
NAP O2A HOA2 sing N N 321 
NAP O5B C5B  sing N N 322 
NAP C5B C4B  sing N N 323 
NAP C5B H51A sing N N 324 
NAP C5B H52A sing N N 325 
NAP C4B O4B  sing N N 326 
NAP C4B C3B  sing N N 327 
NAP C4B H4B  sing N N 328 
NAP O4B C1B  sing N N 329 
NAP C3B O3B  sing N N 330 
NAP C3B C2B  sing N N 331 
NAP C3B H3B  sing N N 332 
NAP O3B HO3A sing N N 333 
NAP C2B O2B  sing N N 334 
NAP C2B C1B  sing N N 335 
NAP C2B H2B  sing N N 336 
NAP O2B P2B  sing N N 337 
NAP C1B N9A  sing N N 338 
NAP C1B H1B  sing N N 339 
NAP N9A C8A  sing Y N 340 
NAP N9A C4A  sing Y N 341 
NAP C8A N7A  doub Y N 342 
NAP C8A H8A  sing N N 343 
NAP N7A C5A  sing Y N 344 
NAP C5A C6A  sing Y N 345 
NAP C5A C4A  doub Y N 346 
NAP C6A N6A  sing N N 347 
NAP C6A N1A  doub Y N 348 
NAP N6A H61A sing N N 349 
NAP N6A H62A sing N N 350 
NAP N1A C2A  sing Y N 351 
NAP C2A N3A  doub Y N 352 
NAP C2A H2A  sing N N 353 
NAP N3A C4A  sing Y N 354 
NAP O3  PN   sing N N 355 
NAP PN  O1N  doub N N 356 
NAP PN  O2N  sing N N 357 
NAP PN  O5D  sing N N 358 
NAP O5D C5D  sing N N 359 
NAP C5D C4D  sing N N 360 
NAP C5D H51N sing N N 361 
NAP C5D H52N sing N N 362 
NAP C4D O4D  sing N N 363 
NAP C4D C3D  sing N N 364 
NAP C4D H4D  sing N N 365 
NAP O4D C1D  sing N N 366 
NAP C3D O3D  sing N N 367 
NAP C3D C2D  sing N N 368 
NAP C3D H3D  sing N N 369 
NAP O3D HO3N sing N N 370 
NAP C2D O2D  sing N N 371 
NAP C2D C1D  sing N N 372 
NAP C2D H2D  sing N N 373 
NAP O2D HO2N sing N N 374 
NAP C1D N1N  sing N N 375 
NAP C1D H1D  sing N N 376 
NAP N1N C2N  sing Y N 377 
NAP N1N C6N  doub Y N 378 
NAP C2N C3N  doub Y N 379 
NAP C2N H2N  sing N N 380 
NAP C3N C7N  sing N N 381 
NAP C3N C4N  sing Y N 382 
NAP C7N O7N  doub N N 383 
NAP C7N N7N  sing N N 384 
NAP N7N H71N sing N N 385 
NAP N7N H72N sing N N 386 
NAP C4N C5N  doub Y N 387 
NAP C4N H4N  sing N N 388 
NAP C5N C6N  sing Y N 389 
NAP C5N H5N  sing N N 390 
NAP C6N H6N  sing N N 391 
NAP P2B O1X  doub N N 392 
NAP P2B O2X  sing N N 393 
NAP P2B O3X  sing N N 394 
NAP O2X HOP2 sing N N 395 
NAP O3X HOP3 sing N N 396 
PHE N   CA   sing N N 397 
PHE N   H    sing N N 398 
PHE N   H2   sing N N 399 
PHE CA  C    sing N N 400 
PHE CA  CB   sing N N 401 
PHE CA  HA   sing N N 402 
PHE C   O    doub N N 403 
PHE C   OXT  sing N N 404 
PHE CB  CG   sing N N 405 
PHE CB  HB2  sing N N 406 
PHE CB  HB3  sing N N 407 
PHE CG  CD1  doub Y N 408 
PHE CG  CD2  sing Y N 409 
PHE CD1 CE1  sing Y N 410 
PHE CD1 HD1  sing N N 411 
PHE CD2 CE2  doub Y N 412 
PHE CD2 HD2  sing N N 413 
PHE CE1 CZ   doub Y N 414 
PHE CE1 HE1  sing N N 415 
PHE CE2 CZ   sing Y N 416 
PHE CE2 HE2  sing N N 417 
PHE CZ  HZ   sing N N 418 
PHE OXT HXT  sing N N 419 
PRO N   CA   sing N N 420 
PRO N   CD   sing N N 421 
PRO N   H    sing N N 422 
PRO CA  C    sing N N 423 
PRO CA  CB   sing N N 424 
PRO CA  HA   sing N N 425 
PRO C   O    doub N N 426 
PRO C   OXT  sing N N 427 
PRO CB  CG   sing N N 428 
PRO CB  HB2  sing N N 429 
PRO CB  HB3  sing N N 430 
PRO CG  CD   sing N N 431 
PRO CG  HG2  sing N N 432 
PRO CG  HG3  sing N N 433 
PRO CD  HD2  sing N N 434 
PRO CD  HD3  sing N N 435 
PRO OXT HXT  sing N N 436 
SER N   CA   sing N N 437 
SER N   H    sing N N 438 
SER N   H2   sing N N 439 
SER CA  C    sing N N 440 
SER CA  CB   sing N N 441 
SER CA  HA   sing N N 442 
SER C   O    doub N N 443 
SER C   OXT  sing N N 444 
SER CB  OG   sing N N 445 
SER CB  HB2  sing N N 446 
SER CB  HB3  sing N N 447 
SER OG  HG   sing N N 448 
SER OXT HXT  sing N N 449 
THR N   CA   sing N N 450 
THR N   H    sing N N 451 
THR N   H2   sing N N 452 
THR CA  C    sing N N 453 
THR CA  CB   sing N N 454 
THR CA  HA   sing N N 455 
THR C   O    doub N N 456 
THR C   OXT  sing N N 457 
THR CB  OG1  sing N N 458 
THR CB  CG2  sing N N 459 
THR CB  HB   sing N N 460 
THR OG1 HG1  sing N N 461 
THR CG2 HG21 sing N N 462 
THR CG2 HG22 sing N N 463 
THR CG2 HG23 sing N N 464 
THR OXT HXT  sing N N 465 
TRP N   CA   sing N N 466 
TRP N   H    sing N N 467 
TRP N   H2   sing N N 468 
TRP CA  C    sing N N 469 
TRP CA  CB   sing N N 470 
TRP CA  HA   sing N N 471 
TRP C   O    doub N N 472 
TRP C   OXT  sing N N 473 
TRP CB  CG   sing N N 474 
TRP CB  HB2  sing N N 475 
TRP CB  HB3  sing N N 476 
TRP CG  CD1  doub Y N 477 
TRP CG  CD2  sing Y N 478 
TRP CD1 NE1  sing Y N 479 
TRP CD1 HD1  sing N N 480 
TRP CD2 CE2  doub Y N 481 
TRP CD2 CE3  sing Y N 482 
TRP NE1 CE2  sing Y N 483 
TRP NE1 HE1  sing N N 484 
TRP CE2 CZ2  sing Y N 485 
TRP CE3 CZ3  doub Y N 486 
TRP CE3 HE3  sing N N 487 
TRP CZ2 CH2  doub Y N 488 
TRP CZ2 HZ2  sing N N 489 
TRP CZ3 CH2  sing Y N 490 
TRP CZ3 HZ3  sing N N 491 
TRP CH2 HH2  sing N N 492 
TRP OXT HXT  sing N N 493 
TYR N   CA   sing N N 494 
TYR N   H    sing N N 495 
TYR N   H2   sing N N 496 
TYR CA  C    sing N N 497 
TYR CA  CB   sing N N 498 
TYR CA  HA   sing N N 499 
TYR C   O    doub N N 500 
TYR C   OXT  sing N N 501 
TYR CB  CG   sing N N 502 
TYR CB  HB2  sing N N 503 
TYR CB  HB3  sing N N 504 
TYR CG  CD1  doub Y N 505 
TYR CG  CD2  sing Y N 506 
TYR CD1 CE1  sing Y N 507 
TYR CD1 HD1  sing N N 508 
TYR CD2 CE2  doub Y N 509 
TYR CD2 HD2  sing N N 510 
TYR CE1 CZ   doub Y N 511 
TYR CE1 HE1  sing N N 512 
TYR CE2 CZ   sing Y N 513 
TYR CE2 HE2  sing N N 514 
TYR CZ  OH   sing N N 515 
TYR OH  HH   sing N N 516 
TYR OXT HXT  sing N N 517 
VAL N   CA   sing N N 518 
VAL N   H    sing N N 519 
VAL N   H2   sing N N 520 
VAL CA  C    sing N N 521 
VAL CA  CB   sing N N 522 
VAL CA  HA   sing N N 523 
VAL C   O    doub N N 524 
VAL C   OXT  sing N N 525 
VAL CB  CG1  sing N N 526 
VAL CB  CG2  sing N N 527 
VAL CB  HB   sing N N 528 
VAL CG1 HG11 sing N N 529 
VAL CG1 HG12 sing N N 530 
VAL CG1 HG13 sing N N 531 
VAL CG2 HG21 sing N N 532 
VAL CG2 HG22 sing N N 533 
VAL CG2 HG23 sing N N 534 
VAL OXT HXT  sing N N 535 
# 
_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                    9JJ4 
_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]   0.011400 
_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]   0.011400 
_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]   0.004423 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   ? -14.561 -1.001  48.947  1.00 81.03  ? -2  LEU A N   1 
ATOM   2    C CA  . LEU A 1 1   ? -15.439 0.051   48.442  1.00 88.03  ? -2  LEU A CA  1 
ATOM   3    C C   . LEU A 1 1   ? -14.714 1.401   48.435  1.00 90.45  ? -2  LEU A C   1 
ATOM   4    O O   . LEU A 1 1   ? -15.062 2.325   49.176  1.00 92.74  ? -2  LEU A O   1 
ATOM   5    C CB  . LEU A 1 1   ? -16.725 0.124   49.282  1.00 96.46  ? -2  LEU A CB  1 
ATOM   6    C CG  . LEU A 1 1   ? -17.568 -1.161  49.358  1.00 98.89  ? -2  LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 1   ? -17.552 -1.774  50.767  1.00 90.11  ? -2  LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 1   ? -19.002 -0.919  48.874  1.00 93.31  ? -2  LEU A CD2 1 
ATOM   9    N N   . GLY A 1 2   ? -13.692 1.500   47.578  1.00 83.03  ? -1  GLY A N   1 
ATOM   10   C CA  . GLY A 1 2   ? -12.854 2.675   47.521  1.00 64.95  ? -1  GLY A CA  1 
ATOM   11   C C   . GLY A 1 2   ? -13.386 3.741   46.580  1.00 61.13  ? -1  GLY A C   1 
ATOM   12   O O   . GLY A 1 2   ? -14.407 3.591   45.900  1.00 54.96  ? -1  GLY A O   1 
ATOM   13   N N   . SER A 1 3   ? -12.660 4.851   46.559  1.00 52.28  ? 0   SER A N   1 
ATOM   14   C CA  . SER A 1 3   ? -13.010 5.991   45.736  1.00 50.50  ? 0   SER A CA  1 
ATOM   15   C C   . SER A 1 3   ? -11.760 6.844   45.605  1.00 56.01  ? 0   SER A C   1 
ATOM   16   O O   . SER A 1 3   ? -10.813 6.707   46.386  1.00 53.51  ? 0   SER A O   1 
ATOM   17   C CB  . SER A 1 3   ? -14.166 6.797   46.337  1.00 46.36  ? 0   SER A CB  1 
ATOM   18   O OG  . SER A 1 3   ? -13.668 7.775   47.227  1.00 43.80  ? 0   SER A OG  1 
ATOM   19   N N   . MET A 1 4   ? -11.763 7.726   44.609  1.00 51.16  ? 1   MET A N   1 
ATOM   20   C CA  . MET A 1 4   ? -10.593 8.541   44.352  1.00 46.02  ? 1   MET A CA  1 
ATOM   21   C C   . MET A 1 4   ? -11.010 9.961   44.014  1.00 46.99  ? 1   MET A C   1 
ATOM   22   O O   . MET A 1 4   ? -12.127 10.214  43.552  1.00 48.03  ? 1   MET A O   1 
ATOM   23   C CB  . MET A 1 4   ? -9.747  7.958   43.222  1.00 49.63  ? 1   MET A CB  1 
ATOM   24   C CG  . MET A 1 4   ? -10.376 8.063   41.846  1.00 50.43  ? 1   MET A CG  1 
ATOM   25   S SD  . MET A 1 4   ? -9.188  7.518   40.614  1.00 51.26  ? 1   MET A SD  1 
ATOM   26   C CE  . MET A 1 4   ? -7.822  8.634   40.898  1.00 37.67  ? 1   MET A CE  1 
ATOM   27   N N   . LYS A 1 5   ? -10.080 10.885  44.261  1.00 47.33  ? 2   LYS A N   1 
ATOM   28   C CA  . LYS A 1 5   ? -10.249 12.286  43.904  1.00 54.75  ? 2   LYS A CA  1 
ATOM   29   C C   . LYS A 1 5   ? -9.944  12.487  42.425  1.00 50.54  ? 2   LYS A C   1 
ATOM   30   O O   . LYS A 1 5   ? -8.884  12.076  41.945  1.00 49.70  ? 2   LYS A O   1 
ATOM   31   C CB  . LYS A 1 5   ? -9.328  13.175  44.748  1.00 52.77  ? 2   LYS A CB  1 
ATOM   32   C CG  . LYS A 1 5   ? -9.653  13.235  46.239  1.00 63.03  ? 2   LYS A CG  1 
ATOM   33   C CD  . LYS A 1 5   ? -8.676  14.122  47.015  1.00 67.38  ? 2   LYS A CD  1 
ATOM   34   C CE  . LYS A 1 5   ? -9.052  14.173  48.492  1.00 70.19  ? 2   LYS A CE  1 
ATOM   35   N NZ  . LYS A 1 5   ? -8.089  15.018  49.267  1.00 66.91  ? 2   LYS A NZ  1 
ATOM   36   N N   . THR A 1 6   ? -10.880 13.116  41.711  1.00 41.22  ? 3   THR A N   1 
ATOM   37   C CA  . THR A 1 6   ? -10.725 13.505  40.319  1.00 45.09  ? 3   THR A CA  1 
ATOM   38   C C   . THR A 1 6   ? -11.156 14.957  40.153  1.00 48.88  ? 3   THR A C   1 
ATOM   39   O O   . THR A 1 6   ? -11.966 15.470  40.921  1.00 54.24  ? 3   THR A O   1 
ATOM   40   C CB  . THR A 1 6   ? -11.579 12.634  39.380  1.00 49.80  ? 3   THR A CB  1 
ATOM   41   O OG1 . THR A 1 6   ? -12.949 13.057  39.454  1.00 49.61  ? 3   THR A OG1 1 
ATOM   42   C CG2 . THR A 1 6   ? -11.494 11.164  39.755  1.00 46.28  ? 3   THR A CG2 1 
ATOM   43   N N   . GLU A 1 7   ? -10.640 15.615  39.124  1.00 50.99  ? 4   GLU A N   1 
ATOM   44   C CA  . GLU A 1 7   ? -11.116 16.939  38.755  1.00 51.46  ? 4   GLU A CA  1 
ATOM   45   C C   . GLU A 1 7   ? -11.866 16.878  37.427  1.00 53.95  ? 4   GLU A C   1 
ATOM   46   O O   . GLU A 1 7   ? -11.547 16.070  36.544  1.00 50.49  ? 4   GLU A O   1 
ATOM   47   C CB  . GLU A 1 7   ? -9.963  17.939  38.655  1.00 49.61  ? 4   GLU A CB  1 
ATOM   48   C CG  . GLU A 1 7   ? -9.432  18.448  39.977  1.00 50.84  ? 4   GLU A CG  1 
ATOM   49   C CD  . GLU A 1 7   ? -8.152  19.248  39.790  1.00 58.07  ? 4   GLU A CD  1 
ATOM   50   O OE1 . GLU A 1 7   ? -7.417  18.958  38.826  1.00 65.34  ? 4   GLU A OE1 1 
ATOM   51   O OE2 . GLU A 1 7   ? -7.875  20.173  40.583  1.00 59.20  ? 4   GLU A OE2 1 
ATOM   52   N N   . ARG A 1 8   ? -12.868 17.742  37.290  1.00 48.39  ? 5   ARG A N   1 
ATOM   53   C CA  . ARG A 1 8   ? -13.680 17.781  36.083  1.00 51.27  ? 5   ARG A CA  1 
ATOM   54   C C   . ARG A 1 8   ? -13.990 19.225  35.703  1.00 53.33  ? 5   ARG A C   1 
ATOM   55   O O   . ARG A 1 8   ? -14.147 20.093  36.568  1.00 54.70  ? 5   ARG A O   1 
ATOM   56   C CB  . ARG A 1 8   ? -14.986 17.000  36.266  1.00 45.11  ? 5   ARG A CB  1 
ATOM   57   C CG  . ARG A 1 8   ? -14.781 15.549  36.660  1.00 45.75  ? 5   ARG A CG  1 
ATOM   58   C CD  . ARG A 1 8   ? -16.100 14.823  36.635  1.00 49.33  ? 5   ARG A CD  1 
ATOM   59   N NE  . ARG A 1 8   ? -17.132 15.639  37.262  1.00 57.37  ? 5   ARG A NE  1 
ATOM   60   C CZ  . ARG A 1 8   ? -18.432 15.496  37.048  1.00 56.78  ? 5   ARG A CZ  1 
ATOM   61   N NH1 . ARG A 1 8   ? -18.894 14.586  36.202  1.00 52.74  ? 5   ARG A NH1 1 
ATOM   62   N NH2 . ARG A 1 8   ? -19.286 16.289  37.694  1.00 49.98  ? 5   ARG A NH2 1 
ATOM   63   N N   . TRP A 1 9   ? -14.063 19.477  34.398  1.00 51.11  ? 6   TRP A N   1 
ATOM   64   C CA  . TRP A 1 9   ? -14.612 20.723  33.876  1.00 48.59  ? 6   TRP A CA  1 
ATOM   65   C C   . TRP A 1 9   ? -16.069 20.494  33.497  1.00 44.46  ? 6   TRP A C   1 
ATOM   66   O O   . TRP A 1 9   ? -16.385 19.573  32.733  1.00 44.12  ? 6   TRP A O   1 
ATOM   67   C CB  . TRP A 1 9   ? -13.825 21.227  32.671  1.00 42.51  ? 6   TRP A CB  1 
ATOM   68   C CG  . TRP A 1 9   ? -12.492 21.787  33.003  1.00 42.12  ? 6   TRP A CG  1 
ATOM   69   C CD1 . TRP A 1 9   ? -11.292 21.140  32.925  1.00 44.37  ? 6   TRP A CD1 1 
ATOM   70   C CD2 . TRP A 1 9   ? -12.199 23.119  33.439  1.00 40.65  ? 6   TRP A CD2 1 
ATOM   71   N NE1 . TRP A 1 9   ? -10.268 21.983  33.288  1.00 41.57  ? 6   TRP A NE1 1 
ATOM   72   C CE2 . TRP A 1 9   ? -10.799 23.206  33.609  1.00 42.71  ? 6   TRP A CE2 1 
ATOM   73   C CE3 . TRP A 1 9   ? -12.982 24.247  33.706  1.00 43.35  ? 6   TRP A CE3 1 
ATOM   74   C CZ2 . TRP A 1 9   ? -10.163 24.382  34.027  1.00 41.33  ? 6   TRP A CZ2 1 
ATOM   75   C CZ3 . TRP A 1 9   ? -12.349 25.410  34.132  1.00 42.13  ? 6   TRP A CZ3 1 
ATOM   76   C CH2 . TRP A 1 9   ? -10.953 25.467  34.283  1.00 37.98  ? 6   TRP A CH2 1 
ATOM   77   N N   . VAL A 1 10  ? -16.951 21.322  34.041  1.00 46.65  ? 7   VAL A N   1 
ATOM   78   C CA  . VAL A 1 10  ? -18.382 21.127  33.869  1.00 49.89  ? 7   VAL A CA  1 
ATOM   79   C C   . VAL A 1 10  ? -18.991 22.369  33.242  1.00 45.30  ? 7   VAL A C   1 
ATOM   80   O O   . VAL A 1 10  ? -18.449 23.475  33.313  1.00 45.36  ? 7   VAL A O   1 
ATOM   81   C CB  . VAL A 1 10  ? -19.090 20.783  35.196  1.00 51.20  ? 7   VAL A CB  1 
ATOM   82   C CG1 . VAL A 1 10  ? -18.696 19.380  35.641  1.00 51.91  ? 7   VAL A CG1 1 
ATOM   83   C CG2 . VAL A 1 10  ? -18.759 21.821  36.280  1.00 48.92  ? 7   VAL A CG2 1 
ATOM   84   N N   . VAL A 1 11  ? -20.146 22.168  32.622  1.00 48.48  ? 8   VAL A N   1 
ATOM   85   C CA  . VAL A 1 11  ? -20.837 23.247  31.934  1.00 50.79  ? 8   VAL A CA  1 
ATOM   86   C C   . VAL A 1 11  ? -21.587 24.071  32.974  1.00 53.35  ? 8   VAL A C   1 
ATOM   87   O O   . VAL A 1 11  ? -22.602 23.631  33.519  1.00 54.98  ? 8   VAL A O   1 
ATOM   88   C CB  . VAL A 1 11  ? -21.780 22.701  30.863  1.00 49.92  ? 8   VAL A CB  1 
ATOM   89   C CG1 . VAL A 1 11  ? -22.524 23.842  30.190  1.00 49.07  ? 8   VAL A CG1 1 
ATOM   90   C CG2 . VAL A 1 11  ? -20.986 21.895  29.859  1.00 45.00  ? 8   VAL A CG2 1 
ATOM   91   N N   . ARG A 1 12  ? -21.081 25.272  33.256  1.00 55.44  ? 9   ARG A N   1 
ATOM   92   C CA  . ARG A 1 12  ? -21.784 26.191  34.148  1.00 57.28  ? 9   ARG A CA  1 
ATOM   93   C C   . ARG A 1 12  ? -23.022 26.772  33.469  1.00 63.87  ? 9   ARG A C   1 
ATOM   94   O O   . ARG A 1 12  ? -24.106 26.814  34.067  1.00 61.45  ? 9   ARG A O   1 
ATOM   95   C CB  . ARG A 1 12  ? -20.839 27.319  34.592  1.00 56.85  ? 9   ARG A CB  1 
ATOM   96   C CG  . ARG A 1 12  ? -20.739 27.527  36.099  1.00 62.77  ? 9   ARG A CG  1 
ATOM   97   C CD  . ARG A 1 12  ? -19.878 28.757  36.447  1.00 67.36  ? 9   ARG A CD  1 
ATOM   98   N NE  . ARG A 1 12  ? -18.572 28.736  35.792  1.00 70.00  ? 9   ARG A NE  1 
ATOM   99   C CZ  . ARG A 1 12  ? -17.690 29.730  35.817  1.00 70.46  ? 9   ARG A CZ  1 
ATOM   100  N NH1 . ARG A 1 12  ? -17.940 30.864  36.451  1.00 78.99  ? 9   ARG A NH1 1 
ATOM   101  N NH2 . ARG A 1 12  ? -16.526 29.583  35.188  1.00 63.77  ? 9   ARG A NH2 1 
ATOM   102  N N   . GLU A 1 13  ? -22.885 27.210  32.212  1.00 57.50  ? 10  GLU A N   1 
ATOM   103  C CA  . GLU A 1 13  ? -23.860 28.111  31.614  1.00 59.40  ? 10  GLU A CA  1 
ATOM   104  C C   . GLU A 1 13  ? -23.881 27.939  30.093  1.00 60.36  ? 10  GLU A C   1 
ATOM   105  O O   . GLU A 1 13  ? -22.865 27.599  29.476  1.00 61.05  ? 10  GLU A O   1 
ATOM   106  C CB  . GLU A 1 13  ? -23.519 29.555  32.006  1.00 54.15  ? 10  GLU A CB  1 
ATOM   107  C CG  . GLU A 1 13  ? -24.651 30.561  31.945  1.00 53.99  ? 10  GLU A CG  1 
ATOM   108  C CD  . GLU A 1 13  ? -24.131 31.982  31.691  1.00 63.16  ? 10  GLU A CD  1 
ATOM   109  O OE1 . GLU A 1 13  ? -22.939 32.263  31.985  1.00 60.68  ? 10  GLU A OE1 1 
ATOM   110  O OE2 . GLU A 1 13  ? -24.910 32.812  31.171  1.00 64.01  ? 10  GLU A OE2 1 
ATOM   111  N N   . HIS A 1 14  ? -25.041 28.204  29.491  1.00 54.43  ? 11  HIS A N   1 
ATOM   112  C CA  . HIS A 1 14  ? -25.238 28.104  28.050  1.00 46.01  ? 11  HIS A CA  1 
ATOM   113  C C   . HIS A 1 14  ? -25.252 29.486  27.415  1.00 52.85  ? 11  HIS A C   1 
ATOM   114  O O   . HIS A 1 14  ? -26.133 30.296  27.713  1.00 54.12  ? 11  HIS A O   1 
ATOM   115  C CB  . HIS A 1 14  ? -26.535 27.375  27.740  1.00 45.42  ? 11  HIS A CB  1 
ATOM   116  C CG  . HIS A 1 14  ? -26.431 25.900  27.920  1.00 51.61  ? 11  HIS A CG  1 
ATOM   117  N ND1 . HIS A 1 14  ? -27.532 25.078  28.025  1.00 54.48  ? 11  HIS A ND1 1 
ATOM   118  C CD2 . HIS A 1 14  ? -25.347 25.095  27.998  1.00 48.25  ? 11  HIS A CD2 1 
ATOM   119  C CE1 . HIS A 1 14  ? -27.129 23.827  28.165  1.00 50.81  ? 11  HIS A CE1 1 
ATOM   120  N NE2 . HIS A 1 14  ? -25.808 23.812  28.158  1.00 50.52  ? 11  HIS A NE2 1 
ATOM   121  N N   . VAL A 1 15  ? -24.284 29.737  26.529  1.00 54.96  ? 12  VAL A N   1 
ATOM   122  C CA  . VAL A 1 15  ? -24.174 30.969  25.753  1.00 55.39  ? 12  VAL A CA  1 
ATOM   123  C C   . VAL A 1 15  ? -23.890 30.599  24.301  1.00 59.90  ? 12  VAL A C   1 
ATOM   124  O O   . VAL A 1 15  ? -22.859 29.981  23.998  1.00 61.35  ? 12  VAL A O   1 
ATOM   125  C CB  . VAL A 1 15  ? -23.066 31.896  26.279  1.00 63.03  ? 12  VAL A CB  1 
ATOM   126  C CG1 . VAL A 1 15  ? -23.152 33.262  25.584  1.00 56.26  ? 12  VAL A CG1 1 
ATOM   127  C CG2 . VAL A 1 15  ? -23.123 32.013  27.805  1.00 52.76  ? 12  VAL A CG2 1 
ATOM   128  N N   . GLU A 1 16  ? -24.775 31.010  23.401  1.00 59.92  ? 13  GLU A N   1 
ATOM   129  C CA  . GLU A 1 16  ? -24.594 30.713  21.994  1.00 52.94  ? 13  GLU A CA  1 
ATOM   130  C C   . GLU A 1 16  ? -23.491 31.585  21.394  1.00 57.73  ? 13  GLU A C   1 
ATOM   131  O O   . GLU A 1 16  ? -22.853 32.414  22.069  1.00 53.03  ? 13  GLU A O   1 
ATOM   132  C CB  . GLU A 1 16  ? -25.902 30.908  21.247  1.00 51.28  ? 13  GLU A CB  1 
ATOM   133  C CG  . GLU A 1 16  ? -27.045 30.175  21.886  1.00 52.00  ? 13  GLU A CG  1 
ATOM   134  C CD  . GLU A 1 16  ? -27.897 29.511  20.858  1.00 62.02  ? 13  GLU A CD  1 
ATOM   135  O OE1 . GLU A 1 16  ? -27.368 29.258  19.750  1.00 67.71  ? 13  GLU A OE1 1 
ATOM   136  O OE2 . GLU A 1 16  ? -29.088 29.254  21.143  1.00 66.92  ? 13  GLU A OE2 1 
ATOM   137  N N   . GLY A 1 17  ? -23.266 31.371  20.095  1.00 54.00  ? 14  GLY A N   1 
ATOM   138  C CA  . GLY A 1 17  ? -22.247 32.101  19.377  1.00 47.71  ? 14  GLY A CA  1 
ATOM   139  C C   . GLY A 1 17  ? -20.854 31.652  19.773  1.00 47.37  ? 14  GLY A C   1 
ATOM   140  O O   . GLY A 1 17  ? -20.623 30.495  20.136  1.00 54.47  ? 14  GLY A O   1 
ATOM   141  N N   . VAL A 1 18  ? -19.916 32.586  19.694  1.00 40.81  ? 15  VAL A N   1 
ATOM   142  C CA  . VAL A 1 18  ? -18.551 32.318  20.140  1.00 55.21  ? 15  VAL A CA  1 
ATOM   143  C C   . VAL A 1 18  ? -18.574 32.136  21.654  1.00 56.73  ? 15  VAL A C   1 
ATOM   144  O O   . VAL A 1 18  ? -18.892 33.087  22.387  1.00 61.24  ? 15  VAL A O   1 
ATOM   145  C CB  . VAL A 1 18  ? -17.585 33.448  19.745  1.00 51.82  ? 15  VAL A CB  1 
ATOM   146  C CG1 . VAL A 1 18  ? -16.199 33.184  20.319  1.00 56.86  ? 15  VAL A CG1 1 
ATOM   147  C CG2 . VAL A 1 18  ? -17.507 33.577  18.252  1.00 42.72  ? 15  VAL A CG2 1 
ATOM   148  N N   . PRO A 1 19  ? -18.252 30.953  22.167  1.00 59.01  ? 16  PRO A N   1 
ATOM   149  C CA  . PRO A 1 19  ? -18.311 30.746  23.609  1.00 59.28  ? 16  PRO A CA  1 
ATOM   150  C C   . PRO A 1 19  ? -17.100 31.363  24.290  1.00 60.90  ? 16  PRO A C   1 
ATOM   151  O O   . PRO A 1 19  ? -16.012 31.511  23.731  1.00 53.18  ? 16  PRO A O   1 
ATOM   152  C CB  . PRO A 1 19  ? -18.317 29.221  23.757  1.00 57.70  ? 16  PRO A CB  1 
ATOM   153  C CG  . PRO A 1 19  ? -17.902 28.682  22.396  1.00 61.08  ? 16  PRO A CG  1 
ATOM   154  C CD  . PRO A 1 19  ? -17.536 29.848  21.511  1.00 59.05  ? 16  PRO A CD  1 
ATOM   155  N N   . ASP A 1 20  ? -17.335 31.733  25.535  1.00 62.96  ? 17  ASP A N   1 
ATOM   156  C CA  . ASP A 1 20  ? -16.385 32.434  26.378  1.00 65.85  ? 17  ASP A CA  1 
ATOM   157  C C   . ASP A 1 20  ? -15.914 31.477  27.472  1.00 62.75  ? 17  ASP A C   1 
ATOM   158  O O   . ASP A 1 20  ? -16.455 31.466  28.567  1.00 65.35  ? 17  ASP A O   1 
ATOM   159  C CB  . ASP A 1 20  ? -17.078 33.712  26.943  1.00 63.72  ? 17  ASP A CB  1 
ATOM   160  C CG  . ASP A 1 20  ? -16.136 34.610  27.755  1.00 69.02  ? 17  ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 20  ? -14.941 34.718  27.427  1.00 75.72  ? 17  ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 20  ? -16.628 35.233  28.732  1.00 64.21  ? 17  ASP A OD2 1 
ATOM   163  N N   . ALA A 1 21  ? -14.938 30.617  27.128  1.00 56.41  ? 18  ALA A N   1 
ATOM   164  C CA  . ALA A 1 21  ? -14.512 29.489  27.964  1.00 59.79  ? 18  ALA A CA  1 
ATOM   165  C C   . ALA A 1 21  ? -14.422 29.828  29.449  1.00 62.88  ? 18  ALA A C   1 
ATOM   166  O O   . ALA A 1 21  ? -14.804 29.020  30.307  1.00 55.78  ? 18  ALA A O   1 
ATOM   167  C CB  . ALA A 1 21  ? -13.173 28.951  27.509  1.00 51.04  ? 18  ALA A CB  1 
ATOM   168  N N   . ALA A 1 22  ? -13.924 31.028  29.759  1.00 60.67  ? 19  ALA A N   1 
ATOM   169  C CA  . ALA A 1 22  ? -13.830 31.458  31.150  1.00 62.18  ? 19  ALA A CA  1 
ATOM   170  C C   . ALA A 1 22  ? -15.189 31.508  31.835  1.00 61.42  ? 19  ALA A C   1 
ATOM   171  O O   . ALA A 1 22  ? -15.249 31.500  33.071  1.00 62.80  ? 19  ALA A O   1 
ATOM   172  C CB  . ALA A 1 22  ? -13.160 32.833  31.227  1.00 60.75  ? 19  ALA A CB  1 
ATOM   173  N N   . ARG A 1 23  ? -16.274 31.530  31.064  1.00 59.15  ? 20  ARG A N   1 
ATOM   174  C CA  . ARG A 1 23  ? -17.616 31.730  31.589  1.00 62.81  ? 20  ARG A CA  1 
ATOM   175  C C   . ARG A 1 23  ? -18.493 30.483  31.568  1.00 63.12  ? 20  ARG A C   1 
ATOM   176  O O   . ARG A 1 23  ? -19.356 30.335  32.446  1.00 58.61  ? 20  ARG A O   1 
ATOM   177  C CB  . ARG A 1 23  ? -18.301 32.847  30.797  1.00 58.41  ? 20  ARG A CB  1 
ATOM   178  C CG  . ARG A 1 23  ? -19.756 33.030  31.076  1.00 57.74  ? 20  ARG A CG  1 
ATOM   179  C CD  . ARG A 1 23  ? -20.250 34.227  30.321  1.00 54.99  ? 20  ARG A CD  1 
ATOM   180  N NE  . ARG A 1 23  ? -21.698 34.285  30.380  1.00 57.79  ? 20  ARG A NE  1 
ATOM   181  C CZ  . ARG A 1 23  ? -22.424 35.231  29.808  1.00 61.60  ? 20  ARG A CZ  1 
ATOM   182  N NH1 . ARG A 1 23  ? -21.857 36.217  29.130  1.00 58.40  ? 20  ARG A NH1 1 
ATOM   183  N NH2 . ARG A 1 23  ? -23.749 35.185  29.920  1.00 59.82  ? 20  ARG A NH2 1 
ATOM   184  N N   . ILE A 1 24  ? -18.274 29.580  30.609  1.00 61.68  ? 21  ILE A N   1 
ATOM   185  C CA  . ILE A 1 24  ? -19.109 28.388  30.463  1.00 61.62  ? 21  ILE A CA  1 
ATOM   186  C C   . ILE A 1 24  ? -18.648 27.229  31.350  1.00 51.56  ? 21  ILE A C   1 
ATOM   187  O O   . ILE A 1 24  ? -19.462 26.388  31.745  1.00 51.56  ? 21  ILE A O   1 
ATOM   188  C CB  . ILE A 1 24  ? -19.145 27.956  28.982  1.00 60.23  ? 21  ILE A CB  1 
ATOM   189  C CG1 . ILE A 1 24  ? -19.773 29.038  28.116  1.00 62.45  ? 21  ILE A CG1 1 
ATOM   190  C CG2 . ILE A 1 24  ? -19.991 26.708  28.788  1.00 55.58  ? 21  ILE A CG2 1 
ATOM   191  C CD1 . ILE A 1 24  ? -18.765 29.919  27.456  1.00 58.67  ? 21  ILE A CD1 1 
ATOM   192  N N   . TYR A 1 25  ? -17.369 27.179  31.693  1.00 53.72  ? 22  TYR A N   1 
ATOM   193  C CA  . TYR A 1 25  ? -16.761 25.997  32.283  1.00 55.01  ? 22  TYR A CA  1 
ATOM   194  C C   . TYR A 1 25  ? -16.234 26.307  33.679  1.00 56.69  ? 22  TYR A C   1 
ATOM   195  O O   . TYR A 1 25  ? -15.560 27.324  33.892  1.00 52.29  ? 22  TYR A O   1 
ATOM   196  C CB  . TYR A 1 25  ? -15.644 25.462  31.367  1.00 49.05  ? 22  TYR A CB  1 
ATOM   197  C CG  . TYR A 1 25  ? -16.162 25.055  30.011  1.00 47.01  ? 22  TYR A CG  1 
ATOM   198  C CD1 . TYR A 1 25  ? -17.168 24.102  29.901  1.00 51.79  ? 22  TYR A CD1 1 
ATOM   199  C CD2 . TYR A 1 25  ? -15.674 25.629  28.844  1.00 47.17  ? 22  TYR A CD2 1 
ATOM   200  C CE1 . TYR A 1 25  ? -17.680 23.716  28.668  1.00 47.20  ? 22  TYR A CE1 1 
ATOM   201  C CE2 . TYR A 1 25  ? -16.187 25.244  27.597  1.00 48.46  ? 22  TYR A CE2 1 
ATOM   202  C CZ  . TYR A 1 25  ? -17.192 24.284  27.524  1.00 46.78  ? 22  TYR A CZ  1 
ATOM   203  O OH  . TYR A 1 25  ? -17.722 23.881  26.315  1.00 52.04  ? 22  TYR A OH  1 
ATOM   204  N N   . GLU A 1 26  ? -16.546 25.426  34.627  1.00 57.03  ? 23  GLU A N   1 
ATOM   205  C CA  . GLU A 1 26  ? -16.075 25.546  36.000  1.00 61.37  ? 23  GLU A CA  1 
ATOM   206  C C   . GLU A 1 26  ? -15.377 24.253  36.413  1.00 59.01  ? 23  GLU A C   1 
ATOM   207  O O   . GLU A 1 26  ? -15.898 23.159  36.169  1.00 57.75  ? 23  GLU A O   1 
ATOM   208  C CB  . GLU A 1 26  ? -17.245 25.864  36.933  1.00 62.49  ? 23  GLU A CB  1 
ATOM   209  C CG  . GLU A 1 26  ? -17.040 25.430  38.356  1.00 65.96  ? 23  GLU A CG  1 
ATOM   210  C CD  . GLU A 1 26  ? -18.310 25.525  39.168  1.00 71.01  ? 23  GLU A CD  1 
ATOM   211  O OE1 . GLU A 1 26  ? -19.395 25.139  38.651  1.00 61.68  ? 23  GLU A OE1 1 
ATOM   212  O OE2 . GLU A 1 26  ? -18.210 25.996  40.325  1.00 78.55  ? 23  GLU A OE2 1 
ATOM   213  N N   . LYS A 1 27  ? -14.202 24.384  37.034  1.00 52.22  ? 24  LYS A N   1 
ATOM   214  C CA  . LYS A 1 27  ? -13.382 23.243  37.427  1.00 45.51  ? 24  LYS A CA  1 
ATOM   215  C C   . LYS A 1 27  ? -13.764 22.779  38.828  1.00 55.24  ? 24  LYS A C   1 
ATOM   216  O O   . LYS A 1 27  ? -13.580 23.514  39.804  1.00 55.39  ? 24  LYS A O   1 
ATOM   217  C CB  . LYS A 1 27  ? -11.905 23.615  37.380  1.00 38.87  ? 24  LYS A CB  1 
ATOM   218  C CG  . LYS A 1 27  ? -10.975 22.463  37.670  1.00 45.47  ? 24  LYS A CG  1 
ATOM   219  C CD  . LYS A 1 27  ? -9.536  22.926  37.556  1.00 51.24  ? 24  LYS A CD  1 
ATOM   220  C CE  . LYS A 1 27  ? -8.654  22.307  38.615  1.00 52.22  ? 24  LYS A CE  1 
ATOM   221  N NZ  . LYS A 1 27  ? -7.217  22.284  38.196  1.00 55.64  ? 24  LYS A NZ  1 
ATOM   222  N N   . VAL A 1 28  ? -14.262 21.551  38.931  1.00 56.23  ? 25  VAL A N   1 
ATOM   223  C CA  . VAL A 1 28  ? -14.722 21.005  40.202  1.00 54.84  ? 25  VAL A CA  1 
ATOM   224  C C   . VAL A 1 28  ? -13.910 19.765  40.551  1.00 54.99  ? 25  VAL A C   1 
ATOM   225  O O   . VAL A 1 28  ? -13.413 19.056  39.669  1.00 52.28  ? 25  VAL A O   1 
ATOM   226  C CB  . VAL A 1 28  ? -16.232 20.671  40.165  1.00 49.14  ? 25  VAL A CB  1 
ATOM   227  C CG1 . VAL A 1 28  ? -17.002 21.813  39.531  1.00 51.81  ? 25  VAL A CG1 1 
ATOM   228  C CG2 . VAL A 1 28  ? -16.487 19.365  39.421  1.00 46.99  ? 25  VAL A CG2 1 
ATOM   229  N N   . GLU A 1 29  ? -13.767 19.519  41.858  1.00 58.81  ? 26  GLU A N   1 
ATOM   230  C CA  . GLU A 1 29  ? -13.263 18.249  42.370  1.00 56.36  ? 26  GLU A CA  1 
ATOM   231  C C   . GLU A 1 29  ? -14.425 17.275  42.524  1.00 52.92  ? 26  GLU A C   1 
ATOM   232  O O   . GLU A 1 29  ? -15.550 17.673  42.836  1.00 53.15  ? 26  GLU A O   1 
ATOM   233  C CB  . GLU A 1 29  ? -12.546 18.423  43.715  1.00 56.91  ? 26  GLU A CB  1 
ATOM   234  C CG  . GLU A 1 29  ? -11.505 19.548  43.734  1.00 72.52  ? 26  GLU A CG  1 
ATOM   235  C CD  . GLU A 1 29  ? -10.321 19.277  44.672  1.00 84.10  ? 26  GLU A CD  1 
ATOM   236  O OE1 . GLU A 1 29  ? -9.913  18.097  44.806  1.00 82.22  ? 26  GLU A OE1 1 
ATOM   237  O OE2 . GLU A 1 29  ? -9.797  20.255  45.266  1.00 84.19  ? 26  GLU A OE2 1 
ATOM   238  N N   . THR A 1 30  ? -14.148 15.991  42.294  1.00 49.70  ? 27  THR A N   1 
ATOM   239  C CA  . THR A 1 30  ? -15.206 14.989  42.272  1.00 52.43  ? 27  THR A CA  1 
ATOM   240  C C   . THR A 1 30  ? -14.690 13.651  42.802  1.00 58.79  ? 27  THR A C   1 
ATOM   241  O O   . THR A 1 30  ? -13.608 13.193  42.417  1.00 54.46  ? 27  THR A O   1 
ATOM   242  C CB  . THR A 1 30  ? -15.774 14.849  40.848  1.00 52.09  ? 27  THR A CB  1 
ATOM   243  O OG1 . THR A 1 30  ? -16.719 15.903  40.608  1.00 56.08  ? 27  THR A OG1 1 
ATOM   244  C CG2 . THR A 1 30  ? -16.484 13.527  40.672  1.00 52.83  ? 27  THR A CG2 1 
ATOM   245  N N   . GLU A 1 31  ? -15.457 13.037  43.706  1.00 56.54  ? 28  GLU A N   1 
ATOM   246  C CA  . GLU A 1 31  ? -15.141 11.700  44.187  1.00 54.96  ? 28  GLU A CA  1 
ATOM   247  C C   . GLU A 1 31  ? -15.662 10.674  43.193  1.00 56.58  ? 28  GLU A C   1 
ATOM   248  O O   . GLU A 1 31  ? -16.846 10.690  42.834  1.00 53.99  ? 28  GLU A O   1 
ATOM   249  C CB  . GLU A 1 31  ? -15.757 11.461  45.569  1.00 55.34  ? 28  GLU A CB  1 
ATOM   250  C CG  . GLU A 1 31  ? -14.832 10.744  46.581  1.00 62.56  ? 28  GLU A CG  1 
ATOM   251  C CD  . GLU A 1 31  ? -13.594 11.579  46.984  1.00 71.43  ? 28  GLU A CD  1 
ATOM   252  O OE1 . GLU A 1 31  ? -13.522 12.793  46.653  1.00 73.73  ? 28  GLU A OE1 1 
ATOM   253  O OE2 . GLU A 1 31  ? -12.685 11.016  47.635  1.00 71.77  ? 28  GLU A OE2 1 
ATOM   254  N N   . LEU A 1 32  ? -14.783 9.787   42.743  1.00 50.85  ? 29  LEU A N   1 
ATOM   255  C CA  . LEU A 1 32  ? -15.127 8.803   41.723  1.00 54.20  ? 29  LEU A CA  1 
ATOM   256  C C   . LEU A 1 32  ? -15.090 7.421   42.344  1.00 45.51  ? 29  LEU A C   1 
ATOM   257  O O   . LEU A 1 32  ? -14.080 7.031   42.934  1.00 49.64  ? 29  LEU A O   1 
ATOM   258  C CB  . LEU A 1 32  ? -14.165 8.877   40.526  1.00 51.32  ? 29  LEU A CB  1 
ATOM   259  C CG  . LEU A 1 32  ? -14.322 7.815   39.432  1.00 45.52  ? 29  LEU A CG  1 
ATOM   260  C CD1 . LEU A 1 32  ? -15.704 7.886   38.834  1.00 45.15  ? 29  LEU A CD1 1 
ATOM   261  C CD2 . LEU A 1 32  ? -13.270 7.940   38.342  1.00 41.51  ? 29  LEU A CD2 1 
ATOM   262  N N   . ASN A 1 33  ? -16.181 6.692   42.226  1.00 39.88  ? 30  ASN A N   1 
ATOM   263  C CA  . ASN A 1 33  ? -16.194 5.364   42.805  1.00 50.06  ? 30  ASN A CA  1 
ATOM   264  C C   . ASN A 1 33  ? -15.318 4.436   41.973  1.00 53.02  ? 30  ASN A C   1 
ATOM   265  O O   . ASN A 1 33  ? -15.540 4.266   40.770  1.00 50.96  ? 30  ASN A O   1 
ATOM   266  C CB  . ASN A 1 33  ? -17.612 4.824   42.896  1.00 49.65  ? 30  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 33  ? -17.627 3.374   43.302  1.00 58.26  ? 30  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 33  ? -17.922 2.498   42.487  1.00 60.79  ? 30  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 33  ? -17.246 3.103   44.554  1.00 63.09  ? 30  ASN A ND2 1 
ATOM   270  N N   . THR A 1 34  ? -14.333 3.819   42.611  1.00 50.60  ? 31  THR A N   1 
ATOM   271  C CA  . THR A 1 34  ? -13.407 2.970   41.889  1.00 50.89  ? 31  THR A CA  1 
ATOM   272  C C   . THR A 1 34  ? -13.828 1.496   41.881  1.00 49.26  ? 31  THR A C   1 
ATOM   273  O O   . THR A 1 34  ? -12.995 0.618   41.602  1.00 50.49  ? 31  THR A O   1 
ATOM   274  C CB  . THR A 1 34  ? -12.001 3.151   42.460  1.00 47.63  ? 31  THR A CB  1 
ATOM   275  O OG1 . THR A 1 34  ? -12.051 3.075   43.882  1.00 49.39  ? 31  THR A OG1 1 
ATOM   276  C CG2 . THR A 1 34  ? -11.487 4.533   42.074  1.00 49.28  ? 31  THR A CG2 1 
ATOM   277  N N   . ARG A 1 35  ? -15.102 1.216   42.153  1.00 48.49  ? 32  ARG A N   1 
ATOM   278  C CA  . ARG A 1 35  ? -15.633 -0.142  42.165  1.00 50.96  ? 32  ARG A CA  1 
ATOM   279  C C   . ARG A 1 35  ? -16.198 -0.461  40.791  1.00 47.38  ? 32  ARG A C   1 
ATOM   280  O O   . ARG A 1 35  ? -17.123 0.211   40.320  1.00 47.12  ? 32  ARG A O   1 
ATOM   281  C CB  . ARG A 1 35  ? -16.761 -0.306  43.185  1.00 64.94  ? 32  ARG A CB  1 
ATOM   282  C CG  . ARG A 1 35  ? -16.509 -0.067  44.640  1.00 70.44  ? 32  ARG A CG  1 
ATOM   283  C CD  . ARG A 1 35  ? -17.861 -0.144  45.333  1.00 78.89  ? 32  ARG A CD  1 
ATOM   284  N NE  . ARG A 1 35  ? -18.346 -1.523  45.453  1.00 96.98  ? 32  ARG A NE  1 
ATOM   285  C CZ  . ARG A 1 35  ? -19.104 -2.177  44.567  1.00 93.88  ? 32  ARG A CZ  1 
ATOM   286  N NH1 . ARG A 1 35  ? -19.467 -1.628  43.403  1.00 84.55  ? 32  ARG A NH1 1 
ATOM   287  N NH2 . ARG A 1 35  ? -19.515 -3.413  44.858  1.00 88.98  ? 32  ARG A NH2 1 
ATOM   288  N N   . LEU A 1 36  ? -15.668 -1.487  40.157  1.00 46.42  ? 33  LEU A N   1 
ATOM   289  C CA  . LEU A 1 36  ? -15.950 -1.743  38.756  1.00 45.05  ? 33  LEU A CA  1 
ATOM   290  C C   . LEU A 1 36  ? -16.956 -2.881  38.589  1.00 45.37  ? 33  LEU A C   1 
ATOM   291  O O   . LEU A 1 36  ? -16.806 -3.946  39.198  1.00 48.65  ? 33  LEU A O   1 
ATOM   292  C CB  . LEU A 1 36  ? -14.646 -2.063  38.014  1.00 40.21  ? 33  LEU A CB  1 
ATOM   293  C CG  . LEU A 1 36  ? -13.541 -1.005  38.089  1.00 40.47  ? 33  LEU A CG  1 
ATOM   294  C CD1 . LEU A 1 36  ? -12.267 -1.492  37.421  1.00 38.98  ? 33  LEU A CD1 1 
ATOM   295  C CD2 . LEU A 1 36  ? -14.013 0.277   37.439  1.00 43.75  ? 33  LEU A CD2 1 
ATOM   296  N N   . GLY A 1 37  ? -17.943 -2.670  37.721  1.00 37.62  ? 34  GLY A N   1 
ATOM   297  C CA  . GLY A 1 37  ? -18.737 -3.764  37.217  1.00 34.41  ? 34  GLY A CA  1 
ATOM   298  C C   . GLY A 1 37  ? -17.917 -4.679  36.328  1.00 43.42  ? 34  GLY A C   1 
ATOM   299  O O   . GLY A 1 37  ? -16.789 -4.375  35.955  1.00 43.34  ? 34  GLY A O   1 
ATOM   300  N N   . GLU A 1 38  ? -18.517 -5.817  35.952  1.00 48.63  ? 35  GLU A N   1 
ATOM   301  C CA  . GLU A 1 38  ? -17.743 -6.932  35.396  1.00 51.94  ? 35  GLU A CA  1 
ATOM   302  C C   . GLU A 1 38  ? -16.977 -6.548  34.130  1.00 55.12  ? 35  GLU A C   1 
ATOM   303  O O   . GLU A 1 38  ? -15.945 -7.159  33.815  1.00 52.52  ? 35  GLU A O   1 
ATOM   304  C CB  . GLU A 1 38  ? -18.659 -8.132  35.100  1.00 56.89  ? 35  GLU A CB  1 
ATOM   305  C CG  . GLU A 1 38  ? -19.270 -8.826  36.322  1.00 58.49  ? 35  GLU A CG  1 
ATOM   306  C CD  . GLU A 1 38  ? -20.437 -8.059  36.934  1.00 61.29  ? 35  GLU A CD  1 
ATOM   307  O OE1 . GLU A 1 38  ? -20.926 -7.090  36.287  1.00 53.58  ? 35  GLU A OE1 1 
ATOM   308  O OE2 . GLU A 1 38  ? -20.852 -8.429  38.064  1.00 61.28  ? 35  GLU A OE2 1 
ATOM   309  N N   . GLU A 1 39  ? -17.464 -5.571  33.373  1.00 49.22  ? 36  GLU A N   1 
ATOM   310  C CA  . GLU A 1 39  ? -16.726 -5.168  32.186  1.00 46.52  ? 36  GLU A CA  1 
ATOM   311  C C   . GLU A 1 39  ? -16.550 -3.652  32.112  1.00 46.59  ? 36  GLU A C   1 
ATOM   312  O O   . GLU A 1 39  ? -16.388 -3.096  31.021  1.00 48.77  ? 36  GLU A O   1 
ATOM   313  C CB  . GLU A 1 39  ? -17.387 -5.719  30.921  1.00 53.44  ? 36  GLU A CB  1 
ATOM   314  C CG  . GLU A 1 39  ? -18.906 -5.568  30.834  1.00 57.92  ? 36  GLU A CG  1 
ATOM   315  C CD  . GLU A 1 39  ? -19.511 -6.328  29.655  1.00 56.63  ? 36  GLU A CD  1 
ATOM   316  O OE1 . GLU A 1 39  ? -20.758 -6.368  29.560  1.00 54.55  ? 36  GLU A OE1 1 
ATOM   317  O OE2 . GLU A 1 39  ? -18.740 -6.881  28.829  1.00 56.99  ? 36  GLU A OE2 1 
ATOM   318  N N   . GLN A 1 40  ? -16.555 -2.978  33.261  1.00 43.85  ? 37  GLN A N   1 
ATOM   319  C CA  . GLN A 1 40  ? -16.176 -1.576  33.356  1.00 38.96  ? 37  GLN A CA  1 
ATOM   320  C C   . GLN A 1 40  ? -14.666 -1.439  33.549  1.00 48.20  ? 37  GLN A C   1 
ATOM   321  O O   . GLN A 1 40  ? -13.971 -2.387  33.941  1.00 44.03  ? 37  GLN A O   1 
ATOM   322  C CB  . GLN A 1 40  ? -16.892 -0.885  34.508  1.00 40.31  ? 37  GLN A CB  1 
ATOM   323  C CG  . GLN A 1 40  ? -18.353 -0.615  34.285  1.00 44.96  ? 37  GLN A CG  1 
ATOM   324  C CD  . GLN A 1 40  ? -19.000 0.076   35.482  1.00 46.93  ? 37  GLN A CD  1 
ATOM   325  O OE1 . GLN A 1 40  ? -18.465 0.056   36.600  1.00 44.09  ? 37  GLN A OE1 1 
ATOM   326  N NE2 . GLN A 1 40  ? -20.153 0.700   35.250  1.00 46.31  ? 37  GLN A NE2 1 
ATOM   327  N N   . MET A 1 41  ? -14.163 -0.223  33.281  1.00 44.51  ? 38  MET A N   1 
ATOM   328  C CA  . MET A 1 41  ? -12.755 0.108   33.449  1.00 37.03  ? 38  MET A CA  1 
ATOM   329  C C   . MET A 1 41  ? -12.607 1.450   34.138  1.00 35.17  ? 38  MET A C   1 
ATOM   330  O O   . MET A 1 41  ? -13.428 2.348   33.941  1.00 32.89  ? 38  MET A O   1 
ATOM   331  C CB  . MET A 1 41  ? -12.039 0.164   32.110  1.00 39.85  ? 38  MET A CB  1 
ATOM   332  C CG  . MET A 1 41  ? -12.242 -1.065  31.259  1.00 38.49  ? 38  MET A CG  1 
ATOM   333  S SD  . MET A 1 41  ? -11.684 -0.804  29.581  1.00 41.50  ? 38  MET A SD  1 
ATOM   334  C CE  . MET A 1 41  ? -13.017 0.251   29.025  1.00 39.18  ? 38  MET A CE  1 
ATOM   335  N N   . LEU A 1 42  ? -11.543 1.574   34.940  1.00 29.95  ? 39  LEU A N   1 
ATOM   336  C CA  . LEU A 1 42  ? -11.096 2.848   35.487  1.00 28.02  ? 39  LEU A CA  1 
ATOM   337  C C   . LEU A 1 42  ? -9.988  3.449   34.616  1.00 36.67  ? 39  LEU A C   1 
ATOM   338  O O   . LEU A 1 42  ? -8.961  2.807   34.377  1.00 40.19  ? 39  LEU A O   1 
ATOM   339  C CB  . LEU A 1 42  ? -10.580 2.672   36.907  1.00 32.09  ? 39  LEU A CB  1 
ATOM   340  C CG  . LEU A 1 42  ? -10.051 3.999   37.446  1.00 38.56  ? 39  LEU A CG  1 
ATOM   341  C CD1 . LEU A 1 42  ? -11.193 5.035   37.635  1.00 28.75  ? 39  LEU A CD1 1 
ATOM   342  C CD2 . LEU A 1 42  ? -9.235  3.790   38.708  1.00 34.81  ? 39  LEU A CD2 1 
ATOM   343  N N   . LEU A 1 43  ? -10.170 4.696   34.179  1.00 32.19  ? 40  LEU A N   1 
ATOM   344  C CA  . LEU A 1 43  ? -9.307  5.281   33.162  1.00 34.05  ? 40  LEU A CA  1 
ATOM   345  C C   . LEU A 1 43  ? -8.691  6.596   33.635  1.00 37.90  ? 40  LEU A C   1 
ATOM   346  O O   . LEU A 1 43  ? -9.329  7.381   34.348  1.00 35.94  ? 40  LEU A O   1 
ATOM   347  C CB  . LEU A 1 43  ? -10.094 5.517   31.856  1.00 33.66  ? 40  LEU A CB  1 
ATOM   348  C CG  . LEU A 1 43  ? -10.764 4.272   31.293  1.00 37.26  ? 40  LEU A CG  1 
ATOM   349  C CD1 . LEU A 1 43  ? -12.191 4.589   30.871  1.00 39.13  ? 40  LEU A CD1 1 
ATOM   350  C CD2 . LEU A 1 43  ? -9.936  3.686   30.140  1.00 33.45  ? 40  LEU A CD2 1 
ATOM   351  N N   . LYS A 1 44  ? -7.444  6.830   33.206  1.00 33.07  ? 41  LYS A N   1 
ATOM   352  C CA  . LYS A 1 44  ? -6.726  8.076   33.439  1.00 35.01  ? 41  LYS A CA  1 
ATOM   353  C C   . LYS A 1 44  ? -6.558  8.803   32.108  1.00 34.26  ? 41  LYS A C   1 
ATOM   354  O O   . LYS A 1 44  ? -6.117  8.202   31.126  1.00 36.68  ? 41  LYS A O   1 
ATOM   355  C CB  . LYS A 1 44  ? -5.362  7.794   34.063  1.00 34.71  ? 41  LYS A CB  1 
ATOM   356  C CG  . LYS A 1 44  ? -4.542  9.033   34.452  1.00 43.52  ? 41  LYS A CG  1 
ATOM   357  C CD  . LYS A 1 44  ? -3.126  8.633   34.959  1.00 44.40  ? 41  LYS A CD  1 
ATOM   358  C CE  . LYS A 1 44  ? -2.381  9.805   35.608  1.00 46.17  ? 41  LYS A CE  1 
ATOM   359  N NZ  . LYS A 1 44  ? -2.177  10.930  34.637  1.00 51.64  ? 41  LYS A NZ  1 
ATOM   360  N N   . THR A 1 45  ? -6.903  10.090  32.077  1.00 32.62  ? 42  THR A N   1 
ATOM   361  C CA  . THR A 1 45  ? -6.833  10.887  30.855  1.00 28.55  ? 42  THR A CA  1 
ATOM   362  C C   . THR A 1 45  ? -5.407  11.372  30.601  1.00 32.63  ? 42  THR A C   1 
ATOM   363  O O   . THR A 1 45  ? -4.832  12.083  31.432  1.00 34.17  ? 42  THR A O   1 
ATOM   364  C CB  . THR A 1 45  ? -7.758  12.090  30.964  1.00 29.51  ? 42  THR A CB  1 
ATOM   365  O OG1 . THR A 1 45  ? -9.113  11.660  31.134  1.00 26.66  ? 42  THR A OG1 1 
ATOM   366  C CG2 . THR A 1 45  ? -7.636  12.938  29.727  1.00 30.16  ? 42  THR A CG2 1 
ATOM   367  N N   . LEU A 1 46  ? -4.847  11.022  29.443  1.00 32.90  ? 43  LEU A N   1 
ATOM   368  C CA  . LEU A 1 46  ? -3.502  11.456  29.070  1.00 32.16  ? 43  LEU A CA  1 
ATOM   369  C C   . LEU A 1 46  ? -3.493  12.671  28.144  1.00 36.69  ? 43  LEU A C   1 
ATOM   370  O O   . LEU A 1 46  ? -2.639  13.548  28.305  1.00 39.98  ? 43  LEU A O   1 
ATOM   371  C CB  . LEU A 1 46  ? -2.728  10.302  28.419  1.00 33.35  ? 43  LEU A CB  1 
ATOM   372  C CG  . LEU A 1 46  ? -2.596  9.062   29.315  1.00 30.94  ? 43  LEU A CG  1 
ATOM   373  C CD1 . LEU A 1 46  ? -1.735  8.049   28.672  1.00 28.84  ? 43  LEU A CD1 1 
ATOM   374  C CD2 . LEU A 1 46  ? -2.020  9.423   30.668  1.00 34.26  ? 43  LEU A CD2 1 
ATOM   375  N N   . TYR A 1 47  ? -4.411  12.756  27.176  1.00 33.78  ? 44  TYR A N   1 
ATOM   376  C CA  . TYR A 1 47  ? -4.561  13.955  26.355  1.00 32.73  ? 44  TYR A CA  1 
ATOM   377  C C   . TYR A 1 47  ? -6.037  14.173  26.073  1.00 32.41  ? 44  TYR A C   1 
ATOM   378  O O   . TYR A 1 47  ? -6.803  13.216  25.961  1.00 32.58  ? 44  TYR A O   1 
ATOM   379  C CB  . TYR A 1 47  ? -3.838  13.870  24.998  1.00 29.93  ? 44  TYR A CB  1 
ATOM   380  C CG  . TYR A 1 47  ? -2.383  13.475  25.032  1.00 31.65  ? 44  TYR A CG  1 
ATOM   381  C CD1 . TYR A 1 47  ? -2.008  12.143  25.140  1.00 29.19  ? 44  TYR A CD1 1 
ATOM   382  C CD2 . TYR A 1 47  ? -1.378  14.431  24.909  1.00 33.55  ? 44  TYR A CD2 1 
ATOM   383  C CE1 . TYR A 1 47  ? -0.671  11.771  25.173  1.00 25.68  ? 44  TYR A CE1 1 
ATOM   384  C CE2 . TYR A 1 47  ? -0.044  14.062  24.925  1.00 32.24  ? 44  TYR A CE2 1 
ATOM   385  C CZ  . TYR A 1 47  ? 0.300   12.729  25.065  1.00 31.14  ? 44  TYR A CZ  1 
ATOM   386  O OH  . TYR A 1 47  ? 1.627   12.353  25.095  1.00 37.46  ? 44  TYR A OH  1 
ATOM   387  N N   . VAL A 1 48  ? -6.433  15.434  25.943  1.00 33.38  ? 45  VAL A N   1 
ATOM   388  C CA  . VAL A 1 48  ? -7.762  15.752  25.431  1.00 36.95  ? 45  VAL A CA  1 
ATOM   389  C C   . VAL A 1 48  ? -7.616  16.685  24.234  1.00 36.69  ? 45  VAL A C   1 
ATOM   390  O O   . VAL A 1 48  ? -6.661  17.466  24.122  1.00 38.83  ? 45  VAL A O   1 
ATOM   391  C CB  . VAL A 1 48  ? -8.723  16.382  26.473  1.00 30.90  ? 45  VAL A CB  1 
ATOM   392  C CG1 . VAL A 1 48  ? -8.676  15.638  27.768  1.00 36.06  ? 45  VAL A CG1 1 
ATOM   393  C CG2 . VAL A 1 48  ? -8.386  17.834  26.702  1.00 37.44  ? 45  VAL A CG2 1 
ATOM   394  N N   . SER A 1 49  ? -8.594  16.588  23.338  1.00 34.32  ? 46  SER A N   1 
ATOM   395  C CA  . SER A 1 49  ? -8.735  17.432  22.165  1.00 37.32  ? 46  SER A CA  1 
ATOM   396  C C   . SER A 1 49  ? -9.654  18.612  22.471  1.00 33.44  ? 46  SER A C   1 
ATOM   397  O O   . SER A 1 49  ? -10.601 18.492  23.245  1.00 33.44  ? 46  SER A O   1 
ATOM   398  C CB  . SER A 1 49  ? -9.310  16.599  21.016  1.00 35.92  ? 46  SER A CB  1 
ATOM   399  O OG  . SER A 1 49  ? -9.595  17.382  19.874  1.00 38.10  ? 46  SER A OG  1 
ATOM   400  N N   . VAL A 1 50  ? -9.366  19.759  21.864  1.00 34.22  ? 47  VAL A N   1 
ATOM   401  C CA  . VAL A 1 50  ? -10.301 20.881  21.828  1.00 39.72  ? 47  VAL A CA  1 
ATOM   402  C C   . VAL A 1 50  ? -10.655 21.160  20.374  1.00 40.79  ? 47  VAL A C   1 
ATOM   403  O O   . VAL A 1 50  ? -9.769  21.337  19.531  1.00 34.25  ? 47  VAL A O   1 
ATOM   404  C CB  . VAL A 1 50  ? -9.741  22.141  22.517  1.00 35.22  ? 47  VAL A CB  1 
ATOM   405  C CG1 . VAL A 1 50  ? -9.875  21.987  24.008  1.00 41.84  ? 47  VAL A CG1 1 
ATOM   406  C CG2 . VAL A 1 50  ? -8.285  22.360  22.138  1.00 38.36  ? 47  VAL A CG2 1 
ATOM   407  N N   . ASP A 1 51  ? -11.951 21.198  20.089  1.00 37.21  ? 48  ASP A N   1 
ATOM   408  C CA  . ASP A 1 51  ? -12.451 21.304  18.758  1.00 38.62  ? 48  ASP A CA  1 
ATOM   409  C C   . ASP A 1 51  ? -13.640 22.244  18.686  1.00 46.40  ? 48  ASP A C   1 
ATOM   410  O O   . ASP A 1 51  ? -14.469 22.260  19.604  1.00 48.74  ? 48  ASP A O   1 
ATOM   411  C CB  . ASP A 1 51  ? -12.881 19.933  18.252  1.00 43.13  ? 48  ASP A CB  1 
ATOM   412  C CG  . ASP A 1 51  ? -11.817 18.905  18.429  1.00 44.69  ? 48  ASP A CG  1 
ATOM   413  O OD1 . ASP A 1 51  ? -11.599 18.493  19.595  1.00 43.34  ? 48  ASP A OD1 1 
ATOM   414  O OD2 . ASP A 1 51  ? -11.195 18.525  17.409  1.00 46.45  ? 48  ASP A OD2 1 
ATOM   415  N N   . PRO A 1 52  ? -13.766 23.002  17.590  1.00 55.73  ? 49  PRO A N   1 
ATOM   416  C CA  . PRO A 1 52  ? -14.959 23.852  17.406  1.00 47.64  ? 49  PRO A CA  1 
ATOM   417  C C   . PRO A 1 52  ? -16.289 23.129  17.541  1.00 45.98  ? 49  PRO A C   1 
ATOM   418  O O   . PRO A 1 52  ? -17.218 23.714  18.108  1.00 45.86  ? 49  PRO A O   1 
ATOM   419  C CB  . PRO A 1 52  ? -14.747 24.408  15.998  1.00 48.21  ? 49  PRO A CB  1 
ATOM   420  C CG  . PRO A 1 52  ? -13.246 24.573  15.934  1.00 50.94  ? 49  PRO A CG  1 
ATOM   421  C CD  . PRO A 1 52  ? -12.693 23.351  16.634  1.00 47.72  ? 49  PRO A CD  1 
ATOM   422  N N   . TYR A 1 53  ? -16.415 21.881  17.066  1.00 45.05  ? 50  TYR A N   1 
ATOM   423  C CA  . TYR A 1 53  ? -17.677 21.157  17.223  1.00 40.64  ? 50  TYR A CA  1 
ATOM   424  C C   . TYR A 1 53  ? -18.097 21.003  18.681  1.00 45.18  ? 50  TYR A C   1 
ATOM   425  O O   . TYR A 1 53  ? -19.238 20.602  18.946  1.00 44.33  ? 50  TYR A O   1 
ATOM   426  C CB  . TYR A 1 53  ? -17.610 19.767  16.571  1.00 42.55  ? 50  TYR A CB  1 
ATOM   427  C CG  . TYR A 1 53  ? -16.540 18.783  17.088  1.00 45.16  ? 50  TYR A CG  1 
ATOM   428  C CD1 . TYR A 1 53  ? -16.658 18.148  18.335  1.00 42.10  ? 50  TYR A CD1 1 
ATOM   429  C CD2 . TYR A 1 53  ? -15.447 18.447  16.295  1.00 38.29  ? 50  TYR A CD2 1 
ATOM   430  C CE1 . TYR A 1 53  ? -15.688 17.248  18.783  1.00 41.15  ? 50  TYR A CE1 1 
ATOM   431  C CE2 . TYR A 1 53  ? -14.490 17.546  16.726  1.00 37.78  ? 50  TYR A CE2 1 
ATOM   432  C CZ  . TYR A 1 53  ? -14.605 16.951  17.964  1.00 39.21  ? 50  TYR A CZ  1 
ATOM   433  O OH  . TYR A 1 53  ? -13.625 16.060  18.360  1.00 37.43  ? 50  TYR A OH  1 
ATOM   434  N N   . LEU A 1 54  ? -17.198 21.277  19.629  1.00 44.88  ? 51  LEU A N   1 
ATOM   435  C CA  . LEU A 1 54  ? -17.571 21.245  21.032  1.00 44.12  ? 51  LEU A CA  1 
ATOM   436  C C   . LEU A 1 54  ? -18.527 22.372  21.404  1.00 45.75  ? 51  LEU A C   1 
ATOM   437  O O   . LEU A 1 54  ? -19.287 22.222  22.363  1.00 44.42  ? 51  LEU A O   1 
ATOM   438  C CB  . LEU A 1 54  ? -16.313 21.302  21.883  1.00 42.39  ? 51  LEU A CB  1 
ATOM   439  C CG  . LEU A 1 54  ? -15.430 20.071  21.710  1.00 40.48  ? 51  LEU A CG  1 
ATOM   440  C CD1 . LEU A 1 54  ? -14.176 20.256  22.536  1.00 40.56  ? 51  LEU A CD1 1 
ATOM   441  C CD2 . LEU A 1 54  ? -16.148 18.768  22.091  1.00 34.55  ? 51  LEU A CD2 1 
ATOM   442  N N   . GLN A 1 55  ? -18.519 23.482  20.654  1.00 44.12  ? 52  GLN A N   1 
ATOM   443  C CA  . GLN A 1 55  ? -19.454 24.573  20.911  1.00 47.33  ? 52  GLN A CA  1 
ATOM   444  C C   . GLN A 1 55  ? -20.896 24.087  20.903  1.00 46.28  ? 52  GLN A C   1 
ATOM   445  O O   . GLN A 1 55  ? -21.702 24.506  21.740  1.00 52.26  ? 52  GLN A O   1 
ATOM   446  C CB  . GLN A 1 55  ? -19.260 25.681  19.878  1.00 48.12  ? 52  GLN A CB  1 
ATOM   447  C CG  . GLN A 1 55  ? -20.078 26.941  20.138  1.00 44.66  ? 52  GLN A CG  1 
ATOM   448  C CD  . GLN A 1 55  ? -21.383 26.986  19.368  1.00 44.29  ? 52  GLN A CD  1 
ATOM   449  O OE1 . GLN A 1 55  ? -21.925 25.956  18.954  1.00 42.07  ? 52  GLN A OE1 1 
ATOM   450  N NE2 . GLN A 1 55  ? -21.900 28.196  19.174  1.00 48.57  ? 52  GLN A NE2 1 
ATOM   451  N N   . GLY A 1 56  ? -21.242 23.217  19.968  1.00 41.02  ? 53  GLY A N   1 
ATOM   452  C CA  . GLY A 1 56  ? -22.600 22.734  19.883  1.00 40.80  ? 53  GLY A CA  1 
ATOM   453  C C   . GLY A 1 56  ? -22.824 21.476  20.688  1.00 45.94  ? 53  GLY A C   1 
ATOM   454  O O   . GLY A 1 56  ? -23.974 21.077  20.903  1.00 53.10  ? 53  GLY A O   1 
ATOM   455  N N   . ILE A 1 57  ? -21.739 20.816  21.106  1.00 44.75  ? 54  ILE A N   1 
ATOM   456  C CA  . ILE A 1 57  ? -21.857 19.738  22.089  1.00 46.81  ? 54  ILE A CA  1 
ATOM   457  C C   . ILE A 1 57  ? -22.247 20.319  23.438  1.00 51.84  ? 54  ILE A C   1 
ATOM   458  O O   . ILE A 1 57  ? -23.159 19.831  24.116  1.00 53.92  ? 54  ILE A O   1 
ATOM   459  C CB  . ILE A 1 57  ? -20.536 18.964  22.213  1.00 45.05  ? 54  ILE A CB  1 
ATOM   460  C CG1 . ILE A 1 57  ? -20.216 18.200  20.938  1.00 49.57  ? 54  ILE A CG1 1 
ATOM   461  C CG2 . ILE A 1 57  ? -20.611 18.012  23.387  1.00 40.11  ? 54  ILE A CG2 1 
ATOM   462  C CD1 . ILE A 1 57  ? -20.868 16.859  20.888  1.00 47.08  ? 54  ILE A CD1 1 
ATOM   463  N N   . CYS A 1 58  ? -21.537 21.376  23.832  1.00 46.36  ? 55  CYS A N   1 
ATOM   464  C CA  . CYS A 1 58  ? -21.744 22.070  25.093  1.00 45.17  ? 55  CYS A CA  1 
ATOM   465  C C   . CYS A 1 58  ? -23.163 22.607  25.215  1.00 44.27  ? 55  CYS A C   1 
ATOM   466  O O   . CYS A 1 58  ? -23.820 22.418  26.240  1.00 46.90  ? 55  CYS A O   1 
ATOM   467  C CB  . CYS A 1 58  ? -20.720 23.193  25.172  1.00 48.84  ? 55  CYS A CB  1 
ATOM   468  S SG  . CYS A 1 58  ? -20.664 24.088  26.654  1.00 45.35  ? 55  CYS A SG  1 
ATOM   469  N N   . LEU A 1 59  ? -23.661 23.275  24.171  1.00 49.33  ? 56  LEU A N   1 
ATOM   470  C CA  . LEU A 1 59  ? -25.037 23.773  24.179  1.00 51.30  ? 56  LEU A CA  1 
ATOM   471  C C   . LEU A 1 59  ? -26.077 22.656  24.235  1.00 48.30  ? 56  LEU A C   1 
ATOM   472  O O   . LEU A 1 59  ? -27.267 22.958  24.344  1.00 51.81  ? 56  LEU A O   1 
ATOM   473  C CB  . LEU A 1 59  ? -25.309 24.652  22.952  1.00 42.87  ? 56  LEU A CB  1 
ATOM   474  C CG  . LEU A 1 59  ? -24.541 25.975  22.873  1.00 49.03  ? 56  LEU A CG  1 
ATOM   475  C CD1 . LEU A 1 59  ? -24.699 26.612  21.509  1.00 43.30  ? 56  LEU A CD1 1 
ATOM   476  C CD2 . LEU A 1 59  ? -24.995 26.937  23.962  1.00 49.27  ? 56  LEU A CD2 1 
ATOM   477  N N   . ASP A 1 60  ? -25.664 21.391  24.161  1.00 46.16  ? 57  ASP A N   1 
ATOM   478  C CA  . ASP A 1 60  ? -26.546 20.250  24.340  1.00 46.82  ? 57  ASP A CA  1 
ATOM   479  C C   . ASP A 1 60  ? -26.216 19.468  25.600  1.00 49.98  ? 57  ASP A C   1 
ATOM   480  O O   . ASP A 1 60  ? -26.820 18.415  25.842  1.00 47.78  ? 57  ASP A O   1 
ATOM   481  C CB  . ASP A 1 60  ? -26.477 19.306  23.132  1.00 57.26  ? 57  ASP A CB  1 
ATOM   482  C CG  . ASP A 1 60  ? -27.215 19.849  21.907  1.00 64.66  ? 57  ASP A CG  1 
ATOM   483  O OD1 . ASP A 1 60  ? -27.609 21.042  21.906  1.00 60.59  ? 57  ASP A OD1 1 
ATOM   484  O OD2 . ASP A 1 60  ? -27.401 19.063  20.945  1.00 68.15  ? 57  ASP A OD2 1 
ATOM   485  N N   . THR A 1 61  ? -25.264 19.945  26.398  1.00 49.62  ? 58  THR A N   1 
ATOM   486  C CA  . THR A 1 61  ? -24.867 19.260  27.627  1.00 53.53  ? 58  THR A CA  1 
ATOM   487  C C   . THR A 1 61  ? -25.666 19.821  28.798  1.00 54.48  ? 58  THR A C   1 
ATOM   488  O O   . THR A 1 61  ? -25.659 21.043  29.005  1.00 54.71  ? 58  THR A O   1 
ATOM   489  C CB  . THR A 1 61  ? -23.374 19.436  27.881  1.00 53.03  ? 58  THR A CB  1 
ATOM   490  O OG1 . THR A 1 61  ? -22.629 18.716  26.885  1.00 51.67  ? 58  THR A OG1 1 
ATOM   491  C CG2 . THR A 1 61  ? -23.002 18.932  29.276  1.00 43.82  ? 58  THR A CG2 1 
ATOM   492  N N   . PRO A 1 62  ? -26.392 18.993  29.553  1.00 56.46  ? 59  PRO A N   1 
ATOM   493  C CA  . PRO A 1 62  ? -27.082 19.493  30.750  1.00 52.27  ? 59  PRO A CA  1 
ATOM   494  C C   . PRO A 1 62  ? -26.159 20.303  31.648  1.00 51.74  ? 59  PRO A C   1 
ATOM   495  O O   . PRO A 1 62  ? -24.993 19.960  31.840  1.00 55.35  ? 59  PRO A O   1 
ATOM   496  C CB  . PRO A 1 62  ? -27.553 18.211  31.431  1.00 45.54  ? 59  PRO A CB  1 
ATOM   497  C CG  . PRO A 1 62  ? -27.860 17.300  30.259  1.00 54.41  ? 59  PRO A CG  1 
ATOM   498  C CD  . PRO A 1 62  ? -26.836 17.631  29.190  1.00 55.80  ? 59  PRO A CD  1 
ATOM   499  N N   . ILE A 1 63  ? -26.684 21.413  32.169  1.00 48.25  ? 60  ILE A N   1 
ATOM   500  C CA  . ILE A 1 63  ? -25.878 22.255  33.038  1.00 48.81  ? 60  ILE A CA  1 
ATOM   501  C C   . ILE A 1 63  ? -25.365 21.426  34.205  1.00 52.48  ? 60  ILE A C   1 
ATOM   502  O O   . ILE A 1 63  ? -26.092 20.612  34.795  1.00 50.00  ? 60  ILE A O   1 
ATOM   503  C CB  . ILE A 1 63  ? -26.691 23.461  33.533  1.00 52.56  ? 60  ILE A CB  1 
ATOM   504  C CG1 . ILE A 1 63  ? -27.211 24.265  32.338  1.00 51.60  ? 60  ILE A CG1 1 
ATOM   505  C CG2 . ILE A 1 63  ? -25.848 24.313  34.479  1.00 44.28  ? 60  ILE A CG2 1 
ATOM   506  C CD1 . ILE A 1 63  ? -26.232 25.320  31.813  1.00 53.87  ? 60  ILE A CD1 1 
ATOM   507  N N   . GLY A 1 64  ? -24.089 21.606  34.521  1.00 55.51  ? 61  GLY A N   1 
ATOM   508  C CA  . GLY A 1 64  ? -23.440 20.852  35.564  1.00 54.66  ? 61  GLY A CA  1 
ATOM   509  C C   . GLY A 1 64  ? -22.712 19.605  35.105  1.00 53.63  ? 61  GLY A C   1 
ATOM   510  O O   . GLY A 1 64  ? -21.851 19.105  35.839  1.00 51.94  ? 61  GLY A O   1 
ATOM   511  N N   . ASP A 1 65  ? -23.019 19.087  33.917  1.00 52.66  ? 62  ASP A N   1 
ATOM   512  C CA  . ASP A 1 65  ? -22.331 17.885  33.479  1.00 48.38  ? 62  ASP A CA  1 
ATOM   513  C C   . ASP A 1 65  ? -20.940 18.214  32.958  1.00 48.77  ? 62  ASP A C   1 
ATOM   514  O O   . ASP A 1 65  ? -20.587 19.372  32.722  1.00 45.69  ? 62  ASP A O   1 
ATOM   515  C CB  . ASP A 1 65  ? -23.133 17.149  32.424  1.00 39.91  ? 62  ASP A CB  1 
ATOM   516  C CG  . ASP A 1 65  ? -24.448 16.668  32.961  1.00 51.54  ? 62  ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 65  ? -24.835 17.142  34.058  1.00 57.82  ? 62  ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 65  ? -25.089 15.815  32.311  1.00 54.51  ? 62  ASP A OD2 1 
ATOM   519  N N   . HIS A 1 66  ? -20.127 17.173  32.827  1.00 50.32  ? 63  HIS A N   1 
ATOM   520  C CA  . HIS A 1 66  ? -18.786 17.408  32.337  1.00 44.39  ? 63  HIS A CA  1 
ATOM   521  C C   . HIS A 1 66  ? -18.849 17.695  30.842  1.00 41.49  ? 63  HIS A C   1 
ATOM   522  O O   . HIS A 1 66  ? -19.824 17.358  30.155  1.00 37.05  ? 63  HIS A O   1 
ATOM   523  C CB  . HIS A 1 66  ? -17.876 16.213  32.650  1.00 43.27  ? 63  HIS A CB  1 
ATOM   524  C CG  . HIS A 1 66  ? -18.146 15.003  31.816  1.00 41.94  ? 63  HIS A CG  1 
ATOM   525  N ND1 . HIS A 1 66  ? -19.204 14.154  32.059  1.00 45.35  ? 63  HIS A ND1 1 
ATOM   526  C CD2 . HIS A 1 66  ? -17.500 14.503  30.734  1.00 39.03  ? 63  HIS A CD2 1 
ATOM   527  C CE1 . HIS A 1 66  ? -19.199 13.186  31.157  1.00 43.58  ? 63  HIS A CE1 1 
ATOM   528  N NE2 . HIS A 1 66  ? -18.179 13.376  30.340  1.00 36.49  ? 63  HIS A NE2 1 
ATOM   529  N N   . MET A 1 67  ? -17.809 18.370  30.349  1.00 47.80  ? 64  MET A N   1 
ATOM   530  C CA  . MET A 1 67  ? -17.690 18.699  28.928  1.00 46.35  ? 64  MET A CA  1 
ATOM   531  C C   . MET A 1 67  ? -17.177 17.467  28.177  1.00 44.07  ? 64  MET A C   1 
ATOM   532  O O   . MET A 1 67  ? -16.043 17.017  28.412  1.00 39.14  ? 64  MET A O   1 
ATOM   533  C CB  . MET A 1 67  ? -16.766 19.904  28.740  1.00 42.64  ? 64  MET A CB  1 
ATOM   534  C CG  . MET A 1 67  ? -16.754 20.474  27.328  1.00 47.14  ? 64  MET A CG  1 
ATOM   535  S SD  . MET A 1 67  ? -18.422 20.824  26.725  1.00 49.61  ? 64  MET A SD  1 
ATOM   536  C CE  . MET A 1 67  ? -18.294 20.364  25.014  1.00 47.83  ? 64  MET A CE  1 
ATOM   537  N N   . GLY A 1 68  ? -18.022 16.892  27.313  1.00 36.78  ? 65  GLY A N   1 
ATOM   538  C CA  . GLY A 1 68  ? -17.557 15.822  26.453  1.00 35.88  ? 65  GLY A CA  1 
ATOM   539  C C   . GLY A 1 68  ? -16.428 16.296  25.554  1.00 39.38  ? 65  GLY A C   1 
ATOM   540  O O   . GLY A 1 68  ? -16.336 17.478  25.206  1.00 35.77  ? 65  GLY A O   1 
ATOM   541  N N   . ALA A 1 69  ? -15.538 15.367  25.203  1.00 36.21  ? 66  ALA A N   1 
ATOM   542  C CA  . ALA A 1 69  ? -14.435 15.650  24.289  1.00 34.23  ? 66  ALA A CA  1 
ATOM   543  C C   . ALA A 1 69  ? -13.712 14.356  23.950  1.00 35.08  ? 66  ALA A C   1 
ATOM   544  O O   . ALA A 1 69  ? -13.798 13.364  24.678  1.00 34.84  ? 66  ALA A O   1 
ATOM   545  C CB  . ALA A 1 69  ? -13.446 16.648  24.873  1.00 31.60  ? 66  ALA A CB  1 
ATOM   546  N N   . ASP A 1 70  ? -12.994 14.384  22.833  1.00 33.28  ? 67  ASP A N   1 
ATOM   547  C CA  . ASP A 1 70  ? -12.174 13.256  22.419  1.00 34.78  ? 67  ASP A CA  1 
ATOM   548  C C   . ASP A 1 70  ? -10.898 13.193  23.271  1.00 32.90  ? 67  ASP A C   1 
ATOM   549  O O   . ASP A 1 70  ? -10.290 14.220  23.577  1.00 33.88  ? 67  ASP A O   1 
ATOM   550  C CB  . ASP A 1 70  ? -11.851 13.401  20.930  1.00 31.35  ? 67  ASP A CB  1 
ATOM   551  C CG  . ASP A 1 70  ? -11.482 12.080  20.261  1.00 34.34  ? 67  ASP A CG  1 
ATOM   552  O OD1 . ASP A 1 70  ? -11.736 11.006  20.835  1.00 31.95  ? 67  ASP A OD1 1 
ATOM   553  O OD2 . ASP A 1 70  ? -10.922 12.123  19.133  1.00 40.84  ? 67  ASP A OD2 1 
ATOM   554  N N   . SER A 1 71  ? -10.484 11.993  23.663  1.00 27.04  ? 68  SER A N   1 
ATOM   555  C CA  . SER A 1 71  ? -9.372  11.921  24.603  1.00 30.32  ? 68  SER A CA  1 
ATOM   556  C C   . SER A 1 71  ? -8.571  10.638  24.423  1.00 30.90  ? 68  SER A C   1 
ATOM   557  O O   . SER A 1 71  ? -9.003  9.685   23.768  1.00 32.09  ? 68  SER A O   1 
ATOM   558  C CB  . SER A 1 71  ? -9.860  11.988  26.038  1.00 32.60  ? 68  SER A CB  1 
ATOM   559  O OG  . SER A 1 71  ? -10.545 10.785  26.338  1.00 34.65  ? 68  SER A OG  1 
ATOM   560  N N   . ILE A 1 72  ? -7.395  10.621  25.041  1.00 26.47  ? 69  ILE A N   1 
ATOM   561  C CA  . ILE A 1 72  ? -6.555  9.436   25.107  1.00 29.15  ? 69  ILE A CA  1 
ATOM   562  C C   . ILE A 1 72  ? -6.456  9.051   26.572  1.00 31.33  ? 69  ILE A C   1 
ATOM   563  O O   . ILE A 1 72  ? -6.141  9.893   27.423  1.00 32.82  ? 69  ILE A O   1 
ATOM   564  C CB  . ILE A 1 72  ? -5.169  9.672   24.466  1.00 33.28  ? 69  ILE A CB  1 
ATOM   565  C CG1 . ILE A 1 72  ? -5.335  9.977   22.970  1.00 27.92  ? 69  ILE A CG1 1 
ATOM   566  C CG2 . ILE A 1 72  ? -4.237  8.460   24.640  1.00 25.77  ? 69  ILE A CG2 1 
ATOM   567  C CD1 . ILE A 1 72  ? -4.068  10.390  22.305  1.00 29.26  ? 69  ILE A CD1 1 
ATOM   568  N N   . MET A 1 73  ? -6.782  7.797   26.868  1.00 27.36  ? 70  MET A N   1 
ATOM   569  C CA  . MET A 1 73  ? -6.900  7.327   28.234  1.00 28.03  ? 70  MET A CA  1 
ATOM   570  C C   . MET A 1 73  ? -6.085  6.062   28.403  1.00 33.28  ? 70  MET A C   1 
ATOM   571  O O   . MET A 1 73  ? -5.881  5.303   27.443  1.00 28.42  ? 70  MET A O   1 
ATOM   572  C CB  . MET A 1 73  ? -8.341  7.041   28.610  1.00 24.89  ? 70  MET A CB  1 
ATOM   573  C CG  . MET A 1 73  ? -9.255  8.220   28.424  1.00 30.62  ? 70  MET A CG  1 
ATOM   574  S SD  . MET A 1 73  ? -11.002 7.766   28.360  1.00 34.50  ? 70  MET A SD  1 
ATOM   575  C CE  . MET A 1 73  ? -11.265 7.247   26.669  1.00 34.10  ? 70  MET A CE  1 
ATOM   576  N N   . GLN A 1 74  ? -5.624  5.850   29.643  1.00 29.27  ? 71  GLN A N   1 
ATOM   577  C CA  . GLN A 1 74  ? -4.946  4.631   30.053  1.00 32.03  ? 71  GLN A CA  1 
ATOM   578  C C   . GLN A 1 74  ? -5.749  3.906   31.128  1.00 35.67  ? 71  GLN A C   1 
ATOM   579  O O   . GLN A 1 74  ? -6.227  4.525   32.087  1.00 30.44  ? 71  GLN A O   1 
ATOM   580  C CB  . GLN A 1 74  ? -3.558  4.933   30.585  1.00 34.67  ? 71  GLN A CB  1 
ATOM   581  C CG  . GLN A 1 74  ? -2.738  3.685   30.851  1.00 35.03  ? 71  GLN A CG  1 
ATOM   582  C CD  . GLN A 1 74  ? -1.255  3.977   30.797  1.00 38.79  ? 71  GLN A CD  1 
ATOM   583  O OE1 . GLN A 1 74  ? -0.774  4.932   31.429  1.00 29.87  ? 71  GLN A OE1 1 
ATOM   584  N NE2 . GLN A 1 74  ? -0.522  3.180   30.019  1.00 37.61  ? 71  GLN A NE2 1 
ATOM   585  N N   . VAL A 1 75  ? -5.880  2.591   30.964  1.00 38.29  ? 72  VAL A N   1 
ATOM   586  C CA  . VAL A 1 75  ? -6.643  1.760   31.895  1.00 37.25  ? 72  VAL A CA  1 
ATOM   587  C C   . VAL A 1 75  ? -5.818  1.531   33.156  1.00 38.34  ? 72  VAL A C   1 
ATOM   588  O O   . VAL A 1 75  ? -4.714  0.967   33.107  1.00 31.97  ? 72  VAL A O   1 
ATOM   589  C CB  . VAL A 1 75  ? -7.052  0.426   31.256  1.00 37.44  ? 72  VAL A CB  1 
ATOM   590  C CG1 . VAL A 1 75  ? -7.827  -0.399  32.237  1.00 33.41  ? 72  VAL A CG1 1 
ATOM   591  C CG2 . VAL A 1 75  ? -7.882  0.666   30.004  1.00 34.61  ? 72  VAL A CG2 1 
ATOM   592  N N   . LEU A 1 76  ? -6.356  1.994   34.288  1.00 36.30  ? 73  LEU A N   1 
ATOM   593  C CA  . LEU A 1 76  ? -5.778  1.805   35.609  1.00 35.59  ? 73  LEU A CA  1 
ATOM   594  C C   . LEU A 1 76  ? -6.261  0.496   36.228  1.00 40.57  ? 73  LEU A C   1 
ATOM   595  O O   . LEU A 1 76  ? -5.452  -0.277  36.748  1.00 45.93  ? 73  LEU A O   1 
ATOM   596  C CB  . LEU A 1 76  ? -6.119  2.998   36.510  1.00 34.39  ? 73  LEU A CB  1 
ATOM   597  C CG  . LEU A 1 76  ? -5.670  4.380   36.018  1.00 34.40  ? 73  LEU A CG  1 
ATOM   598  C CD1 . LEU A 1 76  ? -6.260  5.498   36.868  1.00 30.40  ? 73  LEU A CD1 1 
ATOM   599  C CD2 . LEU A 1 76  ? -4.156  4.505   35.949  1.00 29.50  ? 73  LEU A CD2 1 
ATOM   600  N N   . ASP A 1 77  ? -7.562  0.215   36.140  1.00 39.70  ? 74  ASP A N   1 
ATOM   601  C CA  . ASP A 1 77  ? -8.142  -1.014  36.668  1.00 43.56  ? 74  ASP A CA  1 
ATOM   602  C C   . ASP A 1 77  ? -9.289  -1.469  35.760  1.00 41.30  ? 74  ASP A C   1 
ATOM   603  O O   . ASP A 1 77  ? -9.915  -0.661  35.067  1.00 41.46  ? 74  ASP A O   1 
ATOM   604  C CB  . ASP A 1 77  ? -8.622  -0.795  38.113  1.00 39.50  ? 74  ASP A CB  1 
ATOM   605  C CG  . ASP A 1 77  ? -8.918  -2.087  38.839  1.00 47.73  ? 74  ASP A CG  1 
ATOM   606  O OD1 . ASP A 1 77  ? -8.411  -3.146  38.394  1.00 44.53  ? 74  ASP A OD1 1 
ATOM   607  O OD2 . ASP A 1 77  ? -9.661  -2.041  39.856  1.00 56.77  ? 74  ASP A OD2 1 
ATOM   608  N N   . ALA A 1 78  ? -9.585  -2.770  35.789  1.00 43.00  ? 75  ALA A N   1 
ATOM   609  C CA  . ALA A 1 78  ? -10.573 -3.335  34.869  1.00 45.49  ? 75  ALA A CA  1 
ATOM   610  C C   . ALA A 1 78  ? -11.217 -4.605  35.422  1.00 46.81  ? 75  ALA A C   1 
ATOM   611  O O   . ALA A 1 78  ? -10.517 -5.522  35.857  1.00 44.12  ? 75  ALA A O   1 
ATOM   612  C CB  . ALA A 1 78  ? -9.924  -3.639  33.518  1.00 37.17  ? 75  ALA A CB  1 
ATOM   613  N N   . GLY A 1 79  ? -12.544 -4.665  35.358  1.00 42.81  ? 76  GLY A N   1 
ATOM   614  C CA  . GLY A 1 79  ? -13.285 -5.853  35.699  1.00 40.84  ? 76  GLY A CA  1 
ATOM   615  C C   . GLY A 1 79  ? -12.963 -7.045  34.817  1.00 45.97  ? 76  GLY A C   1 
ATOM   616  O O   . GLY A 1 79  ? -12.278 -6.944  33.797  1.00 43.32  ? 76  GLY A O   1 
ATOM   617  N N   . PRO A 1 80  ? -13.471 -8.212  35.203  1.00 50.98  ? 77  PRO A N   1 
ATOM   618  C CA  . PRO A 1 80  ? -12.988 -9.460  34.587  1.00 48.58  ? 77  PRO A CA  1 
ATOM   619  C C   . PRO A 1 80  ? -13.353 -9.630  33.124  1.00 50.93  ? 77  PRO A C   1 
ATOM   620  O O   . PRO A 1 80  ? -12.715 -10.447 32.442  1.00 50.31  ? 77  PRO A O   1 
ATOM   621  C CB  . PRO A 1 80  ? -13.625 -10.554 35.456  1.00 45.48  ? 77  PRO A CB  1 
ATOM   622  C CG  . PRO A 1 80  ? -14.690 -9.869  36.251  1.00 50.32  ? 77  PRO A CG  1 
ATOM   623  C CD  . PRO A 1 80  ? -14.292 -8.448  36.401  1.00 48.38  ? 77  PRO A CD  1 
ATOM   624  N N   . ASN A 1 81  ? -14.348 -8.903  32.611  1.00 49.48  ? 78  ASN A N   1 
ATOM   625  C CA  . ASN A 1 81  ? -14.710 -9.000  31.198  1.00 46.90  ? 78  ASN A CA  1 
ATOM   626  C C   . ASN A 1 81  ? -14.547 -7.666  30.476  1.00 51.01  ? 78  ASN A C   1 
ATOM   627  O O   . ASN A 1 81  ? -15.183 -7.441  29.441  1.00 43.34  ? 78  ASN A O   1 
ATOM   628  C CB  . ASN A 1 81  ? -16.137 -9.524  31.043  1.00 48.54  ? 78  ASN A CB  1 
ATOM   629  C CG  . ASN A 1 81  ? -16.353 -10.823 31.784  1.00 56.23  ? 78  ASN A CG  1 
ATOM   630  O OD1 . ASN A 1 81  ? -17.097 -10.866 32.770  1.00 58.40  ? 78  ASN A OD1 1 
ATOM   631  N ND2 . ASN A 1 81  ? -15.690 -11.892 31.326  1.00 52.43  ? 78  ASN A ND2 1 
ATOM   632  N N   . ALA A 1 82  ? -13.718 -6.769  31.016  1.00 55.28  ? 79  ALA A N   1 
ATOM   633  C CA  . ALA A 1 82  ? -13.476 -5.492  30.369  1.00 44.47  ? 79  ALA A CA  1 
ATOM   634  C C   . ALA A 1 82  ? -12.805 -5.725  29.019  1.00 42.67  ? 79  ALA A C   1 
ATOM   635  O O   . ALA A 1 82  ? -12.033 -6.677  28.853  1.00 39.55  ? 79  ALA A O   1 
ATOM   636  C CB  . ALA A 1 82  ? -12.592 -4.602  31.236  1.00 38.69  ? 79  ALA A CB  1 
ATOM   637  N N   . PRO A 1 83  ? -13.082 -4.871  28.035  1.00 36.70  ? 80  PRO A N   1 
ATOM   638  C CA  . PRO A 1 83  ? -12.449 -5.065  26.727  1.00 37.12  ? 80  PRO A CA  1 
ATOM   639  C C   . PRO A 1 83  ? -10.942 -4.863  26.756  1.00 37.24  ? 80  PRO A C   1 
ATOM   640  O O   . PRO A 1 83  ? -10.241 -5.462  25.932  1.00 37.36  ? 80  PRO A O   1 
ATOM   641  C CB  . PRO A 1 83  ? -13.163 -4.042  25.837  1.00 31.37  ? 80  PRO A CB  1 
ATOM   642  C CG  . PRO A 1 83  ? -13.759 -3.043  26.789  1.00 35.37  ? 80  PRO A CG  1 
ATOM   643  C CD  . PRO A 1 83  ? -14.026 -3.739  28.058  1.00 38.70  ? 80  PRO A CD  1 
ATOM   644  N N   . PHE A 1 84  ? -10.414 -4.069  27.691  1.00 34.91  ? 81  PHE A N   1 
ATOM   645  C CA  . PHE A 1 84  ? -8.986  -3.790  27.725  1.00 42.75  ? 81  PHE A CA  1 
ATOM   646  C C   . PHE A 1 84  ? -8.440  -4.026  29.126  1.00 42.80  ? 81  PHE A C   1 
ATOM   647  O O   . PHE A 1 84  ? -9.174  -3.930  30.110  1.00 45.31  ? 81  PHE A O   1 
ATOM   648  C CB  . PHE A 1 84  ? -8.717  -2.354  27.225  1.00 39.28  ? 81  PHE A CB  1 
ATOM   649  C CG  . PHE A 1 84  ? -9.357  -2.078  25.899  1.00 34.36  ? 81  PHE A CG  1 
ATOM   650  C CD1 . PHE A 1 84  ? -8.989  -2.815  24.775  1.00 35.14  ? 81  PHE A CD1 1 
ATOM   651  C CD2 . PHE A 1 84  ? -10.370 -1.147  25.778  1.00 33.08  ? 81  PHE A CD2 1 
ATOM   652  C CE1 . PHE A 1 84  ? -9.604  -2.608  23.554  1.00 31.76  ? 81  PHE A CE1 1 
ATOM   653  C CE2 . PHE A 1 84  ? -10.984 -0.930  24.547  1.00 33.81  ? 81  PHE A CE2 1 
ATOM   654  C CZ  . PHE A 1 84  ? -10.603 -1.659  23.441  1.00 30.78  ? 81  PHE A CZ  1 
ATOM   655  N N   . ARG A 1 85  ? -7.137  -4.366  29.204  1.00 41.05  ? 82  ARG A N   1 
ATOM   656  C CA  . ARG A 1 85  ? -6.457  -4.666  30.458  1.00 42.83  ? 82  ARG A CA  1 
ATOM   657  C C   . ARG A 1 85  ? -5.771  -3.419  30.997  1.00 41.85  ? 82  ARG A C   1 
ATOM   658  O O   . ARG A 1 85  ? -5.523  -2.471  30.250  1.00 42.85  ? 82  ARG A O   1 
ATOM   659  C CB  . ARG A 1 85  ? -5.433  -5.773  30.234  1.00 42.53  ? 82  ARG A CB  1 
ATOM   660  C CG  . ARG A 1 85  ? -6.021  -7.039  29.613  1.00 55.02  ? 82  ARG A CG  1 
ATOM   661  C CD  . ARG A 1 85  ? -6.588  -8.020  30.653  1.00 65.23  ? 82  ARG A CD  1 
ATOM   662  N NE  . ARG A 1 85  ? -8.012  -7.852  30.949  1.00 63.14  ? 82  ARG A NE  1 
ATOM   663  C CZ  . ARG A 1 85  ? -8.514  -7.689  32.170  1.00 58.02  ? 82  ARG A CZ  1 
ATOM   664  N NH1 . ARG A 1 85  ? -7.731  -7.593  33.237  1.00 49.32  ? 82  ARG A NH1 1 
ATOM   665  N NH2 . ARG A 1 85  ? -9.834  -7.636  32.329  1.00 55.62  ? 82  ARG A NH2 1 
ATOM   666  N N   . PRO A 1 86  ? -5.458  -3.366  32.293  1.00 42.99  ? 83  PRO A N   1 
ATOM   667  C CA  . PRO A 1 86  ? -4.711  -2.209  32.807  1.00 43.07  ? 83  PRO A CA  1 
ATOM   668  C C   . PRO A 1 86  ? -3.442  -2.012  31.993  1.00 39.97  ? 83  PRO A C   1 
ATOM   669  O O   . PRO A 1 86  ? -2.844  -2.973  31.511  1.00 36.27  ? 83  PRO A O   1 
ATOM   670  C CB  . PRO A 1 86  ? -4.405  -2.586  34.262  1.00 34.13  ? 83  PRO A CB  1 
ATOM   671  C CG  . PRO A 1 86  ? -5.464  -3.555  34.619  1.00 39.08  ? 83  PRO A CG  1 
ATOM   672  C CD  . PRO A 1 86  ? -5.818  -4.311  33.364  1.00 42.74  ? 83  PRO A CD  1 
ATOM   673  N N   . GLY A 1 87  ? -3.059  -0.744  31.811  1.00 43.40  ? 84  GLY A N   1 
ATOM   674  C CA  . GLY A 1 87  ? -1.969  -0.370  30.935  1.00 40.01  ? 84  GLY A CA  1 
ATOM   675  C C   . GLY A 1 87  ? -2.380  -0.036  29.512  1.00 38.99  ? 84  GLY A C   1 
ATOM   676  O O   . GLY A 1 87  ? -1.741  0.808   28.878  1.00 41.44  ? 84  GLY A O   1 
ATOM   677  N N   . ASP A 1 88  ? -3.437  -0.662  29.000  1.00 38.73  ? 85  ASP A N   1 
ATOM   678  C CA  . ASP A 1 88  ? -3.868  -0.391  27.634  1.00 40.57  ? 85  ASP A CA  1 
ATOM   679  C C   . ASP A 1 88  ? -4.237  1.084   27.460  1.00 41.20  ? 85  ASP A C   1 
ATOM   680  O O   . ASP A 1 88  ? -4.822  1.715   28.356  1.00 36.04  ? 85  ASP A O   1 
ATOM   681  C CB  . ASP A 1 88  ? -5.056  -1.283  27.252  1.00 34.01  ? 85  ASP A CB  1 
ATOM   682  C CG  . ASP A 1 88  ? -4.649  -2.719  26.985  1.00 38.78  ? 85  ASP A CG  1 
ATOM   683  O OD1 . ASP A 1 88  ? -3.438  -2.987  26.835  1.00 39.28  ? 85  ASP A OD1 1 
ATOM   684  O OD2 . ASP A 1 88  ? -5.545  -3.588  26.912  1.00 43.63  ? 85  ASP A OD2 1 
ATOM   685  N N   . LEU A 1 89  ? -3.856  1.633   26.304  1.00 30.75  ? 86  LEU A N   1 
ATOM   686  C CA  . LEU A 1 89  ? -4.251  2.966   25.893  1.00 28.32  ? 86  LEU A CA  1 
ATOM   687  C C   . LEU A 1 89  ? -5.446  2.893   24.942  1.00 30.03  ? 86  LEU A C   1 
ATOM   688  O O   . LEU A 1 89  ? -5.489  2.054   24.032  1.00 27.15  ? 86  LEU A O   1 
ATOM   689  C CB  . LEU A 1 89  ? -3.084  3.662   25.213  1.00 32.25  ? 86  LEU A CB  1 
ATOM   690  C CG  . LEU A 1 89  ? -1.862  3.562   26.090  1.00 34.44  ? 86  LEU A CG  1 
ATOM   691  C CD1 . LEU A 1 89  ? -0.609  3.453   25.239  1.00 31.13  ? 86  LEU A CD1 1 
ATOM   692  C CD2 . LEU A 1 89  ? -1.844  4.792   27.006  1.00 31.40  ? 86  LEU A CD2 1 
ATOM   693  N N   . VAL A 1 90  ? -6.407  3.797   25.148  1.00 29.00  ? 87  VAL A N   1 
ATOM   694  C CA  . VAL A 1 90  ? -7.623  3.865   24.348  1.00 31.16  ? 87  VAL A CA  1 
ATOM   695  C C   . VAL A 1 90  ? -7.886  5.298   23.892  1.00 28.52  ? 87  VAL A C   1 
ATOM   696  O O   . VAL A 1 90  ? -7.544  6.264   24.580  1.00 28.48  ? 87  VAL A O   1 
ATOM   697  C CB  . VAL A 1 90  ? -8.839  3.324   25.132  1.00 29.32  ? 87  VAL A CB  1 
ATOM   698  C CG1 . VAL A 1 90  ? -8.662  1.856   25.422  1.00 28.51  ? 87  VAL A CG1 1 
ATOM   699  C CG2 . VAL A 1 90  ? -9.014  4.114   26.417  1.00 26.45  ? 87  VAL A CG2 1 
ATOM   700  N N   . GLN A 1 91  ? -8.525  5.429   22.731  1.00 28.13  ? 88  GLN A N   1 
ATOM   701  C CA  . GLN A 1 91  ? -9.037  6.704   22.243  1.00 27.45  ? 88  GLN A CA  1 
ATOM   702  C C   . GLN A 1 91  ? -10.565 6.642   22.226  1.00 29.20  ? 88  GLN A C   1 
ATOM   703  O O   . GLN A 1 91  ? -11.149 5.654   21.760  1.00 29.26  ? 88  GLN A O   1 
ATOM   704  C CB  . GLN A 1 91  ? -8.466  7.017   20.849  1.00 30.35  ? 88  GLN A CB  1 
ATOM   705  C CG  . GLN A 1 91  ? -9.042  8.275   20.116  1.00 29.07  ? 88  GLN A CG  1 
ATOM   706  C CD  . GLN A 1 91  ? -10.340 7.993   19.385  1.00 28.50  ? 88  GLN A CD  1 
ATOM   707  O OE1 . GLN A 1 91  ? -10.421 7.079   18.551  1.00 26.85  ? 88  GLN A OE1 1 
ATOM   708  N NE2 . GLN A 1 91  ? -11.371 8.753   19.716  1.00 22.29  ? 88  GLN A NE2 1 
ATOM   709  N N   . GLY A 1 92  ? -11.203 7.687   22.739  1.00 26.06  ? 89  GLY A N   1 
ATOM   710  C CA  . GLY A 1 92  ? -12.655 7.738   22.799  1.00 28.08  ? 89  GLY A CA  1 
ATOM   711  C C   . GLY A 1 92  ? -13.117 9.029   23.448  1.00 30.81  ? 89  GLY A C   1 
ATOM   712  O O   . GLY A 1 92  ? -12.310 9.902   23.778  1.00 34.13  ? 89  GLY A O   1 
ATOM   713  N N   . PHE A 1 93  ? -14.429 9.148   23.650  1.00 29.25  ? 90  PHE A N   1 
ATOM   714  C CA  . PHE A 1 93  ? -15.012 10.418  24.107  1.00 32.53  ? 90  PHE A CA  1 
ATOM   715  C C   . PHE A 1 93  ? -14.992 10.512  25.636  1.00 34.40  ? 90  PHE A C   1 
ATOM   716  O O   . PHE A 1 93  ? -16.023 10.519  26.300  1.00 28.84  ? 90  PHE A O   1 
ATOM   717  C CB  . PHE A 1 93  ? -16.426 10.574  23.567  1.00 31.29  ? 90  PHE A CB  1 
ATOM   718  C CG  . PHE A 1 93  ? -16.776 11.982  23.181  1.00 33.30  ? 90  PHE A CG  1 
ATOM   719  C CD1 . PHE A 1 93  ? -16.032 12.659  22.231  1.00 35.31  ? 90  PHE A CD1 1 
ATOM   720  C CD2 . PHE A 1 93  ? -17.867 12.613  23.731  1.00 34.92  ? 90  PHE A CD2 1 
ATOM   721  C CE1 . PHE A 1 93  ? -16.356 13.949  21.856  1.00 36.47  ? 90  PHE A CE1 1 
ATOM   722  C CE2 . PHE A 1 93  ? -18.200 13.907  23.358  1.00 41.54  ? 90  PHE A CE2 1 
ATOM   723  C CZ  . PHE A 1 93  ? -17.447 14.574  22.418  1.00 41.42  ? 90  PHE A CZ  1 
ATOM   724  N N   . GLY A 1 94  ? -13.778 10.627  26.184  1.00 33.40  ? 91  GLY A N   1 
ATOM   725  C CA  . GLY A 1 94  ? -13.615 10.628  27.627  1.00 30.23  ? 91  GLY A CA  1 
ATOM   726  C C   . GLY A 1 94  ? -14.105 11.892  28.306  1.00 31.06  ? 91  GLY A C   1 
ATOM   727  O O   . GLY A 1 94  ? -14.630 11.834  29.416  1.00 39.11  ? 91  GLY A O   1 
ATOM   728  N N   . GLY A 1 95  ? -13.944 13.041  27.665  1.00 35.60  ? 92  GLY A N   1 
ATOM   729  C CA  . GLY A 1 95  ? -14.372 14.307  28.233  1.00 33.16  ? 92  GLY A CA  1 
ATOM   730  C C   . GLY A 1 95  ? -13.262 15.010  28.987  1.00 37.81  ? 92  GLY A C   1 
ATOM   731  O O   . GLY A 1 95  ? -12.135 14.519  29.121  1.00 32.25  ? 92  GLY A O   1 
ATOM   732  N N   . TRP A 1 96  ? -13.599 16.195  29.504  1.00 41.16  ? 93  TRP A N   1 
ATOM   733  C CA  . TRP A 1 96  ? -12.634 17.026  30.235  1.00 39.57  ? 93  TRP A CA  1 
ATOM   734  C C   . TRP A 1 96  ? -12.602 16.623  31.717  1.00 43.06  ? 93  TRP A C   1 
ATOM   735  O O   . TRP A 1 96  ? -13.020 17.352  32.625  1.00 49.31  ? 93  TRP A O   1 
ATOM   736  C CB  . TRP A 1 96  ? -12.962 18.504  30.048  1.00 45.83  ? 93  TRP A CB  1 
ATOM   737  C CG  . TRP A 1 96  ? -12.783 19.036  28.614  1.00 45.84  ? 93  TRP A CG  1 
ATOM   738  C CD1 . TRP A 1 96  ? -12.335 18.340  27.525  1.00 40.78  ? 93  TRP A CD1 1 
ATOM   739  C CD2 . TRP A 1 96  ? -13.063 20.370  28.144  1.00 45.85  ? 93  TRP A CD2 1 
ATOM   740  N NE1 . TRP A 1 96  ? -12.314 19.154  26.416  1.00 44.73  ? 93  TRP A NE1 1 
ATOM   741  C CE2 . TRP A 1 96  ? -12.763 20.400  26.766  1.00 48.75  ? 93  TRP A CE2 1 
ATOM   742  C CE3 . TRP A 1 96  ? -13.538 21.538  28.757  1.00 45.76  ? 93  TRP A CE3 1 
ATOM   743  C CZ2 . TRP A 1 96  ? -12.913 21.552  25.996  1.00 43.05  ? 93  TRP A CZ2 1 
ATOM   744  C CZ3 . TRP A 1 96  ? -13.689 22.677  27.992  1.00 44.21  ? 93  TRP A CZ3 1 
ATOM   745  C CH2 . TRP A 1 96  ? -13.377 22.677  26.627  1.00 45.55  ? 93  TRP A CH2 1 
ATOM   746  N N   . ARG A 1 97  ? -12.073 15.421  31.948  1.00 40.61  ? 94  ARG A N   1 
ATOM   747  C CA  . ARG A 1 97  ? -12.069 14.752  33.243  1.00 37.45  ? 94  ARG A CA  1 
ATOM   748  C C   . ARG A 1 97  ? -10.719 14.074  33.432  1.00 45.76  ? 94  ARG A C   1 
ATOM   749  O O   . ARG A 1 97  ? -10.196 13.446  32.498  1.00 41.53  ? 94  ARG A O   1 
ATOM   750  C CB  . ARG A 1 97  ? -13.191 13.699  33.348  1.00 35.64  ? 94  ARG A CB  1 
ATOM   751  C CG  . ARG A 1 97  ? -14.603 14.261  33.287  1.00 41.45  ? 94  ARG A CG  1 
ATOM   752  C CD  . ARG A 1 97  ? -15.683 13.191  33.496  1.00 39.17  ? 94  ARG A CD  1 
ATOM   753  N NE  . ARG A 1 97  ? -15.704 12.193  32.430  1.00 43.90  ? 94  ARG A NE  1 
ATOM   754  C CZ  . ARG A 1 97  ? -16.628 11.248  32.305  1.00 41.18  ? 94  ARG A CZ  1 
ATOM   755  N NH1 . ARG A 1 97  ? -17.624 11.142  33.166  1.00 49.53  ? 94  ARG A NH1 1 
ATOM   756  N NH2 . ARG A 1 97  ? -16.553 10.392  31.290  1.00 34.65  ? 94  ARG A NH2 1 
ATOM   757  N N   . THR A 1 98  ? -10.155 14.201  34.642  1.00 44.28  ? 95  THR A N   1 
ATOM   758  C CA  . THR A 1 98  ? -8.856  13.584  34.909  1.00 38.87  ? 95  THR A CA  1 
ATOM   759  C C   . THR A 1 98  ? -8.969  12.066  34.902  1.00 35.24  ? 95  THR A C   1 
ATOM   760  O O   . THR A 1 98  ? -8.095  11.365  34.375  1.00 39.73  ? 95  THR A O   1 
ATOM   761  C CB  . THR A 1 98  ? -8.297  14.091  36.245  1.00 47.85  ? 95  THR A CB  1 
ATOM   762  O OG1 . THR A 1 98  ? -9.117  13.642  37.340  1.00 44.06  ? 95  THR A OG1 1 
ATOM   763  C CG2 . THR A 1 98  ? -8.252  15.614  36.249  1.00 45.66  ? 95  THR A CG2 1 
ATOM   764  N N   . HIS A 1 99  ? -10.040 11.542  35.474  1.00 33.06  ? 96  HIS A N   1 
ATOM   765  C CA  . HIS A 1 99  ? -10.283 10.114  35.492  1.00 36.58  ? 96  HIS A CA  1 
ATOM   766  C C   . HIS A 1 99  ? -11.767 9.906   35.288  1.00 35.76  ? 96  HIS A C   1 
ATOM   767  O O   . HIS A 1 99  ? -12.563 10.845  35.415  1.00 39.37  ? 96  HIS A O   1 
ATOM   768  C CB  . HIS A 1 99  ? -9.843  9.463   36.806  1.00 38.74  ? 96  HIS A CB  1 
ATOM   769  C CG  . HIS A 1 99  ? -8.460  9.831   37.238  1.00 40.39  ? 96  HIS A CG  1 
ATOM   770  N ND1 . HIS A 1 99  ? -8.144  11.077  37.736  1.00 39.89  ? 96  HIS A ND1 1 
ATOM   771  C CD2 . HIS A 1 99  ? -7.308  9.115   37.253  1.00 42.03  ? 96  HIS A CD2 1 
ATOM   772  C CE1 . HIS A 1 99  ? -6.856  11.114  38.032  1.00 40.44  ? 96  HIS A CE1 1 
ATOM   773  N NE2 . HIS A 1 99  ? -6.326  9.936   37.753  1.00 40.09  ? 96  HIS A NE2 1 
ATOM   774  N N   . LEU A 1 100 ? -12.138 8.664   34.990  1.00 28.86  ? 97  LEU A N   1 
ATOM   775  C CA  . LEU A 1 100 ? -13.532 8.324   34.737  1.00 33.96  ? 97  LEU A CA  1 
ATOM   776  C C   . LEU A 1 100 ? -13.659 6.812   34.722  1.00 34.09  ? 97  LEU A C   1 
ATOM   777  O O   . LEU A 1 100 ? -12.669 6.092   34.558  1.00 31.37  ? 97  LEU A O   1 
ATOM   778  C CB  . LEU A 1 100 ? -14.032 8.902   33.406  1.00 34.31  ? 97  LEU A CB  1 
ATOM   779  C CG  . LEU A 1 100 ? -13.235 8.444   32.187  1.00 33.93  ? 97  LEU A CG  1 
ATOM   780  C CD1 . LEU A 1 100 ? -14.077 7.559   31.302  1.00 33.67  ? 97  LEU A CD1 1 
ATOM   781  C CD2 . LEU A 1 100 ? -12.695 9.638   31.437  1.00 33.91  ? 97  LEU A CD2 1 
ATOM   782  N N   . VAL A 1 101 ? -14.891 6.342   34.902  1.00 33.24  ? 98  VAL A N   1 
ATOM   783  C CA  . VAL A 1 101 ? -15.224 4.929   34.771  1.00 33.15  ? 98  VAL A CA  1 
ATOM   784  C C   . VAL A 1 101 ? -16.132 4.791   33.564  1.00 35.74  ? 98  VAL A C   1 
ATOM   785  O O   . VAL A 1 101 ? -17.040 5.613   33.364  1.00 36.82  ? 98  VAL A O   1 
ATOM   786  C CB  . VAL A 1 101 ? -15.904 4.358   36.040  1.00 36.96  ? 98  VAL A CB  1 
ATOM   787  C CG1 . VAL A 1 101 ? -16.352 2.891   35.853  1.00 31.73  ? 98  VAL A CG1 1 
ATOM   788  C CG2 . VAL A 1 101 ? -14.986 4.468   37.232  1.00 36.45  ? 98  VAL A CG2 1 
ATOM   789  N N   . SER A 1 102 ? -15.885 3.753   32.763  1.00 31.51  ? 99  SER A N   1 
ATOM   790  C CA  . SER A 1 102 ? -16.712 3.457   31.603  1.00 37.20  ? 99  SER A CA  1 
ATOM   791  C C   . SER A 1 102 ? -16.423 2.026   31.177  1.00 42.01  ? 99  SER A C   1 
ATOM   792  O O   . SER A 1 102 ? -15.346 1.490   31.462  1.00 44.72  ? 99  SER A O   1 
ATOM   793  C CB  . SER A 1 102 ? -16.434 4.453   30.457  1.00 41.57  ? 99  SER A CB  1 
ATOM   794  O OG  . SER A 1 102 ? -16.910 3.980   29.206  1.00 42.70  ? 99  SER A OG  1 
ATOM   795  N N   . ASP A 1 103 ? -17.389 1.397   30.508  1.00 41.66  ? 100 ASP A N   1 
ATOM   796  C CA  . ASP A 1 103 ? -17.124 0.089   29.916  1.00 40.88  ? 100 ASP A CA  1 
ATOM   797  C C   . ASP A 1 103 ? -16.644 0.205   28.482  1.00 46.07  ? 100 ASP A C   1 
ATOM   798  O O   . ASP A 1 103 ? -16.335 -0.817  27.857  1.00 38.26  ? 100 ASP A O   1 
ATOM   799  C CB  . ASP A 1 103 ? -18.362 -0.815  29.988  1.00 45.26  ? 100 ASP A CB  1 
ATOM   800  C CG  . ASP A 1 103 ? -19.634 -0.128  29.499  1.00 55.55  ? 100 ASP A CG  1 
ATOM   801  O OD1 . ASP A 1 103 ? -19.547 0.828   28.691  1.00 57.39  ? 100 ASP A OD1 1 
ATOM   802  O OD2 . ASP A 1 103 ? -20.729 -0.546  29.943  1.00 57.92  ? 100 ASP A OD2 1 
ATOM   803  N N   . GLY A 1 104 ? -16.558 1.432   27.963  1.00 42.92  ? 101 GLY A N   1 
ATOM   804  C CA  . GLY A 1 104 ? -16.084 1.665   26.620  1.00 38.68  ? 101 GLY A CA  1 
ATOM   805  C C   . GLY A 1 104 ? -17.008 1.199   25.522  1.00 41.07  ? 101 GLY A C   1 
ATOM   806  O O   . GLY A 1 104 ? -16.581 1.120   24.368  1.00 35.58  ? 101 GLY A O   1 
ATOM   807  N N   . LYS A 1 105 ? -18.251 0.873   25.841  1.00 47.64  ? 102 LYS A N   1 
ATOM   808  C CA  . LYS A 1 105 ? -19.217 0.485   24.824  1.00 49.15  ? 102 LYS A CA  1 
ATOM   809  C C   . LYS A 1 105 ? -19.802 1.730   24.132  1.00 46.09  ? 102 LYS A C   1 
ATOM   810  O O   . LYS A 1 105 ? -19.738 2.846   24.670  1.00 47.19  ? 102 LYS A O   1 
ATOM   811  C CB  . LYS A 1 105 ? -20.318 -0.367  25.466  1.00 47.69  ? 102 LYS A CB  1 
ATOM   812  C CG  . LYS A 1 105 ? -19.914 -1.804  25.818  1.00 41.39  ? 102 LYS A CG  1 
ATOM   813  C CD  . LYS A 1 105 ? -21.031 -2.483  26.596  1.00 47.12  ? 102 LYS A CD  1 
ATOM   814  C CE  . LYS A 1 105 ? -21.093 -3.980  26.345  1.00 54.61  ? 102 LYS A CE  1 
ATOM   815  N NZ  . LYS A 1 105 ? -19.992 -4.730  26.996  1.00 50.52  ? 102 LYS A NZ  1 
ATOM   816  N N   . PRO A 1 106 ? -20.351 1.576   22.923  1.00 40.76  ? 103 PRO A N   1 
ATOM   817  C CA  . PRO A 1 106 ? -20.977 2.731   22.250  1.00 43.10  ? 103 PRO A CA  1 
ATOM   818  C C   . PRO A 1 106 ? -22.131 3.277   23.075  1.00 40.80  ? 103 PRO A C   1 
ATOM   819  O O   . PRO A 1 106 ? -22.848 2.523   23.733  1.00 37.42  ? 103 PRO A O   1 
ATOM   820  C CB  . PRO A 1 106 ? -21.468 2.157   20.910  1.00 34.19  ? 103 PRO A CB  1 
ATOM   821  C CG  . PRO A 1 106 ? -20.650 0.908   20.685  1.00 32.62  ? 103 PRO A CG  1 
ATOM   822  C CD  . PRO A 1 106 ? -20.275 0.381   22.059  1.00 41.86  ? 103 PRO A CD  1 
ATOM   823  N N   . LYS A 1 107 ? -22.300 4.605   23.037  1.00 38.69  ? 104 LYS A N   1 
ATOM   824  C CA  . LYS A 1 107 ? -23.281 5.295   23.872  1.00 46.34  ? 104 LYS A CA  1 
ATOM   825  C C   . LYS A 1 107 ? -23.989 6.373   23.072  1.00 46.09  ? 104 LYS A C   1 
ATOM   826  O O   . LYS A 1 107 ? -23.335 7.197   22.428  1.00 41.17  ? 104 LYS A O   1 
ATOM   827  C CB  . LYS A 1 107 ? -22.633 5.940   25.116  1.00 48.31  ? 104 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 107 ? -22.063 4.964   26.157  1.00 48.25  ? 104 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 107 ? -21.433 5.745   27.318  1.00 55.17  ? 104 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 107 ? -20.870 4.843   28.398  1.00 58.92  ? 104 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 107 ? -20.242 5.652   29.501  1.00 63.40  ? 104 LYS A NZ  1 
ATOM   832  N N   . LEU A 1 108 ? -25.321 6.382   23.158  1.00 49.94  ? 105 LEU A N   1 
ATOM   833  C CA  . LEU A 1 108 ? -26.145 7.383   22.492  1.00 50.11  ? 105 LEU A CA  1 
ATOM   834  C C   . LEU A 1 108 ? -25.879 8.779   23.053  1.00 48.57  ? 105 LEU A C   1 
ATOM   835  O O   . LEU A 1 108 ? -25.550 8.949   24.226  1.00 51.09  ? 105 LEU A O   1 
ATOM   836  C CB  . LEU A 1 108 ? -27.629 7.036   22.650  1.00 54.60  ? 105 LEU A CB  1 
ATOM   837  C CG  . LEU A 1 108 ? -28.648 8.021   22.070  1.00 57.34  ? 105 LEU A CG  1 
ATOM   838  C CD1 . LEU A 1 108 ? -28.460 8.094   20.562  1.00 57.85  ? 105 LEU A CD1 1 
ATOM   839  C CD2 . LEU A 1 108 ? -30.078 7.644   22.426  1.00 54.45  ? 105 LEU A CD2 1 
ATOM   840  N N   . TRP A 1 109 ? -26.008 9.788   22.198  1.00 51.28  ? 106 TRP A N   1 
ATOM   841  C CA  . TRP A 1 109 ? -25.970 11.178  22.640  1.00 49.52  ? 106 TRP A CA  1 
ATOM   842  C C   . TRP A 1 109 ? -27.427 11.591  22.712  1.00 60.85  ? 106 TRP A C   1 
ATOM   843  O O   . TRP A 1 109 ? -28.018 12.060  21.734  1.00 59.54  ? 106 TRP A O   1 
ATOM   844  C CB  . TRP A 1 109 ? -25.154 12.048  21.703  1.00 53.55  ? 106 TRP A CB  1 
ATOM   845  C CG  . TRP A 1 109 ? -24.924 13.465  22.151  1.00 49.61  ? 106 TRP A CG  1 
ATOM   846  C CD1 . TRP A 1 109 ? -24.931 14.560  21.351  1.00 48.11  ? 106 TRP A CD1 1 
ATOM   847  C CD2 . TRP A 1 109 ? -24.625 13.943  23.480  1.00 53.89  ? 106 TRP A CD2 1 
ATOM   848  N NE1 . TRP A 1 109 ? -24.667 15.689  22.078  1.00 56.71  ? 106 TRP A NE1 1 
ATOM   849  C CE2 . TRP A 1 109 ? -24.476 15.345  23.390  1.00 53.12  ? 106 TRP A CE2 1 
ATOM   850  C CE3 . TRP A 1 109 ? -24.478 13.330  24.734  1.00 55.95  ? 106 TRP A CE3 1 
ATOM   851  C CZ2 . TRP A 1 109 ? -24.186 16.149  24.505  1.00 52.90  ? 106 TRP A CZ2 1 
ATOM   852  C CZ3 . TRP A 1 109 ? -24.189 14.134  25.842  1.00 49.99  ? 106 TRP A CZ3 1 
ATOM   853  C CH2 . TRP A 1 109 ? -24.046 15.528  25.718  1.00 47.89  ? 106 TRP A CH2 1 
ATOM   854  N N   . GLN A 1 110 ? -27.998 11.372  23.901  1.00 66.33  ? 107 GLN A N   1 
ATOM   855  C CA  . GLN A 1 110 ? -29.438 11.480  24.120  1.00 69.39  ? 107 GLN A CA  1 
ATOM   856  C C   . GLN A 1 110 ? -29.949 12.877  23.788  1.00 71.90  ? 107 GLN A C   1 
ATOM   857  O O   . GLN A 1 110 ? -30.921 13.035  23.034  1.00 70.11  ? 107 GLN A O   1 
ATOM   858  C CB  . GLN A 1 110 ? -29.761 11.121  25.579  1.00 77.29  ? 107 GLN A CB  1 
ATOM   859  C CG  . GLN A 1 110 ? -29.383 9.691   26.026  1.00 77.62  ? 107 GLN A CG  1 
ATOM   860  C CD  . GLN A 1 110 ? -30.583 8.746   26.067  1.00 81.34  ? 107 GLN A CD  1 
ATOM   861  O OE1 . GLN A 1 110 ? -31.732 9.174   25.893  1.00 77.46  ? 107 GLN A OE1 1 
ATOM   862  N NE2 . GLN A 1 110 ? -30.321 7.456   26.297  1.00 72.64  ? 107 GLN A NE2 1 
ATOM   863  N N   . THR A 1 111 ? -29.295 13.905  24.345  1.00 68.65  ? 108 THR A N   1 
ATOM   864  C CA  . THR A 1 111 ? -29.690 15.299  24.196  1.00 70.98  ? 108 THR A CA  1 
ATOM   865  C C   . THR A 1 111 ? -29.084 15.969  22.954  1.00 64.97  ? 108 THR A C   1 
ATOM   866  O O   . THR A 1 111 ? -29.065 17.205  22.872  1.00 66.26  ? 108 THR A O   1 
ATOM   867  C CB  . THR A 1 111 ? -29.323 16.075  25.468  1.00 64.40  ? 108 THR A CB  1 
ATOM   868  O OG1 . THR A 1 111 ? -27.900 16.077  25.644  1.00 57.93  ? 108 THR A OG1 1 
ATOM   869  C CG2 . THR A 1 111 ? -29.976 15.419  26.677  1.00 50.89  ? 108 THR A CG2 1 
ATOM   870  N N   . GLY A 1 112 ? -28.598 15.184  21.984  1.00 63.86  ? 109 GLY A N   1 
ATOM   871  C CA  . GLY A 1 112 ? -28.109 15.764  20.758  1.00 63.04  ? 109 GLY A CA  1 
ATOM   872  C C   . GLY A 1 112 ? -29.232 16.094  19.806  1.00 68.84  ? 109 GLY A C   1 
ATOM   873  O O   . GLY A 1 112 ? -30.324 15.527  19.866  1.00 73.51  ? 109 GLY A O   1 
ATOM   874  N N   . THR A 1 113 ? -28.943 17.035  18.909  1.00 65.14  ? 110 THR A N   1 
ATOM   875  C CA  . THR A 1 113 ? -29.882 17.357  17.836  1.00 72.17  ? 110 THR A CA  1 
ATOM   876  C C   . THR A 1 113 ? -30.308 16.108  17.052  1.00 73.19  ? 110 THR A C   1 
ATOM   877  O O   . THR A 1 113 ? -31.462 16.005  16.613  1.00 75.26  ? 110 THR A O   1 
ATOM   878  C CB  . THR A 1 113 ? -29.257 18.394  16.898  1.00 75.63  ? 110 THR A CB  1 
ATOM   879  O OG1 . THR A 1 113 ? -29.038 19.625  17.619  1.00 76.73  ? 110 THR A OG1 1 
ATOM   880  C CG2 . THR A 1 113 ? -30.166 18.629  15.675  1.00 67.81  ? 110 THR A CG2 1 
ATOM   881  N N   . PHE A 1 114 ? -29.390 15.158  16.857  1.00 67.04  ? 111 PHE A N   1 
ATOM   882  C CA  . PHE A 1 114 ? -29.642 13.903  16.172  1.00 65.56  ? 111 PHE A CA  1 
ATOM   883  C C   . PHE A 1 114 ? -29.415 12.745  17.120  1.00 63.46  ? 111 PHE A C   1 
ATOM   884  O O   . PHE A 1 114 ? -28.740 12.893  18.141  1.00 66.21  ? 111 PHE A O   1 
ATOM   885  C CB  . PHE A 1 114 ? -28.722 13.712  14.965  1.00 57.50  ? 111 PHE A CB  1 
ATOM   886  C CG  . PHE A 1 114 ? -28.242 14.981  14.368  1.00 64.39  ? 111 PHE A CG  1 
ATOM   887  C CD1 . PHE A 1 114 ? -29.097 15.735  13.564  1.00 70.96  ? 111 PHE A CD1 1 
ATOM   888  C CD2 . PHE A 1 114 ? -26.943 15.434  14.608  1.00 61.11  ? 111 PHE A CD2 1 
ATOM   889  C CE1 . PHE A 1 114 ? -28.675 16.927  12.992  1.00 73.06  ? 111 PHE A CE1 1 
ATOM   890  C CE2 . PHE A 1 114 ? -26.502 16.628  14.049  1.00 66.03  ? 111 PHE A CE2 1 
ATOM   891  C CZ  . PHE A 1 114 ? -27.374 17.382  13.237  1.00 75.07  ? 111 PHE A CZ  1 
ATOM   892  N N   . PRO A 1 115 ? -29.934 11.577  16.805  1.00 55.87  ? 112 PRO A N   1 
ATOM   893  C CA  . PRO A 1 115 ? -29.544 10.378  17.561  1.00 54.95  ? 112 PRO A CA  1 
ATOM   894  C C   . PRO A 1 115 ? -28.139 9.937   17.170  1.00 52.43  ? 112 PRO A C   1 
ATOM   895  O O   . PRO A 1 115 ? -27.956 8.964   16.423  1.00 50.05  ? 112 PRO A O   1 
ATOM   896  C CB  . PRO A 1 115 ? -30.598 9.345   17.125  1.00 65.69  ? 112 PRO A CB  1 
ATOM   897  C CG  . PRO A 1 115 ? -30.892 9.730   15.727  1.00 63.38  ? 112 PRO A CG  1 
ATOM   898  C CD  . PRO A 1 115 ? -30.922 11.243  15.744  1.00 65.78  ? 112 PRO A CD  1 
ATOM   899  N N   . MET A 1 116 ? -27.167 10.658  17.671  1.00 49.79  ? 113 MET A N   1 
ATOM   900  C CA  . MET A 1 116 ? -25.780 10.328  17.457  1.00 48.77  ? 113 MET A CA  1 
ATOM   901  C C   . MET A 1 116 ? -25.273 9.309   18.472  1.00 48.33  ? 113 MET A C   1 
ATOM   902  O O   . MET A 1 116 ? -25.675 9.309   19.637  1.00 48.29  ? 113 MET A O   1 
ATOM   903  C CB  . MET A 1 116 ? -24.905 11.569  17.529  1.00 39.82  ? 113 MET A CB  1 
ATOM   904  C CG  . MET A 1 116 ? -23.559 11.271  17.040  1.00 42.47  ? 113 MET A CG  1 
ATOM   905  S SD  . MET A 1 116 ? -22.342 12.399  17.646  1.00 58.06  ? 113 MET A SD  1 
ATOM   906  C CE  . MET A 1 116 ? -23.368 13.747  18.209  1.00 59.53  ? 113 MET A CE  1 
ATOM   907  N N   . VAL A 1 117 ? -24.360 8.451   18.016  1.00 44.91  ? 114 VAL A N   1 
ATOM   908  C CA  . VAL A 1 117 ? -23.854 7.335   18.799  1.00 45.77  ? 114 VAL A CA  1 
ATOM   909  C C   . VAL A 1 117 ? -22.336 7.432   18.875  1.00 42.56  ? 114 VAL A C   1 
ATOM   910  O O   . VAL A 1 117 ? -21.636 7.143   17.893  1.00 41.38  ? 114 VAL A O   1 
ATOM   911  C CB  . VAL A 1 117 ? -24.279 5.998   18.203  1.00 47.65  ? 114 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 117 ? -23.930 4.882   19.164  1.00 39.53  ? 114 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 117 ? -25.757 6.040   17.895  1.00 47.99  ? 114 VAL A CG2 1 
ATOM   914  N N   . PHE A 1 118 ? -21.832 7.817   20.050  1.00 37.17  ? 115 PHE A N   1 
ATOM   915  C CA  . PHE A 1 118 ? -20.394 7.947   20.270  1.00 37.10  ? 115 PHE A CA  1 
ATOM   916  C C   . PHE A 1 118 ? -19.726 6.582   20.159  1.00 39.32  ? 115 PHE A C   1 
ATOM   917  O O   . PHE A 1 118 ? -20.197 5.621   20.775  1.00 46.80  ? 115 PHE A O   1 
ATOM   918  C CB  . PHE A 1 118 ? -20.122 8.540   21.644  1.00 35.03  ? 115 PHE A CB  1 
ATOM   919  C CG  . PHE A 1 118 ? -20.511 9.985   21.779  1.00 39.60  ? 115 PHE A CG  1 
ATOM   920  C CD1 . PHE A 1 118 ? -20.223 10.896  20.773  1.00 39.58  ? 115 PHE A CD1 1 
ATOM   921  C CD2 . PHE A 1 118 ? -21.157 10.437  22.926  1.00 40.22  ? 115 PHE A CD2 1 
ATOM   922  C CE1 . PHE A 1 118 ? -20.564 12.245  20.913  1.00 44.24  ? 115 PHE A CE1 1 
ATOM   923  C CE2 . PHE A 1 118 ? -21.507 11.777  23.069  1.00 41.14  ? 115 PHE A CE2 1 
ATOM   924  C CZ  . PHE A 1 118 ? -21.207 12.679  22.065  1.00 46.93  ? 115 PHE A CZ  1 
ATOM   925  N N   . PRO A 1 119 ? -18.625 6.454   19.426  1.00 31.05  ? 116 PRO A N   1 
ATOM   926  C CA  . PRO A 1 119 ? -18.063 5.122   19.193  1.00 34.57  ? 116 PRO A CA  1 
ATOM   927  C C   . PRO A 1 119 ? -17.513 4.484   20.467  1.00 35.71  ? 116 PRO A C   1 
ATOM   928  O O   . PRO A 1 119 ? -17.117 5.160   21.424  1.00 30.88  ? 116 PRO A O   1 
ATOM   929  C CB  . PRO A 1 119 ? -16.945 5.383   18.174  1.00 25.56  ? 116 PRO A CB  1 
ATOM   930  C CG  . PRO A 1 119 ? -16.505 6.753   18.473  1.00 28.88  ? 116 PRO A CG  1 
ATOM   931  C CD  . PRO A 1 119 ? -17.749 7.511   18.900  1.00 30.66  ? 116 PRO A CD  1 
ATOM   932  N N   . ALA A 1 120 ? -17.534 3.151   20.463  1.00 33.89  ? 117 ALA A N   1 
ATOM   933  C CA  . ALA A 1 120 ? -16.727 2.347   21.370  1.00 34.91  ? 117 ALA A CA  1 
ATOM   934  C C   . ALA A 1 120 ? -15.286 2.834   21.386  1.00 32.72  ? 117 ALA A C   1 
ATOM   935  O O   . ALA A 1 120 ? -14.760 3.310   20.374  1.00 31.97  ? 117 ALA A O   1 
ATOM   936  C CB  . ALA A 1 120 ? -16.765 0.879   20.938  1.00 31.99  ? 117 ALA A CB  1 
ATOM   937  N N   . TYR A 1 121 ? -14.655 2.716   22.552  1.00 31.33  ? 118 TYR A N   1 
ATOM   938  C CA  . TYR A 1 121 ? -13.270 3.135   22.711  1.00 31.57  ? 118 TYR A CA  1 
ATOM   939  C C   . TYR A 1 121 ? -12.378 2.285   21.820  1.00 31.90  ? 118 TYR A C   1 
ATOM   940  O O   . TYR A 1 121 ? -12.597 1.081   21.668  1.00 34.53  ? 118 TYR A O   1 
ATOM   941  C CB  . TYR A 1 121 ? -12.815 2.990   24.174  1.00 31.86  ? 118 TYR A CB  1 
ATOM   942  C CG  . TYR A 1 121 ? -13.481 3.923   25.182  1.00 37.51  ? 118 TYR A CG  1 
ATOM   943  C CD1 . TYR A 1 121 ? -14.430 4.870   24.785  1.00 34.49  ? 118 TYR A CD1 1 
ATOM   944  C CD2 . TYR A 1 121 ? -13.150 3.861   26.540  1.00 34.45  ? 118 TYR A CD2 1 
ATOM   945  C CE1 . TYR A 1 121 ? -15.028 5.716   25.726  1.00 34.71  ? 118 TYR A CE1 1 
ATOM   946  C CE2 . TYR A 1 121 ? -13.735 4.707   27.471  1.00 32.50  ? 118 TYR A CE2 1 
ATOM   947  C CZ  . TYR A 1 121 ? -14.668 5.623   27.061  1.00 35.74  ? 118 TYR A CZ  1 
ATOM   948  O OH  . TYR A 1 121 ? -15.242 6.461   27.983  1.00 42.51  ? 118 TYR A OH  1 
ATOM   949  N N   . ARG A 1 122 ? -11.350 2.909   21.258  1.00 28.17  ? 119 ARG A N   1 
ATOM   950  C CA  . ARG A 1 122 ? -10.453 2.261   20.311  1.00 28.38  ? 119 ARG A CA  1 
ATOM   951  C C   . ARG A 1 122 ? -9.122  1.962   20.992  1.00 33.31  ? 119 ARG A C   1 
ATOM   952  O O   . ARG A 1 122 ? -8.527  2.846   21.624  1.00 34.27  ? 119 ARG A O   1 
ATOM   953  C CB  . ARG A 1 122 ? -10.255 3.164   19.083  1.00 29.11  ? 119 ARG A CB  1 
ATOM   954  C CG  . ARG A 1 122 ? -9.316  2.664   18.044  1.00 24.95  ? 119 ARG A CG  1 
ATOM   955  C CD  . ARG A 1 122 ? -9.407  3.569   16.841  1.00 33.12  ? 119 ARG A CD  1 
ATOM   956  N NE  . ARG A 1 122 ? -8.957  4.940   17.085  1.00 35.92  ? 119 ARG A NE  1 
ATOM   957  C CZ  . ARG A 1 122 ? -7.808  5.431   16.631  1.00 32.13  ? 119 ARG A CZ  1 
ATOM   958  N NH1 . ARG A 1 122 ? -6.937  4.664   15.983  1.00 28.60  ? 119 ARG A NH1 1 
ATOM   959  N NH2 . ARG A 1 122 ? -7.530  6.721   16.819  1.00 25.70  ? 119 ARG A NH2 1 
ATOM   960  N N   . LYS A 1 123 ? -8.658  0.722   20.870  1.00 32.89  ? 120 LYS A N   1 
ATOM   961  C CA  . LYS A 1 123 ? -7.366  0.363   21.435  1.00 31.26  ? 120 LYS A CA  1 
ATOM   962  C C   . LYS A 1 123 ? -6.268  0.960   20.587  1.00 32.03  ? 120 LYS A C   1 
ATOM   963  O O   . LYS A 1 123 ? -6.301  0.870   19.357  1.00 37.30  ? 120 LYS A O   1 
ATOM   964  C CB  . LYS A 1 123 ? -7.178  -1.153  21.514  1.00 30.75  ? 120 LYS A CB  1 
ATOM   965  C CG  . LYS A 1 123 ? -6.166  -1.542  22.586  1.00 37.97  ? 120 LYS A CG  1 
ATOM   966  C CD  . LYS A 1 123 ? -5.384  -2.824  22.295  1.00 44.14  ? 120 LYS A CD  1 
ATOM   967  C CE  . LYS A 1 123 ? -4.015  -2.795  22.999  1.00 42.60  ? 120 LYS A CE  1 
ATOM   968  N NZ  . LYS A 1 123 ? -3.828  -3.893  23.975  1.00 47.12  ? 120 LYS A NZ  1 
ATOM   969  N N   . LEU A 1 124 ? -5.297  1.570   21.250  1.00 35.69  ? 121 LEU A N   1 
ATOM   970  C CA  . LEU A 1 124 ? -4.150  2.176   20.599  1.00 30.89  ? 121 LEU A CA  1 
ATOM   971  C C   . LEU A 1 124 ? -2.970  1.232   20.736  1.00 36.60  ? 121 LEU A C   1 
ATOM   972  O O   . LEU A 1 124 ? -2.730  0.689   21.815  1.00 42.62  ? 121 LEU A O   1 
ATOM   973  C CB  . LEU A 1 124 ? -3.840  3.528   21.233  1.00 26.78  ? 121 LEU A CB  1 
ATOM   974  C CG  . LEU A 1 124 ? -5.076  4.408   21.091  1.00 29.81  ? 121 LEU A CG  1 
ATOM   975  C CD1 . LEU A 1 124 ? -4.922  5.698   21.869  1.00 29.10  ? 121 LEU A CD1 1 
ATOM   976  C CD2 . LEU A 1 124 ? -5.391  4.654   19.583  1.00 29.27  ? 121 LEU A CD2 1 
ATOM   977  N N   . ASP A 1 125 ? -2.240  1.025   19.656  1.00 35.62  ? 122 ASP A N   1 
ATOM   978  C CA  . ASP A 1 125 ? -1.079  0.162   19.715  1.00 34.38  ? 122 ASP A CA  1 
ATOM   979  C C   . ASP A 1 125 ? 0.189   0.985   19.519  1.00 36.02  ? 122 ASP A C   1 
ATOM   980  O O   . ASP A 1 125 ? 0.301   1.739   18.545  1.00 40.80  ? 122 ASP A O   1 
ATOM   981  C CB  . ASP A 1 125 ? -1.189  -0.947  18.682  1.00 37.96  ? 122 ASP A CB  1 
ATOM   982  C CG  . ASP A 1 125 ? -0.159  -2.005  18.903  1.00 54.61  ? 122 ASP A CG  1 
ATOM   983  O OD1 . ASP A 1 125 ? -0.383  -2.892  19.766  1.00 69.13  ? 122 ASP A OD1 1 
ATOM   984  O OD2 . ASP A 1 125 ? 0.909   -1.919  18.259  1.00 58.95  ? 122 ASP A OD2 1 
ATOM   985  N N   . LEU A 1 126 ? 1.136   0.850   20.451  1.00 30.88  ? 123 LEU A N   1 
ATOM   986  C CA  . LEU A 1 126 ? 2.275   1.765   20.482  1.00 30.16  ? 123 LEU A CA  1 
ATOM   987  C C   . LEU A 1 126 ? 3.149   1.609   19.246  1.00 34.82  ? 123 LEU A C   1 
ATOM   988  O O   . LEU A 1 126 ? 3.809   2.571   18.834  1.00 35.17  ? 123 LEU A O   1 
ATOM   989  C CB  . LEU A 1 126 ? 3.093   1.569   21.774  1.00 24.98  ? 123 LEU A CB  1 
ATOM   990  C CG  . LEU A 1 126 ? 2.336   2.085   23.017  1.00 30.90  ? 123 LEU A CG  1 
ATOM   991  C CD1 . LEU A 1 126 ? 2.963   1.734   24.365  1.00 28.01  ? 123 LEU A CD1 1 
ATOM   992  C CD2 . LEU A 1 126 ? 2.129   3.575   22.906  1.00 26.25  ? 123 LEU A CD2 1 
ATOM   993  N N   . ARG A 1 127 ? 3.132   0.429   18.615  1.00 37.48  ? 124 ARG A N   1 
ATOM   994  C CA  . ARG A 1 127 ? 3.928   0.210   17.410  1.00 37.07  ? 124 ARG A CA  1 
ATOM   995  C C   . ARG A 1 127 ? 3.596   1.201   16.302  1.00 39.39  ? 124 ARG A C   1 
ATOM   996  O O   . ARG A 1 127 ? 4.461   1.465   15.462  1.00 40.85  ? 124 ARG A O   1 
ATOM   997  C CB  . ARG A 1 127 ? 3.743   -1.220  16.895  1.00 38.04  ? 124 ARG A CB  1 
ATOM   998  C CG  . ARG A 1 127 ? 2.637   -1.386  15.857  1.00 44.97  ? 124 ARG A CG  1 
ATOM   999  C CD  . ARG A 1 127 ? 2.372   -2.863  15.488  1.00 47.92  ? 124 ARG A CD  1 
ATOM   1000 N NE  . ARG A 1 127 ? 1.944   -3.629  16.653  1.00 55.54  ? 124 ARG A NE  1 
ATOM   1001 C CZ  . ARG A 1 127 ? 1.431   -4.855  16.629  1.00 58.48  ? 124 ARG A CZ  1 
ATOM   1002 N NH1 . ARG A 1 127 ? 1.248   -5.509  15.491  1.00 56.04  ? 124 ARG A NH1 1 
ATOM   1003 N NH2 . ARG A 1 127 ? 1.095   -5.440  17.780  1.00 56.84  ? 124 ARG A NH2 1 
ATOM   1004 N N   . HIS A 1 128 ? 2.386   1.779   16.295  1.00 39.42  ? 125 HIS A N   1 
ATOM   1005 C CA  . HIS A 1 128 ? 2.004   2.755   15.274  1.00 38.05  ? 125 HIS A CA  1 
ATOM   1006 C C   . HIS A 1 128 ? 2.589   4.142   15.494  1.00 34.40  ? 125 HIS A C   1 
ATOM   1007 O O   . HIS A 1 128 ? 2.392   5.007   14.643  1.00 36.43  ? 125 HIS A O   1 
ATOM   1008 C CB  . HIS A 1 128 ? 0.477   2.905   15.187  1.00 34.50  ? 125 HIS A CB  1 
ATOM   1009 C CG  . HIS A 1 128 ? -0.230  1.641   14.847  1.00 35.28  ? 125 HIS A CG  1 
ATOM   1010 N ND1 . HIS A 1 128 ? -1.438  1.291   15.409  1.00 45.52  ? 125 HIS A ND1 1 
ATOM   1011 C CD2 . HIS A 1 128 ? 0.111   0.624   14.022  1.00 39.25  ? 125 HIS A CD2 1 
ATOM   1012 C CE1 . HIS A 1 128 ? -1.809  0.109   14.949  1.00 47.37  ? 125 HIS A CE1 1 
ATOM   1013 N NE2 . HIS A 1 128 ? -0.887  -0.316  14.103  1.00 47.15  ? 125 HIS A NE2 1 
ATOM   1014 N N   . TYR A 1 129 ? 3.268   4.401   16.598  1.00 34.34  ? 126 TYR A N   1 
ATOM   1015 C CA  . TYR A 1 129 ? 3.635   5.768   16.914  1.00 32.37  ? 126 TYR A CA  1 
ATOM   1016 C C   . TYR A 1 129 ? 5.131   5.859   17.155  1.00 36.67  ? 126 TYR A C   1 
ATOM   1017 O O   . TYR A 1 129 ? 5.743   4.941   17.708  1.00 39.29  ? 126 TYR A O   1 
ATOM   1018 C CB  . TYR A 1 129 ? 2.847   6.278   18.132  1.00 34.63  ? 126 TYR A CB  1 
ATOM   1019 C CG  . TYR A 1 129 ? 1.346   6.063   18.001  1.00 37.03  ? 126 TYR A CG  1 
ATOM   1020 C CD1 . TYR A 1 129 ? 0.569   6.899   17.203  1.00 32.26  ? 126 TYR A CD1 1 
ATOM   1021 C CD2 . TYR A 1 129 ? 0.707   5.014   18.666  1.00 35.75  ? 126 TYR A CD2 1 
ATOM   1022 C CE1 . TYR A 1 129 ? -0.797  6.711   17.073  1.00 33.86  ? 126 TYR A CE1 1 
ATOM   1023 C CE2 . TYR A 1 129 ? -0.676  4.812   18.542  1.00 37.02  ? 126 TYR A CE2 1 
ATOM   1024 C CZ  . TYR A 1 129 ? -1.429  5.670   17.734  1.00 38.72  ? 126 TYR A CZ  1 
ATOM   1025 O OH  . TYR A 1 129 ? -2.801  5.498   17.576  1.00 29.41  ? 126 TYR A OH  1 
ATOM   1026 N N   . ASP A 1 130 ? 5.715   6.960   16.706  1.00 39.02  ? 127 ASP A N   1 
ATOM   1027 C CA  . ASP A 1 130 ? 7.095   7.288   17.011  1.00 38.50  ? 127 ASP A CA  1 
ATOM   1028 C C   . ASP A 1 130 ? 7.200   8.806   17.132  1.00 33.30  ? 127 ASP A C   1 
ATOM   1029 O O   . ASP A 1 130 ? 6.198   9.506   17.290  1.00 32.00  ? 127 ASP A O   1 
ATOM   1030 C CB  . ASP A 1 130 ? 8.039   6.693   15.950  1.00 41.85  ? 127 ASP A CB  1 
ATOM   1031 C CG  . ASP A 1 130 ? 7.642   7.073   14.531  1.00 49.60  ? 127 ASP A CG  1 
ATOM   1032 O OD1 . ASP A 1 130 ? 7.197   8.224   14.299  1.00 48.14  ? 127 ASP A OD1 1 
ATOM   1033 O OD2 . ASP A 1 130 ? 7.790   6.215   13.633  1.00 60.67  ? 127 ASP A OD2 1 
ATOM   1034 N N   . ASP A 1 131 ? 8.418   9.319   17.058  1.00 41.32  ? 128 ASP A N   1 
ATOM   1035 C CA  . ASP A 1 131 ? 8.624   10.746  17.250  1.00 40.97  ? 128 ASP A CA  1 
ATOM   1036 C C   . ASP A 1 131 ? 8.044   11.552  16.092  1.00 38.57  ? 128 ASP A C   1 
ATOM   1037 O O   . ASP A 1 131 ? 7.585   12.685  16.283  1.00 38.11  ? 128 ASP A O   1 
ATOM   1038 C CB  . ASP A 1 131 ? 10.122  11.003  17.441  1.00 46.44  ? 128 ASP A CB  1 
ATOM   1039 C CG  . ASP A 1 131 ? 10.739  10.109  18.544  1.00 54.29  ? 128 ASP A CG  1 
ATOM   1040 O OD1 . ASP A 1 131 ? 10.023  9.780   19.521  1.00 53.69  ? 128 ASP A OD1 1 
ATOM   1041 O OD2 . ASP A 1 131 ? 11.932  9.727   18.433  1.00 53.68  ? 128 ASP A OD2 1 
ATOM   1042 N N   . ALA A 1 132 ? 8.029   10.974  14.892  1.00 38.87  ? 129 ALA A N   1 
ATOM   1043 C CA  . ALA A 1 132 ? 7.399   11.646  13.762  1.00 37.64  ? 129 ALA A CA  1 
ATOM   1044 C C   . ALA A 1 132 ? 5.887   11.629  13.882  1.00 35.08  ? 129 ALA A C   1 
ATOM   1045 O O   . ALA A 1 132 ? 5.220   12.569  13.441  1.00 42.15  ? 129 ALA A O   1 
ATOM   1046 C CB  . ALA A 1 132 ? 7.823   10.989  12.448  1.00 39.93  ? 129 ALA A CB  1 
ATOM   1047 N N   . LEU A 1 133 ? 5.330   10.583  14.474  1.00 34.02  ? 130 LEU A N   1 
ATOM   1048 C CA  . LEU A 1 133 ? 3.886   10.424  14.614  1.00 34.92  ? 130 LEU A CA  1 
ATOM   1049 C C   . LEU A 1 133 ? 3.557   10.032  16.056  1.00 36.63  ? 130 LEU A C   1 
ATOM   1050 O O   . LEU A 1 133 ? 3.223   8.873   16.331  1.00 37.51  ? 130 LEU A O   1 
ATOM   1051 C CB  . LEU A 1 133 ? 3.392   9.376   13.612  1.00 33.98  ? 130 LEU A CB  1 
ATOM   1052 C CG  . LEU A 1 133 ? 1.996   9.532   13.002  1.00 39.06  ? 130 LEU A CG  1 
ATOM   1053 C CD1 . LEU A 1 133 ? 1.802   10.928  12.421  1.00 30.20  ? 130 LEU A CD1 1 
ATOM   1054 C CD2 . LEU A 1 133 ? 1.742   8.451   11.965  1.00 35.98  ? 130 LEU A CD2 1 
ATOM   1055 N N   . PRO A 1 134 ? 3.665   10.965  17.006  1.00 33.14  ? 131 PRO A N   1 
ATOM   1056 C CA  . PRO A 1 134 ? 3.523   10.594  18.424  1.00 36.16  ? 131 PRO A CA  1 
ATOM   1057 C C   . PRO A 1 134 ? 2.119   10.115  18.779  1.00 38.60  ? 131 PRO A C   1 
ATOM   1058 O O   . PRO A 1 134 ? 1.146   10.324  18.043  1.00 31.85  ? 131 PRO A O   1 
ATOM   1059 C CB  . PRO A 1 134 ? 3.868   11.885  19.185  1.00 29.12  ? 131 PRO A CB  1 
ATOM   1060 C CG  . PRO A 1 134 ? 3.772   12.956  18.210  1.00 33.23  ? 131 PRO A CG  1 
ATOM   1061 C CD  . PRO A 1 134 ? 4.075   12.366  16.854  1.00 34.67  ? 131 PRO A CD  1 
ATOM   1062 N N   . LEU A 1 135 ? 2.047   9.451   19.949  1.00 36.37  ? 132 LEU A N   1 
ATOM   1063 C CA  . LEU A 1 135 ? 0.792   8.899   20.463  1.00 34.04  ? 132 LEU A CA  1 
ATOM   1064 C C   . LEU A 1 135 ? -0.336  9.922   20.415  1.00 31.29  ? 132 LEU A C   1 
ATOM   1065 O O   . LEU A 1 135 ? -1.495  9.574   20.156  1.00 30.17  ? 132 LEU A O   1 
ATOM   1066 C CB  . LEU A 1 135 ? 0.995   8.394   21.899  1.00 33.79  ? 132 LEU A CB  1 
ATOM   1067 C CG  . LEU A 1 135 ? -0.216  8.059   22.779  1.00 29.88  ? 132 LEU A CG  1 
ATOM   1068 C CD1 . LEU A 1 135 ? -1.050  6.999   22.109  1.00 27.10  ? 132 LEU A CD1 1 
ATOM   1069 C CD2 . LEU A 1 135 ? 0.238   7.583   24.149  1.00 31.11  ? 132 LEU A CD2 1 
ATOM   1070 N N   . SER A 1 136 ? -0.019  11.189  20.671  1.00 30.28  ? 133 SER A N   1 
ATOM   1071 C CA  . SER A 1 136 ? -1.030  12.234  20.642  1.00 28.51  ? 133 SER A CA  1 
ATOM   1072 C C   . SER A 1 136 ? -1.776  12.301  19.311  1.00 31.38  ? 133 SER A C   1 
ATOM   1073 O O   . SER A 1 136 ? -2.904  12.806  19.274  1.00 32.75  ? 133 SER A O   1 
ATOM   1074 C CB  . SER A 1 136 ? -0.361  13.568  20.928  1.00 29.21  ? 133 SER A CB  1 
ATOM   1075 O OG  . SER A 1 136 ? 0.850   13.651  20.184  1.00 34.19  ? 133 SER A OG  1 
ATOM   1076 N N   . THR A 1 137 ? -1.178  11.816  18.216  1.00 29.51  ? 134 THR A N   1 
ATOM   1077 C CA  . THR A 1 137 ? -1.832  11.937  16.919  1.00 30.91  ? 134 THR A CA  1 
ATOM   1078 C C   . THR A 1 137 ? -3.107  11.118  16.814  1.00 29.75  ? 134 THR A C   1 
ATOM   1079 O O   . THR A 1 137 ? -3.783  11.218  15.790  1.00 28.30  ? 134 THR A O   1 
ATOM   1080 C CB  . THR A 1 137 ? -0.921  11.520  15.759  1.00 34.37  ? 134 THR A CB  1 
ATOM   1081 O OG1 . THR A 1 137 ? -0.526  10.148  15.908  1.00 32.32  ? 134 THR A OG1 1 
ATOM   1082 C CG2 . THR A 1 137 ? 0.279   12.436  15.661  1.00 32.06  ? 134 THR A CG2 1 
ATOM   1083 N N   . ALA A 1 138 ? -3.450  10.313  17.827  1.00 31.92  ? 135 ALA A N   1 
ATOM   1084 C CA  . ALA A 1 138 ? -4.732  9.617   17.831  1.00 26.88  ? 135 ALA A CA  1 
ATOM   1085 C C   . ALA A 1 138 ? -5.894  10.565  18.060  1.00 27.91  ? 135 ALA A C   1 
ATOM   1086 O O   . ALA A 1 138 ? -7.053  10.138  17.986  1.00 33.83  ? 135 ALA A O   1 
ATOM   1087 C CB  . ALA A 1 138 ? -4.725  8.506   18.881  1.00 27.53  ? 135 ALA A CB  1 
ATOM   1088 N N   . LEU A 1 139 ? -5.614  11.836  18.333  1.00 26.65  ? 136 LEU A N   1 
ATOM   1089 C CA  . LEU A 1 139 ? -6.635  12.865  18.410  1.00 28.62  ? 136 LEU A CA  1 
ATOM   1090 C C   . LEU A 1 139 ? -6.550  13.831  17.237  1.00 30.85  ? 136 LEU A C   1 
ATOM   1091 O O   . LEU A 1 139 ? -7.333  14.788  17.163  1.00 30.97  ? 136 LEU A O   1 
ATOM   1092 C CB  . LEU A 1 139 ? -6.524  13.627  19.740  1.00 24.99  ? 136 LEU A CB  1 
ATOM   1093 C CG  . LEU A 1 139 ? -6.634  12.794  21.012  1.00 28.80  ? 136 LEU A CG  1 
ATOM   1094 C CD1 . LEU A 1 139 ? -6.425  13.650  22.295  1.00 28.06  ? 136 LEU A CD1 1 
ATOM   1095 C CD2 . LEU A 1 139 ? -7.963  12.068  21.037  1.00 22.76  ? 136 LEU A CD2 1 
ATOM   1096 N N   . GLY A 1 140 ? -5.611  13.614  16.329  1.00 27.58  ? 137 GLY A N   1 
ATOM   1097 C CA  . GLY A 1 140 ? -5.453  14.475  15.177  1.00 26.77  ? 137 GLY A CA  1 
ATOM   1098 C C   . GLY A 1 140 ? -5.342  13.699  13.881  1.00 29.45  ? 137 GLY A C   1 
ATOM   1099 O O   . GLY A 1 140 ? -6.305  13.057  13.436  1.00 24.91  ? 137 GLY A O   1 
ATOM   1100 N N   . VAL A 1 141 ? -4.158  13.741  13.271  1.00 28.05  ? 138 VAL A N   1 
ATOM   1101 C CA  . VAL A 1 141 ? -3.999  13.138  11.952  1.00 27.51  ? 138 VAL A CA  1 
ATOM   1102 C C   . VAL A 1 141 ? -4.201  11.616  11.984  1.00 28.44  ? 138 VAL A C   1 
ATOM   1103 O O   . VAL A 1 141 ? -4.693  11.037  11.016  1.00 31.03  ? 138 VAL A O   1 
ATOM   1104 C CB  . VAL A 1 141 ? -2.631  13.528  11.363  1.00 31.28  ? 138 VAL A CB  1 
ATOM   1105 C CG1 . VAL A 1 141 ? -1.487  13.060  12.262  1.00 31.63  ? 138 VAL A CG1 1 
ATOM   1106 C CG2 . VAL A 1 141 ? -2.478  12.964  9.972   1.00 30.49  ? 138 VAL A CG2 1 
ATOM   1107 N N   . MET A 1 142 ? -3.852  10.933  13.072  1.00 30.54  ? 139 MET A N   1 
ATOM   1108 C CA  . MET A 1 142 ? -4.239  9.536   13.227  1.00 27.81  ? 139 MET A CA  1 
ATOM   1109 C C   . MET A 1 142 ? -5.472  9.396   14.102  1.00 25.57  ? 139 MET A C   1 
ATOM   1110 O O   . MET A 1 142 ? -5.599  8.424   14.862  1.00 27.56  ? 139 MET A O   1 
ATOM   1111 C CB  . MET A 1 142 ? -3.081  8.721   13.796  1.00 29.75  ? 139 MET A CB  1 
ATOM   1112 C CG  . MET A 1 142 ? -1.847  8.777   12.949  1.00 30.35  ? 139 MET A CG  1 
ATOM   1113 S SD  . MET A 1 142 ? -2.030  7.862   11.405  1.00 37.27  ? 139 MET A SD  1 
ATOM   1114 C CE  . MET A 1 142 ? -2.009  9.232   10.278  1.00 37.10  ? 139 MET A CE  1 
ATOM   1115 N N   . GLY A 1 143 ? -6.378  10.377  14.035  1.00 25.39  ? 140 GLY A N   1 
ATOM   1116 C CA  . GLY A 1 143 ? -7.605  10.379  14.800  1.00 25.35  ? 140 GLY A CA  1 
ATOM   1117 C C   . GLY A 1 143 ? -8.800  10.787  13.950  1.00 25.89  ? 140 GLY A C   1 
ATOM   1118 O O   . GLY A 1 143 ? -8.846  10.572  12.740  1.00 28.62  ? 140 GLY A O   1 
ATOM   1119 N N   . GLY A 1 144 ? -9.786  11.356  14.613  1.00 26.64  ? 141 GLY A N   1 
ATOM   1120 C CA  . GLY A 1 144 ? -10.982 11.818  13.963  1.00 25.68  ? 141 GLY A CA  1 
ATOM   1121 C C   . GLY A 1 144 ? -10.714 12.764  12.810  1.00 29.20  ? 141 GLY A C   1 
ATOM   1122 O O   . GLY A 1 144 ? -11.159 12.544  11.685  1.00 26.26  ? 141 GLY A O   1 
ATOM   1123 N N   . PRO A 1 145 ? -9.969  13.839  13.071  1.00 30.15  ? 142 PRO A N   1 
ATOM   1124 C CA  . PRO A 1 145 ? -9.671  14.798  11.987  1.00 26.73  ? 142 PRO A CA  1 
ATOM   1125 C C   . PRO A 1 145 ? -8.972  14.181  10.785  1.00 29.31  ? 142 PRO A C   1 
ATOM   1126 O O   . PRO A 1 145 ? -9.392  14.407  9.637   1.00 31.49  ? 142 PRO A O   1 
ATOM   1127 C CB  . PRO A 1 145 ? -8.792  15.831  12.690  1.00 27.88  ? 142 PRO A CB  1 
ATOM   1128 C CG  . PRO A 1 145 ? -9.234  15.757  14.120  1.00 28.94  ? 142 PRO A CG  1 
ATOM   1129 C CD  . PRO A 1 145 ? -9.546  14.333  14.391  1.00 24.07  ? 142 PRO A CD  1 
ATOM   1130 N N   . GLY A 1 146 ? -7.902  13.418  11.001  1.00 28.66  ? 143 GLY A N   1 
ATOM   1131 C CA  . GLY A 1 146 ? -7.287  12.735  9.882   1.00 23.23  ? 143 GLY A CA  1 
ATOM   1132 C C   . GLY A 1 146 ? -8.280  11.852  9.158   1.00 25.04  ? 143 GLY A C   1 
ATOM   1133 O O   . GLY A 1 146 ? -8.325  11.828  7.932   1.00 29.82  ? 143 GLY A O   1 
ATOM   1134 N N   . MET A 1 147 ? -9.107  11.132  9.910   1.00 25.84  ? 144 MET A N   1 
ATOM   1135 C CA  . MET A 1 147 ? -10.032 10.204  9.282   1.00 23.99  ? 144 MET A CA  1 
ATOM   1136 C C   . MET A 1 147 ? -11.047 10.945  8.437   1.00 27.47  ? 144 MET A C   1 
ATOM   1137 O O   . MET A 1 147 ? -11.497 10.430  7.408   1.00 23.50  ? 144 MET A O   1 
ATOM   1138 C CB  . MET A 1 147 ? -10.743 9.357   10.337  1.00 25.79  ? 144 MET A CB  1 
ATOM   1139 C CG  . MET A 1 147 ? -11.635 8.250   9.756   1.00 26.54  ? 144 MET A CG  1 
ATOM   1140 S SD  . MET A 1 147 ? -10.812 6.963   8.791   1.00 32.61  ? 144 MET A SD  1 
ATOM   1141 C CE  . MET A 1 147 ? -10.342 5.784   10.052  1.00 25.65  ? 144 MET A CE  1 
ATOM   1142 N N   . THR A 1 148 ? -11.404 12.156  8.857   1.00 26.51  ? 145 THR A N   1 
ATOM   1143 C CA  . THR A 1 148 ? -12.335 12.967  8.094   1.00 27.34  ? 145 THR A CA  1 
ATOM   1144 C C   . THR A 1 148 ? -11.736 13.390  6.759   1.00 25.34  ? 145 THR A C   1 
ATOM   1145 O O   . THR A 1 148 ? -12.359 13.214  5.706   1.00 20.76  ? 145 THR A O   1 
ATOM   1146 C CB  . THR A 1 148 ? -12.727 14.181  8.907   1.00 23.25  ? 145 THR A CB  1 
ATOM   1147 O OG1 . THR A 1 148 ? -13.401 13.732  10.080  1.00 26.94  ? 145 THR A OG1 1 
ATOM   1148 C CG2 . THR A 1 148 ? -13.635 15.029  8.113   1.00 26.17  ? 145 THR A CG2 1 
ATOM   1149 N N   . ALA A 1 149 ? -10.531 13.968  6.789   1.00 28.46  ? 146 ALA A N   1 
ATOM   1150 C CA  . ALA A 1 149 ? -9.870  14.373  5.552   1.00 24.34  ? 146 ALA A CA  1 
ATOM   1151 C C   . ALA A 1 149 ? -9.608  13.170  4.655   1.00 28.33  ? 146 ALA A C   1 
ATOM   1152 O O   . ALA A 1 149 ? -9.970  13.175  3.477   1.00 28.88  ? 146 ALA A O   1 
ATOM   1153 C CB  . ALA A 1 149 ? -8.567  15.097  5.862   1.00 26.33  ? 146 ALA A CB  1 
ATOM   1154 N N   . TRP A 1 150 ? -9.028  12.105  5.210   1.00 26.01  ? 147 TRP A N   1 
ATOM   1155 C CA  . TRP A 1 150 ? -8.645  10.970  4.380   1.00 28.57  ? 147 TRP A CA  1 
ATOM   1156 C C   . TRP A 1 150 ? -9.857  10.217  3.839   1.00 27.42  ? 147 TRP A C   1 
ATOM   1157 O O   . TRP A 1 150 ? -9.860  9.776   2.680   1.00 23.37  ? 147 TRP A O   1 
ATOM   1158 C CB  . TRP A 1 150 ? -7.752  10.042  5.184   1.00 24.69  ? 147 TRP A CB  1 
ATOM   1159 C CG  . TRP A 1 150 ? -7.379  8.812   4.460   1.00 25.74  ? 147 TRP A CG  1 
ATOM   1160 C CD1 . TRP A 1 150 ? -6.308  8.632   3.628   1.00 24.83  ? 147 TRP A CD1 1 
ATOM   1161 C CD2 . TRP A 1 150 ? -8.064  7.562   4.510   1.00 28.16  ? 147 TRP A CD2 1 
ATOM   1162 N NE1 . TRP A 1 150 ? -6.287  7.337   3.150   1.00 28.02  ? 147 TRP A NE1 1 
ATOM   1163 C CE2 . TRP A 1 150 ? -7.355  6.661   3.681   1.00 30.20  ? 147 TRP A CE2 1 
ATOM   1164 C CE3 . TRP A 1 150 ? -9.206  7.113   5.175   1.00 28.06  ? 147 TRP A CE3 1 
ATOM   1165 C CZ2 . TRP A 1 150 ? -7.754  5.350   3.507   1.00 28.64  ? 147 TRP A CZ2 1 
ATOM   1166 C CZ3 . TRP A 1 150 ? -9.598  5.814   4.999   1.00 30.55  ? 147 TRP A CZ3 1 
ATOM   1167 C CH2 . TRP A 1 150 ? -8.877  4.945   4.169   1.00 28.81  ? 147 TRP A CH2 1 
ATOM   1168 N N   . GLY A 1 151 ? -10.878 10.046  4.666   1.00 25.99  ? 148 GLY A N   1 
ATOM   1169 C CA  . GLY A 1 151 ? -12.082 9.389   4.202   1.00 27.58  ? 148 GLY A CA  1 
ATOM   1170 C C   . GLY A 1 151 ? -12.767 10.151  3.083   1.00 30.09  ? 148 GLY A C   1 
ATOM   1171 O O   . GLY A 1 151 ? -13.231 9.549   2.107   1.00 28.52  ? 148 GLY A O   1 
ATOM   1172 N N   . THR A 1 152 ? -12.850 11.484  3.209   1.00 27.75  ? 149 THR A N   1 
ATOM   1173 C CA  . THR A 1 152 ? -13.487 12.284  2.163   1.00 24.99  ? 149 THR A CA  1 
ATOM   1174 C C   . THR A 1 152 ? -12.707 12.177  0.856   1.00 27.11  ? 149 THR A C   1 
ATOM   1175 O O   . THR A 1 152 ? -13.281 11.904  -0.206  1.00 31.76  ? 149 THR A O   1 
ATOM   1176 C CB  . THR A 1 152 ? -13.610 13.745  2.602   1.00 22.88  ? 149 THR A CB  1 
ATOM   1177 O OG1 . THR A 1 152 ? -14.362 13.830  3.819   1.00 23.04  ? 149 THR A OG1 1 
ATOM   1178 C CG2 . THR A 1 152 ? -14.334 14.552  1.546   1.00 24.90  ? 149 THR A CG2 1 
ATOM   1179 N N   . MET A 1 153 ? -11.388 12.324  0.923   1.00 21.17  ? 150 MET A N   1 
ATOM   1180 C CA  . MET A 1 153 ? -10.568 12.301  -0.283  1.00 29.13  ? 150 MET A CA  1 
ATOM   1181 C C   . MET A 1 153 ? -10.369 10.913  -0.885  1.00 30.25  ? 150 MET A C   1 
ATOM   1182 O O   . MET A 1 153 ? -9.752  10.808  -1.950  1.00 29.29  ? 150 MET A O   1 
ATOM   1183 C CB  . MET A 1 153 ? -9.201  12.923  0.001   1.00 24.61  ? 150 MET A CB  1 
ATOM   1184 C CG  . MET A 1 153 ? -9.315  14.277  0.651   1.00 30.86  ? 150 MET A CG  1 
ATOM   1185 S SD  . MET A 1 153 ? -10.259 15.432  -0.377  1.00 41.62  ? 150 MET A SD  1 
ATOM   1186 C CE  . MET A 1 153 ? -9.086  15.625  -1.726  1.00 24.20  ? 150 MET A CE  1 
ATOM   1187 N N   . THR A 1 154 ? -10.829 9.842   -0.257  1.00 24.73  ? 151 THR A N   1 
ATOM   1188 C CA  . THR A 1 154 ? -10.615 8.550   -0.878  1.00 25.18  ? 151 THR A CA  1 
ATOM   1189 C C   . THR A 1 154 ? -11.878 7.750   -1.052  1.00 30.47  ? 151 THR A C   1 
ATOM   1190 O O   . THR A 1 154 ? -11.866 6.793   -1.830  1.00 34.39  ? 151 THR A O   1 
ATOM   1191 C CB  . THR A 1 154 ? -9.592  7.709   -0.091  1.00 25.95  ? 151 THR A CB  1 
ATOM   1192 O OG1 . THR A 1 154 ? -10.064 7.458   1.234   1.00 30.36  ? 151 THR A OG1 1 
ATOM   1193 C CG2 . THR A 1 154 ? -8.231  8.397   -0.035  1.00 23.67  ? 151 THR A CG2 1 
ATOM   1194 N N   . LYS A 1 155 ? -12.960 8.106   -0.371  1.00 28.26  ? 152 LYS A N   1 
ATOM   1195 C CA  . LYS A 1 155 ? -14.238 7.446   -0.520  1.00 22.36  ? 152 LYS A CA  1 
ATOM   1196 C C   . LYS A 1 155 ? -15.302 8.337   -1.139  1.00 32.78  ? 152 LYS A C   1 
ATOM   1197 O O   . LYS A 1 155 ? -16.439 7.885   -1.294  1.00 42.95  ? 152 LYS A O   1 
ATOM   1198 C CB  . LYS A 1 155 ? -14.747 6.961   0.840   1.00 27.25  ? 152 LYS A CB  1 
ATOM   1199 C CG  . LYS A 1 155 ? -13.739 6.185   1.660   1.00 30.71  ? 152 LYS A CG  1 
ATOM   1200 C CD  . LYS A 1 155 ? -14.262 5.874   3.060   1.00 27.96  ? 152 LYS A CD  1 
ATOM   1201 C CE  . LYS A 1 155 ? -13.202 5.097   3.886   1.00 34.97  ? 152 LYS A CE  1 
ATOM   1202 N NZ  . LYS A 1 155 ? -12.654 3.863   3.209   1.00 30.71  ? 152 LYS A NZ  1 
ATOM   1203 N N   . PHE A 1 156 ? -14.997 9.591   -1.466  1.00 32.45  ? 153 PHE A N   1 
ATOM   1204 C CA  . PHE A 1 156 ? -16.021 10.429  -2.081  1.00 30.29  ? 153 PHE A CA  1 
ATOM   1205 C C   . PHE A 1 156 ? -15.425 11.367  -3.119  1.00 28.94  ? 153 PHE A C   1 
ATOM   1206 O O   . PHE A 1 156 ? -15.716 11.249  -4.307  1.00 31.06  ? 153 PHE A O   1 
ATOM   1207 C CB  . PHE A 1 156 ? -16.787 11.238  -1.035  1.00 28.17  ? 153 PHE A CB  1 
ATOM   1208 C CG  . PHE A 1 156 ? -17.586 12.366  -1.627  1.00 28.23  ? 153 PHE A CG  1 
ATOM   1209 C CD1 . PHE A 1 156 ? -18.627 12.114  -2.494  1.00 28.87  ? 153 PHE A CD1 1 
ATOM   1210 C CD2 . PHE A 1 156 ? -17.273 13.679  -1.343  1.00 25.70  ? 153 PHE A CD2 1 
ATOM   1211 C CE1 . PHE A 1 156 ? -19.344 13.154  -3.061  1.00 28.25  ? 153 PHE A CE1 1 
ATOM   1212 C CE2 . PHE A 1 156 ? -17.995 14.715  -1.893  1.00 29.01  ? 153 PHE A CE2 1 
ATOM   1213 C CZ  . PHE A 1 156 ? -19.039 14.452  -2.751  1.00 28.41  ? 153 PHE A CZ  1 
ATOM   1214 N N   . MET A 1 157 ? -14.598 12.306  -2.694  1.00 31.36  ? 154 MET A N   1 
ATOM   1215 C CA  . MET A 1 157 ? -13.981 13.207  -3.650  1.00 31.26  ? 154 MET A CA  1 
ATOM   1216 C C   . MET A 1 157 ? -12.973 12.479  -4.530  1.00 29.74  ? 154 MET A C   1 
ATOM   1217 O O   . MET A 1 157 ? -12.184 11.653  -4.073  1.00 37.10  ? 154 MET A O   1 
ATOM   1218 C CB  . MET A 1 157 ? -13.321 14.370  -2.922  1.00 32.69  ? 154 MET A CB  1 
ATOM   1219 C CG  . MET A 1 157 ? -14.056 15.659  -3.215  1.00 33.89  ? 154 MET A CG  1 
ATOM   1220 S SD  . MET A 1 157 ? -13.421 17.081  -2.340  1.00 43.97  ? 154 MET A SD  1 
ATOM   1221 C CE  . MET A 1 157 ? -14.881 18.125  -2.351  1.00 29.91  ? 154 MET A CE  1 
ATOM   1222 N N   . GLN A 1 158 ? -13.005 12.780  -5.810  1.00 33.06  ? 155 GLN A N   1 
ATOM   1223 C CA  . GLN A 1 158 ? -12.098 12.154  -6.766  1.00 35.88  ? 155 GLN A CA  1 
ATOM   1224 C C   . GLN A 1 158 ? -11.350 13.277  -7.470  1.00 33.34  ? 155 GLN A C   1 
ATOM   1225 O O   . GLN A 1 158 ? -11.711 13.667  -8.579  1.00 33.54  ? 155 GLN A O   1 
ATOM   1226 C CB  . GLN A 1 158 ? -12.860 11.288  -7.735  1.00 34.33  ? 155 GLN A CB  1 
ATOM   1227 C CG  . GLN A 1 158 ? -13.765 10.263  -7.059  1.00 39.26  ? 155 GLN A CG  1 
ATOM   1228 C CD  . GLN A 1 158 ? -14.604 9.444   -8.048  1.00 53.92  ? 155 GLN A CD  1 
ATOM   1229 O OE1 . GLN A 1 158 ? -14.486 8.214   -8.091  1.00 60.19  ? 155 GLN A OE1 1 
ATOM   1230 N NE2 . GLN A 1 158 ? -15.463 10.122  -8.836  1.00 40.72  ? 155 GLN A NE2 1 
ATOM   1231 N N   . VAL A 1 159 ? -10.327 13.816  -6.807  1.00 32.24  ? 156 VAL A N   1 
ATOM   1232 C CA  . VAL A 1 159 ? -9.586  14.926  -7.385  1.00 31.60  ? 156 VAL A CA  1 
ATOM   1233 C C   . VAL A 1 159 ? -8.693  14.412  -8.500  1.00 33.67  ? 156 VAL A C   1 
ATOM   1234 O O   . VAL A 1 159 ? -7.933  13.452  -8.317  1.00 38.88  ? 156 VAL A O   1 
ATOM   1235 C CB  . VAL A 1 159 ? -8.765  15.650  -6.313  1.00 29.30  ? 156 VAL A CB  1 
ATOM   1236 C CG1 . VAL A 1 159 ? -7.913  16.732  -6.964  1.00 26.84  ? 156 VAL A CG1 1 
ATOM   1237 C CG2 . VAL A 1 159 ? -9.687  16.259  -5.290  1.00 28.31  ? 156 VAL A CG2 1 
ATOM   1238 N N   . ARG A 1 160 ? -8.774  15.059  -9.653  1.00 27.79  ? 157 ARG A N   1 
ATOM   1239 C CA  . ARG A 1 160 ? -8.071  14.782  -10.891 1.00 31.57  ? 157 ARG A CA  1 
ATOM   1240 C C   . ARG A 1 160 ? -7.026  15.870  -11.191 1.00 33.99  ? 157 ARG A C   1 
ATOM   1241 O O   . ARG A 1 160 ? -7.218  17.039  -10.836 1.00 35.62  ? 157 ARG A O   1 
ATOM   1242 C CB  . ARG A 1 160 ? -9.074  14.714  -12.053 1.00 34.42  ? 157 ARG A CB  1 
ATOM   1243 C CG  . ARG A 1 160 ? -10.197 13.700  -11.920 1.00 32.43  ? 157 ARG A CG  1 
ATOM   1244 C CD  . ARG A 1 160 ? -9.643  12.302  -11.747 1.00 40.56  ? 157 ARG A CD  1 
ATOM   1245 N NE  . ARG A 1 160 ? -8.524  12.048  -12.648 1.00 39.80  ? 157 ARG A NE  1 
ATOM   1246 C CZ  . ARG A 1 160 ? -7.482  11.272  -12.357 1.00 49.26  ? 157 ARG A CZ  1 
ATOM   1247 N NH1 . ARG A 1 160 ? -7.396  10.623  -11.196 1.00 44.30  ? 157 ARG A NH1 1 
ATOM   1248 N NH2 . ARG A 1 160 ? -6.490  11.157  -13.243 1.00 44.17  ? 157 ARG A NH2 1 
ATOM   1249 N N   . PRO A 1 161 ? -5.925  15.546  -11.872 1.00 32.05  ? 158 PRO A N   1 
ATOM   1250 C CA  . PRO A 1 161 ? -4.943  16.595  -12.186 1.00 29.21  ? 158 PRO A CA  1 
ATOM   1251 C C   . PRO A 1 161 ? -5.577  17.668  -13.059 1.00 31.38  ? 158 PRO A C   1 
ATOM   1252 O O   . PRO A 1 161 ? -6.305  17.371  -14.007 1.00 31.51  ? 158 PRO A O   1 
ATOM   1253 C CB  . PRO A 1 161 ? -3.832  15.847  -12.927 1.00 26.87  ? 158 PRO A CB  1 
ATOM   1254 C CG  . PRO A 1 161 ? -4.100  14.400  -12.701 1.00 31.41  ? 158 PRO A CG  1 
ATOM   1255 C CD  . PRO A 1 161 ? -5.561  14.244  -12.454 1.00 29.30  ? 158 PRO A CD  1 
ATOM   1256 N N   . GLY A 1 162 ? -5.319  18.930  -12.709 1.00 30.90  ? 159 GLY A N   1 
ATOM   1257 C CA  . GLY A 1 162 ? -5.912  20.064  -13.386 1.00 29.51  ? 159 GLY A CA  1 
ATOM   1258 C C   . GLY A 1 162 ? -7.075  20.708  -12.656 1.00 35.67  ? 159 GLY A C   1 
ATOM   1259 O O   . GLY A 1 162 ? -7.367  21.891  -12.900 1.00 34.76  ? 159 GLY A O   1 
ATOM   1260 N N   . ASP A 1 163 ? -7.721  19.976  -11.744 1.00 34.94  ? 160 ASP A N   1 
ATOM   1261 C CA  . ASP A 1 163 ? -8.875  20.501  -11.029 1.00 29.94  ? 160 ASP A CA  1 
ATOM   1262 C C   . ASP A 1 163 ? -8.497  21.705  -10.171 1.00 30.75  ? 160 ASP A C   1 
ATOM   1263 O O   . ASP A 1 163 ? -7.390  21.793  -9.630  1.00 30.70  ? 160 ASP A O   1 
ATOM   1264 C CB  . ASP A 1 163 ? -9.481  19.414  -10.146 1.00 31.57  ? 160 ASP A CB  1 
ATOM   1265 C CG  . ASP A 1 163 ? -10.233 18.376  -10.937 1.00 35.85  ? 160 ASP A CG  1 
ATOM   1266 O OD1 . ASP A 1 163 ? -10.298 18.502  -12.180 1.00 42.99  ? 160 ASP A OD1 1 
ATOM   1267 O OD2 . ASP A 1 163 ? -10.759 17.429  -10.312 1.00 34.04  ? 160 ASP A OD2 1 
ATOM   1268 N N   . THR A 1 164 ? -9.432  22.641  -10.043 1.00 26.50  ? 161 THR A N   1 
ATOM   1269 C CA  . THR A 1 164 ? -9.353  23.639  -8.985  1.00 29.72  ? 161 THR A CA  1 
ATOM   1270 C C   . THR A 1 164 ? -10.182 23.170  -7.789  1.00 31.75  ? 161 THR A C   1 
ATOM   1271 O O   . THR A 1 164 ? -11.356 22.808  -7.941  1.00 32.74  ? 161 THR A O   1 
ATOM   1272 C CB  . THR A 1 164 ? -9.835  25.000  -9.474  1.00 31.02  ? 161 THR A CB  1 
ATOM   1273 O OG1 . THR A 1 164 ? -8.985  25.467  -10.543 1.00 31.64  ? 161 THR A OG1 1 
ATOM   1274 C CG2 . THR A 1 164 ? -9.790  26.001  -8.333  1.00 32.27  ? 161 THR A CG2 1 
ATOM   1275 N N   . VAL A 1 165 ? -9.552  23.127  -6.612  1.00 28.37  ? 162 VAL A N   1 
ATOM   1276 C CA  . VAL A 1 165 ? -10.178 22.686  -5.368  1.00 26.21  ? 162 VAL A CA  1 
ATOM   1277 C C   . VAL A 1 165 ? -10.228 23.866  -4.412  1.00 30.08  ? 162 VAL A C   1 
ATOM   1278 O O   . VAL A 1 165 ? -9.204  24.510  -4.169  1.00 33.89  ? 162 VAL A O   1 
ATOM   1279 C CB  . VAL A 1 165 ? -9.410  21.527  -4.705  1.00 23.82  ? 162 VAL A CB  1 
ATOM   1280 C CG1 . VAL A 1 165 ? -9.944  21.309  -3.321  1.00 21.91  ? 162 VAL A CG1 1 
ATOM   1281 C CG2 . VAL A 1 165 ? -9.532  20.248  -5.499  1.00 23.50  ? 162 VAL A CG2 1 
ATOM   1282 N N   . VAL A 1 166 ? -11.398 24.134  -3.848  1.00 30.51  ? 163 VAL A N   1 
ATOM   1283 C CA  . VAL A 1 166 ? -11.568 25.201  -2.873  1.00 29.87  ? 163 VAL A CA  1 
ATOM   1284 C C   . VAL A 1 166 ? -11.752 24.550  -1.514  1.00 30.46  ? 163 VAL A C   1 
ATOM   1285 O O   . VAL A 1 166 ? -12.555 23.621  -1.380  1.00 29.03  ? 163 VAL A O   1 
ATOM   1286 C CB  . VAL A 1 166 ? -12.759 26.111  -3.234  1.00 29.48  ? 163 VAL A CB  1 
ATOM   1287 C CG1 . VAL A 1 166 ? -13.161 26.993  -2.048  1.00 24.35  ? 163 VAL A CG1 1 
ATOM   1288 C CG2 . VAL A 1 166 ? -12.418 26.986  -4.444  1.00 27.76  ? 163 VAL A CG2 1 
ATOM   1289 N N   . VAL A 1 167 ? -10.997 25.020  -0.518  1.00 28.01  ? 164 VAL A N   1 
ATOM   1290 C CA  . VAL A 1 167 ? -11.112 24.574  0.871   1.00 29.24  ? 164 VAL A CA  1 
ATOM   1291 C C   . VAL A 1 167 ? -11.390 25.794  1.730   1.00 33.80  ? 164 VAL A C   1 
ATOM   1292 O O   . VAL A 1 167 ? -10.523 26.665  1.877   1.00 34.52  ? 164 VAL A O   1 
ATOM   1293 C CB  . VAL A 1 167 ? -9.853  23.854  1.374   1.00 32.96  ? 164 VAL A CB  1 
ATOM   1294 C CG1 . VAL A 1 167 ? -10.029 23.450  2.843   1.00 32.75  ? 164 VAL A CG1 1 
ATOM   1295 C CG2 . VAL A 1 167 ? -9.555  22.646  0.514   1.00 27.43  ? 164 VAL A CG2 1 
ATOM   1296 N N   . SER A 1 168 ? -12.590 25.852  2.307   1.00 34.11  ? 165 SER A N   1 
ATOM   1297 C CA  . SER A 1 168 ? -12.952 26.892  3.253   1.00 32.96  ? 165 SER A CA  1 
ATOM   1298 C C   . SER A 1 168 ? -12.553 26.451  4.657   1.00 39.84  ? 165 SER A C   1 
ATOM   1299 O O   . SER A 1 168 ? -12.681 25.276  5.008   1.00 40.31  ? 165 SER A O   1 
ATOM   1300 C CB  . SER A 1 168 ? -14.450 27.165  3.186   1.00 30.79  ? 165 SER A CB  1 
ATOM   1301 O OG  . SER A 1 168 ? -15.177 26.050  3.649   1.00 31.31  ? 165 SER A OG  1 
ATOM   1302 N N   . GLY A 1 169 ? -12.071 27.390  5.463   1.00 43.40  ? 166 GLY A N   1 
ATOM   1303 C CA  . GLY A 1 169 ? -11.600 26.981  6.774   1.00 42.10  ? 166 GLY A CA  1 
ATOM   1304 C C   . GLY A 1 169 ? -10.334 26.167  6.655   1.00 42.45  ? 166 GLY A C   1 
ATOM   1305 O O   . GLY A 1 169 ? -10.151 25.177  7.382   1.00 39.08  ? 166 GLY A O   1 
ATOM   1306 N N   . ALA A 1 170 ? -9.449  26.570  5.747   1.00 39.23  ? 167 ALA A N   1 
ATOM   1307 C CA  . ALA A 1 170 ? -8.306  25.750  5.400   1.00 35.89  ? 167 ALA A CA  1 
ATOM   1308 C C   . ALA A 1 170 ? -7.234  25.716  6.481   1.00 42.77  ? 167 ALA A C   1 
ATOM   1309 O O   . ALA A 1 170 ? -6.389  24.819  6.454   1.00 46.07  ? 167 ALA A O   1 
ATOM   1310 C CB  . ALA A 1 170 ? -7.697  26.248  4.101   1.00 34.09  ? 167 ALA A CB  1 
ATOM   1311 N N   . SER A 1 171 ? -7.236  26.650  7.431   1.00 42.19  ? 168 SER A N   1 
ATOM   1312 C CA  . SER A 1 171 ? -6.075  26.758  8.312   1.00 40.85  ? 168 SER A CA  1 
ATOM   1313 C C   . SER A 1 171 ? -6.004  25.605  9.315   1.00 42.86  ? 168 SER A C   1 
ATOM   1314 O O   . SER A 1 171 ? -4.909  25.241  9.768   1.00 40.75  ? 168 SER A O   1 
ATOM   1315 C CB  . SER A 1 171 ? -6.106  28.113  9.010   1.00 44.78  ? 168 SER A CB  1 
ATOM   1316 O OG  . SER A 1 171 ? -7.432  28.615  8.960   1.00 60.55  ? 168 SER A OG  1 
ATOM   1317 N N   . GLY A 1 172 ? -7.145  24.998  9.640   1.00 40.42  ? 169 GLY A N   1 
ATOM   1318 C CA  . GLY A 1 172 ? -7.191  23.898  10.573  1.00 37.26  ? 169 GLY A CA  1 
ATOM   1319 C C   . GLY A 1 172 ? -6.633  22.608  10.001  1.00 43.50  ? 169 GLY A C   1 
ATOM   1320 O O   . GLY A 1 172 ? -6.262  22.500  8.827   1.00 38.87  ? 169 GLY A O   1 
ATOM   1321 N N   . MET A 1 173 ? -6.583  21.595  10.870  1.00 38.34  ? 170 MET A N   1 
ATOM   1322 C CA  . MET A 1 173 ? -5.905  20.361  10.499  1.00 39.53  ? 170 MET A CA  1 
ATOM   1323 C C   . MET A 1 173 ? -6.598  19.697  9.322   1.00 33.80  ? 170 MET A C   1 
ATOM   1324 O O   . MET A 1 173 ? -5.946  19.295  8.350   1.00 30.83  ? 170 MET A O   1 
ATOM   1325 C CB  . MET A 1 173 ? -5.825  19.386  11.681  1.00 36.20  ? 170 MET A CB  1 
ATOM   1326 C CG  . MET A 1 173 ? -5.453  18.000  11.190  1.00 36.50  ? 170 MET A CG  1 
ATOM   1327 S SD  . MET A 1 173 ? -4.687  16.877  12.339  1.00 42.78  ? 170 MET A SD  1 
ATOM   1328 C CE  . MET A 1 173 ? -3.115  17.667  12.699  1.00 36.35  ? 170 MET A CE  1 
ATOM   1329 N N   . ILE A 1 174 ? -7.924  19.569  9.403   1.00 30.65  ? 171 ILE A N   1 
ATOM   1330 C CA  . ILE A 1 174 ? -8.676  18.900  8.348   1.00 35.98  ? 171 ILE A CA  1 
ATOM   1331 C C   . ILE A 1 174 ? -8.502  19.650  7.033   1.00 34.65  ? 171 ILE A C   1 
ATOM   1332 O O   . ILE A 1 174 ? -8.208  19.049  5.985   1.00 31.59  ? 171 ILE A O   1 
ATOM   1333 C CB  . ILE A 1 174 ? -10.161 18.779  8.734   1.00 33.26  ? 171 ILE A CB  1 
ATOM   1334 C CG1 . ILE A 1 174 ? -10.346 17.892  9.952   1.00 31.20  ? 171 ILE A CG1 1 
ATOM   1335 C CG2 . ILE A 1 174 ? -10.960 18.178  7.610   1.00 29.00  ? 171 ILE A CG2 1 
ATOM   1336 C CD1 . ILE A 1 174 ? -11.805 17.646  10.255  1.00 32.68  ? 171 ILE A CD1 1 
ATOM   1337 N N   . GLY A 1 175 ? -8.659  20.978  7.082   1.00 30.05  ? 172 GLY A N   1 
ATOM   1338 C CA  . GLY A 1 175 ? -8.493  21.789  5.886   1.00 35.16  ? 172 GLY A CA  1 
ATOM   1339 C C   . GLY A 1 175 ? -7.121  21.646  5.253   1.00 35.30  ? 172 GLY A C   1 
ATOM   1340 O O   . GLY A 1 175 ? -7.005  21.489  4.031   1.00 30.45  ? 172 GLY A O   1 
ATOM   1341 N N   . THR A 1 176 ? -6.055  21.698  6.072   1.00 34.90  ? 173 THR A N   1 
ATOM   1342 C CA  . THR A 1 176 ? -4.719  21.595  5.491   1.00 33.54  ? 173 THR A CA  1 
ATOM   1343 C C   . THR A 1 176 ? -4.459  20.200  4.955   1.00 33.87  ? 173 THR A C   1 
ATOM   1344 O O   . THR A 1 176 ? -3.727  20.050  3.968   1.00 32.68  ? 173 THR A O   1 
ATOM   1345 C CB  . THR A 1 176 ? -3.616  21.947  6.489   1.00 36.14  ? 173 THR A CB  1 
ATOM   1346 O OG1 . THR A 1 176 ? -3.492  20.891  7.443   1.00 41.13  ? 173 THR A OG1 1 
ATOM   1347 C CG2 . THR A 1 176 ? -3.892  23.267  7.189   1.00 36.95  ? 173 THR A CG2 1 
ATOM   1348 N N   . LEU A 1 177 ? -5.024  19.170  5.591   1.00 30.79  ? 174 LEU A N   1 
ATOM   1349 C CA  . LEU A 1 177 ? -4.843  17.820  5.067   1.00 31.05  ? 174 LEU A CA  1 
ATOM   1350 C C   . LEU A 1 177 ? -5.574  17.657  3.735   1.00 32.81  ? 174 LEU A C   1 
ATOM   1351 O O   . LEU A 1 177 ? -5.027  17.089  2.782   1.00 29.12  ? 174 LEU A O   1 
ATOM   1352 C CB  . LEU A 1 177 ? -5.320  16.781  6.085   1.00 28.52  ? 174 LEU A CB  1 
ATOM   1353 C CG  . LEU A 1 177 ? -4.551  16.605  7.400   1.00 31.30  ? 174 LEU A CG  1 
ATOM   1354 C CD1 . LEU A 1 177 ? -5.325  15.726  8.372   1.00 32.10  ? 174 LEU A CD1 1 
ATOM   1355 C CD2 . LEU A 1 177 ? -3.194  16.011  7.166   1.00 27.03  ? 174 LEU A CD2 1 
ATOM   1356 N N   . VAL A 1 178 ? -6.810  18.155  3.646   1.00 27.45  ? 175 VAL A N   1 
ATOM   1357 C CA  . VAL A 1 178 ? -7.521  18.077  2.376   1.00 30.50  ? 175 VAL A CA  1 
ATOM   1358 C C   . VAL A 1 178 ? -6.742  18.806  1.289   1.00 31.03  ? 175 VAL A C   1 
ATOM   1359 O O   . VAL A 1 178 ? -6.598  18.312  0.163   1.00 28.74  ? 175 VAL A O   1 
ATOM   1360 C CB  . VAL A 1 178 ? -8.947  18.643  2.505   1.00 31.54  ? 175 VAL A CB  1 
ATOM   1361 C CG1 . VAL A 1 178 ? -9.572  18.747  1.122   1.00 27.09  ? 175 VAL A CG1 1 
ATOM   1362 C CG2 . VAL A 1 178 ? -9.803  17.767  3.410   1.00 30.42  ? 175 VAL A CG2 1 
ATOM   1363 N N   . GLY A 1 179 ? -6.228  19.992  1.606   1.00 28.87  ? 176 GLY A N   1 
ATOM   1364 C CA  . GLY A 1 179 ? -5.509  20.755  0.605   1.00 27.71  ? 176 GLY A CA  1 
ATOM   1365 C C   . GLY A 1 179 ? -4.278  20.029  0.110   1.00 30.02  ? 176 GLY A C   1 
ATOM   1366 O O   . GLY A 1 179 ? -4.024  19.956  -1.094  1.00 30.26  ? 176 GLY A O   1 
ATOM   1367 N N   . GLN A 1 180 ? -3.505  19.467  1.038   1.00 29.94  ? 177 GLN A N   1 
ATOM   1368 C CA  . GLN A 1 180 ? -2.263  18.809  0.668   1.00 26.36  ? 177 GLN A CA  1 
ATOM   1369 C C   . GLN A 1 180 ? -2.538  17.536  -0.105  1.00 27.49  ? 177 GLN A C   1 
ATOM   1370 O O   . GLN A 1 180 ? -1.781  17.174  -1.012  1.00 30.27  ? 177 GLN A O   1 
ATOM   1371 C CB  . GLN A 1 180 ? -1.431  18.515  1.915   1.00 27.17  ? 177 GLN A CB  1 
ATOM   1372 C CG  . GLN A 1 180 ? -0.951  19.761  2.628   1.00 29.87  ? 177 GLN A CG  1 
ATOM   1373 C CD  . GLN A 1 180 ? -0.344  19.442  3.971   1.00 34.78  ? 177 GLN A CD  1 
ATOM   1374 O OE1 . GLN A 1 180 ? 0.801   19.010  4.050   1.00 32.48  ? 177 GLN A OE1 1 
ATOM   1375 N NE2 . GLN A 1 180 ? -1.119  19.626  5.039   1.00 33.28  ? 177 GLN A NE2 1 
ATOM   1376 N N   . MET A 1 181 ? -3.601  16.829  0.256   1.00 27.88  ? 178 MET A N   1 
ATOM   1377 C CA  . MET A 1 181 ? -3.975  15.656  -0.516  1.00 29.03  ? 178 MET A CA  1 
ATOM   1378 C C   . MET A 1 181 ? -4.420  16.061  -1.912  1.00 26.02  ? 178 MET A C   1 
ATOM   1379 O O   . MET A 1 181 ? -4.075  15.399  -2.889  1.00 27.24  ? 178 MET A O   1 
ATOM   1380 C CB  . MET A 1 181 ? -5.081  14.874  0.206   1.00 25.09  ? 178 MET A CB  1 
ATOM   1381 C CG  . MET A 1 181 ? -4.592  14.099  1.409   1.00 28.58  ? 178 MET A CG  1 
ATOM   1382 S SD  . MET A 1 181 ? -5.834  13.296  2.438   1.00 33.55  ? 178 MET A SD  1 
ATOM   1383 C CE  . MET A 1 181 ? -6.063  11.777  1.511   1.00 41.15  ? 178 MET A CE  1 
ATOM   1384 N N   . ALA A 1 182 ? -5.187  17.147  -2.015  1.00 21.55  ? 179 ALA A N   1 
ATOM   1385 C CA  . ALA A 1 182 ? -5.668  17.592  -3.310  1.00 26.96  ? 179 ALA A CA  1 
ATOM   1386 C C   . ALA A 1 182 ? -4.500  17.971  -4.211  1.00 29.78  ? 179 ALA A C   1 
ATOM   1387 O O   . ALA A 1 182 ? -4.438  17.574  -5.384  1.00 27.90  ? 179 ALA A O   1 
ATOM   1388 C CB  . ALA A 1 182 ? -6.630  18.773  -3.132  1.00 23.46  ? 179 ALA A CB  1 
ATOM   1389 N N   . LYS A 1 183 ? -3.567  18.745  -3.667  1.00 27.88  ? 180 LYS A N   1 
ATOM   1390 C CA  . LYS A 1 183 ? -2.347  19.104  -4.378  1.00 30.15  ? 180 LYS A CA  1 
ATOM   1391 C C   . LYS A 1 183 ? -1.603  17.863  -4.867  1.00 33.09  ? 180 LYS A C   1 
ATOM   1392 O O   . LYS A 1 183 ? -1.165  17.808  -6.024  1.00 35.47  ? 180 LYS A O   1 
ATOM   1393 C CB  . LYS A 1 183 ? -1.482  19.976  -3.457  1.00 27.64  ? 180 LYS A CB  1 
ATOM   1394 C CG  . LYS A 1 183 ? -0.049  20.174  -3.871  1.00 33.99  ? 180 LYS A CG  1 
ATOM   1395 C CD  . LYS A 1 183 ? 0.133   21.268  -4.905  1.00 42.02  ? 180 LYS A CD  1 
ATOM   1396 C CE  . LYS A 1 183 ? -0.936  22.346  -4.807  1.00 44.32  ? 180 LYS A CE  1 
ATOM   1397 N NZ  . LYS A 1 183 ? -0.902  23.196  -6.033  1.00 42.69  ? 180 LYS A NZ  1 
ATOM   1398 N N   . ARG A 1 184 ? -1.487  16.834  -4.018  1.00 30.09  ? 181 ARG A N   1 
ATOM   1399 C CA  . ARG A 1 184 ? -0.862  15.586  -4.454  1.00 29.29  ? 181 ARG A CA  1 
ATOM   1400 C C   . ARG A 1 184 ? -1.630  14.962  -5.609  1.00 35.44  ? 181 ARG A C   1 
ATOM   1401 O O   . ARG A 1 184 ? -1.037  14.348  -6.502  1.00 34.68  ? 181 ARG A O   1 
ATOM   1402 C CB  . ARG A 1 184 ? -0.774  14.593  -3.298  1.00 29.51  ? 181 ARG A CB  1 
ATOM   1403 C CG  . ARG A 1 184 ? 0.402   14.836  -2.373  1.00 39.55  ? 181 ARG A CG  1 
ATOM   1404 C CD  . ARG A 1 184 ? 0.464   13.792  -1.276  1.00 37.22  ? 181 ARG A CD  1 
ATOM   1405 N NE  . ARG A 1 184 ? 0.158   12.444  -1.749  1.00 34.14  ? 181 ARG A NE  1 
ATOM   1406 C CZ  . ARG A 1 184 ? 1.065   11.581  -2.180  1.00 37.50  ? 181 ARG A CZ  1 
ATOM   1407 N NH1 . ARG A 1 184 ? 2.347   11.915  -2.276  1.00 38.21  ? 181 ARG A NH1 1 
ATOM   1408 N NH2 . ARG A 1 184 ? 0.679   10.355  -2.521  1.00 36.69  ? 181 ARG A NH2 1 
ATOM   1409 N N   . ALA A 1 185 ? -2.955  15.079  -5.591  1.00 29.73  ? 182 ALA A N   1 
ATOM   1410 C CA  . ALA A 1 185 ? -3.742  14.534  -6.672  1.00 27.67  ? 182 ALA A CA  1 
ATOM   1411 C C   . ALA A 1 185 ? -3.703  15.425  -7.904  1.00 34.77  ? 182 ALA A C   1 
ATOM   1412 O O   . ALA A 1 185 ? -4.362  15.095  -8.896  1.00 29.99  ? 182 ALA A O   1 
ATOM   1413 C CB  . ALA A 1 185 ? -5.177  14.325  -6.216  1.00 24.57  ? 182 ALA A CB  1 
ATOM   1414 N N   . GLY A 1 186 ? -2.992  16.556  -7.842  1.00 29.55  ? 183 GLY A N   1 
ATOM   1415 C CA  . GLY A 1 186 ? -2.709  17.354  -9.014  1.00 30.45  ? 183 GLY A CA  1 
ATOM   1416 C C   . GLY A 1 186 ? -3.493  18.636  -9.180  1.00 31.24  ? 183 GLY A C   1 
ATOM   1417 O O   . GLY A 1 186 ? -3.483  19.206  -10.280 1.00 35.04  ? 183 GLY A O   1 
ATOM   1418 N N   . ALA A 1 187 ? -4.141  19.122  -8.133  1.00 27.59  ? 184 ALA A N   1 
ATOM   1419 C CA  . ALA A 1 187 ? -5.110  20.192  -8.264  1.00 25.58  ? 184 ALA A CA  1 
ATOM   1420 C C   . ALA A 1 187 ? -4.492  21.552  -7.982  1.00 30.00  ? 184 ALA A C   1 
ATOM   1421 O O   . ALA A 1 187 ? -3.522  21.677  -7.230  1.00 35.84  ? 184 ALA A O   1 
ATOM   1422 C CB  . ALA A 1 187 ? -6.281  19.957  -7.310  1.00 25.60  ? 184 ALA A CB  1 
ATOM   1423 N N   . ARG A 1 188 ? -5.074  22.583  -8.588  1.00 28.63  ? 185 ARG A N   1 
ATOM   1424 C CA  . ARG A 1 188 ? -4.952  23.910  -8.016  1.00 28.88  ? 185 ARG A CA  1 
ATOM   1425 C C   . ARG A 1 188 ? -5.774  23.950  -6.728  1.00 27.39  ? 185 ARG A C   1 
ATOM   1426 O O   . ARG A 1 188 ? -6.921  23.501  -6.685  1.00 28.11  ? 185 ARG A O   1 
ATOM   1427 C CB  . ARG A 1 188 ? -5.413  24.980  -9.006  1.00 24.27  ? 185 ARG A CB  1 
ATOM   1428 C CG  . ARG A 1 188 ? -5.263  26.407  -8.482  1.00 27.00  ? 185 ARG A CG  1 
ATOM   1429 C CD  . ARG A 1 188 ? -5.670  27.439  -9.526  1.00 30.99  ? 185 ARG A CD  1 
ATOM   1430 N NE  . ARG A 1 188 ? -5.656  28.817  -9.029  1.00 31.25  ? 185 ARG A NE  1 
ATOM   1431 C CZ  . ARG A 1 188 ? -4.561  29.532  -8.788  1.00 31.23  ? 185 ARG A CZ  1 
ATOM   1432 N NH1 . ARG A 1 188 ? -3.354  29.008  -8.908  1.00 39.48  ? 185 ARG A NH1 1 
ATOM   1433 N NH2 . ARG A 1 188 ? -4.681  30.803  -8.406  1.00 29.08  ? 185 ARG A NH2 1 
ATOM   1434 N N   . VAL A 1 189 ? -5.177  24.468  -5.674  1.00 24.39  ? 186 VAL A N   1 
ATOM   1435 C CA  . VAL A 1 189 ? -5.784  24.492  -4.358  1.00 29.53  ? 186 VAL A CA  1 
ATOM   1436 C C   . VAL A 1 189 ? -5.897  25.941  -3.914  1.00 29.83  ? 186 VAL A C   1 
ATOM   1437 O O   . VAL A 1 189 ? -4.884  26.640  -3.803  1.00 34.50  ? 186 VAL A O   1 
ATOM   1438 C CB  . VAL A 1 189 ? -4.958  23.678  -3.349  1.00 33.05  ? 186 VAL A CB  1 
ATOM   1439 C CG1 . VAL A 1 189 ? -5.599  23.721  -1.993  1.00 25.95  ? 186 VAL A CG1 1 
ATOM   1440 C CG2 . VAL A 1 189 ? -4.746  22.247  -3.855  1.00 29.94  ? 186 VAL A CG2 1 
ATOM   1441 N N   . VAL A 1 190 ? -7.124  26.383  -3.655  1.00 28.66  ? 187 VAL A N   1 
ATOM   1442 C CA  . VAL A 1 190 ? -7.433  27.704  -3.120  1.00 28.39  ? 187 VAL A CA  1 
ATOM   1443 C C   . VAL A 1 190 ? -8.012  27.508  -1.726  1.00 33.60  ? 187 VAL A C   1 
ATOM   1444 O O   . VAL A 1 190 ? -8.898  26.666  -1.537  1.00 32.50  ? 187 VAL A O   1 
ATOM   1445 C CB  . VAL A 1 190 ? -8.439  28.435  -4.024  1.00 27.33  ? 187 VAL A CB  1 
ATOM   1446 C CG1 . VAL A 1 190 ? -8.754  29.828  -3.502  1.00 30.72  ? 187 VAL A CG1 1 
ATOM   1447 C CG2 . VAL A 1 190 ? -7.919  28.481  -5.439  1.00 33.32  ? 187 VAL A CG2 1 
ATOM   1448 N N   . GLY A 1 191 ? -7.533  28.286  -0.754  1.00 31.68  ? 188 GLY A N   1 
ATOM   1449 C CA  . GLY A 1 191 ? -8.057  28.220  0.590   1.00 34.95  ? 188 GLY A CA  1 
ATOM   1450 C C   . GLY A 1 191 ? -8.472  29.588  1.112   1.00 42.80  ? 188 GLY A C   1 
ATOM   1451 O O   . GLY A 1 191 ? -8.116  30.633  0.555   1.00 39.81  ? 188 GLY A O   1 
ATOM   1452 N N   . THR A 1 192 ? -9.230  29.558  2.212   1.00 42.15  ? 189 THR A N   1 
ATOM   1453 C CA  . THR A 1 192 ? -9.530  30.730  3.027   1.00 42.82  ? 189 THR A CA  1 
ATOM   1454 C C   . THR A 1 192 ? -8.834  30.633  4.384   1.00 50.08  ? 189 THR A C   1 
ATOM   1455 O O   . THR A 1 192 ? -8.990  29.635  5.098   1.00 56.62  ? 189 THR A O   1 
ATOM   1456 C CB  . THR A 1 192 ? -11.027 30.865  3.246   1.00 39.89  ? 189 THR A CB  1 
ATOM   1457 O OG1 . THR A 1 192 ? -11.453 29.875  4.190   1.00 47.07  ? 189 THR A OG1 1 
ATOM   1458 C CG2 . THR A 1 192 ? -11.730 30.639  1.957   1.00 40.59  ? 189 THR A CG2 1 
ATOM   1459 N N   . ALA A 1 193 ? -8.080  31.672  4.741   1.00 44.18  ? 190 ALA A N   1 
ATOM   1460 C CA  . ALA A 1 193 ? -7.474  31.820  6.057   1.00 52.50  ? 190 ALA A CA  1 
ATOM   1461 C C   . ALA A 1 193 ? -7.893  33.170  6.638   1.00 60.26  ? 190 ALA A C   1 
ATOM   1462 O O   . ALA A 1 193 ? -8.636  33.931  6.018   1.00 56.34  ? 190 ALA A O   1 
ATOM   1463 C CB  . ALA A 1 193 ? -5.945  31.691  5.999   1.00 47.43  ? 190 ALA A CB  1 
ATOM   1464 N N   . GLY A 1 194 ? -7.394  33.483  7.832   1.00 64.06  ? 191 GLY A N   1 
ATOM   1465 C CA  . GLY A 1 194 ? -7.877  34.636  8.565   1.00 61.95  ? 191 GLY A CA  1 
ATOM   1466 C C   . GLY A 1 194 ? -6.864  35.730  8.852   1.00 60.23  ? 191 GLY A C   1 
ATOM   1467 O O   . GLY A 1 194 ? -7.178  36.654  9.602   1.00 63.13  ? 191 GLY A O   1 
ATOM   1468 N N   . SER A 1 195 ? -5.654  35.638  8.306   1.00 54.89  ? 192 SER A N   1 
ATOM   1469 C CA  . SER A 1 195 ? -4.665  36.705  8.434   1.00 57.62  ? 192 SER A CA  1 
ATOM   1470 C C   . SER A 1 195 ? -3.437  36.369  7.608   1.00 60.44  ? 192 SER A C   1 
ATOM   1471 O O   . SER A 1 195 ? -3.192  35.212  7.246   1.00 58.45  ? 192 SER A O   1 
ATOM   1472 C CB  . SER A 1 195 ? -4.197  36.934  9.875   1.00 59.53  ? 192 SER A CB  1 
ATOM   1473 O OG  . SER A 1 195 ? -2.917  36.286  10.091  1.00 69.14  ? 192 SER A OG  1 
ATOM   1474 N N   . ALA A 1 196 ? -2.590  37.391  7.451   1.00 57.95  ? 193 ALA A N   1 
ATOM   1475 C CA  . ALA A 1 196 ? -1.436  37.280  6.567   1.00 58.80  ? 193 ALA A CA  1 
ATOM   1476 C C   . ALA A 1 196 ? -0.534  36.136  6.976   1.00 61.00  ? 193 ALA A C   1 
ATOM   1477 O O   . ALA A 1 196 ? -0.031  35.411  6.115   1.00 56.10  ? 193 ALA A O   1 
ATOM   1478 C CB  . ALA A 1 196 ? -0.639  38.585  6.541   1.00 57.21  ? 193 ALA A CB  1 
ATOM   1479 N N   . GLY A 1 197 ? -0.306  35.963  8.280   1.00 64.99  ? 194 GLY A N   1 
ATOM   1480 C CA  . GLY A 1 197 ? 0.506   34.842  8.726   1.00 67.36  ? 194 GLY A CA  1 
ATOM   1481 C C   . GLY A 1 197 ? -0.108  33.504  8.360   1.00 60.34  ? 194 GLY A C   1 
ATOM   1482 O O   . GLY A 1 197 ? 0.555   32.640  7.778   1.00 61.34  ? 194 GLY A O   1 
ATOM   1483 N N   . LYS A 1 198 ? -1.382  33.333  8.648   1.00 57.45  ? 195 LYS A N   1 
ATOM   1484 C CA  . LYS A 1 198 ? -2.035  32.070  8.389   1.00 56.62  ? 195 LYS A CA  1 
ATOM   1485 C C   . LYS A 1 198 ? -2.088  31.802  6.921   1.00 53.87  ? 195 LYS A C   1 
ATOM   1486 O O   . LYS A 1 198 ? -1.916  30.681  6.478   1.00 46.99  ? 195 LYS A O   1 
ATOM   1487 C CB  . LYS A 1 198 ? -3.443  32.129  8.932   1.00 60.52  ? 195 LYS A CB  1 
ATOM   1488 C CG  . LYS A 1 198 ? -3.738  31.109  9.997   1.00 69.93  ? 195 LYS A CG  1 
ATOM   1489 C CD  . LYS A 1 198 ? -3.681  31.758  11.359  1.00 74.80  ? 195 LYS A CD  1 
ATOM   1490 C CE  . LYS A 1 198 ? -3.332  30.717  12.395  1.00 76.41  ? 195 LYS A CE  1 
ATOM   1491 N NZ  . LYS A 1 198 ? -4.479  29.793  12.612  1.00 69.57  ? 195 LYS A NZ  1 
ATOM   1492 N N   . ALA A 1 199 ? -2.375  32.840  6.166   1.00 53.78  ? 196 ALA A N   1 
ATOM   1493 C CA  . ALA A 1 199 ? -2.387  32.713  4.715   1.00 44.79  ? 196 ALA A CA  1 
ATOM   1494 C C   . ALA A 1 199 ? -1.004  32.394  4.160   1.00 48.31  ? 196 ALA A C   1 
ATOM   1495 O O   . ALA A 1 199 ? -0.887  31.656  3.169   1.00 43.49  ? 196 ALA A O   1 
ATOM   1496 C CB  . ALA A 1 199 ? -2.922  33.997  4.098   1.00 41.23  ? 196 ALA A CB  1 
ATOM   1497 N N   . ARG A 1 200 ? 0.050   32.944  4.774   1.00 53.67  ? 197 ARG A N   1 
ATOM   1498 C CA  . ARG A 1 200 ? 1.410   32.562  4.397   1.00 50.92  ? 197 ARG A CA  1 
ATOM   1499 C C   . ARG A 1 200 ? 1.681   31.107  4.755   1.00 49.10  ? 197 ARG A C   1 
ATOM   1500 O O   . ARG A 1 200 ? 2.277   30.372  3.958   1.00 48.79  ? 197 ARG A O   1 
ATOM   1501 C CB  . ARG A 1 200 ? 2.438   33.479  5.072   1.00 56.55  ? 197 ARG A CB  1 
ATOM   1502 C CG  . ARG A 1 200 ? 2.415   34.955  4.632   1.00 57.78  ? 197 ARG A CG  1 
ATOM   1503 C CD  . ARG A 1 200 ? 2.552   35.117  3.121   1.00 58.28  ? 197 ARG A CD  1 
ATOM   1504 N NE  . ARG A 1 200 ? 3.917   34.855  2.682   1.00 61.70  ? 197 ARG A NE  1 
ATOM   1505 C CZ  . ARG A 1 200 ? 4.240   34.227  1.558   1.00 68.41  ? 197 ARG A CZ  1 
ATOM   1506 N NH1 . ARG A 1 200 ? 3.311   33.772  0.727   1.00 63.31  ? 197 ARG A NH1 1 
ATOM   1507 N NH2 . ARG A 1 200 ? 5.528   34.041  1.265   1.00 62.84  ? 197 ARG A NH2 1 
ATOM   1508 N N   . TYR A 1 201 ? 1.235   30.679  5.948   1.00 45.64  ? 198 TYR A N   1 
ATOM   1509 C CA  . TYR A 1 201 ? 1.373   29.289  6.375   1.00 47.89  ? 198 TYR A CA  1 
ATOM   1510 C C   . TYR A 1 201 ? 0.715   28.335  5.377   1.00 47.17  ? 198 TYR A C   1 
ATOM   1511 O O   . TYR A 1 201 ? 1.330   27.354  4.936   1.00 43.86  ? 198 TYR A O   1 
ATOM   1512 C CB  . TYR A 1 201 ? 0.778   29.133  7.781   1.00 56.96  ? 198 TYR A CB  1 
ATOM   1513 C CG  . TYR A 1 201 ? 0.645   27.711  8.297   1.00 56.68  ? 198 TYR A CG  1 
ATOM   1514 C CD1 . TYR A 1 201 ? 1.768   26.915  8.508   1.00 55.93  ? 198 TYR A CD1 1 
ATOM   1515 C CD2 . TYR A 1 201 ? -0.606  27.179  8.608   1.00 54.77  ? 198 TYR A CD2 1 
ATOM   1516 C CE1 . TYR A 1 201 ? 1.650   25.613  9.000   1.00 55.06  ? 198 TYR A CE1 1 
ATOM   1517 C CE2 . TYR A 1 201 ? -0.741  25.877  9.094   1.00 61.63  ? 198 TYR A CE2 1 
ATOM   1518 C CZ  . TYR A 1 201 ? 0.394   25.097  9.289   1.00 64.57  ? 198 TYR A CZ  1 
ATOM   1519 O OH  . TYR A 1 201 ? 0.269   23.804  9.770   1.00 60.08  ? 198 TYR A OH  1 
ATOM   1520 N N   . LEU A 1 202 ? -0.533  28.612  4.992   1.00 41.74  ? 199 LEU A N   1 
ATOM   1521 C CA  . LEU A 1 202 ? -1.170  27.792  3.965   1.00 40.66  ? 199 LEU A CA  1 
ATOM   1522 C C   . LEU A 1 202 ? -0.382  27.825  2.659   1.00 43.94  ? 199 LEU A C   1 
ATOM   1523 O O   . LEU A 1 202 ? -0.266  26.806  1.964   1.00 41.69  ? 199 LEU A O   1 
ATOM   1524 C CB  . LEU A 1 202 ? -2.606  28.254  3.746   1.00 39.30  ? 199 LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 202 ? -3.480  27.967  4.966   1.00 39.72  ? 199 LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 202 ? -4.916  28.284  4.667   1.00 37.49  ? 199 LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 202 ? -3.318  26.520  5.386   1.00 38.96  ? 199 LEU A CD2 1 
ATOM   1528 N N   . SER A 1 203 ? 0.193   28.978  2.317   1.00 43.10  ? 200 SER A N   1 
ATOM   1529 C CA  . SER A 1 203 ? 1.028   29.016  1.128   1.00 41.33  ? 200 SER A CA  1 
ATOM   1530 C C   . SER A 1 203 ? 2.279   28.153  1.288   1.00 44.83  ? 200 SER A C   1 
ATOM   1531 O O   . SER A 1 203 ? 2.747   27.552  0.314   1.00 40.69  ? 200 SER A O   1 
ATOM   1532 C CB  . SER A 1 203 ? 1.392   30.455  0.797   1.00 42.64  ? 200 SER A CB  1 
ATOM   1533 O OG  . SER A 1 203 ? 1.638   30.584  -0.589  1.00 45.83  ? 200 SER A OG  1 
ATOM   1534 N N   . GLN A 1 204 ? 2.816   28.041  2.500   1.00 45.95  ? 201 GLN A N   1 
ATOM   1535 C CA  . GLN A 1 204 ? 3.949   27.135  2.689   1.00 53.66  ? 201 GLN A CA  1 
ATOM   1536 C C   . GLN A 1 204 ? 3.547   25.666  2.655   1.00 45.49  ? 201 GLN A C   1 
ATOM   1537 O O   . GLN A 1 204 ? 4.405   24.818  2.408   1.00 39.31  ? 201 GLN A O   1 
ATOM   1538 C CB  . GLN A 1 204 ? 4.662   27.406  4.018   1.00 57.50  ? 201 GLN A CB  1 
ATOM   1539 C CG  . GLN A 1 204 ? 5.156   28.825  4.186   1.00 66.24  ? 201 GLN A CG  1 
ATOM   1540 C CD  . GLN A 1 204 ? 6.251   28.947  5.235   1.00 73.74  ? 201 GLN A CD  1 
ATOM   1541 O OE1 . GLN A 1 204 ? 7.095   29.846  5.147   1.00 67.97  ? 201 GLN A OE1 1 
ATOM   1542 N NE2 . GLN A 1 204 ? 6.249   28.046  6.233   1.00 69.32  ? 201 GLN A NE2 1 
ATOM   1543 N N   . LEU A 1 205 ? 2.285   25.340  2.947   1.00 45.12  ? 202 LEU A N   1 
ATOM   1544 C CA  . LEU A 1 205 ? 1.823   23.961  2.850   1.00 40.17  ? 202 LEU A CA  1 
ATOM   1545 C C   . LEU A 1 205 ? 1.479   23.573  1.422   1.00 44.42  ? 202 LEU A C   1 
ATOM   1546 O O   . LEU A 1 205 ? 1.229   22.390  1.160   1.00 48.23  ? 202 LEU A O   1 
ATOM   1547 C CB  . LEU A 1 205 ? 0.606   23.727  3.760   1.00 42.67  ? 202 LEU A CB  1 
ATOM   1548 C CG  . LEU A 1 205 ? 0.882   23.880  5.262   1.00 42.22  ? 202 LEU A CG  1 
ATOM   1549 C CD1 . LEU A 1 205 ? -0.371  23.741  6.111   1.00 45.49  ? 202 LEU A CD1 1 
ATOM   1550 C CD2 . LEU A 1 205 ? 1.898   22.864  5.676   1.00 37.66  ? 202 LEU A CD2 1 
ATOM   1551 N N   . GLY A 1 206 ? 1.475   24.533  0.497   1.00 48.94  ? 203 GLY A N   1 
ATOM   1552 C CA  . GLY A 1 206 ? 1.281   24.261  -0.922  1.00 38.77  ? 203 GLY A CA  1 
ATOM   1553 C C   . GLY A 1 206 ? 0.015   24.848  -1.499  1.00 38.63  ? 203 GLY A C   1 
ATOM   1554 O O   . GLY A 1 206 ? -0.244  24.649  -2.691  1.00 39.16  ? 203 GLY A O   1 
ATOM   1555 N N   . PHE A 1 207 ? -0.803  25.548  -0.714  1.00 37.14  ? 204 PHE A N   1 
ATOM   1556 C CA  . PHE A 1 207 ? -1.967  26.222  -1.260  1.00 31.41  ? 204 PHE A CA  1 
ATOM   1557 C C   . PHE A 1 207 ? -1.529  27.193  -2.352  1.00 36.76  ? 204 PHE A C   1 
ATOM   1558 O O   . PHE A 1 207 ? -0.536  27.910  -2.203  1.00 39.57  ? 204 PHE A O   1 
ATOM   1559 C CB  . PHE A 1 207 ? -2.725  26.938  -0.139  1.00 28.84  ? 204 PHE A CB  1 
ATOM   1560 C CG  . PHE A 1 207 ? -3.690  26.047  0.591   1.00 30.35  ? 204 PHE A CG  1 
ATOM   1561 C CD1 . PHE A 1 207 ? -3.233  25.006  1.384   1.00 30.34  ? 204 PHE A CD1 1 
ATOM   1562 C CD2 . PHE A 1 207 ? -5.062  26.222  0.457   1.00 33.84  ? 204 PHE A CD2 1 
ATOM   1563 C CE1 . PHE A 1 207 ? -4.115  24.165  2.042   1.00 29.77  ? 204 PHE A CE1 1 
ATOM   1564 C CE2 . PHE A 1 207 ? -5.948  25.381  1.103   1.00 31.80  ? 204 PHE A CE2 1 
ATOM   1565 C CZ  . PHE A 1 207 ? -5.466  24.346  1.900   1.00 31.97  ? 204 PHE A CZ  1 
ATOM   1566 N N   . ASP A 1 208 ? -2.236  27.174  -3.479  1.00 36.65  ? 205 ASP A N   1 
ATOM   1567 C CA  . ASP A 1 208 ? -1.852  28.022  -4.598  1.00 36.52  ? 205 ASP A CA  1 
ATOM   1568 C C   . ASP A 1 208 ? -2.405  29.425  -4.470  1.00 37.80  ? 205 ASP A C   1 
ATOM   1569 O O   . ASP A 1 208 ? -1.873  30.356  -5.094  1.00 36.97  ? 205 ASP A O   1 
ATOM   1570 C CB  . ASP A 1 208 ? -2.318  27.403  -5.908  1.00 34.19  ? 205 ASP A CB  1 
ATOM   1571 C CG  . ASP A 1 208 ? -1.634  26.090  -6.184  1.00 42.50  ? 205 ASP A CG  1 
ATOM   1572 O OD1 . ASP A 1 208 ? -0.392  26.077  -6.346  1.00 51.47  ? 205 ASP A OD1 1 
ATOM   1573 O OD2 . ASP A 1 208 ? -2.327  25.051  -6.190  1.00 46.56  ? 205 ASP A OD2 1 
ATOM   1574 N N   . ALA A 1 209 ? -3.447  29.590  -3.668  1.00 36.22  ? 206 ALA A N   1 
ATOM   1575 C CA  . ALA A 1 209 ? -4.086  30.877  -3.473  1.00 37.70  ? 206 ALA A CA  1 
ATOM   1576 C C   . ALA A 1 209 ? -4.825  30.821  -2.148  1.00 35.77  ? 206 ALA A C   1 
ATOM   1577 O O   . ALA A 1 209 ? -5.394  29.787  -1.788  1.00 38.80  ? 206 ALA A O   1 
ATOM   1578 C CB  . ALA A 1 209 ? -5.040  31.211  -4.624  1.00 34.03  ? 206 ALA A CB  1 
ATOM   1579 N N   . VAL A 1 210 ? -4.770  31.920  -1.415  1.00 32.28  ? 207 VAL A N   1 
ATOM   1580 C CA  . VAL A 1 210 ? -5.385  32.028  -0.109  1.00 34.51  ? 207 VAL A CA  1 
ATOM   1581 C C   . VAL A 1 210 ? -6.152  33.335  -0.069  1.00 41.54  ? 207 VAL A C   1 
ATOM   1582 O O   . VAL A 1 210 ? -5.625  34.384  -0.454  1.00 47.15  ? 207 VAL A O   1 
ATOM   1583 C CB  . VAL A 1 210 ? -4.340  31.972  1.013   1.00 38.92  ? 207 VAL A CB  1 
ATOM   1584 C CG1 . VAL A 1 210 ? -5.036  31.698  2.339   1.00 42.17  ? 207 VAL A CG1 1 
ATOM   1585 C CG2 . VAL A 1 210 ? -3.302  30.906  0.710   1.00 36.23  ? 207 VAL A CG2 1 
ATOM   1586 N N   . ILE A 1 211 ? -7.395  33.273  0.376   1.00 39.19  ? 208 ILE A N   1 
ATOM   1587 C CA  . ILE A 1 211 ? -8.273  34.426  0.402   1.00 38.07  ? 208 ILE A CA  1 
ATOM   1588 C C   . ILE A 1 211 ? -8.589  34.737  1.848   1.00 45.39  ? 208 ILE A C   1 
ATOM   1589 O O   . ILE A 1 211 ? -8.977  33.839  2.597   1.00 50.20  ? 208 ILE A O   1 
ATOM   1590 C CB  . ILE A 1 211 ? -9.565  34.149  -0.371  1.00 43.98  ? 208 ILE A CB  1 
ATOM   1591 C CG1 . ILE A 1 211 ? -9.267  34.035  -1.869  1.00 40.95  ? 208 ILE A CG1 1 
ATOM   1592 C CG2 . ILE A 1 211 ? -10.626 35.186  0.011   1.00 46.11  ? 208 ILE A CG2 1 
ATOM   1593 C CD1 . ILE A 1 211 ? -10.392 33.415  -2.675  1.00 39.31  ? 208 ILE A CD1 1 
ATOM   1594 N N   . ASP A 1 212 ? -8.443  36.001  2.239   1.00 54.66  ? 209 ASP A N   1 
ATOM   1595 C CA  . ASP A 1 212 ? -8.754  36.432  3.601   1.00 52.12  ? 209 ASP A CA  1 
ATOM   1596 C C   . ASP A 1 212 ? -10.267 36.564  3.755   1.00 56.18  ? 209 ASP A C   1 
ATOM   1597 O O   . ASP A 1 212 ? -10.879 37.443  3.139   1.00 61.33  ? 209 ASP A O   1 
ATOM   1598 C CB  . ASP A 1 212 ? -8.047  37.750  3.889   1.00 60.90  ? 209 ASP A CB  1 
ATOM   1599 C CG  . ASP A 1 212 ? -8.238  38.223  5.309   1.00 65.91  ? 209 ASP A CG  1 
ATOM   1600 O OD1 . ASP A 1 212 ? -9.395  38.485  5.712   1.00 60.98  ? 209 ASP A OD1 1 
ATOM   1601 O OD2 . ASP A 1 212 ? -7.215  38.334  6.020   1.00 66.91  ? 209 ASP A OD2 1 
ATOM   1602 N N   . TYR A 1 213 ? -10.875 35.700  4.582   1.00 55.48  ? 210 TYR A N   1 
ATOM   1603 C CA  . TYR A 1 213 ? -12.328 35.737  4.745   1.00 58.25  ? 210 TYR A CA  1 
ATOM   1604 C C   . TYR A 1 213 ? -12.772 36.907  5.606   1.00 63.88  ? 210 TYR A C   1 
ATOM   1605 O O   . TYR A 1 213 ? -13.957 37.261  5.580   1.00 62.79  ? 210 TYR A O   1 
ATOM   1606 C CB  . TYR A 1 213 ? -12.870 34.422  5.338   1.00 55.27  ? 210 TYR A CB  1 
ATOM   1607 C CG  . TYR A 1 213 ? -12.376 34.088  6.737   1.00 66.28  ? 210 TYR A CG  1 
ATOM   1608 C CD1 . TYR A 1 213 ? -13.054 34.534  7.882   1.00 66.54  ? 210 TYR A CD1 1 
ATOM   1609 C CD2 . TYR A 1 213 ? -11.233 33.326  6.915   1.00 62.93  ? 210 TYR A CD2 1 
ATOM   1610 C CE1 . TYR A 1 213 ? -12.583 34.240  9.163   1.00 62.58  ? 210 TYR A CE1 1 
ATOM   1611 C CE2 . TYR A 1 213 ? -10.759 33.024  8.180   1.00 68.20  ? 210 TYR A CE2 1 
ATOM   1612 C CZ  . TYR A 1 213 ? -11.432 33.477  9.303   1.00 71.29  ? 210 TYR A CZ  1 
ATOM   1613 O OH  . TYR A 1 213 ? -10.939 33.151  10.553  1.00 68.53  ? 210 TYR A OH  1 
ATOM   1614 N N   . LYS A 1 214 ? -11.854 37.513  6.368   1.00 62.07  ? 211 LYS A N   1 
ATOM   1615 C CA  . LYS A 1 214 ? -12.213 38.702  7.138   1.00 68.23  ? 211 LYS A CA  1 
ATOM   1616 C C   . LYS A 1 214 ? -12.372 39.911  6.227   1.00 73.97  ? 211 LYS A C   1 
ATOM   1617 O O   . LYS A 1 214 ? -13.328 40.684  6.368   1.00 76.66  ? 211 LYS A O   1 
ATOM   1618 C CB  . LYS A 1 214 ? -11.168 38.972  8.221   1.00 66.64  ? 211 LYS A CB  1 
ATOM   1619 C CG  . LYS A 1 214 ? -11.343 38.093  9.440   1.00 66.74  ? 211 LYS A CG  1 
ATOM   1620 C CD  . LYS A 1 214 ? -10.149 38.180  10.360  1.00 70.38  ? 211 LYS A CD  1 
ATOM   1621 C CE  . LYS A 1 214 ? -10.171 37.065  11.410  1.00 71.75  ? 211 LYS A CE  1 
ATOM   1622 N NZ  . LYS A 1 214 ? -9.036  37.184  12.381  1.00 63.17  ? 211 LYS A NZ  1 
ATOM   1623 N N   . LEU A 1 215 ? -11.462 40.080  5.270   1.00 70.52  ? 212 LEU A N   1 
ATOM   1624 C CA  . LEU A 1 215 ? -11.623 41.162  4.307   1.00 71.18  ? 212 LEU A CA  1 
ATOM   1625 C C   . LEU A 1 215 ? -12.832 40.906  3.409   1.00 75.04  ? 212 LEU A C   1 
ATOM   1626 O O   . LEU A 1 215 ? -13.765 41.719  3.352   1.00 76.71  ? 212 LEU A O   1 
ATOM   1627 C CB  . LEU A 1 215 ? -10.342 41.334  3.488   1.00 65.35  ? 212 LEU A CB  1 
ATOM   1628 C CG  . LEU A 1 215 ? -9.038  41.552  4.277   1.00 71.68  ? 212 LEU A CG  1 
ATOM   1629 C CD1 . LEU A 1 215 ? -8.102  42.449  3.464   1.00 64.99  ? 212 LEU A CD1 1 
ATOM   1630 C CD2 . LEU A 1 215 ? -9.234  42.090  5.732   1.00 63.38  ? 212 LEU A CD2 1 
ATOM   1631 N N   . ALA A 1 216 ? -12.852 39.759  2.726   1.00 73.13  ? 213 ALA A N   1 
ATOM   1632 C CA  . ALA A 1 216 ? -13.952 39.407  1.823   1.00 68.80  ? 213 ALA A CA  1 
ATOM   1633 C C   . ALA A 1 216 ? -15.124 38.866  2.643   1.00 71.52  ? 213 ALA A C   1 
ATOM   1634 O O   . ALA A 1 216 ? -15.379 37.660  2.708   1.00 66.51  ? 213 ALA A O   1 
ATOM   1635 C CB  . ALA A 1 216 ? -13.479 38.403  0.784   1.00 57.66  ? 213 ALA A CB  1 
ATOM   1636 N N   . ASP A 1 217 ? -15.874 39.795  3.250   1.00 75.37  ? 214 ASP A N   1 
ATOM   1637 C CA  . ASP A 1 217 ? -16.855 39.471  4.285   1.00 71.28  ? 214 ASP A CA  1 
ATOM   1638 C C   . ASP A 1 217 ? -18.255 39.162  3.759   1.00 70.98  ? 214 ASP A C   1 
ATOM   1639 O O   . ASP A 1 217 ? -19.071 38.604  4.506   1.00 71.47  ? 214 ASP A O   1 
ATOM   1640 C CB  . ASP A 1 217 ? -16.948 40.621  5.290   1.00 69.22  ? 214 ASP A CB  1 
ATOM   1641 C CG  . ASP A 1 217 ? -17.052 41.968  4.615   1.00 77.75  ? 214 ASP A CG  1 
ATOM   1642 O OD1 . ASP A 1 217 ? -18.069 42.228  3.924   1.00 79.28  ? 214 ASP A OD1 1 
ATOM   1643 O OD2 . ASP A 1 217 ? -16.104 42.764  4.769   1.00 79.65  ? 214 ASP A OD2 1 
ATOM   1644 N N   . ASP A 1 218 ? -18.554 39.548  2.527   1.00 73.08  ? 215 ASP A N   1 
ATOM   1645 C CA  . ASP A 1 218 ? -19.849 39.208  1.934   1.00 72.78  ? 215 ASP A CA  1 
ATOM   1646 C C   . ASP A 1 218 ? -19.669 38.436  0.653   1.00 68.10  ? 215 ASP A C   1 
ATOM   1647 O O   . ASP A 1 218 ? -18.594 38.436  0.076   1.00 70.08  ? 215 ASP A O   1 
ATOM   1648 C CB  . ASP A 1 218 ? -20.781 40.429  1.763   1.00 76.06  ? 215 ASP A CB  1 
ATOM   1649 C CG  . ASP A 1 218 ? -20.504 41.259  0.536   1.00 87.43  ? 215 ASP A CG  1 
ATOM   1650 O OD1 . ASP A 1 218 ? -20.142 40.733  -0.524  1.00 82.31  ? 215 ASP A OD1 1 
ATOM   1651 O OD2 . ASP A 1 218 ? -20.707 42.483  0.626   1.00 92.27  ? 215 ASP A OD2 1 
ATOM   1652 N N   . ALA A 1 219 ? -20.728 37.794  0.199   1.00 61.42  ? 216 ALA A N   1 
ATOM   1653 C CA  . ALA A 1 219 ? -20.613 36.929  -0.973  1.00 62.41  ? 216 ALA A CA  1 
ATOM   1654 C C   . ALA A 1 219 ? -20.146 37.685  -2.212  1.00 63.31  ? 216 ALA A C   1 
ATOM   1655 O O   . ALA A 1 219 ? -19.492 37.102  -3.079  1.00 57.10  ? 216 ALA A O   1 
ATOM   1656 C CB  . ALA A 1 219 ? -21.948 36.231  -1.250  1.00 54.89  ? 216 ALA A CB  1 
ATOM   1657 N N   . ASP A 1 220 ? -20.443 38.983  -2.306  1.00 66.95  ? 217 ASP A N   1 
ATOM   1658 C CA  . ASP A 1 220 ? -19.977 39.743  -3.458  1.00 62.49  ? 217 ASP A CA  1 
ATOM   1659 C C   . ASP A 1 220 ? -18.474 39.950  -3.407  1.00 57.77  ? 217 ASP A C   1 
ATOM   1660 O O   . ASP A 1 220 ? -17.762 39.593  -4.346  1.00 57.37  ? 217 ASP A O   1 
ATOM   1661 C CB  . ASP A 1 220 ? -20.704 41.079  -3.542  1.00 69.88  ? 217 ASP A CB  1 
ATOM   1662 C CG  . ASP A 1 220 ? -21.890 41.025  -4.477  1.00 72.98  ? 217 ASP A CG  1 
ATOM   1663 O OD1 . ASP A 1 220 ? -21.758 40.455  -5.593  1.00 69.15  ? 217 ASP A OD1 1 
ATOM   1664 O OD2 . ASP A 1 220 ? -22.956 41.544  -4.084  1.00 77.23  ? 217 ASP A OD2 1 
ATOM   1665 N N   . LYS A 1 221 ? -17.959 40.458  -2.319  1.00 62.50  ? 218 LYS A N   1 
ATOM   1666 C CA  . LYS A 1 221 ? -16.530 40.591  -2.210  1.00 61.47  ? 218 LYS A CA  1 
ATOM   1667 C C   . LYS A 1 221 ? -15.910 39.217  -2.317  1.00 60.58  ? 218 LYS A C   1 
ATOM   1668 O O   . LYS A 1 221 ? -14.834 39.054  -2.873  1.00 57.38  ? 218 LYS A O   1 
ATOM   1669 C CB  . LYS A 1 221 ? -16.197 41.239  -0.883  1.00 60.32  ? 218 LYS A CB  1 
ATOM   1670 C CG  . LYS A 1 221 ? -16.659 42.678  -0.782  1.00 69.49  ? 218 LYS A CG  1 
ATOM   1671 C CD  . LYS A 1 221 ? -16.321 43.263  0.571   1.00 70.34  ? 218 LYS A CD  1 
ATOM   1672 C CE  . LYS A 1 221 ? -16.761 44.711  0.665   1.00 73.00  ? 218 LYS A CE  1 
ATOM   1673 N NZ  . LYS A 1 221 ? -16.450 45.279  2.005   1.00 73.51  ? 218 LYS A NZ  1 
ATOM   1674 N N   . MET A 1 222 ? -16.596 38.224  -1.787  1.00 57.09  ? 219 MET A N   1 
ATOM   1675 C CA  . MET A 1 222 ? -16.105 36.850  -1.831  1.00 50.75  ? 219 MET A CA  1 
ATOM   1676 C C   . MET A 1 222 ? -16.126 36.295  -3.254  1.00 54.39  ? 219 MET A C   1 
ATOM   1677 O O   . MET A 1 222 ? -15.150 35.672  -3.692  1.00 51.87  ? 219 MET A O   1 
ATOM   1678 C CB  . MET A 1 222 ? -16.942 35.972  -0.900  1.00 57.45  ? 219 MET A CB  1 
ATOM   1679 C CG  . MET A 1 222 ? -16.235 34.700  -0.470  1.00 58.11  ? 219 MET A CG  1 
ATOM   1680 S SD  . MET A 1 222 ? -14.568 35.068  0.111   1.00 63.08  ? 219 MET A SD  1 
ATOM   1681 C CE  . MET A 1 222 ? -13.729 33.539  -0.206  1.00 52.54  ? 219 MET A CE  1 
ATOM   1682 N N   . ARG A 1 223 ? -17.236 36.494  -3.987  1.00 51.42  ? 220 ARG A N   1 
ATOM   1683 C CA  . ARG A 1 223 ? -17.266 36.145  -5.406  1.00 45.25  ? 220 ARG A CA  1 
ATOM   1684 C C   . ARG A 1 223 ? -16.077 36.743  -6.134  1.00 51.57  ? 220 ARG A C   1 
ATOM   1685 O O   . ARG A 1 223 ? -15.458 36.074  -6.967  1.00 49.78  ? 220 ARG A O   1 
ATOM   1686 C CB  . ARG A 1 223 ? -18.568 36.610  -6.064  1.00 45.65  ? 220 ARG A CB  1 
ATOM   1687 C CG  . ARG A 1 223 ? -19.602 35.507  -6.236  1.00 50.28  ? 220 ARG A CG  1 
ATOM   1688 C CD  . ARG A 1 223 ? -20.900 35.970  -6.898  1.00 52.39  ? 220 ARG A CD  1 
ATOM   1689 N NE  . ARG A 1 223 ? -21.727 36.805  -6.032  1.00 62.94  ? 220 ARG A NE  1 
ATOM   1690 C CZ  . ARG A 1 223 ? -22.695 36.353  -5.244  1.00 64.18  ? 220 ARG A CZ  1 
ATOM   1691 N NH1 . ARG A 1 223 ? -22.984 35.060  -5.172  1.00 62.65  ? 220 ARG A NH1 1 
ATOM   1692 N NH2 . ARG A 1 223 ? -23.396 37.221  -4.517  1.00 63.25  ? 220 ARG A NH2 1 
ATOM   1693 N N   . GLU A 1 224 ? -15.732 37.997  -5.813  1.00 51.68  ? 221 GLU A N   1 
ATOM   1694 C CA  . GLU A 1 224 ? -14.607 38.665  -6.457  1.00 49.86  ? 221 GLU A CA  1 
ATOM   1695 C C   . GLU A 1 224 ? -13.313 37.910  -6.216  1.00 48.29  ? 221 GLU A C   1 
ATOM   1696 O O   . GLU A 1 224 ? -12.540 37.662  -7.149  1.00 45.24  ? 221 GLU A O   1 
ATOM   1697 C CB  . GLU A 1 224 ? -14.475 40.095  -5.940  1.00 56.12  ? 221 GLU A CB  1 
ATOM   1698 C CG  . GLU A 1 224 ? -14.183 41.088  -7.033  1.00 61.96  ? 221 GLU A CG  1 
ATOM   1699 C CD  . GLU A 1 224 ? -15.212 41.000  -8.158  1.00 77.60  ? 221 GLU A CD  1 
ATOM   1700 O OE1 . GLU A 1 224 ? -14.814 40.886  -9.343  1.00 76.07  ? 221 GLU A OE1 1 
ATOM   1701 O OE2 . GLU A 1 224 ? -16.433 41.006  -7.831  1.00 83.04  ? 221 GLU A OE2 1 
ATOM   1702 N N   . ALA A 1 225 ? -13.066 37.534  -4.961  1.00 46.69  ? 222 ALA A N   1 
ATOM   1703 C CA  . ALA A 1 225 ? -11.794 36.923  -4.601  1.00 42.15  ? 222 ALA A CA  1 
ATOM   1704 C C   . ALA A 1 225 ? -11.667 35.541  -5.214  1.00 37.36  ? 222 ALA A C   1 
ATOM   1705 O O   . ALA A 1 225 ? -10.586 35.157  -5.679  1.00 34.64  ? 222 ALA A O   1 
ATOM   1706 C CB  . ALA A 1 225 ? -11.663 36.868  -3.073  1.00 38.91  ? 222 ALA A CB  1 
ATOM   1707 N N   . LEU A 1 226 ? -12.768 34.790  -5.237  1.00 35.32  ? 223 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 226 ? -12.762 33.481  -5.880  1.00 41.83  ? 223 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 226 ? -12.502 33.599  -7.373  1.00 40.70  ? 223 LEU A C   1 
ATOM   1710 O O   . LEU A 1 226 ? -11.676 32.868  -7.932  1.00 38.66  ? 223 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 226 ? -14.087 32.777  -5.637  1.00 40.08  ? 223 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 226 ? -14.159 32.423  -4.178  1.00 42.34  ? 223 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 226 ? -15.593 32.137  -3.770  1.00 40.56  ? 223 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 226 ? -13.220 31.236  -4.013  1.00 35.80  ? 223 LEU A CD2 1 
ATOM   1715 N N   . ARG A 1 227 ? -13.228 34.490  -8.047  1.00 42.41  ? 224 ARG A N   1 
ATOM   1716 C CA  . ARG A 1 227 ? -13.037 34.597  -9.482  1.00 39.77  ? 224 ARG A CA  1 
ATOM   1717 C C   . ARG A 1 227 ? -11.598 34.940  -9.799  1.00 41.64  ? 224 ARG A C   1 
ATOM   1718 O O   . ARG A 1 227 ? -11.049 34.449  -10.789 1.00 43.65  ? 224 ARG A O   1 
ATOM   1719 C CB  . ARG A 1 227 ? -14.010 35.608  -10.072 1.00 40.95  ? 224 ARG A CB  1 
ATOM   1720 C CG  . ARG A 1 227 ? -15.312 34.950  -10.510 1.00 50.83  ? 224 ARG A CG  1 
ATOM   1721 C CD  . ARG A 1 227 ? -16.241 35.877  -11.283 1.00 55.43  ? 224 ARG A CD  1 
ATOM   1722 N NE  . ARG A 1 227 ? -17.121 36.615  -10.387 1.00 59.00  ? 224 ARG A NE  1 
ATOM   1723 C CZ  . ARG A 1 227 ? -16.886 37.847  -9.949  1.00 66.46  ? 224 ARG A CZ  1 
ATOM   1724 N NH1 . ARG A 1 227 ? -15.812 38.529  -10.333 1.00 62.59  ? 224 ARG A NH1 1 
ATOM   1725 N NH2 . ARG A 1 227 ? -17.748 38.410  -9.104  1.00 68.38  ? 224 ARG A NH2 1 
ATOM   1726 N N   . GLU A 1 228 ? -10.943 35.707  -8.936  1.00 39.89  ? 225 GLU A N   1 
ATOM   1727 C CA  . GLU A 1 228 ? -9.534  35.973  -9.179  1.00 38.10  ? 225 GLU A CA  1 
ATOM   1728 C C   . GLU A 1 228 ? -8.669  34.778  -8.803  1.00 37.74  ? 225 GLU A C   1 
ATOM   1729 O O   . GLU A 1 228 ? -7.667  34.511  -9.466  1.00 41.99  ? 225 GLU A O   1 
ATOM   1730 C CB  . GLU A 1 228 ? -9.095  37.216  -8.417  1.00 47.23  ? 225 GLU A CB  1 
ATOM   1731 C CG  . GLU A 1 228 ? -7.727  37.735  -8.823  1.00 60.74  ? 225 GLU A CG  1 
ATOM   1732 C CD  . GLU A 1 228 ? -7.722  39.244  -9.017  1.00 79.79  ? 225 GLU A CD  1 
ATOM   1733 O OE1 . GLU A 1 228 ? -7.770  39.965  -7.988  1.00 85.77  ? 225 GLU A OE1 1 
ATOM   1734 O OE2 . GLU A 1 228 ? -7.692  39.702  -10.192 1.00 71.60  ? 225 GLU A OE2 1 
ATOM   1735 N N   . ALA A 1 229 ? -9.040  34.038  -7.754  1.00 41.96  ? 226 ALA A N   1 
ATOM   1736 C CA  . ALA A 1 229 ? -8.230  32.906  -7.309  1.00 36.37  ? 226 ALA A CA  1 
ATOM   1737 C C   . ALA A 1 229 ? -8.506  31.637  -8.099  1.00 37.42  ? 226 ALA A C   1 
ATOM   1738 O O   . ALA A 1 229 ? -7.667  30.731  -8.099  1.00 39.25  ? 226 ALA A O   1 
ATOM   1739 C CB  . ALA A 1 229 ? -8.466  32.628  -5.823  1.00 30.01  ? 226 ALA A CB  1 
ATOM   1740 N N   . ALA A 1 230 ? -9.655  31.553  -8.765  1.00 31.07  ? 227 ALA A N   1 
ATOM   1741 C CA  . ALA A 1 230 ? -10.110 30.328  -9.415  1.00 33.32  ? 227 ALA A CA  1 
ATOM   1742 C C   . ALA A 1 230 ? -10.750 30.735  -10.730 1.00 35.79  ? 227 ALA A C   1 
ATOM   1743 O O   . ALA A 1 230 ? -11.960 30.596  -10.937 1.00 31.90  ? 227 ALA A O   1 
ATOM   1744 C CB  . ALA A 1 230 ? -11.081 29.556  -8.517  1.00 31.41  ? 227 ALA A CB  1 
ATOM   1745 N N   . PRO A 1 231 ? -9.955  31.266  -11.651 1.00 40.36  ? 228 PRO A N   1 
ATOM   1746 C CA  . PRO A 1 231 ? -10.547 31.848  -12.865 1.00 37.94  ? 228 PRO A CA  1 
ATOM   1747 C C   . PRO A 1 231 ? -11.226 30.830  -13.756 1.00 37.11  ? 228 PRO A C   1 
ATOM   1748 O O   . PRO A 1 231 ? -12.136 31.206  -14.503 1.00 37.43  ? 228 PRO A O   1 
ATOM   1749 C CB  . PRO A 1 231 ? -9.353  32.501  -13.566 1.00 31.84  ? 228 PRO A CB  1 
ATOM   1750 C CG  . PRO A 1 231 ? -8.180  31.736  -13.074 1.00 41.95  ? 228 PRO A CG  1 
ATOM   1751 C CD  . PRO A 1 231 ? -8.485  31.243  -11.688 1.00 38.04  ? 228 PRO A CD  1 
ATOM   1752 N N   . ASP A 1 232 ? -10.854 29.556  -13.689 1.00 29.69  ? 229 ASP A N   1 
ATOM   1753 C CA  . ASP A 1 232 ? -11.505 28.555  -14.518 1.00 32.44  ? 229 ASP A CA  1 
ATOM   1754 C C   . ASP A 1 232 ? -12.655 27.834  -13.813 1.00 31.33  ? 229 ASP A C   1 
ATOM   1755 O O   . ASP A 1 232 ? -13.152 26.830  -14.332 1.00 32.62  ? 229 ASP A O   1 
ATOM   1756 C CB  . ASP A 1 232 ? -10.470 27.551  -15.031 1.00 35.63  ? 229 ASP A CB  1 
ATOM   1757 C CG  . ASP A 1 232 ? -9.426  28.203  -15.935 1.00 46.82  ? 229 ASP A CG  1 
ATOM   1758 O OD1 . ASP A 1 232 ? -9.823  28.949  -16.872 1.00 44.63  ? 229 ASP A OD1 1 
ATOM   1759 O OD2 . ASP A 1 232 ? -8.211  27.988  -15.696 1.00 46.05  ? 229 ASP A OD2 1 
ATOM   1760 N N   . GLY A 1 233 ? -13.107 28.321  -12.663 1.00 29.69  ? 230 GLY A N   1 
ATOM   1761 C CA  . GLY A 1 233 ? -14.205 27.683  -11.959 1.00 28.30  ? 230 GLY A CA  1 
ATOM   1762 C C   . GLY A 1 233 ? -13.742 26.720  -10.864 1.00 32.43  ? 230 GLY A C   1 
ATOM   1763 O O   . GLY A 1 233 ? -12.550 26.492  -10.627 1.00 29.62  ? 230 GLY A O   1 
ATOM   1764 N N   . VAL A 1 234 ? -14.733 26.146  -10.187 1.00 31.36  ? 231 VAL A N   1 
ATOM   1765 C CA  . VAL A 1 234 ? -14.514 25.280  -9.040  1.00 29.83  ? 231 VAL A CA  1 
ATOM   1766 C C   . VAL A 1 234 ? -14.999 23.891  -9.393  1.00 29.94  ? 231 VAL A C   1 
ATOM   1767 O O   . VAL A 1 234 ? -16.164 23.712  -9.769  1.00 30.57  ? 231 VAL A O   1 
ATOM   1768 C CB  . VAL A 1 234 ? -15.229 25.793  -7.789  1.00 30.43  ? 231 VAL A CB  1 
ATOM   1769 C CG1 . VAL A 1 234 ? -14.897 24.885  -6.602  1.00 31.15  ? 231 VAL A CG1 1 
ATOM   1770 C CG2 . VAL A 1 234 ? -14.806 27.212  -7.520  1.00 33.66  ? 231 VAL A CG2 1 
ATOM   1771 N N   . ASP A 1 235 ? -14.111 22.908  -9.264  1.00 33.10  ? 232 ASP A N   1 
ATOM   1772 C CA  . ASP A 1 235 ? -14.445 21.502  -9.439  1.00 29.85  ? 232 ASP A CA  1 
ATOM   1773 C C   . ASP A 1 235 ? -14.750 20.814  -8.128  1.00 28.19  ? 232 ASP A C   1 
ATOM   1774 O O   . ASP A 1 235 ? -15.682 20.014  -8.073  1.00 25.25  ? 232 ASP A O   1 
ATOM   1775 C CB  . ASP A 1 235 ? -13.304 20.773  -10.129 1.00 27.27  ? 232 ASP A CB  1 
ATOM   1776 C CG  . ASP A 1 235 ? -12.878 21.474  -11.376 1.00 32.81  ? 232 ASP A CG  1 
ATOM   1777 O OD1 . ASP A 1 235 ? -13.730 21.591  -12.281 1.00 32.39  ? 232 ASP A OD1 1 
ATOM   1778 O OD2 . ASP A 1 235 ? -11.722 21.961  -11.433 1.00 35.51  ? 232 ASP A OD2 1 
ATOM   1779 N N   . LYS A 1 236 ? -13.989 21.117  -7.081  1.00 24.26  ? 233 LYS A N   1 
ATOM   1780 C CA  . LYS A 1 236 ? -14.176 20.493  -5.789  1.00 26.78  ? 233 LYS A CA  1 
ATOM   1781 C C   . LYS A 1 236 ? -14.236 21.585  -4.735  1.00 28.73  ? 233 LYS A C   1 
ATOM   1782 O O   . LYS A 1 236 ? -13.451 22.535  -4.770  1.00 34.29  ? 233 LYS A O   1 
ATOM   1783 C CB  . LYS A 1 236 ? -13.047 19.493  -5.440  1.00 24.97  ? 233 LYS A CB  1 
ATOM   1784 C CG  . LYS A 1 236 ? -12.648 18.495  -6.515  1.00 27.19  ? 233 LYS A CG  1 
ATOM   1785 C CD  . LYS A 1 236 ? -13.796 17.689  -7.059  1.00 30.00  ? 233 LYS A CD  1 
ATOM   1786 C CE  . LYS A 1 236 ? -13.301 16.437  -7.787  1.00 30.48  ? 233 LYS A CE  1 
ATOM   1787 N NZ  . LYS A 1 236 ? -13.427 16.504  -9.242  1.00 23.32  ? 233 LYS A NZ  1 
ATOM   1788 N N   . TYR A 1 237 ? -15.174 21.438  -3.804  1.00 24.55  ? 234 TYR A N   1 
ATOM   1789 C CA  . TYR A 1 237 ? -15.316 22.313  -2.648  1.00 25.07  ? 234 TYR A CA  1 
ATOM   1790 C C   . TYR A 1 237 ? -15.412 21.453  -1.383  1.00 31.20  ? 234 TYR A C   1 
ATOM   1791 O O   . TYR A 1 237 ? -16.345 20.650  -1.240  1.00 26.82  ? 234 TYR A O   1 
ATOM   1792 C CB  . TYR A 1 237 ? -16.556 23.184  -2.797  1.00 24.38  ? 234 TYR A CB  1 
ATOM   1793 C CG  . TYR A 1 237 ? -16.769 24.199  -1.693  1.00 27.19  ? 234 TYR A CG  1 
ATOM   1794 C CD1 . TYR A 1 237 ? -15.693 24.762  -1.028  1.00 26.25  ? 234 TYR A CD1 1 
ATOM   1795 C CD2 . TYR A 1 237 ? -18.055 24.595  -1.326  1.00 24.35  ? 234 TYR A CD2 1 
ATOM   1796 C CE1 . TYR A 1 237 ? -15.884 25.701  -0.037  1.00 27.39  ? 234 TYR A CE1 1 
ATOM   1797 C CE2 . TYR A 1 237 ? -18.252 25.522  -0.349  1.00 28.38  ? 234 TYR A CE2 1 
ATOM   1798 C CZ  . TYR A 1 237 ? -17.159 26.078  0.298   1.00 29.97  ? 234 TYR A CZ  1 
ATOM   1799 O OH  . TYR A 1 237 ? -17.341 27.017  1.280   1.00 29.65  ? 234 TYR A OH  1 
ATOM   1800 N N   . PHE A 1 238 ? -14.439 21.608  -0.480  1.00 24.72  ? 235 PHE A N   1 
ATOM   1801 C CA  . PHE A 1 238 ? -14.502 21.038  0.855   1.00 27.73  ? 235 PHE A CA  1 
ATOM   1802 C C   . PHE A 1 238 ? -14.908 22.178  1.796   1.00 30.45  ? 235 PHE A C   1 
ATOM   1803 O O   . PHE A 1 238 ? -14.153 23.138  1.980   1.00 30.40  ? 235 PHE A O   1 
ATOM   1804 C CB  . PHE A 1 238 ? -13.162 20.416  1.238   1.00 26.41  ? 235 PHE A CB  1 
ATOM   1805 C CG  . PHE A 1 238 ? -13.228 19.578  2.470   1.00 28.39  ? 235 PHE A CG  1 
ATOM   1806 C CD1 . PHE A 1 238 ? -13.199 20.163  3.734   1.00 26.30  ? 235 PHE A CD1 1 
ATOM   1807 C CD2 . PHE A 1 238 ? -13.349 18.202  2.376   1.00 27.52  ? 235 PHE A CD2 1 
ATOM   1808 C CE1 . PHE A 1 238 ? -13.273 19.388  4.875   1.00 23.98  ? 235 PHE A CE1 1 
ATOM   1809 C CE2 . PHE A 1 238 ? -13.428 17.424  3.517   1.00 24.92  ? 235 PHE A CE2 1 
ATOM   1810 C CZ  . PHE A 1 238 ? -13.396 18.023  4.767   1.00 23.65  ? 235 PHE A CZ  1 
ATOM   1811 N N   . ASP A 1 239 ? -16.107 22.086  2.369   1.00 27.90  ? 236 ASP A N   1 
ATOM   1812 C CA  . ASP A 1 239 ? -16.762 23.205  3.052   1.00 32.77  ? 236 ASP A CA  1 
ATOM   1813 C C   . ASP A 1 239 ? -16.821 22.965  4.561   1.00 31.40  ? 236 ASP A C   1 
ATOM   1814 O O   . ASP A 1 239 ? -17.453 22.011  5.021   1.00 28.48  ? 236 ASP A O   1 
ATOM   1815 C CB  . ASP A 1 239 ? -18.179 23.401  2.508   1.00 29.62  ? 236 ASP A CB  1 
ATOM   1816 C CG  . ASP A 1 239 ? -18.827 24.687  2.989   1.00 33.47  ? 236 ASP A CG  1 
ATOM   1817 O OD1 . ASP A 1 239 ? -18.125 25.561  3.542   1.00 35.38  ? 236 ASP A OD1 1 
ATOM   1818 O OD2 . ASP A 1 239 ? -20.050 24.839  2.793   1.00 36.36  ? 236 ASP A OD2 1 
ATOM   1819 N N   . SER A 1 240 ? -16.187 23.836  5.332   1.00 31.37  ? 237 SER A N   1 
ATOM   1820 C CA  . SER A 1 240 ? -16.363 23.805  6.779   1.00 36.99  ? 237 SER A CA  1 
ATOM   1821 C C   . SER A 1 240 ? -17.052 25.051  7.300   1.00 34.71  ? 237 SER A C   1 
ATOM   1822 O O   . SER A 1 240 ? -17.331 25.123  8.497   1.00 37.36  ? 237 SER A O   1 
ATOM   1823 C CB  . SER A 1 240 ? -15.015 23.626  7.495   1.00 29.85  ? 237 SER A CB  1 
ATOM   1824 O OG  . SER A 1 240 ? -14.495 22.331  7.270   1.00 35.62  ? 237 SER A OG  1 
ATOM   1825 N N   . ILE A 1 241 ? -17.354 26.016  6.430   1.00 36.16  ? 238 ILE A N   1 
ATOM   1826 C CA  . ILE A 1 241 ? -17.771 27.356  6.830   1.00 37.90  ? 238 ILE A CA  1 
ATOM   1827 C C   . ILE A 1 241 ? -19.240 27.621  6.502   1.00 39.61  ? 238 ILE A C   1 
ATOM   1828 O O   . ILE A 1 241 ? -19.977 28.148  7.333   1.00 37.87  ? 238 ILE A O   1 
ATOM   1829 C CB  . ILE A 1 241 ? -16.866 28.424  6.185   1.00 36.23  ? 238 ILE A CB  1 
ATOM   1830 C CG1 . ILE A 1 241 ? -15.405 28.185  6.585   1.00 38.48  ? 238 ILE A CG1 1 
ATOM   1831 C CG2 . ILE A 1 241 ? -17.372 29.814  6.532   1.00 37.41  ? 238 ILE A CG2 1 
ATOM   1832 C CD1 . ILE A 1 241 ? -15.199 27.919  8.053   1.00 42.44  ? 238 ILE A CD1 1 
ATOM   1833 N N   . GLY A 1 242 ? -19.677 27.283  5.286   1.00 36.35  ? 239 GLY A N   1 
ATOM   1834 C CA  . GLY A 1 242 ? -21.013 27.690  4.879   1.00 36.99  ? 239 GLY A CA  1 
ATOM   1835 C C   . GLY A 1 242 ? -21.133 29.208  4.738   1.00 38.44  ? 239 GLY A C   1 
ATOM   1836 O O   . GLY A 1 242 ? -20.146 29.940  4.607   1.00 40.55  ? 239 GLY A O   1 
ATOM   1837 N N   . GLY A 1 243 ? -22.377 29.683  4.796   1.00 41.91  ? 240 GLY A N   1 
ATOM   1838 C CA  . GLY A 1 243 ? -22.592 31.112  4.694   1.00 44.81  ? 240 GLY A CA  1 
ATOM   1839 C C   . GLY A 1 243 ? -22.198 31.655  3.330   1.00 44.08  ? 240 GLY A C   1 
ATOM   1840 O O   . GLY A 1 243 ? -22.333 30.989  2.296   1.00 45.72  ? 240 GLY A O   1 
ATOM   1841 N N   . SER A 1 244 ? -21.676 32.885  3.335   1.00 42.33  ? 241 SER A N   1 
ATOM   1842 C CA  . SER A 1 244 ? -21.541 33.650  2.099   1.00 47.42  ? 241 SER A CA  1 
ATOM   1843 C C   . SER A 1 244 ? -20.349 33.209  1.258   1.00 45.84  ? 241 SER A C   1 
ATOM   1844 O O   . SER A 1 244 ? -20.332 33.471  0.048   1.00 45.91  ? 241 SER A O   1 
ATOM   1845 C CB  . SER A 1 244 ? -21.443 35.150  2.406   1.00 47.45  ? 241 SER A CB  1 
ATOM   1846 O OG  . SER A 1 244 ? -20.193 35.466  2.975   1.00 47.14  ? 241 SER A OG  1 
ATOM   1847 N N   . VAL A 1 245 ? -19.359 32.552  1.859   1.00 38.02  ? 242 VAL A N   1 
ATOM   1848 C CA  . VAL A 1 245 ? -18.320 31.947  1.037   1.00 38.47  ? 242 VAL A CA  1 
ATOM   1849 C C   . VAL A 1 245 ? -18.867 30.728  0.314   1.00 36.56  ? 242 VAL A C   1 
ATOM   1850 O O   . VAL A 1 245 ? -18.464 30.443  -0.813  1.00 35.33  ? 242 VAL A O   1 
ATOM   1851 C CB  . VAL A 1 245 ? -17.077 31.582  1.876   1.00 46.45  ? 242 VAL A CB  1 
ATOM   1852 C CG1 . VAL A 1 245 ? -17.439 30.596  2.994   1.00 40.63  ? 242 VAL A CG1 1 
ATOM   1853 C CG2 . VAL A 1 245 ? -15.996 30.988  1.002   1.00 34.27  ? 242 VAL A CG2 1 
ATOM   1854 N N   . THR A 1 246 ? -19.773 29.976  0.942   1.00 36.21  ? 243 THR A N   1 
ATOM   1855 C CA  . THR A 1 246 ? -20.361 28.839  0.246   1.00 35.06  ? 243 THR A CA  1 
ATOM   1856 C C   . THR A 1 246 ? -21.341 29.303  -0.814  1.00 34.20  ? 243 THR A C   1 
ATOM   1857 O O   . THR A 1 246 ? -21.410 28.711  -1.896  1.00 37.97  ? 243 THR A O   1 
ATOM   1858 C CB  . THR A 1 246 ? -21.043 27.895  1.231   1.00 36.96  ? 243 THR A CB  1 
ATOM   1859 O OG1 . THR A 1 246 ? -20.032 27.148  1.916   1.00 34.66  ? 243 THR A OG1 1 
ATOM   1860 C CG2 . THR A 1 246 ? -21.995 26.933  0.512   1.00 26.76  ? 243 THR A CG2 1 
ATOM   1861 N N   . ASP A 1 247 ? -22.097 30.371  -0.528  1.00 39.96  ? 244 ASP A N   1 
ATOM   1862 C CA  . ASP A 1 247 ? -22.941 30.986  -1.557  1.00 41.78  ? 244 ASP A CA  1 
ATOM   1863 C C   . ASP A 1 247 ? -22.103 31.407  -2.764  1.00 38.54  ? 244 ASP A C   1 
ATOM   1864 O O   . ASP A 1 247 ? -22.525 31.246  -3.917  1.00 33.62  ? 244 ASP A O   1 
ATOM   1865 C CB  . ASP A 1 247 ? -23.687 32.208  -0.996  1.00 39.43  ? 244 ASP A CB  1 
ATOM   1866 C CG  . ASP A 1 247 ? -24.596 31.887  0.207   1.00 46.06  ? 244 ASP A CG  1 
ATOM   1867 O OD1 . ASP A 1 247 ? -25.255 30.812  0.257   1.00 44.68  ? 244 ASP A OD1 1 
ATOM   1868 O OD2 . ASP A 1 247 ? -24.664 32.764  1.103   1.00 46.42  ? 244 ASP A OD2 1 
ATOM   1869 N N   . ALA A 1 248 ? -20.909 31.948  -2.507  1.00 35.53  ? 245 ALA A N   1 
ATOM   1870 C CA  . ALA A 1 248 ? -20.027 32.377  -3.577  1.00 33.14  ? 245 ALA A CA  1 
ATOM   1871 C C   . ALA A 1 248 ? -19.562 31.194  -4.421  1.00 36.04  ? 245 ALA A C   1 
ATOM   1872 O O   . ALA A 1 248 ? -19.631 31.240  -5.653  1.00 38.94  ? 245 ALA A O   1 
ATOM   1873 C CB  . ALA A 1 248 ? -18.841 33.123  -2.982  1.00 36.01  ? 245 ALA A CB  1 
ATOM   1874 N N   . VAL A 1 249 ? -19.085 30.125  -3.776  1.00 31.35  ? 246 VAL A N   1 
ATOM   1875 C CA  . VAL A 1 249 ? -18.572 28.973  -4.513  1.00 31.50  ? 246 VAL A CA  1 
ATOM   1876 C C   . VAL A 1 249 ? -19.663 28.353  -5.375  1.00 32.57  ? 246 VAL A C   1 
ATOM   1877 O O   . VAL A 1 249 ? -19.396 27.867  -6.476  1.00 28.95  ? 246 VAL A O   1 
ATOM   1878 C CB  . VAL A 1 249 ? -17.962 27.928  -3.552  1.00 32.85  ? 246 VAL A CB  1 
ATOM   1879 C CG1 . VAL A 1 249 ? -17.512 26.705  -4.332  1.00 30.82  ? 246 VAL A CG1 1 
ATOM   1880 C CG2 . VAL A 1 249 ? -16.787 28.499  -2.798  1.00 28.07  ? 246 VAL A CG2 1 
ATOM   1881 N N   . PHE A 1 250 ? -20.910 28.388  -4.911  1.00 35.85  ? 247 PHE A N   1 
ATOM   1882 C CA  . PHE A 1 250 ? -21.995 27.750  -5.648  1.00 31.49  ? 247 PHE A CA  1 
ATOM   1883 C C   . PHE A 1 250 ? -22.377 28.515  -6.906  1.00 32.71  ? 247 PHE A C   1 
ATOM   1884 O O   . PHE A 1 250 ? -23.034 27.950  -7.789  1.00 40.04  ? 247 PHE A O   1 
ATOM   1885 C CB  . PHE A 1 250 ? -23.210 27.575  -4.732  1.00 28.05  ? 247 PHE A CB  1 
ATOM   1886 C CG  . PHE A 1 250 ? -23.267 26.241  -4.084  1.00 27.68  ? 247 PHE A CG  1 
ATOM   1887 C CD1 . PHE A 1 250 ? -22.244 25.824  -3.240  1.00 25.93  ? 247 PHE A CD1 1 
ATOM   1888 C CD2 . PHE A 1 250 ? -24.328 25.375  -4.337  1.00 34.32  ? 247 PHE A CD2 1 
ATOM   1889 C CE1 . PHE A 1 250 ? -22.281 24.566  -2.657  1.00 25.66  ? 247 PHE A CE1 1 
ATOM   1890 C CE2 . PHE A 1 250 ? -24.379 24.106  -3.752  1.00 34.33  ? 247 PHE A CE2 1 
ATOM   1891 C CZ  . PHE A 1 250 ? -23.352 23.704  -2.910  1.00 27.49  ? 247 PHE A CZ  1 
ATOM   1892 N N   . SER A 1 251 ? -21.987 29.781  -7.014  1.00 31.22  ? 248 SER A N   1 
ATOM   1893 C CA  . SER A 1 251 ? -22.235 30.528  -8.237  1.00 33.82  ? 248 SER A CA  1 
ATOM   1894 C C   . SER A 1 251 ? -21.287 30.137  -9.362  1.00 33.35  ? 248 SER A C   1 
ATOM   1895 O O   . SER A 1 251 ? -21.595 30.415  -10.523 1.00 34.50  ? 248 SER A O   1 
ATOM   1896 C CB  . SER A 1 251 ? -22.094 32.023  -7.978  1.00 35.70  ? 248 SER A CB  1 
ATOM   1897 O OG  . SER A 1 251 ? -20.742 32.332  -7.693  1.00 36.12  ? 248 SER A OG  1 
ATOM   1898 N N   . MET A 1 252 ? -20.148 29.496  -9.043  1.00 32.49  ? 249 MET A N   1 
ATOM   1899 C CA  . MET A 1 252 ? -19.102 29.188  -10.015 1.00 30.81  ? 249 MET A CA  1 
ATOM   1900 C C   . MET A 1 252 ? -18.755 27.696  -10.047 1.00 26.45  ? 249 MET A C   1 
ATOM   1901 O O   . MET A 1 252 ? -17.609 27.329  -10.307 1.00 29.18  ? 249 MET A O   1 
ATOM   1902 C CB  . MET A 1 252 ? -17.845 30.028  -9.751  1.00 26.21  ? 249 MET A CB  1 
ATOM   1903 C CG  . MET A 1 252 ? -17.230 29.892  -8.339  1.00 34.99  ? 249 MET A CG  1 
ATOM   1904 S SD  . MET A 1 252 ? -16.085 31.234  -7.887  1.00 40.56  ? 249 MET A SD  1 
ATOM   1905 C CE  . MET A 1 252 ? -17.256 32.570  -7.996  1.00 41.53  ? 249 MET A CE  1 
ATOM   1906 N N   . LEU A 1 253 ? -19.724 26.821  -9.807  1.00 22.63  ? 250 LEU A N   1 
ATOM   1907 C CA  . LEU A 1 253 ? -19.469 25.383  -9.878  1.00 30.31  ? 250 LEU A CA  1 
ATOM   1908 C C   . LEU A 1 253 ? -19.332 24.917  -11.326 1.00 29.13  ? 250 LEU A C   1 
ATOM   1909 O O   . LEU A 1 253 ? -20.156 25.265  -12.180 1.00 28.43  ? 250 LEU A O   1 
ATOM   1910 C CB  . LEU A 1 253 ? -20.580 24.595  -9.179  1.00 25.88  ? 250 LEU A CB  1 
ATOM   1911 C CG  . LEU A 1 253 ? -20.621 24.791  -7.656  1.00 30.59  ? 250 LEU A CG  1 
ATOM   1912 C CD1 . LEU A 1 253 ? -21.928 24.271  -7.118  1.00 30.05  ? 250 LEU A CD1 1 
ATOM   1913 C CD2 . LEU A 1 253 ? -19.433 24.118  -6.952  1.00 19.37  ? 250 LEU A CD2 1 
ATOM   1914 N N   . ASN A 1 254 ? -18.291 24.124  -11.591 1.00 25.88  ? 251 ASN A N   1 
ATOM   1915 C CA  . ASN A 1 254 ? -18.045 23.527  -12.895 1.00 24.44  ? 251 ASN A CA  1 
ATOM   1916 C C   . ASN A 1 254 ? -18.860 22.248  -13.073 1.00 25.40  ? 251 ASN A C   1 
ATOM   1917 O O   . ASN A 1 254 ? -19.492 21.734  -12.147 1.00 28.21  ? 251 ASN A O   1 
ATOM   1918 C CB  . ASN A 1 254 ? -16.560 23.213  -13.081 1.00 25.73  ? 251 ASN A CB  1 
ATOM   1919 C CG  . ASN A 1 254 ? -15.712 24.448  -13.320 1.00 23.73  ? 251 ASN A CG  1 
ATOM   1920 O OD1 . ASN A 1 254 ? -16.195 25.459  -13.813 1.00 30.14  ? 251 ASN A OD1 1 
ATOM   1921 N ND2 . ASN A 1 254 ? -14.430 24.359  -12.991 1.00 21.89  ? 251 ASN A ND2 1 
ATOM   1922 N N   . VAL A 1 255 ? -18.824 21.720  -14.294 1.00 28.80  ? 252 VAL A N   1 
ATOM   1923 C CA  . VAL A 1 255 ? -19.647 20.572  -14.635 1.00 27.50  ? 252 VAL A CA  1 
ATOM   1924 C C   . VAL A 1 255 ? -19.068 19.315  -14.000 1.00 27.25  ? 252 VAL A C   1 
ATOM   1925 O O   . VAL A 1 255 ? -17.858 19.069  -14.064 1.00 29.18  ? 252 VAL A O   1 
ATOM   1926 C CB  . VAL A 1 255 ? -19.778 20.459  -16.159 1.00 25.01  ? 252 VAL A CB  1 
ATOM   1927 C CG1 . VAL A 1 255 ? -20.230 19.054  -16.588 1.00 21.08  ? 252 VAL A CG1 1 
ATOM   1928 C CG2 . VAL A 1 255 ? -20.778 21.490  -16.622 1.00 25.54  ? 252 VAL A CG2 1 
ATOM   1929 N N   . GLY A 1 256 ? -19.934 18.518  -13.373 1.00 24.52  ? 253 GLY A N   1 
ATOM   1930 C CA  . GLY A 1 256 ? -19.470 17.349  -12.658 1.00 27.02  ? 253 GLY A CA  1 
ATOM   1931 C C   . GLY A 1 256 ? -18.698 17.655  -11.398 1.00 28.54  ? 253 GLY A C   1 
ATOM   1932 O O   . GLY A 1 256 ? -17.904 16.831  -10.962 1.00 28.08  ? 253 GLY A O   1 
ATOM   1933 N N   . SER A 1 257 ? -18.914 18.823  -10.800 1.00 27.26  ? 254 SER A N   1 
ATOM   1934 C CA  . SER A 1 257 ? -18.228 19.192  -9.580  1.00 30.35  ? 254 SER A CA  1 
ATOM   1935 C C   . SER A 1 257 ? -18.761 18.391  -8.374  1.00 29.50  ? 254 SER A C   1 
ATOM   1936 O O   . SER A 1 257 ? -19.776 17.692  -8.441  1.00 28.39  ? 254 SER A O   1 
ATOM   1937 C CB  . SER A 1 257 ? -18.366 20.693  -9.356  1.00 28.08  ? 254 SER A CB  1 
ATOM   1938 O OG  . SER A 1 257 ? -19.695 21.092  -9.608  1.00 29.95  ? 254 SER A OG  1 
ATOM   1939 N N   . GLN A 1 258 ? -18.031 18.491  -7.263  1.00 24.46  ? 255 GLN A N   1 
ATOM   1940 C CA  . GLN A 1 258 ? -18.307 17.750  -6.038  1.00 28.68  ? 255 GLN A CA  1 
ATOM   1941 C C   . GLN A 1 258 ? -18.110 18.652  -4.827  1.00 28.04  ? 255 GLN A C   1 
ATOM   1942 O O   . GLN A 1 258 ? -17.050 19.272  -4.682  1.00 26.86  ? 255 GLN A O   1 
ATOM   1943 C CB  . GLN A 1 258 ? -17.384 16.545  -5.888  1.00 27.35  ? 255 GLN A CB  1 
ATOM   1944 C CG  . GLN A 1 258 ? -17.544 15.454  -6.892  1.00 25.30  ? 255 GLN A CG  1 
ATOM   1945 C CD  . GLN A 1 258 ? -16.655 14.292  -6.542  1.00 27.79  ? 255 GLN A CD  1 
ATOM   1946 O OE1 . GLN A 1 258 ? -15.420 14.398  -6.567  1.00 27.87  ? 255 GLN A OE1 1 
ATOM   1947 N NE2 . GLN A 1 258 ? -17.270 13.184  -6.168  1.00 30.55  ? 255 GLN A NE2 1 
ATOM   1948 N N   . VAL A 1 259 ? -19.109 18.684  -3.945  1.00 24.25  ? 256 VAL A N   1 
ATOM   1949 C CA  . VAL A 1 259 ? -19.079 19.469  -2.718  1.00 23.54  ? 256 VAL A CA  1 
ATOM   1950 C C   . VAL A 1 259 ? -19.187 18.521  -1.522  1.00 26.47  ? 256 VAL A C   1 
ATOM   1951 O O   . VAL A 1 259 ? -20.089 17.674  -1.460  1.00 26.69  ? 256 VAL A O   1 
ATOM   1952 C CB  . VAL A 1 259 ? -20.204 20.521  -2.704  1.00 26.25  ? 256 VAL A CB  1 
ATOM   1953 C CG1 . VAL A 1 259 ? -20.321 21.160  -1.326  1.00 25.65  ? 256 VAL A CG1 1 
ATOM   1954 C CG2 . VAL A 1 259 ? -19.939 21.586  -3.761  1.00 22.18  ? 256 VAL A CG2 1 
ATOM   1955 N N   . ALA A 1 260 ? -18.257 18.647  -0.586  1.00 27.11  ? 257 ALA A N   1 
ATOM   1956 C CA  . ALA A 1 260 ? -18.295 17.897  0.656   1.00 22.89  ? 257 ALA A CA  1 
ATOM   1957 C C   . ALA A 1 260 ? -18.585 18.876  1.788   1.00 27.52  ? 257 ALA A C   1 
ATOM   1958 O O   . ALA A 1 260 ? -17.809 19.809  2.014   1.00 25.83  ? 257 ALA A O   1 
ATOM   1959 C CB  . ALA A 1 260 ? -16.986 17.152  0.881   1.00 21.84  ? 257 ALA A CB  1 
ATOM   1960 N N   . VAL A 1 261 ? -19.710 18.676  2.477   1.00 29.28  ? 258 VAL A N   1 
ATOM   1961 C CA  . VAL A 1 261 ? -20.113 19.502  3.606   1.00 27.97  ? 258 VAL A CA  1 
ATOM   1962 C C   . VAL A 1 261 ? -19.630 18.805  4.869   1.00 31.08  ? 258 VAL A C   1 
ATOM   1963 O O   . VAL A 1 261 ? -20.235 17.842  5.350   1.00 33.27  ? 258 VAL A O   1 
ATOM   1964 C CB  . VAL A 1 261 ? -21.621 19.743  3.646   1.00 30.26  ? 258 VAL A CB  1 
ATOM   1965 C CG1 . VAL A 1 261 ? -21.938 20.883  4.629   1.00 26.36  ? 258 VAL A CG1 1 
ATOM   1966 C CG2 . VAL A 1 261 ? -22.148 20.040  2.244   1.00 29.00  ? 258 VAL A CG2 1 
ATOM   1967 N N   . CYS A 1 262 ? -18.542 19.324  5.408   1.00 28.84  ? 259 CYS A N   1 
ATOM   1968 C CA  . CYS A 1 262 ? -17.929 18.874  6.640   1.00 31.45  ? 259 CYS A CA  1 
ATOM   1969 C C   . CYS A 1 262 ? -18.450 19.639  7.861   1.00 37.55  ? 259 CYS A C   1 
ATOM   1970 O O   . CYS A 1 262 ? -18.676 19.039  8.917   1.00 40.27  ? 259 CYS A O   1 
ATOM   1971 C CB  . CYS A 1 262 ? -16.418 19.019  6.492   1.00 33.96  ? 259 CYS A CB  1 
ATOM   1972 S SG  . CYS A 1 262 ? -15.486 18.630  7.914   1.00 40.37  ? 259 CYS A SG  1 
ATOM   1973 N N   . TRP A 1 263 ? -18.676 20.945  7.743   1.00 34.84  ? 260 TRP A N   1 
ATOM   1974 C CA  . TRP A 1 263 ? -19.228 21.723  8.844   1.00 35.54  ? 260 TRP A CA  1 
ATOM   1975 C C   . TRP A 1 263 ? -19.826 23.006  8.269   1.00 36.37  ? 260 TRP A C   1 
ATOM   1976 O O   . TRP A 1 263 ? -19.570 23.367  7.119   1.00 33.53  ? 260 TRP A O   1 
ATOM   1977 C CB  . TRP A 1 263 ? -18.149 22.003  9.908   1.00 40.12  ? 260 TRP A CB  1 
ATOM   1978 C CG  . TRP A 1 263 ? -18.681 22.009  11.315  1.00 45.32  ? 260 TRP A CG  1 
ATOM   1979 C CD1 . TRP A 1 263 ? -19.492 21.060  11.893  1.00 47.40  ? 260 TRP A CD1 1 
ATOM   1980 C CD2 . TRP A 1 263 ? -18.463 23.011  12.322  1.00 48.36  ? 260 TRP A CD2 1 
ATOM   1981 N NE1 . TRP A 1 263 ? -19.800 21.420  13.190  1.00 42.95  ? 260 TRP A NE1 1 
ATOM   1982 C CE2 . TRP A 1 263 ? -19.178 22.606  13.482  1.00 47.24  ? 260 TRP A CE2 1 
ATOM   1983 C CE3 . TRP A 1 263 ? -17.737 24.207  12.363  1.00 47.05  ? 260 TRP A CE3 1 
ATOM   1984 C CZ2 . TRP A 1 263 ? -19.180 23.356  14.664  1.00 42.65  ? 260 TRP A CZ2 1 
ATOM   1985 C CZ3 . TRP A 1 263 ? -17.750 24.954  13.547  1.00 48.87  ? 260 TRP A CZ3 1 
ATOM   1986 C CH2 . TRP A 1 263 ? -18.464 24.521  14.676  1.00 43.81  ? 260 TRP A CH2 1 
ATOM   1987 N N   . GLN A 1 264 ? -20.637 23.695  9.080   1.00 38.19  ? 261 GLN A N   1 
ATOM   1988 C CA  . GLN A 1 264 ? -21.230 24.978  8.691   1.00 32.36  ? 261 GLN A CA  1 
ATOM   1989 C C   . GLN A 1 264 ? -21.026 26.018  9.799   1.00 36.61  ? 261 GLN A C   1 
ATOM   1990 O O   . GLN A 1 264 ? -21.977 26.582  10.336  1.00 41.98  ? 261 GLN A O   1 
ATOM   1991 C CB  . GLN A 1 264 ? -22.710 24.828  8.359   1.00 31.43  ? 261 GLN A CB  1 
ATOM   1992 C CG  . GLN A 1 264 ? -22.994 23.905  7.178   1.00 39.29  ? 261 GLN A CG  1 
ATOM   1993 C CD  . GLN A 1 264 ? -22.698 24.553  5.820   1.00 40.27  ? 261 GLN A CD  1 
ATOM   1994 O OE1 . GLN A 1 264 ? -23.595 25.110  5.176   1.00 45.80  ? 261 GLN A OE1 1 
ATOM   1995 N NE2 . GLN A 1 264 ? -21.439 24.483  5.386   1.00 33.15  ? 261 GLN A NE2 1 
ATOM   1996 N N   . TRP A 1 265 ? -19.761 26.296  10.115  1.00 33.31  ? 262 TRP A N   1 
ATOM   1997 C CA  . TRP A 1 265 ? -19.415 27.242  11.177  1.00 36.50  ? 262 TRP A CA  1 
ATOM   1998 C C   . TRP A 1 265 ? -20.230 28.532  11.122  1.00 40.94  ? 262 TRP A C   1 
ATOM   1999 O O   . TRP A 1 265 ? -20.653 29.050  12.159  1.00 47.29  ? 262 TRP A O   1 
ATOM   2000 C CB  . TRP A 1 265 ? -17.925 27.557  11.094  1.00 36.91  ? 262 TRP A CB  1 
ATOM   2001 C CG  . TRP A 1 265 ? -17.387 28.547  12.083  1.00 46.33  ? 262 TRP A CG  1 
ATOM   2002 C CD1 . TRP A 1 265 ? -17.856 29.808  12.362  1.00 46.50  ? 262 TRP A CD1 1 
ATOM   2003 C CD2 . TRP A 1 265 ? -16.223 28.372  12.882  1.00 50.50  ? 262 TRP A CD2 1 
ATOM   2004 N NE1 . TRP A 1 265 ? -17.067 30.406  13.305  1.00 47.27  ? 262 TRP A NE1 1 
ATOM   2005 C CE2 . TRP A 1 265 ? -16.057 29.544  13.642  1.00 50.38  ? 262 TRP A CE2 1 
ATOM   2006 C CE3 . TRP A 1 265 ? -15.306 27.326  13.041  1.00 52.18  ? 262 TRP A CE3 1 
ATOM   2007 C CZ2 . TRP A 1 265 ? -15.005 29.700  14.534  1.00 55.30  ? 262 TRP A CZ2 1 
ATOM   2008 C CZ3 . TRP A 1 265 ? -14.276 27.479  13.923  1.00 54.34  ? 262 TRP A CZ3 1 
ATOM   2009 C CH2 . TRP A 1 265 ? -14.124 28.655  14.660  1.00 56.53  ? 262 TRP A CH2 1 
ATOM   2010 N N   . ALA A 1 266 ? -20.428 29.095  9.934   1.00 44.38  ? 263 ALA A N   1 
ATOM   2011 C CA  . ALA A 1 266 ? -21.136 30.365  9.865   1.00 46.06  ? 263 ALA A CA  1 
ATOM   2012 C C   . ALA A 1 266 ? -22.603 30.231  10.244  1.00 43.92  ? 263 ALA A C   1 
ATOM   2013 O O   . ALA A 1 266 ? -23.231 31.233  10.585  1.00 49.34  ? 263 ALA A O   1 
ATOM   2014 C CB  . ALA A 1 266 ? -21.003 30.967  8.467   1.00 49.70  ? 263 ALA A CB  1 
ATOM   2015 N N   . THR A 1 267 ? -23.172 29.030  10.178  1.00 41.36  ? 264 THR A N   1 
ATOM   2016 C CA  . THR A 1 267 ? -24.514 28.803  10.712  1.00 47.16  ? 264 THR A CA  1 
ATOM   2017 C C   . THR A 1 267 ? -24.462 28.415  12.198  1.00 50.71  ? 264 THR A C   1 
ATOM   2018 O O   . THR A 1 267 ? -24.998 29.134  13.045  1.00 56.72  ? 264 THR A O   1 
ATOM   2019 C CB  . THR A 1 267 ? -25.232 27.736  9.870   1.00 47.47  ? 264 THR A CB  1 
ATOM   2020 O OG1 . THR A 1 267 ? -25.444 28.243  8.549   1.00 54.93  ? 264 THR A OG1 1 
ATOM   2021 C CG2 . THR A 1 267 ? -26.575 27.358  10.464  1.00 47.74  ? 264 THR A CG2 1 
ATOM   2022 N N   . GLN A 1 268 ? -23.774 27.310  12.528  1.00 45.62  ? 265 GLN A N   1 
ATOM   2023 C CA  . GLN A 1 268 ? -23.696 26.823  13.908  1.00 47.27  ? 265 GLN A CA  1 
ATOM   2024 C C   . GLN A 1 268 ? -23.220 27.903  14.881  1.00 50.13  ? 265 GLN A C   1 
ATOM   2025 O O   . GLN A 1 268 ? -23.814 28.098  15.945  1.00 55.33  ? 265 GLN A O   1 
ATOM   2026 C CB  . GLN A 1 268 ? -22.772 25.605  13.979  1.00 44.19  ? 265 GLN A CB  1 
ATOM   2027 C CG  . GLN A 1 268 ? -22.316 25.259  15.383  1.00 50.94  ? 265 GLN A CG  1 
ATOM   2028 C CD  . GLN A 1 268 ? -23.440 24.671  16.224  1.00 58.63  ? 265 GLN A CD  1 
ATOM   2029 O OE1 . GLN A 1 268 ? -24.256 23.898  15.710  1.00 61.20  ? 265 GLN A OE1 1 
ATOM   2030 N NE2 . GLN A 1 268 ? -23.499 25.038  17.520  1.00 47.47  ? 265 GLN A NE2 1 
ATOM   2031 N N   . VAL A 1 269 ? -22.157 28.619  14.534  1.00 44.34  ? 266 VAL A N   1 
ATOM   2032 C CA  . VAL A 1 269 ? -21.514 29.548  15.450  1.00 48.30  ? 266 VAL A CA  1 
ATOM   2033 C C   . VAL A 1 269 ? -22.009 30.974  15.252  1.00 50.30  ? 266 VAL A C   1 
ATOM   2034 O O   . VAL A 1 269 ? -22.154 31.716  16.219  1.00 54.07  ? 266 VAL A O   1 
ATOM   2035 C CB  . VAL A 1 269 ? -19.974 29.467  15.307  1.00 55.32  ? 266 VAL A CB  1 
ATOM   2036 C CG1 . VAL A 1 269 ? -19.292 30.565  16.118  1.00 48.25  ? 266 VAL A CG1 1 
ATOM   2037 C CG2 . VAL A 1 269 ? -19.439 28.067  15.698  1.00 45.66  ? 266 VAL A CG2 1 
ATOM   2038 N N   . GLN A 1 270 ? -22.256 31.394  14.019  1.00 52.90  ? 267 GLN A N   1 
ATOM   2039 C CA  . GLN A 1 270 ? -22.691 32.763  13.771  1.00 52.99  ? 267 GLN A CA  1 
ATOM   2040 C C   . GLN A 1 270 ? -24.188 32.882  13.517  1.00 48.47  ? 267 GLN A C   1 
ATOM   2041 O O   . GLN A 1 270 ? -24.648 33.962  13.146  1.00 50.05  ? 267 GLN A O   1 
ATOM   2042 C CB  . GLN A 1 270 ? -21.939 33.372  12.591  1.00 51.00  ? 267 GLN A CB  1 
ATOM   2043 C CG  . GLN A 1 270 ? -20.499 33.737  12.849  1.00 55.33  ? 267 GLN A CG  1 
ATOM   2044 C CD  . GLN A 1 270 ? -19.810 34.184  11.555  1.00 70.04  ? 267 GLN A CD  1 
ATOM   2045 O OE1 . GLN A 1 270 ? -20.196 33.768  10.457  1.00 58.80  ? 267 GLN A OE1 1 
ATOM   2046 N NE2 . GLN A 1 270 ? -18.799 35.042  11.680  1.00 71.78  ? 267 GLN A NE2 1 
ATOM   2047 N N   . ARG A 1 271 ? -24.947 31.805  13.682  1.00 46.69  ? 268 ARG A N   1 
ATOM   2048 C CA  . ARG A 1 271 ? -26.407 31.859  13.674  1.00 52.29  ? 268 ARG A CA  1 
ATOM   2049 C C   . ARG A 1 271 ? -26.956 32.504  12.397  1.00 55.44  ? 268 ARG A C   1 
ATOM   2050 O O   . ARG A 1 271 ? -27.875 33.324  12.425  1.00 56.34  ? 268 ARG A O   1 
ATOM   2051 C CB  . ARG A 1 271 ? -26.911 32.568  14.927  1.00 54.53  ? 268 ARG A CB  1 
ATOM   2052 C CG  . ARG A 1 271 ? -26.476 31.857  16.204  1.00 60.44  ? 268 ARG A CG  1 
ATOM   2053 C CD  . ARG A 1 271 ? -27.099 32.427  17.469  1.00 58.24  ? 268 ARG A CD  1 
ATOM   2054 N NE  . ARG A 1 271 ? -26.931 33.872  17.583  1.00 60.61  ? 268 ARG A NE  1 
ATOM   2055 C CZ  . ARG A 1 271 ? -27.886 34.762  17.334  1.00 61.34  ? 268 ARG A CZ  1 
ATOM   2056 N NH1 . ARG A 1 271 ? -29.096 34.388  16.937  1.00 57.26  ? 268 ARG A NH1 1 
ATOM   2057 N NH2 . ARG A 1 271 ? -27.626 36.057  17.503  1.00 63.06  ? 268 ARG A NH2 1 
ATOM   2058 N N   . ASP A 1 272 ? -26.381 32.101  11.261  1.00 57.43  ? 269 ASP A N   1 
ATOM   2059 C CA  . ASP A 1 272 ? -26.769 32.572  9.930   1.00 50.27  ? 269 ASP A CA  1 
ATOM   2060 C C   . ASP A 1 272 ? -27.655 31.488  9.328   1.00 46.06  ? 269 ASP A C   1 
ATOM   2061 O O   . ASP A 1 272 ? -27.179 30.569  8.671   1.00 52.56  ? 269 ASP A O   1 
ATOM   2062 C CB  . ASP A 1 272 ? -25.519 32.844  9.092   1.00 52.34  ? 269 ASP A CB  1 
ATOM   2063 C CG  . ASP A 1 272 ? -25.810 33.585  7.775   1.00 65.59  ? 269 ASP A CG  1 
ATOM   2064 O OD1 . ASP A 1 272 ? -26.694 33.139  7.000   1.00 66.07  ? 269 ASP A OD1 1 
ATOM   2065 O OD2 . ASP A 1 272 ? -25.128 34.608  7.502   1.00 62.41  ? 269 ASP A OD2 1 
ATOM   2066 N N   . TYR A 1 273 ? -28.958 31.585  9.560   1.00 49.71  ? 270 TYR A N   1 
ATOM   2067 C CA  . TYR A 1 273 ? -29.855 30.486  9.203   1.00 52.22  ? 270 TYR A CA  1 
ATOM   2068 C C   . TYR A 1 273 ? -30.479 30.623  7.816   1.00 50.73  ? 270 TYR A C   1 
ATOM   2069 O O   . TYR A 1 273 ? -30.866 29.611  7.219   1.00 49.47  ? 270 TYR A O   1 
ATOM   2070 C CB  . TYR A 1 273 ? -30.964 30.347  10.263  1.00 51.89  ? 270 TYR A CB  1 
ATOM   2071 C CG  . TYR A 1 273 ? -30.418 30.125  11.661  1.00 60.20  ? 270 TYR A CG  1 
ATOM   2072 C CD1 . TYR A 1 273 ? -29.832 28.904  12.012  1.00 61.71  ? 270 TYR A CD1 1 
ATOM   2073 C CD2 . TYR A 1 273 ? -30.459 31.137  12.623  1.00 59.46  ? 270 TYR A CD2 1 
ATOM   2074 C CE1 . TYR A 1 273 ? -29.305 28.689  13.288  1.00 60.13  ? 270 TYR A CE1 1 
ATOM   2075 C CE2 . TYR A 1 273 ? -29.942 30.932  13.907  1.00 64.06  ? 270 TYR A CE2 1 
ATOM   2076 C CZ  . TYR A 1 273 ? -29.368 29.704  14.232  1.00 64.58  ? 270 TYR A CZ  1 
ATOM   2077 O OH  . TYR A 1 273 ? -28.851 29.497  15.495  1.00 63.72  ? 270 TYR A OH  1 
ATOM   2078 N N   . HIS A 1 274 ? -30.592 31.830  7.286   1.00 48.90  ? 271 HIS A N   1 
ATOM   2079 C CA  . HIS A 1 274 ? -31.267 32.032  6.020   1.00 53.98  ? 271 HIS A CA  1 
ATOM   2080 C C   . HIS A 1 274 ? -30.285 32.598  5.013   1.00 52.66  ? 271 HIS A C   1 
ATOM   2081 O O   . HIS A 1 274 ? -29.327 33.292  5.372   1.00 51.38  ? 271 HIS A O   1 
ATOM   2082 C CB  . HIS A 1 274 ? -32.495 32.937  6.175   1.00 48.80  ? 271 HIS A CB  1 
ATOM   2083 C CG  . HIS A 1 274 ? -33.638 32.255  6.866   1.00 62.53  ? 271 HIS A CG  1 
ATOM   2084 N ND1 . HIS A 1 274 ? -33.580 31.865  8.188   1.00 65.43  ? 271 HIS A ND1 1 
ATOM   2085 C CD2 . HIS A 1 274 ? -34.851 31.854  6.411   1.00 65.24  ? 271 HIS A CD2 1 
ATOM   2086 C CE1 . HIS A 1 274 ? -34.712 31.267  8.521   1.00 64.11  ? 271 HIS A CE1 1 
ATOM   2087 N NE2 . HIS A 1 274 ? -35.502 31.249  7.463   1.00 59.26  ? 271 HIS A NE2 1 
ATOM   2088 N N   . GLY A 1 275 ? -30.516 32.262  3.752   1.00 48.35  ? 272 GLY A N   1 
ATOM   2089 C CA  . GLY A 1 275 ? -29.636 32.707  2.702   1.00 52.75  ? 272 GLY A CA  1 
ATOM   2090 C C   . GLY A 1 275 ? -30.124 32.331  1.324   1.00 46.65  ? 272 GLY A C   1 
ATOM   2091 O O   . GLY A 1 275 ? -31.166 31.691  1.150   1.00 45.13  ? 272 GLY A O   1 
ATOM   2092 N N   . PRO A 1 276 ? -29.365 32.729  0.312   1.00 47.18  ? 273 PRO A N   1 
ATOM   2093 C CA  . PRO A 1 276 ? -29.762 32.427  -1.072  1.00 44.70  ? 273 PRO A CA  1 
ATOM   2094 C C   . PRO A 1 276 ? -29.899 30.925  -1.280  1.00 42.54  ? 273 PRO A C   1 
ATOM   2095 O O   . PRO A 1 276 ? -29.052 30.145  -0.836  1.00 38.80  ? 273 PRO A O   1 
ATOM   2096 C CB  . PRO A 1 276 ? -28.622 33.024  -1.904  1.00 40.21  ? 273 PRO A CB  1 
ATOM   2097 C CG  . PRO A 1 276 ? -27.477 33.239  -0.935  1.00 41.86  ? 273 PRO A CG  1 
ATOM   2098 C CD  . PRO A 1 276 ? -28.090 33.462  0.404   1.00 42.77  ? 273 PRO A CD  1 
ATOM   2099 N N   . ARG A 1 277 ? -30.996 30.517  -1.931  1.00 36.35  ? 274 ARG A N   1 
ATOM   2100 C CA  . ARG A 1 277 ? -31.212 29.098  -2.183  1.00 38.53  ? 274 ARG A CA  1 
ATOM   2101 C C   . ARG A 1 277 ? -30.131 28.560  -3.106  1.00 41.90  ? 274 ARG A C   1 
ATOM   2102 O O   . ARG A 1 277 ? -29.838 29.153  -4.144  1.00 36.80  ? 274 ARG A O   1 
ATOM   2103 C CB  . ARG A 1 277 ? -32.589 28.866  -2.776  1.00 35.07  ? 274 ARG A CB  1 
ATOM   2104 C CG  . ARG A 1 277 ? -33.676 29.451  -1.927  1.00 44.99  ? 274 ARG A CG  1 
ATOM   2105 C CD  . ARG A 1 277 ? -35.052 29.033  -2.380  1.00 48.90  ? 274 ARG A CD  1 
ATOM   2106 N NE  . ARG A 1 277 ? -36.045 29.312  -1.350  1.00 48.79  ? 274 ARG A NE  1 
ATOM   2107 C CZ  . ARG A 1 277 ? -36.580 28.390  -0.562  1.00 53.38  ? 274 ARG A CZ  1 
ATOM   2108 N NH1 . ARG A 1 277 ? -36.237 27.112  -0.655  1.00 53.37  ? 274 ARG A NH1 1 
ATOM   2109 N NH2 . ARG A 1 277 ? -37.486 28.756  0.336   1.00 54.77  ? 274 ARG A NH2 1 
ATOM   2110 N N   . LEU A 1 278 ? -29.507 27.453  -2.707  1.00 39.68  ? 275 LEU A N   1 
ATOM   2111 C CA  . LEU A 1 278 ? -28.361 26.964  -3.456  1.00 39.19  ? 275 LEU A CA  1 
ATOM   2112 C C   . LEU A 1 278 ? -28.723 25.901  -4.471  1.00 39.72  ? 275 LEU A C   1 
ATOM   2113 O O   . LEU A 1 278 ? -28.119 25.868  -5.542  1.00 36.97  ? 275 LEU A O   1 
ATOM   2114 C CB  . LEU A 1 278 ? -27.286 26.424  -2.509  1.00 36.36  ? 275 LEU A CB  1 
ATOM   2115 C CG  . LEU A 1 278 ? -26.703 27.532  -1.619  1.00 37.61  ? 275 LEU A CG  1 
ATOM   2116 C CD1 . LEU A 1 278 ? -25.492 27.055  -0.828  1.00 31.54  ? 275 LEU A CD1 1 
ATOM   2117 C CD2 . LEU A 1 278 ? -26.362 28.769  -2.437  1.00 30.40  ? 275 LEU A CD2 1 
ATOM   2118 N N   . LEU A 1 279 ? -29.714 25.060  -4.185  1.00 38.68  ? 276 LEU A N   1 
ATOM   2119 C CA  . LEU A 1 279 ? -30.082 23.987  -5.110  1.00 38.80  ? 276 LEU A CA  1 
ATOM   2120 C C   . LEU A 1 279 ? -30.411 24.444  -6.540  1.00 42.85  ? 276 LEU A C   1 
ATOM   2121 O O   . LEU A 1 279 ? -30.135 23.695  -7.494  1.00 35.81  ? 276 LEU A O   1 
ATOM   2122 C CB  . LEU A 1 279 ? -31.249 23.186  -4.528  1.00 33.51  ? 276 LEU A CB  1 
ATOM   2123 C CG  . LEU A 1 279 ? -30.873 22.574  -3.183  1.00 37.69  ? 276 LEU A CG  1 
ATOM   2124 C CD1 . LEU A 1 279 ? -31.911 21.590  -2.745  1.00 32.83  ? 276 LEU A CD1 1 
ATOM   2125 C CD2 . LEU A 1 279 ? -29.527 21.889  -3.299  1.00 35.59  ? 276 LEU A CD2 1 
ATOM   2126 N N   . PRO A 1 280 ? -31.001 25.626  -6.765  1.00 41.28  ? 277 PRO A N   1 
ATOM   2127 C CA  . PRO A 1 280 ? -31.241 26.052  -8.160  1.00 41.06  ? 277 PRO A CA  1 
ATOM   2128 C C   . PRO A 1 280 ? -29.971 26.196  -9.002  1.00 41.12  ? 277 PRO A C   1 
ATOM   2129 O O   . PRO A 1 280 ? -30.071 26.296  -10.236 1.00 41.15  ? 277 PRO A O   1 
ATOM   2130 C CB  . PRO A 1 280 ? -31.978 27.394  -8.004  1.00 37.11  ? 277 PRO A CB  1 
ATOM   2131 C CG  . PRO A 1 280 ? -31.948 27.712  -6.525  1.00 43.37  ? 277 PRO A CG  1 
ATOM   2132 C CD  . PRO A 1 280 ? -31.810 26.421  -5.824  1.00 38.15  ? 277 PRO A CD  1 
ATOM   2133 N N   . TYR A 1 281 ? -28.792 26.158  -8.381  1.00 38.91  ? 278 TYR A N   1 
ATOM   2134 C CA  . TYR A 1 281 ? -27.516 26.419  -9.029  1.00 34.61  ? 278 TYR A CA  1 
ATOM   2135 C C   . TYR A 1 281 ? -26.729 25.164  -9.372  1.00 32.93  ? 278 TYR A C   1 
ATOM   2136 O O   . TYR A 1 281 ? -25.608 25.278  -9.883  1.00 34.11  ? 278 TYR A O   1 
ATOM   2137 C CB  . TYR A 1 281 ? -26.663 27.311  -8.125  1.00 40.32  ? 278 TYR A CB  1 
ATOM   2138 C CG  . TYR A 1 281 ? -27.098 28.752  -8.097  1.00 46.31  ? 278 TYR A CG  1 
ATOM   2139 C CD1 . TYR A 1 281 ? -28.312 29.141  -7.521  1.00 47.23  ? 278 TYR A CD1 1 
ATOM   2140 C CD2 . TYR A 1 281 ? -26.295 29.732  -8.659  1.00 52.04  ? 278 TYR A CD2 1 
ATOM   2141 C CE1 . TYR A 1 281 ? -28.714 30.468  -7.516  1.00 51.54  ? 278 TYR A CE1 1 
ATOM   2142 C CE2 . TYR A 1 281 ? -26.693 31.092  -8.651  1.00 58.28  ? 278 TYR A CE2 1 
ATOM   2143 C CZ  . TYR A 1 281 ? -27.899 31.443  -8.079  1.00 58.77  ? 278 TYR A CZ  1 
ATOM   2144 O OH  . TYR A 1 281 ? -28.256 32.771  -8.077  1.00 65.70  ? 278 TYR A OH  1 
ATOM   2145 N N   . ILE A 1 282 ? -27.277 23.980  -9.114  1.00 28.57  ? 279 ILE A N   1 
ATOM   2146 C CA  . ILE A 1 282 ? -26.517 22.740  -9.235  1.00 29.36  ? 279 ILE A CA  1 
ATOM   2147 C C   . ILE A 1 282 ? -27.019 21.865  -10.352 1.00 28.72  ? 279 ILE A C   1 
ATOM   2148 O O   . ILE A 1 282 ? -26.383 20.840  -10.639 1.00 33.55  ? 279 ILE A O   1 
ATOM   2149 C CB  . ILE A 1 282 ? -26.494 21.927  -7.914  1.00 33.69  ? 279 ILE A CB  1 
ATOM   2150 C CG1 . ILE A 1 282 ? -27.856 21.266  -7.627  1.00 31.94  ? 279 ILE A CG1 1 
ATOM   2151 C CG2 . ILE A 1 282 ? -26.055 22.788  -6.720  1.00 29.63  ? 279 ILE A CG2 1 
ATOM   2152 C CD1 . ILE A 1 282 ? -27.801 20.106  -6.642  1.00 30.92  ? 279 ILE A CD1 1 
ATOM   2153 N N   . MET A 1 283 ? -28.121 22.229  -11.004 1.00 29.79  ? 280 MET A N   1 
ATOM   2154 C CA  . MET A 1 283 ? -28.669 21.385  -12.064 1.00 32.72  ? 280 MET A CA  1 
ATOM   2155 C C   . MET A 1 283 ? -27.764 21.331  -13.288 1.00 32.71  ? 280 MET A C   1 
ATOM   2156 O O   . MET A 1 283 ? -27.307 20.251  -13.681 1.00 34.82  ? 280 MET A O   1 
ATOM   2157 C CB  . MET A 1 283 ? -30.057 21.862  -12.447 1.00 34.87  ? 280 MET A CB  1 
ATOM   2158 C CG  . MET A 1 283 ? -31.081 21.374  -11.457 1.00 36.56  ? 280 MET A CG  1 
ATOM   2159 S SD  . MET A 1 283 ? -32.607 22.274  -11.553 1.00 38.14  ? 280 MET A SD  1 
ATOM   2160 C CE  . MET A 1 283 ? -32.099 23.967  -11.226 1.00 31.47  ? 280 MET A CE  1 
ATOM   2161 N N   . PHE A 1 284 ? -27.510 22.468  -13.933 1.00 30.90  ? 281 PHE A N   1 
ATOM   2162 C CA  . PHE A 1 284 ? -26.628 22.393  -15.093 1.00 35.57  ? 281 PHE A CA  1 
ATOM   2163 C C   . PHE A 1 284 ? -25.253 21.853  -14.723 1.00 29.79  ? 281 PHE A C   1 
ATOM   2164 O O   . PHE A 1 284 ? -24.760 20.968  -15.443 1.00 31.52  ? 281 PHE A O   1 
ATOM   2165 C CB  . PHE A 1 284 ? -26.494 23.738  -15.829 1.00 35.23  ? 281 PHE A CB  1 
ATOM   2166 C CG  . PHE A 1 284 ? -25.496 23.683  -16.965 1.00 37.12  ? 281 PHE A CG  1 
ATOM   2167 C CD1 . PHE A 1 284 ? -25.833 23.094  -18.183 1.00 32.49  ? 281 PHE A CD1 1 
ATOM   2168 C CD2 . PHE A 1 284 ? -24.203 24.162  -16.801 1.00 32.59  ? 281 PHE A CD2 1 
ATOM   2169 C CE1 . PHE A 1 284 ? -24.901 23.009  -19.227 1.00 32.25  ? 281 PHE A CE1 1 
ATOM   2170 C CE2 . PHE A 1 284 ? -23.271 24.078  -17.851 1.00 30.41  ? 281 PHE A CE2 1 
ATOM   2171 C CZ  . PHE A 1 284 ? -23.623 23.497  -19.054 1.00 30.60  ? 281 PHE A CZ  1 
ATOM   2172 N N   . PRO A 1 285 ? -24.601 22.293  -13.644 1.00 28.20  ? 282 PRO A N   1 
ATOM   2173 C CA  . PRO A 1 285 ? -23.312 21.673  -13.268 1.00 32.06  ? 282 PRO A CA  1 
ATOM   2174 C C   . PRO A 1 285 ? -23.384 20.176  -12.993 1.00 32.32  ? 282 PRO A C   1 
ATOM   2175 O O   . PRO A 1 285 ? -22.329 19.518  -13.009 1.00 30.02  ? 282 PRO A O   1 
ATOM   2176 C CB  . PRO A 1 285 ? -22.902 22.436  -11.999 1.00 26.79  ? 282 PRO A CB  1 
ATOM   2177 C CG  . PRO A 1 285 ? -23.601 23.740  -12.110 1.00 32.89  ? 282 PRO A CG  1 
ATOM   2178 C CD  . PRO A 1 285 ? -24.897 23.480  -12.826 1.00 31.68  ? 282 PRO A CD  1 
ATOM   2179 N N   . ARG A 1 286 ? -24.575 19.626  -12.727 1.00 27.99  ? 283 ARG A N   1 
ATOM   2180 C CA  . ARG A 1 286 ? -24.700 18.250  -12.285 1.00 26.61  ? 283 ARG A CA  1 
ATOM   2181 C C   . ARG A 1 286 ? -23.755 18.004  -11.112 1.00 26.56  ? 283 ARG A C   1 
ATOM   2182 O O   . ARG A 1 286 ? -22.923 17.094  -11.122 1.00 26.16  ? 283 ARG A O   1 
ATOM   2183 C CB  . ARG A 1 286 ? -24.414 17.286  -13.432 1.00 31.61  ? 283 ARG A CB  1 
ATOM   2184 C CG  . ARG A 1 286 ? -25.396 17.323  -14.577 1.00 32.92  ? 283 ARG A CG  1 
ATOM   2185 C CD  . ARG A 1 286 ? -24.686 17.158  -15.910 1.00 29.94  ? 283 ARG A CD  1 
ATOM   2186 N NE  . ARG A 1 286 ? -24.341 18.453  -16.480 1.00 28.89  ? 283 ARG A NE  1 
ATOM   2187 C CZ  . ARG A 1 286 ? -23.744 18.616  -17.650 1.00 31.07  ? 283 ARG A CZ  1 
ATOM   2188 N NH1 . ARG A 1 286 ? -23.350 17.584  -18.374 1.00 34.40  ? 283 ARG A NH1 1 
ATOM   2189 N NH2 . ARG A 1 286 ? -23.544 19.846  -18.111 1.00 34.10  ? 283 ARG A NH2 1 
ATOM   2190 N N   . ALA A 1 287 ? -23.846 18.877  -10.118 1.00 27.11  ? 284 ALA A N   1 
ATOM   2191 C CA  . ALA A 1 287 ? -22.942 18.800  -8.986  1.00 30.40  ? 284 ALA A CA  1 
ATOM   2192 C C   . ALA A 1 287 ? -23.454 17.780  -7.978  1.00 29.84  ? 284 ALA A C   1 
ATOM   2193 O O   . ALA A 1 287 ? -24.660 17.577  -7.830  1.00 33.32  ? 284 ALA A O   1 
ATOM   2194 C CB  . ALA A 1 287 ? -22.783 20.172  -8.332  1.00 28.87  ? 284 ALA A CB  1 
ATOM   2195 N N   . THR A 1 288 ? -22.527 17.109  -7.310  1.00 32.12  ? 285 THR A N   1 
ATOM   2196 C CA  . THR A 1 288 ? -22.859 16.163  -6.254  1.00 31.71  ? 285 THR A CA  1 
ATOM   2197 C C   . THR A 1 288 ? -22.421 16.751  -4.924  1.00 31.66  ? 285 THR A C   1 
ATOM   2198 O O   . THR A 1 288 ? -21.272 17.181  -4.790  1.00 28.45  ? 285 THR A O   1 
ATOM   2199 C CB  . THR A 1 288 ? -22.184 14.814  -6.490  1.00 34.62  ? 285 THR A CB  1 
ATOM   2200 O OG1 . THR A 1 288 ? -22.424 14.397  -7.842  1.00 33.59  ? 285 THR A OG1 1 
ATOM   2201 C CG2 . THR A 1 288 ? -22.728 13.777  -5.525  1.00 31.64  ? 285 THR A CG2 1 
ATOM   2202 N N   . ILE A 1 289 ? -23.351 16.820  -3.972  1.00 30.15  ? 286 ILE A N   1 
ATOM   2203 C CA  . ILE A 1 289 ? -23.094 17.345  -2.637  1.00 25.67  ? 286 ILE A CA  1 
ATOM   2204 C C   . ILE A 1 289 ? -23.346 16.222  -1.650  1.00 30.22  ? 286 ILE A C   1 
ATOM   2205 O O   . ILE A 1 289 ? -24.445 15.660  -1.621  1.00 29.76  ? 286 ILE A O   1 
ATOM   2206 C CB  . ILE A 1 289 ? -23.980 18.547  -2.307  1.00 26.39  ? 286 ILE A CB  1 
ATOM   2207 C CG1 . ILE A 1 289 ? -23.827 19.617  -3.371  1.00 33.02  ? 286 ILE A CG1 1 
ATOM   2208 C CG2 . ILE A 1 289 ? -23.604 19.128  -0.956  1.00 25.61  ? 286 ILE A CG2 1 
ATOM   2209 C CD1 . ILE A 1 289 ? -24.837 19.506  -4.452  1.00 35.47  ? 286 ILE A CD1 1 
ATOM   2210 N N   . ARG A 1 290 ? -22.338 15.886  -0.855  1.00 29.57  ? 287 ARG A N   1 
ATOM   2211 C CA  . ARG A 1 290 ? -22.455 14.831  0.137   1.00 31.52  ? 287 ARG A CA  1 
ATOM   2212 C C   . ARG A 1 290 ? -22.137 15.385  1.521   1.00 31.38  ? 287 ARG A C   1 
ATOM   2213 O O   . ARG A 1 290 ? -21.072 15.966  1.732   1.00 31.22  ? 287 ARG A O   1 
ATOM   2214 C CB  . ARG A 1 290 ? -21.529 13.644  -0.186  1.00 30.43  ? 287 ARG A CB  1 
ATOM   2215 C CG  . ARG A 1 290 ? -21.842 12.393  0.674   1.00 32.77  ? 287 ARG A CG  1 
ATOM   2216 C CD  . ARG A 1 290 ? -20.977 11.214  0.283   1.00 32.59  ? 287 ARG A CD  1 
ATOM   2217 N NE  . ARG A 1 290 ? -21.225 10.002  1.060   1.00 43.14  ? 287 ARG A NE  1 
ATOM   2218 C CZ  . ARG A 1 290 ? -20.937 9.825   2.351   1.00 41.44  ? 287 ARG A CZ  1 
ATOM   2219 N NH1 . ARG A 1 290 ? -20.543 10.827  3.134   1.00 36.35  ? 287 ARG A NH1 1 
ATOM   2220 N NH2 . ARG A 1 290 ? -21.059 8.613   2.879   1.00 37.66  ? 287 ARG A NH2 1 
ATOM   2221 N N   . GLY A 1 291 ? -23.066 15.204  2.454   1.00 29.40  ? 288 GLY A N   1 
ATOM   2222 C CA  . GLY A 1 291 ? -22.778 15.485  3.845   1.00 29.70  ? 288 GLY A CA  1 
ATOM   2223 C C   . GLY A 1 291 ? -21.735 14.530  4.402   1.00 29.56  ? 288 GLY A C   1 
ATOM   2224 O O   . GLY A 1 291 ? -21.704 13.343  4.067   1.00 29.15  ? 288 GLY A O   1 
ATOM   2225 N N   . ILE A 1 292 ? -20.852 15.069  5.247   1.00 25.29  ? 289 ILE A N   1 
ATOM   2226 C CA  . ILE A 1 292 ? -19.781 14.291  5.867   1.00 32.89  ? 289 ILE A CA  1 
ATOM   2227 C C   . ILE A 1 292 ? -20.105 14.084  7.338   1.00 34.71  ? 289 ILE A C   1 
ATOM   2228 O O   . ILE A 1 292 ? -20.294 15.055  8.088   1.00 35.21  ? 289 ILE A O   1 
ATOM   2229 C CB  . ILE A 1 292 ? -18.406 14.959  5.739   1.00 34.40  ? 289 ILE A CB  1 
ATOM   2230 C CG1 . ILE A 1 292 ? -18.095 15.322  4.284   1.00 25.41  ? 289 ILE A CG1 1 
ATOM   2231 C CG2 . ILE A 1 292 ? -17.352 14.020  6.329   1.00 27.17  ? 289 ILE A CG2 1 
ATOM   2232 C CD1 . ILE A 1 292 ? -18.224 14.156  3.344   1.00 26.45  ? 289 ILE A CD1 1 
ATOM   2233 N N   . PHE A 1 293 ? -20.140 12.818  7.753   1.00 32.57  ? 290 PHE A N   1 
ATOM   2234 C CA  . PHE A 1 293 ? -20.255 12.445  9.169   1.00 35.16  ? 290 PHE A CA  1 
ATOM   2235 C C   . PHE A 1 293 ? -19.254 11.309  9.372   1.00 30.17  ? 290 PHE A C   1 
ATOM   2236 O O   . PHE A 1 293 ? -19.614 10.135  9.289   1.00 30.53  ? 290 PHE A O   1 
ATOM   2237 C CB  . PHE A 1 293 ? -21.672 12.041  9.544   1.00 32.05  ? 290 PHE A CB  1 
ATOM   2238 C CG  . PHE A 1 293 ? -21.926 12.023  11.016  1.00 36.07  ? 290 PHE A CG  1 
ATOM   2239 C CD1 . PHE A 1 293 ? -21.981 13.210  11.733  1.00 39.66  ? 290 PHE A CD1 1 
ATOM   2240 C CD2 . PHE A 1 293 ? -22.123 10.821  11.694  1.00 34.27  ? 290 PHE A CD2 1 
ATOM   2241 C CE1 . PHE A 1 293 ? -22.214 13.201  13.102  1.00 42.41  ? 290 PHE A CE1 1 
ATOM   2242 C CE2 . PHE A 1 293 ? -22.353 10.805  13.072  1.00 36.67  ? 290 PHE A CE2 1 
ATOM   2243 C CZ  . PHE A 1 293 ? -22.400 11.994  13.771  1.00 38.64  ? 290 PHE A CZ  1 
ATOM   2244 N N   . SER A 1 294 ? -17.999 11.678  9.639   1.00 28.47  ? 291 SER A N   1 
ATOM   2245 C CA  . SER A 1 294 ? -16.876 10.743  9.584   1.00 32.16  ? 291 SER A CA  1 
ATOM   2246 C C   . SER A 1 294 ? -16.995 9.557   10.560  1.00 33.64  ? 291 SER A C   1 
ATOM   2247 O O   . SER A 1 294 ? -16.267 8.566   10.393  1.00 27.17  ? 291 SER A O   1 
ATOM   2248 C CB  . SER A 1 294 ? -15.585 11.501  9.872   1.00 31.20  ? 291 SER A CB  1 
ATOM   2249 O OG  . SER A 1 294 ? -15.603 11.996  11.202  1.00 37.09  ? 291 SER A OG  1 
ATOM   2250 N N   . LEU A 1 295 ? -17.884 9.628   11.568  1.00 26.19  ? 292 LEU A N   1 
ATOM   2251 C CA  . LEU A 1 295 ? -18.058 8.498   12.478  1.00 27.68  ? 292 LEU A CA  1 
ATOM   2252 C C   . LEU A 1 295 ? -18.353 7.204   11.739  1.00 29.31  ? 292 LEU A C   1 
ATOM   2253 O O   . LEU A 1 295 ? -17.961 6.134   12.206  1.00 33.23  ? 292 LEU A O   1 
ATOM   2254 C CB  . LEU A 1 295 ? -19.167 8.778   13.485  1.00 26.09  ? 292 LEU A CB  1 
ATOM   2255 C CG  . LEU A 1 295 ? -18.686 9.754   14.559  1.00 31.26  ? 292 LEU A CG  1 
ATOM   2256 C CD1 . LEU A 1 295 ? -19.697 9.960   15.678  1.00 36.26  ? 292 LEU A CD1 1 
ATOM   2257 C CD2 . LEU A 1 295 ? -17.345 9.283   15.111  1.00 28.41  ? 292 LEU A CD2 1 
ATOM   2258 N N   . GLU A 1 296 ? -19.015 7.282   10.581  1.00 30.77  ? 293 GLU A N   1 
ATOM   2259 C CA  . GLU A 1 296 ? -19.362 6.103   9.785   1.00 30.30  ? 293 GLU A CA  1 
ATOM   2260 C C   . GLU A 1 296 ? -18.138 5.376   9.248   1.00 30.41  ? 293 GLU A C   1 
ATOM   2261 O O   . GLU A 1 296 ? -18.271 4.241   8.782   1.00 31.82  ? 293 GLU A O   1 
ATOM   2262 C CB  . GLU A 1 296 ? -20.267 6.499   8.598   1.00 27.83  ? 293 GLU A CB  1 
ATOM   2263 C CG  . GLU A 1 296 ? -19.516 7.022   7.370   1.00 32.58  ? 293 GLU A CG  1 
ATOM   2264 C CD  . GLU A 1 296 ? -20.400 7.154   6.138   1.00 37.90  ? 293 GLU A CD  1 
ATOM   2265 O OE1 . GLU A 1 296 ? -21.302 6.315   5.967   1.00 43.48  ? 293 GLU A OE1 1 
ATOM   2266 O OE2 . GLU A 1 296 ? -20.203 8.097   5.342   1.00 32.52  ? 293 GLU A OE2 1 
ATOM   2267 N N   . TRP A 1 297 ? -16.961 6.006   9.261   1.00 27.18  ? 294 TRP A N   1 
ATOM   2268 C CA  . TRP A 1 297 ? -15.751 5.378   8.755   1.00 28.59  ? 294 TRP A CA  1 
ATOM   2269 C C   . TRP A 1 297 ? -14.878 4.794   9.872   1.00 36.30  ? 294 TRP A C   1 
ATOM   2270 O O   . TRP A 1 297 ? -13.800 4.254   9.587   1.00 35.34  ? 294 TRP A O   1 
ATOM   2271 C CB  . TRP A 1 297 ? -14.946 6.385   7.915   1.00 27.15  ? 294 TRP A CB  1 
ATOM   2272 C CG  . TRP A 1 297 ? -15.663 6.878   6.662   1.00 34.26  ? 294 TRP A CG  1 
ATOM   2273 C CD1 . TRP A 1 297 ? -16.469 6.143   5.827   1.00 32.56  ? 294 TRP A CD1 1 
ATOM   2274 C CD2 . TRP A 1 297 ? -15.629 8.208   6.109   1.00 30.11  ? 294 TRP A CD2 1 
ATOM   2275 N NE1 . TRP A 1 297 ? -16.923 6.930   4.798   1.00 35.81  ? 294 TRP A NE1 1 
ATOM   2276 C CE2 . TRP A 1 297 ? -16.430 8.200   4.950   1.00 32.98  ? 294 TRP A CE2 1 
ATOM   2277 C CE3 . TRP A 1 297 ? -14.987 9.400   6.476   1.00 28.21  ? 294 TRP A CE3 1 
ATOM   2278 C CZ2 . TRP A 1 297 ? -16.621 9.345   4.164   1.00 32.02  ? 294 TRP A CZ2 1 
ATOM   2279 C CZ3 . TRP A 1 297 ? -15.172 10.535  5.698   1.00 28.83  ? 294 TRP A CZ3 1 
ATOM   2280 C CH2 . TRP A 1 297 ? -15.992 10.503  4.555   1.00 28.62  ? 294 TRP A CH2 1 
ATOM   2281 N N   . PHE A 1 298 ? -15.324 4.863   11.132  1.00 28.82  ? 295 PHE A N   1 
ATOM   2282 C CA  . PHE A 1 298 ? -14.530 4.400   12.271  1.00 29.52  ? 295 PHE A CA  1 
ATOM   2283 C C   . PHE A 1 298 ? -14.623 2.877   12.334  1.00 28.40  ? 295 PHE A C   1 
ATOM   2284 O O   . PHE A 1 298 ? -15.351 2.289   13.142  1.00 36.31  ? 295 PHE A O   1 
ATOM   2285 C CB  . PHE A 1 298 ? -15.008 5.048   13.574  1.00 28.73  ? 295 PHE A CB  1 
ATOM   2286 C CG  . PHE A 1 298 ? -14.586 6.491   13.766  1.00 29.48  ? 295 PHE A CG  1 
ATOM   2287 C CD1 . PHE A 1 298 ? -14.589 7.400   12.717  1.00 30.19  ? 295 PHE A CD1 1 
ATOM   2288 C CD2 . PHE A 1 298 ? -14.228 6.952   15.025  1.00 27.46  ? 295 PHE A CD2 1 
ATOM   2289 C CE1 . PHE A 1 298 ? -14.207 8.736   12.924  1.00 28.10  ? 295 PHE A CE1 1 
ATOM   2290 C CE2 . PHE A 1 298 ? -13.844 8.272   15.219  1.00 28.02  ? 295 PHE A CE2 1 
ATOM   2291 C CZ  . PHE A 1 298 ? -13.843 9.163   14.175  1.00 22.67  ? 295 PHE A CZ  1 
ATOM   2292 N N   . THR A 1 299 ? -13.861 2.225   11.464  1.00 28.10  ? 296 THR A N   1 
ATOM   2293 C CA  . THR A 1 299 ? -13.804 0.768   11.384  1.00 33.57  ? 296 THR A CA  1 
ATOM   2294 C C   . THR A 1 299 ? -12.349 0.360   11.489  1.00 35.34  ? 296 THR A C   1 
ATOM   2295 O O   . THR A 1 299 ? -11.460 1.150   11.182  1.00 43.44  ? 296 THR A O   1 
ATOM   2296 C CB  . THR A 1 299 ? -14.405 0.216   10.063  1.00 37.78  ? 296 THR A CB  1 
ATOM   2297 O OG1 . THR A 1 299 ? -13.554 0.540   8.947   1.00 36.69  ? 296 THR A OG1 1 
ATOM   2298 C CG2 . THR A 1 299 ? -15.797 0.791   9.815   1.00 25.51  ? 296 THR A CG2 1 
ATOM   2299 N N   . GLU A 1 300 ? -12.091 -0.874  11.914  1.00 38.10  ? 297 GLU A N   1 
ATOM   2300 C CA  . GLU A 1 300 ? -10.693 -1.271  12.027  1.00 34.36  ? 297 GLU A CA  1 
ATOM   2301 C C   . GLU A 1 300 ? -10.018 -1.309  10.657  1.00 39.15  ? 297 GLU A C   1 
ATOM   2302 O O   . GLU A 1 300 ? -8.831  -0.989  10.545  1.00 36.73  ? 297 GLU A O   1 
ATOM   2303 C CB  . GLU A 1 300 ? -10.571 -2.614  12.753  1.00 36.74  ? 297 GLU A CB  1 
ATOM   2304 C CG  . GLU A 1 300 ? -9.142  -3.123  13.007  1.00 59.87  ? 297 GLU A CG  1 
ATOM   2305 C CD  . GLU A 1 300 ? -9.078  -4.460  13.787  1.00 77.19  ? 297 GLU A CD  1 
ATOM   2306 O OE1 . GLU A 1 300 ? -10.158 -5.042  14.115  1.00 68.03  ? 297 GLU A OE1 1 
ATOM   2307 O OE2 . GLU A 1 300 ? -7.932  -4.921  14.060  1.00 78.97  ? 297 GLU A OE2 1 
ATOM   2308 N N   . GLN A 1 301 ? -10.760 -1.638  9.594   1.00 40.66  ? 298 GLN A N   1 
ATOM   2309 C CA  . GLN A 1 301 ? -10.168 -1.582  8.261   1.00 43.88  ? 298 GLN A CA  1 
ATOM   2310 C C   . GLN A 1 301 ? -9.740  -0.166  7.903   1.00 37.19  ? 298 GLN A C   1 
ATOM   2311 O O   . GLN A 1 301 ? -8.643  0.042   7.372   1.00 32.38  ? 298 GLN A O   1 
ATOM   2312 C CB  . GLN A 1 301 ? -11.142 -2.103  7.212   1.00 49.01  ? 298 GLN A CB  1 
ATOM   2313 C CG  . GLN A 1 301 ? -10.510 -3.081  6.255   1.00 54.35  ? 298 GLN A CG  1 
ATOM   2314 C CD  . GLN A 1 301 ? -10.397 -4.466  6.864   1.00 72.57  ? 298 GLN A CD  1 
ATOM   2315 O OE1 . GLN A 1 301 ? -11.332 -4.942  7.519   1.00 77.37  ? 298 GLN A OE1 1 
ATOM   2316 N NE2 . GLN A 1 301 ? -9.246  -5.115  6.671   1.00 78.34  ? 298 GLN A NE2 1 
ATOM   2317 N N   . ASN A 1 302 ? -10.592 0.824   8.175   1.00 34.68  ? 299 ASN A N   1 
ATOM   2318 C CA  . ASN A 1 302 ? -10.234 2.181   7.781   1.00 36.04  ? 299 ASN A CA  1 
ATOM   2319 C C   . ASN A 1 302 ? -9.077  2.708   8.619   1.00 36.58  ? 299 ASN A C   1 
ATOM   2320 O O   . ASN A 1 302 ? -8.182  3.376   8.079   1.00 32.42  ? 299 ASN A O   1 
ATOM   2321 C CB  . ASN A 1 302 ? -11.444 3.105   7.864   1.00 35.55  ? 299 ASN A CB  1 
ATOM   2322 C CG  . ASN A 1 302 ? -12.426 2.872   6.734   1.00 34.10  ? 299 ASN A CG  1 
ATOM   2323 O OD1 . ASN A 1 302 ? -12.023 2.561   5.622   1.00 36.42  ? 299 ASN A OD1 1 
ATOM   2324 N ND2 . ASN A 1 302 ? -13.723 2.999   7.023   1.00 31.43  ? 299 ASN A ND2 1 
ATOM   2325 N N   . TRP A 1 303 ? -9.044  2.375   9.926   1.00 27.91  ? 300 TRP A N   1 
ATOM   2326 C CA  . TRP A 1 303 ? -7.926  2.826   10.763  1.00 33.04  ? 300 TRP A CA  1 
ATOM   2327 C C   . TRP A 1 303 ? -6.585  2.258   10.297  1.00 32.02  ? 300 TRP A C   1 
ATOM   2328 O O   . TRP A 1 303 ? -5.574  2.961   10.360  1.00 32.40  ? 300 TRP A O   1 
ATOM   2329 C CB  . TRP A 1 303 ? -8.153  2.507   12.251  1.00 25.62  ? 300 TRP A CB  1 
ATOM   2330 C CG  . TRP A 1 303 ? -9.245  3.357   12.925  1.00 28.58  ? 300 TRP A CG  1 
ATOM   2331 C CD1 . TRP A 1 303 ? -10.418 2.901   13.438  1.00 26.51  ? 300 TRP A CD1 1 
ATOM   2332 C CD2 . TRP A 1 303 ? -9.258  4.797   13.129  1.00 26.83  ? 300 TRP A CD2 1 
ATOM   2333 N NE1 . TRP A 1 303 ? -11.158 3.945   13.945  1.00 31.26  ? 300 TRP A NE1 1 
ATOM   2334 C CE2 . TRP A 1 303 ? -10.471 5.116   13.773  1.00 28.26  ? 300 TRP A CE2 1 
ATOM   2335 C CE3 . TRP A 1 303 ? -8.361  5.836   12.836  1.00 25.88  ? 300 TRP A CE3 1 
ATOM   2336 C CZ2 . TRP A 1 303 ? -10.817 6.426   14.127  1.00 24.08  ? 300 TRP A CZ2 1 
ATOM   2337 C CZ3 . TRP A 1 303 ? -8.715  7.145   13.187  1.00 24.80  ? 300 TRP A CZ3 1 
ATOM   2338 C CH2 . TRP A 1 303 ? -9.929  7.420   13.820  1.00 25.68  ? 300 TRP A CH2 1 
ATOM   2339 N N   . SER A 1 304 ? -6.542  1.021   9.796   1.00 34.24  ? 301 SER A N   1 
ATOM   2340 C CA  . SER A 1 304 ? -5.278  0.515   9.264   1.00 30.68  ? 301 SER A CA  1 
ATOM   2341 C C   . SER A 1 304 ? -4.896  1.241   7.982   1.00 34.55  ? 301 SER A C   1 
ATOM   2342 O O   . SER A 1 304 ? -3.728  1.602   7.788   1.00 40.39  ? 301 SER A O   1 
ATOM   2343 C CB  . SER A 1 304 ? -5.350  -0.985  8.997   1.00 29.79  ? 301 SER A CB  1 
ATOM   2344 O OG  . SER A 1 304 ? -5.942  -1.671  10.069  1.00 46.10  ? 301 SER A OG  1 
ATOM   2345 N N   . ALA A 1 305 ? -5.861  1.441   7.077   1.00 31.96  ? 302 ALA A N   1 
ATOM   2346 C CA  . ALA A 1 305 ? -5.544  2.133   5.836   1.00 31.33  ? 302 ALA A CA  1 
ATOM   2347 C C   . ALA A 1 305 ? -5.076  3.549   6.119   1.00 29.85  ? 302 ALA A C   1 
ATOM   2348 O O   . ALA A 1 305 ? -4.153  4.045   5.464   1.00 34.45  ? 302 ALA A O   1 
ATOM   2349 C CB  . ALA A 1 305 ? -6.752  2.132   4.906   1.00 31.15  ? 302 ALA A CB  1 
ATOM   2350 N N   . LEU A 1 306 ? -5.698  4.204   7.102   1.00 26.78  ? 303 LEU A N   1 
ATOM   2351 C CA  . LEU A 1 306 ? -5.260  5.528   7.547   1.00 32.11  ? 303 LEU A CA  1 
ATOM   2352 C C   . LEU A 1 306 ? -3.787  5.529   7.940   1.00 34.24  ? 303 LEU A C   1 
ATOM   2353 O O   . LEU A 1 306 ? -3.007  6.377   7.474   1.00 31.42  ? 303 LEU A O   1 
ATOM   2354 C CB  . LEU A 1 306 ? -6.111  5.983   8.731   1.00 30.16  ? 303 LEU A CB  1 
ATOM   2355 C CG  . LEU A 1 306 ? -5.904  7.423   9.174   1.00 25.53  ? 303 LEU A CG  1 
ATOM   2356 C CD1 . LEU A 1 306 ? -6.349  8.340   8.074   1.00 30.34  ? 303 LEU A CD1 1 
ATOM   2357 C CD2 . LEU A 1 306 ? -6.683  7.699   10.424  1.00 28.33  ? 303 LEU A CD2 1 
ATOM   2358 N N   . HIS A 1 307 ? -3.396  4.586   8.812   1.00 27.77  ? 304 HIS A N   1 
ATOM   2359 C CA  . HIS A 1 307 ? -2.020  4.531   9.288   1.00 34.52  ? 304 HIS A CA  1 
ATOM   2360 C C   . HIS A 1 307 ? -1.045  4.172   8.169   1.00 37.68  ? 304 HIS A C   1 
ATOM   2361 O O   . HIS A 1 307 ? 0.095   4.652   8.180   1.00 35.70  ? 304 HIS A O   1 
ATOM   2362 C CB  . HIS A 1 307 ? -1.910  3.544   10.453  1.00 33.79  ? 304 HIS A CB  1 
ATOM   2363 C CG  . HIS A 1 307 ? -2.415  4.083   11.764  1.00 38.53  ? 304 HIS A CG  1 
ATOM   2364 N ND1 . HIS A 1 307 ? -1.598  4.723   12.673  1.00 42.49  ? 304 HIS A ND1 1 
ATOM   2365 C CD2 . HIS A 1 307 ? -3.653  4.069   12.321  1.00 35.80  ? 304 HIS A CD2 1 
ATOM   2366 C CE1 . HIS A 1 307 ? -2.311  5.081   13.729  1.00 40.86  ? 304 HIS A CE1 1 
ATOM   2367 N NE2 . HIS A 1 307 ? -3.562  4.698   13.539  1.00 36.43  ? 304 HIS A NE2 1 
ATOM   2368 N N   . GLU A 1 308 ? -1.477  3.356   7.194   1.00 37.08  ? 305 GLU A N   1 
ATOM   2369 C CA  . GLU A 1 308 ? -0.633  3.012   6.048   1.00 42.27  ? 305 GLU A CA  1 
ATOM   2370 C C   . GLU A 1 308 ? -0.475  4.192   5.103   1.00 39.02  ? 305 GLU A C   1 
ATOM   2371 O O   . GLU A 1 308 ? 0.637   4.686   4.879   1.00 40.83  ? 305 GLU A O   1 
ATOM   2372 C CB  . GLU A 1 308 ? -1.218  1.824   5.277   1.00 46.78  ? 305 GLU A CB  1 
ATOM   2373 C CG  . GLU A 1 308 ? -0.188  0.744   4.989   1.00 53.90  ? 305 GLU A CG  1 
ATOM   2374 C CD  . GLU A 1 308 ? 0.379   0.162   6.290   1.00 77.31  ? 305 GLU A CD  1 
ATOM   2375 O OE1 . GLU A 1 308 ? -0.336  -0.643  6.950   1.00 80.76  ? 305 GLU A OE1 1 
ATOM   2376 O OE2 . GLU A 1 308 ? 1.518   0.537   6.674   1.00 74.34  ? 305 GLU A OE2 1 
ATOM   2377 N N   . GLU A 1 309 ? -1.584  4.640   4.519   1.00 41.04  ? 306 GLU A N   1 
ATOM   2378 C CA  . GLU A 1 309 ? -1.542  5.744   3.568   1.00 42.82  ? 306 GLU A CA  1 
ATOM   2379 C C   . GLU A 1 309 ? -1.062  7.028   4.234   1.00 40.26  ? 306 GLU A C   1 
ATOM   2380 O O   . GLU A 1 309 ? 0.001   7.569   3.901   1.00 40.84  ? 306 GLU A O   1 
ATOM   2381 C CB  . GLU A 1 309 ? -2.927  5.945   2.947   1.00 40.84  ? 306 GLU A CB  1 
ATOM   2382 C CG  . GLU A 1 309 ? -3.457  4.741   2.181   1.00 46.93  ? 306 GLU A CG  1 
ATOM   2383 C CD  . GLU A 1 309 ? -4.660  5.085   1.326   1.00 50.09  ? 306 GLU A CD  1 
ATOM   2384 O OE1 . GLU A 1 309 ? -4.683  6.203   0.742   1.00 44.47  ? 306 GLU A OE1 1 
ATOM   2385 O OE2 . GLU A 1 309 ? -5.572  4.231   1.254   1.00 47.37  ? 306 GLU A OE2 1 
ATOM   2386 N N   . LEU A 1 310 ? -1.840  7.528   5.187   1.00 38.44  ? 307 LEU A N   1 
ATOM   2387 C CA  . LEU A 1 310 ? -1.612  8.878   5.661   1.00 35.79  ? 307 LEU A CA  1 
ATOM   2388 C C   . LEU A 1 310 ? -0.419  8.929   6.599   1.00 40.29  ? 307 LEU A C   1 
ATOM   2389 O O   . LEU A 1 310 ? 0.413   9.838   6.499   1.00 38.61  ? 307 LEU A O   1 
ATOM   2390 C CB  . LEU A 1 310 ? -2.867  9.399   6.340   1.00 35.30  ? 307 LEU A CB  1 
ATOM   2391 C CG  . LEU A 1 310 ? -2.838  10.910  6.467   1.00 38.24  ? 307 LEU A CG  1 
ATOM   2392 C CD1 . LEU A 1 310 ? -2.706  11.508  5.086   1.00 37.41  ? 307 LEU A CD1 1 
ATOM   2393 C CD2 . LEU A 1 310 ? -4.083  11.391  7.173   1.00 35.23  ? 307 LEU A CD2 1 
ATOM   2394 N N   . GLY A 1 311 ? -0.319  7.958   7.510   1.00 39.60  ? 308 GLY A N   1 
ATOM   2395 C CA  . GLY A 1 311 ? 0.846   7.885   8.364   1.00 37.39  ? 308 GLY A CA  1 
ATOM   2396 C C   . GLY A 1 311 ? 2.136   7.776   7.579   1.00 40.51  ? 308 GLY A C   1 
ATOM   2397 O O   . GLY A 1 311 ? 3.178   8.283   8.020   1.00 36.76  ? 308 GLY A O   1 
ATOM   2398 N N   . GLY A 1 312 ? 2.087   7.119   6.412   1.00 35.74  ? 309 GLY A N   1 
ATOM   2399 C CA  . GLY A 1 312 ? 3.268   7.047   5.569   1.00 35.16  ? 309 GLY A CA  1 
ATOM   2400 C C   . GLY A 1 312 ? 3.687   8.407   5.046   1.00 39.76  ? 309 GLY A C   1 
ATOM   2401 O O   . GLY A 1 312 ? 4.838   8.820   5.198   1.00 37.47  ? 309 GLY A O   1 
ATOM   2402 N N   . LEU A 1 313 ? 2.744   9.139   4.453   1.00 41.82  ? 310 LEU A N   1 
ATOM   2403 C CA  . LEU A 1 313 ? 3.082   10.437  3.889   1.00 40.16  ? 310 LEU A CA  1 
ATOM   2404 C C   . LEU A 1 313 ? 3.604   11.392  4.958   1.00 37.49  ? 310 LEU A C   1 
ATOM   2405 O O   . LEU A 1 313 ? 4.501   12.203  4.694   1.00 36.74  ? 310 LEU A O   1 
ATOM   2406 C CB  . LEU A 1 313 ? 1.864   11.017  3.182   1.00 37.39  ? 310 LEU A CB  1 
ATOM   2407 C CG  . LEU A 1 313 ? 1.388   10.133  2.047   1.00 34.26  ? 310 LEU A CG  1 
ATOM   2408 C CD1 . LEU A 1 313 ? 0.030   10.570  1.585   1.00 34.17  ? 310 LEU A CD1 1 
ATOM   2409 C CD2 . LEU A 1 313 ? 2.367   10.217  0.932   1.00 41.90  ? 310 LEU A CD2 1 
ATOM   2410 N N   . VAL A 1 314 ? 3.068   11.305  6.175   1.00 39.22  ? 311 VAL A N   1 
ATOM   2411 C CA  . VAL A 1 314 ? 3.545   12.178  7.243   1.00 36.79  ? 311 VAL A CA  1 
ATOM   2412 C C   . VAL A 1 314 ? 4.970   11.817  7.613   1.00 42.05  ? 311 VAL A C   1 
ATOM   2413 O O   . VAL A 1 314 ? 5.804   12.694  7.874   1.00 44.02  ? 311 VAL A O   1 
ATOM   2414 C CB  . VAL A 1 314 ? 2.617   12.095  8.464   1.00 32.81  ? 311 VAL A CB  1 
ATOM   2415 C CG1 . VAL A 1 314 ? 3.220   12.857  9.637   1.00 31.15  ? 311 VAL A CG1 1 
ATOM   2416 C CG2 . VAL A 1 314 ? 1.252   12.626  8.120   1.00 30.38  ? 311 VAL A CG2 1 
ATOM   2417 N N   . ARG A 1 315 ? 5.278   10.517  7.622   1.00 47.33  ? 312 ARG A N   1 
ATOM   2418 C CA  . ARG A 1 315 ? 6.589   10.056  8.059   1.00 48.58  ? 312 ARG A CA  1 
ATOM   2419 C C   . ARG A 1 315 ? 7.652   10.304  7.002   1.00 47.44  ? 312 ARG A C   1 
ATOM   2420 O O   . ARG A 1 315 ? 8.759   10.738  7.332   1.00 54.08  ? 312 ARG A O   1 
ATOM   2421 C CB  . ARG A 1 315 ? 6.536   8.574   8.438   1.00 45.02  ? 312 ARG A CB  1 
ATOM   2422 C CG  . ARG A 1 315 ? 7.009   8.330   9.894   1.00 57.94  ? 312 ARG A CG  1 
ATOM   2423 C CD  . ARG A 1 315 ? 7.241   6.869   10.143  1.00 52.27  ? 312 ARG A CD  1 
ATOM   2424 N NE  . ARG A 1 315 ? 6.147   6.145   9.524   1.00 50.66  ? 312 ARG A NE  1 
ATOM   2425 C CZ  . ARG A 1 315 ? 5.052   5.782   10.167  1.00 49.77  ? 312 ARG A CZ  1 
ATOM   2426 N NH1 . ARG A 1 315 ? 4.946   5.931   11.482  1.00 47.64  ? 312 ARG A NH1 1 
ATOM   2427 N NH2 . ARG A 1 315 ? 4.039   5.255   9.474   1.00 48.04  ? 312 ARG A NH2 1 
ATOM   2428 N N   . ARG A 1 316 ? 7.334   10.046  5.731   1.00 44.81  ? 313 ARG A N   1 
ATOM   2429 C CA  . ARG A 1 316 ? 8.230   10.395  4.634   1.00 48.22  ? 313 ARG A CA  1 
ATOM   2430 C C   . ARG A 1 316 ? 8.360   11.900  4.436   1.00 50.94  ? 313 ARG A C   1 
ATOM   2431 O O   . ARG A 1 316 ? 9.067   12.325  3.514   1.00 55.87  ? 313 ARG A O   1 
ATOM   2432 C CB  . ARG A 1 316 ? 7.749   9.739   3.337   1.00 44.08  ? 313 ARG A CB  1 
ATOM   2433 C CG  . ARG A 1 316 ? 7.808   8.228   3.376   1.00 48.64  ? 313 ARG A CG  1 
ATOM   2434 C CD  . ARG A 1 316 ? 7.281   7.644   2.089   1.00 56.73  ? 313 ARG A CD  1 
ATOM   2435 N NE  . ARG A 1 316 ? 6.017   6.957   2.312   1.00 56.12  ? 313 ARG A NE  1 
ATOM   2436 C CZ  . ARG A 1 316 ? 5.042   6.906   1.417   1.00 57.02  ? 313 ARG A CZ  1 
ATOM   2437 N NH1 . ARG A 1 316 ? 5.160   7.498   0.231   1.00 53.43  ? 313 ARG A NH1 1 
ATOM   2438 N NH2 . ARG A 1 316 ? 3.920   6.253   1.720   1.00 55.26  ? 313 ARG A NH2 1 
ATOM   2439 N N   . GLN A 1 317 ? 7.687   12.697  5.270   1.00 47.43  ? 314 GLN A N   1 
ATOM   2440 C CA  . GLN A 1 317 ? 7.716   14.155  5.209   1.00 47.54  ? 314 GLN A CA  1 
ATOM   2441 C C   . GLN A 1 317 ? 7.129   14.688  3.908   1.00 42.97  ? 314 GLN A C   1 
ATOM   2442 O O   . GLN A 1 317 ? 7.534   15.738  3.418   1.00 48.38  ? 314 GLN A O   1 
ATOM   2443 C CB  . GLN A 1 317 ? 9.130   14.691  5.419   1.00 50.76  ? 314 GLN A CB  1 
ATOM   2444 C CG  . GLN A 1 317 ? 9.784   14.227  6.705   1.00 50.39  ? 314 GLN A CG  1 
ATOM   2445 C CD  . GLN A 1 317 ? 10.992  15.068  7.045   1.00 61.75  ? 314 GLN A CD  1 
ATOM   2446 O OE1 . GLN A 1 317 ? 12.001  15.022  6.339   1.00 65.80  ? 314 GLN A OE1 1 
ATOM   2447 N NE2 . GLN A 1 317 ? 10.890  15.865  8.118   1.00 61.85  ? 314 GLN A NE2 1 
ATOM   2448 N N   . GLU A 1 318 ? 6.164   13.981  3.344   1.00 42.46  ? 315 GLU A N   1 
ATOM   2449 C CA  . GLU A 1 318 ? 5.445   14.459  2.176   1.00 45.64  ? 315 GLU A CA  1 
ATOM   2450 C C   . GLU A 1 318 ? 4.161   15.171  2.557   1.00 48.17  ? 315 GLU A C   1 
ATOM   2451 O O   . GLU A 1 318 ? 3.320   15.428  1.688   1.00 48.91  ? 315 GLU A O   1 
ATOM   2452 C CB  . GLU A 1 318 ? 5.134   13.293  1.235   1.00 43.53  ? 315 GLU A CB  1 
ATOM   2453 C CG  . GLU A 1 318 ? 6.373   12.499  0.816   1.00 58.42  ? 315 GLU A CG  1 
ATOM   2454 C CD  . GLU A 1 318 ? 6.070   11.451  -0.240  1.00 61.12  ? 315 GLU A CD  1 
ATOM   2455 O OE1 . GLU A 1 318 ? 5.282   11.776  -1.164  1.00 54.05  ? 315 GLU A OE1 1 
ATOM   2456 O OE2 . GLU A 1 318 ? 6.608   10.314  -0.137  1.00 57.88  ? 315 GLU A OE2 1 
ATOM   2457 N N   . LEU A 1 319 ? 3.993   15.497  3.835   1.00 38.68  ? 316 LEU A N   1 
ATOM   2458 C CA  . LEU A 1 319 ? 2.690   15.930  4.311   1.00 36.37  ? 316 LEU A CA  1 
ATOM   2459 C C   . LEU A 1 319 ? 2.769   16.394  5.756   1.00 40.64  ? 316 LEU A C   1 
ATOM   2460 O O   . LEU A 1 319 ? 3.223   15.654  6.632   1.00 49.93  ? 316 LEU A O   1 
ATOM   2461 C CB  . LEU A 1 319 ? 1.696   14.790  4.167   1.00 37.09  ? 316 LEU A CB  1 
ATOM   2462 C CG  . LEU A 1 319 ? 0.249   15.229  4.134   1.00 41.47  ? 316 LEU A CG  1 
ATOM   2463 C CD1 . LEU A 1 319 ? -0.479  14.482  3.032   1.00 35.94  ? 316 LEU A CD1 1 
ATOM   2464 C CD2 . LEU A 1 319 ? -0.338  14.947  5.482   1.00 36.72  ? 316 LEU A CD2 1 
ATOM   2465 N N   . VAL A 1 320 ? 2.339   17.610  6.028   1.00 36.75  ? 317 VAL A N   1 
ATOM   2466 C CA  . VAL A 1 320 ? 2.567   18.229  7.321   1.00 30.35  ? 317 VAL A CA  1 
ATOM   2467 C C   . VAL A 1 320 ? 1.278   18.132  8.116   1.00 36.95  ? 317 VAL A C   1 
ATOM   2468 O O   . VAL A 1 320 ? 0.257   18.719  7.747   1.00 39.27  ? 317 VAL A O   1 
ATOM   2469 C CB  . VAL A 1 320 ? 3.026   19.683  7.172   1.00 31.63  ? 317 VAL A CB  1 
ATOM   2470 C CG1 . VAL A 1 320 ? 2.877   20.440  8.491   1.00 41.32  ? 317 VAL A CG1 1 
ATOM   2471 C CG2 . VAL A 1 320 ? 4.457   19.718  6.674   1.00 27.34  ? 317 VAL A CG2 1 
ATOM   2472 N N   . ALA A 1 321 ? 1.326   17.386  9.206   1.00 39.35  ? 318 ALA A N   1 
ATOM   2473 C CA  . ALA A 1 321 ? 0.261   17.350  10.200  1.00 39.30  ? 318 ALA A CA  1 
ATOM   2474 C C   . ALA A 1 321 ? 0.798   18.029  11.456  1.00 40.38  ? 318 ALA A C   1 
ATOM   2475 O O   . ALA A 1 321 ? 1.538   17.425  12.234  1.00 45.02  ? 318 ALA A O   1 
ATOM   2476 C CB  . ALA A 1 321 ? -0.165  15.913  10.474  1.00 36.26  ? 318 ALA A CB  1 
ATOM   2477 N N   . HIS A 1 322 ? 0.435   19.279  11.656  1.00 40.33  ? 319 HIS A N   1 
ATOM   2478 C CA  . HIS A 1 322 ? 0.963   20.038  12.773  1.00 42.89  ? 319 HIS A CA  1 
ATOM   2479 C C   . HIS A 1 322 ? -0.036  20.040  13.921  1.00 44.55  ? 319 HIS A C   1 
ATOM   2480 O O   . HIS A 1 322 ? -1.237  20.212  13.707  1.00 42.70  ? 319 HIS A O   1 
ATOM   2481 C CB  . HIS A 1 322 ? 1.298   21.470  12.342  1.00 45.31  ? 319 HIS A CB  1 
ATOM   2482 C CG  . HIS A 1 322 ? 1.984   22.267  13.408  1.00 67.45  ? 319 HIS A CG  1 
ATOM   2483 N ND1 . HIS A 1 322 ? 1.507   23.482  13.851  1.00 64.84  ? 319 HIS A ND1 1 
ATOM   2484 C CD2 . HIS A 1 322 ? 3.095   22.008  14.148  1.00 67.65  ? 319 HIS A CD2 1 
ATOM   2485 C CE1 . HIS A 1 322 ? 2.300   23.947  14.803  1.00 69.47  ? 319 HIS A CE1 1 
ATOM   2486 N NE2 . HIS A 1 322 ? 3.270   23.071  15.005  1.00 67.48  ? 319 HIS A NE2 1 
ATOM   2487 N N   . GLU A 1 323 ? 0.464   19.848  15.143  1.00 50.68  ? 320 GLU A N   1 
ATOM   2488 C CA  . GLU A 1 323 ? -0.357  19.975  16.343  1.00 48.86  ? 320 GLU A CA  1 
ATOM   2489 C C   . GLU A 1 323 ? 0.304   20.917  17.341  1.00 43.77  ? 320 GLU A C   1 
ATOM   2490 O O   . GLU A 1 323 ? 1.510   21.154  17.303  1.00 44.16  ? 320 GLU A O   1 
ATOM   2491 C CB  . GLU A 1 323 ? -0.635  18.610  17.012  1.00 44.27  ? 320 GLU A CB  1 
ATOM   2492 C CG  . GLU A 1 323 ? 0.608   17.772  17.299  1.00 41.60  ? 320 GLU A CG  1 
ATOM   2493 C CD  . GLU A 1 323 ? 0.289   16.478  18.062  1.00 44.93  ? 320 GLU A CD  1 
ATOM   2494 O OE1 . GLU A 1 323 ? -0.756  15.826  17.803  1.00 47.17  ? 320 GLU A OE1 1 
ATOM   2495 O OE2 . GLU A 1 323 ? 1.093   16.108  18.936  1.00 48.29  ? 320 GLU A OE2 1 
ATOM   2496 N N   . THR A 1 324 ? -0.518  21.444  18.244  1.00 44.36  ? 321 THR A N   1 
ATOM   2497 C CA  . THR A 1 324 ? -0.097  22.379  19.284  1.00 46.66  ? 321 THR A CA  1 
ATOM   2498 C C   . THR A 1 324 ? -0.550  21.845  20.642  1.00 48.89  ? 321 THR A C   1 
ATOM   2499 O O   . THR A 1 324 ? -1.744  21.897  20.969  1.00 47.73  ? 321 THR A O   1 
ATOM   2500 C CB  . THR A 1 324 ? -0.675  23.765  19.003  1.00 49.88  ? 321 THR A CB  1 
ATOM   2501 O OG1 . THR A 1 324 ? 0.079   24.369  17.948  1.00 62.18  ? 321 THR A OG1 1 
ATOM   2502 C CG2 . THR A 1 324 ? -0.650  24.661  20.242  1.00 47.01  ? 321 THR A CG2 1 
ATOM   2503 N N   . VAL A 1 325 ? 0.399   21.341  21.431  1.00 44.73  ? 322 VAL A N   1 
ATOM   2504 C CA  . VAL A 1 325 ? 0.100   20.609  22.669  1.00 47.34  ? 322 VAL A CA  1 
ATOM   2505 C C   . VAL A 1 325 ? 0.288   21.560  23.852  1.00 47.40  ? 322 VAL A C   1 
ATOM   2506 O O   . VAL A 1 325 ? 1.391   21.708  24.384  1.00 42.70  ? 322 VAL A O   1 
ATOM   2507 C CB  . VAL A 1 325 ? 0.976   19.360  22.822  1.00 41.23  ? 322 VAL A CB  1 
ATOM   2508 C CG1 . VAL A 1 325 ? 0.527   18.555  24.031  1.00 42.28  ? 322 VAL A CG1 1 
ATOM   2509 C CG2 . VAL A 1 325 ? 0.981   18.499  21.559  1.00 35.91  ? 322 VAL A CG2 1 
ATOM   2510 N N   . GLN A 1 326 ? -0.808  22.185  24.294  1.00 47.65  ? 323 GLN A N   1 
ATOM   2511 C CA  . GLN A 1 326 ? -0.828  22.896  25.572  1.00 47.17  ? 323 GLN A CA  1 
ATOM   2512 C C   . GLN A 1 326 ? -0.726  21.917  26.741  1.00 48.37  ? 323 GLN A C   1 
ATOM   2513 O O   . GLN A 1 326 ? -1.374  20.868  26.746  1.00 44.00  ? 323 GLN A O   1 
ATOM   2514 C CB  . GLN A 1 326 ? -2.124  23.695  25.710  1.00 48.19  ? 323 GLN A CB  1 
ATOM   2515 C CG  . GLN A 1 326 ? -2.014  24.953  26.583  1.00 63.07  ? 323 GLN A CG  1 
ATOM   2516 C CD  . GLN A 1 326 ? -1.981  26.252  25.748  1.00 73.71  ? 323 GLN A CD  1 
ATOM   2517 O OE1 . GLN A 1 326 ? -1.430  26.276  24.624  1.00 64.18  ? 323 GLN A OE1 1 
ATOM   2518 N NE2 . GLN A 1 326 ? -2.587  27.321  26.285  1.00 56.43  ? 323 GLN A NE2 1 
ATOM   2519 N N   . ASP A 1 327 ? 0.061   22.267  27.757  1.00 50.56  ? 324 ASP A N   1 
ATOM   2520 C CA  . ASP A 1 327 ? 0.179   21.402  28.926  1.00 43.35  ? 324 ASP A CA  1 
ATOM   2521 C C   . ASP A 1 327 ? -0.738  21.868  30.056  1.00 46.69  ? 324 ASP A C   1 
ATOM   2522 O O   . ASP A 1 327 ? -0.986  23.062  30.237  1.00 51.28  ? 324 ASP A O   1 
ATOM   2523 C CB  . ASP A 1 327 ? 1.618   21.338  29.425  1.00 38.65  ? 324 ASP A CB  1 
ATOM   2524 C CG  . ASP A 1 327 ? 2.428   20.238  28.744  1.00 52.80  ? 324 ASP A CG  1 
ATOM   2525 O OD1 . ASP A 1 327 ? 2.128   19.878  27.589  1.00 52.04  ? 324 ASP A OD1 1 
ATOM   2526 O OD2 . ASP A 1 327 ? 3.369   19.711  29.367  1.00 57.96  ? 324 ASP A OD2 1 
ATOM   2527 N N   . GLY A 1 328 ? -1.270  20.900  30.802  1.00 49.12  ? 325 GLY A N   1 
ATOM   2528 C CA  . GLY A 1 328 ? -1.979  21.180  32.034  1.00 33.19  ? 325 GLY A CA  1 
ATOM   2529 C C   . GLY A 1 328 ? -3.480  21.071  31.949  1.00 39.95  ? 325 GLY A C   1 
ATOM   2530 O O   . GLY A 1 328 ? -4.116  21.903  31.301  1.00 43.80  ? 325 GLY A O   1 
ATOM   2531 N N   . PHE A 1 329 ? -4.056  20.073  32.633  1.00 39.92  ? 326 PHE A N   1 
ATOM   2532 C CA  . PHE A 1 329 ? -5.509  19.908  32.670  1.00 38.66  ? 326 PHE A CA  1 
ATOM   2533 C C   . PHE A 1 329 ? -6.246  21.201  33.014  1.00 43.19  ? 326 PHE A C   1 
ATOM   2534 O O   . PHE A 1 329 ? -7.399  21.384  32.610  1.00 40.22  ? 326 PHE A O   1 
ATOM   2535 C CB  . PHE A 1 329 ? -5.892  18.822  33.680  1.00 39.63  ? 326 PHE A CB  1 
ATOM   2536 C CG  . PHE A 1 329 ? -7.388  18.614  33.813  1.00 40.65  ? 326 PHE A CG  1 
ATOM   2537 C CD1 . PHE A 1 329 ? -8.132  19.333  34.729  1.00 38.78  ? 326 PHE A CD1 1 
ATOM   2538 C CD2 . PHE A 1 329 ? -8.050  17.707  33.008  1.00 40.77  ? 326 PHE A CD2 1 
ATOM   2539 C CE1 . PHE A 1 329 ? -9.505  19.146  34.838  1.00 40.57  ? 326 PHE A CE1 1 
ATOM   2540 C CE2 . PHE A 1 329 ? -9.424  17.521  33.116  1.00 38.94  ? 326 PHE A CE2 1 
ATOM   2541 C CZ  . PHE A 1 329 ? -10.148 18.240  34.037  1.00 39.38  ? 326 PHE A CZ  1 
ATOM   2542 N N   . GLU A 1 330 ? -5.621  22.095  33.779  1.00 48.48  ? 327 GLU A N   1 
ATOM   2543 C CA  . GLU A 1 330 ? -6.293  23.332  34.163  1.00 51.98  ? 327 GLU A CA  1 
ATOM   2544 C C   . GLU A 1 330 ? -6.337  24.360  33.033  1.00 51.15  ? 327 GLU A C   1 
ATOM   2545 O O   . GLU A 1 330 ? -7.165  25.275  33.081  1.00 53.50  ? 327 GLU A O   1 
ATOM   2546 C CB  . GLU A 1 330 ? -5.615  23.954  35.394  1.00 50.62  ? 327 GLU A CB  1 
ATOM   2547 C CG  . GLU A 1 330 ? -4.231  24.555  35.145  1.00 47.30  ? 327 GLU A CG  1 
ATOM   2548 C CD  . GLU A 1 330 ? -3.100  23.522  35.150  1.00 54.31  ? 327 GLU A CD  1 
ATOM   2549 O OE1 . GLU A 1 330 ? -3.295  22.355  35.585  1.00 43.78  ? 327 GLU A OE1 1 
ATOM   2550 O OE2 . GLU A 1 330 ? -1.990  23.894  34.715  1.00 58.17  ? 327 GLU A OE2 1 
ATOM   2551 N N   . HIS A 1 331 ? -5.483  24.237  32.021  1.00 45.08  ? 328 HIS A N   1 
ATOM   2552 C CA  . HIS A 1 331 ? -5.514  25.160  30.902  1.00 51.51  ? 328 HIS A CA  1 
ATOM   2553 C C   . HIS A 1 331 ? -6.353  24.639  29.742  1.00 52.20  ? 328 HIS A C   1 
ATOM   2554 O O   . HIS A 1 331 ? -6.229  25.161  28.622  1.00 49.48  ? 328 HIS A O   1 
ATOM   2555 C CB  . HIS A 1 331 ? -4.086  25.464  30.431  1.00 53.19  ? 328 HIS A CB  1 
ATOM   2556 C CG  . HIS A 1 331 ? -3.220  26.055  31.494  1.00 61.86  ? 328 HIS A CG  1 
ATOM   2557 N ND1 . HIS A 1 331 ? -1.949  25.594  31.759  1.00 64.45  ? 328 HIS A ND1 1 
ATOM   2558 C CD2 . HIS A 1 331 ? -3.449  27.058  32.376  1.00 61.61  ? 328 HIS A CD2 1 
ATOM   2559 C CE1 . HIS A 1 331 ? -1.427  26.288  32.757  1.00 62.54  ? 328 HIS A CE1 1 
ATOM   2560 N NE2 . HIS A 1 331 ? -2.317  27.183  33.149  1.00 61.67  ? 328 HIS A NE2 1 
ATOM   2561 N N   . ILE A 1 332 ? -7.200  23.624  29.981  1.00 45.36  ? 329 ILE A N   1 
ATOM   2562 C CA  . ILE A 1 332 ? -8.055  23.104  28.906  1.00 48.51  ? 329 ILE A CA  1 
ATOM   2563 C C   . ILE A 1 332 ? -8.957  24.192  28.316  1.00 50.90  ? 329 ILE A C   1 
ATOM   2564 O O   . ILE A 1 332 ? -8.923  24.390  27.092  1.00 53.89  ? 329 ILE A O   1 
ATOM   2565 C CB  . ILE A 1 332 ? -8.831  21.869  29.390  1.00 43.48  ? 329 ILE A CB  1 
ATOM   2566 C CG1 . ILE A 1 332 ? -7.985  20.606  29.324  1.00 38.20  ? 329 ILE A CG1 1 
ATOM   2567 C CG2 . ILE A 1 332 ? -10.081 21.626  28.562  1.00 39.09  ? 329 ILE A CG2 1 
ATOM   2568 C CD1 . ILE A 1 332 ? -8.735  19.425  29.880  1.00 37.59  ? 329 ILE A CD1 1 
ATOM   2569 N N   . PRO A 1 333 ? -9.751  24.932  29.103  1.00 50.07  ? 330 PRO A N   1 
ATOM   2570 C CA  . PRO A 1 333 ? -10.588 25.978  28.488  1.00 48.23  ? 330 PRO A CA  1 
ATOM   2571 C C   . PRO A 1 333 ? -9.791  27.118  27.861  1.00 46.63  ? 330 PRO A C   1 
ATOM   2572 O O   . PRO A 1 333 ? -10.266 27.752  26.912  1.00 42.94  ? 330 PRO A O   1 
ATOM   2573 C CB  . PRO A 1 333 ? -11.448 26.462  29.665  1.00 48.37  ? 330 PRO A CB  1 
ATOM   2574 C CG  . PRO A 1 333 ? -11.463 25.330  30.637  1.00 42.77  ? 330 PRO A CG  1 
ATOM   2575 C CD  . PRO A 1 333 ? -10.083 24.749  30.531  1.00 46.38  ? 330 PRO A CD  1 
ATOM   2576 N N   . ALA A 1 334 ? -8.603  27.416  28.377  1.00 47.61  ? 331 ALA A N   1 
ATOM   2577 C CA  . ALA A 1 334 ? -7.763  28.413  27.731  1.00 48.27  ? 331 ALA A CA  1 
ATOM   2578 C C   . ALA A 1 334 ? -7.279  27.908  26.371  1.00 54.97  ? 331 ALA A C   1 
ATOM   2579 O O   . ALA A 1 334 ? -7.192  28.680  25.408  1.00 48.78  ? 331 ALA A O   1 
ATOM   2580 C CB  . ALA A 1 334 ? -6.588  28.770  28.645  1.00 35.29  ? 331 ALA A CB  1 
ATOM   2581 N N   . ALA A 1 335 ? -6.972  26.609  26.272  1.00 53.76  ? 332 ALA A N   1 
ATOM   2582 C CA  . ALA A 1 335 ? -6.676  26.017  24.971  1.00 48.69  ? 332 ALA A CA  1 
ATOM   2583 C C   . ALA A 1 335 ? -7.902  26.042  24.058  1.00 48.66  ? 332 ALA A C   1 
ATOM   2584 O O   . ALA A 1 335 ? -7.795  26.390  22.877  1.00 53.60  ? 332 ALA A O   1 
ATOM   2585 C CB  . ALA A 1 335 ? -6.148  24.588  25.143  1.00 43.20  ? 332 ALA A CB  1 
ATOM   2586 N N   . TYR A 1 336 ? -9.080  25.692  24.577  1.00 40.34  ? 333 TYR A N   1 
ATOM   2587 C CA  . TYR A 1 336 ? -10.274 25.731  23.737  1.00 47.34  ? 333 TYR A CA  1 
ATOM   2588 C C   . TYR A 1 336 ? -10.577 27.134  23.246  1.00 50.20  ? 333 TYR A C   1 
ATOM   2589 O O   . TYR A 1 336 ? -11.070 27.302  22.126  1.00 49.41  ? 333 TYR A O   1 
ATOM   2590 C CB  . TYR A 1 336 ? -11.445 25.187  24.515  1.00 40.40  ? 333 TYR A CB  1 
ATOM   2591 C CG  . TYR A 1 336 ? -12.804 25.226  23.874  1.00 36.89  ? 333 TYR A CG  1 
ATOM   2592 C CD1 . TYR A 1 336 ? -13.115 24.445  22.771  1.00 37.77  ? 333 TYR A CD1 1 
ATOM   2593 C CD2 . TYR A 1 336 ? -13.832 25.945  24.480  1.00 43.79  ? 333 TYR A CD2 1 
ATOM   2594 C CE1 . TYR A 1 336 ? -14.434 24.436  22.246  1.00 44.28  ? 333 TYR A CE1 1 
ATOM   2595 C CE2 . TYR A 1 336 ? -15.132 25.948  23.973  1.00 47.85  ? 333 TYR A CE2 1 
ATOM   2596 C CZ  . TYR A 1 336 ? -15.428 25.201  22.861  1.00 47.64  ? 333 TYR A CZ  1 
ATOM   2597 O OH  . TYR A 1 336 ? -16.717 25.242  22.407  1.00 46.57  ? 333 TYR A OH  1 
ATOM   2598 N N   . GLN A 1 337 ? -10.302 28.148  24.073  1.00 52.37  ? 334 GLN A N   1 
ATOM   2599 C CA  . GLN A 1 337 ? -10.609 29.518  23.684  1.00 54.22  ? 334 GLN A CA  1 
ATOM   2600 C C   . GLN A 1 337 ? -9.752  29.934  22.505  1.00 52.97  ? 334 GLN A C   1 
ATOM   2601 O O   . GLN A 1 337 ? -10.215 30.661  21.625  1.00 50.07  ? 334 GLN A O   1 
ATOM   2602 C CB  . GLN A 1 337 ? -10.400 30.483  24.861  1.00 51.46  ? 334 GLN A CB  1 
ATOM   2603 C CG  . GLN A 1 337 ? -10.991 31.902  24.654  1.00 47.03  ? 334 GLN A CG  1 
ATOM   2604 C CD  . GLN A 1 337 ? -12.508 31.957  24.844  1.00 56.54  ? 334 GLN A CD  1 
ATOM   2605 O OE1 . GLN A 1 337 ? -13.027 31.630  25.915  1.00 63.34  ? 334 GLN A OE1 1 
ATOM   2606 N NE2 . GLN A 1 337 ? -13.225 32.372  23.803  1.00 58.24  ? 334 GLN A NE2 1 
ATOM   2607 N N   . THR A 1 338 ? -8.511  29.464  22.462  1.00 47.66  ? 335 THR A N   1 
ATOM   2608 C CA  . THR A 1 338 ? -7.626  29.867  21.386  1.00 56.31  ? 335 THR A CA  1 
ATOM   2609 C C   . THR A 1 338 ? -8.083  29.358  20.000  1.00 59.72  ? 335 THR A C   1 
ATOM   2610 O O   . THR A 1 338 ? -7.488  29.743  18.994  1.00 61.07  ? 335 THR A O   1 
ATOM   2611 C CB  . THR A 1 338 ? -6.196  29.426  21.731  1.00 50.55  ? 335 THR A CB  1 
ATOM   2612 O OG1 . THR A 1 338 ? -5.261  30.264  21.049  1.00 71.40  ? 335 THR A OG1 1 
ATOM   2613 C CG2 . THR A 1 338 ? -5.930  28.015  21.325  1.00 47.97  ? 335 THR A CG2 1 
ATOM   2614 N N   . LEU A 1 339 ? -9.145  28.554  19.908  1.00 59.67  ? 336 LEU A N   1 
ATOM   2615 C CA  . LEU A 1 339 ? -9.691  28.167  18.605  1.00 59.33  ? 336 LEU A CA  1 
ATOM   2616 C C   . LEU A 1 339 ? -10.586 29.255  18.038  1.00 59.38  ? 336 LEU A C   1 
ATOM   2617 O O   . LEU A 1 339 ? -10.573 29.517  16.833  1.00 56.82  ? 336 LEU A O   1 
ATOM   2618 C CB  . LEU A 1 339 ? -10.488 26.867  18.716  1.00 51.14  ? 336 LEU A CB  1 
ATOM   2619 C CG  . LEU A 1 339 ? -9.684  25.579  18.818  1.00 54.92  ? 336 LEU A CG  1 
ATOM   2620 C CD1 . LEU A 1 339 ? -10.556 24.504  19.415  1.00 47.72  ? 336 LEU A CD1 1 
ATOM   2621 C CD2 . LEU A 1 339 ? -9.181  25.176  17.444  1.00 61.57  ? 336 LEU A CD2 1 
ATOM   2622 N N   . PHE A 1 340 ? -11.422 29.845  18.883  1.00 66.08  ? 337 PHE A N   1 
ATOM   2623 C CA  . PHE A 1 340 ? -12.260 30.964  18.488  1.00 64.82  ? 337 PHE A CA  1 
ATOM   2624 C C   . PHE A 1 340 ? -11.536 32.240  18.876  1.00 70.36  ? 337 PHE A C   1 
ATOM   2625 O O   . PHE A 1 340 ? -11.105 32.383  20.023  1.00 81.80  ? 337 PHE A O   1 
ATOM   2626 C CB  . PHE A 1 340 ? -13.623 30.936  19.170  1.00 56.30  ? 337 PHE A CB  1 
ATOM   2627 C CG  . PHE A 1 340 ? -14.250 29.590  19.249  1.00 57.44  ? 337 PHE A CG  1 
ATOM   2628 C CD1 . PHE A 1 340 ? -13.887 28.693  20.246  1.00 51.66  ? 337 PHE A CD1 1 
ATOM   2629 C CD2 . PHE A 1 340 ? -15.251 29.241  18.366  1.00 52.45  ? 337 PHE A CD2 1 
ATOM   2630 C CE1 . PHE A 1 340 ? -14.496 27.463  20.333  1.00 50.55  ? 337 PHE A CE1 1 
ATOM   2631 C CE2 . PHE A 1 340 ? -15.862 28.011  18.450  1.00 56.43  ? 337 PHE A CE2 1 
ATOM   2632 C CZ  . PHE A 1 340 ? -15.486 27.120  19.437  1.00 52.86  ? 337 PHE A CZ  1 
ATOM   2633 N N   . SER A 1 341 ? -11.514 33.224  18.002  1.00 61.56  ? 338 SER A N   1 
ATOM   2634 C CA  . SER A 1 341 ? -10.970 34.527  18.362  1.00 77.47  ? 338 SER A CA  1 
ATOM   2635 C C   . SER A 1 341 ? -9.464  34.639  18.466  1.00 81.77  ? 338 SER A C   1 
ATOM   2636 O O   . SER A 1 341 ? -8.910  35.664  18.113  1.00 84.57  ? 338 SER A O   1 
ATOM   2637 C CB  . SER A 1 341 ? -11.585 35.043  19.688  1.00 82.91  ? 338 SER A CB  1 
ATOM   2638 O OG  . SER A 1 341 ? -12.883 34.526  19.922  1.00 76.67  ? 338 SER A OG  1 
ATOM   2639 N N   . ALA A 1 342 ? -8.810  33.629  18.980  1.00 73.13  ? 339 ALA A N   1 
ATOM   2640 C CA  . ALA A 1 342 ? -7.367  33.707  19.180  1.00 75.01  ? 339 ALA A CA  1 
ATOM   2641 C C   . ALA A 1 342 ? -6.618  32.780  18.232  1.00 84.19  ? 339 ALA A C   1 
ATOM   2642 O O   . ALA A 1 342 ? -5.484  32.375  18.519  1.00 85.57  ? 339 ALA A O   1 
ATOM   2643 C CB  . ALA A 1 342 ? -6.991  33.407  20.629  1.00 70.71  ? 339 ALA A CB  1 
ATOM   2644 N N   . SER A 1 343 ? -7.239  32.461  17.084  1.00 83.68  ? 340 SER A N   1 
ATOM   2645 C CA  . SER A 1 343 ? -6.653  31.567  16.083  1.00 80.31  ? 340 SER A CA  1 
ATOM   2646 C C   . SER A 1 343 ? -5.252  32.002  15.641  1.00 87.83  ? 340 SER A C   1 
ATOM   2647 O O   . SER A 1 343 ? -4.547  31.228  14.974  1.00 89.34  ? 340 SER A O   1 
ATOM   2648 C CB  . SER A 1 343 ? -7.603  31.469  14.875  1.00 84.60  ? 340 SER A CB  1 
ATOM   2649 O OG  . SER A 1 343 ? -8.673  32.416  14.924  1.00 74.95  ? 340 SER A OG  1 
ATOM   2650 N N   . GLU A 1 344 ? -4.843  33.225  15.997  1.00 86.87  ? 341 GLU A N   1 
ATOM   2651 C CA  . GLU A 1 344 ? -3.481  33.700  15.787  1.00 82.54  ? 341 GLU A CA  1 
ATOM   2652 C C   . GLU A 1 344 ? -2.508  32.917  16.647  1.00 88.88  ? 341 GLU A C   1 
ATOM   2653 O O   . GLU A 1 344 ? -2.710  32.790  17.859  1.00 89.84  ? 341 GLU A O   1 
ATOM   2654 C CB  . GLU A 1 344 ? -3.397  35.192  16.116  1.00 86.16  ? 341 GLU A CB  1 
ATOM   2655 C CG  . GLU A 1 344 ? -4.220  36.073  15.184  1.00 82.08  ? 341 GLU A CG  1 
ATOM   2656 C CD  . GLU A 1 344 ? -5.667  36.180  15.625  1.00 83.45  ? 341 GLU A CD  1 
ATOM   2657 O OE1 . GLU A 1 344 ? -6.026  35.515  16.625  1.00 81.80  ? 341 GLU A OE1 1 
ATOM   2658 O OE2 . GLU A 1 344 ? -6.431  36.942  14.994  1.00 69.05  ? 341 GLU A OE2 1 
ATOM   2659 N N   . SER A 1 345 ? -1.510  32.296  16.012  1.00 87.54  ? 342 SER A N   1 
ATOM   2660 C CA  . SER A 1 345 ? -0.503  31.457  16.709  1.00 90.27  ? 342 SER A CA  1 
ATOM   2661 C C   . SER A 1 345 ? -0.953  30.032  16.712  1.00 86.69  ? 342 SER A C   1 
ATOM   2662 O O   . SER A 1 345 ? -0.216  29.148  17.134  1.00 81.75  ? 342 SER A O   1 
ATOM   2663 C CB  . SER A 1 345 ? -0.216  31.880  18.157  1.00 88.18  ? 342 SER A CB  1 
ATOM   2664 O OG  . SER A 1 345 ? 0.024   33.271  18.253  1.00 81.58  ? 342 SER A OG  1 
ATOM   2665 N N   . ASN A 1 346 ? -2.150  29.790  16.211  1.00 85.22  ? 343 ASN A N   1 
ATOM   2666 C CA  . ASN A 1 346 ? -2.717  28.447  16.291  1.00 83.41  ? 343 ASN A CA  1 
ATOM   2667 C C   . ASN A 1 346 ? -2.505  27.738  14.964  1.00 77.57  ? 343 ASN A C   1 
ATOM   2668 O O   . ASN A 1 346 ? -3.124  28.094  13.956  1.00 82.19  ? 343 ASN A O   1 
ATOM   2669 C CB  . ASN A 1 346 ? -4.205  28.505  16.620  1.00 80.42  ? 343 ASN A CB  1 
ATOM   2670 C CG  . ASN A 1 346 ? -4.512  27.999  18.002  1.00 74.22  ? 343 ASN A CG  1 
ATOM   2671 O OD1 . ASN A 1 346 ? -3.630  27.935  18.875  1.00 66.04  ? 343 ASN A OD1 1 
ATOM   2672 N ND2 . ASN A 1 346 ? -5.770  27.634  18.221  1.00 71.95  ? 343 ASN A ND2 1 
ATOM   2673 N N   . ARG A 1 347 ? -1.641  26.731  14.962  1.00 68.19  ? 344 ARG A N   1 
ATOM   2674 C CA  . ARG A 1 347 ? -1.440  25.899  13.788  1.00 70.07  ? 344 ARG A CA  1 
ATOM   2675 C C   . ARG A 1 347 ? -1.895  24.486  14.119  1.00 60.75  ? 344 ARG A C   1 
ATOM   2676 O O   . ARG A 1 347 ? -1.455  23.908  15.119  1.00 54.31  ? 344 ARG A O   1 
ATOM   2677 C CB  . ARG A 1 347 ? 0.022   25.916  13.328  1.00 66.13  ? 344 ARG A CB  1 
ATOM   2678 C CG  . ARG A 1 347 ? 0.581   27.272  13.025  1.00 73.48  ? 344 ARG A CG  1 
ATOM   2679 C CD  . ARG A 1 347 ? -0.367  28.093  12.160  1.00 74.09  ? 344 ARG A CD  1 
ATOM   2680 N NE  . ARG A 1 347 ? -0.430  29.455  12.670  1.00 77.99  ? 344 ARG A NE  1 
ATOM   2681 C CZ  . ARG A 1 347 ? 0.550   30.338  12.535  1.00 80.57  ? 344 ARG A CZ  1 
ATOM   2682 N NH1 . ARG A 1 347 ? 1.640   30.055  11.837  1.00 73.61  ? 344 ARG A NH1 1 
ATOM   2683 N NH2 . ARG A 1 347 ? 0.435   31.530  13.118  1.00 80.09  ? 344 ARG A NH2 1 
ATOM   2684 N N   . GLY A 1 348 ? -2.815  23.960  13.306  1.00 55.05  ? 345 GLY A N   1 
ATOM   2685 C CA  . GLY A 1 348 ? -3.141  22.546  13.333  1.00 49.51  ? 345 GLY A CA  1 
ATOM   2686 C C   . GLY A 1 348 ? -4.049  22.132  14.483  1.00 45.77  ? 345 GLY A C   1 
ATOM   2687 O O   . GLY A 1 348 ? -4.904  22.883  14.950  1.00 40.33  ? 345 GLY A O   1 
ATOM   2688 N N   . LYS A 1 349 ? -3.860  20.898  14.927  1.00 39.80  ? 346 LYS A N   1 
ATOM   2689 C CA  . LYS A 1 349 ? -4.667  20.363  16.006  1.00 42.22  ? 346 LYS A CA  1 
ATOM   2690 C C   . LYS A 1 349 ? -4.166  20.891  17.344  1.00 42.80  ? 346 LYS A C   1 
ATOM   2691 O O   . LYS A 1 349 ? -2.974  20.791  17.656  1.00 40.98  ? 346 LYS A O   1 
ATOM   2692 C CB  . LYS A 1 349 ? -4.628  18.832  15.998  1.00 40.79  ? 346 LYS A CB  1 
ATOM   2693 C CG  . LYS A 1 349 ? -5.553  18.182  17.030  1.00 39.72  ? 346 LYS A CG  1 
ATOM   2694 C CD  . LYS A 1 349 ? -6.925  17.936  16.435  1.00 38.32  ? 346 LYS A CD  1 
ATOM   2695 C CE  . LYS A 1 349 ? -8.024  18.310  17.375  1.00 37.26  ? 346 LYS A CE  1 
ATOM   2696 N NZ  . LYS A 1 349 ? -8.315  19.752  17.239  1.00 44.75  ? 346 LYS A NZ  1 
ATOM   2697 N N   . VAL A 1 350 ? -5.082  21.434  18.138  1.00 38.92  ? 347 VAL A N   1 
ATOM   2698 C CA  . VAL A 1 350 ? -4.780  21.820  19.509  1.00 47.46  ? 347 VAL A CA  1 
ATOM   2699 C C   . VAL A 1 350 ? -5.173  20.677  20.435  1.00 43.72  ? 347 VAL A C   1 
ATOM   2700 O O   . VAL A 1 350 ? -6.321  20.221  20.423  1.00 46.50  ? 347 VAL A O   1 
ATOM   2701 C CB  . VAL A 1 350 ? -5.504  23.114  19.899  1.00 48.57  ? 347 VAL A CB  1 
ATOM   2702 C CG1 . VAL A 1 350 ? -5.002  23.581  21.251  1.00 41.69  ? 347 VAL A CG1 1 
ATOM   2703 C CG2 . VAL A 1 350 ? -5.298  24.178  18.822  1.00 43.76  ? 347 VAL A CG2 1 
ATOM   2704 N N   . LEU A 1 351 ? -4.219  20.213  21.229  1.00 39.80  ? 348 LEU A N   1 
ATOM   2705 C CA  . LEU A 1 351 ? -4.441  19.210  22.258  1.00 44.64  ? 348 LEU A CA  1 
ATOM   2706 C C   . LEU A 1 351 ? -4.042  19.778  23.615  1.00 47.49  ? 348 LEU A C   1 
ATOM   2707 O O   . LEU A 1 351 ? -3.295  20.755  23.704  1.00 50.23  ? 348 LEU A O   1 
ATOM   2708 C CB  . LEU A 1 351 ? -3.612  17.958  21.994  1.00 39.31  ? 348 LEU A CB  1 
ATOM   2709 C CG  . LEU A 1 351 ? -3.680  17.460  20.580  1.00 39.91  ? 348 LEU A CG  1 
ATOM   2710 C CD1 . LEU A 1 351 ? -2.775  16.256  20.415  1.00 36.25  ? 348 LEU A CD1 1 
ATOM   2711 C CD2 . LEU A 1 351 ? -5.133  17.109  20.367  1.00 46.88  ? 348 LEU A CD2 1 
ATOM   2712 N N   . VAL A 1 352 ? -4.501  19.138  24.683  1.00 39.50  ? 349 VAL A N   1 
ATOM   2713 C CA  . VAL A 1 352 ? -3.937  19.376  26.005  1.00 45.20  ? 349 VAL A CA  1 
ATOM   2714 C C   . VAL A 1 352 ? -3.341  18.070  26.517  1.00 41.10  ? 349 VAL A C   1 
ATOM   2715 O O   . VAL A 1 352 ? -4.042  17.056  26.616  1.00 46.24  ? 349 VAL A O   1 
ATOM   2716 C CB  . VAL A 1 352 ? -4.967  19.929  27.000  1.00 40.02  ? 349 VAL A CB  1 
ATOM   2717 C CG1 . VAL A 1 352 ? -4.265  20.184  28.310  1.00 42.21  ? 349 VAL A CG1 1 
ATOM   2718 C CG2 . VAL A 1 352 ? -5.596  21.198  26.470  1.00 34.80  ? 349 VAL A CG2 1 
ATOM   2719 N N   . ARG A 1 353 ? -2.052  18.090  26.834  1.00 39.19  ? 350 ARG A N   1 
ATOM   2720 C CA  . ARG A 1 353 ? -1.423  16.991  27.557  1.00 43.02  ? 350 ARG A CA  1 
ATOM   2721 C C   . ARG A 1 353 ? -1.663  17.188  29.053  1.00 47.40  ? 350 ARG A C   1 
ATOM   2722 O O   . ARG A 1 353 ? -1.286  18.223  29.615  1.00 44.97  ? 350 ARG A O   1 
ATOM   2723 C CB  . ARG A 1 353 ? 0.074   16.917  27.260  1.00 42.87  ? 350 ARG A CB  1 
ATOM   2724 C CG  . ARG A 1 353 ? 0.778   15.738  27.906  1.00 39.72  ? 350 ARG A CG  1 
ATOM   2725 C CD  . ARG A 1 353 ? 2.243   15.665  27.492  1.00 40.20  ? 350 ARG A CD  1 
ATOM   2726 N NE  . ARG A 1 353 ? 2.937   16.923  27.757  1.00 44.31  ? 350 ARG A NE  1 
ATOM   2727 C CZ  . ARG A 1 353 ? 4.246   17.112  27.617  1.00 47.31  ? 350 ARG A CZ  1 
ATOM   2728 N NH1 . ARG A 1 353 ? 5.064   16.119  27.285  1.00 32.42  ? 350 ARG A NH1 1 
ATOM   2729 N NH2 . ARG A 1 353 ? 4.747   18.330  27.805  1.00 50.53  ? 350 ARG A NH2 1 
ATOM   2730 N N   . VAL A 1 354 ? -2.309  16.205  29.682  1.00 48.18  ? 351 VAL A N   1 
ATOM   2731 C CA  . VAL A 1 354 ? -2.558  16.199  31.118  1.00 46.66  ? 351 VAL A CA  1 
ATOM   2732 C C   . VAL A 1 354 ? -1.436  15.491  31.846  1.00 43.90  ? 351 VAL A C   1 
ATOM   2733 O O   . VAL A 1 354 ? -0.517  16.134  32.336  1.00 53.23  ? 351 VAL A O   1 
ATOM   2734 C CB  . VAL A 1 354 ? -3.882  15.530  31.445  1.00 45.90  ? 351 VAL A CB  1 
ATOM   2735 C CG1 . VAL A 1 354 ? -4.000  15.337  32.952  1.00 42.12  ? 351 VAL A CG1 1 
ATOM   2736 C CG2 . VAL A 1 354 ? -5.037  16.353  30.888  1.00 41.62  ? 351 VAL A CG2 1 
ATOM   2737 N N   . LEU B 1 1   ? -33.679 25.941  -55.728 1.00 46.37  ? -2  LEU B N   1 
ATOM   2738 C CA  . LEU B 1 1   ? -34.154 27.301  -55.444 1.00 60.96  ? -2  LEU B CA  1 
ATOM   2739 C C   . LEU B 1 1   ? -35.679 27.430  -55.283 1.00 69.52  ? -2  LEU B C   1 
ATOM   2740 O O   . LEU B 1 1   ? -36.466 26.698  -55.913 1.00 64.59  ? -2  LEU B O   1 
ATOM   2741 C CB  . LEU B 1 1   ? -33.717 28.279  -56.533 1.00 61.17  ? -2  LEU B CB  1 
ATOM   2742 C CG  . LEU B 1 1   ? -32.277 28.768  -56.578 1.00 65.44  ? -2  LEU B CG  1 
ATOM   2743 C CD1 . LEU B 1 1   ? -31.366 27.633  -57.024 1.00 72.82  ? -2  LEU B CD1 1 
ATOM   2744 C CD2 . LEU B 1 1   ? -32.174 29.956  -57.517 1.00 60.26  ? -2  LEU B CD2 1 
ATOM   2745 N N   . GLY B 1 2   ? -36.067 28.400  -54.458 1.00 59.31  ? -1  GLY B N   1 
ATOM   2746 C CA  . GLY B 1 2   ? -37.453 28.674  -54.124 1.00 49.25  ? -1  GLY B CA  1 
ATOM   2747 C C   . GLY B 1 2   ? -37.574 29.128  -52.683 1.00 53.73  ? -1  GLY B C   1 
ATOM   2748 O O   . GLY B 1 2   ? -36.580 29.195  -51.952 1.00 55.25  ? -1  GLY B O   1 
ATOM   2749 N N   . SER B 1 3   ? -38.789 29.456  -52.265 1.00 49.94  ? 0   SER B N   1 
ATOM   2750 C CA  . SER B 1 3   ? -39.076 29.822  -50.887 1.00 42.58  ? 0   SER B CA  1 
ATOM   2751 C C   . SER B 1 3   ? -40.392 29.165  -50.503 1.00 39.10  ? 0   SER B C   1 
ATOM   2752 O O   . SER B 1 3   ? -41.121 28.662  -51.359 1.00 37.84  ? 0   SER B O   1 
ATOM   2753 C CB  . SER B 1 3   ? -39.159 31.339  -50.717 1.00 44.94  ? 0   SER B CB  1 
ATOM   2754 O OG  . SER B 1 3   ? -40.439 31.811  -51.122 1.00 47.91  ? 0   SER B OG  1 
ATOM   2755 N N   . MET B 1 4   ? -40.705 29.160  -49.211 1.00 38.73  ? 1   MET B N   1 
ATOM   2756 C CA  . MET B 1 4   ? -42.047 28.772  -48.791 1.00 37.79  ? 1   MET B CA  1 
ATOM   2757 C C   . MET B 1 4   ? -42.482 29.569  -47.573 1.00 31.75  ? 1   MET B C   1 
ATOM   2758 O O   . MET B 1 4   ? -41.666 29.891  -46.713 1.00 29.92  ? 1   MET B O   1 
ATOM   2759 C CB  . MET B 1 4   ? -42.157 27.265  -48.501 1.00 38.15  ? 1   MET B CB  1 
ATOM   2760 C CG  . MET B 1 4   ? -41.259 26.713  -47.415 1.00 42.94  ? 1   MET B CG  1 
ATOM   2761 S SD  . MET B 1 4   ? -41.940 25.193  -46.695 1.00 58.64  ? 1   MET B SD  1 
ATOM   2762 C CE  . MET B 1 4   ? -42.381 24.221  -48.156 1.00 38.49  ? 1   MET B CE  1 
ATOM   2763 N N   . LYS B 1 5   ? -43.765 29.907  -47.524 1.00 32.82  ? 2   LYS B N   1 
ATOM   2764 C CA  . LYS B 1 5   ? -44.302 30.649  -46.394 1.00 34.38  ? 2   LYS B CA  1 
ATOM   2765 C C   . LYS B 1 5   ? -44.414 29.735  -45.168 1.00 37.09  ? 2   LYS B C   1 
ATOM   2766 O O   . LYS B 1 5   ? -44.899 28.601  -45.264 1.00 35.74  ? 2   LYS B O   1 
ATOM   2767 C CB  . LYS B 1 5   ? -45.671 31.242  -46.742 1.00 30.94  ? 2   LYS B CB  1 
ATOM   2768 C CG  . LYS B 1 5   ? -45.704 32.178  -47.930 1.00 35.20  ? 2   LYS B CG  1 
ATOM   2769 C CD  . LYS B 1 5   ? -44.867 33.419  -47.734 1.00 36.51  ? 2   LYS B CD  1 
ATOM   2770 C CE  . LYS B 1 5   ? -44.564 34.112  -49.060 1.00 42.68  ? 2   LYS B CE  1 
ATOM   2771 N NZ  . LYS B 1 5   ? -43.884 33.204  -50.069 1.00 49.54  ? 2   LYS B NZ  1 
ATOM   2772 N N   . THR B 1 6   ? -43.965 30.228  -44.012 1.00 31.15  ? 3   THR B N   1 
ATOM   2773 C CA  . THR B 1 6   ? -44.073 29.495  -42.763 1.00 30.51  ? 3   THR B CA  1 
ATOM   2774 C C   . THR B 1 6   ? -44.661 30.405  -41.691 1.00 32.89  ? 3   THR B C   1 
ATOM   2775 O O   . THR B 1 6   ? -44.650 31.633  -41.804 1.00 32.36  ? 3   THR B O   1 
ATOM   2776 C CB  . THR B 1 6   ? -42.707 28.945  -42.280 1.00 29.50  ? 3   THR B CB  1 
ATOM   2777 O OG1 . THR B 1 6   ? -41.855 30.013  -41.824 1.00 31.59  ? 3   THR B OG1 1 
ATOM   2778 C CG2 . THR B 1 6   ? -42.020 28.206  -43.380 1.00 32.64  ? 3   THR B CG2 1 
ATOM   2779 N N   . GLU B 1 7   ? -45.165 29.789  -40.630 1.00 29.70  ? 4   GLU B N   1 
ATOM   2780 C CA  . GLU B 1 7   ? -45.566 30.538  -39.460 1.00 30.26  ? 4   GLU B CA  1 
ATOM   2781 C C   . GLU B 1 7   ? -44.614 30.244  -38.298 1.00 31.97  ? 4   GLU B C   1 
ATOM   2782 O O   . GLU B 1 7   ? -44.047 29.150  -38.182 1.00 30.67  ? 4   GLU B O   1 
ATOM   2783 C CB  . GLU B 1 7   ? -47.010 30.221  -39.103 1.00 29.51  ? 4   GLU B CB  1 
ATOM   2784 C CG  . GLU B 1 7   ? -47.989 30.949  -40.008 1.00 36.37  ? 4   GLU B CG  1 
ATOM   2785 C CD  . GLU B 1 7   ? -49.442 30.810  -39.551 1.00 47.03  ? 4   GLU B CD  1 
ATOM   2786 O OE1 . GLU B 1 7   ? -49.768 29.774  -38.918 1.00 45.88  ? 4   GLU B OE1 1 
ATOM   2787 O OE2 . GLU B 1 7   ? -50.250 31.739  -39.815 1.00 50.42  ? 4   GLU B OE2 1 
ATOM   2788 N N   . ARG B 1 8   ? -44.417 31.251  -37.455 1.00 26.29  ? 5   ARG B N   1 
ATOM   2789 C CA  . ARG B 1 8   ? -43.504 31.163  -36.327 1.00 28.56  ? 5   ARG B CA  1 
ATOM   2790 C C   . ARG B 1 8   ? -44.126 31.899  -35.154 1.00 31.72  ? 5   ARG B C   1 
ATOM   2791 O O   . ARG B 1 8   ? -44.807 32.920  -35.331 1.00 27.33  ? 5   ARG B O   1 
ATOM   2792 C CB  . ARG B 1 8   ? -42.124 31.784  -36.626 1.00 23.63  ? 5   ARG B CB  1 
ATOM   2793 C CG  . ARG B 1 8   ? -41.365 31.138  -37.767 1.00 26.92  ? 5   ARG B CG  1 
ATOM   2794 C CD  . ARG B 1 8   ? -39.976 31.707  -37.863 1.00 26.79  ? 5   ARG B CD  1 
ATOM   2795 N NE  . ARG B 1 8   ? -40.010 33.161  -37.918 1.00 29.52  ? 5   ARG B NE  1 
ATOM   2796 C CZ  . ARG B 1 8   ? -39.100 33.948  -37.360 1.00 33.64  ? 5   ARG B CZ  1 
ATOM   2797 N NH1 . ARG B 1 8   ? -38.059 33.448  -36.700 1.00 31.49  ? 5   ARG B NH1 1 
ATOM   2798 N NH2 . ARG B 1 8   ? -39.243 35.269  -37.451 1.00 28.99  ? 5   ARG B NH2 1 
ATOM   2799 N N   . TRP B 1 9   ? -43.895 31.371  -33.950 1.00 26.58  ? 6   TRP B N   1 
ATOM   2800 C CA  . TRP B 1 9   ? -44.161 32.110  -32.733 1.00 24.80  ? 6   TRP B CA  1 
ATOM   2801 C C   . TRP B 1 9   ? -42.850 32.760  -32.317 1.00 27.29  ? 6   TRP B C   1 
ATOM   2802 O O   . TRP B 1 9   ? -41.834 32.074  -32.155 1.00 31.12  ? 6   TRP B O   1 
ATOM   2803 C CB  . TRP B 1 9   ? -44.729 31.209  -31.637 1.00 24.44  ? 6   TRP B CB  1 
ATOM   2804 C CG  . TRP B 1 9   ? -46.197 30.859  -31.826 1.00 29.67  ? 6   TRP B CG  1 
ATOM   2805 C CD1 . TRP B 1 9   ? -46.708 29.709  -32.370 1.00 27.87  ? 6   TRP B CD1 1 
ATOM   2806 C CD2 . TRP B 1 9   ? -47.329 31.662  -31.459 1.00 29.15  ? 6   TRP B CD2 1 
ATOM   2807 N NE1 . TRP B 1 9   ? -48.084 29.755  -32.369 1.00 27.10  ? 6   TRP B NE1 1 
ATOM   2808 C CE2 . TRP B 1 9   ? -48.486 30.946  -31.822 1.00 29.04  ? 6   TRP B CE2 1 
ATOM   2809 C CE3 . TRP B 1 9   ? -47.475 32.920  -30.863 1.00 30.21  ? 6   TRP B CE3 1 
ATOM   2810 C CZ2 . TRP B 1 9   ? -49.769 31.449  -31.607 1.00 30.36  ? 6   TRP B CZ2 1 
ATOM   2811 C CZ3 . TRP B 1 9   ? -48.747 33.410  -30.650 1.00 26.54  ? 6   TRP B CZ3 1 
ATOM   2812 C CH2 . TRP B 1 9   ? -49.874 32.676  -31.013 1.00 25.20  ? 6   TRP B CH2 1 
ATOM   2813 N N   . VAL B 1 10  ? -42.862 34.078  -32.172 1.00 25.98  ? 7   VAL B N   1 
ATOM   2814 C CA  . VAL B 1 10  ? -41.676 34.827  -31.788 1.00 27.84  ? 7   VAL B CA  1 
ATOM   2815 C C   . VAL B 1 10  ? -41.944 35.477  -30.443 1.00 28.26  ? 7   VAL B C   1 
ATOM   2816 O O   . VAL B 1 10  ? -43.094 35.687  -30.049 1.00 25.38  ? 7   VAL B O   1 
ATOM   2817 C CB  . VAL B 1 10  ? -41.306 35.896  -32.832 1.00 27.05  ? 7   VAL B CB  1 
ATOM   2818 C CG1 . VAL B 1 10  ? -41.002 35.232  -34.146 1.00 27.50  ? 7   VAL B CG1 1 
ATOM   2819 C CG2 . VAL B 1 10  ? -42.454 36.877  -32.995 1.00 26.14  ? 7   VAL B CG2 1 
ATOM   2820 N N   . VAL B 1 11  ? -40.863 35.807  -29.744 1.00 27.32  ? 8   VAL B N   1 
ATOM   2821 C CA  . VAL B 1 11  ? -40.964 36.421  -28.428 1.00 26.49  ? 8   VAL B CA  1 
ATOM   2822 C C   . VAL B 1 11  ? -41.104 37.922  -28.648 1.00 28.86  ? 8   VAL B C   1 
ATOM   2823 O O   . VAL B 1 11  ? -40.155 38.584  -29.068 1.00 30.04  ? 8   VAL B O   1 
ATOM   2824 C CB  . VAL B 1 11  ? -39.744 36.096  -27.553 1.00 29.09  ? 8   VAL B CB  1 
ATOM   2825 C CG1 . VAL B 1 11  ? -39.887 36.702  -26.155 1.00 28.95  ? 8   VAL B CG1 1 
ATOM   2826 C CG2 . VAL B 1 11  ? -39.547 34.615  -27.445 1.00 26.25  ? 8   VAL B CG2 1 
ATOM   2827 N N   . ARG B 1 12  ? -42.287 38.464  -28.362 1.00 31.27  ? 9   ARG B N   1 
ATOM   2828 C CA  . ARG B 1 12  ? -42.502 39.893  -28.529 1.00 33.36  ? 9   ARG B CA  1 
ATOM   2829 C C   . ARG B 1 12  ? -42.207 40.663  -27.264 1.00 35.51  ? 9   ARG B C   1 
ATOM   2830 O O   . ARG B 1 12  ? -41.809 41.833  -27.343 1.00 36.30  ? 9   ARG B O   1 
ATOM   2831 C CB  . ARG B 1 12  ? -43.937 40.189  -28.984 1.00 34.20  ? 9   ARG B CB  1 
ATOM   2832 C CG  . ARG B 1 12  ? -45.004 39.826  -27.994 1.00 38.03  ? 9   ARG B CG  1 
ATOM   2833 C CD  . ARG B 1 12  ? -46.384 40.185  -28.494 1.00 38.75  ? 9   ARG B CD  1 
ATOM   2834 N NE  . ARG B 1 12  ? -46.338 41.450  -29.211 1.00 43.33  ? 9   ARG B NE  1 
ATOM   2835 C CZ  . ARG B 1 12  ? -46.382 42.653  -28.650 1.00 52.49  ? 9   ARG B CZ  1 
ATOM   2836 N NH1 . ARG B 1 12  ? -46.535 42.806  -27.341 1.00 47.67  ? 9   ARG B NH1 1 
ATOM   2837 N NH2 . ARG B 1 12  ? -46.265 43.733  -29.426 1.00 56.73  ? 9   ARG B NH2 1 
ATOM   2838 N N   . GLU B 1 13  ? -42.390 40.039  -26.103 1.00 35.65  ? 10  GLU B N   1 
ATOM   2839 C CA  . GLU B 1 13  ? -42.097 40.716  -24.849 1.00 38.07  ? 10  GLU B CA  1 
ATOM   2840 C C   . GLU B 1 13  ? -41.662 39.705  -23.795 1.00 37.10  ? 10  GLU B C   1 
ATOM   2841 O O   . GLU B 1 13  ? -42.154 38.570  -23.755 1.00 36.84  ? 10  GLU B O   1 
ATOM   2842 C CB  . GLU B 1 13  ? -43.299 41.509  -24.348 1.00 39.55  ? 10  GLU B CB  1 
ATOM   2843 C CG  . GLU B 1 13  ? -42.937 42.544  -23.291 1.00 43.90  ? 10  GLU B CG  1 
ATOM   2844 C CD  . GLU B 1 13  ? -44.139 43.382  -22.915 1.00 50.90  ? 10  GLU B CD  1 
ATOM   2845 O OE1 . GLU B 1 13  ? -45.267 42.887  -23.146 1.00 53.62  ? 10  GLU B OE1 1 
ATOM   2846 O OE2 . GLU B 1 13  ? -43.964 44.525  -22.421 1.00 54.66  ? 10  GLU B OE2 1 
ATOM   2847 N N   . HIS B 1 14  ? -40.726 40.142  -22.951 1.00 31.85  ? 11  HIS B N   1 
ATOM   2848 C CA  . HIS B 1 14  ? -40.254 39.382  -21.792 1.00 36.69  ? 11  HIS B CA  1 
ATOM   2849 C C   . HIS B 1 14  ? -41.096 39.689  -20.554 1.00 38.75  ? 11  HIS B C   1 
ATOM   2850 O O   . HIS B 1 14  ? -41.198 40.847  -20.131 1.00 37.72  ? 11  HIS B O   1 
ATOM   2851 C CB  . HIS B 1 14  ? -38.794 39.709  -21.490 1.00 28.42  ? 11  HIS B CB  1 
ATOM   2852 C CG  . HIS B 1 14  ? -37.832 39.118  -22.463 1.00 30.60  ? 11  HIS B CG  1 
ATOM   2853 N ND1 . HIS B 1 14  ? -36.707 39.789  -22.895 1.00 27.14  ? 11  HIS B ND1 1 
ATOM   2854 C CD2 . HIS B 1 14  ? -37.819 37.915  -23.086 1.00 29.91  ? 11  HIS B CD2 1 
ATOM   2855 C CE1 . HIS B 1 14  ? -36.039 39.019  -23.734 1.00 25.52  ? 11  HIS B CE1 1 
ATOM   2856 N NE2 . HIS B 1 14  ? -36.696 37.881  -23.873 1.00 27.84  ? 11  HIS B NE2 1 
ATOM   2857 N N   . VAL B 1 15  ? -41.646 38.644  -19.941 1.00 41.98  ? 12  VAL B N   1 
ATOM   2858 C CA  . VAL B 1 15  ? -42.456 38.762  -18.731 1.00 44.39  ? 12  VAL B CA  1 
ATOM   2859 C C   . VAL B 1 15  ? -41.935 37.768  -17.691 1.00 42.29  ? 12  VAL B C   1 
ATOM   2860 O O   . VAL B 1 15  ? -42.004 36.548  -17.904 1.00 44.25  ? 12  VAL B O   1 
ATOM   2861 C CB  . VAL B 1 15  ? -43.946 38.519  -19.035 1.00 50.11  ? 12  VAL B CB  1 
ATOM   2862 C CG1 . VAL B 1 15  ? -44.800 38.512  -17.757 1.00 39.19  ? 12  VAL B CG1 1 
ATOM   2863 C CG2 . VAL B 1 15  ? -44.444 39.567  -20.041 1.00 48.82  ? 12  VAL B CG2 1 
ATOM   2864 N N   . GLU B 1 16  ? -41.429 38.288  -16.568 1.00 45.94  ? 13  GLU B N   1 
ATOM   2865 C CA  . GLU B 1 16  ? -40.936 37.468  -15.462 1.00 45.21  ? 13  GLU B CA  1 
ATOM   2866 C C   . GLU B 1 16  ? -42.077 36.726  -14.772 1.00 46.07  ? 13  GLU B C   1 
ATOM   2867 O O   . GLU B 1 16  ? -43.270 37.005  -14.974 1.00 46.67  ? 13  GLU B O   1 
ATOM   2868 C CB  . GLU B 1 16  ? -40.240 38.325  -14.407 1.00 43.60  ? 13  GLU B CB  1 
ATOM   2869 C CG  . GLU B 1 16  ? -39.243 39.308  -14.940 1.00 50.52  ? 13  GLU B CG  1 
ATOM   2870 C CD  . GLU B 1 16  ? -37.838 38.753  -14.945 1.00 59.59  ? 13  GLU B CD  1 
ATOM   2871 O OE1 . GLU B 1 16  ? -37.652 37.575  -15.331 1.00 54.29  ? 13  GLU B OE1 1 
ATOM   2872 O OE2 . GLU B 1 16  ? -36.917 39.498  -14.547 1.00 72.55  ? 13  GLU B OE2 1 
ATOM   2873 N N   . GLY B 1 17  ? -41.695 35.798  -13.900 1.00 41.01  ? 14  GLY B N   1 
ATOM   2874 C CA  . GLY B 1 17  ? -42.688 35.130  -13.087 1.00 41.66  ? 14  GLY B CA  1 
ATOM   2875 C C   . GLY B 1 17  ? -43.501 34.142  -13.903 1.00 40.49  ? 14  GLY B C   1 
ATOM   2876 O O   . GLY B 1 17  ? -43.009 33.531  -14.862 1.00 38.01  ? 14  GLY B O   1 
ATOM   2877 N N   . VAL B 1 18  ? -44.758 33.975  -13.509 1.00 41.84  ? 15  VAL B N   1 
ATOM   2878 C CA  . VAL B 1 18  ? -45.623 33.086  -14.301 1.00 45.34  ? 15  VAL B CA  1 
ATOM   2879 C C   . VAL B 1 18  ? -45.850 33.716  -15.669 1.00 43.28  ? 15  VAL B C   1 
ATOM   2880 O O   . VAL B 1 18  ? -46.111 34.936  -15.756 1.00 43.78  ? 15  VAL B O   1 
ATOM   2881 C CB  . VAL B 1 18  ? -46.947 32.827  -13.586 1.00 39.43  ? 15  VAL B CB  1 
ATOM   2882 C CG1 . VAL B 1 18  ? -47.860 32.024  -14.477 1.00 35.28  ? 15  VAL B CG1 1 
ATOM   2883 C CG2 . VAL B 1 18  ? -46.693 32.071  -12.315 1.00 37.44  ? 15  VAL B CG2 1 
ATOM   2884 N N   . PRO B 1 19  ? -45.721 32.956  -16.749 1.00 41.22  ? 16  PRO B N   1 
ATOM   2885 C CA  . PRO B 1 19  ? -45.834 33.551  -18.081 1.00 42.39  ? 16  PRO B CA  1 
ATOM   2886 C C   . PRO B 1 19  ? -47.252 34.020  -18.372 1.00 39.41  ? 16  PRO B C   1 
ATOM   2887 O O   . PRO B 1 19  ? -48.235 33.360  -18.024 1.00 42.23  ? 16  PRO B O   1 
ATOM   2888 C CB  . PRO B 1 19  ? -45.422 32.403  -19.016 1.00 43.41  ? 16  PRO B CB  1 
ATOM   2889 C CG  . PRO B 1 19  ? -44.650 31.460  -18.167 1.00 42.14  ? 16  PRO B CG  1 
ATOM   2890 C CD  . PRO B 1 19  ? -45.299 31.546  -16.809 1.00 44.67  ? 16  PRO B CD  1 
ATOM   2891 N N   . ASP B 1 20  ? -47.346 35.177  -19.016 1.00 40.35  ? 17  ASP B N   1 
ATOM   2892 C CA  . ASP B 1 20  ? -48.569 35.595  -19.707 1.00 40.99  ? 17  ASP B CA  1 
ATOM   2893 C C   . ASP B 1 20  ? -48.401 35.204  -21.176 1.00 38.71  ? 17  ASP B C   1 
ATOM   2894 O O   . ASP B 1 20  ? -47.853 35.955  -21.980 1.00 39.85  ? 17  ASP B O   1 
ATOM   2895 C CB  . ASP B 1 20  ? -48.800 37.091  -19.526 1.00 39.65  ? 17  ASP B CB  1 
ATOM   2896 C CG  . ASP B 1 20  ? -50.130 37.540  -20.086 1.00 45.94  ? 17  ASP B CG  1 
ATOM   2897 O OD1 . ASP B 1 20  ? -50.837 36.709  -20.713 1.00 39.69  ? 17  ASP B OD1 1 
ATOM   2898 O OD2 . ASP B 1 20  ? -50.459 38.729  -19.892 1.00 46.42  ? 17  ASP B OD2 1 
ATOM   2899 N N   . ALA B 1 21  ? -48.854 34.002  -21.529 1.00 39.19  ? 18  ALA B N   1 
ATOM   2900 C CA  . ALA B 1 21  ? -48.455 33.439  -22.817 1.00 38.33  ? 18  ALA B CA  1 
ATOM   2901 C C   . ALA B 1 21  ? -49.035 34.217  -24.004 1.00 39.42  ? 18  ALA B C   1 
ATOM   2902 O O   . ALA B 1 21  ? -48.437 34.216  -25.088 1.00 40.53  ? 18  ALA B O   1 
ATOM   2903 C CB  . ALA B 1 21  ? -48.846 31.961  -22.894 1.00 36.48  ? 18  ALA B CB  1 
ATOM   2904 N N   . ALA B 1 22  ? -50.179 34.892  -23.831 1.00 39.21  ? 19  ALA B N   1 
ATOM   2905 C CA  . ALA B 1 22  ? -50.729 35.693  -24.920 1.00 36.22  ? 19  ALA B CA  1 
ATOM   2906 C C   . ALA B 1 22  ? -50.082 37.066  -25.031 1.00 36.22  ? 19  ALA B C   1 
ATOM   2907 O O   . ALA B 1 22  ? -50.175 37.686  -26.094 1.00 42.60  ? 19  ALA B O   1 
ATOM   2908 C CB  . ALA B 1 22  ? -52.238 35.851  -24.769 1.00 31.39  ? 19  ALA B CB  1 
ATOM   2909 N N   . ARG B 1 23  ? -49.423 37.546  -23.976 1.00 36.72  ? 20  ARG B N   1 
ATOM   2910 C CA  . ARG B 1 23  ? -48.700 38.812  -24.026 1.00 37.53  ? 20  ARG B CA  1 
ATOM   2911 C C   . ARG B 1 23  ? -47.255 38.662  -24.493 1.00 39.35  ? 20  ARG B C   1 
ATOM   2912 O O   . ARG B 1 23  ? -46.711 39.579  -25.127 1.00 45.28  ? 20  ARG B O   1 
ATOM   2913 C CB  . ARG B 1 23  ? -48.724 39.471  -22.649 1.00 39.71  ? 20  ARG B CB  1 
ATOM   2914 C CG  . ARG B 1 23  ? -47.767 40.628  -22.509 1.00 47.77  ? 20  ARG B CG  1 
ATOM   2915 C CD  . ARG B 1 23  ? -48.405 41.793  -21.814 1.00 46.72  ? 20  ARG B CD  1 
ATOM   2916 N NE  . ARG B 1 23  ? -47.404 42.747  -21.357 1.00 55.38  ? 20  ARG B NE  1 
ATOM   2917 C CZ  . ARG B 1 23  ? -46.914 42.784  -20.125 1.00 64.40  ? 20  ARG B CZ  1 
ATOM   2918 N NH1 . ARG B 1 23  ? -47.283 41.903  -19.203 1.00 55.13  ? 20  ARG B NH1 1 
ATOM   2919 N NH2 . ARG B 1 23  ? -46.041 43.738  -19.803 1.00 63.16  ? 20  ARG B NH2 1 
ATOM   2920 N N   . ILE B 1 24  ? -46.639 37.514  -24.206 1.00 41.46  ? 21  ILE B N   1 
ATOM   2921 C CA  . ILE B 1 24  ? -45.244 37.234  -24.543 1.00 40.21  ? 21  ILE B CA  1 
ATOM   2922 C C   . ILE B 1 24  ? -45.066 36.933  -26.035 1.00 32.90  ? 21  ILE B C   1 
ATOM   2923 O O   . ILE B 1 24  ? -44.070 37.322  -26.646 1.00 31.16  ? 21  ILE B O   1 
ATOM   2924 C CB  . ILE B 1 24  ? -44.760 36.061  -23.669 1.00 36.02  ? 21  ILE B CB  1 
ATOM   2925 C CG1 . ILE B 1 24  ? -44.701 36.476  -22.212 1.00 37.32  ? 21  ILE B CG1 1 
ATOM   2926 C CG2 . ILE B 1 24  ? -43.427 35.518  -24.139 1.00 34.49  ? 21  ILE B CG2 1 
ATOM   2927 C CD1 . ILE B 1 24  ? -44.563 35.291  -21.308 1.00 39.66  ? 21  ILE B CD1 1 
ATOM   2928 N N   . TYR B 1 25  ? -46.003 36.225  -26.641 1.00 33.74  ? 22  TYR B N   1 
ATOM   2929 C CA  . TYR B 1 25  ? -45.784 35.628  -27.946 1.00 31.56  ? 22  TYR B CA  1 
ATOM   2930 C C   . TYR B 1 25  ? -46.673 36.257  -29.013 1.00 32.80  ? 22  TYR B C   1 
ATOM   2931 O O   . TYR B 1 25  ? -47.768 36.763  -28.736 1.00 32.61  ? 22  TYR B O   1 
ATOM   2932 C CB  . TYR B 1 25  ? -46.023 34.116  -27.884 1.00 29.15  ? 22  TYR B CB  1 
ATOM   2933 C CG  . TYR B 1 25  ? -45.084 33.398  -26.945 1.00 34.48  ? 22  TYR B CG  1 
ATOM   2934 C CD1 . TYR B 1 25  ? -43.765 33.161  -27.301 1.00 34.44  ? 22  TYR B CD1 1 
ATOM   2935 C CD2 . TYR B 1 25  ? -45.513 32.955  -25.700 1.00 37.00  ? 22  TYR B CD2 1 
ATOM   2936 C CE1 . TYR B 1 25  ? -42.896 32.503  -26.449 1.00 39.03  ? 22  TYR B CE1 1 
ATOM   2937 C CE2 . TYR B 1 25  ? -44.656 32.296  -24.837 1.00 37.61  ? 22  TYR B CE2 1 
ATOM   2938 C CZ  . TYR B 1 25  ? -43.346 32.074  -25.213 1.00 42.32  ? 22  TYR B CZ  1 
ATOM   2939 O OH  . TYR B 1 25  ? -42.483 31.419  -24.357 1.00 36.22  ? 22  TYR B OH  1 
ATOM   2940 N N   . GLU B 1 26  ? -46.175 36.203  -30.245 1.00 34.96  ? 23  GLU B N   1 
ATOM   2941 C CA  . GLU B 1 26  ? -46.833 36.747  -31.423 1.00 30.94  ? 23  GLU B CA  1 
ATOM   2942 C C   . GLU B 1 26  ? -46.551 35.800  -32.566 1.00 30.67  ? 23  GLU B C   1 
ATOM   2943 O O   . GLU B 1 26  ? -45.403 35.387  -32.742 1.00 31.02  ? 23  GLU B O   1 
ATOM   2944 C CB  . GLU B 1 26  ? -46.311 38.140  -31.771 1.00 28.95  ? 23  GLU B CB  1 
ATOM   2945 C CG  . GLU B 1 26  ? -46.838 38.653  -33.094 1.00 36.33  ? 23  GLU B CG  1 
ATOM   2946 C CD  . GLU B 1 26  ? -46.559 40.133  -33.300 1.00 39.59  ? 23  GLU B CD  1 
ATOM   2947 O OE1 . GLU B 1 26  ? -46.240 40.819  -32.302 1.00 37.70  ? 23  GLU B OE1 1 
ATOM   2948 O OE2 . GLU B 1 26  ? -46.659 40.606  -34.457 1.00 47.34  ? 23  GLU B OE2 1 
ATOM   2949 N N   . LYS B 1 27  ? -47.590 35.455  -33.327 1.00 29.32  ? 24  LYS B N   1 
ATOM   2950 C CA  . LYS B 1 27  ? -47.470 34.534  -34.444 1.00 27.90  ? 24  LYS B CA  1 
ATOM   2951 C C   . LYS B 1 27  ? -47.255 35.327  -35.733 1.00 29.97  ? 24  LYS B C   1 
ATOM   2952 O O   . LYS B 1 27  ? -47.997 36.269  -36.025 1.00 34.36  ? 24  LYS B O   1 
ATOM   2953 C CB  . LYS B 1 27  ? -48.726 33.666  -34.532 1.00 29.78  ? 24  LYS B CB  1 
ATOM   2954 C CG  . LYS B 1 27  ? -48.695 32.553  -35.571 1.00 28.73  ? 24  LYS B CG  1 
ATOM   2955 C CD  . LYS B 1 27  ? -50.012 31.775  -35.592 1.00 31.86  ? 24  LYS B CD  1 
ATOM   2956 C CE  . LYS B 1 27  ? -51.050 32.505  -36.447 1.00 39.79  ? 24  LYS B CE  1 
ATOM   2957 N NZ  . LYS B 1 27  ? -52.205 31.661  -36.844 1.00 45.10  ? 24  LYS B NZ  1 
ATOM   2958 N N   . VAL B 1 28  ? -46.235 34.961  -36.498 1.00 26.87  ? 25  VAL B N   1 
ATOM   2959 C CA  . VAL B 1 28  ? -45.884 35.705  -37.699 1.00 30.76  ? 25  VAL B CA  1 
ATOM   2960 C C   . VAL B 1 28  ? -45.766 34.770  -38.903 1.00 31.99  ? 25  VAL B C   1 
ATOM   2961 O O   . VAL B 1 28  ? -45.399 33.595  -38.780 1.00 27.60  ? 25  VAL B O   1 
ATOM   2962 C CB  . VAL B 1 28  ? -44.565 36.499  -37.508 1.00 27.60  ? 25  VAL B CB  1 
ATOM   2963 C CG1 . VAL B 1 28  ? -44.730 37.580  -36.483 1.00 27.00  ? 25  VAL B CG1 1 
ATOM   2964 C CG2 . VAL B 1 28  ? -43.474 35.579  -37.104 1.00 25.44  ? 25  VAL B CG2 1 
ATOM   2965 N N   . GLU B 1 29  ? -46.063 35.314  -40.089 1.00 33.40  ? 26  GLU B N   1 
ATOM   2966 C CA  . GLU B 1 29  ? -45.720 34.631  -41.327 1.00 33.04  ? 26  GLU B CA  1 
ATOM   2967 C C   . GLU B 1 29  ? -44.273 34.954  -41.700 1.00 28.63  ? 26  GLU B C   1 
ATOM   2968 O O   . GLU B 1 29  ? -43.808 36.085  -41.557 1.00 32.48  ? 26  GLU B O   1 
ATOM   2969 C CB  . GLU B 1 29  ? -46.682 35.006  -42.458 1.00 31.54  ? 26  GLU B CB  1 
ATOM   2970 C CG  . GLU B 1 29  ? -46.471 34.202  -43.750 1.00 37.04  ? 26  GLU B CG  1 
ATOM   2971 C CD  . GLU B 1 29  ? -47.576 34.404  -44.798 1.00 44.58  ? 26  GLU B CD  1 
ATOM   2972 O OE1 . GLU B 1 29  ? -48.774 34.369  -44.423 1.00 39.49  ? 26  GLU B OE1 1 
ATOM   2973 O OE2 . GLU B 1 29  ? -47.241 34.588  -46.002 1.00 49.25  ? 26  GLU B OE2 1 
ATOM   2974 N N   . THR B 1 30  ? -43.541 33.933  -42.110 1.00 28.11  ? 27  THR B N   1 
ATOM   2975 C CA  . THR B 1 30  ? -42.116 34.064  -42.368 1.00 32.41  ? 27  THR B CA  1 
ATOM   2976 C C   . THR B 1 30  ? -41.822 33.307  -43.647 1.00 34.11  ? 27  THR B C   1 
ATOM   2977 O O   . THR B 1 30  ? -42.100 32.106  -43.741 1.00 30.61  ? 27  THR B O   1 
ATOM   2978 C CB  . THR B 1 30  ? -41.266 33.526  -41.199 1.00 34.27  ? 27  THR B CB  1 
ATOM   2979 O OG1 . THR B 1 30  ? -41.355 34.414  -40.074 1.00 30.93  ? 27  THR B OG1 1 
ATOM   2980 C CG2 . THR B 1 30  ? -39.819 33.415  -41.611 1.00 34.30  ? 27  THR B CG2 1 
ATOM   2981 N N   . GLU B 1 31  ? -41.319 34.025  -44.640 1.00 37.16  ? 28  GLU B N   1 
ATOM   2982 C CA  . GLU B 1 31  ? -40.850 33.414  -45.870 1.00 32.98  ? 28  GLU B CA  1 
ATOM   2983 C C   . GLU B 1 31  ? -39.466 32.830  -45.618 1.00 36.69  ? 28  GLU B C   1 
ATOM   2984 O O   . GLU B 1 31  ? -38.528 33.546  -45.249 1.00 33.53  ? 28  GLU B O   1 
ATOM   2985 C CB  . GLU B 1 31  ? -40.806 34.439  -46.995 1.00 40.12  ? 28  GLU B CB  1 
ATOM   2986 C CG  . GLU B 1 31  ? -40.995 33.853  -48.384 1.00 46.43  ? 28  GLU B CG  1 
ATOM   2987 C CD  . GLU B 1 31  ? -40.766 34.869  -49.490 1.00 50.74  ? 28  GLU B CD  1 
ATOM   2988 O OE1 . GLU B 1 31  ? -40.156 35.927  -49.225 1.00 55.44  ? 28  GLU B OE1 1 
ATOM   2989 O OE2 . GLU B 1 31  ? -41.185 34.598  -50.634 1.00 60.25  ? 28  GLU B OE2 1 
ATOM   2990 N N   . LEU B 1 32  ? -39.360 31.528  -45.797 1.00 36.08  ? 29  LEU B N   1 
ATOM   2991 C CA  . LEU B 1 32  ? -38.134 30.781  -45.613 1.00 32.23  ? 29  LEU B CA  1 
ATOM   2992 C C   . LEU B 1 32  ? -37.518 30.566  -46.986 1.00 38.83  ? 29  LEU B C   1 
ATOM   2993 O O   . LEU B 1 32  ? -38.199 30.107  -47.911 1.00 38.24  ? 29  LEU B O   1 
ATOM   2994 C CB  . LEU B 1 32  ? -38.462 29.455  -44.934 1.00 32.23  ? 29  LEU B CB  1 
ATOM   2995 C CG  . LEU B 1 32  ? -37.420 28.486  -44.440 1.00 32.61  ? 29  LEU B CG  1 
ATOM   2996 C CD1 . LEU B 1 32  ? -36.612 29.179  -43.402 1.00 38.52  ? 29  LEU B CD1 1 
ATOM   2997 C CD2 . LEU B 1 32  ? -38.143 27.295  -43.854 1.00 31.28  ? 29  LEU B CD2 1 
ATOM   2998 N N   . ASN B 1 33  ? -36.259 30.959  -47.141 1.00 46.45  ? 30  ASN B N   1 
ATOM   2999 C CA  . ASN B 1 33  ? -35.515 30.543  -48.318 1.00 40.71  ? 30  ASN B CA  1 
ATOM   3000 C C   . ASN B 1 33  ? -35.285 29.048  -48.180 1.00 42.54  ? 30  ASN B C   1 
ATOM   3001 O O   . ASN B 1 33  ? -34.959 28.571  -47.091 1.00 39.87  ? 30  ASN B O   1 
ATOM   3002 C CB  . ASN B 1 33  ? -34.189 31.298  -48.429 1.00 46.63  ? 30  ASN B CB  1 
ATOM   3003 C CG  . ASN B 1 33  ? -33.637 31.337  -49.866 1.00 53.31  ? 30  ASN B CG  1 
ATOM   3004 O OD1 . ASN B 1 33  ? -34.381 31.210  -50.843 1.00 56.28  ? 30  ASN B OD1 1 
ATOM   3005 N ND2 . ASN B 1 33  ? -32.329 31.528  -49.989 1.00 52.79  ? 30  ASN B ND2 1 
ATOM   3006 N N   . THR B 1 34  ? -35.522 28.297  -49.254 1.00 45.25  ? 31  THR B N   1 
ATOM   3007 C CA  . THR B 1 34  ? -35.422 26.847  -49.199 1.00 37.35  ? 31  THR B CA  1 
ATOM   3008 C C   . THR B 1 34  ? -34.245 26.312  -49.999 1.00 40.70  ? 31  THR B C   1 
ATOM   3009 O O   . THR B 1 34  ? -34.104 25.090  -50.120 1.00 41.93  ? 31  THR B O   1 
ATOM   3010 C CB  . THR B 1 34  ? -36.720 26.205  -49.673 1.00 37.20  ? 31  THR B CB  1 
ATOM   3011 O OG1 . THR B 1 34  ? -36.972 26.575  -51.030 1.00 44.76  ? 31  THR B OG1 1 
ATOM   3012 C CG2 . THR B 1 34  ? -37.870 26.676  -48.802 1.00 40.20  ? 31  THR B CG2 1 
ATOM   3013 N N   . ARG B 1 35  ? -33.391 27.200  -50.534 1.00 47.15  ? 32  ARG B N   1 
ATOM   3014 C CA  . ARG B 1 35  ? -32.113 26.817  -51.138 1.00 44.93  ? 32  ARG B CA  1 
ATOM   3015 C C   . ARG B 1 35  ? -31.181 26.296  -50.049 1.00 42.83  ? 32  ARG B C   1 
ATOM   3016 O O   . ARG B 1 35  ? -30.800 27.048  -49.147 1.00 50.30  ? 32  ARG B O   1 
ATOM   3017 C CB  . ARG B 1 35  ? -31.490 28.019  -51.850 1.00 45.85  ? 32  ARG B CB  1 
ATOM   3018 C CG  . ARG B 1 35  ? -30.534 27.655  -52.965 1.00 54.11  ? 32  ARG B CG  1 
ATOM   3019 C CD  . ARG B 1 35  ? -29.962 28.882  -53.674 1.00 67.79  ? 32  ARG B CD  1 
ATOM   3020 N NE  . ARG B 1 35  ? -28.581 29.161  -53.292 1.00 71.44  ? 32  ARG B NE  1 
ATOM   3021 C CZ  . ARG B 1 35  ? -27.510 28.784  -53.982 1.00 75.17  ? 32  ARG B CZ  1 
ATOM   3022 N NH1 . ARG B 1 35  ? -27.616 28.097  -55.112 1.00 76.37  ? 32  ARG B NH1 1 
ATOM   3023 N NH2 . ARG B 1 35  ? -26.301 29.117  -53.533 1.00 72.29  ? 32  ARG B NH2 1 
ATOM   3024 N N   . LEU B 1 36  ? -30.826 25.016  -50.114 1.00 41.43  ? 33  LEU B N   1 
ATOM   3025 C CA  . LEU B 1 36  ? -30.137 24.333  -49.023 1.00 43.88  ? 33  LEU B CA  1 
ATOM   3026 C C   . LEU B 1 36  ? -28.630 24.283  -49.257 1.00 45.69  ? 33  LEU B C   1 
ATOM   3027 O O   . LEU B 1 36  ? -28.177 23.828  -50.310 1.00 50.80  ? 33  LEU B O   1 
ATOM   3028 C CB  . LEU B 1 36  ? -30.670 22.910  -48.855 1.00 35.67  ? 33  LEU B CB  1 
ATOM   3029 C CG  . LEU B 1 36  ? -32.159 22.807  -48.557 1.00 41.08  ? 33  LEU B CG  1 
ATOM   3030 C CD1 . LEU B 1 36  ? -32.529 21.391  -48.120 1.00 42.48  ? 33  LEU B CD1 1 
ATOM   3031 C CD2 . LEU B 1 36  ? -32.525 23.813  -47.496 1.00 41.54  ? 33  LEU B CD2 1 
ATOM   3032 N N   . GLY B 1 37  ? -27.860 24.734  -48.272 1.00 50.31  ? 34  GLY B N   1 
ATOM   3033 C CA  . GLY B 1 37  ? -26.446 24.411  -48.221 1.00 52.10  ? 34  GLY B CA  1 
ATOM   3034 C C   . GLY B 1 37  ? -26.222 22.910  -48.162 1.00 51.30  ? 34  GLY B C   1 
ATOM   3035 O O   . GLY B 1 37  ? -27.135 22.116  -47.954 1.00 50.44  ? 34  GLY B O   1 
ATOM   3036 N N   . GLU B 1 38  ? -24.960 22.514  -48.338 1.00 63.15  ? 35  GLU B N   1 
ATOM   3037 C CA  . GLU B 1 38  ? -24.664 21.106  -48.603 1.00 66.35  ? 35  GLU B CA  1 
ATOM   3038 C C   . GLU B 1 38  ? -25.038 20.182  -47.452 1.00 59.29  ? 35  GLU B C   1 
ATOM   3039 O O   . GLU B 1 38  ? -25.250 18.986  -47.687 1.00 57.73  ? 35  GLU B O   1 
ATOM   3040 C CB  . GLU B 1 38  ? -23.185 20.916  -48.940 1.00 69.59  ? 35  GLU B CB  1 
ATOM   3041 C CG  . GLU B 1 38  ? -22.732 21.675  -50.167 1.00 72.34  ? 35  GLU B CG  1 
ATOM   3042 C CD  . GLU B 1 38  ? -21.238 21.567  -50.404 1.00 87.30  ? 35  GLU B CD  1 
ATOM   3043 O OE1 . GLU B 1 38  ? -20.647 20.522  -50.042 1.00 90.70  ? 35  GLU B OE1 1 
ATOM   3044 O OE2 . GLU B 1 38  ? -20.654 22.533  -50.947 1.00 88.03  ? 35  GLU B OE2 1 
ATOM   3045 N N   . GLU B 1 39  ? -25.118 20.681  -46.220 1.00 54.07  ? 36  GLU B N   1 
ATOM   3046 C CA  . GLU B 1 39  ? -25.535 19.819  -45.121 1.00 59.10  ? 36  GLU B CA  1 
ATOM   3047 C C   . GLU B 1 39  ? -26.828 20.276  -44.471 1.00 55.81  ? 36  GLU B C   1 
ATOM   3048 O O   . GLU B 1 39  ? -27.236 19.698  -43.450 1.00 51.11  ? 36  GLU B O   1 
ATOM   3049 C CB  . GLU B 1 39  ? -24.449 19.706  -44.060 1.00 59.15  ? 36  GLU B CB  1 
ATOM   3050 C CG  . GLU B 1 39  ? -23.296 20.628  -44.250 1.00 68.97  ? 36  GLU B CG  1 
ATOM   3051 C CD  . GLU B 1 39  ? -22.082 20.068  -43.561 1.00 78.26  ? 36  GLU B CD  1 
ATOM   3052 O OE1 . GLU B 1 39  ? -22.156 18.867  -43.200 1.00 73.88  ? 36  GLU B OE1 1 
ATOM   3053 O OE2 . GLU B 1 39  ? -21.079 20.805  -43.376 1.00 80.77  ? 36  GLU B OE2 1 
ATOM   3054 N N   . GLN B 1 40  ? -27.482 21.279  -45.038 1.00 48.48  ? 37  GLN B N   1 
ATOM   3055 C CA  . GLN B 1 40  ? -28.740 21.757  -44.502 1.00 47.74  ? 37  GLN B CA  1 
ATOM   3056 C C   . GLN B 1 40  ? -29.891 20.850  -44.927 1.00 45.17  ? 37  GLN B C   1 
ATOM   3057 O O   . GLN B 1 40  ? -29.834 20.171  -45.957 1.00 42.99  ? 37  GLN B O   1 
ATOM   3058 C CB  . GLN B 1 40  ? -28.997 23.187  -44.961 1.00 48.13  ? 37  GLN B CB  1 
ATOM   3059 C CG  . GLN B 1 40  ? -27.850 24.123  -44.696 1.00 41.61  ? 37  GLN B CG  1 
ATOM   3060 C CD  . GLN B 1 40  ? -28.304 25.553  -44.704 1.00 48.91  ? 37  GLN B CD  1 
ATOM   3061 O OE1 . GLN B 1 40  ? -28.809 26.051  -45.716 1.00 50.73  ? 37  GLN B OE1 1 
ATOM   3062 N NE2 . GLN B 1 40  ? -28.169 26.225  -43.558 1.00 42.56  ? 37  GLN B NE2 1 
ATOM   3063 N N   . MET B 1 41  ? -30.932 20.825  -44.097 1.00 43.18  ? 38  MET B N   1 
ATOM   3064 C CA  . MET B 1 41  ? -32.162 20.118  -44.399 1.00 40.67  ? 38  MET B CA  1 
ATOM   3065 C C   . MET B 1 41  ? -33.339 21.067  -44.225 1.00 44.81  ? 38  MET B C   1 
ATOM   3066 O O   . MET B 1 41  ? -33.312 21.965  -43.378 1.00 49.42  ? 38  MET B O   1 
ATOM   3067 C CB  . MET B 1 41  ? -32.361 18.902  -43.503 1.00 33.96  ? 38  MET B CB  1 
ATOM   3068 C CG  . MET B 1 41  ? -31.233 17.905  -43.522 1.00 38.83  ? 38  MET B CG  1 
ATOM   3069 S SD  . MET B 1 41  ? -31.371 16.794  -42.093 1.00 55.83  ? 38  MET B SD  1 
ATOM   3070 C CE  . MET B 1 41  ? -31.074 17.932  -40.727 1.00 39.20  ? 38  MET B CE  1 
ATOM   3071 N N   . LEU B 1 42  ? -34.370 20.870  -45.046 1.00 39.62  ? 39  LEU B N   1 
ATOM   3072 C CA  . LEU B 1 42  ? -35.669 21.497  -44.841 1.00 40.94  ? 39  LEU B CA  1 
ATOM   3073 C C   . LEU B 1 42  ? -36.565 20.519  -44.091 1.00 39.80  ? 39  LEU B C   1 
ATOM   3074 O O   . LEU B 1 42  ? -36.780 19.396  -44.559 1.00 40.00  ? 39  LEU B O   1 
ATOM   3075 C CB  . LEU B 1 42  ? -36.313 21.899  -46.169 1.00 39.54  ? 39  LEU B CB  1 
ATOM   3076 C CG  . LEU B 1 42  ? -37.767 22.365  -46.045 1.00 41.88  ? 39  LEU B CG  1 
ATOM   3077 C CD1 . LEU B 1 42  ? -37.899 23.580  -45.099 1.00 38.32  ? 39  LEU B CD1 1 
ATOM   3078 C CD2 . LEU B 1 42  ? -38.339 22.684  -47.405 1.00 39.72  ? 39  LEU B CD2 1 
ATOM   3079 N N   . LEU B 1 43  ? -37.096 20.958  -42.949 1.00 31.72  ? 40  LEU B N   1 
ATOM   3080 C CA  . LEU B 1 43  ? -37.892 20.126  -42.060 1.00 37.78  ? 40  LEU B CA  1 
ATOM   3081 C C   . LEU B 1 43  ? -39.271 20.731  -41.822 1.00 39.00  ? 40  LEU B C   1 
ATOM   3082 O O   . LEU B 1 43  ? -39.458 21.953  -41.858 1.00 36.55  ? 40  LEU B O   1 
ATOM   3083 C CB  . LEU B 1 43  ? -37.195 19.927  -40.716 1.00 32.07  ? 40  LEU B CB  1 
ATOM   3084 C CG  . LEU B 1 43  ? -35.840 19.247  -40.870 1.00 31.89  ? 40  LEU B CG  1 
ATOM   3085 C CD1 . LEU B 1 43  ? -34.700 20.247  -40.847 1.00 31.35  ? 40  LEU B CD1 1 
ATOM   3086 C CD2 . LEU B 1 43  ? -35.689 18.214  -39.812 1.00 29.36  ? 40  LEU B CD2 1 
ATOM   3087 N N   . LYS B 1 44  ? -40.232 19.854  -41.555 1.00 35.08  ? 41  LYS B N   1 
ATOM   3088 C CA  . LYS B 1 44  ? -41.612 20.217  -41.275 1.00 35.64  ? 41  LYS B CA  1 
ATOM   3089 C C   . LYS B 1 44  ? -41.980 19.686  -39.884 1.00 38.64  ? 41  LYS B C   1 
ATOM   3090 O O   . LYS B 1 44  ? -41.654 18.542  -39.546 1.00 40.09  ? 41  LYS B O   1 
ATOM   3091 C CB  . LYS B 1 44  ? -42.516 19.648  -42.384 1.00 35.39  ? 41  LYS B CB  1 
ATOM   3092 C CG  . LYS B 1 44  ? -44.019 19.705  -42.141 1.00 40.81  ? 41  LYS B CG  1 
ATOM   3093 C CD  . LYS B 1 44  ? -44.758 18.738  -43.081 1.00 41.24  ? 41  LYS B CD  1 
ATOM   3094 C CE  . LYS B 1 44  ? -46.207 18.516  -42.634 1.00 51.84  ? 41  LYS B CE  1 
ATOM   3095 N NZ  . LYS B 1 44  ? -46.810 17.254  -43.182 1.00 50.62  ? 41  LYS B NZ  1 
ATOM   3096 N N   . THR B 1 45  ? -42.637 20.511  -39.070 1.00 32.36  ? 42  THR B N   1 
ATOM   3097 C CA  . THR B 1 45  ? -42.905 20.173  -37.672 1.00 35.33  ? 42  THR B CA  1 
ATOM   3098 C C   . THR B 1 45  ? -44.191 19.370  -37.520 1.00 34.33  ? 42  THR B C   1 
ATOM   3099 O O   . THR B 1 45  ? -45.262 19.826  -37.922 1.00 38.95  ? 42  THR B O   1 
ATOM   3100 C CB  . THR B 1 45  ? -43.014 21.433  -36.811 1.00 29.85  ? 42  THR B CB  1 
ATOM   3101 O OG1 . THR B 1 45  ? -41.855 22.248  -36.991 1.00 30.40  ? 42  THR B OG1 1 
ATOM   3102 C CG2 . THR B 1 45  ? -43.112 21.044  -35.378 1.00 27.69  ? 42  THR B CG2 1 
ATOM   3103 N N   . LEU B 1 46  ? -44.089 18.206  -36.880 1.00 36.24  ? 43  LEU B N   1 
ATOM   3104 C CA  . LEU B 1 46  ? -45.234 17.343  -36.625 1.00 29.93  ? 43  LEU B CA  1 
ATOM   3105 C C   . LEU B 1 46  ? -45.813 17.509  -35.235 1.00 35.06  ? 43  LEU B C   1 
ATOM   3106 O O   . LEU B 1 46  ? -47.037 17.558  -35.082 1.00 35.90  ? 43  LEU B O   1 
ATOM   3107 C CB  . LEU B 1 46  ? -44.844 15.886  -36.831 1.00 33.43  ? 43  LEU B CB  1 
ATOM   3108 C CG  . LEU B 1 46  ? -44.314 15.662  -38.250 1.00 43.84  ? 43  LEU B CG  1 
ATOM   3109 C CD1 . LEU B 1 46  ? -43.920 14.201  -38.490 1.00 40.65  ? 43  LEU B CD1 1 
ATOM   3110 C CD2 . LEU B 1 46  ? -45.316 16.172  -39.308 1.00 36.58  ? 43  LEU B CD2 1 
ATOM   3111 N N   . TYR B 1 47  ? -44.958 17.590  -34.216 1.00 40.90  ? 44  TYR B N   1 
ATOM   3112 C CA  . TYR B 1 47  ? -45.381 17.813  -32.842 1.00 34.02  ? 44  TYR B CA  1 
ATOM   3113 C C   . TYR B 1 47  ? -44.410 18.767  -32.162 1.00 37.16  ? 44  TYR B C   1 
ATOM   3114 O O   . TYR B 1 47  ? -43.220 18.801  -32.482 1.00 38.28  ? 44  TYR B O   1 
ATOM   3115 C CB  . TYR B 1 47  ? -45.402 16.522  -32.029 1.00 31.81  ? 44  TYR B CB  1 
ATOM   3116 C CG  . TYR B 1 47  ? -46.382 15.455  -32.427 1.00 34.78  ? 44  TYR B CG  1 
ATOM   3117 C CD1 . TYR B 1 47  ? -46.051 14.492  -33.369 1.00 37.50  ? 44  TYR B CD1 1 
ATOM   3118 C CD2 . TYR B 1 47  ? -47.615 15.359  -31.800 1.00 41.65  ? 44  TYR B CD2 1 
ATOM   3119 C CE1 . TYR B 1 47  ? -46.944 13.481  -33.708 1.00 39.93  ? 44  TYR B CE1 1 
ATOM   3120 C CE2 . TYR B 1 47  ? -48.511 14.355  -32.127 1.00 39.96  ? 44  TYR B CE2 1 
ATOM   3121 C CZ  . TYR B 1 47  ? -48.174 13.418  -33.075 1.00 43.12  ? 44  TYR B CZ  1 
ATOM   3122 O OH  . TYR B 1 47  ? -49.075 12.426  -33.391 1.00 50.42  ? 44  TYR B OH  1 
ATOM   3123 N N   . VAL B 1 48  ? -44.909 19.512  -31.186 1.00 31.77  ? 45  VAL B N   1 
ATOM   3124 C CA  . VAL B 1 48  ? -44.024 20.242  -30.298 1.00 34.57  ? 45  VAL B CA  1 
ATOM   3125 C C   . VAL B 1 48  ? -44.412 19.965  -28.859 1.00 33.85  ? 45  VAL B C   1 
ATOM   3126 O O   . VAL B 1 48  ? -45.558 19.635  -28.540 1.00 35.75  ? 45  VAL B O   1 
ATOM   3127 C CB  . VAL B 1 48  ? -44.022 21.759  -30.537 1.00 32.91  ? 45  VAL B CB  1 
ATOM   3128 C CG1 . VAL B 1 48  ? -43.552 22.077  -31.957 1.00 32.43  ? 45  VAL B CG1 1 
ATOM   3129 C CG2 . VAL B 1 48  ? -45.390 22.325  -30.232 1.00 31.43  ? 45  VAL B CG2 1 
ATOM   3130 N N   . SER B 1 49  ? -43.418 20.118  -27.999 1.00 29.48  ? 46  SER B N   1 
ATOM   3131 C CA  . SER B 1 49  ? -43.536 19.977  -26.563 1.00 34.15  ? 46  SER B CA  1 
ATOM   3132 C C   . SER B 1 49  ? -43.711 21.354  -25.952 1.00 33.48  ? 46  SER B C   1 
ATOM   3133 O O   . SER B 1 49  ? -43.122 22.327  -26.429 1.00 36.77  ? 46  SER B O   1 
ATOM   3134 C CB  . SER B 1 49  ? -42.282 19.317  -25.992 1.00 33.37  ? 46  SER B CB  1 
ATOM   3135 O OG  . SER B 1 49  ? -42.495 18.915  -24.661 1.00 35.53  ? 46  SER B OG  1 
ATOM   3136 N N   . VAL B 1 50  ? -44.529 21.440  -24.909 1.00 29.41  ? 47  VAL B N   1 
ATOM   3137 C CA  . VAL B 1 50  ? -44.592 22.627  -24.064 1.00 37.47  ? 47  VAL B CA  1 
ATOM   3138 C C   . VAL B 1 50  ? -44.166 22.245  -22.646 1.00 34.47  ? 47  VAL B C   1 
ATOM   3139 O O   . VAL B 1 50  ? -44.684 21.283  -22.061 1.00 33.28  ? 47  VAL B O   1 
ATOM   3140 C CB  . VAL B 1 50  ? -45.989 23.273  -24.096 1.00 40.17  ? 47  VAL B CB  1 
ATOM   3141 C CG1 . VAL B 1 50  ? -46.218 23.897  -25.445 1.00 33.19  ? 47  VAL B CG1 1 
ATOM   3142 C CG2 . VAL B 1 50  ? -47.057 22.254  -23.833 1.00 35.78  ? 47  VAL B CG2 1 
ATOM   3143 N N   . ASP B 1 51  ? -43.188 22.963  -22.113 1.00 35.97  ? 48  ASP B N   1 
ATOM   3144 C CA  . ASP B 1 51  ? -42.643 22.562  -20.827 1.00 34.33  ? 48  ASP B CA  1 
ATOM   3145 C C   . ASP B 1 51  ? -42.412 23.776  -19.949 1.00 35.53  ? 48  ASP B C   1 
ATOM   3146 O O   . ASP B 1 51  ? -42.178 24.883  -20.451 1.00 34.93  ? 48  ASP B O   1 
ATOM   3147 C CB  . ASP B 1 51  ? -41.325 21.795  -20.978 1.00 31.63  ? 48  ASP B CB  1 
ATOM   3148 C CG  . ASP B 1 51  ? -41.471 20.566  -21.835 1.00 34.45  ? 48  ASP B CG  1 
ATOM   3149 O OD1 . ASP B 1 51  ? -41.647 20.708  -23.060 1.00 37.57  ? 48  ASP B OD1 1 
ATOM   3150 O OD2 . ASP B 1 51  ? -41.433 19.453  -21.298 1.00 38.44  ? 48  ASP B OD2 1 
ATOM   3151 N N   . PRO B 1 52  ? -42.463 23.589  -18.633 1.00 38.02  ? 49  PRO B N   1 
ATOM   3152 C CA  . PRO B 1 52  ? -42.122 24.688  -17.714 1.00 38.22  ? 49  PRO B CA  1 
ATOM   3153 C C   . PRO B 1 52  ? -40.712 25.202  -17.893 1.00 39.08  ? 49  PRO B C   1 
ATOM   3154 O O   . PRO B 1 52  ? -40.475 26.402  -17.705 1.00 38.17  ? 49  PRO B O   1 
ATOM   3155 C CB  . PRO B 1 52  ? -42.307 24.063  -16.329 1.00 35.10  ? 49  PRO B CB  1 
ATOM   3156 C CG  . PRO B 1 52  ? -43.193 22.884  -16.559 1.00 40.06  ? 49  PRO B CG  1 
ATOM   3157 C CD  . PRO B 1 52  ? -42.891 22.371  -17.931 1.00 36.32  ? 49  PRO B CD  1 
ATOM   3158 N N   . TYR B 1 53  ? -39.761 24.340  -18.254 1.00 36.10  ? 50  TYR B N   1 
ATOM   3159 C CA  . TYR B 1 53  ? -38.417 24.852  -18.481 1.00 35.30  ? 50  TYR B CA  1 
ATOM   3160 C C   . TYR B 1 53  ? -38.348 25.817  -19.653 1.00 35.78  ? 50  TYR B C   1 
ATOM   3161 O O   . TYR B 1 53  ? -37.315 26.471  -19.825 1.00 37.07  ? 50  TYR B O   1 
ATOM   3162 C CB  . TYR B 1 53  ? -37.421 23.709  -18.687 1.00 31.67  ? 50  TYR B CB  1 
ATOM   3163 C CG  . TYR B 1 53  ? -37.629 22.841  -19.907 1.00 32.80  ? 50  TYR B CG  1 
ATOM   3164 C CD1 . TYR B 1 53  ? -37.375 23.326  -21.192 1.00 36.45  ? 50  TYR B CD1 1 
ATOM   3165 C CD2 . TYR B 1 53  ? -38.025 21.527  -19.775 1.00 28.43  ? 50  TYR B CD2 1 
ATOM   3166 C CE1 . TYR B 1 53  ? -37.543 22.530  -22.308 1.00 29.16  ? 50  TYR B CE1 1 
ATOM   3167 C CE2 . TYR B 1 53  ? -38.188 20.720  -20.872 1.00 29.26  ? 50  TYR B CE2 1 
ATOM   3168 C CZ  . TYR B 1 53  ? -37.947 21.220  -22.142 1.00 34.70  ? 50  TYR B CZ  1 
ATOM   3169 O OH  . TYR B 1 53  ? -38.119 20.404  -23.248 1.00 32.36  ? 50  TYR B OH  1 
ATOM   3170 N N   . LEU B 1 54  ? -39.407 25.921  -20.459 1.00 33.51  ? 51  LEU B N   1 
ATOM   3171 C CA  . LEU B 1 54  ? -39.432 26.917  -21.522 1.00 34.76  ? 51  LEU B CA  1 
ATOM   3172 C C   . LEU B 1 54  ? -39.528 28.333  -20.978 1.00 33.67  ? 51  LEU B C   1 
ATOM   3173 O O   . LEU B 1 54  ? -39.162 29.276  -21.682 1.00 31.53  ? 51  LEU B O   1 
ATOM   3174 C CB  . LEU B 1 54  ? -40.593 26.647  -22.482 1.00 33.02  ? 51  LEU B CB  1 
ATOM   3175 C CG  . LEU B 1 54  ? -40.417 25.433  -23.398 1.00 31.24  ? 51  LEU B CG  1 
ATOM   3176 C CD1 . LEU B 1 54  ? -41.543 25.324  -24.415 1.00 29.65  ? 51  LEU B CD1 1 
ATOM   3177 C CD2 . LEU B 1 54  ? -39.073 25.471  -24.086 1.00 27.33  ? 51  LEU B CD2 1 
ATOM   3178 N N   . GLN B 1 55  ? -39.982 28.504  -19.734 1.00 33.93  ? 52  GLN B N   1 
ATOM   3179 C CA  . GLN B 1 55  ? -40.066 29.844  -19.159 1.00 34.93  ? 52  GLN B CA  1 
ATOM   3180 C C   . GLN B 1 55  ? -38.696 30.518  -19.120 1.00 36.37  ? 52  GLN B C   1 
ATOM   3181 O O   . GLN B 1 55  ? -38.576 31.728  -19.366 1.00 32.15  ? 52  GLN B O   1 
ATOM   3182 C CB  . GLN B 1 55  ? -40.681 29.763  -17.759 1.00 30.71  ? 52  GLN B CB  1 
ATOM   3183 C CG  . GLN B 1 55  ? -40.995 31.111  -17.123 1.00 34.23  ? 52  GLN B CG  1 
ATOM   3184 C CD  . GLN B 1 55  ? -39.993 31.539  -16.035 1.00 40.56  ? 52  GLN B CD  1 
ATOM   3185 O OE1 . GLN B 1 55  ? -38.998 30.861  -15.762 1.00 38.94  ? 52  GLN B OE1 1 
ATOM   3186 N NE2 . GLN B 1 55  ? -40.273 32.672  -15.407 1.00 41.55  ? 52  GLN B NE2 1 
ATOM   3187 N N   . GLY B 1 56  ? -37.651 29.748  -18.825 1.00 36.95  ? 53  GLY B N   1 
ATOM   3188 C CA  . GLY B 1 56  ? -36.303 30.279  -18.774 1.00 37.61  ? 53  GLY B CA  1 
ATOM   3189 C C   . GLY B 1 56  ? -35.662 30.432  -20.136 1.00 31.41  ? 53  GLY B C   1 
ATOM   3190 O O   . GLY B 1 56  ? -34.966 31.419  -20.371 1.00 32.09  ? 53  GLY B O   1 
ATOM   3191 N N   . ILE B 1 57  ? -35.868 29.453  -21.023 1.00 28.99  ? 54  ILE B N   1 
ATOM   3192 C CA  . ILE B 1 57  ? -35.487 29.613  -22.424 1.00 33.23  ? 54  ILE B CA  1 
ATOM   3193 C C   . ILE B 1 57  ? -36.008 30.938  -22.963 1.00 33.71  ? 54  ILE B C   1 
ATOM   3194 O O   . ILE B 1 57  ? -35.268 31.723  -23.565 1.00 34.85  ? 54  ILE B O   1 
ATOM   3195 C CB  . ILE B 1 57  ? -36.016 28.445  -23.270 1.00 34.11  ? 54  ILE B CB  1 
ATOM   3196 C CG1 . ILE B 1 57  ? -35.364 27.125  -22.857 1.00 30.07  ? 54  ILE B CG1 1 
ATOM   3197 C CG2 . ILE B 1 57  ? -35.833 28.765  -24.769 1.00 32.52  ? 54  ILE B CG2 1 
ATOM   3198 C CD1 . ILE B 1 57  ? -33.907 27.089  -23.112 1.00 35.34  ? 54  ILE B CD1 1 
ATOM   3199 N N   . CYS B 1 58  ? -37.290 31.207  -22.745 1.00 28.55  ? 55  CYS B N   1 
ATOM   3200 C CA  . CYS B 1 58  ? -37.895 32.441  -23.234 1.00 30.75  ? 55  CYS B CA  1 
ATOM   3201 C C   . CYS B 1 58  ? -37.155 33.684  -22.724 1.00 31.93  ? 55  CYS B C   1 
ATOM   3202 O O   . CYS B 1 58  ? -36.780 34.567  -23.501 1.00 34.06  ? 55  CYS B O   1 
ATOM   3203 C CB  . CYS B 1 58  ? -39.366 32.457  -22.815 1.00 32.51  ? 55  CYS B CB  1 
ATOM   3204 S SG  . CYS B 1 58  ? -40.348 33.838  -23.370 1.00 35.38  ? 55  CYS B SG  1 
ATOM   3205 N N   . LEU B 1 59  ? -36.932 33.777  -21.415 1.00 37.03  ? 56  LEU B N   1 
ATOM   3206 C CA  . LEU B 1 59  ? -36.287 34.971  -20.880 1.00 36.84  ? 56  LEU B CA  1 
ATOM   3207 C C   . LEU B 1 59  ? -34.866 35.137  -21.401 1.00 34.97  ? 56  LEU B C   1 
ATOM   3208 O O   . LEU B 1 59  ? -34.301 36.230  -21.286 1.00 34.34  ? 56  LEU B O   1 
ATOM   3209 C CB  . LEU B 1 59  ? -36.290 34.935  -19.350 1.00 29.06  ? 56  LEU B CB  1 
ATOM   3210 C CG  . LEU B 1 59  ? -37.672 35.014  -18.714 1.00 34.98  ? 56  LEU B CG  1 
ATOM   3211 C CD1 . LEU B 1 59  ? -37.619 34.477  -17.297 1.00 33.92  ? 56  LEU B CD1 1 
ATOM   3212 C CD2 . LEU B 1 59  ? -38.190 36.451  -18.743 1.00 35.31  ? 56  LEU B CD2 1 
ATOM   3213 N N   . ASP B 1 60  ? -34.276 34.081  -21.963 1.00 29.64  ? 57  ASP B N   1 
ATOM   3214 C CA  . ASP B 1 60  ? -32.964 34.169  -22.578 1.00 31.68  ? 57  ASP B CA  1 
ATOM   3215 C C   . ASP B 1 60  ? -33.017 34.335  -24.091 1.00 34.74  ? 57  ASP B C   1 
ATOM   3216 O O   . ASP B 1 60  ? -31.966 34.337  -24.730 1.00 40.73  ? 57  ASP B O   1 
ATOM   3217 C CB  . ASP B 1 60  ? -32.144 32.935  -22.226 1.00 35.71  ? 57  ASP B CB  1 
ATOM   3218 C CG  . ASP B 1 60  ? -31.707 32.942  -20.792 1.00 37.20  ? 57  ASP B CG  1 
ATOM   3219 O OD1 . ASP B 1 60  ? -31.720 34.039  -20.210 1.00 34.19  ? 57  ASP B OD1 1 
ATOM   3220 O OD2 . ASP B 1 60  ? -31.366 31.871  -20.251 1.00 43.31  ? 57  ASP B OD2 1 
ATOM   3221 N N   . THR B 1 61  ? -34.211 34.473  -24.677 1.00 33.46  ? 58  THR B N   1 
ATOM   3222 C CA  . THR B 1 61  ? -34.386 34.545  -26.119 1.00 31.23  ? 58  THR B CA  1 
ATOM   3223 C C   . THR B 1 61  ? -34.491 36.000  -26.534 1.00 33.14  ? 58  THR B C   1 
ATOM   3224 O O   . THR B 1 61  ? -35.377 36.697  -26.021 1.00 32.21  ? 58  THR B O   1 
ATOM   3225 C CB  . THR B 1 61  ? -35.649 33.802  -26.523 1.00 31.77  ? 58  THR B CB  1 
ATOM   3226 O OG1 . THR B 1 61  ? -35.519 32.431  -26.165 1.00 33.28  ? 58  THR B OG1 1 
ATOM   3227 C CG2 . THR B 1 61  ? -35.905 33.919  -28.030 1.00 30.89  ? 58  THR B CG2 1 
ATOM   3228 N N   . PRO B 1 62  ? -33.648 36.512  -27.432 1.00 27.98  ? 59  PRO B N   1 
ATOM   3229 C CA  . PRO B 1 62  ? -33.738 37.941  -27.774 1.00 27.51  ? 59  PRO B CA  1 
ATOM   3230 C C   . PRO B 1 62  ? -35.093 38.265  -28.380 1.00 30.80  ? 59  PRO B C   1 
ATOM   3231 O O   . PRO B 1 62  ? -35.657 37.458  -29.126 1.00 30.27  ? 59  PRO B O   1 
ATOM   3232 C CB  . PRO B 1 62  ? -32.595 38.146  -28.778 1.00 27.39  ? 59  PRO B CB  1 
ATOM   3233 C CG  . PRO B 1 62  ? -31.616 37.033  -28.488 1.00 29.22  ? 59  PRO B CG  1 
ATOM   3234 C CD  . PRO B 1 62  ? -32.446 35.866  -27.993 1.00 28.58  ? 59  PRO B CD  1 
ATOM   3235 N N   . ILE B 1 63  ? -35.627 39.446  -28.027 1.00 29.15  ? 60  ILE B N   1 
ATOM   3236 C CA  . ILE B 1 63  ? -36.862 39.963  -28.628 1.00 29.57  ? 60  ILE B CA  1 
ATOM   3237 C C   . ILE B 1 63  ? -36.823 39.749  -30.134 1.00 29.98  ? 60  ILE B C   1 
ATOM   3238 O O   . ILE B 1 63  ? -35.805 40.023  -30.778 1.00 31.78  ? 60  ILE B O   1 
ATOM   3239 C CB  . ILE B 1 63  ? -37.089 41.457  -28.317 1.00 32.66  ? 60  ILE B CB  1 
ATOM   3240 C CG1 . ILE B 1 63  ? -37.225 41.690  -26.815 1.00 28.75  ? 60  ILE B CG1 1 
ATOM   3241 C CG2 . ILE B 1 63  ? -38.323 41.974  -29.043 1.00 28.35  ? 60  ILE B CG2 1 
ATOM   3242 C CD1 . ILE B 1 63  ? -38.063 40.659  -26.129 1.00 25.66  ? 60  ILE B CD1 1 
ATOM   3243 N N   . GLY B 1 64  ? -37.924 39.253  -30.697 1.00 30.42  ? 61  GLY B N   1 
ATOM   3244 C CA  . GLY B 1 64  ? -38.037 38.964  -32.107 1.00 27.42  ? 61  GLY B CA  1 
ATOM   3245 C C   . GLY B 1 64  ? -37.624 37.561  -32.510 1.00 27.89  ? 61  GLY B C   1 
ATOM   3246 O O   . GLY B 1 64  ? -38.090 37.065  -33.534 1.00 28.63  ? 61  GLY B O   1 
ATOM   3247 N N   . ASP B 1 65  ? -36.758 36.907  -31.742 1.00 31.05  ? 62  ASP B N   1 
ATOM   3248 C CA  . ASP B 1 65  ? -36.375 35.543  -32.094 1.00 29.40  ? 62  ASP B CA  1 
ATOM   3249 C C   . ASP B 1 65  ? -37.553 34.582  -31.908 1.00 28.72  ? 62  ASP B C   1 
ATOM   3250 O O   . ASP B 1 65  ? -38.505 34.856  -31.169 1.00 26.85  ? 62  ASP B O   1 
ATOM   3251 C CB  . ASP B 1 65  ? -35.187 35.076  -31.251 1.00 29.19  ? 62  ASP B CB  1 
ATOM   3252 C CG  . ASP B 1 65  ? -33.845 35.437  -31.863 1.00 35.27  ? 62  ASP B CG  1 
ATOM   3253 O OD1 . ASP B 1 65  ? -33.799 36.272  -32.791 1.00 31.17  ? 62  ASP B OD1 1 
ATOM   3254 O OD2 . ASP B 1 65  ? -32.826 34.852  -31.422 1.00 48.64  ? 62  ASP B OD2 1 
ATOM   3255 N N   . HIS B 1 66  ? -37.484 33.444  -32.601 1.00 29.00  ? 63  HIS B N   1 
ATOM   3256 C CA  . HIS B 1 66  ? -38.500 32.411  -32.451 1.00 28.16  ? 63  HIS B CA  1 
ATOM   3257 C C   . HIS B 1 66  ? -38.307 31.655  -31.133 1.00 31.75  ? 63  HIS B C   1 
ATOM   3258 O O   . HIS B 1 66  ? -37.189 31.534  -30.612 1.00 32.72  ? 63  HIS B O   1 
ATOM   3259 C CB  . HIS B 1 66  ? -38.463 31.450  -33.644 1.00 29.38  ? 63  HIS B CB  1 
ATOM   3260 C CG  . HIS B 1 66  ? -37.426 30.372  -33.534 1.00 31.34  ? 63  HIS B CG  1 
ATOM   3261 N ND1 . HIS B 1 66  ? -36.129 30.538  -33.969 1.00 32.51  ? 63  HIS B ND1 1 
ATOM   3262 C CD2 . HIS B 1 66  ? -37.498 29.110  -33.039 1.00 31.11  ? 63  HIS B CD2 1 
ATOM   3263 C CE1 . HIS B 1 66  ? -35.441 29.432  -33.735 1.00 33.22  ? 63  HIS B CE1 1 
ATOM   3264 N NE2 . HIS B 1 66  ? -36.250 28.548  -33.178 1.00 33.83  ? 63  HIS B NE2 1 
ATOM   3265 N N   . MET B 1 67  ? -39.417 31.180  -30.567 1.00 28.18  ? 64  MET B N   1 
ATOM   3266 C CA  . MET B 1 67  ? -39.366 30.433  -29.313 1.00 29.25  ? 64  MET B CA  1 
ATOM   3267 C C   . MET B 1 67  ? -38.861 29.013  -29.571 1.00 29.80  ? 64  MET B C   1 
ATOM   3268 O O   . MET B 1 67  ? -39.422 28.281  -30.403 1.00 28.99  ? 64  MET B O   1 
ATOM   3269 C CB  . MET B 1 67  ? -40.745 30.411  -28.651 1.00 29.89  ? 64  MET B CB  1 
ATOM   3270 C CG  . MET B 1 67  ? -40.814 29.668  -27.319 1.00 29.54  ? 64  MET B CG  1 
ATOM   3271 S SD  . MET B 1 67  ? -39.816 30.428  -25.988 1.00 31.84  ? 64  MET B SD  1 
ATOM   3272 C CE  . MET B 1 67  ? -39.747 29.018  -24.948 1.00 32.84  ? 64  MET B CE  1 
ATOM   3273 N N   . GLY B 1 68  ? -37.789 28.631  -28.882 1.00 22.24  ? 65  GLY B N   1 
ATOM   3274 C CA  . GLY B 1 68  ? -37.309 27.270  -28.975 1.00 23.79  ? 65  GLY B CA  1 
ATOM   3275 C C   . GLY B 1 68  ? -38.133 26.317  -28.128 1.00 27.51  ? 65  GLY B C   1 
ATOM   3276 O O   . GLY B 1 68  ? -38.733 26.703  -27.123 1.00 24.81  ? 65  GLY B O   1 
ATOM   3277 N N   . ALA B 1 69  ? -38.160 25.052  -28.563 1.00 28.45  ? 66  ALA B N   1 
ATOM   3278 C CA  . ALA B 1 69  ? -38.880 23.969  -27.898 1.00 26.65  ? 66  ALA B CA  1 
ATOM   3279 C C   . ALA B 1 69  ? -38.486 22.644  -28.552 1.00 29.95  ? 66  ALA B C   1 
ATOM   3280 O O   . ALA B 1 69  ? -37.887 22.616  -29.631 1.00 25.15  ? 66  ALA B O   1 
ATOM   3281 C CB  . ALA B 1 69  ? -40.386 24.182  -27.970 1.00 26.24  ? 66  ALA B CB  1 
ATOM   3282 N N   . ASP B 1 70  ? -38.816 21.543  -27.865 1.00 28.99  ? 67  ASP B N   1 
ATOM   3283 C CA  . ASP B 1 70  ? -38.574 20.192  -28.361 1.00 28.38  ? 67  ASP B CA  1 
ATOM   3284 C C   . ASP B 1 70  ? -39.632 19.798  -29.397 1.00 29.93  ? 67  ASP B C   1 
ATOM   3285 O O   . ASP B 1 70  ? -40.827 20.042  -29.205 1.00 30.51  ? 67  ASP B O   1 
ATOM   3286 C CB  . ASP B 1 70  ? -38.606 19.201  -27.185 1.00 29.02  ? 67  ASP B CB  1 
ATOM   3287 C CG  . ASP B 1 70  ? -37.904 17.846  -27.500 1.00 41.17  ? 67  ASP B CG  1 
ATOM   3288 O OD1 . ASP B 1 70  ? -37.208 17.714  -28.548 1.00 34.80  ? 67  ASP B OD1 1 
ATOM   3289 O OD2 . ASP B 1 70  ? -38.059 16.894  -26.686 1.00 45.59  ? 67  ASP B OD2 1 
ATOM   3290 N N   . SER B 1 71  ? -39.212 19.135  -30.476 1.00 25.74  ? 68  SER B N   1 
ATOM   3291 C CA  . SER B 1 71  ? -40.178 18.820  -31.527 1.00 32.71  ? 68  SER B CA  1 
ATOM   3292 C C   . SER B 1 71  ? -39.818 17.534  -32.252 1.00 34.01  ? 68  SER B C   1 
ATOM   3293 O O   . SER B 1 71  ? -38.673 17.077  -32.232 1.00 32.82  ? 68  SER B O   1 
ATOM   3294 C CB  . SER B 1 71  ? -40.298 19.958  -32.565 1.00 32.22  ? 68  SER B CB  1 
ATOM   3295 O OG  . SER B 1 71  ? -39.082 20.178  -33.269 1.00 31.02  ? 68  SER B OG  1 
ATOM   3296 N N   . ILE B 1 72  ? -40.832 16.962  -32.906 1.00 37.49  ? 69  ILE B N   1 
ATOM   3297 C CA  . ILE B 1 72  ? -40.669 15.885  -33.878 1.00 36.79  ? 69  ILE B CA  1 
ATOM   3298 C C   . ILE B 1 72  ? -40.873 16.479  -35.272 1.00 39.10  ? 69  ILE B C   1 
ATOM   3299 O O   . ILE B 1 72  ? -41.880 17.155  -35.529 1.00 37.39  ? 69  ILE B O   1 
ATOM   3300 C CB  . ILE B 1 72  ? -41.644 14.721  -33.620 1.00 38.45  ? 69  ILE B CB  1 
ATOM   3301 C CG1 . ILE B 1 72  ? -41.499 14.167  -32.207 1.00 36.36  ? 69  ILE B CG1 1 
ATOM   3302 C CG2 . ILE B 1 72  ? -41.410 13.598  -34.627 1.00 43.05  ? 69  ILE B CG2 1 
ATOM   3303 C CD1 . ILE B 1 72  ? -42.740 13.433  -31.756 1.00 41.81  ? 69  ILE B CD1 1 
ATOM   3304 N N   . MET B 1 73  ? -39.914 16.233  -36.164 1.00 35.26  ? 70  MET B N   1 
ATOM   3305 C CA  . MET B 1 73  ? -39.844 16.869  -37.470 1.00 36.92  ? 70  MET B CA  1 
ATOM   3306 C C   . MET B 1 73  ? -39.679 15.803  -38.543 1.00 42.16  ? 70  MET B C   1 
ATOM   3307 O O   . MET B 1 73  ? -39.378 14.641  -38.256 1.00 42.29  ? 70  MET B O   1 
ATOM   3308 C CB  . MET B 1 73  ? -38.687 17.876  -37.546 1.00 33.79  ? 70  MET B CB  1 
ATOM   3309 C CG  . MET B 1 73  ? -38.845 19.077  -36.629 1.00 30.46  ? 70  MET B CG  1 
ATOM   3310 S SD  . MET B 1 73  ? -37.290 19.978  -36.406 1.00 40.66  ? 70  MET B SD  1 
ATOM   3311 C CE  . MET B 1 73  ? -36.438 18.960  -35.194 1.00 39.16  ? 70  MET B CE  1 
ATOM   3312 N N   . GLN B 1 74  ? -39.893 16.210  -39.793 1.00 38.72  ? 71  GLN B N   1 
ATOM   3313 C CA  . GLN B 1 74  ? -39.786 15.306  -40.927 1.00 39.77  ? 71  GLN B CA  1 
ATOM   3314 C C   . GLN B 1 74  ? -38.996 15.994  -42.019 1.00 41.83  ? 71  GLN B C   1 
ATOM   3315 O O   . GLN B 1 74  ? -39.300 17.134  -42.383 1.00 39.44  ? 71  GLN B O   1 
ATOM   3316 C CB  . GLN B 1 74  ? -41.162 14.897  -41.463 1.00 44.22  ? 71  GLN B CB  1 
ATOM   3317 C CG  . GLN B 1 74  ? -41.099 14.246  -42.840 1.00 40.69  ? 71  GLN B CG  1 
ATOM   3318 C CD  . GLN B 1 74  ? -42.407 13.627  -43.261 1.00 43.42  ? 71  GLN B CD  1 
ATOM   3319 O OE1 . GLN B 1 74  ? -43.327 14.325  -43.681 1.00 51.94  ? 71  GLN B OE1 1 
ATOM   3320 N NE2 . GLN B 1 74  ? -42.499 12.306  -43.154 1.00 46.56  ? 71  GLN B NE2 1 
ATOM   3321 N N   . VAL B 1 75  ? -37.990 15.299  -42.541 1.00 45.82  ? 72  VAL B N   1 
ATOM   3322 C CA  . VAL B 1 75  ? -37.121 15.886  -43.551 1.00 43.95  ? 72  VAL B CA  1 
ATOM   3323 C C   . VAL B 1 75  ? -37.879 15.954  -44.869 1.00 45.46  ? 72  VAL B C   1 
ATOM   3324 O O   . VAL B 1 75  ? -38.235 14.921  -45.446 1.00 47.04  ? 72  VAL B O   1 
ATOM   3325 C CB  . VAL B 1 75  ? -35.828 15.079  -43.693 1.00 40.69  ? 72  VAL B CB  1 
ATOM   3326 C CG1 . VAL B 1 75  ? -34.751 15.921  -44.328 1.00 40.25  ? 72  VAL B CG1 1 
ATOM   3327 C CG2 . VAL B 1 75  ? -35.394 14.587  -42.342 1.00 41.99  ? 72  VAL B CG2 1 
ATOM   3328 N N   . LEU B 1 76  ? -38.136 17.176  -45.342 1.00 43.23  ? 73  LEU B N   1 
ATOM   3329 C CA  . LEU B 1 76  ? -38.690 17.379  -46.676 1.00 39.71  ? 73  LEU B CA  1 
ATOM   3330 C C   . LEU B 1 76  ? -37.613 17.265  -47.739 1.00 47.37  ? 73  LEU B C   1 
ATOM   3331 O O   . LEU B 1 76  ? -37.775 16.549  -48.730 1.00 55.21  ? 73  LEU B O   1 
ATOM   3332 C CB  . LEU B 1 76  ? -39.331 18.759  -46.797 1.00 34.97  ? 73  LEU B CB  1 
ATOM   3333 C CG  . LEU B 1 76  ? -40.424 19.189  -45.843 1.00 39.87  ? 73  LEU B CG  1 
ATOM   3334 C CD1 . LEU B 1 76  ? -41.051 20.459  -46.399 1.00 38.11  ? 73  LEU B CD1 1 
ATOM   3335 C CD2 . LEU B 1 76  ? -41.433 18.068  -45.639 1.00 33.59  ? 73  LEU B CD2 1 
ATOM   3336 N N   . ASP B 1 77  ? -36.525 18.001  -47.560 1.00 47.98  ? 74  ASP B N   1 
ATOM   3337 C CA  . ASP B 1 77  ? -35.502 18.143  -48.574 1.00 42.90  ? 74  ASP B CA  1 
ATOM   3338 C C   . ASP B 1 77  ? -34.172 18.228  -47.854 1.00 47.78  ? 74  ASP B C   1 
ATOM   3339 O O   . ASP B 1 77  ? -34.103 18.707  -46.722 1.00 51.30  ? 74  ASP B O   1 
ATOM   3340 C CB  . ASP B 1 77  ? -35.750 19.388  -49.428 1.00 47.83  ? 74  ASP B CB  1 
ATOM   3341 C CG  . ASP B 1 77  ? -34.917 19.402  -50.697 1.00 62.10  ? 74  ASP B CG  1 
ATOM   3342 O OD1 . ASP B 1 77  ? -34.378 18.332  -51.084 1.00 59.75  ? 74  ASP B OD1 1 
ATOM   3343 O OD2 . ASP B 1 77  ? -34.799 20.491  -51.307 1.00 62.38  ? 74  ASP B OD2 1 
ATOM   3344 N N   . ALA B 1 78  ? -33.117 17.761  -48.511 1.00 51.87  ? 75  ALA B N   1 
ATOM   3345 C CA  . ALA B 1 78  ? -31.844 17.581  -47.833 1.00 49.09  ? 75  ALA B CA  1 
ATOM   3346 C C   . ALA B 1 78  ? -30.710 17.774  -48.815 1.00 53.69  ? 75  ALA B C   1 
ATOM   3347 O O   . ALA B 1 78  ? -30.745 17.235  -49.924 1.00 60.84  ? 75  ALA B O   1 
ATOM   3348 C CB  . ALA B 1 78  ? -31.750 16.189  -47.206 1.00 49.79  ? 75  ALA B CB  1 
ATOM   3349 N N   . GLY B 1 79  ? -29.704 18.533  -48.400 1.00 54.12  ? 76  GLY B N   1 
ATOM   3350 C CA  . GLY B 1 79  ? -28.503 18.665  -49.187 1.00 59.68  ? 76  GLY B CA  1 
ATOM   3351 C C   . GLY B 1 79  ? -27.820 17.320  -49.363 1.00 63.83  ? 76  GLY B C   1 
ATOM   3352 O O   . GLY B 1 79  ? -28.197 16.321  -48.741 1.00 64.37  ? 76  GLY B O   1 
ATOM   3353 N N   . PRO B 1 80  ? -26.802 17.263  -50.225 1.00 65.38  ? 77  PRO B N   1 
ATOM   3354 C CA  . PRO B 1 80  ? -26.124 15.972  -50.438 1.00 64.54  ? 77  PRO B CA  1 
ATOM   3355 C C   . PRO B 1 80  ? -25.404 15.473  -49.198 1.00 65.77  ? 77  PRO B C   1 
ATOM   3356 O O   . PRO B 1 80  ? -25.461 14.271  -48.896 1.00 65.74  ? 77  PRO B O   1 
ATOM   3357 C CB  . PRO B 1 80  ? -25.160 16.273  -51.593 1.00 67.36  ? 77  PRO B CB  1 
ATOM   3358 C CG  . PRO B 1 80  ? -24.958 17.783  -51.546 1.00 67.74  ? 77  PRO B CG  1 
ATOM   3359 C CD  . PRO B 1 80  ? -26.249 18.350  -51.059 1.00 66.78  ? 77  PRO B CD  1 
ATOM   3360 N N   . ASN B 1 81  ? -24.758 16.374  -48.449 1.00 62.45  ? 78  ASN B N   1 
ATOM   3361 C CA  . ASN B 1 81  ? -24.025 16.036  -47.234 1.00 65.72  ? 78  ASN B CA  1 
ATOM   3362 C C   . ASN B 1 81  ? -24.876 16.144  -45.966 1.00 60.99  ? 78  ASN B C   1 
ATOM   3363 O O   . ASN B 1 81  ? -24.322 16.294  -44.868 1.00 60.20  ? 78  ASN B O   1 
ATOM   3364 C CB  . ASN B 1 81  ? -22.789 16.933  -47.100 1.00 71.81  ? 78  ASN B CB  1 
ATOM   3365 C CG  . ASN B 1 81  ? -21.757 16.685  -48.189 1.00 71.63  ? 78  ASN B CG  1 
ATOM   3366 O OD1 . ASN B 1 81  ? -22.021 15.970  -49.155 1.00 66.61  ? 78  ASN B OD1 1 
ATOM   3367 N ND2 . ASN B 1 81  ? -20.576 17.283  -48.036 1.00 66.87  ? 78  ASN B ND2 1 
ATOM   3368 N N   . ALA B 1 82  ? -26.198 16.080  -46.089 1.00 61.31  ? 79  ALA B N   1 
ATOM   3369 C CA  . ALA B 1 82  ? -27.058 16.194  -44.929 1.00 54.53  ? 79  ALA B CA  1 
ATOM   3370 C C   . ALA B 1 82  ? -26.939 14.946  -44.066 1.00 50.88  ? 79  ALA B C   1 
ATOM   3371 O O   . ALA B 1 82  ? -26.551 13.882  -44.547 1.00 51.21  ? 79  ALA B O   1 
ATOM   3372 C CB  . ALA B 1 82  ? -28.507 16.396  -45.354 1.00 53.43  ? 79  ALA B CB  1 
ATOM   3373 N N   . PRO B 1 83  ? -27.248 15.064  -42.774 1.00 48.02  ? 80  PRO B N   1 
ATOM   3374 C CA  . PRO B 1 83  ? -27.195 13.896  -41.888 1.00 49.16  ? 80  PRO B CA  1 
ATOM   3375 C C   . PRO B 1 83  ? -28.396 12.988  -41.999 1.00 52.30  ? 80  PRO B C   1 
ATOM   3376 O O   . PRO B 1 83  ? -28.415 11.935  -41.342 1.00 53.02  ? 80  PRO B O   1 
ATOM   3377 C CB  . PRO B 1 83  ? -27.139 14.525  -40.497 1.00 47.24  ? 80  PRO B CB  1 
ATOM   3378 C CG  . PRO B 1 83  ? -27.854 15.812  -40.676 1.00 44.70  ? 80  PRO B CG  1 
ATOM   3379 C CD  . PRO B 1 83  ? -27.449 16.309  -42.022 1.00 45.49  ? 80  PRO B CD  1 
ATOM   3380 N N   . PHE B 1 84  ? -29.404 13.373  -42.779 1.00 55.05  ? 81  PHE B N   1 
ATOM   3381 C CA  . PHE B 1 84  ? -30.642 12.613  -42.871 1.00 55.39  ? 81  PHE B CA  1 
ATOM   3382 C C   . PHE B 1 84  ? -31.230 12.793  -44.263 1.00 51.23  ? 81  PHE B C   1 
ATOM   3383 O O   . PHE B 1 84  ? -30.926 13.759  -44.970 1.00 51.85  ? 81  PHE B O   1 
ATOM   3384 C CB  . PHE B 1 84  ? -31.648 13.040  -41.794 1.00 56.43  ? 81  PHE B CB  1 
ATOM   3385 C CG  . PHE B 1 84  ? -31.117 12.929  -40.387 1.00 56.31  ? 81  PHE B CG  1 
ATOM   3386 C CD1 . PHE B 1 84  ? -31.020 11.692  -39.764 1.00 55.44  ? 81  PHE B CD1 1 
ATOM   3387 C CD2 . PHE B 1 84  ? -30.719 14.060  -39.688 1.00 52.30  ? 81  PHE B CD2 1 
ATOM   3388 C CE1 . PHE B 1 84  ? -30.529 11.586  -38.485 1.00 47.94  ? 81  PHE B CE1 1 
ATOM   3389 C CE2 . PHE B 1 84  ? -30.233 13.954  -38.408 1.00 50.21  ? 81  PHE B CE2 1 
ATOM   3390 C CZ  . PHE B 1 84  ? -30.136 12.716  -37.809 1.00 46.37  ? 81  PHE B CZ  1 
ATOM   3391 N N   . ARG B 1 85  ? -32.072 11.827  -44.660 1.00 55.13  ? 82  ARG B N   1 
ATOM   3392 C CA  . ARG B 1 85  ? -32.645 11.838  -46.002 1.00 53.85  ? 82  ARG B CA  1 
ATOM   3393 C C   . ARG B 1 85  ? -34.133 12.184  -45.950 1.00 50.60  ? 82  ARG B C   1 
ATOM   3394 O O   . ARG B 1 85  ? -34.806 11.939  -44.939 1.00 44.77  ? 82  ARG B O   1 
ATOM   3395 C CB  . ARG B 1 85  ? -32.474 10.490  -46.721 1.00 50.79  ? 82  ARG B CB  1 
ATOM   3396 C CG  . ARG B 1 85  ? -31.034 10.003  -46.921 1.00 58.26  ? 82  ARG B CG  1 
ATOM   3397 C CD  . ARG B 1 85  ? -29.999 11.132  -47.019 1.00 59.04  ? 82  ARG B CD  1 
ATOM   3398 N NE  . ARG B 1 85  ? -30.240 12.047  -48.130 1.00 64.44  ? 82  ARG B NE  1 
ATOM   3399 C CZ  . ARG B 1 85  ? -29.488 13.106  -48.415 1.00 69.47  ? 82  ARG B CZ  1 
ATOM   3400 N NH1 . ARG B 1 85  ? -28.441 13.438  -47.665 1.00 62.42  ? 82  ARG B NH1 1 
ATOM   3401 N NH2 . ARG B 1 85  ? -29.789 13.849  -49.482 1.00 63.01  ? 82  ARG B NH2 1 
ATOM   3402 N N   . PRO B 1 86  ? -34.664 12.769  -47.026 1.00 46.21  ? 83  PRO B N   1 
ATOM   3403 C CA  . PRO B 1 86  ? -36.088 13.111  -47.060 1.00 43.74  ? 83  PRO B CA  1 
ATOM   3404 C C   . PRO B 1 86  ? -36.969 11.950  -46.627 1.00 45.64  ? 83  PRO B C   1 
ATOM   3405 O O   . PRO B 1 86  ? -36.698 10.787  -46.918 1.00 50.74  ? 83  PRO B O   1 
ATOM   3406 C CB  . PRO B 1 86  ? -36.309 13.488  -48.521 1.00 39.87  ? 83  PRO B CB  1 
ATOM   3407 C CG  . PRO B 1 86  ? -35.023 14.155  -48.882 1.00 42.31  ? 83  PRO B CG  1 
ATOM   3408 C CD  . PRO B 1 86  ? -33.943 13.362  -48.166 1.00 46.19  ? 83  PRO B CD  1 
ATOM   3409 N N   . GLY B 1 87  ? -38.006 12.273  -45.879 1.00 44.34  ? 84  GLY B N   1 
ATOM   3410 C CA  . GLY B 1 87  ? -38.838 11.267  -45.292 1.00 45.85  ? 84  GLY B CA  1 
ATOM   3411 C C   . GLY B 1 87  ? -38.426 10.859  -43.902 1.00 51.86  ? 84  GLY B C   1 
ATOM   3412 O O   . GLY B 1 87  ? -39.273 10.371  -43.144 1.00 53.38  ? 84  GLY B O   1 
ATOM   3413 N N   . ASP B 1 88  ? -37.157 11.066  -43.538 1.00 51.87  ? 85  ASP B N   1 
ATOM   3414 C CA  . ASP B 1 88  ? -36.697 10.716  -42.198 1.00 49.41  ? 85  ASP B CA  1 
ATOM   3415 C C   . ASP B 1 88  ? -37.415 11.556  -41.144 1.00 45.25  ? 85  ASP B C   1 
ATOM   3416 O O   . ASP B 1 88  ? -37.742 12.724  -41.371 1.00 44.38  ? 85  ASP B O   1 
ATOM   3417 C CB  . ASP B 1 88  ? -35.175 10.904  -42.075 1.00 50.79  ? 85  ASP B CB  1 
ATOM   3418 C CG  . ASP B 1 88  ? -34.365 9.862   -42.874 1.00 51.91  ? 85  ASP B CG  1 
ATOM   3419 O OD1 . ASP B 1 88  ? -34.903 8.791   -43.222 1.00 51.18  ? 85  ASP B OD1 1 
ATOM   3420 O OD2 . ASP B 1 88  ? -33.174 10.115  -43.146 1.00 49.20  ? 85  ASP B OD2 1 
ATOM   3421 N N   . LEU B 1 89  ? -37.684 10.937  -39.995 1.00 47.45  ? 86  LEU B N   1 
ATOM   3422 C CA  . LEU B 1 89  ? -38.263 11.601  -38.834 1.00 41.34  ? 86  LEU B CA  1 
ATOM   3423 C C   . LEU B 1 89  ? -37.182 11.823  -37.786 1.00 48.30  ? 86  LEU B C   1 
ATOM   3424 O O   . LEU B 1 89  ? -36.373 10.928  -37.523 1.00 50.41  ? 86  LEU B O   1 
ATOM   3425 C CB  . LEU B 1 89  ? -39.400 10.772  -38.255 1.00 35.66  ? 86  LEU B CB  1 
ATOM   3426 C CG  . LEU B 1 89  ? -40.506 10.501  -39.270 1.00 40.35  ? 86  LEU B CG  1 
ATOM   3427 C CD1 . LEU B 1 89  ? -41.412 9.438   -38.734 1.00 39.12  ? 86  LEU B CD1 1 
ATOM   3428 C CD2 . LEU B 1 89  ? -41.297 11.767  -39.556 1.00 34.60  ? 86  LEU B CD2 1 
ATOM   3429 N N   . VAL B 1 90  ? -37.149 13.026  -37.205 1.00 44.92  ? 87  VAL B N   1 
ATOM   3430 C CA  . VAL B 1 90  ? -36.111 13.377  -36.242 1.00 43.42  ? 87  VAL B CA  1 
ATOM   3431 C C   . VAL B 1 90  ? -36.716 14.136  -35.072 1.00 37.45  ? 87  VAL B C   1 
ATOM   3432 O O   . VAL B 1 90  ? -37.686 14.879  -35.216 1.00 35.44  ? 87  VAL B O   1 
ATOM   3433 C CB  . VAL B 1 90  ? -34.966 14.202  -36.876 1.00 40.44  ? 87  VAL B CB  1 
ATOM   3434 C CG1 . VAL B 1 90  ? -34.264 13.404  -37.979 1.00 48.71  ? 87  VAL B CG1 1 
ATOM   3435 C CG2 . VAL B 1 90  ? -35.480 15.523  -37.407 1.00 41.01  ? 87  VAL B CG2 1 
ATOM   3436 N N   . GLN B 1 91  ? -36.126 13.933  -33.900 1.00 38.05  ? 88  GLN B N   1 
ATOM   3437 C CA  . GLN B 1 91  ? -36.412 14.724  -32.711 1.00 39.35  ? 88  GLN B CA  1 
ATOM   3438 C C   . GLN B 1 91  ? -35.255 15.686  -32.474 1.00 36.61  ? 88  GLN B C   1 
ATOM   3439 O O   . GLN B 1 91  ? -34.088 15.285  -32.519 1.00 39.23  ? 88  GLN B O   1 
ATOM   3440 C CB  . GLN B 1 91  ? -36.626 13.826  -31.488 1.00 38.52  ? 88  GLN B CB  1 
ATOM   3441 C CG  . GLN B 1 91  ? -36.867 14.577  -30.196 1.00 34.61  ? 88  GLN B CG  1 
ATOM   3442 C CD  . GLN B 1 91  ? -35.595 14.786  -29.381 1.00 44.33  ? 88  GLN B CD  1 
ATOM   3443 O OE1 . GLN B 1 91  ? -34.724 13.906  -29.316 1.00 45.74  ? 88  GLN B OE1 1 
ATOM   3444 N NE2 . GLN B 1 91  ? -35.483 15.957  -28.748 1.00 41.55  ? 88  GLN B NE2 1 
ATOM   3445 N N   . GLY B 1 92  ? -35.581 16.950  -32.250 1.00 32.84  ? 89  GLY B N   1 
ATOM   3446 C CA  . GLY B 1 92  ? -34.582 17.979  -32.033 1.00 33.07  ? 89  GLY B CA  1 
ATOM   3447 C C   . GLY B 1 92  ? -35.267 19.211  -31.489 1.00 34.44  ? 89  GLY B C   1 
ATOM   3448 O O   . GLY B 1 92  ? -36.490 19.240  -31.321 1.00 31.86  ? 89  GLY B O   1 
ATOM   3449 N N   . PHE B 1 93  ? -34.460 20.240  -31.209 1.00 35.96  ? 90  PHE B N   1 
ATOM   3450 C CA  . PHE B 1 93  ? -34.980 21.470  -30.607 1.00 32.67  ? 90  PHE B CA  1 
ATOM   3451 C C   . PHE B 1 93  ? -35.411 22.431  -31.724 1.00 33.49  ? 90  PHE B C   1 
ATOM   3452 O O   . PHE B 1 93  ? -34.849 23.513  -31.926 1.00 34.49  ? 90  PHE B O   1 
ATOM   3453 C CB  . PHE B 1 93  ? -33.939 22.084  -29.680 1.00 27.84  ? 90  PHE B CB  1 
ATOM   3454 C CG  . PHE B 1 93  ? -34.514 22.976  -28.589 1.00 27.49  ? 90  PHE B CG  1 
ATOM   3455 C CD1 . PHE B 1 93  ? -35.247 22.442  -27.542 1.00 27.04  ? 90  PHE B CD1 1 
ATOM   3456 C CD2 . PHE B 1 93  ? -34.265 24.333  -28.582 1.00 25.18  ? 90  PHE B CD2 1 
ATOM   3457 C CE1 . PHE B 1 93  ? -35.757 23.241  -26.536 1.00 25.17  ? 90  PHE B CE1 1 
ATOM   3458 C CE2 . PHE B 1 93  ? -34.761 25.137  -27.564 1.00 30.75  ? 90  PHE B CE2 1 
ATOM   3459 C CZ  . PHE B 1 93  ? -35.516 24.588  -26.543 1.00 26.87  ? 90  PHE B CZ  1 
ATOM   3460 N N   . GLY B 1 94  ? -36.464 22.015  -32.446 1.00 29.47  ? 91  GLY B N   1 
ATOM   3461 C CA  . GLY B 1 94  ? -36.909 22.753  -33.618 1.00 30.21  ? 91  GLY B CA  1 
ATOM   3462 C C   . GLY B 1 94  ? -37.662 24.038  -33.335 1.00 28.04  ? 91  GLY B C   1 
ATOM   3463 O O   . GLY B 1 94  ? -37.591 24.978  -34.128 1.00 34.04  ? 91  GLY B O   1 
ATOM   3464 N N   . GLY B 1 95  ? -38.400 24.104  -32.237 1.00 23.57  ? 92  GLY B N   1 
ATOM   3465 C CA  . GLY B 1 95  ? -39.065 25.333  -31.847 1.00 27.13  ? 92  GLY B CA  1 
ATOM   3466 C C   . GLY B 1 95  ? -40.500 25.442  -32.345 1.00 30.07  ? 92  GLY B C   1 
ATOM   3467 O O   . GLY B 1 95  ? -41.036 24.572  -33.046 1.00 25.25  ? 92  GLY B O   1 
ATOM   3468 N N   . TRP B 1 96  ? -41.142 26.550  -31.952 1.00 27.43  ? 93  TRP B N   1 
ATOM   3469 C CA  . TRP B 1 96  ? -42.515 26.853  -32.361 1.00 23.43  ? 93  TRP B CA  1 
ATOM   3470 C C   . TRP B 1 96  ? -42.498 27.490  -33.759 1.00 28.27  ? 93  TRP B C   1 
ATOM   3471 O O   . TRP B 1 96  ? -42.700 28.693  -33.952 1.00 29.05  ? 93  TRP B O   1 
ATOM   3472 C CB  . TRP B 1 96  ? -43.184 27.750  -31.327 1.00 23.50  ? 93  TRP B CB  1 
ATOM   3473 C CG  . TRP B 1 96  ? -43.361 27.127  -29.990 1.00 24.84  ? 93  TRP B CG  1 
ATOM   3474 C CD1 . TRP B 1 96  ? -43.142 25.813  -29.655 1.00 27.40  ? 93  TRP B CD1 1 
ATOM   3475 C CD2 . TRP B 1 96  ? -43.786 27.780  -28.786 1.00 26.62  ? 93  TRP B CD2 1 
ATOM   3476 N NE1 . TRP B 1 96  ? -43.389 25.617  -28.311 1.00 25.44  ? 93  TRP B NE1 1 
ATOM   3477 C CE2 . TRP B 1 96  ? -43.791 26.805  -27.757 1.00 29.32  ? 93  TRP B CE2 1 
ATOM   3478 C CE3 . TRP B 1 96  ? -44.153 29.089  -28.475 1.00 27.34  ? 93  TRP B CE3 1 
ATOM   3479 C CZ2 . TRP B 1 96  ? -44.156 27.106  -26.434 1.00 32.73  ? 93  TRP B CZ2 1 
ATOM   3480 C CZ3 . TRP B 1 96  ? -44.510 29.390  -27.163 1.00 32.98  ? 93  TRP B CZ3 1 
ATOM   3481 C CH2 . TRP B 1 96  ? -44.523 28.392  -26.159 1.00 33.25  ? 93  TRP B CH2 1 
ATOM   3482 N N   . ARG B 1 97  ? -42.194 26.648  -34.757 1.00 30.20  ? 94  ARG B N   1 
ATOM   3483 C CA  . ARG B 1 97  ? -42.150 27.015  -36.166 1.00 21.76  ? 94  ARG B CA  1 
ATOM   3484 C C   . ARG B 1 97  ? -42.754 25.873  -36.960 1.00 27.69  ? 94  ARG B C   1 
ATOM   3485 O O   . ARG B 1 97  ? -42.493 24.711  -36.653 1.00 29.86  ? 94  ARG B O   1 
ATOM   3486 C CB  . ARG B 1 97  ? -40.722 27.260  -36.648 1.00 26.43  ? 94  ARG B CB  1 
ATOM   3487 C CG  . ARG B 1 97  ? -39.958 28.344  -35.882 1.00 32.61  ? 94  ARG B CG  1 
ATOM   3488 C CD  . ARG B 1 97  ? -38.539 28.511  -36.410 1.00 33.27  ? 94  ARG B CD  1 
ATOM   3489 N NE  . ARG B 1 97  ? -37.664 27.421  -36.000 1.00 31.83  ? 94  ARG B NE  1 
ATOM   3490 C CZ  . ARG B 1 97  ? -36.383 27.331  -36.329 1.00 35.68  ? 94  ARG B CZ  1 
ATOM   3491 N NH1 . ARG B 1 97  ? -35.792 28.256  -37.069 1.00 38.28  ? 94  ARG B NH1 1 
ATOM   3492 N NH2 . ARG B 1 97  ? -35.678 26.287  -35.907 1.00 32.67  ? 94  ARG B NH2 1 
ATOM   3493 N N   . THR B 1 98  ? -43.542 26.186  -37.992 1.00 29.36  ? 95  THR B N   1 
ATOM   3494 C CA  . THR B 1 98  ? -44.117 25.108  -38.800 1.00 29.03  ? 95  THR B CA  1 
ATOM   3495 C C   . THR B 1 98  ? -43.070 24.462  -39.710 1.00 30.52  ? 95  THR B C   1 
ATOM   3496 O O   . THR B 1 98  ? -43.189 23.279  -40.046 1.00 29.84  ? 95  THR B O   1 
ATOM   3497 C CB  . THR B 1 98  ? -45.299 25.624  -39.627 1.00 30.42  ? 95  THR B CB  1 
ATOM   3498 O OG1 . THR B 1 98  ? -44.832 26.608  -40.561 1.00 32.03  ? 95  THR B OG1 1 
ATOM   3499 C CG2 . THR B 1 98  ? -46.378 26.249  -38.723 1.00 26.40  ? 95  THR B CG2 1 
ATOM   3500 N N   . HIS B 1 99  ? -42.044 25.215  -40.119 1.00 33.75  ? 96  HIS B N   1 
ATOM   3501 C CA  . HIS B 1 99  ? -40.945 24.681  -40.921 1.00 32.85  ? 96  HIS B CA  1 
ATOM   3502 C C   . HIS B 1 99  ? -39.671 25.435  -40.563 1.00 32.81  ? 96  HIS B C   1 
ATOM   3503 O O   . HIS B 1 99  ? -39.725 26.531  -39.998 1.00 34.63  ? 96  HIS B O   1 
ATOM   3504 C CB  . HIS B 1 99  ? -41.202 24.820  -42.423 1.00 31.75  ? 96  HIS B CB  1 
ATOM   3505 C CG  . HIS B 1 99  ? -42.559 24.372  -42.860 1.00 34.90  ? 96  HIS B CG  1 
ATOM   3506 N ND1 . HIS B 1 99  ? -43.699 25.105  -42.615 1.00 34.86  ? 96  HIS B ND1 1 
ATOM   3507 C CD2 . HIS B 1 99  ? -42.955 23.279  -43.558 1.00 31.90  ? 96  HIS B CD2 1 
ATOM   3508 C CE1 . HIS B 1 99  ? -44.741 24.476  -43.131 1.00 34.20  ? 96  HIS B CE1 1 
ATOM   3509 N NE2 . HIS B 1 99  ? -44.317 23.364  -43.705 1.00 30.97  ? 96  HIS B NE2 1 
ATOM   3510 N N   . LEU B 1 100 ? -38.522 24.854  -40.925 1.00 34.32  ? 97  LEU B N   1 
ATOM   3511 C CA  . LEU B 1 100 ? -37.224 25.451  -40.614 1.00 34.26  ? 97  LEU B CA  1 
ATOM   3512 C C   . LEU B 1 100 ? -36.143 24.821  -41.483 1.00 33.28  ? 97  LEU B C   1 
ATOM   3513 O O   . LEU B 1 100 ? -36.286 23.698  -41.963 1.00 34.10  ? 97  LEU B O   1 
ATOM   3514 C CB  . LEU B 1 100 ? -36.865 25.267  -39.133 1.00 30.59  ? 97  LEU B CB  1 
ATOM   3515 C CG  . LEU B 1 100 ? -36.704 23.812  -38.718 1.00 31.43  ? 97  LEU B CG  1 
ATOM   3516 C CD1 . LEU B 1 100 ? -35.550 23.673  -37.769 1.00 34.34  ? 97  LEU B CD1 1 
ATOM   3517 C CD2 . LEU B 1 100 ? -37.958 23.324  -38.065 1.00 30.34  ? 97  LEU B CD2 1 
ATOM   3518 N N   . VAL B 1 101 ? -35.046 25.555  -41.665 1.00 34.74  ? 98  VAL B N   1 
ATOM   3519 C CA  . VAL B 1 101 ? -33.819 25.015  -42.248 1.00 37.74  ? 98  VAL B CA  1 
ATOM   3520 C C   . VAL B 1 101 ? -32.775 24.873  -41.139 1.00 42.87  ? 98  VAL B C   1 
ATOM   3521 O O   . VAL B 1 101 ? -32.407 25.855  -40.480 1.00 39.02  ? 98  VAL B O   1 
ATOM   3522 C CB  . VAL B 1 101 ? -33.292 25.896  -43.392 1.00 37.81  ? 98  VAL B CB  1 
ATOM   3523 C CG1 . VAL B 1 101 ? -31.927 25.416  -43.849 1.00 36.27  ? 98  VAL B CG1 1 
ATOM   3524 C CG2 . VAL B 1 101 ? -34.257 25.869  -44.548 1.00 39.39  ? 98  VAL B CG2 1 
ATOM   3525 N N   . SER B 1 102 ? -32.283 23.652  -40.946 1.00 37.65  ? 99  SER B N   1 
ATOM   3526 C CA  . SER B 1 102 ? -31.204 23.402  -40.005 1.00 38.56  ? 99  SER B CA  1 
ATOM   3527 C C   . SER B 1 102 ? -30.309 22.303  -40.563 1.00 42.87  ? 99  SER B C   1 
ATOM   3528 O O   . SER B 1 102 ? -30.712 21.521  -41.434 1.00 41.52  ? 99  SER B O   1 
ATOM   3529 C CB  . SER B 1 102 ? -31.755 23.025  -38.620 1.00 36.43  ? 99  SER B CB  1 
ATOM   3530 O OG  . SER B 1 102 ? -30.913 22.111  -37.933 1.00 32.55  ? 99  SER B OG  1 
ATOM   3531 N N   . ASP B 1 103 ? -29.077 22.254  -40.060 1.00 40.01  ? 100 ASP B N   1 
ATOM   3532 C CA  . ASP B 1 103 ? -28.164 21.174  -40.408 1.00 39.82  ? 100 ASP B CA  1 
ATOM   3533 C C   . ASP B 1 103 ? -28.119 20.066  -39.363 1.00 36.78  ? 100 ASP B C   1 
ATOM   3534 O O   . ASP B 1 103 ? -27.262 19.188  -39.455 1.00 35.77  ? 100 ASP B O   1 
ATOM   3535 C CB  . ASP B 1 103 ? -26.756 21.715  -40.651 1.00 43.70  ? 100 ASP B CB  1 
ATOM   3536 C CG  . ASP B 1 103 ? -26.208 22.499  -39.473 1.00 49.42  ? 100 ASP B CG  1 
ATOM   3537 O OD1 . ASP B 1 103 ? -26.895 22.603  -38.424 1.00 47.87  ? 100 ASP B OD1 1 
ATOM   3538 O OD2 . ASP B 1 103 ? -25.076 23.016  -39.610 1.00 49.71  ? 100 ASP B OD2 1 
ATOM   3539 N N   . GLY B 1 104 ? -29.018 20.077  -38.382 1.00 31.40  ? 101 GLY B N   1 
ATOM   3540 C CA  . GLY B 1 104 ? -29.046 19.030  -37.382 1.00 38.87  ? 101 GLY B CA  1 
ATOM   3541 C C   . GLY B 1 104 ? -27.864 18.967  -36.420 1.00 43.62  ? 101 GLY B C   1 
ATOM   3542 O O   . GLY B 1 104 ? -27.886 18.140  -35.499 1.00 38.40  ? 101 GLY B O   1 
ATOM   3543 N N   . LYS B 1 105 ? -26.844 19.812  -36.576 1.00 39.80  ? 102 LYS B N   1 
ATOM   3544 C CA  . LYS B 1 105 ? -25.660 19.685  -35.744 1.00 41.88  ? 102 LYS B CA  1 
ATOM   3545 C C   . LYS B 1 105 ? -25.888 20.314  -34.362 1.00 45.21  ? 102 LYS B C   1 
ATOM   3546 O O   . LYS B 1 105 ? -26.786 21.147  -34.191 1.00 42.44  ? 102 LYS B O   1 
ATOM   3547 C CB  . LYS B 1 105 ? -24.471 20.317  -36.462 1.00 41.90  ? 102 LYS B CB  1 
ATOM   3548 C CG  . LYS B 1 105 ? -24.024 19.545  -37.694 1.00 42.72  ? 102 LYS B CG  1 
ATOM   3549 C CD  . LYS B 1 105 ? -22.559 19.804  -38.020 1.00 49.48  ? 102 LYS B CD  1 
ATOM   3550 C CE  . LYS B 1 105 ? -22.409 20.870  -39.081 1.00 51.98  ? 102 LYS B CE  1 
ATOM   3551 N NZ  . LYS B 1 105 ? -21.703 20.323  -40.266 1.00 57.21  ? 102 LYS B NZ  1 
ATOM   3552 N N   . PRO B 1 106 ? -25.106 19.912  -33.349 1.00 42.44  ? 103 PRO B N   1 
ATOM   3553 C CA  . PRO B 1 106 ? -25.284 20.491  -32.011 1.00 36.83  ? 103 PRO B CA  1 
ATOM   3554 C C   . PRO B 1 106 ? -25.055 21.987  -32.053 1.00 36.87  ? 103 PRO B C   1 
ATOM   3555 O O   . PRO B 1 106 ? -24.179 22.475  -32.769 1.00 45.38  ? 103 PRO B O   1 
ATOM   3556 C CB  . PRO B 1 106 ? -24.218 19.789  -31.171 1.00 33.32  ? 103 PRO B CB  1 
ATOM   3557 C CG  . PRO B 1 106 ? -23.902 18.540  -31.941 1.00 41.16  ? 103 PRO B CG  1 
ATOM   3558 C CD  . PRO B 1 106 ? -23.990 18.954  -33.368 1.00 40.00  ? 103 PRO B CD  1 
ATOM   3559 N N   . LYS B 1 107 ? -25.870 22.717  -31.309 1.00 34.48  ? 104 LYS B N   1 
ATOM   3560 C CA  . LYS B 1 107 ? -25.840 24.166  -31.361 1.00 37.10  ? 104 LYS B CA  1 
ATOM   3561 C C   . LYS B 1 107 ? -25.687 24.728  -29.966 1.00 34.50  ? 104 LYS B C   1 
ATOM   3562 O O   . LYS B 1 107 ? -26.351 24.285  -29.022 1.00 36.01  ? 104 LYS B O   1 
ATOM   3563 C CB  . LYS B 1 107 ? -27.106 24.747  -32.006 1.00 40.74  ? 104 LYS B CB  1 
ATOM   3564 C CG  . LYS B 1 107 ? -26.907 25.152  -33.461 1.00 52.44  ? 104 LYS B CG  1 
ATOM   3565 C CD  . LYS B 1 107 ? -27.483 26.550  -33.750 1.00 57.31  ? 104 LYS B CD  1 
ATOM   3566 C CE  . LYS B 1 107 ? -28.938 26.477  -34.235 1.00 54.10  ? 104 LYS B CE  1 
ATOM   3567 N NZ  . LYS B 1 107 ? -29.443 27.788  -34.729 1.00 39.89  ? 104 LYS B NZ  1 
ATOM   3568 N N   . LEU B 1 108 ? -24.803 25.703  -29.849 1.00 37.10  ? 105 LEU B N   1 
ATOM   3569 C CA  . LEU B 1 108 ? -24.582 26.351  -28.572 1.00 39.05  ? 105 LEU B CA  1 
ATOM   3570 C C   . LEU B 1 108 ? -25.765 27.263  -28.287 1.00 40.29  ? 105 LEU B C   1 
ATOM   3571 O O   . LEU B 1 108 ? -26.247 27.959  -29.179 1.00 40.36  ? 105 LEU B O   1 
ATOM   3572 C CB  . LEU B 1 108 ? -23.272 27.130  -28.608 1.00 38.70  ? 105 LEU B CB  1 
ATOM   3573 C CG  . LEU B 1 108 ? -22.847 27.817  -27.316 1.00 48.21  ? 105 LEU B CG  1 
ATOM   3574 C CD1 . LEU B 1 108 ? -22.461 26.791  -26.272 1.00 45.07  ? 105 LEU B CD1 1 
ATOM   3575 C CD2 . LEU B 1 108 ? -21.712 28.763  -27.594 1.00 45.30  ? 105 LEU B CD2 1 
ATOM   3576 N N   . TRP B 1 109 ? -26.280 27.213  -27.063 1.00 38.75  ? 106 TRP B N   1 
ATOM   3577 C CA  . TRP B 1 109 ? -27.312 28.160  -26.657 1.00 38.90  ? 106 TRP B CA  1 
ATOM   3578 C C   . TRP B 1 109 ? -26.561 29.394  -26.178 1.00 46.09  ? 106 TRP B C   1 
ATOM   3579 O O   . TRP B 1 109 ? -26.184 29.528  -25.003 1.00 33.12  ? 106 TRP B O   1 
ATOM   3580 C CB  . TRP B 1 109 ? -28.252 27.573  -25.615 1.00 39.15  ? 106 TRP B CB  1 
ATOM   3581 C CG  . TRP B 1 109 ? -29.369 28.494  -25.236 1.00 36.23  ? 106 TRP B CG  1 
ATOM   3582 C CD1 . TRP B 1 109 ? -29.782 28.771  -23.976 1.00 38.01  ? 106 TRP B CD1 1 
ATOM   3583 C CD2 . TRP B 1 109 ? -30.202 29.274  -26.109 1.00 36.57  ? 106 TRP B CD2 1 
ATOM   3584 N NE1 . TRP B 1 109 ? -30.822 29.656  -23.999 1.00 39.08  ? 106 TRP B NE1 1 
ATOM   3585 C CE2 . TRP B 1 109 ? -31.102 29.985  -25.296 1.00 38.60  ? 106 TRP B CE2 1 
ATOM   3586 C CE3 . TRP B 1 109 ? -30.285 29.431  -27.491 1.00 37.46  ? 106 TRP B CE3 1 
ATOM   3587 C CZ2 . TRP B 1 109 ? -32.064 30.850  -25.822 1.00 34.97  ? 106 TRP B CZ2 1 
ATOM   3588 C CZ3 . TRP B 1 109 ? -31.234 30.291  -28.010 1.00 27.51  ? 106 TRP B CZ3 1 
ATOM   3589 C CH2 . TRP B 1 109 ? -32.109 30.991  -27.177 1.00 33.60  ? 106 TRP B CH2 1 
ATOM   3590 N N   . GLN B 1 110 ? -26.352 30.291  -27.152 1.00 51.21  ? 107 GLN B N   1 
ATOM   3591 C CA  . GLN B 1 110 ? -25.508 31.472  -27.017 1.00 51.27  ? 107 GLN B CA  1 
ATOM   3592 C C   . GLN B 1 110 ? -25.901 32.316  -25.819 1.00 52.76  ? 107 GLN B C   1 
ATOM   3593 O O   . GLN B 1 110 ? -25.047 32.787  -25.059 1.00 54.31  ? 107 GLN B O   1 
ATOM   3594 C CB  . GLN B 1 110 ? -25.628 32.305  -28.294 1.00 56.54  ? 107 GLN B CB  1 
ATOM   3595 C CG  . GLN B 1 110 ? -25.174 31.610  -29.547 1.00 60.59  ? 107 GLN B CG  1 
ATOM   3596 C CD  . GLN B 1 110 ? -23.661 31.569  -29.629 1.00 77.18  ? 107 GLN B CD  1 
ATOM   3597 O OE1 . GLN B 1 110 ? -22.974 32.380  -28.992 1.00 79.27  ? 107 GLN B OE1 1 
ATOM   3598 N NE2 . GLN B 1 110 ? -23.128 30.615  -30.401 1.00 74.45  ? 107 GLN B NE2 1 
ATOM   3599 N N   . THR B 1 111 ? -27.200 32.538  -25.654 1.00 49.80  ? 108 THR B N   1 
ATOM   3600 C CA  . THR B 1 111 ? -27.722 33.501  -24.700 1.00 51.29  ? 108 THR B CA  1 
ATOM   3601 C C   . THR B 1 111 ? -28.162 32.846  -23.389 1.00 47.57  ? 108 THR B C   1 
ATOM   3602 O O   . THR B 1 111 ? -28.860 33.488  -22.594 1.00 58.38  ? 108 THR B O   1 
ATOM   3603 C CB  . THR B 1 111 ? -28.876 34.300  -25.341 1.00 52.07  ? 108 THR B CB  1 
ATOM   3604 O OG1 . THR B 1 111 ? -29.895 33.413  -25.837 1.00 47.47  ? 108 THR B OG1 1 
ATOM   3605 C CG2 . THR B 1 111 ? -28.366 35.193  -26.522 1.00 40.46  ? 108 THR B CG2 1 
ATOM   3606 N N   . GLY B 1 112 ? -27.738 31.602  -23.123 1.00 39.27  ? 109 GLY B N   1 
ATOM   3607 C CA  . GLY B 1 112 ? -28.171 30.926  -21.909 1.00 44.54  ? 109 GLY B CA  1 
ATOM   3608 C C   . GLY B 1 112 ? -27.623 31.551  -20.633 1.00 47.41  ? 109 GLY B C   1 
ATOM   3609 O O   . GLY B 1 112 ? -26.672 32.333  -20.624 1.00 48.07  ? 109 GLY B O   1 
ATOM   3610 N N   . THR B 1 113 ? -28.250 31.205  -19.509 1.00 49.56  ? 110 THR B N   1 
ATOM   3611 C CA  . THR B 1 113 ? -27.581 31.436  -18.233 1.00 55.63  ? 110 THR B CA  1 
ATOM   3612 C C   . THR B 1 113 ? -26.262 30.674  -18.173 1.00 52.09  ? 110 THR B C   1 
ATOM   3613 O O   . THR B 1 113 ? -25.273 31.168  -17.614 1.00 54.04  ? 110 THR B O   1 
ATOM   3614 C CB  . THR B 1 113 ? -28.490 31.017  -17.073 1.00 58.47  ? 110 THR B CB  1 
ATOM   3615 O OG1 . THR B 1 113 ? -29.753 31.682  -17.192 1.00 53.07  ? 110 THR B OG1 1 
ATOM   3616 C CG2 . THR B 1 113 ? -27.834 31.332  -15.698 1.00 43.74  ? 110 THR B CG2 1 
ATOM   3617 N N   . PHE B 1 114 ? -26.235 29.480  -18.765 1.00 50.90  ? 111 PHE B N   1 
ATOM   3618 C CA  . PHE B 1 114 ? -25.178 28.492  -18.827 1.00 49.62  ? 111 PHE B CA  1 
ATOM   3619 C C   . PHE B 1 114 ? -24.774 28.267  -20.269 1.00 47.29  ? 111 PHE B C   1 
ATOM   3620 O O   . PHE B 1 114 ? -25.612 28.354  -21.166 1.00 49.28  ? 111 PHE B O   1 
ATOM   3621 C CB  . PHE B 1 114 ? -25.640 27.155  -18.237 1.00 43.38  ? 111 PHE B CB  1 
ATOM   3622 C CG  . PHE B 1 114 ? -26.185 27.282  -16.864 1.00 49.27  ? 111 PHE B CG  1 
ATOM   3623 C CD1 . PHE B 1 114 ? -25.348 27.658  -15.811 1.00 51.81  ? 111 PHE B CD1 1 
ATOM   3624 C CD2 . PHE B 1 114 ? -27.537 27.053  -16.611 1.00 47.28  ? 111 PHE B CD2 1 
ATOM   3625 C CE1 . PHE B 1 114 ? -25.839 27.784  -14.497 1.00 54.66  ? 111 PHE B CE1 1 
ATOM   3626 C CE2 . PHE B 1 114 ? -28.044 27.181  -15.315 1.00 48.33  ? 111 PHE B CE2 1 
ATOM   3627 C CZ  . PHE B 1 114 ? -27.185 27.545  -14.247 1.00 53.73  ? 111 PHE B CZ  1 
ATOM   3628 N N   . PRO B 1 115 ? -23.531 27.950  -20.519 1.00 45.59  ? 112 PRO B N   1 
ATOM   3629 C CA  . PRO B 1 115 ? -23.120 27.615  -21.885 1.00 44.26  ? 112 PRO B CA  1 
ATOM   3630 C C   . PRO B 1 115 ? -23.623 26.246  -22.296 1.00 44.76  ? 112 PRO B C   1 
ATOM   3631 O O   . PRO B 1 115 ? -22.826 25.328  -22.497 1.00 51.37  ? 112 PRO B O   1 
ATOM   3632 C CB  . PRO B 1 115 ? -21.595 27.640  -21.791 1.00 50.50  ? 112 PRO B CB  1 
ATOM   3633 C CG  . PRO B 1 115 ? -21.341 27.144  -20.374 1.00 43.30  ? 112 PRO B CG  1 
ATOM   3634 C CD  . PRO B 1 115 ? -22.417 27.834  -19.563 1.00 45.54  ? 112 PRO B CD  1 
ATOM   3635 N N   . MET B 1 116 ? -24.932 26.099  -22.431 1.00 42.02  ? 113 MET B N   1 
ATOM   3636 C CA  . MET B 1 116 ? -25.542 24.830  -22.795 1.00 38.25  ? 113 MET B CA  1 
ATOM   3637 C C   . MET B 1 116 ? -25.504 24.597  -24.311 1.00 39.37  ? 113 MET B C   1 
ATOM   3638 O O   . MET B 1 116 ? -25.518 25.540  -25.107 1.00 42.29  ? 113 MET B O   1 
ATOM   3639 C CB  . MET B 1 116 ? -26.978 24.811  -22.281 1.00 38.96  ? 113 MET B CB  1 
ATOM   3640 C CG  . MET B 1 116 ? -27.854 23.757  -22.897 1.00 44.65  ? 113 MET B CG  1 
ATOM   3641 S SD  . MET B 1 116 ? -29.556 24.079  -22.470 1.00 53.24  ? 113 MET B SD  1 
ATOM   3642 C CE  . MET B 1 116 ? -29.526 25.854  -22.553 1.00 45.94  ? 113 MET B CE  1 
ATOM   3643 N N   . VAL B 1 117 ? -25.441 23.324  -24.706 1.00 37.53  ? 114 VAL B N   1 
ATOM   3644 C CA  . VAL B 1 117 ? -25.336 22.910  -26.112 1.00 39.81  ? 114 VAL B CA  1 
ATOM   3645 C C   . VAL B 1 117 ? -26.544 22.040  -26.456 1.00 37.86  ? 114 VAL B C   1 
ATOM   3646 O O   . VAL B 1 117 ? -26.654 20.909  -25.963 1.00 38.70  ? 114 VAL B O   1 
ATOM   3647 C CB  . VAL B 1 117 ? -24.037 22.141  -26.381 1.00 29.29  ? 114 VAL B CB  1 
ATOM   3648 C CG1 . VAL B 1 117 ? -23.988 21.691  -27.796 1.00 27.90  ? 114 VAL B CG1 1 
ATOM   3649 C CG2 . VAL B 1 117 ? -22.856 23.000  -26.069 1.00 35.33  ? 114 VAL B CG2 1 
ATOM   3650 N N   . PHE B 1 118 ? -27.450 22.547  -27.285 1.00 31.05  ? 115 PHE B N   1 
ATOM   3651 C CA  . PHE B 1 118 ? -28.572 21.704  -27.678 1.00 34.39  ? 115 PHE B CA  1 
ATOM   3652 C C   . PHE B 1 118 ? -28.056 20.531  -28.513 1.00 34.40  ? 115 PHE B C   1 
ATOM   3653 O O   . PHE B 1 118 ? -27.114 20.700  -29.294 1.00 32.52  ? 115 PHE B O   1 
ATOM   3654 C CB  . PHE B 1 118 ? -29.613 22.486  -28.468 1.00 28.69  ? 115 PHE B CB  1 
ATOM   3655 C CG  . PHE B 1 118 ? -30.267 23.570  -27.689 1.00 30.15  ? 115 PHE B CG  1 
ATOM   3656 C CD1 . PHE B 1 118 ? -31.030 23.278  -26.582 1.00 32.30  ? 115 PHE B CD1 1 
ATOM   3657 C CD2 . PHE B 1 118 ? -30.137 24.881  -28.075 1.00 31.46  ? 115 PHE B CD2 1 
ATOM   3658 C CE1 . PHE B 1 118 ? -31.651 24.274  -25.871 1.00 31.94  ? 115 PHE B CE1 1 
ATOM   3659 C CE2 . PHE B 1 118 ? -30.748 25.884  -27.363 1.00 36.13  ? 115 PHE B CE2 1 
ATOM   3660 C CZ  . PHE B 1 118 ? -31.509 25.578  -26.255 1.00 33.61  ? 115 PHE B CZ  1 
ATOM   3661 N N   . PRO B 1 119 ? -28.621 19.332  -28.343 1.00 31.42  ? 116 PRO B N   1 
ATOM   3662 C CA  . PRO B 1 119 ? -28.048 18.148  -28.989 1.00 35.22  ? 116 PRO B CA  1 
ATOM   3663 C C   . PRO B 1 119 ? -28.286 18.140  -30.491 1.00 37.20  ? 116 PRO B C   1 
ATOM   3664 O O   . PRO B 1 119 ? -29.054 18.931  -31.050 1.00 36.71  ? 116 PRO B O   1 
ATOM   3665 C CB  . PRO B 1 119 ? -28.765 16.984  -28.311 1.00 29.10  ? 116 PRO B CB  1 
ATOM   3666 C CG  . PRO B 1 119 ? -30.034 17.568  -27.838 1.00 33.11  ? 116 PRO B CG  1 
ATOM   3667 C CD  . PRO B 1 119 ? -29.705 18.964  -27.417 1.00 32.88  ? 116 PRO B CD  1 
ATOM   3668 N N   . ALA B 1 120 ? -27.560 17.234  -31.144 1.00 37.21  ? 117 ALA B N   1 
ATOM   3669 C CA  . ALA B 1 120 ? -27.804 16.917  -32.539 1.00 38.68  ? 117 ALA B CA  1 
ATOM   3670 C C   . ALA B 1 120 ? -29.187 16.306  -32.699 1.00 36.96  ? 117 ALA B C   1 
ATOM   3671 O O   . ALA B 1 120 ? -29.700 15.635  -31.798 1.00 38.57  ? 117 ALA B O   1 
ATOM   3672 C CB  . ALA B 1 120 ? -26.743 15.950  -33.057 1.00 32.59  ? 117 ALA B CB  1 
ATOM   3673 N N   . TYR B 1 121 ? -29.800 16.553  -33.856 1.00 40.67  ? 118 TYR B N   1 
ATOM   3674 C CA  . TYR B 1 121 ? -31.062 15.892  -34.176 1.00 42.53  ? 118 TYR B CA  1 
ATOM   3675 C C   . TYR B 1 121 ? -30.880 14.380  -34.154 1.00 43.22  ? 118 TYR B C   1 
ATOM   3676 O O   . TYR B 1 121 ? -29.894 13.849  -34.686 1.00 40.99  ? 118 TYR B O   1 
ATOM   3677 C CB  . TYR B 1 121 ? -31.576 16.305  -35.551 1.00 37.23  ? 118 TYR B CB  1 
ATOM   3678 C CG  . TYR B 1 121 ? -32.007 17.747  -35.690 1.00 42.12  ? 118 TYR B CG  1 
ATOM   3679 C CD1 . TYR B 1 121 ? -31.959 18.626  -34.618 1.00 39.84  ? 118 TYR B CD1 1 
ATOM   3680 C CD2 . TYR B 1 121 ? -32.474 18.229  -36.910 1.00 43.91  ? 118 TYR B CD2 1 
ATOM   3681 C CE1 . TYR B 1 121 ? -32.352 19.941  -34.760 1.00 40.34  ? 118 TYR B CE1 1 
ATOM   3682 C CE2 . TYR B 1 121 ? -32.883 19.540  -37.055 1.00 39.57  ? 118 TYR B CE2 1 
ATOM   3683 C CZ  . TYR B 1 121 ? -32.816 20.389  -35.982 1.00 40.51  ? 118 TYR B CZ  1 
ATOM   3684 O OH  . TYR B 1 121 ? -33.211 21.692  -36.135 1.00 41.06  ? 118 TYR B OH  1 
ATOM   3685 N N   . ARG B 1 122 ? -31.853 13.692  -33.549 1.00 34.74  ? 119 ARG B N   1 
ATOM   3686 C CA  . ARG B 1 122 ? -31.836 12.248  -33.368 1.00 37.22  ? 119 ARG B CA  1 
ATOM   3687 C C   . ARG B 1 122 ? -32.893 11.600  -34.270 1.00 46.25  ? 119 ARG B C   1 
ATOM   3688 O O   . ARG B 1 122 ? -34.100 11.820  -34.093 1.00 43.40  ? 119 ARG B O   1 
ATOM   3689 C CB  . ARG B 1 122 ? -32.067 11.915  -31.897 1.00 39.42  ? 119 ARG B CB  1 
ATOM   3690 C CG  . ARG B 1 122 ? -32.558 10.531  -31.628 1.00 38.68  ? 119 ARG B CG  1 
ATOM   3691 C CD  . ARG B 1 122 ? -32.751 10.383  -30.154 1.00 35.19  ? 119 ARG B CD  1 
ATOM   3692 N NE  . ARG B 1 122 ? -34.074 10.765  -29.675 1.00 35.44  ? 119 ARG B NE  1 
ATOM   3693 C CZ  . ARG B 1 122 ? -35.040 9.903   -29.384 1.00 36.98  ? 119 ARG B CZ  1 
ATOM   3694 N NH1 . ARG B 1 122 ? -34.920 8.611   -29.657 1.00 38.46  ? 119 ARG B NH1 1 
ATOM   3695 N NH2 . ARG B 1 122 ? -36.139 10.342  -28.777 1.00 35.60  ? 119 ARG B NH2 1 
ATOM   3696 N N   . LYS B 1 123 ? -32.435 10.799  -35.233 1.00 42.40  ? 120 LYS B N   1 
ATOM   3697 C CA  . LYS B 1 123 ? -33.343 10.090  -36.124 1.00 44.09  ? 120 LYS B CA  1 
ATOM   3698 C C   . LYS B 1 123 ? -34.235 9.157   -35.335 1.00 42.88  ? 120 LYS B C   1 
ATOM   3699 O O   . LYS B 1 123 ? -33.761 8.403   -34.490 1.00 43.64  ? 120 LYS B O   1 
ATOM   3700 C CB  . LYS B 1 123 ? -32.555 9.292   -37.162 1.00 49.65  ? 120 LYS B CB  1 
ATOM   3701 C CG  . LYS B 1 123 ? -33.375 8.314   -38.008 1.00 48.07  ? 120 LYS B CG  1 
ATOM   3702 C CD  . LYS B 1 123 ? -32.802 8.271   -39.417 1.00 49.46  ? 120 LYS B CD  1 
ATOM   3703 C CE  . LYS B 1 123 ? -32.983 6.921   -40.095 1.00 58.01  ? 120 LYS B CE  1 
ATOM   3704 N NZ  . LYS B 1 123 ? -32.321 6.967   -41.434 1.00 55.39  ? 120 LYS B NZ  1 
ATOM   3705 N N   . LEU B 1 124 ? -35.530 9.227   -35.593 1.00 46.31  ? 121 LEU B N   1 
ATOM   3706 C CA  . LEU B 1 124 ? -36.471 8.272   -35.041 1.00 50.38  ? 121 LEU B CA  1 
ATOM   3707 C C   . LEU B 1 124 ? -36.700 7.152   -36.049 1.00 55.10  ? 121 LEU B C   1 
ATOM   3708 O O   . LEU B 1 124 ? -36.400 7.296   -37.235 1.00 57.65  ? 121 LEU B O   1 
ATOM   3709 C CB  . LEU B 1 124 ? -37.780 8.969   -34.690 1.00 47.24  ? 121 LEU B CB  1 
ATOM   3710 C CG  . LEU B 1 124 ? -37.625 10.089  -33.665 1.00 48.52  ? 121 LEU B CG  1 
ATOM   3711 C CD1 . LEU B 1 124 ? -38.905 10.898  -33.589 1.00 45.74  ? 121 LEU B CD1 1 
ATOM   3712 C CD2 . LEU B 1 124 ? -37.242 9.542   -32.272 1.00 41.96  ? 121 LEU B CD2 1 
ATOM   3713 N N   . ASP B 1 125 ? -37.201 6.012   -35.564 1.00 61.91  ? 122 ASP B N   1 
ATOM   3714 C CA  . ASP B 1 125 ? -37.498 4.878   -36.439 1.00 70.73  ? 122 ASP B CA  1 
ATOM   3715 C C   . ASP B 1 125 ? -38.919 4.405   -36.195 1.00 70.34  ? 122 ASP B C   1 
ATOM   3716 O O   . ASP B 1 125 ? -39.243 3.964   -35.087 1.00 69.93  ? 122 ASP B O   1 
ATOM   3717 C CB  . ASP B 1 125 ? -36.523 3.718   -36.241 1.00 79.95  ? 122 ASP B CB  1 
ATOM   3718 C CG  . ASP B 1 125 ? -36.547 2.738   -37.413 1.00 89.09  ? 122 ASP B CG  1 
ATOM   3719 O OD1 . ASP B 1 125 ? -37.475 2.824   -38.261 1.00 85.76  ? 122 ASP B OD1 1 
ATOM   3720 O OD2 . ASP B 1 125 ? -35.644 1.875   -37.488 1.00 94.36  ? 122 ASP B OD2 1 
ATOM   3721 N N   . LEU B 1 126 ? -39.746 4.468   -37.247 1.00 67.93  ? 123 LEU B N   1 
ATOM   3722 C CA  . LEU B 1 126 ? -41.175 4.215   -37.106 1.00 64.29  ? 123 LEU B CA  1 
ATOM   3723 C C   . LEU B 1 126 ? -41.452 2.785   -36.676 1.00 74.07  ? 123 LEU B C   1 
ATOM   3724 O O   . LEU B 1 126 ? -42.442 2.533   -35.970 1.00 71.39  ? 123 LEU B O   1 
ATOM   3725 C CB  . LEU B 1 126 ? -41.901 4.508   -38.414 1.00 60.51  ? 123 LEU B CB  1 
ATOM   3726 C CG  . LEU B 1 126 ? -41.858 5.896   -39.051 1.00 62.71  ? 123 LEU B CG  1 
ATOM   3727 C CD1 . LEU B 1 126 ? -40.534 6.159   -39.781 1.00 57.30  ? 123 LEU B CD1 1 
ATOM   3728 C CD2 . LEU B 1 126 ? -43.039 6.033   -40.004 1.00 56.89  ? 123 LEU B CD2 1 
ATOM   3729 N N   . ARG B 1 127 ? -40.607 1.835   -37.102 1.00 74.49  ? 124 ARG B N   1 
ATOM   3730 C CA  . ARG B 1 127 ? -40.745 0.470   -36.612 1.00 75.89  ? 124 ARG B CA  1 
ATOM   3731 C C   . ARG B 1 127 ? -40.878 0.468   -35.092 1.00 74.69  ? 124 ARG B C   1 
ATOM   3732 O O   . ARG B 1 127 ? -41.740 -0.221  -34.535 1.00 78.03  ? 124 ARG B O   1 
ATOM   3733 C CB  . ARG B 1 127 ? -39.558 -0.388  -37.074 1.00 80.03  ? 124 ARG B CB  1 
ATOM   3734 C CG  . ARG B 1 127 ? -38.193 0.112   -36.629 1.00 85.00  ? 124 ARG B CG  1 
ATOM   3735 C CD  . ARG B 1 127 ? -37.170 -1.003  -36.409 1.00 91.56  ? 124 ARG B CD  1 
ATOM   3736 N NE  . ARG B 1 127 ? -36.167 -0.605  -35.421 1.00 102.39 ? 124 ARG B NE  1 
ATOM   3737 C CZ  . ARG B 1 127 ? -34.853 -0.600  -35.622 1.00 104.01 ? 124 ARG B CZ  1 
ATOM   3738 N NH1 . ARG B 1 127 ? -34.322 -1.027  -36.761 1.00 93.17  ? 124 ARG B NH1 1 
ATOM   3739 N NH2 . ARG B 1 127 ? -34.052 -0.162  -34.653 1.00 90.03  ? 124 ARG B NH2 1 
ATOM   3740 N N   . HIS B 1 128 ? -40.095 1.311   -34.413 1.00 75.11  ? 125 HIS B N   1 
ATOM   3741 C CA  . HIS B 1 128 ? -40.085 1.369   -32.957 1.00 70.21  ? 125 HIS B CA  1 
ATOM   3742 C C   . HIS B 1 128 ? -41.408 1.826   -32.352 1.00 65.43  ? 125 HIS B C   1 
ATOM   3743 O O   . HIS B 1 128 ? -41.538 1.820   -31.124 1.00 61.37  ? 125 HIS B O   1 
ATOM   3744 C CB  . HIS B 1 128 ? -38.963 2.300   -32.501 1.00 70.92  ? 125 HIS B CB  1 
ATOM   3745 C CG  . HIS B 1 128 ? -37.781 1.587   -31.927 1.00 83.48  ? 125 HIS B CG  1 
ATOM   3746 N ND1 . HIS B 1 128 ? -37.761 1.108   -30.632 1.00 86.63  ? 125 HIS B ND1 1 
ATOM   3747 C CD2 . HIS B 1 128 ? -36.576 1.280   -32.463 1.00 86.42  ? 125 HIS B CD2 1 
ATOM   3748 C CE1 . HIS B 1 128 ? -36.596 0.530   -30.397 1.00 85.14  ? 125 HIS B CE1 1 
ATOM   3749 N NE2 . HIS B 1 128 ? -35.857 0.624   -31.490 1.00 94.06  ? 125 HIS B NE2 1 
ATOM   3750 N N   . TYR B 1 129 ? -42.389 2.224   -33.154 1.00 64.68  ? 126 TYR B N   1 
ATOM   3751 C CA  . TYR B 1 129 ? -43.616 2.789   -32.614 1.00 65.18  ? 126 TYR B CA  1 
ATOM   3752 C C   . TYR B 1 129 ? -44.824 2.036   -33.151 1.00 67.29  ? 126 TYR B C   1 
ATOM   3753 O O   . TYR B 1 129 ? -44.835 1.581   -34.300 1.00 68.98  ? 126 TYR B O   1 
ATOM   3754 C CB  . TYR B 1 129 ? -43.723 4.302   -32.923 1.00 62.05  ? 126 TYR B CB  1 
ATOM   3755 C CG  . TYR B 1 129 ? -42.468 5.067   -32.527 1.00 65.63  ? 126 TYR B CG  1 
ATOM   3756 C CD1 . TYR B 1 129 ? -41.396 5.192   -33.411 1.00 61.69  ? 126 TYR B CD1 1 
ATOM   3757 C CD2 . TYR B 1 129 ? -42.333 5.623   -31.263 1.00 62.14  ? 126 TYR B CD2 1 
ATOM   3758 C CE1 . TYR B 1 129 ? -40.243 5.849   -33.056 1.00 56.50  ? 126 TYR B CE1 1 
ATOM   3759 C CE2 . TYR B 1 129 ? -41.171 6.291   -30.899 1.00 59.10  ? 126 TYR B CE2 1 
ATOM   3760 C CZ  . TYR B 1 129 ? -40.133 6.399   -31.804 1.00 57.21  ? 126 TYR B CZ  1 
ATOM   3761 O OH  . TYR B 1 129 ? -38.975 7.061   -31.457 1.00 59.05  ? 126 TYR B OH  1 
ATOM   3762 N N   . ASP B 1 130 ? -45.822 1.894   -32.285 1.00 59.18  ? 127 ASP B N   1 
ATOM   3763 C CA  . ASP B 1 130 ? -47.089 1.249   -32.581 1.00 64.38  ? 127 ASP B CA  1 
ATOM   3764 C C   . ASP B 1 130 ? -48.175 2.049   -31.871 1.00 66.93  ? 127 ASP B C   1 
ATOM   3765 O O   . ASP B 1 130 ? -47.937 3.155   -31.383 1.00 59.25  ? 127 ASP B O   1 
ATOM   3766 C CB  . ASP B 1 130 ? -47.076 -0.230  -32.160 1.00 67.42  ? 127 ASP B CB  1 
ATOM   3767 C CG  . ASP B 1 130 ? -46.322 -0.478  -30.840 1.00 77.08  ? 127 ASP B CG  1 
ATOM   3768 O OD1 . ASP B 1 130 ? -46.617 0.213   -29.829 1.00 74.28  ? 127 ASP B OD1 1 
ATOM   3769 O OD2 . ASP B 1 130 ? -45.444 -1.379  -30.809 1.00 73.44  ? 127 ASP B OD2 1 
ATOM   3770 N N   . ASP B 1 131 ? -49.380 1.492   -31.800 1.00 69.91  ? 128 ASP B N   1 
ATOM   3771 C CA  . ASP B 1 131 ? -50.452 2.206   -31.118 1.00 69.42  ? 128 ASP B CA  1 
ATOM   3772 C C   . ASP B 1 131 ? -50.202 2.275   -29.611 1.00 67.79  ? 128 ASP B C   1 
ATOM   3773 O O   . ASP B 1 131 ? -50.670 3.208   -28.945 1.00 64.38  ? 128 ASP B O   1 
ATOM   3774 C CB  . ASP B 1 131 ? -51.801 1.542   -31.435 1.00 78.07  ? 128 ASP B CB  1 
ATOM   3775 C CG  . ASP B 1 131 ? -52.891 2.552   -31.837 1.00 80.86  ? 128 ASP B CG  1 
ATOM   3776 O OD1 . ASP B 1 131 ? -52.879 3.679   -31.299 1.00 78.19  ? 128 ASP B OD1 1 
ATOM   3777 O OD2 . ASP B 1 131 ? -53.764 2.218   -32.683 1.00 76.41  ? 128 ASP B OD2 1 
ATOM   3778 N N   . ALA B 1 132 ? -49.456 1.309   -29.059 1.00 69.35  ? 129 ALA B N   1 
ATOM   3779 C CA  . ALA B 1 132 ? -49.160 1.312   -27.624 1.00 71.71  ? 129 ALA B CA  1 
ATOM   3780 C C   . ALA B 1 132 ? -48.146 2.392   -27.277 1.00 68.95  ? 129 ALA B C   1 
ATOM   3781 O O   . ALA B 1 132 ? -48.265 3.079   -26.249 1.00 58.03  ? 129 ALA B O   1 
ATOM   3782 C CB  . ALA B 1 132 ? -48.634 -0.061  -27.195 1.00 70.07  ? 129 ALA B CB  1 
ATOM   3783 N N   . LEU B 1 133 ? -47.146 2.550   -28.140 1.00 65.86  ? 130 LEU B N   1 
ATOM   3784 C CA  . LEU B 1 133 ? -46.085 3.533   -28.007 1.00 59.64  ? 130 LEU B CA  1 
ATOM   3785 C C   . LEU B 1 133 ? -46.097 4.383   -29.272 1.00 53.05  ? 130 LEU B C   1 
ATOM   3786 O O   . LEU B 1 133 ? -45.285 4.159   -30.183 1.00 56.55  ? 130 LEU B O   1 
ATOM   3787 C CB  . LEU B 1 133 ? -44.748 2.827   -27.819 1.00 61.82  ? 130 LEU B CB  1 
ATOM   3788 C CG  . LEU B 1 133 ? -43.824 3.523   -26.842 1.00 60.09  ? 130 LEU B CG  1 
ATOM   3789 C CD1 . LEU B 1 133 ? -44.583 3.769   -25.551 1.00 54.00  ? 130 LEU B CD1 1 
ATOM   3790 C CD2 . LEU B 1 133 ? -42.594 2.666   -26.626 1.00 62.96  ? 130 LEU B CD2 1 
ATOM   3791 N N   . PRO B 1 134 ? -47.017 5.345   -29.381 1.00 51.24  ? 131 PRO B N   1 
ATOM   3792 C CA  . PRO B 1 134 ? -47.117 6.137   -30.618 1.00 50.40  ? 131 PRO B CA  1 
ATOM   3793 C C   . PRO B 1 134 ? -45.849 6.937   -30.889 1.00 51.46  ? 131 PRO B C   1 
ATOM   3794 O O   . PRO B 1 134 ? -45.013 7.153   -30.007 1.00 52.52  ? 131 PRO B O   1 
ATOM   3795 C CB  . PRO B 1 134 ? -48.319 7.058   -30.359 1.00 44.40  ? 131 PRO B CB  1 
ATOM   3796 C CG  . PRO B 1 134 ? -48.488 7.098   -28.870 1.00 49.13  ? 131 PRO B CG  1 
ATOM   3797 C CD  . PRO B 1 134 ? -48.024 5.745   -28.380 1.00 52.87  ? 131 PRO B CD  1 
ATOM   3798 N N   . LEU B 1 135 ? -45.704 7.374   -32.142 1.00 48.49  ? 132 LEU B N   1 
ATOM   3799 C CA  . LEU B 1 135 ? -44.570 8.220   -32.505 1.00 45.20  ? 132 LEU B CA  1 
ATOM   3800 C C   . LEU B 1 135 ? -44.426 9.437   -31.598 1.00 45.24  ? 132 LEU B C   1 
ATOM   3801 O O   . LEU B 1 135 ? -43.307 9.891   -31.344 1.00 45.38  ? 132 LEU B O   1 
ATOM   3802 C CB  . LEU B 1 135 ? -44.702 8.695   -33.943 1.00 44.72  ? 132 LEU B CB  1 
ATOM   3803 C CG  . LEU B 1 135 ? -43.668 9.755   -34.338 1.00 52.04  ? 132 LEU B CG  1 
ATOM   3804 C CD1 . LEU B 1 135 ? -42.291 9.131   -34.576 1.00 45.75  ? 132 LEU B CD1 1 
ATOM   3805 C CD2 . LEU B 1 135 ? -44.120 10.576  -35.536 1.00 48.25  ? 132 LEU B CD2 1 
ATOM   3806 N N   . SER B 1 136 ? -45.532 9.974   -31.087 1.00 44.10  ? 133 SER B N   1 
ATOM   3807 C CA  . SER B 1 136 ? -45.427 11.159  -30.246 1.00 39.89  ? 133 SER B CA  1 
ATOM   3808 C C   . SER B 1 136 ? -44.661 10.891  -28.951 1.00 47.18  ? 133 SER B C   1 
ATOM   3809 O O   . SER B 1 136 ? -44.219 11.843  -28.293 1.00 46.68  ? 133 SER B O   1 
ATOM   3810 C CB  . SER B 1 136 ? -46.817 11.717  -29.948 1.00 35.45  ? 133 SER B CB  1 
ATOM   3811 O OG  . SER B 1 136 ? -47.279 11.335  -28.674 1.00 38.59  ? 133 SER B OG  1 
ATOM   3812 N N   . THR B 1 137 ? -44.474 9.624   -28.575 1.00 47.03  ? 134 THR B N   1 
ATOM   3813 C CA  . THR B 1 137 ? -43.708 9.322   -27.372 1.00 45.54  ? 134 THR B CA  1 
ATOM   3814 C C   . THR B 1 137 ? -42.260 9.770   -27.474 1.00 44.49  ? 134 THR B C   1 
ATOM   3815 O O   . THR B 1 137 ? -41.589 9.833   -26.443 1.00 48.20  ? 134 THR B O   1 
ATOM   3816 C CB  . THR B 1 137 ? -43.744 7.823   -27.048 1.00 46.76  ? 134 THR B CB  1 
ATOM   3817 O OG1 . THR B 1 137 ? -43.269 7.057   -28.171 1.00 49.88  ? 134 THR B OG1 1 
ATOM   3818 C CG2 . THR B 1 137 ? -45.150 7.392   -26.687 1.00 44.28  ? 134 THR B CG2 1 
ATOM   3819 N N   . ALA B 1 138 ? -41.763 10.095  -28.671 1.00 43.80  ? 135 ALA B N   1 
ATOM   3820 C CA  . ALA B 1 138 ? -40.398 10.600  -28.803 1.00 45.63  ? 135 ALA B CA  1 
ATOM   3821 C C   . ALA B 1 138 ? -40.206 11.978  -28.164 1.00 46.36  ? 135 ALA B C   1 
ATOM   3822 O O   . ALA B 1 138 ? -39.059 12.443  -28.050 1.00 43.65  ? 135 ALA B O   1 
ATOM   3823 C CB  . ALA B 1 138 ? -39.994 10.641  -30.278 1.00 41.95  ? 135 ALA B CB  1 
ATOM   3824 N N   . LEU B 1 139 ? -41.295 12.641  -27.764 1.00 44.59  ? 136 LEU B N   1 
ATOM   3825 C CA  . LEU B 1 139 ? -41.250 13.872  -26.995 1.00 40.63  ? 136 LEU B CA  1 
ATOM   3826 C C   . LEU B 1 139 ? -41.625 13.648  -25.539 1.00 45.07  ? 136 LEU B C   1 
ATOM   3827 O O   . LEU B 1 139 ? -41.573 14.597  -24.745 1.00 45.03  ? 136 LEU B O   1 
ATOM   3828 C CB  . LEU B 1 139 ? -42.178 14.926  -27.619 1.00 41.79  ? 136 LEU B CB  1 
ATOM   3829 C CG  . LEU B 1 139 ? -41.660 15.461  -28.954 1.00 35.92  ? 136 LEU B CG  1 
ATOM   3830 C CD1 . LEU B 1 139 ? -42.615 16.438  -29.636 1.00 36.67  ? 136 LEU B CD1 1 
ATOM   3831 C CD2 . LEU B 1 139 ? -40.359 16.112  -28.698 1.00 30.65  ? 136 LEU B CD2 1 
ATOM   3832 N N   . GLY B 1 140 ? -42.006 12.421  -25.171 1.00 42.73  ? 137 GLY B N   1 
ATOM   3833 C CA  . GLY B 1 140 ? -42.318 12.081  -23.791 1.00 50.28  ? 137 GLY B CA  1 
ATOM   3834 C C   . GLY B 1 140 ? -41.533 10.887  -23.277 1.00 52.85  ? 137 GLY B C   1 
ATOM   3835 O O   . GLY B 1 140 ? -40.301 10.953  -23.189 1.00 49.01  ? 137 GLY B O   1 
ATOM   3836 N N   . VAL B 1 141 ? -42.225 9.780   -22.974 1.00 54.26  ? 138 VAL B N   1 
ATOM   3837 C CA  . VAL B 1 141 ? -41.565 8.648   -22.323 1.00 54.25  ? 138 VAL B CA  1 
ATOM   3838 C C   . VAL B 1 141 ? -40.415 8.121   -23.162 1.00 48.86  ? 138 VAL B C   1 
ATOM   3839 O O   . VAL B 1 141 ? -39.408 7.662   -22.617 1.00 53.63  ? 138 VAL B O   1 
ATOM   3840 C CB  . VAL B 1 141 ? -42.561 7.520   -22.000 1.00 55.19  ? 138 VAL B CB  1 
ATOM   3841 C CG1 . VAL B 1 141 ? -43.058 6.845   -23.284 1.00 45.21  ? 138 VAL B CG1 1 
ATOM   3842 C CG2 . VAL B 1 141 ? -41.887 6.510   -21.116 1.00 44.63  ? 138 VAL B CG2 1 
ATOM   3843 N N   . MET B 1 142 ? -40.531 8.169   -24.486 1.00 44.65  ? 139 MET B N   1 
ATOM   3844 C CA  . MET B 1 142 ? -39.420 7.824   -25.366 1.00 48.31  ? 139 MET B CA  1 
ATOM   3845 C C   . MET B 1 142 ? -38.653 9.056   -25.823 1.00 47.26  ? 139 MET B C   1 
ATOM   3846 O O   . MET B 1 142 ? -38.086 9.063   -26.923 1.00 47.07  ? 139 MET B O   1 
ATOM   3847 C CB  . MET B 1 142 ? -39.896 7.036   -26.593 1.00 52.62  ? 139 MET B CB  1 
ATOM   3848 C CG  . MET B 1 142 ? -40.500 5.663   -26.313 1.00 55.91  ? 139 MET B CG  1 
ATOM   3849 S SD  . MET B 1 142 ? -39.457 4.508   -25.393 1.00 60.86  ? 139 MET B SD  1 
ATOM   3850 C CE  . MET B 1 142 ? -40.280 4.558   -23.799 1.00 48.79  ? 139 MET B CE  1 
ATOM   3851 N N   . GLY B 1 143 ? -38.641 10.105  -25.013 1.00 42.06  ? 140 GLY B N   1 
ATOM   3852 C CA  . GLY B 1 143 ? -37.884 11.284  -25.352 1.00 40.95  ? 140 GLY B CA  1 
ATOM   3853 C C   . GLY B 1 143 ? -37.196 11.900  -24.156 1.00 47.48  ? 140 GLY B C   1 
ATOM   3854 O O   . GLY B 1 143 ? -36.657 11.199  -23.295 1.00 44.78  ? 140 GLY B O   1 
ATOM   3855 N N   . GLY B 1 144 ? -37.233 13.227  -24.092 1.00 50.23  ? 141 GLY B N   1 
ATOM   3856 C CA  . GLY B 1 144 ? -36.642 13.963  -23.001 1.00 38.10  ? 141 GLY B CA  1 
ATOM   3857 C C   . GLY B 1 144 ? -37.096 13.504  -21.635 1.00 40.53  ? 141 GLY B C   1 
ATOM   3858 O O   . GLY B 1 144 ? -36.297 13.002  -20.841 1.00 40.35  ? 141 GLY B O   1 
ATOM   3859 N N   . PRO B 1 145 ? -38.384 13.687  -21.322 1.00 43.84  ? 142 PRO B N   1 
ATOM   3860 C CA  . PRO B 1 145 ? -38.829 13.411  -19.948 1.00 35.89  ? 142 PRO B CA  1 
ATOM   3861 C C   . PRO B 1 145 ? -38.631 11.961  -19.545 1.00 40.52  ? 142 PRO B C   1 
ATOM   3862 O O   . PRO B 1 145 ? -38.199 11.691  -18.421 1.00 45.24  ? 142 PRO B O   1 
ATOM   3863 C CB  . PRO B 1 145 ? -40.310 13.811  -19.972 1.00 41.23  ? 142 PRO B CB  1 
ATOM   3864 C CG  . PRO B 1 145 ? -40.462 14.675  -21.190 1.00 41.79  ? 142 PRO B CG  1 
ATOM   3865 C CD  . PRO B 1 145 ? -39.497 14.127  -22.180 1.00 38.28  ? 142 PRO B CD  1 
ATOM   3866 N N   . GLY B 1 146 ? -38.897 11.013  -20.438 1.00 46.32  ? 143 GLY B N   1 
ATOM   3867 C CA  . GLY B 1 146 ? -38.611 9.621   -20.123 1.00 47.19  ? 143 GLY B CA  1 
ATOM   3868 C C   . GLY B 1 146 ? -37.145 9.361   -19.804 1.00 44.42  ? 143 GLY B C   1 
ATOM   3869 O O   . GLY B 1 146 ? -36.828 8.536   -18.947 1.00 42.37  ? 143 GLY B O   1 
ATOM   3870 N N   . MET B 1 147 ? -36.229 10.039  -20.504 1.00 42.95  ? 144 MET B N   1 
ATOM   3871 C CA  . MET B 1 147 ? -34.809 9.836   -20.227 1.00 41.08  ? 144 MET B CA  1 
ATOM   3872 C C   . MET B 1 147 ? -34.391 10.489  -18.918 1.00 42.53  ? 144 MET B C   1 
ATOM   3873 O O   . MET B 1 147 ? -33.457 10.010  -18.267 1.00 42.59  ? 144 MET B O   1 
ATOM   3874 C CB  . MET B 1 147 ? -33.947 10.363  -21.378 1.00 40.04  ? 144 MET B CB  1 
ATOM   3875 C CG  . MET B 1 147 ? -32.444 10.300  -21.111 1.00 39.31  ? 144 MET B CG  1 
ATOM   3876 S SD  . MET B 1 147 ? -31.775 8.638   -21.260 1.00 44.16  ? 144 MET B SD  1 
ATOM   3877 C CE  . MET B 1 147 ? -31.530 8.518   -23.035 1.00 41.28  ? 144 MET B CE  1 
ATOM   3878 N N   . THR B 1 148 ? -35.086 11.552  -18.505 1.00 41.00  ? 145 THR B N   1 
ATOM   3879 C CA  . THR B 1 148 ? -34.831 12.153  -17.201 1.00 40.35  ? 145 THR B CA  1 
ATOM   3880 C C   . THR B 1 148 ? -35.198 11.204  -16.064 1.00 41.62  ? 145 THR B C   1 
ATOM   3881 O O   . THR B 1 148 ? -34.413 11.010  -15.130 1.00 44.49  ? 145 THR B O   1 
ATOM   3882 C CB  . THR B 1 148 ? -35.595 13.468  -17.081 1.00 37.32  ? 145 THR B CB  1 
ATOM   3883 O OG1 . THR B 1 148 ? -35.016 14.414  -17.982 1.00 46.82  ? 145 THR B OG1 1 
ATOM   3884 C CG2 . THR B 1 148 ? -35.507 14.017  -15.688 1.00 36.75  ? 145 THR B CG2 1 
ATOM   3885 N N   . ALA B 1 149 ? -36.386 10.601  -16.118 1.00 38.66  ? 146 ALA B N   1 
ATOM   3886 C CA  . ALA B 1 149 ? -36.810 9.709   -15.038 1.00 42.36  ? 146 ALA B CA  1 
ATOM   3887 C C   . ALA B 1 149 ? -35.961 8.435   -15.002 1.00 40.45  ? 146 ALA B C   1 
ATOM   3888 O O   . ALA B 1 149 ? -35.353 8.104   -13.975 1.00 38.35  ? 146 ALA B O   1 
ATOM   3889 C CB  . ALA B 1 149 ? -38.296 9.374   -15.190 1.00 38.65  ? 146 ALA B CB  1 
ATOM   3890 N N   . TRP B 1 150 ? -35.891 7.722   -16.126 1.00 39.39  ? 147 TRP B N   1 
ATOM   3891 C CA  . TRP B 1 150 ? -35.175 6.450   -16.185 1.00 42.93  ? 147 TRP B CA  1 
ATOM   3892 C C   . TRP B 1 150 ? -33.694 6.607   -15.856 1.00 44.05  ? 147 TRP B C   1 
ATOM   3893 O O   . TRP B 1 150 ? -33.113 5.787   -15.130 1.00 40.00  ? 147 TRP B O   1 
ATOM   3894 C CB  . TRP B 1 150 ? -35.332 5.841   -17.570 1.00 37.41  ? 147 TRP B CB  1 
ATOM   3895 C CG  . TRP B 1 150 ? -34.505 4.641   -17.766 1.00 38.41  ? 147 TRP B CG  1 
ATOM   3896 C CD1 . TRP B 1 150 ? -34.763 3.388   -17.302 1.00 40.69  ? 147 TRP B CD1 1 
ATOM   3897 C CD2 . TRP B 1 150 ? -33.276 4.558   -18.488 1.00 38.37  ? 147 TRP B CD2 1 
ATOM   3898 N NE1 . TRP B 1 150 ? -33.774 2.528   -17.694 1.00 45.93  ? 147 TRP B NE1 1 
ATOM   3899 C CE2 . TRP B 1 150 ? -32.846 3.225   -18.424 1.00 41.71  ? 147 TRP B CE2 1 
ATOM   3900 C CE3 . TRP B 1 150 ? -32.494 5.484   -19.175 1.00 42.66  ? 147 TRP B CE3 1 
ATOM   3901 C CZ2 . TRP B 1 150 ? -31.666 2.797   -19.011 1.00 42.60  ? 147 TRP B CZ2 1 
ATOM   3902 C CZ3 . TRP B 1 150 ? -31.321 5.056   -19.766 1.00 46.83  ? 147 TRP B CZ3 1 
ATOM   3903 C CH2 . TRP B 1 150 ? -30.919 3.724   -19.680 1.00 46.10  ? 147 TRP B CH2 1 
ATOM   3904 N N   . GLY B 1 151 ? -33.057 7.633   -16.410 1.00 41.53  ? 148 GLY B N   1 
ATOM   3905 C CA  . GLY B 1 151 ? -31.657 7.865   -16.103 1.00 39.98  ? 148 GLY B CA  1 
ATOM   3906 C C   . GLY B 1 151 ? -31.402 8.101   -14.626 1.00 42.15  ? 148 GLY B C   1 
ATOM   3907 O O   . GLY B 1 151 ? -30.442 7.569   -14.066 1.00 47.72  ? 148 GLY B O   1 
ATOM   3908 N N   . THR B 1 152 ? -32.260 8.889   -13.967 1.00 37.55  ? 149 THR B N   1 
ATOM   3909 C CA  . THR B 1 152 ? -32.067 9.121   -12.540 1.00 41.69  ? 149 THR B CA  1 
ATOM   3910 C C   . THR B 1 152 ? -32.193 7.826   -11.747 1.00 41.28  ? 149 THR B C   1 
ATOM   3911 O O   . THR B 1 152 ? -31.374 7.554   -10.862 1.00 40.75  ? 149 THR B O   1 
ATOM   3912 C CB  . THR B 1 152 ? -33.053 10.170  -12.031 1.00 38.93  ? 149 THR B CB  1 
ATOM   3913 O OG1 . THR B 1 152 ? -32.716 11.417  -12.630 1.00 42.16  ? 149 THR B OG1 1 
ATOM   3914 C CG2 . THR B 1 152 ? -32.969 10.324  -10.507 1.00 37.75  ? 149 THR B CG2 1 
ATOM   3915 N N   . MET B 1 153 ? -33.182 6.993   -12.086 1.00 40.90  ? 150 MET B N   1 
ATOM   3916 C CA  . MET B 1 153 ? -33.495 5.813   -11.294 1.00 42.20  ? 150 MET B CA  1 
ATOM   3917 C C   . MET B 1 153 ? -32.585 4.631   -11.579 1.00 43.25  ? 150 MET B C   1 
ATOM   3918 O O   . MET B 1 153 ? -32.611 3.664   -10.809 1.00 57.53  ? 150 MET B O   1 
ATOM   3919 C CB  . MET B 1 153 ? -34.943 5.400   -11.520 1.00 34.61  ? 150 MET B CB  1 
ATOM   3920 C CG  . MET B 1 153 ? -35.881 6.524   -11.326 1.00 37.07  ? 150 MET B CG  1 
ATOM   3921 S SD  . MET B 1 153 ? -35.579 7.392   -9.782  1.00 48.65  ? 150 MET B SD  1 
ATOM   3922 C CE  . MET B 1 153 ? -36.477 6.333   -8.656  1.00 39.51  ? 150 MET B CE  1 
ATOM   3923 N N   . THR B 1 154 ? -31.796 4.674   -12.649 1.00 35.64  ? 151 THR B N   1 
ATOM   3924 C CA  . THR B 1 154 ? -30.816 3.636   -12.925 1.00 42.47  ? 151 THR B CA  1 
ATOM   3925 C C   . THR B 1 154 ? -29.385 4.123   -12.856 1.00 42.09  ? 151 THR B C   1 
ATOM   3926 O O   . THR B 1 154 ? -28.480 3.288   -12.743 1.00 41.09  ? 151 THR B O   1 
ATOM   3927 C CB  . THR B 1 154 ? -31.033 2.994   -14.316 1.00 39.48  ? 151 THR B CB  1 
ATOM   3928 O OG1 . THR B 1 154 ? -30.730 3.931   -15.353 1.00 38.11  ? 151 THR B OG1 1 
ATOM   3929 C CG2 . THR B 1 154 ? -32.445 2.541   -14.484 1.00 38.81  ? 151 THR B CG2 1 
ATOM   3930 N N   . LYS B 1 155 ? -29.147 5.437   -12.938 1.00 43.14  ? 152 LYS B N   1 
ATOM   3931 C CA  . LYS B 1 155 ? -27.787 5.956   -12.903 1.00 38.99  ? 152 LYS B CA  1 
ATOM   3932 C C   . LYS B 1 155 ? -27.434 6.709   -11.623 1.00 37.93  ? 152 LYS B C   1 
ATOM   3933 O O   . LYS B 1 155 ? -26.241 6.907   -11.366 1.00 40.75  ? 152 LYS B O   1 
ATOM   3934 C CB  . LYS B 1 155 ? -27.526 6.875   -14.105 1.00 35.14  ? 152 LYS B CB  1 
ATOM   3935 C CG  . LYS B 1 155 ? -27.874 6.274   -15.456 1.00 39.48  ? 152 LYS B CG  1 
ATOM   3936 C CD  . LYS B 1 155 ? -27.310 7.134   -16.609 1.00 40.59  ? 152 LYS B CD  1 
ATOM   3937 C CE  . LYS B 1 155 ? -27.971 6.800   -17.944 1.00 35.93  ? 152 LYS B CE  1 
ATOM   3938 N NZ  . LYS B 1 155 ? -27.928 5.334   -18.200 1.00 43.93  ? 152 LYS B NZ  1 
ATOM   3939 N N   . PHE B 1 156 ? -28.419 7.118   -10.807 1.00 36.46  ? 153 PHE B N   1 
ATOM   3940 C CA  . PHE B 1 156 ? -28.116 7.834   -9.564  1.00 34.73  ? 153 PHE B CA  1 
ATOM   3941 C C   . PHE B 1 156 ? -28.784 7.210   -8.351  1.00 34.22  ? 153 PHE B C   1 
ATOM   3942 O O   . PHE B 1 156 ? -28.109 6.695   -7.457  1.00 36.62  ? 153 PHE B O   1 
ATOM   3943 C CB  . PHE B 1 156 ? -28.539 9.299   -9.648  1.00 33.39  ? 153 PHE B CB  1 
ATOM   3944 C CG  . PHE B 1 156 ? -28.501 10.018  -8.326  1.00 37.88  ? 153 PHE B CG  1 
ATOM   3945 C CD1 . PHE B 1 156 ? -27.299 10.185  -7.639  1.00 40.13  ? 153 PHE B CD1 1 
ATOM   3946 C CD2 . PHE B 1 156 ? -29.658 10.533  -7.765  1.00 35.13  ? 153 PHE B CD2 1 
ATOM   3947 C CE1 . PHE B 1 156 ? -27.251 10.849  -6.404  1.00 30.36  ? 153 PHE B CE1 1 
ATOM   3948 C CE2 . PHE B 1 156 ? -29.615 11.202  -6.539  1.00 37.54  ? 153 PHE B CE2 1 
ATOM   3949 C CZ  . PHE B 1 156 ? -28.400 11.359  -5.865  1.00 33.74  ? 153 PHE B CZ  1 
ATOM   3950 N N   . MET B 1 157 ? -30.107 7.281   -8.299  1.00 37.76  ? 154 MET B N   1 
ATOM   3951 C CA  . MET B 1 157 ? -30.830 6.753   -7.151  1.00 44.67  ? 154 MET B CA  1 
ATOM   3952 C C   . MET B 1 157 ? -30.829 5.237   -7.156  1.00 47.55  ? 154 MET B C   1 
ATOM   3953 O O   . MET B 1 157 ? -31.026 4.591   -8.194  1.00 43.05  ? 154 MET B O   1 
ATOM   3954 C CB  . MET B 1 157 ? -32.261 7.260   -7.132  1.00 39.94  ? 154 MET B CB  1 
ATOM   3955 C CG  . MET B 1 157 ? -32.367 8.630   -6.531  1.00 35.51  ? 154 MET B CG  1 
ATOM   3956 S SD  . MET B 1 157 ? -34.087 9.151   -6.503  1.00 45.02  ? 154 MET B SD  1 
ATOM   3957 C CE  . MET B 1 157 ? -33.986 10.747  -5.676  1.00 38.35  ? 154 MET B CE  1 
ATOM   3958 N N   . GLN B 1 158 ? -30.571 4.673   -5.983  1.00 46.80  ? 155 GLN B N   1 
ATOM   3959 C CA  . GLN B 1 158 ? -30.611 3.236   -5.777  1.00 48.23  ? 155 GLN B CA  1 
ATOM   3960 C C   . GLN B 1 158 ? -31.805 2.972   -4.872  1.00 47.64  ? 155 GLN B C   1 
ATOM   3961 O O   . GLN B 1 158 ? -31.676 2.869   -3.657  1.00 49.30  ? 155 GLN B O   1 
ATOM   3962 C CB  . GLN B 1 158 ? -29.338 2.747   -5.175  1.00 47.60  ? 155 GLN B CB  1 
ATOM   3963 C CG  . GLN B 1 158 ? -28.109 3.002   -6.006  1.00 51.47  ? 155 GLN B CG  1 
ATOM   3964 C CD  . GLN B 1 158 ? -26.848 2.881   -5.172  1.00 63.68  ? 155 GLN B CD  1 
ATOM   3965 O OE1 . GLN B 1 158 ? -26.144 1.869   -5.233  1.00 65.47  ? 155 GLN B OE1 1 
ATOM   3966 N NE2 . GLN B 1 158 ? -26.569 3.909   -4.359  1.00 63.15  ? 155 GLN B NE2 1 
ATOM   3967 N N   . VAL B 1 159 ? -32.991 2.903   -5.472  1.00 55.05  ? 156 VAL B N   1 
ATOM   3968 C CA  . VAL B 1 159 ? -34.185 2.629   -4.680  1.00 53.42  ? 156 VAL B CA  1 
ATOM   3969 C C   . VAL B 1 159 ? -34.181 1.166   -4.275  1.00 51.57  ? 156 VAL B C   1 
ATOM   3970 O O   . VAL B 1 159 ? -34.021 0.267   -5.114  1.00 48.71  ? 156 VAL B O   1 
ATOM   3971 C CB  . VAL B 1 159 ? -35.459 2.997   -5.450  1.00 50.35  ? 156 VAL B CB  1 
ATOM   3972 C CG1 . VAL B 1 159 ? -36.647 3.039   -4.503  1.00 49.00  ? 156 VAL B CG1 1 
ATOM   3973 C CG2 . VAL B 1 159 ? -35.273 4.331   -6.105  1.00 47.35  ? 156 VAL B CG2 1 
ATOM   3974 N N   . ARG B 1 160 ? -34.329 0.927   -2.982  1.00 49.38  ? 157 ARG B N   1 
ATOM   3975 C CA  . ARG B 1 160 ? -34.260 -0.390  -2.395  1.00 51.02  ? 157 ARG B CA  1 
ATOM   3976 C C   . ARG B 1 160 ? -35.583 -0.708  -1.713  1.00 50.08  ? 157 ARG B C   1 
ATOM   3977 O O   . ARG B 1 160 ? -36.247 0.201   -1.202  1.00 49.56  ? 157 ARG B O   1 
ATOM   3978 C CB  . ARG B 1 160 ? -33.120 -0.465  -1.375  1.00 50.03  ? 157 ARG B CB  1 
ATOM   3979 C CG  . ARG B 1 160 ? -31.730 -0.480  -1.986  1.00 54.13  ? 157 ARG B CG  1 
ATOM   3980 C CD  . ARG B 1 160 ? -30.688 -0.178  -0.900  1.00 65.92  ? 157 ARG B CD  1 
ATOM   3981 N NE  . ARG B 1 160 ? -30.277 1.221   -0.927  1.00 65.98  ? 157 ARG B NE  1 
ATOM   3982 C CZ  . ARG B 1 160 ? -29.087 1.642   -1.337  1.00 60.77  ? 157 ARG B CZ  1 
ATOM   3983 N NH1 . ARG B 1 160 ? -28.128 0.786   -1.667  1.00 53.00  ? 157 ARG B NH1 1 
ATOM   3984 N NH2 . ARG B 1 160 ? -28.856 2.953   -1.423  1.00 57.29  ? 157 ARG B NH2 1 
ATOM   3985 N N   . PRO B 1 161 ? -35.996 -1.977  -1.699  1.00 51.94  ? 158 PRO B N   1 
ATOM   3986 C CA  . PRO B 1 161 ? -37.289 -2.327  -1.093  1.00 45.83  ? 158 PRO B CA  1 
ATOM   3987 C C   . PRO B 1 161 ? -37.388 -1.808  0.332   1.00 44.96  ? 158 PRO B C   1 
ATOM   3988 O O   . PRO B 1 161 ? -36.500 -2.030  1.155   1.00 48.21  ? 158 PRO B O   1 
ATOM   3989 C CB  . PRO B 1 161 ? -37.302 -3.859  -1.147  1.00 41.89  ? 158 PRO B CB  1 
ATOM   3990 C CG  . PRO B 1 161 ? -36.392 -4.216  -2.277  1.00 41.75  ? 158 PRO B CG  1 
ATOM   3991 C CD  . PRO B 1 161 ? -35.336 -3.144  -2.325  1.00 50.43  ? 158 PRO B CD  1 
ATOM   3992 N N   . GLY B 1 162 ? -38.455 -1.070  0.609   1.00 44.11  ? 159 GLY B N   1 
ATOM   3993 C CA  . GLY B 1 162 ? -38.697 -0.522  1.929   1.00 41.72  ? 159 GLY B CA  1 
ATOM   3994 C C   . GLY B 1 162 ? -38.439 0.959   2.071   1.00 48.80  ? 159 GLY B C   1 
ATOM   3995 O O   . GLY B 1 162 ? -38.834 1.540   3.095   1.00 44.93  ? 159 GLY B O   1 
ATOM   3996 N N   . ASP B 1 163 ? -37.794 1.588   1.085   1.00 49.85  ? 160 ASP B N   1 
ATOM   3997 C CA  . ASP B 1 163 ? -37.524 3.019   1.140   1.00 50.73  ? 160 ASP B CA  1 
ATOM   3998 C C   . ASP B 1 163 ? -38.823 3.821   1.217   1.00 47.29  ? 160 ASP B C   1 
ATOM   3999 O O   . ASP B 1 163 ? -39.895 3.355   0.832   1.00 46.97  ? 160 ASP B O   1 
ATOM   4000 C CB  . ASP B 1 163 ? -36.740 3.463   -0.098  1.00 49.80  ? 160 ASP B CB  1 
ATOM   4001 C CG  . ASP B 1 163 ? -35.293 3.004   -0.085  1.00 53.21  ? 160 ASP B CG  1 
ATOM   4002 O OD1 . ASP B 1 163 ? -34.634 3.136   0.977   1.00 47.76  ? 160 ASP B OD1 1 
ATOM   4003 O OD2 . ASP B 1 163 ? -34.821 2.529   -1.152  1.00 51.21  ? 160 ASP B OD2 1 
ATOM   4004 N N   . THR B 1 164 ? -38.718 5.051   1.706   1.00 44.98  ? 161 THR B N   1 
ATOM   4005 C CA  . THR B 1 164 ? -39.758 6.051   1.502   1.00 47.94  ? 161 THR B CA  1 
ATOM   4006 C C   . THR B 1 164 ? -39.267 7.082   0.477   1.00 54.51  ? 161 THR B C   1 
ATOM   4007 O O   . THR B 1 164 ? -38.314 7.830   0.745   1.00 52.38  ? 161 THR B O   1 
ATOM   4008 C CB  . THR B 1 164 ? -40.142 6.726   2.814   1.00 49.94  ? 161 THR B CB  1 
ATOM   4009 O OG1 . THR B 1 164 ? -40.889 5.809   3.618   1.00 58.66  ? 161 THR B OG1 1 
ATOM   4010 C CG2 . THR B 1 164 ? -40.991 7.932   2.537   1.00 52.11  ? 161 THR B CG2 1 
ATOM   4011 N N   . VAL B 1 165 ? -39.914 7.116   -0.694  1.00 49.66  ? 162 VAL B N   1 
ATOM   4012 C CA  . VAL B 1 165 ? -39.560 8.013   -1.795  1.00 48.16  ? 162 VAL B CA  1 
ATOM   4013 C C   . VAL B 1 165 ? -40.564 9.157   -1.846  1.00 45.16  ? 162 VAL B C   1 
ATOM   4014 O O   . VAL B 1 165 ? -41.773 8.921   -1.828  1.00 52.77  ? 162 VAL B O   1 
ATOM   4015 C CB  . VAL B 1 165 ? -39.533 7.268   -3.141  1.00 51.11  ? 162 VAL B CB  1 
ATOM   4016 C CG1 . VAL B 1 165 ? -39.363 8.258   -4.271  1.00 48.06  ? 162 VAL B CG1 1 
ATOM   4017 C CG2 . VAL B 1 165 ? -38.418 6.211   -3.187  1.00 40.84  ? 162 VAL B CG2 1 
ATOM   4018 N N   . VAL B 1 166 ? -40.072 10.390  -1.929  1.00 43.10  ? 163 VAL B N   1 
ATOM   4019 C CA  . VAL B 1 166 ? -40.925 11.577  -2.011  1.00 45.88  ? 163 VAL B CA  1 
ATOM   4020 C C   . VAL B 1 166 ? -40.650 12.299  -3.333  1.00 49.63  ? 163 VAL B C   1 
ATOM   4021 O O   . VAL B 1 166 ? -39.497 12.638  -3.633  1.00 44.09  ? 163 VAL B O   1 
ATOM   4022 C CB  . VAL B 1 166 ? -40.707 12.520  -0.818  1.00 36.51  ? 163 VAL B CB  1 
ATOM   4023 C CG1 . VAL B 1 166 ? -41.393 13.840  -1.055  1.00 34.90  ? 163 VAL B CG1 1 
ATOM   4024 C CG2 . VAL B 1 166 ? -41.244 11.891  0.433   1.00 46.96  ? 163 VAL B CG2 1 
ATOM   4025 N N   . VAL B 1 167 ? -41.704 12.548  -4.115  1.00 47.69  ? 164 VAL B N   1 
ATOM   4026 C CA  . VAL B 1 167 ? -41.593 13.234  -5.406  1.00 46.85  ? 164 VAL B CA  1 
ATOM   4027 C C   . VAL B 1 167 ? -42.396 14.528  -5.350  1.00 43.96  ? 164 VAL B C   1 
ATOM   4028 O O   . VAL B 1 167 ? -43.631 14.488  -5.397  1.00 46.82  ? 164 VAL B O   1 
ATOM   4029 C CB  . VAL B 1 167 ? -42.076 12.354  -6.567  1.00 46.16  ? 164 VAL B CB  1 
ATOM   4030 C CG1 . VAL B 1 167 ? -41.869 13.073  -7.899  1.00 47.70  ? 164 VAL B CG1 1 
ATOM   4031 C CG2 . VAL B 1 167 ? -41.351 11.010  -6.563  1.00 44.95  ? 164 VAL B CG2 1 
ATOM   4032 N N   . SER B 1 168 ? -41.705 15.674  -5.271  1.00 43.84  ? 165 SER B N   1 
ATOM   4033 C CA  . SER B 1 168 ? -42.342 16.974  -5.498  1.00 45.60  ? 165 SER B CA  1 
ATOM   4034 C C   . SER B 1 168 ? -42.571 17.199  -6.995  1.00 45.70  ? 165 SER B C   1 
ATOM   4035 O O   . SER B 1 168 ? -41.715 16.881  -7.822  1.00 44.30  ? 165 SER B O   1 
ATOM   4036 C CB  . SER B 1 168 ? -41.497 18.114  -4.918  1.00 42.58  ? 165 SER B CB  1 
ATOM   4037 O OG  . SER B 1 168 ? -40.230 18.203  -5.549  1.00 41.04  ? 165 SER B OG  1 
ATOM   4038 N N   . GLY B 1 169 ? -43.747 17.733  -7.343  1.00 52.40  ? 166 GLY B N   1 
ATOM   4039 C CA  . GLY B 1 169 ? -44.174 17.809  -8.732  1.00 44.50  ? 166 GLY B CA  1 
ATOM   4040 C C   . GLY B 1 169 ? -44.477 16.458  -9.358  1.00 48.79  ? 166 GLY B C   1 
ATOM   4041 O O   . GLY B 1 169 ? -43.902 16.108  -10.394 1.00 50.36  ? 166 GLY B O   1 
ATOM   4042 N N   . ALA B 1 170 ? -45.402 15.698  -8.764  1.00 49.78  ? 167 ALA B N   1 
ATOM   4043 C CA  . ALA B 1 170 ? -45.625 14.313  -9.165  1.00 46.15  ? 167 ALA B CA  1 
ATOM   4044 C C   . ALA B 1 170 ? -46.651 14.137  -10.280 1.00 54.60  ? 167 ALA B C   1 
ATOM   4045 O O   . ALA B 1 170 ? -46.660 13.065  -10.909 1.00 49.10  ? 167 ALA B O   1 
ATOM   4046 C CB  . ALA B 1 170 ? -46.069 13.486  -7.959  1.00 49.13  ? 167 ALA B CB  1 
ATOM   4047 N N   . SER B 1 171 ? -47.507 15.110  -10.536 1.00 58.14  ? 168 SER B N   1 
ATOM   4048 C CA  . SER B 1 171 ? -48.566 14.941  -11.531 1.00 50.46  ? 168 SER B CA  1 
ATOM   4049 C C   . SER B 1 171 ? -48.067 14.761  -12.953 1.00 54.37  ? 168 SER B C   1 
ATOM   4050 O O   . SER B 1 171 ? -48.642 13.996  -13.705 1.00 46.69  ? 168 SER B O   1 
ATOM   4051 C CB  . SER B 1 171 ? -49.482 16.141  -11.467 1.00 48.54  ? 168 SER B CB  1 
ATOM   4052 O OG  . SER B 1 171 ? -49.634 16.567  -10.136 1.00 58.85  ? 168 SER B OG  1 
ATOM   4053 N N   . GLY B 1 172 ? -47.002 15.462  -13.323 1.00 51.67  ? 169 GLY B N   1 
ATOM   4054 C CA  . GLY B 1 172 ? -46.511 15.406  -14.685 1.00 52.09  ? 169 GLY B CA  1 
ATOM   4055 C C   . GLY B 1 172 ? -45.910 14.064  -15.040 1.00 52.21  ? 169 GLY B C   1 
ATOM   4056 O O   . GLY B 1 172 ? -45.840 13.145  -14.226 1.00 50.36  ? 169 GLY B O   1 
ATOM   4057 N N   . MET B 1 173 ? -45.456 13.957  -16.299 1.00 50.53  ? 170 MET B N   1 
ATOM   4058 C CA  . MET B 1 173 ? -44.912 12.692  -16.781 1.00 48.10  ? 170 MET B CA  1 
ATOM   4059 C C   . MET B 1 173 ? -43.662 12.280  -16.014 1.00 51.33  ? 170 MET B C   1 
ATOM   4060 O O   . MET B 1 173 ? -43.438 11.086  -15.776 1.00 50.91  ? 170 MET B O   1 
ATOM   4061 C CB  . MET B 1 173 ? -44.605 12.761  -18.281 1.00 51.11  ? 170 MET B CB  1 
ATOM   4062 C CG  . MET B 1 173 ? -43.713 11.617  -18.755 1.00 45.49  ? 170 MET B CG  1 
ATOM   4063 S SD  . MET B 1 173 ? -43.655 11.290  -20.517 1.00 59.38  ? 170 MET B SD  1 
ATOM   4064 C CE  . MET B 1 173 ? -45.362 10.835  -20.806 1.00 58.76  ? 170 MET B CE  1 
ATOM   4065 N N   . ILE B 1 174 ? -42.850 13.241  -15.591 1.00 51.86  ? 171 ILE B N   1 
ATOM   4066 C CA  . ILE B 1 174 ? -41.604 12.880  -14.931 1.00 49.38  ? 171 ILE B CA  1 
ATOM   4067 C C   . ILE B 1 174 ? -41.863 12.392  -13.506 1.00 48.44  ? 171 ILE B C   1 
ATOM   4068 O O   . ILE B 1 174 ? -41.387 11.319  -13.120 1.00 45.09  ? 171 ILE B O   1 
ATOM   4069 C CB  . ILE B 1 174 ? -40.610 14.049  -14.991 1.00 47.22  ? 171 ILE B CB  1 
ATOM   4070 C CG1 . ILE B 1 174 ? -39.894 13.997  -16.336 1.00 47.96  ? 171 ILE B CG1 1 
ATOM   4071 C CG2 . ILE B 1 174 ? -39.581 13.952  -13.877 1.00 47.67  ? 171 ILE B CG2 1 
ATOM   4072 C CD1 . ILE B 1 174 ? -39.446 15.321  -16.807 1.00 44.16  ? 171 ILE B CD1 1 
ATOM   4073 N N   . GLY B 1 175 ? -42.628 13.150  -12.711 1.00 44.27  ? 172 GLY B N   1 
ATOM   4074 C CA  . GLY B 1 175 ? -42.962 12.676  -11.368 1.00 53.91  ? 172 GLY B CA  1 
ATOM   4075 C C   . GLY B 1 175 ? -43.700 11.344  -11.378 1.00 52.78  ? 172 GLY B C   1 
ATOM   4076 O O   . GLY B 1 175 ? -43.348 10.411  -10.652 1.00 49.88  ? 172 GLY B O   1 
ATOM   4077 N N   . THR B 1 176 ? -44.727 11.242  -12.223 1.00 51.51  ? 173 THR B N   1 
ATOM   4078 C CA  . THR B 1 176 ? -45.456 9.997   -12.438 1.00 48.60  ? 173 THR B CA  1 
ATOM   4079 C C   . THR B 1 176 ? -44.527 8.845   -12.797 1.00 47.05  ? 173 THR B C   1 
ATOM   4080 O O   . THR B 1 176 ? -44.693 7.726   -12.305 1.00 52.53  ? 173 THR B O   1 
ATOM   4081 C CB  . THR B 1 176 ? -46.507 10.224  -13.541 1.00 52.46  ? 173 THR B CB  1 
ATOM   4082 O OG1 . THR B 1 176 ? -45.844 10.642  -14.745 1.00 50.86  ? 173 THR B OG1 1 
ATOM   4083 C CG2 . THR B 1 176 ? -47.612 11.233  -13.137 1.00 48.93  ? 173 THR B CG2 1 
ATOM   4084 N N   . LEU B 1 177 ? -43.561 9.085   -13.672 1.00 52.09  ? 174 LEU B N   1 
ATOM   4085 C CA  . LEU B 1 177 ? -42.671 8.003   -14.084 1.00 51.35  ? 174 LEU B CA  1 
ATOM   4086 C C   . LEU B 1 177 ? -41.729 7.595   -12.957 1.00 51.55  ? 174 LEU B C   1 
ATOM   4087 O O   . LEU B 1 177 ? -41.452 6.403   -12.769 1.00 47.91  ? 174 LEU B O   1 
ATOM   4088 C CB  . LEU B 1 177 ? -41.870 8.431   -15.304 1.00 47.40  ? 174 LEU B CB  1 
ATOM   4089 C CG  . LEU B 1 177 ? -42.257 7.680   -16.560 1.00 56.39  ? 174 LEU B CG  1 
ATOM   4090 C CD1 . LEU B 1 177 ? -43.681 8.056   -16.989 1.00 62.95  ? 174 LEU B CD1 1 
ATOM   4091 C CD2 . LEU B 1 177 ? -41.242 7.915   -17.680 1.00 59.56  ? 174 LEU B CD2 1 
ATOM   4092 N N   . VAL B 1 178 ? -41.206 8.578   -12.221 1.00 49.11  ? 175 VAL B N   1 
ATOM   4093 C CA  . VAL B 1 178 ? -40.368 8.291   -11.060 1.00 51.72  ? 175 VAL B CA  1 
ATOM   4094 C C   . VAL B 1 178 ? -41.128 7.420   -10.060 1.00 51.25  ? 175 VAL B C   1 
ATOM   4095 O O   . VAL B 1 178 ? -40.642 6.362   -9.644  1.00 47.05  ? 175 VAL B O   1 
ATOM   4096 C CB  . VAL B 1 178 ? -39.863 9.604   -10.424 1.00 45.90  ? 175 VAL B CB  1 
ATOM   4097 C CG1 . VAL B 1 178 ? -39.277 9.359   -9.053  1.00 48.09  ? 175 VAL B CG1 1 
ATOM   4098 C CG2 . VAL B 1 178 ? -38.810 10.246  -11.301 1.00 38.87  ? 175 VAL B CG2 1 
ATOM   4099 N N   . GLY B 1 179 ? -42.338 7.843   -9.676  1.00 50.97  ? 176 GLY B N   1 
ATOM   4100 C CA  . GLY B 1 179 ? -43.086 7.101   -8.669  1.00 46.37  ? 176 GLY B CA  1 
ATOM   4101 C C   . GLY B 1 179 ? -43.291 5.647   -9.051  1.00 47.58  ? 176 GLY B C   1 
ATOM   4102 O O   . GLY B 1 179 ? -43.070 4.739   -8.252  1.00 51.27  ? 176 GLY B O   1 
ATOM   4103 N N   . GLN B 1 180 ? -43.691 5.406   -10.290 1.00 49.50  ? 177 GLN B N   1 
ATOM   4104 C CA  . GLN B 1 180 ? -43.985 4.043   -10.714 1.00 52.83  ? 177 GLN B CA  1 
ATOM   4105 C C   . GLN B 1 180 ? -42.735 3.167   -10.720 1.00 50.99  ? 177 GLN B C   1 
ATOM   4106 O O   . GLN B 1 180 ? -42.815 1.971   -10.429 1.00 58.62  ? 177 GLN B O   1 
ATOM   4107 C CB  . GLN B 1 180 ? -44.635 4.061   -12.100 1.00 52.81  ? 177 GLN B CB  1 
ATOM   4108 C CG  . GLN B 1 180 ? -46.152 4.216   -12.115 1.00 50.79  ? 177 GLN B CG  1 
ATOM   4109 C CD  . GLN B 1 180 ? -46.676 4.422   -13.525 1.00 61.53  ? 177 GLN B CD  1 
ATOM   4110 O OE1 . GLN B 1 180 ? -46.686 3.500   -14.350 1.00 58.75  ? 177 GLN B OE1 1 
ATOM   4111 N NE2 . GLN B 1 180 ? -47.087 5.648   -13.821 1.00 65.49  ? 177 GLN B NE2 1 
ATOM   4112 N N   . MET B 1 181 ? -41.579 3.724   -11.080 1.00 49.53  ? 178 MET B N   1 
ATOM   4113 C CA  . MET B 1 181 ? -40.352 2.937   -11.023 1.00 51.26  ? 178 MET B CA  1 
ATOM   4114 C C   . MET B 1 181 ? -39.905 2.724   -9.579  1.00 48.29  ? 178 MET B C   1 
ATOM   4115 O O   . MET B 1 181 ? -39.374 1.662   -9.240  1.00 46.12  ? 178 MET B O   1 
ATOM   4116 C CB  . MET B 1 181 ? -39.251 3.623   -11.824 1.00 44.45  ? 178 MET B CB  1 
ATOM   4117 C CG  . MET B 1 181 ? -39.264 3.318   -13.295 1.00 46.42  ? 178 MET B CG  1 
ATOM   4118 S SD  . MET B 1 181 ? -38.070 4.358   -14.149 1.00 56.08  ? 178 MET B SD  1 
ATOM   4119 C CE  . MET B 1 181 ? -38.537 5.953   -13.470 1.00 43.46  ? 178 MET B CE  1 
ATOM   4120 N N   . ALA B 1 182 ? -40.096 3.741   -8.730  1.00 44.07  ? 179 ALA B N   1 
ATOM   4121 C CA  . ALA B 1 182 ? -39.813 3.619   -7.308  1.00 41.73  ? 179 ALA B CA  1 
ATOM   4122 C C   . ALA B 1 182 ? -40.695 2.559   -6.670  1.00 56.24  ? 179 ALA B C   1 
ATOM   4123 O O   . ALA B 1 182 ? -40.237 1.769   -5.832  1.00 53.10  ? 179 ALA B O   1 
ATOM   4124 C CB  . ALA B 1 182 ? -40.031 4.965   -6.621  1.00 40.76  ? 179 ALA B CB  1 
ATOM   4125 N N   . LYS B 1 183 ? -41.968 2.526   -7.058  1.00 54.53  ? 180 LYS B N   1 
ATOM   4126 C CA  . LYS B 1 183 ? -42.860 1.515   -6.520  1.00 52.44  ? 180 LYS B CA  1 
ATOM   4127 C C   . LYS B 1 183 ? -42.438 0.114   -6.954  1.00 50.73  ? 180 LYS B C   1 
ATOM   4128 O O   . LYS B 1 183 ? -42.503 -0.827  -6.155  1.00 49.06  ? 180 LYS B O   1 
ATOM   4129 C CB  . LYS B 1 183 ? -44.290 1.817   -6.936  1.00 51.11  ? 180 LYS B CB  1 
ATOM   4130 C CG  . LYS B 1 183 ? -45.271 0.890   -6.301  1.00 52.07  ? 180 LYS B CG  1 
ATOM   4131 C CD  . LYS B 1 183 ? -45.134 0.907   -4.807  1.00 50.44  ? 180 LYS B CD  1 
ATOM   4132 C CE  . LYS B 1 183 ? -45.816 2.126   -4.247  1.00 54.81  ? 180 LYS B CE  1 
ATOM   4133 N NZ  . LYS B 1 183 ? -46.180 1.861   -2.835  1.00 55.30  ? 180 LYS B NZ  1 
ATOM   4134 N N   . ARG B 1 184 ? -41.970 -0.042  -8.198  1.00 49.58  ? 181 ARG B N   1 
ATOM   4135 C CA  . ARG B 1 184 ? -41.516 -1.352  -8.675  1.00 51.93  ? 181 ARG B CA  1 
ATOM   4136 C C   . ARG B 1 184 ? -40.262 -1.840  -7.953  1.00 54.24  ? 181 ARG B C   1 
ATOM   4137 O O   . ARG B 1 184 ? -39.994 -3.050  -7.944  1.00 50.19  ? 181 ARG B O   1 
ATOM   4138 C CB  . ARG B 1 184 ? -41.247 -1.322  -10.185 1.00 49.26  ? 181 ARG B CB  1 
ATOM   4139 C CG  . ARG B 1 184 ? -42.481 -1.094  -11.052 1.00 59.96  ? 181 ARG B CG  1 
ATOM   4140 C CD  . ARG B 1 184 ? -42.105 -0.873  -12.524 1.00 62.77  ? 181 ARG B CD  1 
ATOM   4141 N NE  . ARG B 1 184 ? -41.222 -1.920  -13.024 1.00 62.49  ? 181 ARG B NE  1 
ATOM   4142 C CZ  . ARG B 1 184 ? -41.644 -3.072  -13.528 1.00 68.91  ? 181 ARG B CZ  1 
ATOM   4143 N NH1 . ARG B 1 184 ? -42.937 -3.342  -13.646 1.00 70.54  ? 181 ARG B NH1 1 
ATOM   4144 N NH2 . ARG B 1 184 ? -40.749 -3.975  -13.923 1.00 60.65  ? 181 ARG B NH2 1 
ATOM   4145 N N   . ALA B 1 185 ? -39.479 -0.932  -7.369  1.00 49.84  ? 182 ALA B N   1 
ATOM   4146 C CA  . ALA B 1 185 ? -38.331 -1.305  -6.553  1.00 55.15  ? 182 ALA B CA  1 
ATOM   4147 C C   . ALA B 1 185 ? -38.705 -1.527  -5.089  1.00 56.42  ? 182 ALA B C   1 
ATOM   4148 O O   . ALA B 1 185 ? -37.827 -1.811  -4.271  1.00 54.85  ? 182 ALA B O   1 
ATOM   4149 C CB  . ALA B 1 185 ? -37.226 -0.240  -6.662  1.00 45.57  ? 182 ALA B CB  1 
ATOM   4150 N N   . GLY B 1 186 ? -39.979 -1.404  -4.741  1.00 46.47  ? 183 GLY B N   1 
ATOM   4151 C CA  . GLY B 1 186 ? -40.429 -1.716  -3.416  1.00 40.30  ? 183 GLY B CA  1 
ATOM   4152 C C   . GLY B 1 186 ? -40.687 -0.523  -2.541  1.00 45.66  ? 183 GLY B C   1 
ATOM   4153 O O   . GLY B 1 186 ? -41.025 -0.701  -1.370  1.00 51.62  ? 183 GLY B O   1 
ATOM   4154 N N   . ALA B 1 187 ? -40.573 0.683   -3.064  1.00 51.27  ? 184 ALA B N   1 
ATOM   4155 C CA  . ALA B 1 187 ? -40.631 1.830   -2.173  1.00 52.73  ? 184 ALA B CA  1 
ATOM   4156 C C   . ALA B 1 187 ? -42.066 2.196   -1.804  1.00 47.48  ? 184 ALA B C   1 
ATOM   4157 O O   . ALA B 1 187 ? -43.038 1.797   -2.449  1.00 47.55  ? 184 ALA B O   1 
ATOM   4158 C CB  . ALA B 1 187 ? -39.949 3.047   -2.807  1.00 53.92  ? 184 ALA B CB  1 
ATOM   4159 N N   . ARG B 1 188 ? -42.179 2.978   -0.743  1.00 42.05  ? 185 ARG B N   1 
ATOM   4160 C CA  . ARG B 1 188 ? -43.390 3.727   -0.462  1.00 47.42  ? 185 ARG B CA  1 
ATOM   4161 C C   . ARG B 1 188 ? -43.241 5.084   -1.142  1.00 54.17  ? 185 ARG B C   1 
ATOM   4162 O O   . ARG B 1 188 ? -42.362 5.873   -0.779  1.00 51.41  ? 185 ARG B O   1 
ATOM   4163 C CB  . ARG B 1 188 ? -43.599 3.869   1.041   1.00 41.33  ? 185 ARG B CB  1 
ATOM   4164 C CG  . ARG B 1 188 ? -44.541 4.969   1.424   1.00 43.73  ? 185 ARG B CG  1 
ATOM   4165 C CD  . ARG B 1 188 ? -44.496 5.187   2.913   1.00 43.46  ? 185 ARG B CD  1 
ATOM   4166 N NE  . ARG B 1 188 ? -45.510 6.140   3.343   1.00 50.77  ? 185 ARG B NE  1 
ATOM   4167 C CZ  . ARG B 1 188 ? -46.803 5.859   3.454   1.00 51.93  ? 185 ARG B CZ  1 
ATOM   4168 N NH1 . ARG B 1 188 ? -47.275 4.647   3.190   1.00 48.51  ? 185 ARG B NH1 1 
ATOM   4169 N NH2 . ARG B 1 188 ? -47.644 6.823   3.824   1.00 53.47  ? 185 ARG B NH2 1 
ATOM   4170 N N   . VAL B 1 189 ? -44.081 5.352   -2.137  1.00 51.90  ? 186 VAL B N   1 
ATOM   4171 C CA  . VAL B 1 189 ? -43.963 6.549   -2.958  1.00 51.39  ? 186 VAL B CA  1 
ATOM   4172 C C   . VAL B 1 189 ? -44.973 7.589   -2.481  1.00 53.68  ? 186 VAL B C   1 
ATOM   4173 O O   . VAL B 1 189 ? -46.183 7.349   -2.506  1.00 56.46  ? 186 VAL B O   1 
ATOM   4174 C CB  . VAL B 1 189 ? -44.171 6.222   -4.441  1.00 52.75  ? 186 VAL B CB  1 
ATOM   4175 C CG1 . VAL B 1 189 ? -43.994 7.473   -5.258  1.00 54.30  ? 186 VAL B CG1 1 
ATOM   4176 C CG2 . VAL B 1 189 ? -43.229 5.090   -4.888  1.00 50.91  ? 186 VAL B CG2 1 
ATOM   4177 N N   . VAL B 1 190 ? -44.487 8.746   -2.052  1.00 49.69  ? 187 VAL B N   1 
ATOM   4178 C CA  . VAL B 1 190 ? -45.331 9.880   -1.709  1.00 47.18  ? 187 VAL B CA  1 
ATOM   4179 C C   . VAL B 1 190 ? -45.102 10.979  -2.740  1.00 52.98  ? 187 VAL B C   1 
ATOM   4180 O O   . VAL B 1 190 ? -43.978 11.166  -3.219  1.00 49.51  ? 187 VAL B O   1 
ATOM   4181 C CB  . VAL B 1 190 ? -45.024 10.364  -0.286  1.00 45.76  ? 187 VAL B CB  1 
ATOM   4182 C CG1 . VAL B 1 190 ? -46.001 11.432  0.129   1.00 47.80  ? 187 VAL B CG1 1 
ATOM   4183 C CG2 . VAL B 1 190 ? -45.074 9.186   0.657   1.00 50.73  ? 187 VAL B CG2 1 
ATOM   4184 N N   . GLY B 1 191 ? -46.172 11.695  -3.099  1.00 60.08  ? 188 GLY B N   1 
ATOM   4185 C CA  . GLY B 1 191 ? -46.102 12.745  -4.097  1.00 55.03  ? 188 GLY B CA  1 
ATOM   4186 C C   . GLY B 1 191 ? -46.778 14.032  -3.642  1.00 52.58  ? 188 GLY B C   1 
ATOM   4187 O O   . GLY B 1 191 ? -47.268 14.143  -2.517  1.00 48.99  ? 188 GLY B O   1 
ATOM   4188 N N   . THR B 1 192 ? -46.762 15.015  -4.541  1.00 60.34  ? 189 THR B N   1 
ATOM   4189 C CA  . THR B 1 192 ? -47.661 16.158  -4.448  1.00 61.73  ? 189 THR B CA  1 
ATOM   4190 C C   . THR B 1 192 ? -48.378 16.313  -5.780  1.00 59.71  ? 189 THR B C   1 
ATOM   4191 O O   . THR B 1 192 ? -47.881 15.872  -6.821  1.00 57.27  ? 189 THR B O   1 
ATOM   4192 C CB  . THR B 1 192 ? -46.948 17.471  -4.082  1.00 58.82  ? 189 THR B CB  1 
ATOM   4193 O OG1 . THR B 1 192 ? -46.095 17.882  -5.161  1.00 61.03  ? 189 THR B OG1 1 
ATOM   4194 C CG2 . THR B 1 192 ? -46.135 17.292  -2.811  1.00 49.05  ? 189 THR B CG2 1 
ATOM   4195 N N   . ALA B 1 193 ? -49.579 16.896  -5.717  1.00 65.61  ? 190 ALA B N   1 
ATOM   4196 C CA  . ALA B 1 193 ? -50.368 17.250  -6.893  1.00 62.29  ? 190 ALA B CA  1 
ATOM   4197 C C   . ALA B 1 193 ? -51.255 18.433  -6.521  1.00 55.00  ? 190 ALA B C   1 
ATOM   4198 O O   . ALA B 1 193 ? -51.278 18.878  -5.371  1.00 57.23  ? 190 ALA B O   1 
ATOM   4199 C CB  . ALA B 1 193 ? -51.182 16.056  -7.419  1.00 55.57  ? 190 ALA B CB  1 
ATOM   4200 N N   . GLY B 1 194 ? -51.978 18.956  -7.511  1.00 62.46  ? 191 GLY B N   1 
ATOM   4201 C CA  . GLY B 1 194 ? -52.657 20.233  -7.346  1.00 63.24  ? 191 GLY B CA  1 
ATOM   4202 C C   . GLY B 1 194 ? -54.158 20.175  -7.162  1.00 60.71  ? 191 GLY B C   1 
ATOM   4203 O O   . GLY B 1 194 ? -54.794 21.166  -6.785  1.00 55.79  ? 191 GLY B O   1 
ATOM   4204 N N   . SER B 1 195 ? -54.736 19.017  -7.422  1.00 55.87  ? 192 SER B N   1 
ATOM   4205 C CA  . SER B 1 195 ? -56.178 18.873  -7.375  1.00 68.52  ? 192 SER B CA  1 
ATOM   4206 C C   . SER B 1 195 ? -56.559 17.796  -6.358  1.00 72.56  ? 192 SER B C   1 
ATOM   4207 O O   . SER B 1 195 ? -55.744 17.351  -5.535  1.00 65.89  ? 192 SER B O   1 
ATOM   4208 C CB  . SER B 1 195 ? -56.702 18.537  -8.771  1.00 56.37  ? 192 SER B CB  1 
ATOM   4209 O OG  . SER B 1 195 ? -56.197 17.278  -9.159  1.00 55.72  ? 192 SER B OG  1 
ATOM   4210 N N   . ALA B 1 196 ? -57.828 17.400  -6.402  1.00 66.47  ? 193 ALA B N   1 
ATOM   4211 C CA  . ALA B 1 196 ? -58.214 16.087  -5.916  1.00 62.85  ? 193 ALA B CA  1 
ATOM   4212 C C   . ALA B 1 196 ? -58.236 15.067  -7.047  1.00 66.91  ? 193 ALA B C   1 
ATOM   4213 O O   . ALA B 1 196 ? -57.932 13.884  -6.820  1.00 59.74  ? 193 ALA B O   1 
ATOM   4214 C CB  . ALA B 1 196 ? -59.581 16.157  -5.238  1.00 55.50  ? 193 ALA B CB  1 
ATOM   4215 N N   . GLY B 1 197 ? -58.553 15.520  -8.268  1.00 62.83  ? 194 GLY B N   1 
ATOM   4216 C CA  . GLY B 1 197 ? -58.664 14.610  -9.396  1.00 62.98  ? 194 GLY B CA  1 
ATOM   4217 C C   . GLY B 1 197 ? -57.333 14.044  -9.847  1.00 68.45  ? 194 GLY B C   1 
ATOM   4218 O O   . GLY B 1 197 ? -57.275 12.919  -10.358 1.00 63.28  ? 194 GLY B O   1 
ATOM   4219 N N   . LYS B 1 198 ? -56.251 14.817  -9.690  1.00 72.40  ? 195 LYS B N   1 
ATOM   4220 C CA  . LYS B 1 198 ? -54.927 14.303  -10.029 1.00 68.47  ? 195 LYS B CA  1 
ATOM   4221 C C   . LYS B 1 198 ? -54.364 13.505  -8.867  1.00 63.00  ? 195 LYS B C   1 
ATOM   4222 O O   . LYS B 1 198 ? -53.749 12.454  -9.077  1.00 59.48  ? 195 LYS B O   1 
ATOM   4223 C CB  . LYS B 1 198 ? -53.979 15.449  -10.420 1.00 64.25  ? 195 LYS B CB  1 
ATOM   4224 C CG  . LYS B 1 198 ? -53.842 15.692  -11.934 1.00 56.34  ? 195 LYS B CG  1 
ATOM   4225 C CD  . LYS B 1 198 ? -53.310 17.083  -12.203 1.00 55.86  ? 195 LYS B CD  1 
ATOM   4226 C CE  . LYS B 1 198 ? -52.914 17.276  -13.654 1.00 60.86  ? 195 LYS B CE  1 
ATOM   4227 N NZ  . LYS B 1 198 ? -51.483 16.921  -13.930 1.00 59.55  ? 195 LYS B NZ  1 
ATOM   4228 N N   . ALA B 1 199 ? -54.586 13.998  -7.643  1.00 63.32  ? 196 ALA B N   1 
ATOM   4229 C CA  . ALA B 1 199 ? -54.289 13.229  -6.439  1.00 61.31  ? 196 ALA B CA  1 
ATOM   4230 C C   . ALA B 1 199 ? -54.833 11.810  -6.542  1.00 63.82  ? 196 ALA B C   1 
ATOM   4231 O O   . ALA B 1 199 ? -54.144 10.842  -6.194  1.00 60.48  ? 196 ALA B O   1 
ATOM   4232 C CB  . ALA B 1 199 ? -54.876 13.942  -5.220  1.00 51.05  ? 196 ALA B CB  1 
ATOM   4233 N N   . ARG B 1 200 ? -56.069 11.669  -7.034  1.00 62.01  ? 197 ARG B N   1 
ATOM   4234 C CA  . ARG B 1 200 ? -56.681 10.356  -7.225  1.00 65.53  ? 197 ARG B CA  1 
ATOM   4235 C C   . ARG B 1 200 ? -56.128 9.637   -8.451  1.00 64.61  ? 197 ARG B C   1 
ATOM   4236 O O   . ARG B 1 200 ? -56.131 8.398   -8.491  1.00 61.10  ? 197 ARG B O   1 
ATOM   4237 C CB  . ARG B 1 200 ? -58.206 10.509  -7.321  1.00 67.17  ? 197 ARG B CB  1 
ATOM   4238 C CG  . ARG B 1 200 ? -58.973 9.316   -7.924  1.00 69.37  ? 197 ARG B CG  1 
ATOM   4239 C CD  . ARG B 1 200 ? -60.496 9.569   -8.009  1.00 72.64  ? 197 ARG B CD  1 
ATOM   4240 N NE  . ARG B 1 200 ? -60.840 10.902  -8.503  1.00 75.29  ? 197 ARG B NE  1 
ATOM   4241 C CZ  . ARG B 1 200 ? -61.175 11.929  -7.728  1.00 71.72  ? 197 ARG B CZ  1 
ATOM   4242 N NH1 . ARG B 1 200 ? -61.235 11.810  -6.409  1.00 59.95  ? 197 ARG B NH1 1 
ATOM   4243 N NH2 . ARG B 1 200 ? -61.452 13.108  -8.288  1.00 65.36  ? 197 ARG B NH2 1 
ATOM   4244 N N   . TYR B 1 201 ? -55.657 10.398  -9.452  1.00 67.18  ? 198 TYR B N   1 
ATOM   4245 C CA  . TYR B 1 201 ? -54.991 9.804   -10.610 1.00 61.68  ? 198 TYR B CA  1 
ATOM   4246 C C   . TYR B 1 201 ? -53.651 9.183   -10.212 1.00 64.79  ? 198 TYR B C   1 
ATOM   4247 O O   . TYR B 1 201 ? -53.299 8.095   -10.687 1.00 62.70  ? 198 TYR B O   1 
ATOM   4248 C CB  . TYR B 1 201 ? -54.815 10.863  -11.715 1.00 57.63  ? 198 TYR B CB  1 
ATOM   4249 C CG  . TYR B 1 201 ? -53.915 10.449  -12.889 1.00 59.67  ? 198 TYR B CG  1 
ATOM   4250 C CD1 . TYR B 1 201 ? -54.338 9.515   -13.830 1.00 60.26  ? 198 TYR B CD1 1 
ATOM   4251 C CD2 . TYR B 1 201 ? -52.645 11.004  -13.058 1.00 58.32  ? 198 TYR B CD2 1 
ATOM   4252 C CE1 . TYR B 1 201 ? -53.517 9.132   -14.895 1.00 59.16  ? 198 TYR B CE1 1 
ATOM   4253 C CE2 . TYR B 1 201 ? -51.821 10.626  -14.118 1.00 56.28  ? 198 TYR B CE2 1 
ATOM   4254 C CZ  . TYR B 1 201 ? -52.264 9.691   -15.033 1.00 60.96  ? 198 TYR B CZ  1 
ATOM   4255 O OH  . TYR B 1 201 ? -51.458 9.309   -16.091 1.00 61.80  ? 198 TYR B OH  1 
ATOM   4256 N N   . LEU B 1 202 ? -52.897 9.849   -9.325  1.00 59.23  ? 199 LEU B N   1 
ATOM   4257 C CA  . LEU B 1 202 ? -51.610 9.317   -8.888  1.00 55.52  ? 199 LEU B CA  1 
ATOM   4258 C C   . LEU B 1 202 ? -51.788 8.088   -8.008  1.00 58.96  ? 199 LEU B C   1 
ATOM   4259 O O   . LEU B 1 202 ? -51.162 7.048   -8.240  1.00 59.60  ? 199 LEU B O   1 
ATOM   4260 C CB  . LEU B 1 202 ? -50.837 10.391  -8.135  1.00 59.00  ? 199 LEU B CB  1 
ATOM   4261 C CG  . LEU B 1 202 ? -50.220 11.501  -8.976  1.00 57.46  ? 199 LEU B CG  1 
ATOM   4262 C CD1 . LEU B 1 202 ? -49.651 12.596  -8.064  1.00 53.45  ? 199 LEU B CD1 1 
ATOM   4263 C CD2 . LEU B 1 202 ? -49.160 10.909  -9.893  1.00 53.03  ? 199 LEU B CD2 1 
ATOM   4264 N N   . SER B 1 203 ? -52.616 8.207   -6.969  1.00 62.92  ? 200 SER B N   1 
ATOM   4265 C CA  . SER B 1 203 ? -52.948 7.062   -6.128  1.00 59.13  ? 200 SER B CA  1 
ATOM   4266 C C   . SER B 1 203 ? -53.324 5.856   -6.971  1.00 59.56  ? 200 SER B C   1 
ATOM   4267 O O   . SER B 1 203 ? -52.726 4.780   -6.848  1.00 57.38  ? 200 SER B O   1 
ATOM   4268 C CB  . SER B 1 203 ? -54.092 7.430   -5.189  1.00 51.47  ? 200 SER B CB  1 
ATOM   4269 O OG  . SER B 1 203 ? -54.014 8.796   -4.835  1.00 56.41  ? 200 SER B OG  1 
ATOM   4270 N N   . GLN B 1 204 ? -54.303 6.031   -7.859  1.00 60.28  ? 201 GLN B N   1 
ATOM   4271 C CA  . GLN B 1 204 ? -54.709 4.948   -8.744  1.00 64.45  ? 201 GLN B CA  1 
ATOM   4272 C C   . GLN B 1 204 ? -53.550 4.452   -9.596  1.00 65.81  ? 201 GLN B C   1 
ATOM   4273 O O   . GLN B 1 204 ? -53.616 3.336   -10.121 1.00 67.06  ? 201 GLN B O   1 
ATOM   4274 C CB  . GLN B 1 204 ? -55.878 5.406   -9.627  1.00 73.78  ? 201 GLN B CB  1 
ATOM   4275 C CG  . GLN B 1 204 ? -56.729 4.267   -10.233 1.00 81.27  ? 201 GLN B CG  1 
ATOM   4276 C CD  . GLN B 1 204 ? -58.212 4.629   -10.342 1.00 79.12  ? 201 GLN B CD  1 
ATOM   4277 O OE1 . GLN B 1 204 ? -58.740 5.376   -9.505  1.00 76.79  ? 201 GLN B OE1 1 
ATOM   4278 N NE2 . GLN B 1 204 ? -58.889 4.102   -11.369 1.00 69.06  ? 201 GLN B NE2 1 
ATOM   4279 N N   . LEU B 1 205 ? -52.490 5.254   -9.743  1.00 66.88  ? 202 LEU B N   1 
ATOM   4280 C CA  . LEU B 1 205 ? -51.279 4.789   -10.405 1.00 63.61  ? 202 LEU B CA  1 
ATOM   4281 C C   . LEU B 1 205 ? -50.354 4.044   -9.456  1.00 63.54  ? 202 LEU B C   1 
ATOM   4282 O O   . LEU B 1 205 ? -49.378 3.447   -9.918  1.00 62.12  ? 202 LEU B O   1 
ATOM   4283 C CB  . LEU B 1 205 ? -50.536 5.966   -11.054 1.00 62.75  ? 202 LEU B CB  1 
ATOM   4284 C CG  . LEU B 1 205 ? -50.967 6.246   -12.499 1.00 61.91  ? 202 LEU B CG  1 
ATOM   4285 C CD1 . LEU B 1 205 ? -50.223 7.403   -13.142 1.00 56.55  ? 202 LEU B CD1 1 
ATOM   4286 C CD2 . LEU B 1 205 ? -50.765 4.984   -13.289 1.00 64.15  ? 202 LEU B CD2 1 
ATOM   4287 N N   . GLY B 1 206 ? -50.647 4.048   -8.157  1.00 65.80  ? 203 GLY B N   1 
ATOM   4288 C CA  . GLY B 1 206 ? -49.877 3.298   -7.175  1.00 65.71  ? 203 GLY B CA  1 
ATOM   4289 C C   . GLY B 1 206 ? -49.217 4.136   -6.086  1.00 65.10  ? 203 GLY B C   1 
ATOM   4290 O O   . GLY B 1 206 ? -48.494 3.565   -5.253  1.00 53.91  ? 203 GLY B O   1 
ATOM   4291 N N   . PHE B 1 207 ? -49.411 5.461   -6.065  1.00 59.85  ? 204 PHE B N   1 
ATOM   4292 C CA  . PHE B 1 207 ? -48.888 6.287   -4.981  1.00 54.35  ? 204 PHE B CA  1 
ATOM   4293 C C   . PHE B 1 207 ? -49.565 5.903   -3.668  1.00 53.61  ? 204 PHE B C   1 
ATOM   4294 O O   . PHE B 1 207 ? -50.750 5.574   -3.635  1.00 60.64  ? 204 PHE B O   1 
ATOM   4295 C CB  . PHE B 1 207 ? -49.115 7.780   -5.288  1.00 57.63  ? 204 PHE B CB  1 
ATOM   4296 C CG  . PHE B 1 207 ? -48.049 8.410   -6.178  1.00 59.41  ? 204 PHE B CG  1 
ATOM   4297 C CD1 . PHE B 1 207 ? -47.665 7.811   -7.383  1.00 57.27  ? 204 PHE B CD1 1 
ATOM   4298 C CD2 . PHE B 1 207 ? -47.448 9.616   -5.822  1.00 58.01  ? 204 PHE B CD2 1 
ATOM   4299 C CE1 . PHE B 1 207 ? -46.690 8.386   -8.196  1.00 49.65  ? 204 PHE B CE1 1 
ATOM   4300 C CE2 . PHE B 1 207 ? -46.475 10.196  -6.635  1.00 57.60  ? 204 PHE B CE2 1 
ATOM   4301 C CZ  . PHE B 1 207 ? -46.096 9.575   -7.822  1.00 50.79  ? 204 PHE B CZ  1 
ATOM   4302 N N   . ASP B 1 208 ? -48.808 5.931   -2.579  1.00 56.22  ? 205 ASP B N   1 
ATOM   4303 C CA  . ASP B 1 208 ? -49.363 5.586   -1.274  1.00 53.41  ? 205 ASP B CA  1 
ATOM   4304 C C   . ASP B 1 208 ? -49.880 6.787   -0.519  1.00 51.56  ? 205 ASP B C   1 
ATOM   4305 O O   . ASP B 1 208 ? -50.730 6.617   0.358   1.00 61.14  ? 205 ASP B O   1 
ATOM   4306 C CB  . ASP B 1 208 ? -48.318 4.876   -0.422  1.00 44.78  ? 205 ASP B CB  1 
ATOM   4307 C CG  . ASP B 1 208 ? -47.582 3.826   -1.206  1.00 52.48  ? 205 ASP B CG  1 
ATOM   4308 O OD1 . ASP B 1 208 ? -48.214 2.833   -1.641  1.00 52.36  ? 205 ASP B OD1 1 
ATOM   4309 O OD2 . ASP B 1 208 ? -46.375 4.018   -1.447  1.00 53.45  ? 205 ASP B OD2 1 
ATOM   4310 N N   . ALA B 1 209 ? -49.383 7.982   -0.833  1.00 47.22  ? 206 ALA B N   1 
ATOM   4311 C CA  . ALA B 1 209 ? -49.913 9.231   -0.312  1.00 46.29  ? 206 ALA B CA  1 
ATOM   4312 C C   . ALA B 1 209 ? -49.694 10.305  -1.365  1.00 51.17  ? 206 ALA B C   1 
ATOM   4313 O O   . ALA B 1 209 ? -48.795 10.189  -2.203  1.00 49.44  ? 206 ALA B O   1 
ATOM   4314 C CB  . ALA B 1 209 ? -49.252 9.631   1.013   1.00 42.44  ? 206 ALA B CB  1 
ATOM   4315 N N   . VAL B 1 210 ? -50.557 11.325  -1.348  1.00 53.40  ? 207 VAL B N   1 
ATOM   4316 C CA  . VAL B 1 210 ? -50.418 12.502  -2.204  1.00 48.90  ? 207 VAL B CA  1 
ATOM   4317 C C   . VAL B 1 210 ? -50.806 13.739  -1.406  1.00 46.03  ? 207 VAL B C   1 
ATOM   4318 O O   . VAL B 1 210 ? -51.991 13.972  -1.173  1.00 46.55  ? 207 VAL B O   1 
ATOM   4319 C CB  . VAL B 1 210 ? -51.274 12.414  -3.491  1.00 52.69  ? 207 VAL B CB  1 
ATOM   4320 C CG1 . VAL B 1 210 ? -50.825 13.466  -4.508  1.00 59.20  ? 207 VAL B CG1 1 
ATOM   4321 C CG2 . VAL B 1 210 ? -51.229 11.038  -4.139  1.00 53.87  ? 207 VAL B CG2 1 
ATOM   4322 N N   . ILE B 1 211 ? -49.817 14.533  -0.976  1.00 51.31  ? 208 ILE B N   1 
ATOM   4323 C CA  . ILE B 1 211 ? -50.086 15.839  -0.371  1.00 51.74  ? 208 ILE B CA  1 
ATOM   4324 C C   . ILE B 1 211 ? -50.645 16.796  -1.416  1.00 56.07  ? 208 ILE B C   1 
ATOM   4325 O O   . ILE B 1 211 ? -50.270 16.747  -2.593  1.00 61.45  ? 208 ILE B O   1 
ATOM   4326 C CB  . ILE B 1 211 ? -48.808 16.428  0.256   1.00 55.04  ? 208 ILE B CB  1 
ATOM   4327 C CG1 . ILE B 1 211 ? -48.371 15.636  1.492   1.00 58.76  ? 208 ILE B CG1 1 
ATOM   4328 C CG2 . ILE B 1 211 ? -48.990 17.899  0.609   1.00 53.15  ? 208 ILE B CG2 1 
ATOM   4329 C CD1 . ILE B 1 211 ? -47.513 14.432  1.176   1.00 53.30  ? 208 ILE B CD1 1 
ATOM   4330 N N   . ASP B 1 212 ? -51.550 17.677  -0.996  1.00 64.05  ? 209 ASP B N   1 
ATOM   4331 C CA  . ASP B 1 212 ? -52.041 18.755  -1.851  1.00 65.86  ? 209 ASP B CA  1 
ATOM   4332 C C   . ASP B 1 212 ? -51.201 19.999  -1.567  1.00 63.96  ? 209 ASP B C   1 
ATOM   4333 O O   . ASP B 1 212 ? -51.292 20.582  -0.480  1.00 54.15  ? 209 ASP B O   1 
ATOM   4334 C CB  . ASP B 1 212 ? -53.531 18.994  -1.603  1.00 72.01  ? 209 ASP B CB  1 
ATOM   4335 C CG  . ASP B 1 212 ? -54.081 20.201  -2.359  1.00 70.90  ? 209 ASP B CG  1 
ATOM   4336 O OD1 . ASP B 1 212 ? -53.739 21.337  -1.970  1.00 71.80  ? 209 ASP B OD1 1 
ATOM   4337 O OD2 . ASP B 1 212 ? -54.863 20.015  -3.327  1.00 66.24  ? 209 ASP B OD2 1 
ATOM   4338 N N   . TYR B 1 213 ? -50.385 20.409  -2.552  1.00 64.32  ? 210 TYR B N   1 
ATOM   4339 C CA  . TYR B 1 213 ? -49.415 21.477  -2.316  1.00 64.65  ? 210 TYR B CA  1 
ATOM   4340 C C   . TYR B 1 213 ? -50.067 22.844  -2.192  1.00 62.46  ? 210 TYR B C   1 
ATOM   4341 O O   . TYR B 1 213 ? -49.416 23.784  -1.723  1.00 60.05  ? 210 TYR B O   1 
ATOM   4342 C CB  . TYR B 1 213 ? -48.341 21.514  -3.418  1.00 60.53  ? 210 TYR B CB  1 
ATOM   4343 C CG  . TYR B 1 213 ? -48.810 21.845  -4.826  1.00 58.90  ? 210 TYR B CG  1 
ATOM   4344 C CD1 . TYR B 1 213 ? -48.945 23.162  -5.252  1.00 51.98  ? 210 TYR B CD1 1 
ATOM   4345 C CD2 . TYR B 1 213 ? -49.068 20.833  -5.748  1.00 57.60  ? 210 TYR B CD2 1 
ATOM   4346 C CE1 . TYR B 1 213 ? -49.362 23.460  -6.549  1.00 56.02  ? 210 TYR B CE1 1 
ATOM   4347 C CE2 . TYR B 1 213 ? -49.472 21.120  -7.050  1.00 55.46  ? 210 TYR B CE2 1 
ATOM   4348 C CZ  . TYR B 1 213 ? -49.623 22.435  -7.449  1.00 56.26  ? 210 TYR B CZ  1 
ATOM   4349 O OH  . TYR B 1 213 ? -50.033 22.723  -8.741  1.00 50.91  ? 210 TYR B OH  1 
ATOM   4350 N N   . LYS B 1 214 ? -51.329 22.977  -2.610  1.00 67.85  ? 211 LYS B N   1 
ATOM   4351 C CA  . LYS B 1 214 ? -52.035 24.249  -2.473  1.00 66.43  ? 211 LYS B CA  1 
ATOM   4352 C C   . LYS B 1 214 ? -52.593 24.421  -1.057  1.00 68.67  ? 211 LYS B C   1 
ATOM   4353 O O   . LYS B 1 214 ? -52.596 25.538  -0.520  1.00 67.08  ? 211 LYS B O   1 
ATOM   4354 C CB  . LYS B 1 214 ? -53.136 24.345  -3.539  1.00 61.45  ? 211 LYS B CB  1 
ATOM   4355 C CG  . LYS B 1 214 ? -52.622 24.297  -4.988  1.00 55.11  ? 211 LYS B CG  1 
ATOM   4356 C CD  . LYS B 1 214 ? -53.713 23.886  -5.980  1.00 57.48  ? 211 LYS B CD  1 
ATOM   4357 C CE  . LYS B 1 214 ? -53.222 23.966  -7.448  1.00 62.95  ? 211 LYS B CE  1 
ATOM   4358 N NZ  . LYS B 1 214 ? -54.212 23.554  -8.521  1.00 53.05  ? 211 LYS B NZ  1 
ATOM   4359 N N   . LEU B 1 215 ? -53.058 23.331  -0.429  1.00 67.89  ? 212 LEU B N   1 
ATOM   4360 C CA  . LEU B 1 215 ? -53.363 23.389  0.998   1.00 65.17  ? 212 LEU B CA  1 
ATOM   4361 C C   . LEU B 1 215 ? -52.113 23.718  1.795   1.00 66.90  ? 212 LEU B C   1 
ATOM   4362 O O   . LEU B 1 215 ? -52.145 24.566  2.695   1.00 73.03  ? 212 LEU B O   1 
ATOM   4363 C CB  . LEU B 1 215 ? -53.945 22.062  1.481   1.00 68.80  ? 212 LEU B CB  1 
ATOM   4364 C CG  . LEU B 1 215 ? -55.190 21.457  0.834   1.00 69.42  ? 212 LEU B CG  1 
ATOM   4365 C CD1 . LEU B 1 215 ? -55.332 20.014  1.281   1.00 67.78  ? 212 LEU B CD1 1 
ATOM   4366 C CD2 . LEU B 1 215 ? -56.423 22.250  1.197   1.00 64.13  ? 212 LEU B CD2 1 
ATOM   4367 N N   . ALA B 1 216 ? -50.996 23.070  1.451   1.00 62.64  ? 213 ALA B N   1 
ATOM   4368 C CA  . ALA B 1 216 ? -49.718 23.175  2.157   1.00 65.29  ? 213 ALA B CA  1 
ATOM   4369 C C   . ALA B 1 216 ? -48.930 24.396  1.676   1.00 68.94  ? 213 ALA B C   1 
ATOM   4370 O O   . ALA B 1 216 ? -47.936 24.292  0.956   1.00 70.39  ? 213 ALA B O   1 
ATOM   4371 C CB  . ALA B 1 216 ? -48.920 21.892  1.960   1.00 63.75  ? 213 ALA B CB  1 
ATOM   4372 N N   . ASP B 1 217 ? -49.363 25.581  2.121   1.00 72.85  ? 214 ASP B N   1 
ATOM   4373 C CA  . ASP B 1 217 ? -48.679 26.813  1.724   1.00 75.05  ? 214 ASP B CA  1 
ATOM   4374 C C   . ASP B 1 217 ? -47.259 26.865  2.257   1.00 72.51  ? 214 ASP B C   1 
ATOM   4375 O O   . ASP B 1 217 ? -46.351 27.364  1.581   1.00 67.60  ? 214 ASP B O   1 
ATOM   4376 C CB  . ASP B 1 217 ? -49.437 28.036  2.237   1.00 75.11  ? 214 ASP B CB  1 
ATOM   4377 C CG  . ASP B 1 217 ? -50.920 27.885  2.112   1.00 79.67  ? 214 ASP B CG  1 
ATOM   4378 O OD1 . ASP B 1 217 ? -51.397 27.744  0.965   1.00 78.97  ? 214 ASP B OD1 1 
ATOM   4379 O OD2 . ASP B 1 217 ? -51.603 27.894  3.165   1.00 83.85  ? 214 ASP B OD2 1 
ATOM   4380 N N   . ASP B 1 218 ? -47.057 26.361  3.468   1.00 77.21  ? 215 ASP B N   1 
ATOM   4381 C CA  . ASP B 1 218 ? -45.916 26.696  4.302   1.00 75.09  ? 215 ASP B CA  1 
ATOM   4382 C C   . ASP B 1 218 ? -44.958 25.519  4.439   1.00 71.29  ? 215 ASP B C   1 
ATOM   4383 O O   . ASP B 1 218 ? -45.311 24.359  4.199   1.00 64.71  ? 215 ASP B O   1 
ATOM   4384 C CB  . ASP B 1 218 ? -46.388 27.145  5.693   1.00 72.75  ? 215 ASP B CB  1 
ATOM   4385 C CG  . ASP B 1 218 ? -45.290 27.827  6.480   1.00 81.42  ? 215 ASP B CG  1 
ATOM   4386 O OD1 . ASP B 1 218 ? -44.306 28.287  5.856   1.00 84.89  ? 215 ASP B OD1 1 
ATOM   4387 O OD2 . ASP B 1 218 ? -45.400 27.895  7.718   1.00 78.97  ? 215 ASP B OD2 1 
ATOM   4388 N N   . ALA B 1 219 ? -43.718 25.844  4.826   1.00 74.91  ? 216 ALA B N   1 
ATOM   4389 C CA  . ALA B 1 219 ? -42.775 24.812  5.253   1.00 74.18  ? 216 ALA B CA  1 
ATOM   4390 C C   . ALA B 1 219 ? -43.293 24.079  6.489   1.00 73.75  ? 216 ALA B C   1 
ATOM   4391 O O   . ALA B 1 219 ? -43.136 22.857  6.614   1.00 65.37  ? 216 ALA B O   1 
ATOM   4392 C CB  . ALA B 1 219 ? -41.402 25.437  5.524   1.00 63.01  ? 216 ALA B CB  1 
ATOM   4393 N N   . ASP B 1 220 ? -43.925 24.812  7.410   1.00 76.27  ? 217 ASP B N   1 
ATOM   4394 C CA  . ASP B 1 220 ? -44.541 24.181  8.573   1.00 71.60  ? 217 ASP B CA  1 
ATOM   4395 C C   . ASP B 1 220 ? -45.679 23.260  8.147   1.00 69.92  ? 217 ASP B C   1 
ATOM   4396 O O   . ASP B 1 220 ? -45.654 22.053  8.415   1.00 65.74  ? 217 ASP B O   1 
ATOM   4397 C CB  . ASP B 1 220 ? -45.029 25.254  9.546   1.00 69.52  ? 217 ASP B CB  1 
ATOM   4398 C CG  . ASP B 1 220 ? -43.907 26.200  9.986   1.00 81.02  ? 217 ASP B CG  1 
ATOM   4399 O OD1 . ASP B 1 220 ? -43.260 26.840  9.116   1.00 82.45  ? 217 ASP B OD1 1 
ATOM   4400 O OD2 . ASP B 1 220 ? -43.667 26.308  11.205  1.00 80.39  ? 217 ASP B OD2 1 
ATOM   4401 N N   . LYS B 1 221 ? -46.679 23.810  7.452   1.00 69.80  ? 218 LYS B N   1 
ATOM   4402 C CA  . LYS B 1 221 ? -47.807 22.994  7.009   1.00 64.85  ? 218 LYS B CA  1 
ATOM   4403 C C   . LYS B 1 221 ? -47.340 21.777  6.214   1.00 64.56  ? 218 LYS B C   1 
ATOM   4404 O O   . LYS B 1 221 ? -47.943 20.700  6.316   1.00 60.52  ? 218 LYS B O   1 
ATOM   4405 C CB  . LYS B 1 221 ? -48.785 23.858  6.197   1.00 71.36  ? 218 LYS B CB  1 
ATOM   4406 C CG  . LYS B 1 221 ? -49.466 24.962  7.021   1.00 73.10  ? 218 LYS B CG  1 
ATOM   4407 C CD  . LYS B 1 221 ? -50.035 26.068  6.149   1.00 73.85  ? 218 LYS B CD  1 
ATOM   4408 C CE  . LYS B 1 221 ? -51.543 26.198  6.316   1.00 70.87  ? 218 LYS B CE  1 
ATOM   4409 N NZ  . LYS B 1 221 ? -52.054 27.467  5.721   1.00 69.72  ? 218 LYS B NZ  1 
ATOM   4410 N N   . MET B 1 222 ? -46.222 21.906  5.479   1.00 67.75  ? 219 MET B N   1 
ATOM   4411 C CA  . MET B 1 222 ? -45.715 20.814  4.643   1.00 66.22  ? 219 MET B CA  1 
ATOM   4412 C C   . MET B 1 222 ? -44.989 19.746  5.459   1.00 62.55  ? 219 MET B C   1 
ATOM   4413 O O   . MET B 1 222 ? -45.049 18.556  5.124   1.00 54.63  ? 219 MET B O   1 
ATOM   4414 C CB  . MET B 1 222 ? -44.780 21.363  3.554   1.00 67.80  ? 219 MET B CB  1 
ATOM   4415 C CG  . MET B 1 222 ? -45.344 21.328  2.129   1.00 61.20  ? 219 MET B CG  1 
ATOM   4416 S SD  . MET B 1 222 ? -45.839 19.660  1.618   1.00 74.49  ? 219 MET B SD  1 
ATOM   4417 C CE  . MET B 1 222 ? -46.349 19.981  -0.061  1.00 60.36  ? 219 MET B CE  1 
ATOM   4418 N N   . ARG B 1 223 ? -44.260 20.145  6.500   1.00 57.89  ? 220 ARG B N   1 
ATOM   4419 C CA  . ARG B 1 223 ? -43.673 19.149  7.383   1.00 61.66  ? 220 ARG B CA  1 
ATOM   4420 C C   . ARG B 1 223 ? -44.748 18.237  7.955   1.00 64.68  ? 220 ARG B C   1 
ATOM   4421 O O   . ARG B 1 223 ? -44.613 17.006  7.929   1.00 59.23  ? 220 ARG B O   1 
ATOM   4422 C CB  . ARG B 1 223 ? -42.895 19.834  8.500   1.00 67.24  ? 220 ARG B CB  1 
ATOM   4423 C CG  . ARG B 1 223 ? -41.468 20.177  8.137   1.00 64.07  ? 220 ARG B CG  1 
ATOM   4424 C CD  . ARG B 1 223 ? -40.755 20.894  9.275   1.00 65.40  ? 220 ARG B CD  1 
ATOM   4425 N NE  . ARG B 1 223 ? -41.185 22.281  9.415   1.00 71.57  ? 220 ARG B NE  1 
ATOM   4426 C CZ  . ARG B 1 223 ? -40.593 23.317  8.832   1.00 76.75  ? 220 ARG B CZ  1 
ATOM   4427 N NH1 . ARG B 1 223 ? -39.546 23.161  8.030   1.00 72.89  ? 220 ARG B NH1 1 
ATOM   4428 N NH2 . ARG B 1 223 ? -41.059 24.543  9.060   1.00 78.07  ? 220 ARG B NH2 1 
ATOM   4429 N N   . GLU B 1 224 ? -45.841 18.829  8.451   1.00 65.50  ? 221 GLU B N   1 
ATOM   4430 C CA  . GLU B 1 224 ? -46.877 18.041  9.115   1.00 65.88  ? 221 GLU B CA  1 
ATOM   4431 C C   . GLU B 1 224 ? -47.476 17.016  8.167   1.00 63.71  ? 221 GLU B C   1 
ATOM   4432 O O   . GLU B 1 224 ? -47.635 15.843  8.527   1.00 63.65  ? 221 GLU B O   1 
ATOM   4433 C CB  . GLU B 1 224 ? -47.953 18.965  9.694   1.00 59.23  ? 221 GLU B CB  1 
ATOM   4434 C CG  . GLU B 1 224 ? -47.434 19.878  10.818  1.00 67.23  ? 221 GLU B CG  1 
ATOM   4435 C CD  . GLU B 1 224 ? -46.823 19.103  12.011  1.00 78.95  ? 221 GLU B CD  1 
ATOM   4436 O OE1 . GLU B 1 224 ? -47.388 18.048  12.398  1.00 73.02  ? 221 GLU B OE1 1 
ATOM   4437 O OE2 . GLU B 1 224 ? -45.784 19.519  12.566  1.00 79.52  ? 221 GLU B OE2 1 
ATOM   4438 N N   . ALA B 1 225 ? -47.787 17.429  6.937   1.00 57.02  ? 222 ALA B N   1 
ATOM   4439 C CA  . ALA B 1 225 ? -48.364 16.483  5.990   1.00 58.61  ? 222 ALA B CA  1 
ATOM   4440 C C   . ALA B 1 225 ? -47.351 15.416  5.587   1.00 64.22  ? 222 ALA B C   1 
ATOM   4441 O O   . ALA B 1 225 ? -47.718 14.254  5.365   1.00 59.94  ? 222 ALA B O   1 
ATOM   4442 C CB  . ALA B 1 225 ? -48.890 17.230  4.768   1.00 63.53  ? 222 ALA B CB  1 
ATOM   4443 N N   . LEU B 1 226 ? -46.072 15.791  5.509   1.00 67.33  ? 223 LEU B N   1 
ATOM   4444 C CA  . LEU B 1 226 ? -45.020 14.825  5.214   1.00 62.52  ? 223 LEU B CA  1 
ATOM   4445 C C   . LEU B 1 226 ? -44.821 13.843  6.366   1.00 64.78  ? 223 LEU B C   1 
ATOM   4446 O O   . LEU B 1 226 ? -44.825 12.619  6.157   1.00 60.92  ? 223 LEU B O   1 
ATOM   4447 C CB  . LEU B 1 226 ? -43.724 15.569  4.902   1.00 63.02  ? 223 LEU B CB  1 
ATOM   4448 C CG  . LEU B 1 226 ? -43.580 16.049  3.462   1.00 58.77  ? 223 LEU B CG  1 
ATOM   4449 C CD1 . LEU B 1 226 ? -42.425 17.038  3.337   1.00 51.21  ? 223 LEU B CD1 1 
ATOM   4450 C CD2 . LEU B 1 226 ? -43.393 14.831  2.540   1.00 49.09  ? 223 LEU B CD2 1 
ATOM   4451 N N   . ARG B 1 227 ? -44.662 14.377  7.570   1.00 63.76  ? 224 ARG B N   1 
ATOM   4452 C CA  . ARG B 1 227 ? -44.520 13.534  8.745   1.00 65.28  ? 224 ARG B CA  1 
ATOM   4453 C C   . ARG B 1 227 ? -45.564 12.473  8.695   1.00 65.55  ? 224 ARG B C   1 
ATOM   4454 O O   . ARG B 1 227 ? -45.275 11.298  8.867   1.00 66.82  ? 224 ARG B O   1 
ATOM   4455 C CB  . ARG B 1 227 ? -44.737 14.355  10.000  1.00 62.82  ? 224 ARG B CB  1 
ATOM   4456 C CG  . ARG B 1 227 ? -43.648 15.359  10.314  1.00 69.39  ? 224 ARG B CG  1 
ATOM   4457 C CD  . ARG B 1 227 ? -43.870 15.945  11.696  1.00 69.98  ? 224 ARG B CD  1 
ATOM   4458 N NE  . ARG B 1 227 ? -44.009 17.394  11.678  1.00 68.29  ? 224 ARG B NE  1 
ATOM   4459 C CZ  . ARG B 1 227 ? -42.992 18.236  11.810  1.00 71.48  ? 224 ARG B CZ  1 
ATOM   4460 N NH1 . ARG B 1 227 ? -41.763 17.768  11.962  1.00 72.87  ? 224 ARG B NH1 1 
ATOM   4461 N NH2 . ARG B 1 227 ? -43.198 19.545  11.790  1.00 66.01  ? 224 ARG B NH2 1 
ATOM   4462 N N   . GLU B 1 228 ? -46.798 12.885  8.487   1.00 62.11  ? 225 GLU B N   1 
ATOM   4463 C CA  . GLU B 1 228 ? -47.887 11.926  8.336   1.00 55.64  ? 225 GLU B CA  1 
ATOM   4464 C C   . GLU B 1 228 ? -47.648 11.018  7.139   1.00 61.55  ? 225 GLU B C   1 
ATOM   4465 O O   . GLU B 1 228 ? -47.709 9.787   7.253   1.00 59.38  ? 225 GLU B O   1 
ATOM   4466 C CB  . GLU B 1 228 ? -49.219 12.664  8.188   1.00 64.88  ? 225 GLU B CB  1 
ATOM   4467 C CG  . GLU B 1 228 ? -50.472 11.757  8.210   1.00 74.47  ? 225 GLU B CG  1 
ATOM   4468 C CD  . GLU B 1 228 ? -50.789 11.115  6.857   1.00 76.28  ? 225 GLU B CD  1 
ATOM   4469 O OE1 . GLU B 1 228 ? -51.475 11.762  6.032   1.00 75.52  ? 225 GLU B OE1 1 
ATOM   4470 O OE2 . GLU B 1 228 ? -50.345 9.963   6.619   1.00 79.30  ? 225 GLU B OE2 1 
ATOM   4471 N N   . ALA B 1 229 ? -47.379 11.611  5.972   1.00 63.39  ? 226 ALA B N   1 
ATOM   4472 C CA  . ALA B 1 229 ? -47.282 10.817  4.751   1.00 62.26  ? 226 ALA B CA  1 
ATOM   4473 C C   . ALA B 1 229 ? -46.076 9.890   4.770   1.00 59.13  ? 226 ALA B C   1 
ATOM   4474 O O   . ALA B 1 229 ? -46.125 8.798   4.193   1.00 47.61  ? 226 ALA B O   1 
ATOM   4475 C CB  . ALA B 1 229 ? -47.218 11.738  3.535   1.00 62.96  ? 226 ALA B CB  1 
ATOM   4476 N N   . ALA B 1 230 ? -44.990 10.314  5.416   1.00 62.51  ? 227 ALA B N   1 
ATOM   4477 C CA  . ALA B 1 230 ? -43.754 9.543   5.508   1.00 63.62  ? 227 ALA B CA  1 
ATOM   4478 C C   . ALA B 1 230 ? -43.306 9.588   6.961   1.00 63.52  ? 227 ALA B C   1 
ATOM   4479 O O   . ALA B 1 230 ? -42.555 10.491  7.362   1.00 61.24  ? 227 ALA B O   1 
ATOM   4480 C CB  . ALA B 1 230 ? -42.692 10.101  4.565   1.00 57.10  ? 227 ALA B CB  1 
ATOM   4481 N N   . PRO B 1 231 ? -43.755 8.630   7.785   1.00 65.84  ? 228 PRO B N   1 
ATOM   4482 C CA  . PRO B 1 231 ? -43.457 8.677   9.231   1.00 72.08  ? 228 PRO B CA  1 
ATOM   4483 C C   . PRO B 1 231 ? -42.040 8.229   9.560   1.00 64.38  ? 228 PRO B C   1 
ATOM   4484 O O   . PRO B 1 231 ? -41.413 8.735   10.498  1.00 55.00  ? 228 PRO B O   1 
ATOM   4485 C CB  . PRO B 1 231 ? -44.493 7.721   9.828   1.00 68.40  ? 228 PRO B CB  1 
ATOM   4486 C CG  . PRO B 1 231 ? -44.716 6.718   8.726   1.00 65.98  ? 228 PRO B CG  1 
ATOM   4487 C CD  . PRO B 1 231 ? -44.565 7.457   7.418   1.00 57.67  ? 228 PRO B CD  1 
ATOM   4488 N N   . ASP B 1 232 ? -41.533 7.280   8.773   1.00 62.96  ? 229 ASP B N   1 
ATOM   4489 C CA  . ASP B 1 232 ? -40.169 6.782   8.849   1.00 63.16  ? 229 ASP B CA  1 
ATOM   4490 C C   . ASP B 1 232 ? -39.152 7.678   8.146   1.00 65.06  ? 229 ASP B C   1 
ATOM   4491 O O   . ASP B 1 232 ? -38.026 7.220   7.900   1.00 61.04  ? 229 ASP B O   1 
ATOM   4492 C CB  . ASP B 1 232 ? -40.105 5.377   8.257   1.00 59.90  ? 229 ASP B CB  1 
ATOM   4493 C CG  . ASP B 1 232 ? -40.988 4.416   8.997   1.00 71.77  ? 229 ASP B CG  1 
ATOM   4494 O OD1 . ASP B 1 232 ? -41.215 4.659   10.209  1.00 77.00  ? 229 ASP B OD1 1 
ATOM   4495 O OD2 . ASP B 1 232 ? -41.455 3.429   8.382   1.00 73.31  ? 229 ASP B OD2 1 
ATOM   4496 N N   . GLY B 1 233 ? -39.514 8.918   7.808   1.00 66.99  ? 230 GLY B N   1 
ATOM   4497 C CA  . GLY B 1 233 ? -38.601 9.826   7.142   1.00 61.16  ? 230 GLY B CA  1 
ATOM   4498 C C   . GLY B 1 233 ? -38.426 9.536   5.656   1.00 57.56  ? 230 GLY B C   1 
ATOM   4499 O O   . GLY B 1 233 ? -39.027 8.623   5.075   1.00 58.92  ? 230 GLY B O   1 
ATOM   4500 N N   . VAL B 1 234 ? -37.554 10.338  5.038   1.00 56.17  ? 231 VAL B N   1 
ATOM   4501 C CA  . VAL B 1 234 ? -37.279 10.280  3.605   1.00 47.44  ? 231 VAL B CA  1 
ATOM   4502 C C   . VAL B 1 234 ? -35.909 9.661   3.385   1.00 43.31  ? 231 VAL B C   1 
ATOM   4503 O O   . VAL B 1 234 ? -34.906 10.146  3.924   1.00 39.30  ? 231 VAL B O   1 
ATOM   4504 C CB  . VAL B 1 234 ? -37.331 11.676  2.964   1.00 43.94  ? 231 VAL B CB  1 
ATOM   4505 C CG1 . VAL B 1 234 ? -37.309 11.557  1.458   1.00 44.67  ? 231 VAL B CG1 1 
ATOM   4506 C CG2 . VAL B 1 234 ? -38.544 12.455  3.446   1.00 49.45  ? 231 VAL B CG2 1 
ATOM   4507 N N   . ASP B 1 235 ? -35.862 8.618   2.556   1.00 43.66  ? 232 ASP B N   1 
ATOM   4508 C CA  . ASP B 1 235 ? -34.604 8.090   2.045   1.00 45.09  ? 232 ASP B CA  1 
ATOM   4509 C C   . ASP B 1 235 ? -34.278 8.547   0.622   1.00 49.40  ? 232 ASP B C   1 
ATOM   4510 O O   . ASP B 1 235 ? -33.098 8.538   0.243   1.00 38.81  ? 232 ASP B O   1 
ATOM   4511 C CB  . ASP B 1 235 ? -34.628 6.566   2.060   1.00 48.74  ? 232 ASP B CB  1 
ATOM   4512 C CG  . ASP B 1 235 ? -35.370 6.022   3.234   1.00 53.64  ? 232 ASP B CG  1 
ATOM   4513 O OD1 . ASP B 1 235 ? -34.928 6.273   4.384   1.00 46.80  ? 232 ASP B OD1 1 
ATOM   4514 O OD2 . ASP B 1 235 ? -36.411 5.363   2.988   1.00 53.84  ? 232 ASP B OD2 1 
ATOM   4515 N N   . LYS B 1 236 ? -35.287 8.903   -0.184  1.00 44.31  ? 233 LYS B N   1 
ATOM   4516 C CA  . LYS B 1 236 ? -35.067 9.391   -1.540  1.00 42.86  ? 233 LYS B CA  1 
ATOM   4517 C C   . LYS B 1 236 ? -36.025 10.537  -1.812  1.00 40.49  ? 233 LYS B C   1 
ATOM   4518 O O   . LYS B 1 236 ? -37.177 10.498  -1.384  1.00 43.00  ? 233 LYS B O   1 
ATOM   4519 C CB  . LYS B 1 236 ? -35.261 8.297   -2.597  1.00 38.04  ? 233 LYS B CB  1 
ATOM   4520 C CG  . LYS B 1 236 ? -34.592 6.964   -2.279  1.00 45.25  ? 233 LYS B CG  1 
ATOM   4521 C CD  . LYS B 1 236 ? -33.158 6.910   -2.745  1.00 44.74  ? 233 LYS B CD  1 
ATOM   4522 C CE  . LYS B 1 236 ? -32.628 5.477   -2.751  1.00 43.57  ? 233 LYS B CE  1 
ATOM   4523 N NZ  . LYS B 1 236 ? -32.499 4.857   -1.418  1.00 43.88  ? 233 LYS B NZ  1 
ATOM   4524 N N   . TYR B 1 237 ? -35.544 11.546  -2.534  1.00 36.05  ? 234 TYR B N   1 
ATOM   4525 C CA  . TYR B 1 237 ? -36.333 12.726  -2.870  1.00 35.22  ? 234 TYR B CA  1 
ATOM   4526 C C   . TYR B 1 237 ? -36.007 13.166  -4.297  1.00 44.38  ? 234 TYR B C   1 
ATOM   4527 O O   . TYR B 1 237 ? -34.881 13.583  -4.590  1.00 40.31  ? 234 TYR B O   1 
ATOM   4528 C CB  . TYR B 1 237 ? -36.070 13.858  -1.876  1.00 31.57  ? 234 TYR B CB  1 
ATOM   4529 C CG  . TYR B 1 237 ? -36.885 15.113  -2.115  1.00 37.94  ? 234 TYR B CG  1 
ATOM   4530 C CD1 . TYR B 1 237 ? -38.132 15.056  -2.740  1.00 39.70  ? 234 TYR B CD1 1 
ATOM   4531 C CD2 . TYR B 1 237 ? -36.407 16.360  -1.721  1.00 34.85  ? 234 TYR B CD2 1 
ATOM   4532 C CE1 . TYR B 1 237 ? -38.876 16.203  -2.962  1.00 39.10  ? 234 TYR B CE1 1 
ATOM   4533 C CE2 . TYR B 1 237 ? -37.139 17.504  -1.934  1.00 37.53  ? 234 TYR B CE2 1 
ATOM   4534 C CZ  . TYR B 1 237 ? -38.370 17.423  -2.557  1.00 39.32  ? 234 TYR B CZ  1 
ATOM   4535 O OH  . TYR B 1 237 ? -39.088 18.572  -2.765  1.00 45.14  ? 234 TYR B OH  1 
ATOM   4536 N N   . PHE B 1 238 ? -36.996 13.063  -5.187  1.00 47.09  ? 235 PHE B N   1 
ATOM   4537 C CA  . PHE B 1 238 ? -36.935 13.635  -6.528  1.00 39.32  ? 235 PHE B CA  1 
ATOM   4538 C C   . PHE B 1 238 ? -37.606 15.008  -6.487  1.00 38.61  ? 235 PHE B C   1 
ATOM   4539 O O   . PHE B 1 238 ? -38.829 15.101  -6.377  1.00 38.64  ? 235 PHE B O   1 
ATOM   4540 C CB  . PHE B 1 238 ? -37.623 12.710  -7.525  1.00 39.10  ? 235 PHE B CB  1 
ATOM   4541 C CG  . PHE B 1 238 ? -37.380 13.069  -8.945  1.00 38.23  ? 235 PHE B CG  1 
ATOM   4542 C CD1 . PHE B 1 238 ? -38.071 14.113  -9.536  1.00 41.39  ? 235 PHE B CD1 1 
ATOM   4543 C CD2 . PHE B 1 238 ? -36.468 12.357  -9.704  1.00 47.39  ? 235 PHE B CD2 1 
ATOM   4544 C CE1 . PHE B 1 238 ? -37.848 14.453  -10.854 1.00 37.22  ? 235 PHE B CE1 1 
ATOM   4545 C CE2 . PHE B 1 238 ? -36.239 12.688  -11.032 1.00 45.16  ? 235 PHE B CE2 1 
ATOM   4546 C CZ  . PHE B 1 238 ? -36.932 13.744  -11.602 1.00 43.44  ? 235 PHE B CZ  1 
ATOM   4547 N N   . ASP B 1 239 ? -36.799 16.068  -6.580  1.00 42.86  ? 236 ASP B N   1 
ATOM   4548 C CA  . ASP B 1 239 ? -37.235 17.453  -6.409  1.00 41.34  ? 236 ASP B CA  1 
ATOM   4549 C C   . ASP B 1 239 ? -37.421 18.130  -7.766  1.00 45.94  ? 236 ASP B C   1 
ATOM   4550 O O   . ASP B 1 239 ? -36.503 18.128  -8.595  1.00 40.72  ? 236 ASP B O   1 
ATOM   4551 C CB  . ASP B 1 239 ? -36.215 18.235  -5.576  1.00 32.52  ? 236 ASP B CB  1 
ATOM   4552 C CG  . ASP B 1 239 ? -36.774 19.547  -5.044  1.00 42.99  ? 236 ASP B CG  1 
ATOM   4553 O OD1 . ASP B 1 239 ? -37.994 19.767  -5.225  1.00 44.23  ? 236 ASP B OD1 1 
ATOM   4554 O OD2 . ASP B 1 239 ? -36.011 20.357  -4.434  1.00 40.48  ? 236 ASP B OD2 1 
ATOM   4555 N N   . SER B 1 240 ? -38.623 18.695  -7.994  1.00 43.11  ? 237 SER B N   1 
ATOM   4556 C CA  . SER B 1 240 ? -38.908 19.527  -9.162  1.00 36.74  ? 237 SER B CA  1 
ATOM   4557 C C   . SER B 1 240 ? -39.360 20.914  -8.780  1.00 38.93  ? 237 SER B C   1 
ATOM   4558 O O   . SER B 1 240 ? -39.475 21.774  -9.669  1.00 36.19  ? 237 SER B O   1 
ATOM   4559 C CB  . SER B 1 240 ? -39.998 18.910  -10.059 1.00 36.14  ? 237 SER B CB  1 
ATOM   4560 O OG  . SER B 1 240 ? -39.538 17.771  -10.759 1.00 38.01  ? 237 SER B OG  1 
ATOM   4561 N N   . ILE B 1 241 ? -39.581 21.159  -7.488  1.00 32.44  ? 238 ILE B N   1 
ATOM   4562 C CA  . ILE B 1 241 ? -40.279 22.332  -7.020  1.00 28.68  ? 238 ILE B CA  1 
ATOM   4563 C C   . ILE B 1 241 ? -39.371 23.242  -6.214  1.00 37.63  ? 238 ILE B C   1 
ATOM   4564 O O   . ILE B 1 241 ? -39.467 24.469  -6.318  1.00 38.70  ? 238 ILE B O   1 
ATOM   4565 C CB  . ILE B 1 241 ? -41.508 21.915  -6.194  1.00 34.83  ? 238 ILE B CB  1 
ATOM   4566 C CG1 . ILE B 1 241 ? -42.432 21.045  -7.047  1.00 33.28  ? 238 ILE B CG1 1 
ATOM   4567 C CG2 . ILE B 1 241 ? -42.199 23.148  -5.653  1.00 29.17  ? 238 ILE B CG2 1 
ATOM   4568 C CD1 . ILE B 1 241 ? -42.916 21.772  -8.277  1.00 40.24  ? 238 ILE B CD1 1 
ATOM   4569 N N   . GLY B 1 242 ? -38.494 22.661  -5.393  1.00 40.37  ? 239 GLY B N   1 
ATOM   4570 C CA  . GLY B 1 242 ? -37.698 23.461  -4.492  1.00 37.11  ? 239 GLY B CA  1 
ATOM   4571 C C   . GLY B 1 242 ? -38.591 24.175  -3.501  1.00 39.94  ? 239 GLY B C   1 
ATOM   4572 O O   . GLY B 1 242 ? -39.680 23.712  -3.150  1.00 40.43  ? 239 GLY B O   1 
ATOM   4573 N N   . GLY B 1 243 ? -38.125 25.327  -3.043  1.00 40.75  ? 240 GLY B N   1 
ATOM   4574 C CA  . GLY B 1 243 ? -39.001 26.106  -2.205  1.00 46.43  ? 240 GLY B CA  1 
ATOM   4575 C C   . GLY B 1 243 ? -39.312 25.419  -0.892  1.00 49.86  ? 240 GLY B C   1 
ATOM   4576 O O   . GLY B 1 243 ? -38.525 24.630  -0.362  1.00 51.06  ? 240 GLY B O   1 
ATOM   4577 N N   . SER B 1 244 ? -40.511 25.706  -0.379  1.00 56.65  ? 241 SER B N   1 
ATOM   4578 C CA  . SER B 1 244 ? -40.852 25.352  0.996   1.00 52.81  ? 241 SER B CA  1 
ATOM   4579 C C   . SER B 1 244 ? -41.026 23.845  1.173   1.00 50.83  ? 241 SER B C   1 
ATOM   4580 O O   . SER B 1 244 ? -40.739 23.319  2.255   1.00 54.26  ? 241 SER B O   1 
ATOM   4581 C CB  . SER B 1 244 ? -42.113 26.115  1.435   1.00 51.21  ? 241 SER B CB  1 
ATOM   4582 O OG  . SER B 1 244 ? -43.315 25.535  0.924   1.00 49.18  ? 241 SER B OG  1 
ATOM   4583 N N   . VAL B 1 245 ? -41.468 23.134  0.129   1.00 46.55  ? 242 VAL B N   1 
ATOM   4584 C CA  . VAL B 1 245 ? -41.614 21.680  0.217   1.00 47.20  ? 242 VAL B CA  1 
ATOM   4585 C C   . VAL B 1 245 ? -40.252 21.007  0.373   1.00 49.56  ? 242 VAL B C   1 
ATOM   4586 O O   . VAL B 1 245 ? -40.101 20.049  1.144   1.00 48.31  ? 242 VAL B O   1 
ATOM   4587 C CB  . VAL B 1 245 ? -42.374 21.139  -1.013  1.00 51.19  ? 242 VAL B CB  1 
ATOM   4588 C CG1 . VAL B 1 245 ? -41.651 21.484  -2.324  1.00 49.73  ? 242 VAL B CG1 1 
ATOM   4589 C CG2 . VAL B 1 245 ? -42.585 19.628  -0.907  1.00 44.77  ? 242 VAL B CG2 1 
ATOM   4590 N N   . THR B 1 246 ? -39.246 21.496  -0.360  1.00 48.06  ? 243 THR B N   1 
ATOM   4591 C CA  . THR B 1 246 ? -37.882 21.001  -0.228  1.00 48.87  ? 243 THR B CA  1 
ATOM   4592 C C   . THR B 1 246 ? -37.297 21.346  1.140   1.00 49.40  ? 243 THR B C   1 
ATOM   4593 O O   . THR B 1 246 ? -36.601 20.525  1.750   1.00 47.86  ? 243 THR B O   1 
ATOM   4594 C CB  . THR B 1 246 ? -37.032 21.578  -1.365  1.00 48.91  ? 243 THR B CB  1 
ATOM   4595 O OG1 . THR B 1 246 ? -37.461 21.005  -2.608  1.00 41.92  ? 243 THR B OG1 1 
ATOM   4596 C CG2 . THR B 1 246 ? -35.527 21.322  -1.149  1.00 43.10  ? 243 THR B CG2 1 
ATOM   4597 N N   . ASP B 1 247 ? -37.569 22.554  1.637   1.00 46.14  ? 244 ASP B N   1 
ATOM   4598 C CA  . ASP B 1 247 ? -37.152 22.904  2.990   1.00 54.62  ? 244 ASP B CA  1 
ATOM   4599 C C   . ASP B 1 247 ? -37.746 21.948  4.020   1.00 58.52  ? 244 ASP B C   1 
ATOM   4600 O O   . ASP B 1 247 ? -37.126 21.670  5.059   1.00 56.62  ? 244 ASP B O   1 
ATOM   4601 C CB  . ASP B 1 247 ? -37.559 24.342  3.305   1.00 56.72  ? 244 ASP B CB  1 
ATOM   4602 C CG  . ASP B 1 247 ? -36.817 25.364  2.459   1.00 58.49  ? 244 ASP B CG  1 
ATOM   4603 O OD1 . ASP B 1 247 ? -35.705 25.048  1.977   1.00 62.97  ? 244 ASP B OD1 1 
ATOM   4604 O OD2 . ASP B 1 247 ? -37.345 26.486  2.283   1.00 60.33  ? 244 ASP B OD2 1 
ATOM   4605 N N   . ALA B 1 248 ? -38.940 21.431  3.752   1.00 52.24  ? 245 ALA B N   1 
ATOM   4606 C CA  . ALA B 1 248 ? -39.527 20.465  4.665   1.00 54.42  ? 245 ALA B CA  1 
ATOM   4607 C C   . ALA B 1 248 ? -38.817 19.122  4.566   1.00 55.38  ? 245 ALA B C   1 
ATOM   4608 O O   . ALA B 1 248 ? -38.430 18.543  5.588   1.00 55.80  ? 245 ALA B O   1 
ATOM   4609 C CB  . ALA B 1 248 ? -41.020 20.316  4.374   1.00 59.55  ? 245 ALA B CB  1 
ATOM   4610 N N   . VAL B 1 249 ? -38.632 18.615  3.339   1.00 46.74  ? 246 VAL B N   1 
ATOM   4611 C CA  . VAL B 1 249 ? -38.047 17.290  3.159   1.00 48.15  ? 246 VAL B CA  1 
ATOM   4612 C C   . VAL B 1 249 ? -36.641 17.222  3.738   1.00 49.68  ? 246 VAL B C   1 
ATOM   4613 O O   . VAL B 1 249 ? -36.233 16.184  4.274   1.00 47.45  ? 246 VAL B O   1 
ATOM   4614 C CB  . VAL B 1 249 ? -38.057 16.895  1.674   1.00 48.34  ? 246 VAL B CB  1 
ATOM   4615 C CG1 . VAL B 1 249 ? -37.342 15.580  1.476   1.00 45.45  ? 246 VAL B CG1 1 
ATOM   4616 C CG2 . VAL B 1 249 ? -39.484 16.780  1.184   1.00 47.62  ? 246 VAL B CG2 1 
ATOM   4617 N N   . PHE B 1 250 ? -35.886 18.319  3.666   1.00 53.52  ? 247 PHE B N   1 
ATOM   4618 C CA  . PHE B 1 250 ? -34.542 18.362  4.234   1.00 50.97  ? 247 PHE B CA  1 
ATOM   4619 C C   . PHE B 1 250 ? -34.535 18.346  5.757   1.00 46.47  ? 247 PHE B C   1 
ATOM   4620 O O   . PHE B 1 250 ? -33.472 18.165  6.359   1.00 51.46  ? 247 PHE B O   1 
ATOM   4621 C CB  . PHE B 1 250 ? -33.797 19.602  3.725   1.00 47.65  ? 247 PHE B CB  1 
ATOM   4622 C CG  . PHE B 1 250 ? -32.986 19.354  2.495   1.00 42.64  ? 247 PHE B CG  1 
ATOM   4623 C CD1 . PHE B 1 250 ? -33.599 18.991  1.304   1.00 46.11  ? 247 PHE B CD1 1 
ATOM   4624 C CD2 . PHE B 1 250 ? -31.613 19.489  2.516   1.00 44.86  ? 247 PHE B CD2 1 
ATOM   4625 C CE1 . PHE B 1 250 ? -32.847 18.755  0.149   1.00 38.77  ? 247 PHE B CE1 1 
ATOM   4626 C CE2 . PHE B 1 250 ? -30.864 19.256  1.367   1.00 44.20  ? 247 PHE B CE2 1 
ATOM   4627 C CZ  . PHE B 1 250 ? -31.486 18.889  0.186   1.00 34.00  ? 247 PHE B CZ  1 
ATOM   4628 N N   . SER B 1 251 ? -35.675 18.531  6.396   1.00 46.61  ? 248 SER B N   1 
ATOM   4629 C CA  . SER B 1 251 ? -35.738 18.450  7.847   1.00 49.50  ? 248 SER B CA  1 
ATOM   4630 C C   . SER B 1 251 ? -35.959 17.027  8.351   1.00 47.90  ? 248 SER B C   1 
ATOM   4631 O O   . SER B 1 251 ? -35.962 16.810  9.565   1.00 54.43  ? 248 SER B O   1 
ATOM   4632 C CB  . SER B 1 251 ? -36.852 19.358  8.376   1.00 50.45  ? 248 SER B CB  1 
ATOM   4633 O OG  . SER B 1 251 ? -38.128 18.819  8.061   1.00 56.44  ? 248 SER B OG  1 
ATOM   4634 N N   . MET B 1 252 ? -36.146 16.062  7.456   1.00 42.67  ? 249 MET B N   1 
ATOM   4635 C CA  . MET B 1 252 ? -36.445 14.694  7.842   1.00 39.36  ? 249 MET B CA  1 
ATOM   4636 C C   . MET B 1 252 ? -35.695 13.699  6.968   1.00 44.16  ? 249 MET B C   1 
ATOM   4637 O O   . MET B 1 252 ? -36.212 12.615  6.668   1.00 42.71  ? 249 MET B O   1 
ATOM   4638 C CB  . MET B 1 252 ? -37.950 14.422  7.794   1.00 47.54  ? 249 MET B CB  1 
ATOM   4639 C CG  . MET B 1 252 ? -38.612 14.568  6.416   1.00 57.28  ? 249 MET B CG  1 
ATOM   4640 S SD  . MET B 1 252 ? -40.385 14.948  6.509   1.00 67.25  ? 249 MET B SD  1 
ATOM   4641 C CE  . MET B 1 252 ? -40.352 16.450  7.481   1.00 54.26  ? 249 MET B CE  1 
ATOM   4642 N N   . LEU B 1 253 ? -34.482 14.061  6.548   1.00 44.10  ? 250 LEU B N   1 
ATOM   4643 C CA  . LEU B 1 253 ? -33.670 13.191  5.706   1.00 40.31  ? 250 LEU B CA  1 
ATOM   4644 C C   . LEU B 1 253 ? -33.137 12.025  6.527   1.00 37.79  ? 250 LEU B C   1 
ATOM   4645 O O   . LEU B 1 253 ? -32.632 12.218  7.629   1.00 38.22  ? 250 LEU B O   1 
ATOM   4646 C CB  . LEU B 1 253 ? -32.513 13.985  5.088   1.00 37.54  ? 250 LEU B CB  1 
ATOM   4647 C CG  . LEU B 1 253 ? -32.963 14.948  3.989   1.00 42.85  ? 250 LEU B CG  1 
ATOM   4648 C CD1 . LEU B 1 253 ? -31.894 15.937  3.595   1.00 44.53  ? 250 LEU B CD1 1 
ATOM   4649 C CD2 . LEU B 1 253 ? -33.377 14.124  2.791   1.00 35.99  ? 250 LEU B CD2 1 
ATOM   4650 N N   . ASN B 1 254 ? -33.246 10.816  5.992   1.00 45.16  ? 251 ASN B N   1 
ATOM   4651 C CA  . ASN B 1 254 ? -32.696 9.649   6.659   1.00 41.39  ? 251 ASN B CA  1 
ATOM   4652 C C   . ASN B 1 254 ? -31.223 9.476   6.304   1.00 45.61  ? 251 ASN B C   1 
ATOM   4653 O O   . ASN B 1 254 ? -30.639 10.239  5.528   1.00 47.95  ? 251 ASN B O   1 
ATOM   4654 C CB  . ASN B 1 254 ? -33.472 8.390   6.281   1.00 36.88  ? 251 ASN B CB  1 
ATOM   4655 C CG  . ASN B 1 254 ? -34.863 8.371   6.868   1.00 42.39  ? 251 ASN B CG  1 
ATOM   4656 O OD1 . ASN B 1 254 ? -35.195 9.147   7.783   1.00 41.25  ? 251 ASN B OD1 1 
ATOM   4657 N ND2 . ASN B 1 254 ? -35.693 7.484   6.344   1.00 43.69  ? 251 ASN B ND2 1 
ATOM   4658 N N   . VAL B 1 255 ? -30.618 8.446   6.884   1.00 45.27  ? 252 VAL B N   1 
ATOM   4659 C CA  . VAL B 1 255 ? -29.191 8.215   6.729   1.00 38.56  ? 252 VAL B CA  1 
ATOM   4660 C C   . VAL B 1 255 ? -28.949 7.576   5.378   1.00 36.80  ? 252 VAL B C   1 
ATOM   4661 O O   . VAL B 1 255 ? -29.613 6.597   5.014   1.00 36.01  ? 252 VAL B O   1 
ATOM   4662 C CB  . VAL B 1 255 ? -28.650 7.332   7.867   1.00 36.54  ? 252 VAL B CB  1 
ATOM   4663 C CG1 . VAL B 1 255 ? -27.374 6.587   7.423   1.00 25.54  ? 252 VAL B CG1 1 
ATOM   4664 C CG2 . VAL B 1 255 ? -28.389 8.189   9.097   1.00 29.75  ? 252 VAL B CG2 1 
ATOM   4665 N N   . GLY B 1 256 ? -27.978 8.114   4.642   1.00 37.19  ? 253 GLY B N   1 
ATOM   4666 C CA  . GLY B 1 256 ? -27.724 7.617   3.304   1.00 41.22  ? 253 GLY B CA  1 
ATOM   4667 C C   . GLY B 1 256 ? -28.789 8.010   2.308   1.00 36.89  ? 253 GLY B C   1 
ATOM   4668 O O   . GLY B 1 256 ? -28.871 7.418   1.228   1.00 32.12  ? 253 GLY B O   1 
ATOM   4669 N N   . SER B 1 257 ? -29.616 8.994   2.661   1.00 35.41  ? 254 SER B N   1 
ATOM   4670 C CA  . SER B 1 257 ? -30.649 9.455   1.759   1.00 38.17  ? 254 SER B CA  1 
ATOM   4671 C C   . SER B 1 257 ? -30.024 10.095  0.528   1.00 40.31  ? 254 SER B C   1 
ATOM   4672 O O   . SER B 1 257 ? -28.908 10.627  0.575   1.00 41.63  ? 254 SER B O   1 
ATOM   4673 C CB  . SER B 1 257 ? -31.577 10.437  2.468   1.00 37.87  ? 254 SER B CB  1 
ATOM   4674 O OG  . SER B 1 257 ? -30.860 11.509  3.011   1.00 35.22  ? 254 SER B OG  1 
ATOM   4675 N N   . GLN B 1 258 ? -30.748 9.996   -0.588  1.00 35.77  ? 255 GLN B N   1 
ATOM   4676 C CA  . GLN B 1 258 ? -30.376 10.594  -1.858  1.00 34.52  ? 255 GLN B CA  1 
ATOM   4677 C C   . GLN B 1 258 ? -31.412 11.631  -2.268  1.00 37.80  ? 255 GLN B C   1 
ATOM   4678 O O   . GLN B 1 258 ? -32.612 11.374  -2.188  1.00 39.22  ? 255 GLN B O   1 
ATOM   4679 C CB  . GLN B 1 258 ? -30.264 9.533   -2.935  1.00 34.51  ? 255 GLN B CB  1 
ATOM   4680 C CG  . GLN B 1 258 ? -29.080 8.656   -2.796  1.00 30.19  ? 255 GLN B CG  1 
ATOM   4681 C CD  . GLN B 1 258 ? -29.126 7.539   -3.771  1.00 37.44  ? 255 GLN B CD  1 
ATOM   4682 O OE1 . GLN B 1 258 ? -30.165 6.920   -3.972  1.00 42.30  ? 255 GLN B OE1 1 
ATOM   4683 N NE2 . GLN B 1 258 ? -28.002 7.265   -4.401  1.00 42.39  ? 255 GLN B NE2 1 
ATOM   4684 N N   . VAL B 1 259 ? -30.945 12.800  -2.715  1.00 33.26  ? 256 VAL B N   1 
ATOM   4685 C CA  . VAL B 1 259 ? -31.787 13.833  -3.305  1.00 27.80  ? 256 VAL B CA  1 
ATOM   4686 C C   . VAL B 1 259 ? -31.297 14.121  -4.720  1.00 39.95  ? 256 VAL B C   1 
ATOM   4687 O O   . VAL B 1 259 ? -30.107 14.397  -4.934  1.00 36.87  ? 256 VAL B O   1 
ATOM   4688 C CB  . VAL B 1 259 ? -31.775 15.129  -2.482  1.00 32.46  ? 256 VAL B CB  1 
ATOM   4689 C CG1 . VAL B 1 259 ? -32.314 16.283  -3.323  1.00 30.03  ? 256 VAL B CG1 1 
ATOM   4690 C CG2 . VAL B 1 259 ? -32.566 14.953  -1.200  1.00 33.12  ? 256 VAL B CG2 1 
ATOM   4691 N N   . ALA B 1 260 ? -32.218 14.077  -5.677  1.00 41.95  ? 257 ALA B N   1 
ATOM   4692 C CA  . ALA B 1 260 ? -31.962 14.441  -7.058  1.00 32.98  ? 257 ALA B CA  1 
ATOM   4693 C C   . ALA B 1 260 ? -32.702 15.735  -7.349  1.00 37.71  ? 257 ALA B C   1 
ATOM   4694 O O   . ALA B 1 260 ? -33.897 15.844  -7.070  1.00 38.35  ? 257 ALA B O   1 
ATOM   4695 C CB  . ALA B 1 260 ? -32.421 13.334  -8.004  1.00 36.38  ? 257 ALA B CB  1 
ATOM   4696 N N   . VAL B 1 261 ? -31.993 16.720  -7.883  1.00 36.74  ? 258 VAL B N   1 
ATOM   4697 C CA  . VAL B 1 261 ? -32.564 18.038  -8.125  1.00 39.01  ? 258 VAL B CA  1 
ATOM   4698 C C   . VAL B 1 261 ? -32.858 18.166  -9.612  1.00 34.62  ? 258 VAL B C   1 
ATOM   4699 O O   . VAL B 1 261 ? -31.948 18.335  -10.431 1.00 32.74  ? 258 VAL B O   1 
ATOM   4700 C CB  . VAL B 1 261 ? -31.646 19.161  -7.634  1.00 39.13  ? 258 VAL B CB  1 
ATOM   4701 C CG1 . VAL B 1 261 ? -32.236 20.518  -8.038  1.00 34.96  ? 258 VAL B CG1 1 
ATOM   4702 C CG2 . VAL B 1 261 ? -31.481 19.062  -6.123  1.00 34.47  ? 258 VAL B CG2 1 
ATOM   4703 N N   . CYS B 1 262 ? -34.141 18.087  -9.947  1.00 39.74  ? 259 CYS B N   1 
ATOM   4704 C CA  . CYS B 1 262 ? -34.645 18.152  -11.312 1.00 39.96  ? 259 CYS B CA  1 
ATOM   4705 C C   . CYS B 1 262 ? -35.011 19.574  -11.723 1.00 39.32  ? 259 CYS B C   1 
ATOM   4706 O O   . CYS B 1 262 ? -34.711 19.998  -12.845 1.00 35.81  ? 259 CYS B O   1 
ATOM   4707 C CB  . CYS B 1 262 ? -35.867 17.247  -11.445 1.00 39.66  ? 259 CYS B CB  1 
ATOM   4708 S SG  . CYS B 1 262 ? -36.265 16.823  -13.120 1.00 47.22  ? 259 CYS B SG  1 
ATOM   4709 N N   . TRP B 1 263 ? -35.646 20.322  -10.827 1.00 38.21  ? 260 TRP B N   1 
ATOM   4710 C CA  . TRP B 1 263 ? -36.042 21.687  -11.124 1.00 34.35  ? 260 TRP B CA  1 
ATOM   4711 C C   . TRP B 1 263 ? -36.243 22.425  -9.808  1.00 37.61  ? 260 TRP B C   1 
ATOM   4712 O O   . TRP B 1 263 ? -36.223 21.834  -8.727  1.00 39.78  ? 260 TRP B O   1 
ATOM   4713 C CB  . TRP B 1 263 ? -37.293 21.705  -12.012 1.00 40.83  ? 260 TRP B CB  1 
ATOM   4714 C CG  . TRP B 1 263 ? -37.163 22.702  -13.115 1.00 44.34  ? 260 TRP B CG  1 
ATOM   4715 C CD1 . TRP B 1 263 ? -36.139 22.805  -14.012 1.00 39.45  ? 260 TRP B CD1 1 
ATOM   4716 C CD2 . TRP B 1 263 ? -38.067 23.761  -13.416 1.00 40.91  ? 260 TRP B CD2 1 
ATOM   4717 N NE1 . TRP B 1 263 ? -36.350 23.865  -14.848 1.00 37.64  ? 260 TRP B NE1 1 
ATOM   4718 C CE2 . TRP B 1 263 ? -37.529 24.470  -14.501 1.00 42.17  ? 260 TRP B CE2 1 
ATOM   4719 C CE3 . TRP B 1 263 ? -39.285 24.173  -12.882 1.00 39.38  ? 260 TRP B CE3 1 
ATOM   4720 C CZ2 . TRP B 1 263 ? -38.171 25.564  -15.061 1.00 42.08  ? 260 TRP B CZ2 1 
ATOM   4721 C CZ3 . TRP B 1 263 ? -39.916 25.262  -13.439 1.00 42.16  ? 260 TRP B CZ3 1 
ATOM   4722 C CH2 . TRP B 1 263 ? -39.363 25.942  -14.515 1.00 43.16  ? 260 TRP B CH2 1 
ATOM   4723 N N   . GLN B 1 264 ? -36.397 23.736  -9.904  1.00 38.67  ? 261 GLN B N   1 
ATOM   4724 C CA  . GLN B 1 264 ? -36.696 24.554  -8.745  1.00 34.86  ? 261 GLN B CA  1 
ATOM   4725 C C   . GLN B 1 264 ? -37.789 25.549  -9.135  1.00 40.05  ? 261 GLN B C   1 
ATOM   4726 O O   . GLN B 1 264 ? -37.589 26.764  -9.123  1.00 38.53  ? 261 GLN B O   1 
ATOM   4727 C CB  . GLN B 1 264 ? -35.452 25.273  -8.223  1.00 35.49  ? 261 GLN B CB  1 
ATOM   4728 C CG  . GLN B 1 264 ? -34.344 24.361  -7.693  1.00 41.96  ? 261 GLN B CG  1 
ATOM   4729 C CD  . GLN B 1 264 ? -34.715 23.623  -6.405  1.00 37.87  ? 261 GLN B CD  1 
ATOM   4730 O OE1 . GLN B 1 264 ? -34.503 24.125  -5.298  1.00 37.76  ? 261 GLN B OE1 1 
ATOM   4731 N NE2 . GLN B 1 264 ? -35.262 22.426  -6.553  1.00 32.05  ? 261 GLN B NE2 1 
ATOM   4732 N N   . TRP B 1 265 ? -38.965 25.009  -9.476  1.00 37.87  ? 262 TRP B N   1 
ATOM   4733 C CA  . TRP B 1 265 ? -40.102 25.836  -9.880  1.00 36.41  ? 262 TRP B CA  1 
ATOM   4734 C C   . TRP B 1 265 ? -40.291 27.030  -8.952  1.00 38.54  ? 262 TRP B C   1 
ATOM   4735 O O   . TRP B 1 265 ? -40.484 28.158  -9.411  1.00 44.31  ? 262 TRP B O   1 
ATOM   4736 C CB  . TRP B 1 265 ? -41.363 24.968  -9.922  1.00 37.42  ? 262 TRP B CB  1 
ATOM   4737 C CG  . TRP B 1 265 ? -42.647 25.655  -10.361 1.00 42.16  ? 262 TRP B CG  1 
ATOM   4738 C CD1 . TRP B 1 265 ? -43.242 26.751  -9.792  1.00 37.91  ? 262 TRP B CD1 1 
ATOM   4739 C CD2 . TRP B 1 265 ? -43.517 25.239  -11.427 1.00 42.33  ? 262 TRP B CD2 1 
ATOM   4740 N NE1 . TRP B 1 265 ? -44.403 27.053  -10.454 1.00 42.82  ? 262 TRP B NE1 1 
ATOM   4741 C CE2 . TRP B 1 265 ? -44.600 26.138  -11.456 1.00 39.45  ? 262 TRP B CE2 1 
ATOM   4742 C CE3 . TRP B 1 265 ? -43.470 24.207  -12.370 1.00 36.57  ? 262 TRP B CE3 1 
ATOM   4743 C CZ2 . TRP B 1 265 ? -45.627 26.038  -12.392 1.00 43.25  ? 262 TRP B CZ2 1 
ATOM   4744 C CZ3 . TRP B 1 265 ? -44.498 24.104  -13.289 1.00 41.69  ? 262 TRP B CZ3 1 
ATOM   4745 C CH2 . TRP B 1 265 ? -45.559 25.018  -13.300 1.00 42.37  ? 262 TRP B CH2 1 
ATOM   4746 N N   . ALA B 1 266 ? -40.239 26.802  -7.635  1.00 40.84  ? 263 ALA B N   1 
ATOM   4747 C CA  . ALA B 1 266 ? -40.470 27.886  -6.684  1.00 39.61  ? 263 ALA B CA  1 
ATOM   4748 C C   . ALA B 1 266 ? -39.488 29.039  -6.862  1.00 40.55  ? 263 ALA B C   1 
ATOM   4749 O O   . ALA B 1 266 ? -39.814 30.180  -6.522  1.00 46.13  ? 263 ALA B O   1 
ATOM   4750 C CB  . ALA B 1 266 ? -40.395 27.356  -5.259  1.00 35.42  ? 263 ALA B CB  1 
ATOM   4751 N N   . THR B 1 267 ? -38.283 28.775  -7.363  1.00 36.67  ? 264 THR B N   1 
ATOM   4752 C CA  . THR B 1 267 ? -37.344 29.862  -7.614  1.00 40.98  ? 264 THR B CA  1 
ATOM   4753 C C   . THR B 1 267 ? -37.418 30.344  -9.061  1.00 40.00  ? 264 THR B C   1 
ATOM   4754 O O   . THR B 1 267 ? -37.463 31.547  -9.318  1.00 39.43  ? 264 THR B O   1 
ATOM   4755 C CB  . THR B 1 267 ? -35.917 29.419  -7.266  1.00 43.09  ? 264 THR B CB  1 
ATOM   4756 O OG1 . THR B 1 267 ? -35.820 29.187  -5.851  1.00 43.04  ? 264 THR B OG1 1 
ATOM   4757 C CG2 . THR B 1 267 ? -34.885 30.476  -7.688  1.00 34.24  ? 264 THR B CG2 1 
ATOM   4758 N N   . GLN B 1 268 ? -37.449 29.406  -10.007 1.00 40.37  ? 265 GLN B N   1 
ATOM   4759 C CA  . GLN B 1 268 ? -37.494 29.751  -11.420 1.00 37.47  ? 265 GLN B CA  1 
ATOM   4760 C C   . GLN B 1 268 ? -38.776 30.509  -11.780 1.00 46.81  ? 265 GLN B C   1 
ATOM   4761 O O   . GLN B 1 268 ? -38.719 31.568  -12.418 1.00 47.40  ? 265 GLN B O   1 
ATOM   4762 C CB  . GLN B 1 268 ? -37.350 28.481  -12.261 1.00 33.76  ? 265 GLN B CB  1 
ATOM   4763 C CG  . GLN B 1 268 ? -37.289 28.752  -13.751 1.00 43.25  ? 265 GLN B CG  1 
ATOM   4764 C CD  . GLN B 1 268 ? -36.150 29.705  -14.144 1.00 45.33  ? 265 GLN B CD  1 
ATOM   4765 O OE1 . GLN B 1 268 ? -35.087 29.729  -13.502 1.00 42.00  ? 265 GLN B OE1 1 
ATOM   4766 N NE2 . GLN B 1 268 ? -36.368 30.488  -15.210 1.00 46.01  ? 265 GLN B NE2 1 
ATOM   4767 N N   . VAL B 1 269 ? -39.942 29.987  -11.380 1.00 46.21  ? 266 VAL B N   1 
ATOM   4768 C CA  . VAL B 1 269 ? -41.237 30.574  -11.768 1.00 43.46  ? 266 VAL B CA  1 
ATOM   4769 C C   . VAL B 1 269 ? -41.756 31.535  -10.707 1.00 41.26  ? 266 VAL B C   1 
ATOM   4770 O O   . VAL B 1 269 ? -42.151 32.658  -11.028 1.00 36.46  ? 266 VAL B O   1 
ATOM   4771 C CB  . VAL B 1 269 ? -42.287 29.472  -12.078 1.00 45.00  ? 266 VAL B CB  1 
ATOM   4772 C CG1 . VAL B 1 269 ? -43.676 30.082  -12.285 1.00 44.39  ? 266 VAL B CG1 1 
ATOM   4773 C CG2 . VAL B 1 269 ? -41.921 28.674  -13.312 1.00 40.65  ? 266 VAL B CG2 1 
ATOM   4774 N N   . GLN B 1 270 ? -41.766 31.117  -9.434  1.00 44.97  ? 267 GLN B N   1 
ATOM   4775 C CA  . GLN B 1 270 ? -42.349 31.916  -8.352  1.00 44.27  ? 267 GLN B CA  1 
ATOM   4776 C C   . GLN B 1 270 ? -41.365 32.895  -7.714  1.00 43.43  ? 267 GLN B C   1 
ATOM   4777 O O   . GLN B 1 270 ? -41.746 33.607  -6.780  1.00 46.99  ? 267 GLN B O   1 
ATOM   4778 C CB  . GLN B 1 270 ? -42.946 31.003  -7.281  1.00 39.20  ? 267 GLN B CB  1 
ATOM   4779 C CG  . GLN B 1 270 ? -44.082 30.111  -7.797  1.00 48.20  ? 267 GLN B CG  1 
ATOM   4780 C CD  . GLN B 1 270 ? -44.755 29.291  -6.684  1.00 60.47  ? 267 GLN B CD  1 
ATOM   4781 O OE1 . GLN B 1 270 ? -44.195 28.303  -6.189  1.00 58.03  ? 267 GLN B OE1 1 
ATOM   4782 N NE2 . GLN B 1 270 ? -45.961 29.703  -6.286  1.00 56.56  ? 267 GLN B NE2 1 
ATOM   4783 N N   . ARG B 1 271 ? -40.122 32.950  -8.206  1.00 46.19  ? 268 ARG B N   1 
ATOM   4784 C CA  . ARG B 1 271 ? -39.109 33.957  -7.867  1.00 43.43  ? 268 ARG B CA  1 
ATOM   4785 C C   . ARG B 1 271 ? -38.744 33.962  -6.383  1.00 50.10  ? 268 ARG B C   1 
ATOM   4786 O O   . ARG B 1 271 ? -38.281 34.984  -5.857  1.00 51.69  ? 268 ARG B O   1 
ATOM   4787 C CB  . ARG B 1 271 ? -39.551 35.351  -8.315  1.00 44.02  ? 268 ARG B CB  1 
ATOM   4788 C CG  . ARG B 1 271 ? -40.290 35.330  -9.664  1.00 57.30  ? 268 ARG B CG  1 
ATOM   4789 C CD  . ARG B 1 271 ? -40.548 36.715  -10.224 1.00 55.44  ? 268 ARG B CD  1 
ATOM   4790 N NE  . ARG B 1 271 ? -39.292 37.407  -10.484 1.00 58.71  ? 268 ARG B NE  1 
ATOM   4791 C CZ  . ARG B 1 271 ? -39.201 38.685  -10.819 1.00 61.42  ? 268 ARG B CZ  1 
ATOM   4792 N NH1 . ARG B 1 271 ? -40.284 39.441  -10.955 1.00 58.33  ? 268 ARG B NH1 1 
ATOM   4793 N NH2 . ARG B 1 271 ? -37.997 39.219  -11.019 1.00 54.46  ? 268 ARG B NH2 1 
ATOM   4794 N N   . ASP B 1 272 ? -38.910 32.831  -5.694  1.00 44.95  ? 269 ASP B N   1 
ATOM   4795 C CA  . ASP B 1 272 ? -38.505 32.726  -4.290  1.00 52.82  ? 269 ASP B CA  1 
ATOM   4796 C C   . ASP B 1 272 ? -37.018 32.391  -4.237  1.00 50.36  ? 269 ASP B C   1 
ATOM   4797 O O   . ASP B 1 272 ? -36.616 31.249  -4.473  1.00 48.80  ? 269 ASP B O   1 
ATOM   4798 C CB  . ASP B 1 272 ? -39.340 31.677  -3.562  1.00 53.46  ? 269 ASP B CB  1 
ATOM   4799 C CG  . ASP B 1 272 ? -39.145 31.719  -2.052  1.00 59.88  ? 269 ASP B CG  1 
ATOM   4800 O OD1 . ASP B 1 272 ? -38.794 32.798  -1.498  1.00 61.14  ? 269 ASP B OD1 1 
ATOM   4801 O OD2 . ASP B 1 272 ? -39.331 30.655  -1.424  1.00 64.68  ? 269 ASP B OD2 1 
ATOM   4802 N N   . TYR B 1 273 ? -36.193 33.385  -3.910  1.00 49.27  ? 270 TYR B N   1 
ATOM   4803 C CA  . TYR B 1 273 ? -34.749 33.219  -3.976  1.00 49.62  ? 270 TYR B CA  1 
ATOM   4804 C C   . TYR B 1 273 ? -34.082 32.993  -2.627  1.00 54.64  ? 270 TYR B C   1 
ATOM   4805 O O   . TYR B 1 273 ? -32.939 32.524  -2.601  1.00 57.94  ? 270 TYR B O   1 
ATOM   4806 C CB  . TYR B 1 273 ? -34.108 34.441  -4.641  1.00 53.25  ? 270 TYR B CB  1 
ATOM   4807 C CG  . TYR B 1 273 ? -34.691 34.756  -6.004  1.00 63.39  ? 270 TYR B CG  1 
ATOM   4808 C CD1 . TYR B 1 273 ? -34.465 33.911  -7.092  1.00 54.30  ? 270 TYR B CD1 1 
ATOM   4809 C CD2 . TYR B 1 273 ? -35.463 35.908  -6.210  1.00 63.74  ? 270 TYR B CD2 1 
ATOM   4810 C CE1 . TYR B 1 273 ? -34.998 34.200  -8.332  1.00 53.96  ? 270 TYR B CE1 1 
ATOM   4811 C CE2 . TYR B 1 273 ? -35.998 36.202  -7.460  1.00 53.96  ? 270 TYR B CE2 1 
ATOM   4812 C CZ  . TYR B 1 273 ? -35.762 35.343  -8.506  1.00 55.27  ? 270 TYR B CZ  1 
ATOM   4813 O OH  . TYR B 1 273 ? -36.299 35.626  -9.733  1.00 66.24  ? 270 TYR B OH  1 
ATOM   4814 N N   . HIS B 1 274 ? -34.733 33.315  -1.510  1.00 57.69  ? 271 HIS B N   1 
ATOM   4815 C CA  . HIS B 1 274 ? -34.145 33.062  -0.201  1.00 50.66  ? 271 HIS B CA  1 
ATOM   4816 C C   . HIS B 1 274 ? -34.989 32.078  0.600   1.00 50.28  ? 271 HIS B C   1 
ATOM   4817 O O   . HIS B 1 274 ? -36.198 31.920  0.372   1.00 49.92  ? 271 HIS B O   1 
ATOM   4818 C CB  . HIS B 1 274 ? -33.946 34.352  0.584   1.00 49.17  ? 271 HIS B CB  1 
ATOM   4819 C CG  . HIS B 1 274 ? -32.805 35.175  0.082   1.00 63.64  ? 271 HIS B CG  1 
ATOM   4820 N ND1 . HIS B 1 274 ? -31.741 35.541  0.882   1.00 66.52  ? 271 HIS B ND1 1 
ATOM   4821 C CD2 . HIS B 1 274 ? -32.542 35.676  -1.152  1.00 62.00  ? 271 HIS B CD2 1 
ATOM   4822 C CE1 . HIS B 1 274 ? -30.880 36.249  0.167   1.00 70.10  ? 271 HIS B CE1 1 
ATOM   4823 N NE2 . HIS B 1 274 ? -31.342 36.346  -1.071  1.00 66.20  ? 271 HIS B NE2 1 
ATOM   4824 N N   . GLY B 1 275 ? -34.311 31.414  1.535   1.00 47.69  ? 272 GLY B N   1 
ATOM   4825 C CA  . GLY B 1 275 ? -34.858 30.344  2.333   1.00 44.60  ? 272 GLY B CA  1 
ATOM   4826 C C   . GLY B 1 275 ? -33.878 29.907  3.408   1.00 43.58  ? 272 GLY B C   1 
ATOM   4827 O O   . GLY B 1 275 ? -32.769 30.446  3.547   1.00 37.02  ? 272 GLY B O   1 
ATOM   4828 N N   . PRO B 1 276 ? -34.288 28.939  4.223   1.00 53.61  ? 273 PRO B N   1 
ATOM   4829 C CA  . PRO B 1 276 ? -33.352 28.368  5.199   1.00 52.54  ? 273 PRO B CA  1 
ATOM   4830 C C   . PRO B 1 276 ? -32.157 27.759  4.491   1.00 48.45  ? 273 PRO B C   1 
ATOM   4831 O O   . PRO B 1 276 ? -32.276 27.161  3.419   1.00 42.07  ? 273 PRO B O   1 
ATOM   4832 C CB  . PRO B 1 276 ? -34.182 27.301  5.926   1.00 42.10  ? 273 PRO B CB  1 
ATOM   4833 C CG  . PRO B 1 276 ? -35.404 27.096  5.072   1.00 46.63  ? 273 PRO B CG  1 
ATOM   4834 C CD  . PRO B 1 276 ? -35.646 28.382  4.358   1.00 49.54  ? 273 PRO B CD  1 
ATOM   4835 N N   . ARG B 1 277 ? -30.994 27.937  5.084   1.00 48.67  ? 274 ARG B N   1 
ATOM   4836 C CA  . ARG B 1 277 ? -29.841 27.232  4.581   1.00 39.93  ? 274 ARG B CA  1 
ATOM   4837 C C   . ARG B 1 277 ? -30.074 25.745  4.775   1.00 45.66  ? 274 ARG B C   1 
ATOM   4838 O O   . ARG B 1 277 ? -30.403 25.300  5.878   1.00 43.68  ? 274 ARG B O   1 
ATOM   4839 C CB  . ARG B 1 277 ? -28.597 27.727  5.283   1.00 45.27  ? 274 ARG B CB  1 
ATOM   4840 C CG  . ARG B 1 277 ? -28.356 29.201  4.986   1.00 49.68  ? 274 ARG B CG  1 
ATOM   4841 C CD  . ARG B 1 277 ? -26.957 29.548  5.395   1.00 54.69  ? 274 ARG B CD  1 
ATOM   4842 N NE  . ARG B 1 277 ? -26.600 30.951  5.229   1.00 56.29  ? 274 ARG B NE  1 
ATOM   4843 C CZ  . ARG B 1 277 ? -26.213 31.499  4.087   1.00 51.29  ? 274 ARG B CZ  1 
ATOM   4844 N NH1 . ARG B 1 277 ? -26.313 30.844  2.938   1.00 49.17  ? 274 ARG B NH1 1 
ATOM   4845 N NH2 . ARG B 1 277 ? -25.720 32.735  4.099   1.00 44.25  ? 274 ARG B NH2 1 
ATOM   4846 N N   . LEU B 1 278 ? -29.997 25.002  3.672   1.00 50.39  ? 275 LEU B N   1 
ATOM   4847 C CA  . LEU B 1 278 ? -30.293 23.577  3.629   1.00 45.63  ? 275 LEU B CA  1 
ATOM   4848 C C   . LEU B 1 278 ? -29.067 22.711  3.878   1.00 48.03  ? 275 LEU B C   1 
ATOM   4849 O O   . LEU B 1 278 ? -29.197 21.630  4.461   1.00 46.47  ? 275 LEU B O   1 
ATOM   4850 C CB  . LEU B 1 278 ? -30.902 23.203  2.270   1.00 43.07  ? 275 LEU B CB  1 
ATOM   4851 C CG  . LEU B 1 278 ? -32.316 23.712  1.971   1.00 45.62  ? 275 LEU B CG  1 
ATOM   4852 C CD1 . LEU B 1 278 ? -32.949 22.946  0.847   1.00 40.60  ? 275 LEU B CD1 1 
ATOM   4853 C CD2 . LEU B 1 278 ? -33.174 23.575  3.212   1.00 49.32  ? 275 LEU B CD2 1 
ATOM   4854 N N   . LEU B 1 279 ? -27.884 23.151  3.444   1.00 48.86  ? 276 LEU B N   1 
ATOM   4855 C CA  . LEU B 1 279 ? -26.677 22.345  3.623   1.00 43.68  ? 276 LEU B CA  1 
ATOM   4856 C C   . LEU B 1 279 ? -26.452 21.897  5.064   1.00 42.51  ? 276 LEU B C   1 
ATOM   4857 O O   . LEU B 1 279 ? -26.066 20.734  5.257   1.00 38.67  ? 276 LEU B O   1 
ATOM   4858 C CB  . LEU B 1 279 ? -25.442 23.104  3.102   1.00 39.13  ? 276 LEU B CB  1 
ATOM   4859 C CG  . LEU B 1 279 ? -25.303 23.340  1.596   1.00 34.90  ? 276 LEU B CG  1 
ATOM   4860 C CD1 . LEU B 1 279 ? -23.939 23.909  1.281   1.00 30.20  ? 276 LEU B CD1 1 
ATOM   4861 C CD2 . LEU B 1 279 ? -25.534 22.058  0.832   1.00 34.46  ? 276 LEU B CD2 1 
ATOM   4862 N N   . PRO B 1 280 ? -26.680 22.723  6.106   1.00 44.61  ? 277 PRO B N   1 
ATOM   4863 C CA  . PRO B 1 280 ? -26.427 22.246  7.475   1.00 38.29  ? 277 PRO B CA  1 
ATOM   4864 C C   . PRO B 1 280 ? -27.307 21.098  7.961   1.00 39.59  ? 277 PRO B C   1 
ATOM   4865 O O   . PRO B 1 280 ? -27.137 20.640  9.092   1.00 49.50  ? 277 PRO B O   1 
ATOM   4866 C CB  . PRO B 1 280 ? -26.644 23.502  8.334   1.00 38.52  ? 277 PRO B CB  1 
ATOM   4867 C CG  . PRO B 1 280 ? -27.255 24.508  7.459   1.00 43.13  ? 277 PRO B CG  1 
ATOM   4868 C CD  . PRO B 1 280 ? -26.830 24.189  6.071   1.00 43.76  ? 277 PRO B CD  1 
ATOM   4869 N N   . TYR B 1 281 ? -28.222 20.607  7.138   1.00 40.36  ? 278 TYR B N   1 
ATOM   4870 C CA  . TYR B 1 281 ? -29.111 19.514  7.508   1.00 37.39  ? 278 TYR B CA  1 
ATOM   4871 C C   . TYR B 1 281 ? -28.708 18.195  6.888   1.00 34.86  ? 278 TYR B C   1 
ATOM   4872 O O   . TYR B 1 281 ? -29.399 17.190  7.078   1.00 31.78  ? 278 TYR B O   1 
ATOM   4873 C CB  . TYR B 1 281 ? -30.549 19.835  7.086   1.00 40.82  ? 278 TYR B CB  1 
ATOM   4874 C CG  . TYR B 1 281 ? -31.204 20.897  7.935   1.00 47.61  ? 278 TYR B CG  1 
ATOM   4875 C CD1 . TYR B 1 281 ? -31.108 22.243  7.606   1.00 45.33  ? 278 TYR B CD1 1 
ATOM   4876 C CD2 . TYR B 1 281 ? -31.911 20.549  9.083   1.00 52.38  ? 278 TYR B CD2 1 
ATOM   4877 C CE1 . TYR B 1 281 ? -31.711 23.215  8.388   1.00 54.26  ? 278 TYR B CE1 1 
ATOM   4878 C CE2 . TYR B 1 281 ? -32.513 21.506  9.871   1.00 52.47  ? 278 TYR B CE2 1 
ATOM   4879 C CZ  . TYR B 1 281 ? -32.413 22.840  9.525   1.00 62.92  ? 278 TYR B CZ  1 
ATOM   4880 O OH  . TYR B 1 281 ? -33.017 23.799  10.320  1.00 74.37  ? 278 TYR B OH  1 
ATOM   4881 N N   . ILE B 1 282 ? -27.630 18.178  6.125   1.00 33.22  ? 279 ILE B N   1 
ATOM   4882 C CA  . ILE B 1 282 ? -27.265 16.993  5.369   1.00 35.11  ? 279 ILE B CA  1 
ATOM   4883 C C   . ILE B 1 282 ? -26.048 16.294  5.934   1.00 31.83  ? 279 ILE B C   1 
ATOM   4884 O O   . ILE B 1 282 ? -25.758 15.161  5.514   1.00 32.55  ? 279 ILE B O   1 
ATOM   4885 C CB  . ILE B 1 282 ? -27.039 17.326  3.879   1.00 29.83  ? 279 ILE B CB  1 
ATOM   4886 C CG1 . ILE B 1 282 ? -25.735 18.099  3.676   1.00 24.60  ? 279 ILE B CG1 1 
ATOM   4887 C CG2 . ILE B 1 282 ? -28.211 18.101  3.352   1.00 35.48  ? 279 ILE B CG2 1 
ATOM   4888 C CD1 . ILE B 1 282 ? -25.223 18.054  2.275   1.00 27.85  ? 279 ILE B CD1 1 
ATOM   4889 N N   . MET B 1 283 ? -25.336 16.914  6.875   1.00 31.78  ? 280 MET B N   1 
ATOM   4890 C CA  . MET B 1 283 ? -24.070 16.359  7.346   1.00 33.28  ? 280 MET B CA  1 
ATOM   4891 C C   . MET B 1 283 ? -24.276 15.074  8.132   1.00 36.51  ? 280 MET B C   1 
ATOM   4892 O O   . MET B 1 283 ? -23.687 14.037  7.810   1.00 37.56  ? 280 MET B O   1 
ATOM   4893 C CB  . MET B 1 283 ? -23.347 17.372  8.208   1.00 32.24  ? 280 MET B CB  1 
ATOM   4894 C CG  . MET B 1 283 ? -22.779 18.507  7.462   1.00 33.67  ? 280 MET B CG  1 
ATOM   4895 S SD  . MET B 1 283 ? -22.240 19.665  8.696   1.00 37.98  ? 280 MET B SD  1 
ATOM   4896 C CE  . MET B 1 283 ? -23.759 20.544  8.983   1.00 35.94  ? 280 MET B CE  1 
ATOM   4897 N N   . PHE B 1 284 ? -25.086 15.122  9.189   1.00 37.37  ? 281 PHE B N   1 
ATOM   4898 C CA  . PHE B 1 284 ? -25.340 13.888  9.927   1.00 41.31  ? 281 PHE B CA  1 
ATOM   4899 C C   . PHE B 1 284 ? -25.999 12.824  9.066   1.00 38.98  ? 281 PHE B C   1 
ATOM   4900 O O   . PHE B 1 284 ? -25.626 11.647  9.210   1.00 35.50  ? 281 PHE B O   1 
ATOM   4901 C CB  . PHE B 1 284 ? -26.186 14.128  11.194  1.00 46.57  ? 281 PHE B CB  1 
ATOM   4902 C CG  . PHE B 1 284 ? -26.630 12.835  11.859  1.00 47.71  ? 281 PHE B CG  1 
ATOM   4903 C CD1 . PHE B 1 284 ? -25.792 12.171  12.759  1.00 48.64  ? 281 PHE B CD1 1 
ATOM   4904 C CD2 . PHE B 1 284 ? -27.858 12.247  11.541  1.00 43.66  ? 281 PHE B CD2 1 
ATOM   4905 C CE1 . PHE B 1 284 ? -26.180 10.961  13.343  1.00 45.35  ? 281 PHE B CE1 1 
ATOM   4906 C CE2 . PHE B 1 284 ? -28.244 11.032  12.117  1.00 42.41  ? 281 PHE B CE2 1 
ATOM   4907 C CZ  . PHE B 1 284 ? -27.404 10.391  13.013  1.00 42.97  ? 281 PHE B CZ  1 
ATOM   4908 N N   . PRO B 1 285 ? -26.985 13.136  8.213   1.00 40.96  ? 282 PRO B N   1 
ATOM   4909 C CA  . PRO B 1 285 ? -27.609 12.081  7.392   1.00 36.45  ? 282 PRO B CA  1 
ATOM   4910 C C   . PRO B 1 285 ? -26.708 11.514  6.330   1.00 34.89  ? 282 PRO B C   1 
ATOM   4911 O O   . PRO B 1 285 ? -27.082 10.497  5.725   1.00 35.18  ? 282 PRO B O   1 
ATOM   4912 C CB  . PRO B 1 285 ? -28.799 12.786  6.740   1.00 36.48  ? 282 PRO B CB  1 
ATOM   4913 C CG  . PRO B 1 285 ? -29.064 13.970  7.591   1.00 38.43  ? 282 PRO B CG  1 
ATOM   4914 C CD  . PRO B 1 285 ? -27.762 14.389  8.177   1.00 39.47  ? 282 PRO B CD  1 
ATOM   4915 N N   . ARG B 1 286 ? -25.548 12.123  6.086   1.00 33.36  ? 283 ARG B N   1 
ATOM   4916 C CA  . ARG B 1 286 ? -24.720 11.796  4.924   1.00 33.71  ? 283 ARG B CA  1 
ATOM   4917 C C   . ARG B 1 286 ? -25.572 11.781  3.657   1.00 32.58  ? 283 ARG B C   1 
ATOM   4918 O O   . ARG B 1 286 ? -25.517 10.851  2.844   1.00 32.31  ? 283 ARG B O   1 
ATOM   4919 C CB  . ARG B 1 286 ? -23.999 10.459  5.095   1.00 35.28  ? 283 ARG B CB  1 
ATOM   4920 C CG  . ARG B 1 286 ? -22.935 10.421  6.163   1.00 35.71  ? 283 ARG B CG  1 
ATOM   4921 C CD  . ARG B 1 286 ? -23.541 10.168  7.504   1.00 31.84  ? 283 ARG B CD  1 
ATOM   4922 N NE  . ARG B 1 286 ? -23.537 8.771   7.908   1.00 36.83  ? 283 ARG B NE  1 
ATOM   4923 C CZ  . ARG B 1 286 ? -24.202 8.313   8.963   1.00 32.63  ? 283 ARG B CZ  1 
ATOM   4924 N NH1 . ARG B 1 286 ? -24.938 9.112   9.719   1.00 28.93  ? 283 ARG B NH1 1 
ATOM   4925 N NH2 . ARG B 1 286 ? -24.144 7.018   9.254   1.00 32.18  ? 283 ARG B NH2 1 
ATOM   4926 N N   . ALA B 1 287 ? -26.401 12.812  3.509   1.00 31.83  ? 284 ALA B N   1 
ATOM   4927 C CA  . ALA B 1 287 ? -27.257 12.890  2.338   1.00 31.63  ? 284 ALA B CA  1 
ATOM   4928 C C   . ALA B 1 287 ? -26.418 13.188  1.101   1.00 33.17  ? 284 ALA B C   1 
ATOM   4929 O O   . ALA B 1 287 ? -25.457 13.957  1.150   1.00 27.51  ? 284 ALA B O   1 
ATOM   4930 C CB  . ALA B 1 287 ? -28.313 13.961  2.542   1.00 29.08  ? 284 ALA B CB  1 
ATOM   4931 N N   . THR B 1 288 ? -26.757 12.552  -0.007  1.00 31.78  ? 285 THR B N   1 
ATOM   4932 C CA  . THR B 1 288 ? -26.139 12.862  -1.286  1.00 32.01  ? 285 THR B CA  1 
ATOM   4933 C C   . THR B 1 288 ? -27.151 13.631  -2.131  1.00 34.96  ? 285 THR B C   1 
ATOM   4934 O O   . THR B 1 288 ? -28.292 13.186  -2.284  1.00 36.53  ? 285 THR B O   1 
ATOM   4935 C CB  . THR B 1 288 ? -25.662 11.584  -1.991  1.00 34.58  ? 285 THR B CB  1 
ATOM   4936 O OG1 . THR B 1 288 ? -24.676 10.930  -1.176  1.00 36.54  ? 285 THR B OG1 1 
ATOM   4937 C CG2 . THR B 1 288 ? -25.042 11.909  -3.356  1.00 35.22  ? 285 THR B CG2 1 
ATOM   4938 N N   . ILE B 1 289 ? -26.745 14.800  -2.639  1.00 30.19  ? 286 ILE B N   1 
ATOM   4939 C CA  . ILE B 1 289 ? -27.584 15.676  -3.461  1.00 27.13  ? 286 ILE B CA  1 
ATOM   4940 C C   . ILE B 1 289 ? -26.928 15.812  -4.821  1.00 31.66  ? 286 ILE B C   1 
ATOM   4941 O O   . ILE B 1 289 ? -25.762 16.215  -4.910  1.00 34.62  ? 286 ILE B O   1 
ATOM   4942 C CB  . ILE B 1 289 ? -27.742 17.069  -2.831  1.00 27.41  ? 286 ILE B CB  1 
ATOM   4943 C CG1 . ILE B 1 289 ? -28.179 16.949  -1.379  1.00 25.83  ? 286 ILE B CG1 1 
ATOM   4944 C CG2 . ILE B 1 289 ? -28.694 17.912  -3.643  1.00 28.27  ? 286 ILE B CG2 1 
ATOM   4945 C CD1 . ILE B 1 289 ? -28.160 18.225  -0.674  1.00 27.96  ? 286 ILE B CD1 1 
ATOM   4946 N N   . ARG B 1 290 ? -27.664 15.494  -5.879  1.00 29.36  ? 287 ARG B N   1 
ATOM   4947 C CA  . ARG B 1 290 ? -27.112 15.566  -7.224  1.00 28.20  ? 287 ARG B CA  1 
ATOM   4948 C C   . ARG B 1 290 ? -28.006 16.391  -8.143  1.00 35.21  ? 287 ARG B C   1 
ATOM   4949 O O   . ARG B 1 290 ? -29.196 16.094  -8.295  1.00 33.22  ? 287 ARG B O   1 
ATOM   4950 C CB  . ARG B 1 290 ? -26.934 14.186  -7.820  1.00 27.08  ? 287 ARG B CB  1 
ATOM   4951 C CG  . ARG B 1 290 ? -26.289 14.261  -9.134  1.00 29.32  ? 287 ARG B CG  1 
ATOM   4952 C CD  . ARG B 1 290 ? -26.310 12.950  -9.799  1.00 34.70  ? 287 ARG B CD  1 
ATOM   4953 N NE  . ARG B 1 290 ? -25.315 12.873  -10.869 1.00 43.19  ? 287 ARG B NE  1 
ATOM   4954 C CZ  . ARG B 1 290 ? -25.477 13.340  -12.102 1.00 35.81  ? 287 ARG B CZ  1 
ATOM   4955 N NH1 . ARG B 1 290 ? -26.545 14.047  -12.441 1.00 37.18  ? 287 ARG B NH1 1 
ATOM   4956 N NH2 . ARG B 1 290 ? -24.547 13.088  -13.021 1.00 30.77  ? 287 ARG B NH2 1 
ATOM   4957 N N   . GLY B 1 291 ? -27.425 17.401  -8.786  1.00 35.12  ? 288 GLY B N   1 
ATOM   4958 C CA  . GLY B 1 291 ? -28.146 18.118  -9.828  1.00 31.29  ? 288 GLY B CA  1 
ATOM   4959 C C   . GLY B 1 291 ? -28.354 17.233  -11.044 1.00 28.20  ? 288 GLY B C   1 
ATOM   4960 O O   . GLY B 1 291 ? -27.489 16.437  -11.418 1.00 26.73  ? 288 GLY B O   1 
ATOM   4961 N N   . ILE B 1 292 ? -29.525 17.363  -11.664 1.00 33.26  ? 289 ILE B N   1 
ATOM   4962 C CA  . ILE B 1 292 ? -29.859 16.610  -12.876 1.00 30.99  ? 289 ILE B CA  1 
ATOM   4963 C C   . ILE B 1 292 ? -29.817 17.544  -14.083 1.00 30.31  ? 289 ILE B C   1 
ATOM   4964 O O   . ILE B 1 292 ? -30.280 18.688  -14.021 1.00 32.45  ? 289 ILE B O   1 
ATOM   4965 C CB  . ILE B 1 292 ? -31.236 15.926  -12.789 1.00 29.65  ? 289 ILE B CB  1 
ATOM   4966 C CG1 . ILE B 1 292 ? -31.430 15.230  -11.443 1.00 27.86  ? 289 ILE B CG1 1 
ATOM   4967 C CG2 . ILE B 1 292 ? -31.362 14.914  -13.907 1.00 31.14  ? 289 ILE B CG2 1 
ATOM   4968 C CD1 . ILE B 1 292 ? -30.548 14.013  -11.259 1.00 30.01  ? 289 ILE B CD1 1 
ATOM   4969 N N   . PHE B 1 293 ? -29.269 17.045  -15.187 1.00 31.63  ? 290 PHE B N   1 
ATOM   4970 C CA  . PHE B 1 293 ? -29.230 17.749  -16.471 1.00 32.51  ? 290 PHE B CA  1 
ATOM   4971 C C   . PHE B 1 293 ? -29.201 16.650  -17.538 1.00 29.96  ? 290 PHE B C   1 
ATOM   4972 O O   . PHE B 1 293 ? -28.163 16.276  -18.084 1.00 27.19  ? 290 PHE B O   1 
ATOM   4973 C CB  . PHE B 1 293 ? -28.034 18.694  -16.579 1.00 30.57  ? 290 PHE B CB  1 
ATOM   4974 C CG  . PHE B 1 293 ? -28.098 19.626  -17.755 1.00 32.07  ? 290 PHE B CG  1 
ATOM   4975 C CD1 . PHE B 1 293 ? -28.889 20.776  -17.709 1.00 34.52  ? 290 PHE B CD1 1 
ATOM   4976 C CD2 . PHE B 1 293 ? -27.346 19.370  -18.912 1.00 31.34  ? 290 PHE B CD2 1 
ATOM   4977 C CE1 . PHE B 1 293 ? -28.934 21.650  -18.816 1.00 33.96  ? 290 PHE B CE1 1 
ATOM   4978 C CE2 . PHE B 1 293 ? -27.387 20.216  -19.997 1.00 25.39  ? 290 PHE B CE2 1 
ATOM   4979 C CZ  . PHE B 1 293 ? -28.183 21.365  -19.951 1.00 31.31  ? 290 PHE B CZ  1 
ATOM   4980 N N   . SER B 1 294 ? -30.383 16.117  -17.827 1.00 31.76  ? 291 SER B N   1 
ATOM   4981 C CA  . SER B 1 294 ? -30.501 14.868  -18.575 1.00 36.84  ? 291 SER B CA  1 
ATOM   4982 C C   . SER B 1 294 ? -29.851 14.910  -19.959 1.00 36.21  ? 291 SER B C   1 
ATOM   4983 O O   . SER B 1 294 ? -29.541 13.849  -20.515 1.00 37.14  ? 291 SER B O   1 
ATOM   4984 C CB  . SER B 1 294 ? -31.976 14.497  -18.695 1.00 39.72  ? 291 SER B CB  1 
ATOM   4985 O OG  . SER B 1 294 ? -32.736 15.620  -19.110 1.00 39.10  ? 291 SER B OG  1 
ATOM   4986 N N   . LEU B 1 295 ? -29.613 16.096  -20.521 1.00 33.35  ? 292 LEU B N   1 
ATOM   4987 C CA  . LEU B 1 295 ? -28.847 16.172  -21.758 1.00 32.07  ? 292 LEU B CA  1 
ATOM   4988 C C   . LEU B 1 295 ? -27.584 15.311  -21.730 1.00 32.12  ? 292 LEU B C   1 
ATOM   4989 O O   . LEU B 1 295 ? -27.112 14.895  -22.795 1.00 34.53  ? 292 LEU B O   1 
ATOM   4990 C CB  . LEU B 1 295 ? -28.479 17.627  -22.068 1.00 29.30  ? 292 LEU B CB  1 
ATOM   4991 C CG  . LEU B 1 295 ? -29.580 18.504  -22.665 1.00 33.55  ? 292 LEU B CG  1 
ATOM   4992 C CD1 . LEU B 1 295 ? -28.985 19.807  -23.152 1.00 35.00  ? 292 LEU B CD1 1 
ATOM   4993 C CD2 . LEU B 1 295 ? -30.301 17.785  -23.797 1.00 33.06  ? 292 LEU B CD2 1 
ATOM   4994 N N   . GLU B 1 296 ? -27.034 15.012  -20.542 1.00 34.24  ? 293 GLU B N   1 
ATOM   4995 C CA  . GLU B 1 296 ? -25.815 14.210  -20.488 1.00 31.81  ? 293 GLU B CA  1 
ATOM   4996 C C   . GLU B 1 296 ? -26.062 12.760  -20.863 1.00 34.97  ? 293 GLU B C   1 
ATOM   4997 O O   . GLU B 1 296 ? -25.129 12.085  -21.310 1.00 37.23  ? 293 GLU B O   1 
ATOM   4998 C CB  . GLU B 1 296 ? -25.157 14.285  -19.113 1.00 31.75  ? 293 GLU B CB  1 
ATOM   4999 C CG  . GLU B 1 296 ? -25.907 13.621  -17.958 1.00 34.38  ? 293 GLU B CG  1 
ATOM   5000 C CD  . GLU B 1 296 ? -25.089 13.613  -16.660 1.00 34.93  ? 293 GLU B CD  1 
ATOM   5001 O OE1 . GLU B 1 296 ? -23.845 13.653  -16.752 1.00 35.67  ? 293 GLU B OE1 1 
ATOM   5002 O OE2 . GLU B 1 296 ? -25.679 13.577  -15.552 1.00 35.74  ? 293 GLU B OE2 1 
ATOM   5003 N N   . TRP B 1 297 ? -27.292 12.275  -20.724 1.00 35.43  ? 294 TRP B N   1 
ATOM   5004 C CA  . TRP B 1 297 ? -27.603 10.894  -21.060 1.00 39.36  ? 294 TRP B CA  1 
ATOM   5005 C C   . TRP B 1 297 ? -28.035 10.703  -22.519 1.00 41.38  ? 294 TRP B C   1 
ATOM   5006 O O   . TRP B 1 297 ? -28.201 9.561   -22.956 1.00 43.76  ? 294 TRP B O   1 
ATOM   5007 C CB  . TRP B 1 297 ? -28.668 10.375  -20.088 1.00 32.34  ? 294 TRP B CB  1 
ATOM   5008 C CG  . TRP B 1 297 ? -28.180 10.421  -18.690 1.00 33.95  ? 294 TRP B CG  1 
ATOM   5009 C CD1 . TRP B 1 297 ? -26.915 10.129  -18.264 1.00 35.87  ? 294 TRP B CD1 1 
ATOM   5010 C CD2 . TRP B 1 297 ? -28.913 10.811  -17.519 1.00 37.55  ? 294 TRP B CD2 1 
ATOM   5011 N NE1 . TRP B 1 297 ? -26.821 10.293  -16.902 1.00 28.32  ? 294 TRP B NE1 1 
ATOM   5012 C CE2 . TRP B 1 297 ? -28.030 10.719  -16.422 1.00 33.16  ? 294 TRP B CE2 1 
ATOM   5013 C CE3 . TRP B 1 297 ? -30.229 11.215  -17.284 1.00 36.00  ? 294 TRP B CE3 1 
ATOM   5014 C CZ2 . TRP B 1 297 ? -28.424 11.016  -15.113 1.00 33.73  ? 294 TRP B CZ2 1 
ATOM   5015 C CZ3 . TRP B 1 297 ? -30.610 11.514  -15.976 1.00 36.54  ? 294 TRP B CZ3 1 
ATOM   5016 C CH2 . TRP B 1 297 ? -29.711 11.412  -14.912 1.00 27.97  ? 294 TRP B CH2 1 
ATOM   5017 N N   . PHE B 1 298 ? -28.178 11.776  -23.300 1.00 42.76  ? 295 PHE B N   1 
ATOM   5018 C CA  . PHE B 1 298 ? -28.599 11.663  -24.702 1.00 41.26  ? 295 PHE B CA  1 
ATOM   5019 C C   . PHE B 1 298 ? -27.474 11.025  -25.518 1.00 38.53  ? 295 PHE B C   1 
ATOM   5020 O O   . PHE B 1 298 ? -26.727 11.688  -26.235 1.00 36.21  ? 295 PHE B O   1 
ATOM   5021 C CB  . PHE B 1 298 ? -28.991 13.025  -25.282 1.00 38.10  ? 295 PHE B CB  1 
ATOM   5022 C CG  . PHE B 1 298 ? -30.309 13.581  -24.751 1.00 36.46  ? 295 PHE B CG  1 
ATOM   5023 C CD1 . PHE B 1 298 ? -30.737 13.314  -23.465 1.00 35.49  ? 295 PHE B CD1 1 
ATOM   5024 C CD2 . PHE B 1 298 ? -31.112 14.374  -25.558 1.00 38.43  ? 295 PHE B CD2 1 
ATOM   5025 C CE1 . PHE B 1 298 ? -31.934 13.826  -22.993 1.00 36.68  ? 295 PHE B CE1 1 
ATOM   5026 C CE2 . PHE B 1 298 ? -32.311 14.883  -25.090 1.00 38.19  ? 295 PHE B CE2 1 
ATOM   5027 C CZ  . PHE B 1 298 ? -32.721 14.608  -23.806 1.00 36.51  ? 295 PHE B CZ  1 
ATOM   5028 N N   . THR B 1 299 ? -27.357 9.704   -25.405 1.00 40.23  ? 296 THR B N   1 
ATOM   5029 C CA  . THR B 1 299 ? -26.365 8.926   -26.136 1.00 42.28  ? 296 THR B CA  1 
ATOM   5030 C C   . THR B 1 299 ? -27.071 7.774   -26.839 1.00 47.83  ? 296 THR B C   1 
ATOM   5031 O O   . THR B 1 299 ? -28.135 7.321   -26.393 1.00 47.28  ? 296 THR B O   1 
ATOM   5032 C CB  . THR B 1 299 ? -25.240 8.387   -25.189 1.00 47.76  ? 296 THR B CB  1 
ATOM   5033 O OG1 . THR B 1 299 ? -25.701 7.255   -24.433 1.00 45.23  ? 296 THR B OG1 1 
ATOM   5034 C CG2 . THR B 1 299 ? -24.790 9.471   -24.209 1.00 43.73  ? 296 THR B CG2 1 
ATOM   5035 N N   . GLU B 1 300 ? -26.486 7.301   -27.949 1.00 46.14  ? 297 GLU B N   1 
ATOM   5036 C CA  . GLU B 1 300 ? -27.127 6.214   -28.691 1.00 49.31  ? 297 GLU B CA  1 
ATOM   5037 C C   . GLU B 1 300 ? -27.360 5.000   -27.795 1.00 51.45  ? 297 GLU B C   1 
ATOM   5038 O O   . GLU B 1 300 ? -28.459 4.432   -27.774 1.00 50.91  ? 297 GLU B O   1 
ATOM   5039 C CB  . GLU B 1 300 ? -26.301 5.824   -29.917 1.00 54.72  ? 297 GLU B CB  1 
ATOM   5040 C CG  . GLU B 1 300 ? -26.748 4.497   -30.554 1.00 65.79  ? 297 GLU B CG  1 
ATOM   5041 C CD  . GLU B 1 300 ? -26.028 4.190   -31.865 1.00 81.98  ? 297 GLU B CD  1 
ATOM   5042 O OE1 . GLU B 1 300 ? -24.880 4.667   -32.024 1.00 76.13  ? 297 GLU B OE1 1 
ATOM   5043 O OE2 . GLU B 1 300 ? -26.612 3.485   -32.732 1.00 76.23  ? 297 GLU B OE2 1 
ATOM   5044 N N   . GLN B 1 301 ? -26.338 4.599   -27.032 1.00 51.49  ? 298 GLN B N   1 
ATOM   5045 C CA  . GLN B 1 301 ? -26.488 3.461   -26.131 1.00 50.84  ? 298 GLN B CA  1 
ATOM   5046 C C   . GLN B 1 301 ? -27.624 3.689   -25.145 1.00 49.58  ? 298 GLN B C   1 
ATOM   5047 O O   . GLN B 1 301 ? -28.373 2.761   -24.819 1.00 55.80  ? 298 GLN B O   1 
ATOM   5048 C CB  . GLN B 1 301 ? -25.180 3.188   -25.377 1.00 52.62  ? 298 GLN B CB  1 
ATOM   5049 C CG  . GLN B 1 301 ? -25.209 1.876   -24.586 1.00 64.58  ? 298 GLN B CG  1 
ATOM   5050 C CD  . GLN B 1 301 ? -24.397 1.911   -23.291 1.00 74.60  ? 298 GLN B CD  1 
ATOM   5051 O OE1 . GLN B 1 301 ? -24.853 2.431   -22.262 1.00 71.90  ? 298 GLN B OE1 1 
ATOM   5052 N NE2 . GLN B 1 301 ? -23.199 1.330   -23.332 1.00 69.49  ? 298 GLN B NE2 1 
ATOM   5053 N N   . ASN B 1 302 ? -27.776 4.920   -24.658 1.00 47.24  ? 299 ASN B N   1 
ATOM   5054 C CA  . ASN B 1 302 ? -28.781 5.153   -23.629 1.00 49.95  ? 299 ASN B CA  1 
ATOM   5055 C C   . ASN B 1 302 ? -30.193 5.152   -24.197 1.00 51.50  ? 299 ASN B C   1 
ATOM   5056 O O   . ASN B 1 302 ? -31.147 4.836   -23.474 1.00 44.89  ? 299 ASN B O   1 
ATOM   5057 C CB  . ASN B 1 302 ? -28.494 6.460   -22.904 1.00 45.15  ? 299 ASN B CB  1 
ATOM   5058 C CG  . ASN B 1 302 ? -27.485 6.288   -21.800 1.00 50.85  ? 299 ASN B CG  1 
ATOM   5059 O OD1 . ASN B 1 302 ? -27.621 5.397   -20.956 1.00 53.64  ? 299 ASN B OD1 1 
ATOM   5060 N ND2 . ASN B 1 302 ? -26.447 7.119   -21.811 1.00 45.25  ? 299 ASN B ND2 1 
ATOM   5061 N N   . TRP B 1 303 ? -30.357 5.510   -25.475 1.00 47.12  ? 300 TRP B N   1 
ATOM   5062 C CA  . TRP B 1 303 ? -31.697 5.480   -26.049 1.00 50.49  ? 300 TRP B CA  1 
ATOM   5063 C C   . TRP B 1 303 ? -32.167 4.043   -26.252 1.00 50.00  ? 300 TRP B C   1 
ATOM   5064 O O   . TRP B 1 303 ? -33.269 3.678   -25.823 1.00 47.12  ? 300 TRP B O   1 
ATOM   5065 C CB  . TRP B 1 303 ? -31.742 6.275   -27.360 1.00 52.36  ? 300 TRP B CB  1 
ATOM   5066 C CG  . TRP B 1 303 ? -31.640 7.792   -27.189 1.00 46.23  ? 300 TRP B CG  1 
ATOM   5067 C CD1 . TRP B 1 303 ? -30.631 8.595   -27.625 1.00 42.91  ? 300 TRP B CD1 1 
ATOM   5068 C CD2 . TRP B 1 303 ? -32.582 8.660   -26.537 1.00 41.46  ? 300 TRP B CD2 1 
ATOM   5069 N NE1 . TRP B 1 303 ? -30.883 9.901   -27.295 1.00 37.57  ? 300 TRP B NE1 1 
ATOM   5070 C CE2 . TRP B 1 303 ? -32.070 9.965   -26.615 1.00 40.19  ? 300 TRP B CE2 1 
ATOM   5071 C CE3 . TRP B 1 303 ? -33.797 8.458   -25.888 1.00 40.50  ? 300 TRP B CE3 1 
ATOM   5072 C CZ2 . TRP B 1 303 ? -32.740 11.061  -26.077 1.00 35.98  ? 300 TRP B CZ2 1 
ATOM   5073 C CZ3 . TRP B 1 303 ? -34.453 9.545   -25.353 1.00 35.80  ? 300 TRP B CZ3 1 
ATOM   5074 C CH2 . TRP B 1 303 ? -33.922 10.827  -25.447 1.00 36.87  ? 300 TRP B CH2 1 
ATOM   5075 N N   . SER B 1 304 ? -31.331 3.210   -26.892 1.00 48.28  ? 301 SER B N   1 
ATOM   5076 C CA  . SER B 1 304 ? -31.676 1.803   -27.090 1.00 49.25  ? 301 SER B CA  1 
ATOM   5077 C C   . SER B 1 304 ? -32.016 1.148   -25.771 1.00 50.53  ? 301 SER B C   1 
ATOM   5078 O O   . SER B 1 304 ? -32.959 0.353   -25.683 1.00 57.00  ? 301 SER B O   1 
ATOM   5079 C CB  . SER B 1 304 ? -30.525 1.037   -27.749 1.00 48.36  ? 301 SER B CB  1 
ATOM   5080 O OG  . SER B 1 304 ? -29.802 1.838   -28.662 1.00 54.60  ? 301 SER B OG  1 
ATOM   5081 N N   . ALA B 1 305 ? -31.241 1.468   -24.735 1.00 52.10  ? 302 ALA B N   1 
ATOM   5082 C CA  . ALA B 1 305 ? -31.549 1.004   -23.390 1.00 54.85  ? 302 ALA B CA  1 
ATOM   5083 C C   . ALA B 1 305 ? -32.931 1.482   -22.946 1.00 51.25  ? 302 ALA B C   1 
ATOM   5084 O O   . ALA B 1 305 ? -33.750 0.686   -22.470 1.00 51.33  ? 302 ALA B O   1 
ATOM   5085 C CB  . ALA B 1 305 ? -30.456 1.477   -22.428 1.00 42.28  ? 302 ALA B CB  1 
ATOM   5086 N N   . LEU B 1 306 ? -33.215 2.782   -23.114 1.00 51.05  ? 303 LEU B N   1 
ATOM   5087 C CA  . LEU B 1 306 ? -34.496 3.327   -22.663 1.00 53.38  ? 303 LEU B CA  1 
ATOM   5088 C C   . LEU B 1 306 ? -35.662 2.668   -23.387 1.00 58.04  ? 303 LEU B C   1 
ATOM   5089 O O   . LEU B 1 306 ? -36.671 2.311   -22.761 1.00 52.76  ? 303 LEU B O   1 
ATOM   5090 C CB  . LEU B 1 306 ? -34.534 4.841   -22.867 1.00 51.67  ? 303 LEU B CB  1 
ATOM   5091 C CG  . LEU B 1 306 ? -35.830 5.533   -22.441 1.00 46.38  ? 303 LEU B CG  1 
ATOM   5092 C CD1 . LEU B 1 306 ? -36.048 5.404   -20.964 1.00 42.82  ? 303 LEU B CD1 1 
ATOM   5093 C CD2 . LEU B 1 306 ? -35.801 6.988   -22.826 1.00 45.88  ? 303 LEU B CD2 1 
ATOM   5094 N N   . HIS B 1 307 ? -35.545 2.504   -24.707 1.00 55.99  ? 304 HIS B N   1 
ATOM   5095 C CA  . HIS B 1 307 ? -36.568 1.778   -25.446 1.00 62.12  ? 304 HIS B CA  1 
ATOM   5096 C C   . HIS B 1 307 ? -36.802 0.418   -24.803 1.00 61.62  ? 304 HIS B C   1 
ATOM   5097 O O   . HIS B 1 307 ? -37.910 0.115   -24.352 1.00 63.86  ? 304 HIS B O   1 
ATOM   5098 C CB  . HIS B 1 307 ? -36.173 1.635   -26.929 1.00 64.73  ? 304 HIS B CB  1 
ATOM   5099 C CG  . HIS B 1 307 ? -36.447 2.859   -27.754 1.00 71.90  ? 304 HIS B CG  1 
ATOM   5100 N ND1 . HIS B 1 307 ? -37.685 3.129   -28.301 1.00 78.50  ? 304 HIS B ND1 1 
ATOM   5101 C CD2 . HIS B 1 307 ? -35.642 3.885   -28.127 1.00 69.79  ? 304 HIS B CD2 1 
ATOM   5102 C CE1 . HIS B 1 307 ? -37.633 4.270   -28.970 1.00 76.92  ? 304 HIS B CE1 1 
ATOM   5103 N NE2 . HIS B 1 307 ? -36.404 4.749   -28.880 1.00 70.19  ? 304 HIS B NE2 1 
ATOM   5104 N N   . GLU B 1 308 ? -35.738 -0.378  -24.667 1.00 55.98  ? 305 GLU B N   1 
ATOM   5105 C CA  . GLU B 1 308 ? -35.913 -1.764  -24.252 1.00 55.24  ? 305 GLU B CA  1 
ATOM   5106 C C   . GLU B 1 308 ? -36.424 -1.875  -22.819 1.00 55.61  ? 305 GLU B C   1 
ATOM   5107 O O   . GLU B 1 308 ? -37.298 -2.699  -22.530 1.00 56.92  ? 305 GLU B O   1 
ATOM   5108 C CB  . GLU B 1 308 ? -34.607 -2.531  -24.419 1.00 58.00  ? 305 GLU B CB  1 
ATOM   5109 C CG  . GLU B 1 308 ? -34.806 -3.876  -25.093 1.00 66.06  ? 305 GLU B CG  1 
ATOM   5110 C CD  . GLU B 1 308 ? -33.758 -4.894  -24.701 1.00 79.52  ? 305 GLU B CD  1 
ATOM   5111 O OE1 . GLU B 1 308 ? -32.591 -4.487  -24.503 1.00 80.79  ? 305 GLU B OE1 1 
ATOM   5112 O OE2 . GLU B 1 308 ? -34.103 -6.098  -24.578 1.00 82.08  ? 305 GLU B OE2 1 
ATOM   5113 N N   . GLU B 1 309 ? -35.910 -1.061  -21.906 1.00 58.26  ? 306 GLU B N   1 
ATOM   5114 C CA  . GLU B 1 309 ? -36.359 -1.200  -20.526 1.00 60.77  ? 306 GLU B CA  1 
ATOM   5115 C C   . GLU B 1 309 ? -37.771 -0.662  -20.353 1.00 62.08  ? 306 GLU B C   1 
ATOM   5116 O O   . GLU B 1 309 ? -38.624 -1.321  -19.749 1.00 68.43  ? 306 GLU B O   1 
ATOM   5117 C CB  . GLU B 1 309 ? -35.394 -0.509  -19.567 1.00 54.38  ? 306 GLU B CB  1 
ATOM   5118 C CG  . GLU B 1 309 ? -34.074 -1.239  -19.424 1.00 55.38  ? 306 GLU B CG  1 
ATOM   5119 C CD  . GLU B 1 309 ? -33.213 -0.671  -18.299 1.00 60.36  ? 306 GLU B CD  1 
ATOM   5120 O OE1 . GLU B 1 309 ? -33.788 -0.281  -17.236 1.00 50.01  ? 306 GLU B OE1 1 
ATOM   5121 O OE2 . GLU B 1 309 ? -31.965 -0.621  -18.498 1.00 46.21  ? 306 GLU B OE2 1 
ATOM   5122 N N   . LEU B 1 310 ? -38.042 0.531   -20.882 1.00 66.54  ? 307 LEU B N   1 
ATOM   5123 C CA  . LEU B 1 310 ? -39.336 1.170   -20.658 1.00 63.68  ? 307 LEU B CA  1 
ATOM   5124 C C   . LEU B 1 310 ? -40.365 0.797   -21.715 1.00 66.07  ? 307 LEU B C   1 
ATOM   5125 O O   . LEU B 1 310 ? -41.546 0.624   -21.386 1.00 66.29  ? 307 LEU B O   1 
ATOM   5126 C CB  . LEU B 1 310 ? -39.180 2.690   -20.613 1.00 55.96  ? 307 LEU B CB  1 
ATOM   5127 C CG  . LEU B 1 310 ? -38.578 3.270   -19.349 1.00 52.48  ? 307 LEU B CG  1 
ATOM   5128 C CD1 . LEU B 1 310 ? -38.944 4.734   -19.229 1.00 49.40  ? 307 LEU B CD1 1 
ATOM   5129 C CD2 . LEU B 1 310 ? -39.072 2.485   -18.154 1.00 55.85  ? 307 LEU B CD2 1 
ATOM   5130 N N   . GLY B 1 311 ? -39.938 0.683   -22.982 1.00 66.22  ? 308 GLY B N   1 
ATOM   5131 C CA  . GLY B 1 311 ? -40.859 0.301   -24.041 1.00 66.97  ? 308 GLY B CA  1 
ATOM   5132 C C   . GLY B 1 311 ? -41.501 -1.048  -23.803 1.00 72.96  ? 308 GLY B C   1 
ATOM   5133 O O   . GLY B 1 311 ? -42.659 -1.261  -24.174 1.00 77.01  ? 308 GLY B O   1 
ATOM   5134 N N   . GLY B 1 312 ? -40.767 -1.973  -23.187 1.00 69.22  ? 309 GLY B N   1 
ATOM   5135 C CA  . GLY B 1 312 ? -41.379 -3.165  -22.648 1.00 68.61  ? 309 GLY B CA  1 
ATOM   5136 C C   . GLY B 1 312 ? -42.517 -2.806  -21.715 1.00 77.72  ? 309 GLY B C   1 
ATOM   5137 O O   . GLY B 1 312 ? -43.690 -3.047  -22.028 1.00 80.52  ? 309 GLY B O   1 
ATOM   5138 N N   . LEU B 1 313 ? -42.182 -2.170  -20.589 1.00 74.51  ? 310 LEU B N   1 
ATOM   5139 C CA  . LEU B 1 313 ? -43.164 -1.971  -19.524 1.00 79.26  ? 310 LEU B CA  1 
ATOM   5140 C C   . LEU B 1 313 ? -44.335 -1.111  -19.986 1.00 77.18  ? 310 LEU B C   1 
ATOM   5141 O O   . LEU B 1 313 ? -45.494 -1.415  -19.675 1.00 76.43  ? 310 LEU B O   1 
ATOM   5142 C CB  . LEU B 1 313 ? -42.488 -1.356  -18.293 1.00 81.05  ? 310 LEU B CB  1 
ATOM   5143 C CG  . LEU B 1 313 ? -41.079 -1.867  -17.925 1.00 77.06  ? 310 LEU B CG  1 
ATOM   5144 C CD1 . LEU B 1 313 ? -40.504 -1.118  -16.738 1.00 69.16  ? 310 LEU B CD1 1 
ATOM   5145 C CD2 . LEU B 1 313 ? -41.036 -3.372  -17.663 1.00 79.31  ? 310 LEU B CD2 1 
ATOM   5146 N N   . VAL B 1 314 ? -44.060 -0.040  -20.737 1.00 77.98  ? 311 VAL B N   1 
ATOM   5147 C CA  . VAL B 1 314 ? -45.139 0.826   -21.207 1.00 78.62  ? 311 VAL B CA  1 
ATOM   5148 C C   . VAL B 1 314 ? -46.101 0.045   -22.086 1.00 83.43  ? 311 VAL B C   1 
ATOM   5149 O O   . VAL B 1 314 ? -47.326 0.126   -21.920 1.00 81.40  ? 311 VAL B O   1 
ATOM   5150 C CB  . VAL B 1 314 ? -44.585 2.042   -21.964 1.00 71.21  ? 311 VAL B CB  1 
ATOM   5151 C CG1 . VAL B 1 314 ? -45.747 2.856   -22.469 1.00 67.73  ? 311 VAL B CG1 1 
ATOM   5152 C CG2 . VAL B 1 314 ? -43.693 2.884   -21.069 1.00 65.03  ? 311 VAL B CG2 1 
ATOM   5153 N N   . ARG B 1 315 ? -45.554 -0.723  -23.041 1.00 82.22  ? 312 ARG B N   1 
ATOM   5154 C CA  . ARG B 1 315 ? -46.390 -1.480  -23.973 1.00 87.42  ? 312 ARG B CA  1 
ATOM   5155 C C   . ARG B 1 315 ? -47.215 -2.543  -23.257 1.00 90.13  ? 312 ARG B C   1 
ATOM   5156 O O   . ARG B 1 315 ? -48.403 -2.718  -23.558 1.00 85.83  ? 312 ARG B O   1 
ATOM   5157 C CB  . ARG B 1 315 ? -45.534 -2.126  -25.065 1.00 83.24  ? 312 ARG B CB  1 
ATOM   5158 C CG  . ARG B 1 315 ? -45.154 -1.177  -26.209 1.00 83.79  ? 312 ARG B CG  1 
ATOM   5159 C CD  . ARG B 1 315 ? -44.972 -1.920  -27.537 1.00 82.94  ? 312 ARG B CD  1 
ATOM   5160 N NE  . ARG B 1 315 ? -44.096 -1.205  -28.462 1.00 83.69  ? 312 ARG B NE  1 
ATOM   5161 C CZ  . ARG B 1 315 ? -42.769 -1.260  -28.426 1.00 80.67  ? 312 ARG B CZ  1 
ATOM   5162 N NH1 . ARG B 1 315 ? -42.133 -1.974  -27.508 1.00 76.22  ? 312 ARG B NH1 1 
ATOM   5163 N NH2 . ARG B 1 315 ? -42.062 -0.581  -29.329 1.00 66.02  ? 312 ARG B NH2 1 
ATOM   5164 N N   . ARG B 1 316 ? -46.604 -3.264  -22.304 1.00 91.64  ? 313 ARG B N   1 
ATOM   5165 C CA  . ARG B 1 316 ? -47.273 -4.325  -21.549 1.00 88.16  ? 313 ARG B CA  1 
ATOM   5166 C C   . ARG B 1 316 ? -48.155 -3.802  -20.407 1.00 87.36  ? 313 ARG B C   1 
ATOM   5167 O O   . ARG B 1 316 ? -48.540 -4.599  -19.543 1.00 90.22  ? 313 ARG B O   1 
ATOM   5168 C CB  . ARG B 1 316 ? -46.240 -5.312  -20.987 1.00 80.46  ? 313 ARG B CB  1 
ATOM   5169 C CG  . ARG B 1 316 ? -45.301 -5.932  -22.021 1.00 84.35  ? 313 ARG B CG  1 
ATOM   5170 C CD  . ARG B 1 316 ? -44.247 -6.821  -21.357 1.00 83.38  ? 313 ARG B CD  1 
ATOM   5171 N NE  . ARG B 1 316 ? -42.975 -6.140  -21.121 1.00 84.81  ? 313 ARG B NE  1 
ATOM   5172 C CZ  . ARG B 1 316 ? -42.024 -6.569  -20.297 1.00 89.33  ? 313 ARG B CZ  1 
ATOM   5173 N NH1 . ARG B 1 316 ? -42.179 -7.663  -19.568 1.00 86.58  ? 313 ARG B NH1 1 
ATOM   5174 N NH2 . ARG B 1 316 ? -40.887 -5.880  -20.199 1.00 84.05  ? 313 ARG B NH2 1 
ATOM   5175 N N   . GLN B 1 317 ? -48.467 -2.500  -20.379 1.00 88.08  ? 314 GLN B N   1 
ATOM   5176 C CA  . GLN B 1 317 ? -49.394 -1.848  -19.448 1.00 87.23  ? 314 GLN B CA  1 
ATOM   5177 C C   . GLN B 1 317 ? -48.876 -1.779  -18.012 1.00 89.01  ? 314 GLN B C   1 
ATOM   5178 O O   . GLN B 1 317 ? -49.626 -1.367  -17.112 1.00 83.04  ? 314 GLN B O   1 
ATOM   5179 C CB  . GLN B 1 317 ? -50.771 -2.527  -19.445 1.00 89.86  ? 314 GLN B CB  1 
ATOM   5180 C CG  . GLN B 1 317 ? -51.472 -2.575  -20.786 1.00 85.21  ? 314 GLN B CG  1 
ATOM   5181 C CD  . GLN B 1 317 ? -52.038 -1.230  -21.187 1.00 85.12  ? 314 GLN B CD  1 
ATOM   5182 O OE1 . GLN B 1 317 ? -51.915 -0.247  -20.452 1.00 86.14  ? 314 GLN B OE1 1 
ATOM   5183 N NE2 . GLN B 1 317 ? -52.669 -1.178  -22.354 1.00 78.28  ? 314 GLN B NE2 1 
ATOM   5184 N N   . GLU B 1 318 ? -47.621 -2.172  -17.769 1.00 86.44  ? 315 GLU B N   1 
ATOM   5185 C CA  . GLU B 1 318 ? -46.986 -2.081  -16.458 1.00 80.58  ? 315 GLU B CA  1 
ATOM   5186 C C   . GLU B 1 318 ? -46.428 -0.690  -16.156 1.00 80.37  ? 315 GLU B C   1 
ATOM   5187 O O   . GLU B 1 318 ? -45.869 -0.480  -15.072 1.00 75.10  ? 315 GLU B O   1 
ATOM   5188 C CB  . GLU B 1 318 ? -45.850 -3.107  -16.357 1.00 84.20  ? 315 GLU B CB  1 
ATOM   5189 C CG  . GLU B 1 318 ? -46.065 -4.388  -17.169 1.00 90.18  ? 315 GLU B CG  1 
ATOM   5190 C CD  . GLU B 1 318 ? -44.750 -5.107  -17.505 1.00 97.24  ? 315 GLU B CD  1 
ATOM   5191 O OE1 . GLU B 1 318 ? -43.720 -4.810  -16.849 1.00 92.02  ? 315 GLU B OE1 1 
ATOM   5192 O OE2 . GLU B 1 318 ? -44.748 -5.961  -18.426 1.00 95.39  ? 315 GLU B OE2 1 
ATOM   5193 N N   . LEU B 1 319 ? -46.547 0.255   -17.084 1.00 81.30  ? 316 LEU B N   1 
ATOM   5194 C CA  . LEU B 1 319 ? -45.999 1.593   -16.900 1.00 70.85  ? 316 LEU B CA  1 
ATOM   5195 C C   . LEU B 1 319 ? -46.865 2.548   -17.701 1.00 65.62  ? 316 LEU B C   1 
ATOM   5196 O O   . LEU B 1 319 ? -46.947 2.424   -18.927 1.00 74.55  ? 316 LEU B O   1 
ATOM   5197 C CB  . LEU B 1 319 ? -44.544 1.646   -17.358 1.00 72.74  ? 316 LEU B CB  1 
ATOM   5198 C CG  . LEU B 1 319 ? -43.560 2.544   -16.612 1.00 69.02  ? 316 LEU B CG  1 
ATOM   5199 C CD1 . LEU B 1 319 ? -43.893 2.644   -15.153 1.00 65.06  ? 316 LEU B CD1 1 
ATOM   5200 C CD2 . LEU B 1 319 ? -42.185 1.964   -16.755 1.00 67.81  ? 316 LEU B CD2 1 
ATOM   5201 N N   . VAL B 1 320 ? -47.512 3.478   -17.008 1.00 60.37  ? 317 VAL B N   1 
ATOM   5202 C CA  . VAL B 1 320 ? -48.492 4.378   -17.605 1.00 60.09  ? 317 VAL B CA  1 
ATOM   5203 C C   . VAL B 1 320 ? -47.788 5.656   -18.051 1.00 66.74  ? 317 VAL B C   1 
ATOM   5204 O O   . VAL B 1 320 ? -47.360 6.464   -17.216 1.00 66.66  ? 317 VAL B O   1 
ATOM   5205 C CB  . VAL B 1 320 ? -49.620 4.685   -16.617 1.00 60.76  ? 317 VAL B CB  1 
ATOM   5206 C CG1 . VAL B 1 320 ? -50.325 5.973   -16.993 1.00 65.50  ? 317 VAL B CG1 1 
ATOM   5207 C CG2 . VAL B 1 320 ? -50.591 3.526   -16.562 1.00 63.83  ? 317 VAL B CG2 1 
ATOM   5208 N N   . ALA B 1 321 ? -47.677 5.842   -19.370 1.00 71.49  ? 318 ALA B N   1 
ATOM   5209 C CA  . ALA B 1 321 ? -47.086 7.041   -19.979 1.00 66.96  ? 318 ALA B CA  1 
ATOM   5210 C C   . ALA B 1 321 ? -48.164 7.768   -20.779 1.00 62.46  ? 318 ALA B C   1 
ATOM   5211 O O   . ALA B 1 321 ? -48.124 7.819   -22.009 1.00 65.48  ? 318 ALA B O   1 
ATOM   5212 C CB  . ALA B 1 321 ? -45.872 6.683   -20.861 1.00 58.42  ? 318 ALA B CB  1 
ATOM   5213 N N   . HIS B 1 322 ? -49.131 8.329   -20.064 1.00 62.89  ? 319 HIS B N   1 
ATOM   5214 C CA  . HIS B 1 322 ? -50.217 9.078   -20.673 1.00 58.06  ? 319 HIS B CA  1 
ATOM   5215 C C   . HIS B 1 322 ? -49.688 10.339  -21.362 1.00 60.65  ? 319 HIS B C   1 
ATOM   5216 O O   . HIS B 1 322 ? -48.577 10.812  -21.096 1.00 58.28  ? 319 HIS B O   1 
ATOM   5217 C CB  . HIS B 1 322 ? -51.248 9.453   -19.604 1.00 68.50  ? 319 HIS B CB  1 
ATOM   5218 C CG  . HIS B 1 322 ? -52.054 8.293   -19.096 1.00 71.86  ? 319 HIS B CG  1 
ATOM   5219 N ND1 . HIS B 1 322 ? -52.920 8.400   -18.026 1.00 70.30  ? 319 HIS B ND1 1 
ATOM   5220 C CD2 . HIS B 1 322 ? -52.145 7.010   -19.523 1.00 63.01  ? 319 HIS B CD2 1 
ATOM   5221 C CE1 . HIS B 1 322 ? -53.502 7.233   -17.811 1.00 66.36  ? 319 HIS B CE1 1 
ATOM   5222 N NE2 . HIS B 1 322 ? -53.047 6.373   -18.704 1.00 67.69  ? 319 HIS B NE2 1 
ATOM   5223 N N   . GLU B 1 323 ? -50.505 10.893  -22.258 1.00 57.73  ? 320 GLU B N   1 
ATOM   5224 C CA  . GLU B 1 323 ? -50.137 12.112  -22.963 1.00 54.30  ? 320 GLU B CA  1 
ATOM   5225 C C   . GLU B 1 323 ? -51.396 12.886  -23.314 1.00 49.52  ? 320 GLU B C   1 
ATOM   5226 O O   . GLU B 1 323 ? -52.462 12.307  -23.528 1.00 56.43  ? 320 GLU B O   1 
ATOM   5227 C CB  . GLU B 1 323 ? -49.320 11.826  -24.231 1.00 44.51  ? 320 GLU B CB  1 
ATOM   5228 C CG  . GLU B 1 323 ? -50.112 11.223  -25.355 1.00 48.10  ? 320 GLU B CG  1 
ATOM   5229 C CD  . GLU B 1 323 ? -49.227 10.704  -26.501 1.00 64.15  ? 320 GLU B CD  1 
ATOM   5230 O OE1 . GLU B 1 323 ? -48.019 11.062  -26.545 1.00 59.03  ? 320 GLU B OE1 1 
ATOM   5231 O OE2 . GLU B 1 323 ? -49.737 9.928   -27.358 1.00 61.86  ? 320 GLU B OE2 1 
ATOM   5232 N N   . THR B 1 324 ? -51.253 14.206  -23.366 1.00 47.13  ? 321 THR B N   1 
ATOM   5233 C CA  . THR B 1 324 ? -52.334 15.147  -23.653 1.00 45.08  ? 321 THR B CA  1 
ATOM   5234 C C   . THR B 1 324 ? -51.927 15.971  -24.877 1.00 47.91  ? 321 THR B C   1 
ATOM   5235 O O   . THR B 1 324 ? -51.207 16.967  -24.745 1.00 48.06  ? 321 THR B O   1 
ATOM   5236 C CB  . THR B 1 324 ? -52.596 16.028  -22.436 1.00 44.53  ? 321 THR B CB  1 
ATOM   5237 O OG1 . THR B 1 324 ? -53.087 15.214  -21.367 1.00 53.19  ? 321 THR B OG1 1 
ATOM   5238 C CG2 . THR B 1 324 ? -53.596 17.121  -22.735 1.00 41.57  ? 321 THR B CG2 1 
ATOM   5239 N N   . VAL B 1 325 ? -52.391 15.561  -26.060 1.00 43.71  ? 322 VAL B N   1 
ATOM   5240 C CA  . VAL B 1 325 ? -51.981 16.143  -27.335 1.00 41.65  ? 322 VAL B CA  1 
ATOM   5241 C C   . VAL B 1 325 ? -53.032 17.144  -27.799 1.00 42.95  ? 322 VAL B C   1 
ATOM   5242 O O   . VAL B 1 325 ? -54.077 16.755  -28.324 1.00 48.29  ? 322 VAL B O   1 
ATOM   5243 C CB  . VAL B 1 325 ? -51.775 15.059  -28.383 1.00 45.23  ? 322 VAL B CB  1 
ATOM   5244 C CG1 . VAL B 1 325 ? -51.491 15.679  -29.758 1.00 38.98  ? 322 VAL B CG1 1 
ATOM   5245 C CG2 . VAL B 1 325 ? -50.673 14.129  -27.918 1.00 50.32  ? 322 VAL B CG2 1 
ATOM   5246 N N   . GLN B 1 326 ? -52.727 18.436  -27.656 1.00 44.22  ? 323 GLN B N   1 
ATOM   5247 C CA  . GLN B 1 326 ? -53.539 19.516  -28.211 1.00 41.72  ? 323 GLN B CA  1 
ATOM   5248 C C   . GLN B 1 326 ? -53.328 19.654  -29.725 1.00 42.76  ? 323 GLN B C   1 
ATOM   5249 O O   . GLN B 1 326 ? -52.214 19.486  -30.223 1.00 42.95  ? 323 GLN B O   1 
ATOM   5250 C CB  . GLN B 1 326 ? -53.180 20.823  -27.510 1.00 40.16  ? 323 GLN B CB  1 
ATOM   5251 C CG  . GLN B 1 326 ? -53.956 22.010  -27.991 1.00 47.16  ? 323 GLN B CG  1 
ATOM   5252 C CD  . GLN B 1 326 ? -55.436 21.826  -27.754 1.00 57.32  ? 323 GLN B CD  1 
ATOM   5253 O OE1 . GLN B 1 326 ? -55.856 21.440  -26.651 1.00 59.22  ? 323 GLN B OE1 1 
ATOM   5254 N NE2 . GLN B 1 326 ? -56.241 22.066  -28.794 1.00 49.70  ? 323 GLN B NE2 1 
ATOM   5255 N N   . ASP B 1 327 ? -54.401 19.962  -30.463 1.00 44.06  ? 324 ASP B N   1 
ATOM   5256 C CA  . ASP B 1 327 ? -54.356 20.044  -31.927 1.00 43.97  ? 324 ASP B CA  1 
ATOM   5257 C C   . ASP B 1 327 ? -54.332 21.499  -32.377 1.00 42.03  ? 324 ASP B C   1 
ATOM   5258 O O   . ASP B 1 327 ? -55.116 22.318  -31.889 1.00 39.29  ? 324 ASP B O   1 
ATOM   5259 C CB  . ASP B 1 327 ? -55.557 19.346  -32.576 1.00 46.30  ? 324 ASP B CB  1 
ATOM   5260 C CG  . ASP B 1 327 ? -55.208 17.982  -33.185 1.00 56.34  ? 324 ASP B CG  1 
ATOM   5261 O OD1 . ASP B 1 327 ? -54.321 17.263  -32.658 1.00 54.88  ? 324 ASP B OD1 1 
ATOM   5262 O OD2 . ASP B 1 327 ? -55.832 17.625  -34.213 1.00 62.50  ? 324 ASP B OD2 1 
ATOM   5263 N N   . GLY B 1 328 ? -53.437 21.818  -33.307 1.00 40.35  ? 325 GLY B N   1 
ATOM   5264 C CA  . GLY B 1 328 ? -53.436 23.144  -33.899 1.00 38.05  ? 325 GLY B CA  1 
ATOM   5265 C C   . GLY B 1 328 ? -52.264 24.043  -33.555 1.00 42.08  ? 325 GLY B C   1 
ATOM   5266 O O   . GLY B 1 328 ? -52.078 24.429  -32.391 1.00 42.63  ? 325 GLY B O   1 
ATOM   5267 N N   . PHE B 1 329 ? -51.479 24.405  -34.578 1.00 38.26  ? 326 PHE B N   1 
ATOM   5268 C CA  . PHE B 1 329 ? -50.303 25.245  -34.364 1.00 36.45  ? 326 PHE B CA  1 
ATOM   5269 C C   . PHE B 1 329 ? -50.663 26.579  -33.718 1.00 32.74  ? 326 PHE B C   1 
ATOM   5270 O O   . PHE B 1 329 ? -49.879 27.122  -32.935 1.00 30.46  ? 326 PHE B O   1 
ATOM   5271 C CB  . PHE B 1 329 ? -49.571 25.484  -35.689 1.00 37.78  ? 326 PHE B CB  1 
ATOM   5272 C CG  . PHE B 1 329 ? -48.342 26.358  -35.555 1.00 34.37  ? 326 PHE B CG  1 
ATOM   5273 C CD1 . PHE B 1 329 ? -48.435 27.740  -35.666 1.00 31.09  ? 326 PHE B CD1 1 
ATOM   5274 C CD2 . PHE B 1 329 ? -47.096 25.789  -35.306 1.00 30.35  ? 326 PHE B CD2 1 
ATOM   5275 C CE1 . PHE B 1 329 ? -47.316 28.538  -35.537 1.00 30.28  ? 326 PHE B CE1 1 
ATOM   5276 C CE2 . PHE B 1 329 ? -45.978 26.571  -35.180 1.00 26.24  ? 326 PHE B CE2 1 
ATOM   5277 C CZ  . PHE B 1 329 ? -46.084 27.954  -35.306 1.00 30.18  ? 326 PHE B CZ  1 
ATOM   5278 N N   . GLU B 1 330 ? -51.829 27.135  -34.051 1.00 37.14  ? 327 GLU B N   1 
ATOM   5279 C CA  . GLU B 1 330 ? -52.233 28.417  -33.477 1.00 40.36  ? 327 GLU B CA  1 
ATOM   5280 C C   . GLU B 1 330 ? -52.494 28.331  -31.977 1.00 40.96  ? 327 GLU B C   1 
ATOM   5281 O O   . GLU B 1 330 ? -52.642 29.383  -31.324 1.00 37.86  ? 327 GLU B O   1 
ATOM   5282 C CB  . GLU B 1 330 ? -53.494 28.946  -34.174 1.00 37.46  ? 327 GLU B CB  1 
ATOM   5283 C CG  . GLU B 1 330 ? -54.740 28.118  -33.925 1.00 35.58  ? 327 GLU B CG  1 
ATOM   5284 C CD  . GLU B 1 330 ? -54.966 27.019  -34.967 1.00 46.30  ? 327 GLU B CD  1 
ATOM   5285 O OE1 . GLU B 1 330 ? -53.975 26.514  -35.545 1.00 47.37  ? 327 GLU B OE1 1 
ATOM   5286 O OE2 . GLU B 1 330 ? -56.147 26.657  -35.211 1.00 47.01  ? 327 GLU B OE2 1 
ATOM   5287 N N   . HIS B 1 331 ? -52.556 27.118  -31.416 1.00 34.94  ? 328 HIS B N   1 
ATOM   5288 C CA  . HIS B 1 331 ? -52.899 26.944  -30.010 1.00 40.70  ? 328 HIS B CA  1 
ATOM   5289 C C   . HIS B 1 331 ? -51.702 26.646  -29.126 1.00 40.62  ? 328 HIS B C   1 
ATOM   5290 O O   . HIS B 1 331 ? -51.884 26.491  -27.914 1.00 41.37  ? 328 HIS B O   1 
ATOM   5291 C CB  . HIS B 1 331 ? -53.956 25.842  -29.847 1.00 37.07  ? 328 HIS B CB  1 
ATOM   5292 C CG  . HIS B 1 331 ? -55.306 26.254  -30.346 1.00 42.16  ? 328 HIS B CG  1 
ATOM   5293 N ND1 . HIS B 1 331 ? -56.036 25.501  -31.241 1.00 40.83  ? 328 HIS B ND1 1 
ATOM   5294 C CD2 . HIS B 1 331 ? -56.026 27.380  -30.124 1.00 43.36  ? 328 HIS B CD2 1 
ATOM   5295 C CE1 . HIS B 1 331 ? -57.157 26.137  -31.534 1.00 42.15  ? 328 HIS B CE1 1 
ATOM   5296 N NE2 . HIS B 1 331 ? -57.176 27.277  -30.868 1.00 42.89  ? 328 HIS B NE2 1 
ATOM   5297 N N   . ILE B 1 332 ? -50.490 26.589  -29.692 1.00 37.79  ? 329 ILE B N   1 
ATOM   5298 C CA  . ILE B 1 332 ? -49.312 26.242  -28.891 1.00 35.52  ? 329 ILE B CA  1 
ATOM   5299 C C   . ILE B 1 332 ? -49.178 27.099  -27.639 1.00 36.97  ? 329 ILE B C   1 
ATOM   5300 O O   . ILE B 1 332 ? -48.986 26.530  -26.549 1.00 35.62  ? 329 ILE B O   1 
ATOM   5301 C CB  . ILE B 1 332 ? -48.050 26.270  -29.770 1.00 29.68  ? 329 ILE B CB  1 
ATOM   5302 C CG1 . ILE B 1 332 ? -48.127 25.204  -30.850 1.00 27.88  ? 329 ILE B CG1 1 
ATOM   5303 C CG2 . ILE B 1 332 ? -46.835 26.043  -28.918 1.00 28.24  ? 329 ILE B CG2 1 
ATOM   5304 C CD1 . ILE B 1 332 ? -46.877 25.131  -31.637 1.00 24.75  ? 329 ILE B CD1 1 
ATOM   5305 N N   . PRO B 1 333 ? -49.279 28.433  -27.682 1.00 36.28  ? 330 PRO B N   1 
ATOM   5306 C CA  . PRO B 1 333 ? -49.106 29.198  -26.437 1.00 33.21  ? 330 PRO B CA  1 
ATOM   5307 C C   . PRO B 1 333 ? -50.242 29.000  -25.429 1.00 37.97  ? 330 PRO B C   1 
ATOM   5308 O O   . PRO B 1 333 ? -50.021 29.153  -24.223 1.00 37.64  ? 330 PRO B O   1 
ATOM   5309 C CB  . PRO B 1 333 ? -49.009 30.657  -26.917 1.00 28.80  ? 330 PRO B CB  1 
ATOM   5310 C CG  . PRO B 1 333 ? -48.750 30.579  -28.387 1.00 31.26  ? 330 PRO B CG  1 
ATOM   5311 C CD  . PRO B 1 333 ? -49.438 29.328  -28.849 1.00 31.61  ? 330 PRO B CD  1 
ATOM   5312 N N   . ALA B 1 334 ? -51.455 28.672  -25.873 1.00 40.94  ? 331 ALA B N   1 
ATOM   5313 C CA  . ALA B 1 334 ? -52.516 28.370  -24.918 1.00 35.73  ? 331 ALA B CA  1 
ATOM   5314 C C   . ALA B 1 334 ? -52.252 27.053  -24.205 1.00 32.18  ? 331 ALA B C   1 
ATOM   5315 O O   . ALA B 1 334 ? -52.475 26.946  -22.997 1.00 37.13  ? 331 ALA B O   1 
ATOM   5316 C CB  . ALA B 1 334 ? -53.871 28.330  -25.625 1.00 30.01  ? 331 ALA B CB  1 
ATOM   5317 N N   . ALA B 1 335 ? -51.793 26.040  -24.943 1.00 29.73  ? 332 ALA B N   1 
ATOM   5318 C CA  . ALA B 1 335 ? -51.405 24.777  -24.332 1.00 32.37  ? 332 ALA B CA  1 
ATOM   5319 C C   . ALA B 1 335 ? -50.251 24.968  -23.363 1.00 39.37  ? 332 ALA B C   1 
ATOM   5320 O O   . ALA B 1 335 ? -50.198 24.338  -22.299 1.00 47.20  ? 332 ALA B O   1 
ATOM   5321 C CB  . ALA B 1 335 ? -51.025 23.774  -25.415 1.00 35.13  ? 332 ALA B CB  1 
ATOM   5322 N N   . TYR B 1 336 ? -49.311 25.835  -23.712 1.00 37.72  ? 333 TYR B N   1 
ATOM   5323 C CA  . TYR B 1 336 ? -48.212 26.124  -22.806 1.00 38.13  ? 333 TYR B CA  1 
ATOM   5324 C C   . TYR B 1 336 ? -48.717 26.791  -21.538 1.00 41.46  ? 333 TYR B C   1 
ATOM   5325 O O   . TYR B 1 336 ? -48.184 26.555  -20.446 1.00 39.81  ? 333 TYR B O   1 
ATOM   5326 C CB  . TYR B 1 336 ? -47.201 27.005  -23.532 1.00 36.44  ? 333 TYR B CB  1 
ATOM   5327 C CG  . TYR B 1 336 ? -46.129 27.645  -22.703 1.00 33.96  ? 333 TYR B CG  1 
ATOM   5328 C CD1 . TYR B 1 336 ? -45.127 26.888  -22.126 1.00 33.49  ? 333 TYR B CD1 1 
ATOM   5329 C CD2 . TYR B 1 336 ? -46.083 29.024  -22.554 1.00 35.80  ? 333 TYR B CD2 1 
ATOM   5330 C CE1 . TYR B 1 336 ? -44.125 27.487  -21.386 1.00 35.43  ? 333 TYR B CE1 1 
ATOM   5331 C CE2 . TYR B 1 336 ? -45.082 29.636  -21.823 1.00 36.97  ? 333 TYR B CE2 1 
ATOM   5332 C CZ  . TYR B 1 336 ? -44.103 28.861  -21.244 1.00 36.96  ? 333 TYR B CZ  1 
ATOM   5333 O OH  . TYR B 1 336 ? -43.103 29.458  -20.513 1.00 33.28  ? 333 TYR B OH  1 
ATOM   5334 N N   . GLN B 1 337 ? -49.749 27.630  -21.668 1.00 40.90  ? 334 GLN B N   1 
ATOM   5335 C CA  . GLN B 1 337 ? -50.244 28.396  -20.536 1.00 38.03  ? 334 GLN B CA  1 
ATOM   5336 C C   . GLN B 1 337 ? -50.915 27.491  -19.507 1.00 47.24  ? 334 GLN B C   1 
ATOM   5337 O O   . GLN B 1 337 ? -50.895 27.803  -18.304 1.00 44.22  ? 334 GLN B O   1 
ATOM   5338 C CB  . GLN B 1 337 ? -51.202 29.476  -21.034 1.00 34.08  ? 334 GLN B CB  1 
ATOM   5339 C CG  . GLN B 1 337 ? -51.753 30.384  -19.963 1.00 38.24  ? 334 GLN B CG  1 
ATOM   5340 C CD  . GLN B 1 337 ? -50.724 31.324  -19.379 1.00 37.74  ? 334 GLN B CD  1 
ATOM   5341 O OE1 . GLN B 1 337 ? -50.082 32.074  -20.099 1.00 41.94  ? 334 GLN B OE1 1 
ATOM   5342 N NE2 . GLN B 1 337 ? -50.578 31.303  -18.062 1.00 45.26  ? 334 GLN B NE2 1 
ATOM   5343 N N   . THR B 1 338 ? -51.477 26.352  -19.948 1.00 40.54  ? 335 THR B N   1 
ATOM   5344 C CA  . THR B 1 338 ? -52.210 25.506  -19.010 1.00 45.76  ? 335 THR B CA  1 
ATOM   5345 C C   . THR B 1 338 ? -51.272 24.841  -18.005 1.00 48.52  ? 335 THR B C   1 
ATOM   5346 O O   . THR B 1 338 ? -51.675 24.590  -16.866 1.00 51.86  ? 335 THR B O   1 
ATOM   5347 C CB  . THR B 1 338 ? -53.051 24.451  -19.745 1.00 47.19  ? 335 THR B CB  1 
ATOM   5348 O OG1 . THR B 1 338 ? -52.200 23.487  -20.364 1.00 49.44  ? 335 THR B OG1 1 
ATOM   5349 C CG2 . THR B 1 338 ? -53.926 25.081  -20.817 1.00 41.09  ? 335 THR B CG2 1 
ATOM   5350 N N   . LEU B 1 339 ? -50.020 24.574  -18.389 1.00 42.55  ? 336 LEU B N   1 
ATOM   5351 C CA  . LEU B 1 339 ? -49.034 24.088  -17.430 1.00 39.33  ? 336 LEU B CA  1 
ATOM   5352 C C   . LEU B 1 339 ? -48.963 24.974  -16.187 1.00 47.62  ? 336 LEU B C   1 
ATOM   5353 O O   . LEU B 1 339 ? -48.602 24.501  -15.099 1.00 50.45  ? 336 LEU B O   1 
ATOM   5354 C CB  . LEU B 1 339 ? -47.653 24.007  -18.081 1.00 36.59  ? 336 LEU B CB  1 
ATOM   5355 C CG  . LEU B 1 339 ? -47.370 23.083  -19.268 1.00 33.45  ? 336 LEU B CG  1 
ATOM   5356 C CD1 . LEU B 1 339 ? -45.957 23.308  -19.780 1.00 31.03  ? 336 LEU B CD1 1 
ATOM   5357 C CD2 . LEU B 1 339 ? -47.558 21.644  -18.881 1.00 41.16  ? 336 LEU B CD2 1 
ATOM   5358 N N   . PHE B 1 340 ? -49.320 26.251  -16.314 1.00 40.60  ? 337 PHE B N   1 
ATOM   5359 C CA  . PHE B 1 340 ? -49.193 27.170  -15.199 1.00 44.09  ? 337 PHE B CA  1 
ATOM   5360 C C   . PHE B 1 340 ? -50.512 27.601  -14.592 1.00 43.35  ? 337 PHE B C   1 
ATOM   5361 O O   . PHE B 1 340 ? -50.514 28.067  -13.454 1.00 50.31  ? 337 PHE B O   1 
ATOM   5362 C CB  . PHE B 1 340 ? -48.448 28.438  -15.629 1.00 47.04  ? 337 PHE B CB  1 
ATOM   5363 C CG  . PHE B 1 340 ? -47.145 28.176  -16.333 1.00 50.90  ? 337 PHE B CG  1 
ATOM   5364 C CD1 . PHE B 1 340 ? -45.968 28.050  -15.618 1.00 45.11  ? 337 PHE B CD1 1 
ATOM   5365 C CD2 . PHE B 1 340 ? -47.097 28.076  -17.718 1.00 49.34  ? 337 PHE B CD2 1 
ATOM   5366 C CE1 . PHE B 1 340 ? -44.770 27.828  -16.260 1.00 45.20  ? 337 PHE B CE1 1 
ATOM   5367 C CE2 . PHE B 1 340 ? -45.904 27.849  -18.367 1.00 43.69  ? 337 PHE B CE2 1 
ATOM   5368 C CZ  . PHE B 1 340 ? -44.735 27.733  -17.636 1.00 44.80  ? 337 PHE B CZ  1 
ATOM   5369 N N   . SER B 1 341 ? -51.614 27.494  -15.321 1.00 45.36  ? 338 SER B N   1 
ATOM   5370 C CA  . SER B 1 341 ? -52.873 28.090  -14.897 1.00 47.10  ? 338 SER B CA  1 
ATOM   5371 C C   . SER B 1 341 ? -54.037 27.126  -14.896 1.00 51.43  ? 338 SER B C   1 
ATOM   5372 O O   . SER B 1 341 ? -55.019 27.388  -14.194 1.00 64.55  ? 338 SER B O   1 
ATOM   5373 C CB  . SER B 1 341 ? -53.251 29.275  -15.801 1.00 48.43  ? 338 SER B CB  1 
ATOM   5374 O OG  . SER B 1 341 ? -52.120 30.008  -16.225 1.00 43.59  ? 338 SER B OG  1 
ATOM   5375 N N   . ALA B 1 342 ? -53.964 26.028  -15.640 1.00 50.33  ? 339 ALA B N   1 
ATOM   5376 C CA  . ALA B 1 342 ? -55.120 25.185  -15.917 1.00 56.21  ? 339 ALA B CA  1 
ATOM   5377 C C   . ALA B 1 342 ? -54.652 23.750  -16.134 1.00 58.27  ? 339 ALA B C   1 
ATOM   5378 O O   . ALA B 1 342 ? -55.055 23.073  -17.087 1.00 55.27  ? 339 ALA B O   1 
ATOM   5379 C CB  . ALA B 1 342 ? -55.899 25.703  -17.129 1.00 50.44  ? 339 ALA B CB  1 
ATOM   5380 N N   . SER B 1 343 ? -53.772 23.277  -15.249 1.00 58.43  ? 340 SER B N   1 
ATOM   5381 C CA  . SER B 1 343 ? -53.264 21.915  -15.349 1.00 57.17  ? 340 SER B CA  1 
ATOM   5382 C C   . SER B 1 343 ? -54.278 20.876  -14.889 1.00 62.08  ? 340 SER B C   1 
ATOM   5383 O O   . SER B 1 343 ? -54.121 19.696  -15.239 1.00 58.01  ? 340 SER B O   1 
ATOM   5384 C CB  . SER B 1 343 ? -51.968 21.776  -14.543 1.00 54.17  ? 340 SER B CB  1 
ATOM   5385 O OG  . SER B 1 343 ? -51.977 22.634  -13.414 1.00 59.15  ? 340 SER B OG  1 
ATOM   5386 N N   . GLU B 1 344 ? -55.325 21.301  -14.156 1.00 64.55  ? 341 GLU B N   1 
ATOM   5387 C CA  . GLU B 1 344 ? -56.318 20.400  -13.569 1.00 60.44  ? 341 GLU B CA  1 
ATOM   5388 C C   . GLU B 1 344 ? -56.867 19.406  -14.574 1.00 59.78  ? 341 GLU B C   1 
ATOM   5389 O O   . GLU B 1 344 ? -57.362 18.346  -14.180 1.00 61.64  ? 341 GLU B O   1 
ATOM   5390 C CB  . GLU B 1 344 ? -57.482 21.198  -12.972 1.00 59.66  ? 341 GLU B CB  1 
ATOM   5391 C CG  . GLU B 1 344 ? -57.097 22.526  -12.304 1.00 65.07  ? 341 GLU B CG  1 
ATOM   5392 C CD  . GLU B 1 344 ? -57.178 23.723  -13.267 1.00 73.25  ? 341 GLU B CD  1 
ATOM   5393 O OE1 . GLU B 1 344 ? -57.647 23.529  -14.423 1.00 66.62  ? 341 GLU B OE1 1 
ATOM   5394 O OE2 . GLU B 1 344 ? -56.774 24.849  -12.864 1.00 63.73  ? 341 GLU B OE2 1 
ATOM   5395 N N   . SER B 1 345 ? -56.756 19.713  -15.861 1.00 66.02  ? 342 SER B N   1 
ATOM   5396 C CA  . SER B 1 345 ? -57.280 18.885  -16.931 1.00 64.78  ? 342 SER B CA  1 
ATOM   5397 C C   . SER B 1 345 ? -56.204 18.134  -17.717 1.00 65.41  ? 342 SER B C   1 
ATOM   5398 O O   . SER B 1 345 ? -56.557 17.317  -18.575 1.00 61.18  ? 342 SER B O   1 
ATOM   5399 C CB  . SER B 1 345 ? -58.104 19.769  -17.883 1.00 68.94  ? 342 SER B CB  1 
ATOM   5400 O OG  . SER B 1 345 ? -58.392 21.029  -17.266 1.00 65.82  ? 342 SER B OG  1 
ATOM   5401 N N   . ASN B 1 346 ? -54.913 18.373  -17.448 1.00 64.62  ? 343 ASN B N   1 
ATOM   5402 C CA  . ASN B 1 346 ? -53.815 17.757  -18.190 1.00 58.20  ? 343 ASN B CA  1 
ATOM   5403 C C   . ASN B 1 346 ? -53.453 16.395  -17.613 1.00 57.41  ? 343 ASN B C   1 
ATOM   5404 O O   . ASN B 1 346 ? -53.706 16.106  -16.444 1.00 58.13  ? 343 ASN B O   1 
ATOM   5405 C CB  . ASN B 1 346 ? -52.575 18.649  -18.182 1.00 59.76  ? 343 ASN B CB  1 
ATOM   5406 C CG  . ASN B 1 346 ? -52.723 19.860  -19.077 1.00 55.68  ? 343 ASN B CG  1 
ATOM   5407 O OD1 . ASN B 1 346 ? -53.373 19.804  -20.126 1.00 54.27  ? 343 ASN B OD1 1 
ATOM   5408 N ND2 . ASN B 1 346 ? -52.125 20.968  -18.661 1.00 49.29  ? 343 ASN B ND2 1 
ATOM   5409 N N   . ARG B 1 347 ? -52.932 15.540  -18.479 1.00 53.16  ? 344 ARG B N   1 
ATOM   5410 C CA  . ARG B 1 347 ? -52.608 14.181  -18.069 1.00 60.24  ? 344 ARG B CA  1 
ATOM   5411 C C   . ARG B 1 347 ? -51.327 13.735  -18.711 1.00 55.79  ? 344 ARG B C   1 
ATOM   5412 O O   . ARG B 1 347 ? -51.276 13.454  -19.897 1.00 53.72  ? 344 ARG B O   1 
ATOM   5413 C CB  . ARG B 1 347 ? -53.733 13.199  -18.415 1.00 60.23  ? 344 ARG B CB  1 
ATOM   5414 C CG  . ARG B 1 347 ? -53.975 12.141  -17.357 1.00 58.31  ? 344 ARG B CG  1 
ATOM   5415 C CD  . ARG B 1 347 ? -54.028 12.762  -15.976 1.00 58.46  ? 344 ARG B CD  1 
ATOM   5416 N NE  . ARG B 1 347 ? -55.359 12.665  -15.392 1.00 71.75  ? 344 ARG B NE  1 
ATOM   5417 C CZ  . ARG B 1 347 ? -56.022 13.689  -14.868 1.00 68.10  ? 344 ARG B CZ  1 
ATOM   5418 N NH1 . ARG B 1 347 ? -55.481 14.897  -14.851 1.00 65.27  ? 344 ARG B NH1 1 
ATOM   5419 N NH2 . ARG B 1 347 ? -57.229 13.508  -14.361 1.00 57.72  ? 344 ARG B NH2 1 
ATOM   5420 N N   . GLY B 1 348 ? -50.290 13.665  -17.907 1.00 56.34  ? 345 GLY B N   1 
ATOM   5421 C CA  . GLY B 1 348 ? -48.982 13.286  -18.404 1.00 56.39  ? 345 GLY B CA  1 
ATOM   5422 C C   . GLY B 1 348 ? -48.349 14.416  -19.189 1.00 50.78  ? 345 GLY B C   1 
ATOM   5423 O O   . GLY B 1 348 ? -48.451 15.599  -18.827 1.00 43.12  ? 345 GLY B O   1 
ATOM   5424 N N   . LYS B 1 349 ? -47.702 14.032  -20.293 1.00 48.73  ? 346 LYS B N   1 
ATOM   5425 C CA  . LYS B 1 349 ? -46.976 14.954  -21.154 1.00 50.65  ? 346 LYS B CA  1 
ATOM   5426 C C   . LYS B 1 349 ? -47.946 15.775  -21.998 1.00 50.39  ? 346 LYS B C   1 
ATOM   5427 O O   . LYS B 1 349 ? -48.866 15.220  -22.610 1.00 48.49  ? 346 LYS B O   1 
ATOM   5428 C CB  . LYS B 1 349 ? -46.025 14.165  -22.060 1.00 46.75  ? 346 LYS B CB  1 
ATOM   5429 C CG  . LYS B 1 349 ? -44.999 15.007  -22.801 1.00 46.59  ? 346 LYS B CG  1 
ATOM   5430 C CD  . LYS B 1 349 ? -44.045 15.676  -21.824 1.00 49.53  ? 346 LYS B CD  1 
ATOM   5431 C CE  . LYS B 1 349 ? -43.342 16.872  -22.447 1.00 46.45  ? 346 LYS B CE  1 
ATOM   5432 N NZ  . LYS B 1 349 ? -44.214 18.089  -22.583 1.00 42.75  ? 346 LYS B NZ  1 
ATOM   5433 N N   . VAL B 1 350 ? -47.744 17.094  -22.042 1.00 45.42  ? 347 VAL B N   1 
ATOM   5434 C CA  . VAL B 1 350 ? -48.540 17.969  -22.900 1.00 45.66  ? 347 VAL B CA  1 
ATOM   5435 C C   . VAL B 1 350 ? -47.775 18.238  -24.187 1.00 47.68  ? 347 VAL B C   1 
ATOM   5436 O O   . VAL B 1 350 ? -46.623 18.690  -24.150 1.00 50.66  ? 347 VAL B O   1 
ATOM   5437 C CB  . VAL B 1 350 ? -48.893 19.285  -22.199 1.00 46.27  ? 347 VAL B CB  1 
ATOM   5438 C CG1 . VAL B 1 350 ? -49.745 20.143  -23.135 1.00 38.57  ? 347 VAL B CG1 1 
ATOM   5439 C CG2 . VAL B 1 350 ? -49.620 18.991  -20.904 1.00 41.99  ? 347 VAL B CG2 1 
ATOM   5440 N N   . LEU B 1 351 ? -48.405 17.947  -25.322 1.00 41.96  ? 348 LEU B N   1 
ATOM   5441 C CA  . LEU B 1 351 ? -47.828 18.168  -26.637 1.00 40.21  ? 348 LEU B CA  1 
ATOM   5442 C C   . LEU B 1 351 ? -48.825 18.953  -27.467 1.00 43.43  ? 348 LEU B C   1 
ATOM   5443 O O   . LEU B 1 351 ? -49.961 19.198  -27.045 1.00 42.35  ? 348 LEU B O   1 
ATOM   5444 C CB  . LEU B 1 351 ? -47.507 16.861  -27.349 1.00 36.92  ? 348 LEU B CB  1 
ATOM   5445 C CG  . LEU B 1 351 ? -46.596 15.881  -26.641 1.00 40.82  ? 348 LEU B CG  1 
ATOM   5446 C CD1 . LEU B 1 351 ? -46.617 14.572  -27.389 1.00 46.77  ? 348 LEU B CD1 1 
ATOM   5447 C CD2 . LEU B 1 351 ? -45.195 16.436  -26.602 1.00 44.69  ? 348 LEU B CD2 1 
ATOM   5448 N N   . VAL B 1 352 ? -48.401 19.345  -28.664 1.00 39.21  ? 349 VAL B N   1 
ATOM   5449 C CA  . VAL B 1 352 ? -49.313 19.966  -29.623 1.00 39.28  ? 349 VAL B CA  1 
ATOM   5450 C C   . VAL B 1 352 ? -49.082 19.328  -30.979 1.00 37.58  ? 349 VAL B C   1 
ATOM   5451 O O   . VAL B 1 352 ? -47.960 19.351  -31.494 1.00 39.78  ? 349 VAL B O   1 
ATOM   5452 C CB  . VAL B 1 352 ? -49.140 21.488  -29.718 1.00 31.76  ? 349 VAL B CB  1 
ATOM   5453 C CG1 . VAL B 1 352 ? -49.946 22.006  -30.857 1.00 37.65  ? 349 VAL B CG1 1 
ATOM   5454 C CG2 . VAL B 1 352 ? -49.606 22.124  -28.449 1.00 31.56  ? 349 VAL B CG2 1 
ATOM   5455 N N   . ARG B 1 353 ? -50.132 18.756  -31.561 1.00 41.70  ? 350 ARG B N   1 
ATOM   5456 C CA  . ARG B 1 353 ? -50.027 18.183  -32.894 1.00 41.01  ? 350 ARG B CA  1 
ATOM   5457 C C   . ARG B 1 353 ? -50.283 19.288  -33.913 1.00 44.23  ? 350 ARG B C   1 
ATOM   5458 O O   . ARG B 1 353 ? -51.322 19.958  -33.861 1.00 46.09  ? 350 ARG B O   1 
ATOM   5459 C CB  . ARG B 1 353 ? -51.001 17.028  -33.084 1.00 42.21  ? 350 ARG B CB  1 
ATOM   5460 C CG  . ARG B 1 353 ? -50.676 16.228  -34.300 1.00 43.03  ? 350 ARG B CG  1 
ATOM   5461 C CD  . ARG B 1 353 ? -51.485 14.965  -34.361 1.00 50.52  ? 350 ARG B CD  1 
ATOM   5462 N NE  . ARG B 1 353 ? -52.009 14.793  -35.707 1.00 62.93  ? 350 ARG B NE  1 
ATOM   5463 C CZ  . ARG B 1 353 ? -53.097 15.405  -36.154 1.00 64.31  ? 350 ARG B CZ  1 
ATOM   5464 N NH1 . ARG B 1 353 ? -53.866 16.122  -35.347 1.00 61.39  ? 350 ARG B NH1 1 
ATOM   5465 N NH2 . ARG B 1 353 ? -53.406 15.316  -37.446 1.00 56.17  ? 350 ARG B NH2 1 
ATOM   5466 N N   . VAL B 1 354 ? -49.317 19.491  -34.807 1.00 36.19  ? 351 VAL B N   1 
ATOM   5467 C CA  . VAL B 1 354 ? -49.355 20.520  -35.834 1.00 37.53  ? 351 VAL B CA  1 
ATOM   5468 C C   . VAL B 1 354 ? -49.795 19.935  -37.169 1.00 39.83  ? 351 VAL B C   1 
ATOM   5469 O O   . VAL B 1 354 ? -50.991 19.792  -37.426 1.00 47.29  ? 351 VAL B O   1 
ATOM   5470 C CB  . VAL B 1 354 ? -47.995 21.191  -35.986 1.00 38.66  ? 351 VAL B CB  1 
ATOM   5471 C CG1 . VAL B 1 354 ? -47.992 22.039  -37.247 1.00 42.52  ? 351 VAL B CG1 1 
ATOM   5472 C CG2 . VAL B 1 354 ? -47.664 22.031  -34.754 1.00 34.70  ? 351 VAL B CG2 1 
HETATM 5473 P PA  . NAP C 2 .   ? -10.494 24.507  12.653  1.00 62.49  ? 501 NAP A PA  1 
HETATM 5474 O O1A . NAP C 2 .   ? -9.578  24.371  13.837  1.00 71.90  ? 501 NAP A O1A 1 
HETATM 5475 O O2A . NAP C 2 .   ? -9.960  24.931  11.322  1.00 63.34  ? 501 NAP A O2A 1 
HETATM 5476 O O5B . NAP C 2 .   ? -11.618 25.631  13.072  1.00 74.99  ? 501 NAP A O5B 1 
HETATM 5477 C C5B . NAP C 2 .   ? -11.175 26.973  13.314  1.00 73.68  ? 501 NAP A C5B 1 
HETATM 5478 C C4B . NAP C 2 .   ? -10.393 27.577  12.130  1.00 83.31  ? 501 NAP A C4B 1 
HETATM 5479 O O4B . NAP C 2 .   ? -11.236 27.988  11.033  1.00 82.42  ? 501 NAP A O4B 1 
HETATM 5480 C C3B . NAP C 2 .   ? -9.488  28.776  12.504  1.00 84.33  ? 501 NAP A C3B 1 
HETATM 5481 O O3B . NAP C 2 .   ? -8.124  28.420  12.568  1.00 78.30  ? 501 NAP A O3B 1 
HETATM 5482 C C2B . NAP C 2 .   ? -9.833  29.880  11.451  1.00 79.65  ? 501 NAP A C2B 1 
HETATM 5483 O O2B . NAP C 2 .   ? -8.756  30.081  10.590  1.00 70.73  ? 501 NAP A O2B 1 
HETATM 5484 C C1B . NAP C 2 .   ? -10.999 29.321  10.617  1.00 79.98  ? 501 NAP A C1B 1 
HETATM 5485 N N9A . NAP C 2 .   ? -12.222 30.117  10.685  1.00 74.43  ? 501 NAP A N9A 1 
HETATM 5486 C C8A . NAP C 2 .   ? -12.910 30.528  11.800  1.00 70.61  ? 501 NAP A C8A 1 
HETATM 5487 N N7A . NAP C 2 .   ? -13.977 31.219  11.528  1.00 65.20  ? 501 NAP A N7A 1 
HETATM 5488 C C5A . NAP C 2 .   ? -14.013 31.274  10.165  1.00 64.62  ? 501 NAP A C5A 1 
HETATM 5489 C C6A . NAP C 2 .   ? -14.927 31.875  9.279   1.00 67.17  ? 501 NAP A C6A 1 
HETATM 5490 N N6A . NAP C 2 .   ? -15.995 32.550  9.733   1.00 65.84  ? 501 NAP A N6A 1 
HETATM 5491 N N1A . NAP C 2 .   ? -14.687 31.758  7.959   1.00 62.65  ? 501 NAP A N1A 1 
HETATM 5492 C C2A . NAP C 2 .   ? -13.606 31.077  7.549   1.00 64.57  ? 501 NAP A C2A 1 
HETATM 5493 N N3A . NAP C 2 .   ? -12.683 30.464  8.290   1.00 72.35  ? 501 NAP A N3A 1 
HETATM 5494 C C4A . NAP C 2 .   ? -12.932 30.595  9.606   1.00 71.50  ? 501 NAP A C4A 1 
HETATM 5495 O O3  . NAP C 2 .   ? -11.218 23.068  12.289  1.00 58.71  ? 501 NAP A O3  1 
HETATM 5496 P PN  . NAP C 2 .   ? -10.566 21.805  11.378  1.00 74.29  ? 501 NAP A PN  1 
HETATM 5497 O O1N . NAP C 2 .   ? -9.672  20.928  12.222  1.00 58.46  ? 501 NAP A O1N 1 
HETATM 5498 O O2N . NAP C 2 .   ? -10.192 22.236  9.965   1.00 45.94  ? 501 NAP A O2N 1 
HETATM 5499 O O5D . NAP C 2 .   ? -11.935 20.913  11.177  1.00 63.63  ? 501 NAP A O5D 1 
HETATM 5500 C C5D . NAP C 2 .   ? -12.964 21.361  10.326  1.00 54.97  ? 501 NAP A C5D 1 
HETATM 5501 C C4D . NAP C 2 .   ? -14.296 21.594  11.059  1.00 59.14  ? 501 NAP A C4D 1 
HETATM 5502 O O4D . NAP C 2 .   ? -15.197 20.481  10.785  1.00 51.87  ? 501 NAP A O4D 1 
HETATM 5503 C C3D . NAP C 2 .   ? -14.217 21.749  12.578  1.00 58.18  ? 501 NAP A C3D 1 
HETATM 5504 O O3D . NAP C 2 .   ? -14.845 22.969  12.890  1.00 58.97  ? 501 NAP A O3D 1 
HETATM 5505 C C2D . NAP C 2 .   ? -15.003 20.535  13.122  1.00 53.15  ? 501 NAP A C2D 1 
HETATM 5506 O O2D . NAP C 2 .   ? -15.863 20.870  14.166  1.00 55.72  ? 501 NAP A O2D 1 
HETATM 5507 C C1D . NAP C 2 .   ? -15.807 19.994  11.914  1.00 48.99  ? 501 NAP A C1D 1 
HETATM 5508 N N1N . NAP C 2 .   ? -15.783 18.510  11.732  1.00 41.52  ? 501 NAP A N1N 1 
HETATM 5509 C C2N . NAP C 2 .   ? -16.799 17.828  11.179  1.00 41.37  ? 501 NAP A C2N 1 
HETATM 5510 C C3N . NAP C 2 .   ? -16.717 16.452  10.991  1.00 39.83  ? 501 NAP A C3N 1 
HETATM 5511 C C7N . NAP C 2 .   ? -17.822 15.593  10.424  1.00 38.60  ? 501 NAP A C7N 1 
HETATM 5512 O O7N . NAP C 2 .   ? -17.672 14.375  10.444  1.00 35.62  ? 501 NAP A O7N 1 
HETATM 5513 N N7N . NAP C 2 .   ? -18.918 16.218  9.956   1.00 39.51  ? 501 NAP A N7N 1 
HETATM 5514 C C4N . NAP C 2 .   ? -15.549 15.802  11.382  1.00 42.43  ? 501 NAP A C4N 1 
HETATM 5515 C C5N . NAP C 2 .   ? -14.516 16.537  11.938  1.00 46.62  ? 501 NAP A C5N 1 
HETATM 5516 C C6N . NAP C 2 .   ? -14.653 17.898  12.091  1.00 43.49  ? 501 NAP A C6N 1 
HETATM 5517 P P2B . NAP C 2 .   ? -7.645  31.362  10.962  1.00 84.20  ? 501 NAP A P2B 1 
HETATM 5518 O O1X . NAP C 2 .   ? -8.575  32.499  11.373  1.00 80.91  ? 501 NAP A O1X 1 
HETATM 5519 O O2X . NAP C 2 .   ? -6.796  30.738  12.064  1.00 89.55  ? 501 NAP A O2X 1 
HETATM 5520 O O3X . NAP C 2 .   ? -6.874  31.560  9.660   1.00 70.61  ? 501 NAP A O3X 1 
HETATM 5521 C C1  . E8T D 3 .   ? -18.770 15.773  14.626  1.00 41.69  ? 502 E8T A C1  1 
HETATM 5522 C C2  . E8T D 3 .   ? -19.301 14.915  15.809  1.00 48.55  ? 502 E8T A C2  1 
HETATM 5523 C C3  . E8T D 3 .   ? -19.911 16.127  13.719  1.00 46.49  ? 502 E8T A C3  1 
HETATM 5524 C C4  . E8T D 3 .   ? -20.558 15.476  16.513  1.00 48.39  ? 502 E8T A C4  1 
HETATM 5525 C C6  . E8T D 3 .   ? -22.670 17.757  17.155  1.00 55.66  ? 502 E8T A C6  1 
HETATM 5526 O O5  . E8T D 3 .   ? -23.254 16.793  16.634  1.00 55.40  ? 502 E8T A O5  1 
HETATM 5527 C C7  . E8T D 3 .   ? -21.218 17.718  17.505  1.00 56.18  ? 502 E8T A C7  1 
HETATM 5528 C C8  . E8T D 3 .   ? -20.336 16.759  17.252  1.00 49.74  ? 502 E8T A C8  1 
HETATM 5529 C C9  . E8T D 3 .   ? -24.976 19.423  15.711  1.00 54.11  ? 502 E8T A C9  1 
HETATM 5530 C C10 . E8T D 3 .   ? -24.722 19.149  17.188  1.00 56.77  ? 502 E8T A C10 1 
HETATM 5531 N N11 . E8T D 3 .   ? -23.306 18.912  17.477  1.00 48.63  ? 502 E8T A N11 1 
HETATM 5532 C C12 . E8T D 3 .   ? -24.368 20.724  15.197  1.00 53.49  ? 502 E8T A C12 1 
HETATM 5533 C C13 . E8T D 3 .   ? -21.824 17.467  12.957  1.00 50.05  ? 502 E8T A C13 1 
HETATM 5534 C C14 . E8T D 3 .   ? -20.607 17.255  13.708  1.00 44.28  ? 502 E8T A C14 1 
HETATM 5535 C C15 . E8T D 3 .   ? -23.955 18.755  12.445  1.00 47.11  ? 502 E8T A C15 1 
HETATM 5536 C C16 . E8T D 3 .   ? -22.667 18.557  13.126  1.00 50.79  ? 502 E8T A C16 1 
HETATM 5537 N N17 . E8T D 3 .   ? -24.491 19.911  12.848  1.00 48.28  ? 502 E8T A N17 1 
HETATM 5538 C C18 . E8T D 3 .   ? -23.682 20.602  13.834  1.00 53.82  ? 502 E8T A C18 1 
HETATM 5539 C C19 . E8T D 3 .   ? -22.440 19.715  13.947  1.00 51.87  ? 502 E8T A C19 1 
HETATM 5540 O O20 . E8T D 3 .   ? -24.467 17.977  11.611  1.00 50.99  ? 502 E8T A O20 1 
HETATM 5541 O O21 . E8T D 3 .   ? -21.478 19.997  14.656  1.00 50.25  ? 502 E8T A O21 1 
HETATM 5542 C C22 . E8T D 3 .   ? -18.154 14.649  16.755  1.00 44.34  ? 502 E8T A C22 1 
HETATM 5543 C C23 . E8T D 3 .   ? -17.013 13.896  16.048  1.00 37.68  ? 502 E8T A C23 1 
HETATM 5544 C C24 . E8T D 3 .   ? -16.467 14.682  14.866  1.00 44.90  ? 502 E8T A C24 1 
HETATM 5545 C C25 . E8T D 3 .   ? -17.613 15.049  13.927  1.00 42.08  ? 502 E8T A C25 1 
HETATM 5546 C C26 . E8T D 3 .   ? -18.415 13.759  17.969  1.00 37.97  ? 502 E8T A C26 1 
HETATM 5547 C C27 . E8T D 3 .   ? -17.012 13.364  18.437  1.00 37.90  ? 502 E8T A C27 1 
HETATM 5548 C C28 . E8T D 3 .   ? -16.066 13.575  17.221  1.00 36.15  ? 502 E8T A C28 1 
HETATM 5549 C C29 . E8T D 3 .   ? -16.794 11.884  18.766  1.00 34.08  ? 502 E8T A C29 1 
HETATM 5550 C C30 . E8T D 3 .   ? -15.295 11.677  18.517  1.00 34.65  ? 502 E8T A C30 1 
HETATM 5551 C C31 . E8T D 3 .   ? -15.122 12.348  17.131  1.00 35.25  ? 502 E8T A C31 1 
HETATM 5552 O O32 . E8T D 3 .   ? -15.427 13.962  14.191  1.00 42.02  ? 502 E8T A O32 1 
HETATM 5553 C C33 . E8T D 3 .   ? -13.690 12.703  16.762  1.00 32.37  ? 502 E8T A C33 1 
HETATM 5554 C C34 . E8T D 3 .   ? -14.772 10.251  18.691  1.00 38.10  ? 502 E8T A C34 1 
HETATM 5555 O O35 . E8T D 3 .   ? -22.218 16.502  12.133  1.00 44.69  ? 502 E8T A O35 1 
HETATM 5556 C C36 . E8T D 3 .   ? -14.948 9.722   20.107  1.00 33.37  ? 502 E8T A C36 1 
HETATM 5557 C C1  . E8T E 3 .   ? -33.484 21.746  -19.439 1.00 33.63  ? 503 E8T A C1  1 
HETATM 5558 C C2  . E8T E 3 .   ? -32.796 22.264  -20.733 1.00 35.24  ? 503 E8T A C2  1 
HETATM 5559 C C3  . E8T E 3 .   ? -32.725 22.105  -18.202 1.00 33.88  ? 503 E8T A C3  1 
HETATM 5560 C C4  . E8T E 3 .   ? -32.582 23.792  -20.739 1.00 35.22  ? 503 E8T A C4  1 
HETATM 5561 C C6  . E8T E 3 .   ? -32.687 26.515  -19.248 1.00 35.62  ? 503 E8T A C6  1 
HETATM 5562 O O5  . E8T E 3 .   ? -31.513 26.134  -19.328 1.00 38.34  ? 503 E8T A O5  1 
HETATM 5563 C C7  . E8T E 3 .   ? -33.857 25.753  -19.774 1.00 35.38  ? 503 E8T A C7  1 
HETATM 5564 C C8  . E8T E 3 .   ? -33.807 24.589  -20.407 1.00 37.70  ? 503 E8T A C8  1 
HETATM 5565 C C9  . E8T E 3 .   ? -31.627 27.882  -16.652 1.00 31.14  ? 503 E8T A C9  1 
HETATM 5566 C C10 . E8T E 3 .   ? -31.903 28.443  -18.030 1.00 39.07  ? 503 E8T A C10 1 
HETATM 5567 N N11 . E8T E 3 .   ? -32.969 27.674  -18.670 1.00 34.51  ? 503 E8T A N11 1 
HETATM 5568 C C12 . E8T E 3 .   ? -32.799 28.014  -15.678 1.00 31.77  ? 503 E8T A C12 1 
HETATM 5569 C C13 . E8T E 3 .   ? -32.212 23.461  -16.258 1.00 31.02  ? 503 E8T A C13 1 
HETATM 5570 C C14 . E8T E 3 .   ? -32.929 23.180  -17.460 1.00 35.09  ? 503 E8T A C14 1 
HETATM 5571 C C15 . E8T E 3 .   ? -31.297 25.169  -14.633 1.00 30.87  ? 503 E8T A C15 1 
HETATM 5572 C C16 . E8T E 3 .   ? -32.287 24.660  -15.575 1.00 33.89  ? 503 E8T A C16 1 
HETATM 5573 N N17 . E8T E 3 .   ? -31.674 26.377  -14.198 1.00 35.72  ? 503 E8T A N17 1 
HETATM 5574 C C18 . E8T E 3 .   ? -32.942 26.809  -14.757 1.00 28.84  ? 503 E8T A C18 1 
HETATM 5575 C C19 . E8T E 3 .   ? -33.378 25.597  -15.581 1.00 35.60  ? 503 E8T A C19 1 
HETATM 5576 O O20 . E8T E 3 .   ? -30.252 24.565  -14.318 1.00 31.77  ? 503 E8T A O20 1 
HETATM 5577 O O21 . E8T E 3 .   ? -34.453 25.535  -16.171 1.00 40.19  ? 503 E8T A O21 1 
HETATM 5578 C C22 . E8T E 3 .   ? -33.616 21.847  -21.930 1.00 34.64  ? 503 E8T A C22 1 
HETATM 5579 C C23 . E8T E 3 .   ? -33.872 20.328  -21.981 1.00 32.74  ? 503 E8T A C23 1 
HETATM 5580 C C24 . E8T E 3 .   ? -34.615 19.900  -20.727 1.00 35.65  ? 503 E8T A C24 1 
HETATM 5581 C C25 . E8T E 3 .   ? -33.768 20.240  -19.507 1.00 36.07  ? 503 E8T A C25 1 
HETATM 5582 C C26 . E8T E 3 .   ? -33.092 22.141  -23.338 1.00 36.92  ? 503 E8T A C26 1 
HETATM 5583 C C27 . E8T E 3 .   ? -33.974 21.275  -24.243 1.00 30.64  ? 503 E8T A C27 1 
HETATM 5584 C C28 . E8T E 3 .   ? -34.599 20.174  -23.335 1.00 28.30  ? 503 E8T A C28 1 
HETATM 5585 C C29 . E8T E 3 .   ? -33.248 20.465  -25.322 1.00 32.55  ? 503 E8T A C29 1 
HETATM 5586 C C30 . E8T E 3 .   ? -34.170 19.246  -25.534 1.00 40.07  ? 503 E8T A C30 1 
HETATM 5587 C C31 . E8T E 3 .   ? -34.512 18.819  -24.078 1.00 33.89  ? 503 E8T A C31 1 
HETATM 5588 O O32 . E8T E 3 .   ? -34.988 18.524  -20.751 1.00 35.44  ? 503 E8T A O32 1 
HETATM 5589 C C33 . E8T E 3 .   ? -35.733 17.928  -23.903 1.00 33.73  ? 503 E8T A C33 1 
HETATM 5590 C C34 . E8T E 3 .   ? -33.638 18.198  -26.511 1.00 34.07  ? 503 E8T A C34 1 
HETATM 5591 O O35 . E8T E 3 .   ? -31.381 22.531  -15.827 1.00 29.41  ? 503 E8T A O35 1 
HETATM 5592 C C36 . E8T E 3 .   ? -33.335 18.779  -27.865 1.00 33.15  ? 503 E8T A C36 1 
HETATM 5593 P PA  . NAP F 2 .   ? -44.947 18.905  -14.917 1.00 47.06  ? 501 NAP B PA  1 
HETATM 5594 O O1A . NAP F 2 .   ? -46.133 18.490  -15.730 1.00 45.56  ? 501 NAP B O1A 1 
HETATM 5595 O O2A . NAP F 2 .   ? -44.619 18.317  -13.570 1.00 49.18  ? 501 NAP B O2A 1 
HETATM 5596 O O5B . NAP F 2 .   ? -44.955 20.543  -14.845 1.00 46.79  ? 501 NAP B O5B 1 
HETATM 5597 C C5B . NAP F 2 .   ? -46.116 21.252  -14.458 1.00 51.83  ? 501 NAP B C5B 1 
HETATM 5598 C C4B . NAP F 2 .   ? -46.838 20.503  -13.332 1.00 59.39  ? 501 NAP B C4B 1 
HETATM 5599 O O4B . NAP F 2 .   ? -46.268 20.770  -12.039 1.00 57.77  ? 501 NAP B O4B 1 
HETATM 5600 C C3B . NAP F 2 .   ? -48.337 20.830  -13.277 1.00 53.45  ? 501 NAP B C3B 1 
HETATM 5601 O O3B . NAP F 2 .   ? -49.081 19.791  -13.851 1.00 59.77  ? 501 NAP B O3B 1 
HETATM 5602 C C2B . NAP F 2 .   ? -48.629 20.987  -11.772 1.00 55.14  ? 501 NAP B C2B 1 
HETATM 5603 O O2B . NAP F 2 .   ? -49.244 19.797  -11.428 1.00 61.64  ? 501 NAP B O2B 1 
HETATM 5604 C C1B . NAP F 2 .   ? -47.264 20.975  -11.068 1.00 56.63  ? 501 NAP B C1B 1 
HETATM 5605 N N9A . NAP F 2 .   ? -46.972 22.113  -10.192 1.00 51.45  ? 501 NAP B N9A 1 
HETATM 5606 C C8A . NAP F 2 .   ? -47.034 23.463  -10.421 1.00 49.19  ? 501 NAP B C8A 1 
HETATM 5607 N N7A . NAP F 2 .   ? -46.704 24.197  -9.395  1.00 46.24  ? 501 NAP B N7A 1 
HETATM 5608 C C5A . NAP F 2 .   ? -46.400 23.287  -8.414  1.00 50.33  ? 501 NAP B C5A 1 
HETATM 5609 C C6A . NAP F 2 .   ? -45.962 23.433  -7.073  1.00 47.82  ? 501 NAP B C6A 1 
HETATM 5610 N N6A . NAP F 2 .   ? -45.765 24.625  -6.494  1.00 42.86  ? 501 NAP B N6A 1 
HETATM 5611 N N1A . NAP F 2 .   ? -45.743 22.311  -6.368  1.00 47.78  ? 501 NAP B N1A 1 
HETATM 5612 C C2A . NAP F 2 .   ? -45.942 21.110  -6.952  1.00 51.47  ? 501 NAP B C2A 1 
HETATM 5613 N N3A . NAP F 2 .   ? -46.343 20.839  -8.193  1.00 50.44  ? 501 NAP B N3A 1 
HETATM 5614 C C4A . NAP F 2 .   ? -46.560 21.978  -8.889  1.00 54.88  ? 501 NAP B C4A 1 
HETATM 5615 O O3  . NAP F 2 .   ? -43.580 18.651  -15.764 1.00 48.35  ? 501 NAP B O3  1 
HETATM 5616 P PN  . NAP F 2 .   ? -42.898 17.206  -16.104 1.00 61.63  ? 501 NAP B PN  1 
HETATM 5617 O O1N . NAP F 2 .   ? -42.898 17.034  -17.590 1.00 47.90  ? 501 NAP B O1N 1 
HETATM 5618 O O2N . NAP F 2 .   ? -43.389 16.189  -15.093 1.00 50.49  ? 501 NAP B O2N 1 
HETATM 5619 O O5D . NAP F 2 .   ? -41.339 17.562  -15.687 1.00 56.84  ? 501 NAP B O5D 1 
HETATM 5620 C C5D . NAP F 2 .   ? -40.950 17.766  -14.357 1.00 47.62  ? 501 NAP B C5D 1 
HETATM 5621 C C4D . NAP F 2 .   ? -40.095 19.021  -14.141 1.00 47.44  ? 501 NAP B C4D 1 
HETATM 5622 O O4D . NAP F 2 .   ? -38.712 18.729  -14.469 1.00 48.92  ? 501 NAP B O4D 1 
HETATM 5623 C C3D . NAP F 2 .   ? -40.432 20.264  -14.953 1.00 46.18  ? 501 NAP B C3D 1 
HETATM 5624 O O3D . NAP F 2 .   ? -40.163 21.358  -14.102 1.00 45.97  ? 501 NAP B O3D 1 
HETATM 5625 C C2D . NAP F 2 .   ? -39.403 20.210  -16.101 1.00 44.15  ? 501 NAP B C2D 1 
HETATM 5626 O O2D . NAP F 2 .   ? -39.119 21.441  -16.693 1.00 40.75  ? 501 NAP B O2D 1 
HETATM 5627 C C1D . NAP F 2 .   ? -38.184 19.662  -15.333 1.00 45.57  ? 501 NAP B C1D 1 
HETATM 5628 N N1N . NAP F 2 .   ? -37.143 18.954  -16.151 1.00 39.94  ? 501 NAP B N1N 1 
HETATM 5629 C C2N . NAP F 2 .   ? -35.846 18.983  -15.798 1.00 39.42  ? 501 NAP B C2N 1 
HETATM 5630 C C3N . NAP F 2 .   ? -34.896 18.294  -16.547 1.00 43.15  ? 501 NAP B C3N 1 
HETATM 5631 C C7N . NAP F 2 .   ? -33.430 18.310  -16.177 1.00 37.04  ? 501 NAP B C7N 1 
HETATM 5632 O O7N . NAP F 2 .   ? -32.605 17.698  -16.836 1.00 33.00  ? 501 NAP B O7N 1 
HETATM 5633 N N7N . NAP F 2 .   ? -33.142 19.019  -15.087 1.00 33.59  ? 501 NAP B N7N 1 
HETATM 5634 C C4N . NAP F 2 .   ? -35.311 17.573  -17.665 1.00 35.00  ? 501 NAP B C4N 1 
HETATM 5635 C C5N . NAP F 2 .   ? -36.648 17.562  -18.002 1.00 34.83  ? 501 NAP B C5N 1 
HETATM 5636 C C6N . NAP F 2 .   ? -37.547 18.256  -17.222 1.00 40.92  ? 501 NAP B C6N 1 
HETATM 5637 P P2B . NAP F 2 .   ? -50.872 19.856  -10.861 1.00 64.97  ? 501 NAP B P2B 1 
HETATM 5638 O O1X . NAP F 2 .   ? -50.999 21.222  -10.179 1.00 52.72  ? 501 NAP B O1X 1 
HETATM 5639 O O2X . NAP F 2 .   ? -51.645 19.691  -12.173 1.00 53.94  ? 501 NAP B O2X 1 
HETATM 5640 O O3X . NAP F 2 .   ? -50.795 18.648  -9.937  1.00 55.49  ? 501 NAP B O3X 1 
HETATM 5641 O O   . HOH G 4 .   ? -26.787 27.346  18.592  1.00 42.35  ? 601 HOH A O   1 
HETATM 5642 O O   . HOH G 4 .   ? -17.490 9.908   -5.127  1.00 42.04  ? 602 HOH A O   1 
HETATM 5643 O O   . HOH G 4 .   ? -17.116 7.711   27.130  1.00 35.76  ? 603 HOH A O   1 
HETATM 5644 O O   . HOH G 4 .   ? -4.114  12.995  -3.035  1.00 31.71  ? 604 HOH A O   1 
HETATM 5645 O O   . HOH G 4 .   ? 3.293   15.923  20.044  1.00 38.57  ? 605 HOH A O   1 
HETATM 5646 O O   . HOH G 4 .   ? -15.232 17.601  -10.553 1.00 26.69  ? 606 HOH A O   1 
HETATM 5647 O O   . HOH G 4 .   ? -7.250  21.974  16.909  1.00 38.26  ? 607 HOH A O   1 
HETATM 5648 O O   . HOH G 4 .   ? -35.621 27.153  -17.662 1.00 33.60  ? 608 HOH A O   1 
HETATM 5649 O O   . HOH G 4 .   ? -11.148 12.229  28.879  1.00 36.77  ? 609 HOH A O   1 
HETATM 5650 O O   . HOH G 4 .   ? -1.818  -0.267  8.942   1.00 42.03  ? 610 HOH A O   1 
HETATM 5651 O O   . HOH G 4 .   ? 12.800  7.384   19.010  1.00 27.52  ? 611 HOH A O   1 
HETATM 5652 O O   . HOH G 4 .   ? -12.967 16.757  20.896  1.00 34.69  ? 612 HOH A O   1 
HETATM 5653 O O   . HOH G 4 .   ? -19.591 -4.119  33.398  1.00 47.96  ? 613 HOH A O   1 
HETATM 5654 O O   . HOH G 4 .   ? -20.808 37.227  5.827   1.00 47.28  ? 614 HOH A O   1 
HETATM 5655 O O   . HOH G 4 .   ? -27.771 35.264  4.755   1.00 40.85  ? 615 HOH A O   1 
HETATM 5656 O O   . HOH G 4 .   ? -14.355 -0.785  6.873   1.00 43.82  ? 616 HOH A O   1 
HETATM 5657 O O   . HOH G 4 .   ? -9.702  14.640  18.206  1.00 31.61  ? 617 HOH A O   1 
HETATM 5658 O O   . HOH G 4 .   ? -10.719 4.963   1.530   1.00 28.39  ? 618 HOH A O   1 
HETATM 5659 O O   . HOH G 4 .   ? -4.563  6.038   15.705  1.00 30.08  ? 619 HOH A O   1 
HETATM 5660 O O   . HOH G 4 .   ? -26.482 17.892  9.890   1.00 39.47  ? 620 HOH A O   1 
HETATM 5661 O O   . HOH G 4 .   ? -12.489 5.723   17.576  1.00 29.41  ? 621 HOH A O   1 
HETATM 5662 O O   . HOH G 4 .   ? -28.464 24.978  -12.374 1.00 36.30  ? 622 HOH A O   1 
HETATM 5663 O O   . HOH G 4 .   ? -14.707 35.580  24.905  1.00 39.81  ? 623 HOH A O   1 
HETATM 5664 O O   . HOH G 4 .   ? -17.120 12.566  27.632  1.00 36.95  ? 624 HOH A O   1 
HETATM 5665 O O   . HOH G 4 .   ? -6.597  31.283  25.642  1.00 38.22  ? 625 HOH A O   1 
HETATM 5666 O O   . HOH G 4 .   ? -3.285  2.865   17.270  1.00 38.19  ? 626 HOH A O   1 
HETATM 5667 O O   . HOH G 4 .   ? -9.312  28.110  -12.016 1.00 39.55  ? 627 HOH A O   1 
HETATM 5668 O O   . HOH G 4 .   ? -18.805 8.574   -0.127  1.00 36.90  ? 628 HOH A O   1 
HETATM 5669 O O   . HOH G 4 .   ? 3.993   13.644  25.540  1.00 33.96  ? 629 HOH A O   1 
HETATM 5670 O O   . HOH G 4 .   ? -24.521 27.726  6.020   1.00 40.77  ? 630 HOH A O   1 
HETATM 5671 O O   . HOH G 4 .   ? -31.211 25.985  -1.133  1.00 46.18  ? 631 HOH A O   1 
HETATM 5672 O O   . HOH G 4 .   ? -5.362  12.588  -9.419  1.00 32.07  ? 632 HOH A O   1 
HETATM 5673 O O   . HOH G 4 .   ? -15.712 19.668  -12.315 1.00 25.15  ? 633 HOH A O   1 
HETATM 5674 O O   . HOH G 4 .   ? 0.850   -1.038  22.449  1.00 32.29  ? 634 HOH A O   1 
HETATM 5675 O O   . HOH G 4 .   ? -13.539 5.794   20.207  1.00 28.15  ? 635 HOH A O   1 
HETATM 5676 O O   . HOH G 4 .   ? -19.747 11.960  -6.578  1.00 35.20  ? 636 HOH A O   1 
HETATM 5677 O O   . HOH G 4 .   ? 0.416   0.957   27.103  1.00 38.35  ? 637 HOH A O   1 
HETATM 5678 O O   . HOH G 4 .   ? -2.213  14.963  14.875  1.00 28.10  ? 638 HOH A O   1 
HETATM 5679 O O   . HOH G 4 .   ? -2.688  -0.382  24.423  1.00 32.13  ? 639 HOH A O   1 
HETATM 5680 O O   . HOH G 4 .   ? -13.420 27.066  37.583  1.00 41.00  ? 640 HOH A O   1 
HETATM 5681 O O   . HOH G 4 .   ? 1.082   4.477   11.731  1.00 36.50  ? 641 HOH A O   1 
HETATM 5682 O O   . HOH G 4 .   ? -31.364 11.609  20.596  1.00 56.34  ? 642 HOH A O   1 
HETATM 5683 O O   . HOH G 4 .   ? -20.889 -3.043  31.374  1.00 46.01  ? 643 HOH A O   1 
HETATM 5684 O O   . HOH G 4 .   ? -11.697 22.578  6.583   1.00 36.80  ? 644 HOH A O   1 
HETATM 5685 O O   . HOH G 4 .   ? -23.652 11.805  -8.216  1.00 38.82  ? 645 HOH A O   1 
HETATM 5686 O O   . HOH G 4 .   ? -19.203 10.779  5.772   1.00 30.77  ? 646 HOH A O   1 
HETATM 5687 O O   . HOH G 4 .   ? -5.975  1.957   16.421  1.00 32.53  ? 647 HOH A O   1 
HETATM 5688 O O   . HOH G 4 .   ? -9.502  12.858  -4.102  1.00 33.58  ? 648 HOH A O   1 
HETATM 5689 O O   . HOH G 4 .   ? -2.290  18.507  34.405  1.00 39.37  ? 649 HOH A O   1 
HETATM 5690 O O   . HOH G 4 .   ? -13.498 -3.209  41.185  1.00 36.38  ? 650 HOH A O   1 
HETATM 5691 O O   . HOH G 4 .   ? -20.153 2.080   31.396  1.00 41.17  ? 651 HOH A O   1 
HETATM 5692 O O   . HOH G 4 .   ? -14.377 2.558   1.136   1.00 30.06  ? 652 HOH A O   1 
HETATM 5693 O O   . HOH G 4 .   ? -37.644 17.244  -21.305 1.00 39.48  ? 653 HOH A O   1 
HETATM 5694 O O   . HOH G 4 .   ? -29.891 31.413  17.565  1.00 49.19  ? 654 HOH A O   1 
HETATM 5695 O O   . HOH G 4 .   ? -21.674 20.393  -20.445 1.00 33.05  ? 655 HOH A O   1 
HETATM 5696 O O   . HOH G 4 .   ? -12.756 15.368  14.626  1.00 34.61  ? 656 HOH A O   1 
HETATM 5697 O O   . HOH G 4 .   ? -19.059 8.445   33.421  1.00 35.37  ? 657 HOH A O   1 
HETATM 5698 O O   . HOH G 4 .   ? 4.404   8.335   21.575  1.00 33.83  ? 658 HOH A O   1 
HETATM 5699 O O   . HOH G 4 .   ? -6.234  35.060  -12.129 1.00 37.08  ? 659 HOH A O   1 
HETATM 5700 O O   . HOH G 4 .   ? -11.426 8.868   -5.172  1.00 39.65  ? 660 HOH A O   1 
HETATM 5701 O O   . HOH G 4 .   ? 2.692   11.413  22.258  1.00 34.81  ? 661 HOH A O   1 
HETATM 5702 O O   . HOH G 4 .   ? -19.642 3.662   5.304   1.00 39.17  ? 662 HOH A O   1 
HETATM 5703 O O   . HOH G 4 .   ? -11.066 0.921   3.032   1.00 36.34  ? 663 HOH A O   1 
HETATM 5704 O O   . HOH G 4 .   ? -29.907 28.720  -12.342 1.00 31.87  ? 664 HOH A O   1 
HETATM 5705 O O   . HOH G 4 .   ? -24.134 27.263  37.251  1.00 35.95  ? 665 HOH A O   1 
HETATM 5706 O O   . HOH G 4 .   ? -11.902 22.837  42.465  1.00 51.52  ? 666 HOH A O   1 
HETATM 5707 O O   . HOH G 4 .   ? -23.905 30.112  -12.823 1.00 42.82  ? 667 HOH A O   1 
HETATM 5708 O O   . HOH G 4 .   ? -20.442 26.581  23.951  1.00 49.27  ? 668 HOH A O   1 
HETATM 5709 O O   . HOH G 4 .   ? -12.207 18.353  14.253  1.00 43.19  ? 669 HOH A O   1 
HETATM 5710 O O   . HOH G 4 .   ? -23.071 17.982  -21.677 1.00 32.44  ? 670 HOH A O   1 
HETATM 5711 O O   . HOH G 4 .   ? -24.632 31.670  -11.284 1.00 42.44  ? 671 HOH A O   1 
HETATM 5712 O O   . HOH G 4 .   ? -3.262  8.681   38.495  1.00 37.26  ? 672 HOH A O   1 
HETATM 5713 O O   . HOH G 4 .   ? -12.538 3.497   -1.269  1.00 39.01  ? 673 HOH A O   1 
HETATM 5714 O O   . HOH G 4 .   ? -23.387 7.708   14.774  1.00 40.12  ? 674 HOH A O   1 
HETATM 5715 O O   . HOH G 4 .   ? 11.418  7.853   15.500  1.00 43.94  ? 675 HOH A O   1 
HETATM 5716 O O   . HOH G 4 .   ? -6.135  18.850  -17.313 1.00 33.04  ? 676 HOH A O   1 
HETATM 5717 O O   . HOH G 4 .   ? -28.603 37.172  13.406  1.00 36.90  ? 677 HOH A O   1 
HETATM 5718 O O   . HOH G 4 .   ? -4.172  14.419  36.224  1.00 37.10  ? 678 HOH A O   1 
HETATM 5719 O O   . HOH G 4 .   ? -8.780  -9.583  26.013  1.00 41.31  ? 679 HOH A O   1 
HETATM 5720 O O   . HOH G 4 .   ? -22.263 6.332   13.478  1.00 37.38  ? 680 HOH A O   1 
HETATM 5721 O O   . HOH G 4 .   ? -23.845 10.258  -6.061  1.00 29.18  ? 681 HOH A O   1 
HETATM 5722 O O   . HOH H 4 .   ? -51.073 4.629   -27.249 1.00 51.29  ? 601 HOH B O   1 
HETATM 5723 O O   . HOH H 4 .   ? -28.385 5.073   -0.833  1.00 45.70  ? 602 HOH B O   1 
HETATM 5724 O O   . HOH H 4 .   ? -35.512 30.468  -27.633 1.00 29.31  ? 603 HOH B O   1 
HETATM 5725 O O   . HOH H 4 .   ? -40.773 15.734  -10.159 1.00 39.28  ? 604 HOH B O   1 
HETATM 5726 O O   . HOH H 4 .   ? -39.919 16.753  -25.087 1.00 30.80  ? 605 HOH B O   1 
HETATM 5727 O O   . HOH H 4 .   ? -39.363 42.175  -23.378 1.00 31.31  ? 606 HOH B O   1 
HETATM 5728 O O   . HOH H 4 .   ? -39.452 18.350  -22.750 1.00 32.97  ? 607 HOH B O   1 
HETATM 5729 O O   . HOH H 4 .   ? -42.171 6.246   5.725   1.00 56.52  ? 608 HOH B O   1 
HETATM 5730 O O   . HOH H 4 .   ? -31.607 29.551  -21.189 1.00 39.93  ? 609 HOH B O   1 
HETATM 5731 O O   . HOH H 4 .   ? -34.406 39.170  -32.715 1.00 23.09  ? 610 HOH B O   1 
HETATM 5732 O O   . HOH H 4 .   ? -32.231 13.855  -28.611 1.00 35.89  ? 611 HOH B O   1 
HETATM 5733 O O   . HOH H 4 .   ? -45.249 38.446  -14.047 1.00 44.91  ? 612 HOH B O   1 
HETATM 5734 O O   . HOH H 4 .   ? -40.676 33.291  -19.348 1.00 32.99  ? 613 HOH B O   1 
HETATM 5735 O O   . HOH H 4 .   ? -35.402 26.079  -31.873 1.00 22.94  ? 614 HOH B O   1 
HETATM 5736 O O   . HOH H 4 .   ? -53.590 19.553  -37.134 1.00 38.84  ? 615 HOH B O   1 
HETATM 5737 O O   . HOH H 4 .   ? -46.347 18.298  -20.147 1.00 43.25  ? 616 HOH B O   1 
HETATM 5738 O O   . HOH H 4 .   ? -42.732 34.024  -17.597 1.00 40.44  ? 617 HOH B O   1 
HETATM 5739 O O   . HOH H 4 .   ? -52.653 29.779  -28.707 1.00 40.39  ? 618 HOH B O   1 
HETATM 5740 O O   . HOH H 4 .   ? -35.711 26.442  -4.818  1.00 36.26  ? 619 HOH B O   1 
HETATM 5741 O O   . HOH H 4 .   ? -42.548 31.931  -21.316 1.00 32.87  ? 620 HOH B O   1 
HETATM 5742 O O   . HOH H 4 .   ? -21.972 15.504  -17.210 1.00 37.66  ? 621 HOH B O   1 
HETATM 5743 O O   . HOH H 4 .   ? -31.981 15.668  -30.396 1.00 31.73  ? 622 HOH B O   1 
HETATM 5744 O O   . HOH H 4 .   ? -33.850 41.719  -30.073 1.00 26.09  ? 623 HOH B O   1 
HETATM 5745 O O   . HOH H 4 .   ? -39.745 21.658  -25.330 1.00 31.20  ? 624 HOH B O   1 
HETATM 5746 O O   . HOH H 4 .   ? -25.437 6.413   -7.153  1.00 38.42  ? 625 HOH B O   1 
HETATM 5747 O O   . HOH H 4 .   ? -28.260 14.365  -15.380 1.00 26.44  ? 626 HOH B O   1 
HETATM 5748 O O   . HOH H 4 .   ? -53.562 21.856  -22.087 1.00 42.85  ? 627 HOH B O   1 
HETATM 5749 O O   . HOH H 4 .   ? -35.177 25.367  -11.772 1.00 38.20  ? 628 HOH B O   1 
HETATM 5750 O O   . HOH H 4 .   ? -47.540 37.645  -39.855 1.00 38.21  ? 629 HOH B O   1 
HETATM 5751 O O   . HOH H 4 .   ? -39.956 22.488  -34.583 1.00 30.47  ? 630 HOH B O   1 
HETATM 5752 O O   . HOH H 4 .   ? -53.664 31.970  -31.731 1.00 43.58  ? 631 HOH B O   1 
HETATM 5753 O O   . HOH H 4 .   ? -24.969 21.194  -22.867 1.00 37.97  ? 632 HOH B O   1 
HETATM 5754 O O   . HOH H 4 .   ? -25.803 15.812  -29.401 1.00 34.43  ? 633 HOH B O   1 
HETATM 5755 O O   . HOH H 4 .   ? -43.791 19.066  -19.689 1.00 38.62  ? 634 HOH B O   1 
HETATM 5756 O O   . HOH H 4 .   ? -25.573 6.367   11.680  1.00 39.35  ? 635 HOH B O   1 
HETATM 5757 O O   . HOH H 4 .   ? -51.534 23.301  -37.267 1.00 38.38  ? 636 HOH B O   1 
HETATM 5758 O O   . HOH H 4 .   ? -40.719 36.133  -21.096 1.00 32.73  ? 637 HOH B O   1 
HETATM 5759 O O   . HOH H 4 .   ? -33.777 26.961  0.909   1.00 47.61  ? 638 HOH B O   1 
HETATM 5760 O O   . HOH H 4 .   ? -28.076 25.127  -39.500 1.00 40.26  ? 639 HOH B O   1 
HETATM 5761 O O   . HOH H 4 .   ? -34.820 28.367  -40.523 1.00 40.73  ? 640 HOH B O   1 
HETATM 5762 O O   . HOH H 4 .   ? -34.149 31.367  -30.563 1.00 34.41  ? 641 HOH B O   1 
HETATM 5763 O O   . HOH H 4 .   ? -44.338 44.363  -31.732 1.00 40.17  ? 642 HOH B O   1 
HETATM 5764 O O   . HOH H 4 .   ? -29.880 12.362  -28.877 1.00 36.83  ? 643 HOH B O   1 
HETATM 5765 O O   . HOH H 4 .   ? -24.291 7.697   -19.627 1.00 39.10  ? 644 HOH B O   1 
HETATM 5766 O O   . HOH H 4 .   ? -30.468 36.798  -32.206 1.00 37.05  ? 645 HOH B O   1 
HETATM 5767 O O   . HOH H 4 .   ? -25.005 8.290   -4.726  1.00 44.30  ? 646 HOH B O   1 
HETATM 5768 O O   . HOH H 4 .   ? -31.533 5.985   2.333   1.00 40.79  ? 647 HOH B O   1 
HETATM 5769 O O   . HOH H 4 .   ? -24.111 13.434  -25.308 1.00 36.49  ? 648 HOH B O   1 
HETATM 5770 O O   . HOH H 4 .   ? -28.034 20.841  12.301  1.00 47.93  ? 649 HOH B O   1 
HETATM 5771 O O   . HOH H 4 .   ? -32.577 32.459  -33.752 1.00 38.91  ? 650 HOH B O   1 
HETATM 5772 O O   . HOH H 4 .   ? -23.010 4.920   11.612  1.00 39.06  ? 651 HOH B O   1 
HETATM 5773 O O   . HOH H 4 .   ? -51.701 34.625  -17.554 1.00 35.11  ? 652 HOH B O   1 
HETATM 5774 O O   . HOH H 4 .   ? -33.703 26.933  11.843  1.00 55.92  ? 653 HOH B O   1 
HETATM 5775 O O   . HOH H 4 .   ? -57.323 24.997  -7.457  1.00 47.34  ? 654 HOH B O   1 
HETATM 5776 O O   . HOH H 4 .   ? -29.874 28.681  -41.550 1.00 41.84  ? 655 HOH B O   1 
HETATM 5777 O O   . HOH H 4 .   ? -47.282 32.397  -51.002 1.00 32.39  ? 656 HOH B O   1 
HETATM 5778 O O   . HOH H 4 .   ? -37.665 29.828  -39.868 1.00 41.01  ? 657 HOH B O   1 
HETATM 5779 O O   . HOH H 4 .   ? -48.890 33.293  -49.077 1.00 33.50  ? 658 HOH B O   1 
HETATM 5780 O O   . HOH H 4 .   ? -33.347 28.485  -30.826 1.00 33.81  ? 659 HOH B O   1 
HETATM 5781 O O   . HOH H 4 .   ? -33.774 28.394  -27.704 1.00 32.39  ? 660 HOH B O   1 
# 
